Tokushima University / Educator and Researcher Directory --- Tabata, Atsushi

Personal Web Page

https://researchmap.jp/tabataatsushi (researchmap)

https://orcid.org/0000-0002-4896-1738 (ORCID)

Field of Study

○	Microbiology

Subject of Study

○	Microbial infection and host response mechanism (Bacterial protein toxin, Infection mechanisms, Host response)

Book / Paper

Book:

1.	Masaki Hashizume, Koichi Ute, Yumiko Izaki, Masaki Oono, Susumu Nakano, Akira Mizobuchi, Junji Tamatani, Naoyuki Shimomura, Takao Ueda, Katsutoshi Ueno, Fumiaki Nagao, Chikanori Hashimoto, Yasunori Muto, Takeshi Watanabe, Takahiro Kido, Tetsuro Katayama, Yoko Yamashita, Atsushi Tabata, Yuka Sasaki, 島木美香, Takeshige Otoi, Kaori Kanemaru, Takefumi Hattori, Tatsuo Hamano, Katsuyuki Miyawaki, Ryo Anma, Ken-ichi Nishiyama and Mutsuki Aoya : 安全マニュアル, Apr. 2021.
2.	Tokuo Ohnishi, Yasuhiro Uosaki, Kenichi Maeda, Masami Shishibori, Susumu Nakano, Yoshihiro Tada, Junji Tamatani, Naoyuki Shimomura, Atsushi Mikami, Masashi Kurashina, Maki Nakamura, Shigeru Sugiyama, Masato Ozawa, Hirotsugu Yamamoto, Tokue Kuroda, Atsushi Tabata, Yuka Sasaki and Mika Shimaki : Safety Manual, Faculty of Engineering, Tokushima, Feb. 2010.

Academic Paper (Judged Full Paper):

1.	Kazuto Ohkura, Atsushi Tabata and Yoshihiro Uto : Interactive Analysis of UTX-114 Family With EGFR-tyk: Molecular Features of Acetyl Glycosylated Gefitinib., Anticancer Research, Vol.44, No.8, 3587-3591, 2024. (Summary) Acetyl glucose adducts (UTX-114, -115, and -116) were prepared from gefitinib, and their characteristics (e.g., anticancer activity, structural property) were analyzed. Cytotoxicity and radiosensitizing properties of the UTX-114 family were examined using A431 cells. Supramolecular associations between the UTX-114 family compounds and the tyrosine kinase domain of epidermal growth factor receptor (EGFR-tyk) were also examined. The interactive analyses of the UTX-114 family compounds with EGFR-tyk were performed using docking simulation technique. The UTX-114 family showed a similar cytotoxicity as gefitinib, yielding IC values of 31.2 μM (gefitinib), 34.3 μM (UTX-114), 36.8 μM (UTX-115), and 39.4 μM (UTX-116). The EGFR-tyk inhibition ratios (IR) of UTX-114, -115, and -116 to gefitinib were 1.515, 0.983, and 0.551, respectively. The EGFR-tyk inhibitory activity of UTX-114 was higher than that of gefitinib. UTX-114 also showed the highest radiosensitizing activity among the tested compounds. UTX-114 expressed 1841 conformers (-8.989~15.718 kcal/mol) with the solvation free energy (dGW) of UTX-114 decreasing with increasing conformational energy, ranging between -354.955~ -260.815 kJ/mol. Interactive energies of gefitinib, UTX-114, -115, and -116 with EGFR-tyk were -123.640, -144.053, -120.830, and -124.658 kcal/mol, respectively. UTX-114 yielded the lowest interaction energy with EGFR-tyk among tested compounds. Given the association behavior between UTX-114 and EGFR-tyk, along with its other observed properties, UTX-114 appears to be a viable therapeutic possibility. (Keyword) EGFR-tyk inhibition / molecular design / UTX-114 / docking simulation / gefitinib / radiosensitizing activity (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.17181 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 39060048 ● Search Scopus @ Elsevier (PMID): 39060048 ● Search Scopus @ Elsevier (DOI): 10.21873/anticanres.17181 (DOI: 10.21873/anticanres.17181, PubMed: 39060048)
2.	Fumitoshi Yagishita, Tetsuro Katayama, Yuta Kawamura, WATANABE Guran, ABE Sota, OGAWA Itsuki, Atsushi Tabata, Yasushi Yoshida, Hyuma Masu, Shoko Ueta, Yukihiro Arakawa, Keiji Minagawa, Akihiro Furube and Yasushi Imada : Blue Luminescent Boron Complexes Based on N,N-Type Imidazo[1,5-a]pyridine Ligand for Mitochondrial Imaging, Asian Journal of Organic Chemistry, Vol.13, No.9, e202400189, 2024. (Link to Publication Site) ● Publication site (DOI): 10.1002/ajoc.202400189 (Link to Search Site for Scientific Articles) ● Summary page in Scopus @ Elsevier: 2-s2.0-85199996380 (DOI: 10.1002/ajoc.202400189, Elsevier: Scopus)
3.	Takuya YAMADA, Yugo YAMAMORI, Nanami Matsuda, Hideaki Nagamune, Kazuto Ohkura, Toshifumi Tomoyasu and Atsushi Tabata : Streptolysin S induces pronounced calcium-ion influx-dependent expression of immediate early genes encoding transcription factors, Scientific Reports, Vol.13, No.13720, 2023. (Summary) Anginosus group streptococci (AGS) are opportunistic human pathogens of the oral cavity. The β-hemolytic subgroup of Streptococcus anginosus subsp. anginosus secretes streptolysin S (SLS) and exhibits not only hemolytic activity but also cytotoxicity toward cultured human cell lines. However, the detailed mechanism of action of SLS and the cellular responses of host cells have not yet been fully clarified. To determine the pathogenic potential of SLS-producing β-hemolytic S. anginosus subsp. anginosus, the SLS-dependent response induced in the human oral squamous cell carcinoma HSC-2 cells was investigated to determine the pathogenic potential of SLS-producing β-hemolytic S. anginosus subsp. anginosus. This study revealed that the Ca influx and the expression of immediate early genes (IEGs) encoding transcription factors such as early growth responses (EGRs) and activator protein-1 (AP-1) were greatly increased in HSC-2 cells incubated with the culture supernatant of SLS-producing β-hemolytic S. anginosus subsp. anginosus. Moreover, this SLS-dependent increase in expression was significantly suppressed by Ca chelation, except for jun. These results suggest that SLS caused Ca influx into the cells following greatly enhanced expression of IEG-encoding transcription factors. The results of this study may help in understanding the pathogenicity of SLS-producing AGS. (Keyword) cytolysin / Streptococcus (Link to Publication Site) ● Publication site (DOI): 10.1038/s41598-023-40981-1 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37608082 ● Search Scopus @ Elsevier (PMID): 37608082 ● Search Scopus @ Elsevier (DOI): 10.1038/s41598-023-40981-1 (DOI: 10.1038/s41598-023-40981-1, PubMed: 37608082)
4.	Toshifumi Tomoyasu, Airi Matsumoto, Ayuko Takao, Atsushi Tabata and Hideaki Nagamune : A simple method to differentiate three classes of cholesterol-dependent cytolysins., Journal of Microbiological Methods, Vol.207, 2023. (Summary) Cholesterol-dependent cytolysins (CDCs) are proteinaceous toxins widely distributed in gram-positive pathogenic bacteria. CDCs can be classified into three groups (I-III) based on the mode of receptor recognition. Group I CDCs recognize cholesterol as their receptor. Group II CDC specifically recognizes human CD59 as the primary receptor on the cell membrane. Only intermedilysin from Streptococcus intermedius has been reported as a group II CDC. Group III CDCs recognize both human CD59 and cholesterol as receptors. CD59 contains five disulfide bridges in its tertiary structure. Therefore, we treated human erythrocytes with dithiothreitol (DTT) to inactivate CD59 on membranes. Our data showed that DTT treatment caused a complete loss of recognition of intermedilysin and an anti-human CD59 monoclonal antibody. In contrast, this treatment did not affect the recognition of group I CDCs, judging from the fact that DTT-treated erythrocytes were lysed with the same efficiency as mock-treated human erythrocytes. The recognition of group III CDCs toward DTT-treated erythrocytes was partially reduced, and these results are likely due to the loss of human CD59 recognition. Therefore, the degree of human CD59 and cholesterol requirements of uncharacterized group III CDCs frequently found in Mitis group streptococci can be easily estimated by comparing the amounts of hemolysis between DTT-treated and mock-treated erythrocytes. (Keyword) bacterial toxins / Cytotoxins / Cell Membrane / Erythrocytes / cholesterol (Link to Publication Site) ● Publication site (DOI): 10.1016/j.mimet.2023.106696 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36898586 ● Search Scopus @ Elsevier (PMID): 36898586 ● Search Scopus @ Elsevier (DOI): 10.1016/j.mimet.2023.106696 (DOI: 10.1016/j.mimet.2023.106696, PubMed: 36898586)
5.	Shuto Yokohata, Kazuto Ohkura, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Human serum albumin stabilizes streptolysin S activity secreted in the extracellular milieu by streptolysin S-producing streptococci., Microbiology and Immunology, Vol.67, No.2, 58-68, 2022. (Summary) Anginosus group streptococci (AGS) are opportunistic pathogens of the human oral cavity; however, their pathogenicity has not been discussed in detail. Oral streptococci live in the gingival sulcus, from where they can easily translocate into the bloodstream due to periodontal diseases and dental treatment and cause hazardous effects on the host through their virulence factors. Streptolysin S (SLS), a pathogenic factor produced by β-hemolytic species/strains belonging to AGS, plays an important role in damaging host cells. Therefore, we investigated the SLS-dependent cytotoxicity of β-hemolytic Streptococcus anginosus subsp. anginosus (SAA), focusing on different growth conditions such as in the bloodstream. Consequently, SLS-dependent hemolytic activity/cytotoxicity in the culture supernatant of β-hemolytic SAA was stabilized by blood components, particularly human serum albumin (HSA). The present study suggests that the secreted SLS, not only from β-hemolytic SAA, but also from other SLS-producing streptococci, is stabilized by HSA. As HSA is the most abundant protein in human plasma, the results of this study provide new insights into the risk of SLS-producing streptococci which can translocate into the bloodstream. (Keyword) Humans / Streptolysins / Serum Albumin, Human / Streptococcus pyogenes / Virulence / Virulence Factors / Bacterial Proteins (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.13042 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36478453 ● Search Scopus @ Elsevier (PMID): 36478453 ● Search Scopus @ Elsevier (DOI): 10.1111/1348-0421.13042 (DOI: 10.1111/1348-0421.13042, PubMed: 36478453)
6.	Atsushi Tabata, Airi Matsumoto, Ai Fujimoto, Kazuto Ohkura, Takuya Ikeda, Hiroki Oda, Shuto Yokohata, Miho Kobayashi, Toshifumi Tomoyasu, Ayuko Takao, Hisashi Ohkuni and Hideaki Nagamune : Dual functions of discoidinolysin, a cholesterol-dependent cytolysin with N-terminal discoidin domain produced from strain Nm-76., Journal of Oral Microbiology, Vol.14, No.1, 2105013, 2022. (Summary) Some strains of exhibit β-hemolysis due to the β-hemolytic activity of cholesterol-dependent cytolysin (CDC). Recently, a gene encoding an atypical lectinolysin-related CDC was found in strain Nm-76. However, the product of this gene remains uncharacterized. We aimed to characterize this atypical CDC and its molecular functions and contribution to the pathogenicity of strain Nm-76. Phylogenetic analysis of the CDC gene was conducted based on the web-deposited information. The molecular characteristics of CDC were investigated using a gene-deletion mutant strain and recombinant proteins expressed in . The gene encoding CDC found in Nm-76 and its homolog are distributed among many strains. This CDC is phylogenetically different from other previously characterized CDCs, such as -derived human platelet aggregation factor (Sm-hPAF)/lectinolysin and mitilysin. Because this CDC possesses an additional N-terminal domain, including a discoidin motif, it was termed discoidinolysin (DLY). In addition to the preferential lysis of human cells, DLY displayed N-terminal domain-dependent facilitation of human erythrocyte aggregation and intercellular associations between human cells. DLY functions as a hemolysin/cytolysin and erythrocyte aggregation/intercellular association molecule. This dual-function DLY could be an additional virulence factor in . (Link to Publication Site) ● Publication site (DOI): 10.1080/20002297.2022.2105013 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35937899 ● Search Scopus @ Elsevier (PMID): 35937899 ● Search Scopus @ Elsevier (DOI): 10.1080/20002297.2022.2105013 (DOI: 10.1080/20002297.2022.2105013, PubMed: 35937899)
7.	Kazuto Ohkura, Atsushi Tabata, Yoshihiro Uto and Hitoshi Hori : Molecular Interaction Between Boron Tracedrug UTX-51 Derivatives and Bovine Serum Albumin: Application to an Analytical Model of AGEs Destruction by Thermal Neutron Irradiation, Anticancer Research, Vol.42, No.8, 4017-4023, 2022. (Summary) Boron tracedrugs possess global molecular tracking abilities and localized destructive power. We investigated the molecular properties of synthesized boron tracedrugs, including UTX-51, and their interactions with the advanced glycation end-product (AGE)-related protein bovine serum albumin (BSA). A conformational analysis of the compounds used in the present study was performed using CAChe (Fujitsu Inc., Tokyo, Japan) and the degree of stereo-hydrophobicity of the conformers obtained was verified using Mopac (Fujitsu Inc.). The interactive properties of global minimum conformers of the derivatives tested with BSA were assessed using Molegro Virtual Docker (CLC bio., Aarhus, Denmark). Among the compounds investigated, UTX-51 was confirmed to interact with BSA based on the formation of hydrogen bonds between BSA and UTX-51. UTX-51 is a promising boron tracedrug and can be used as the lead structure for developing a therapeutic agent for AGE-related diseases, including cancer. (Keyword) BSA / Boron tracedrugs / molecular design / UTX-51 (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.15898 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35896254 ● Search Scopus @ Elsevier (PMID): 35896254 ● Search Scopus @ Elsevier (DOI): 10.21873/anticanres.15898 (DOI: 10.21873/anticanres.15898, PubMed: 35896254)
8.	Atsushi Tabata, Rina Shirai, Haruka Miki, Yukihiro Nishikawa, Tatsuya Kashima, Tomomi Aoyama, Shu Murakami, Momoyo Azuma, Toshifumi Tomoyasu and Hideaki Nagamune : Hapten-labeled fusion-polymerase chain reaction of multiple marker genes for the application of immunochromatographic test., Journal of Bioscience and Bioengineering, Vol.134, No.1, 70-76, 2022. (Summary) A variety of methods have been reported using polymerase chain reaction (PCR)-based nucleic acid testing (NAT) because of its potential to be used in highly sensitive inspection systems. Among these NATs, fusion-PCR (also called as overlap-extension-PCR) has been focused on this study and adopted to generate the fused amplicon composed of plural marker gene fragments for detection. Generally, conventional agarose gel electrophoresis followed by gel staining is employed to check the PCR results. However, these are time-consuming processes that use specific equipment. To overcome these disadvantages, the immunochromatographic test (ICT) for the detection of PCR amplicons with hapten-labels that were generated by PCR using hapten-labeled primers was also adopted in this study. Based on these concepts, we constructed the systems of hapten-labeled fusion-PCR (HL-FuPCR) followed by ICT (HL-FuPCR-ICT) for the two and three marker genes derived from pathogenic microbe. As a result, we successfully developed a two marker genes system for the pathogenic influenza A virus and a three marker genes system for the penicillin-resistant Streptococcus pneumoniae. These detection systems of HL-FuPCR-ICT are characterized by simple handling and rapid detection within few minutes, and also showed the results as clear lines. Thus, the HL-FuPCR-ICT system introduced in this study has potential for use as a user-friendly inspection tool with the advantages especially in the detection of specific strains or groups expressing the characteristic phenotype(s) such as antibiotic resistance and/or high pathogenicity even in the same species. (Keyword) DNA Primers / Haptens / Immunologic Tests / Polymerase Chain Reaction / Sensitivity and Specificity (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jbiosc.2022.03.006 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35450786 ● Search Scopus @ Elsevier (PMID): 35450786 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jbiosc.2022.03.006 (DOI: 10.1016/j.jbiosc.2022.03.006, PubMed: 35450786)
9.	Hiroki Nakai, Daiu Akiyama, Yoshiaki Taniguchi, Iori Kishinobu, Hiromichi Wariishi, Yasuhide Ohno, Masao Nagase, Takuya Ikeda, Atsushi Tabata and Hideaki Nagamune : Charge-independent protein adsorption characteristics of epitaxial graphene field-effect transistor on SiC substrate, Journal of Applied Physics, Vol.130, No.7, 074502-1-074502-8, 2021. (Keyword) graphene (Tokushima University Institutional Repository) ● Metadata: 116163 (Link to Publication Site) ● Publication site (DOI): 10.1063/5.0054688 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1063/5.0054688 (Tokushima University Institutional Repository: 116163, DOI: 10.1063/5.0054688)
10.	Keita Hoshi, Kazuma Kusumoto, Airi Matsumoto, Atsushi Tabata, Hideaki Nagamune, Eiji Hase, Takeo Minamikawa, Takeshi Yasui, Yasushi Yoshida, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : Synthesis of D-π-A type benzothiazolepyridinium salt composite and its application as photo-degradation agent for amyloid fibrils, Bioorganic & Medicinal Chemistry Letters, Vol.50, 128324, 2021. (Summary) We have synthesized a cyan fluorescent benzothiazole-pyridinium salt composite based on D-p-A architecture. This salt was found to work as not only a two- and three-photon excitable fluorophore but also a degradation agent against amyloid fibrils under LED irradiation conditions. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bmcl.2021.128324 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34403727 ● Search Scopus @ Elsevier (PMID): 34403727 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bmcl.2021.128324 (DOI: 10.1016/j.bmcl.2021.128324, PubMed: 34403727)
11.	Kazuto Ohkura, Yohei Tatematsu and Atsushi Tabata : Construction of a Drug Release Evaluation System: Application of Mitochondrial Respiration to Monitor Drug Release, Anticancer Research, Vol.41, No.8, 4083-4088, 2021. (Summary) Efficient drug encapsulation and regulation of drug release are important factors for sustained drug release and application for release-controlled anti-cancer and anti-inflammatory drug delivery. In the present study, a direct evaluation system for drug-release from model carrier (e.g., alginate-gel beads) was examined using the mitochondrial oxygen consumption rate as an index. Alginate-gel beads were coated with the uncoupler SF6847 (SF beads) and used as a model microparticle-type drug. The real-time monitoring of SF6847 release from prepared alginate-gel beads was performed using the mitochondrial oxygen consumption rate. Release profiles of nonsteroidal anti-inflammatory drugs [NSAIDs, mefenamic acid (MEF) and diclofenac (DIC)] from alginate-gel beads as well as SF beads were investigated using the real time monitoring system. SF6847 release from alginate-gel beads was clearly detected using the rat liver mitochondrial oxygen consumption rate. The release features of MEF and DIC from alginate-gel beads were defined by the present trial monitoring system, and these NSAIDs exhibited different release profiles. The present drug monitoring system detected released drugs, and the release profile reflected the molecular properties of the test drugs. This system may be applied to the design and development of precise sustained drug release systems (e.g., anti-cancer and anti-inflammatory drugs). (Keyword) Alginates / Animals / Anti-Inflammatory Agents, Non-Steroidal / Cell Respiration / Diclofenac / Drug Carriers / Drug Liberation / Mefenamic Acid / Mitochondria, Liver / Nitriles / Oxygen / Rats / Uncoupling Agents (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.15210 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34281878 ● Search Scopus @ Elsevier (PMID): 34281878 ● Search Scopus @ Elsevier (DOI): 10.21873/anticanres.15210 (DOI: 10.21873/anticanres.15210, PubMed: 34281878)
12.	Keita Hoshi, Masami Itaya, Koki Tahara, Airi Matsumoto, Atsushi Tabata, Hideaki Nagamune, Yasushi Yoshida, Eiji Hase, Takeo Minamikawa, Takeshi Yasui, Tetsuro Katayama, Akihiro Furube, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : Two-photon excitable boron complex based on tridentate imidazo[1,5-a]pyridine ligand for heavy- atom-free mitochondria-targeted photodynamic therapy, RSC Advances, Vol.11, 26403-26407, 2021. (Tokushima University Institutional Repository) ● Metadata: 116625 (Link to Publication Site) ● Publication site (DOI): 10.1039/d1ra05059a (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1039/d1ra05059a (Tokushima University Institutional Repository: 116625, DOI: 10.1039/d1ra05059a)
13.	Airi Matsumoto, Atsushi Tabata, Kazuto Ohkura, Hiroki Oda, Chihiro Kodama, Hisashi Ohkuni, Ayuko Takao, Ken Kikuchi, Toshifumi Tomoyasu and Hideaki Nagamune : Molecular characteristics of an adhesion molecule containing cholesterol-dependent cytolysin-motif produced by mitis group streptococci, Microbiology and Immunology, Vol.65, No.2, 61-75, 2021. (Summary) Streptococcus pseudopneumoniae (SPpn) is a relatively new species closely related to S. pneumoniae (SPn) and S. mitis (SM) belonging to the Mitis group of the genus Streptococcus (MGS). Although genes encoding various pneumococcal virulence factors have been observed in the SPpn genome, the pathogenicity of SPpn against human, including the roles of virulence factor candidates, is still unclear. The present study focused on and characterized a candidate virulence factor previously reported in SPpn with deduced multiple functional domains, such as lipase domain, two lectin domains, and cholesterol-dependent cytolysin-related domain using various recombinant proteins. The gene was found not only in SPpn but also in the strains of SM and SPn. Moreover, the gene product was expressed in the gene-positive strains as secreted and cell-bound forms. The recombinant of gene product showed lipase activity and human cell-binding activity depending on the function of lectin domain(s), but no hemolytic activity. Thus, based on the distribution of the gene within the MGS and its molecular function, the gene product was named mitilectin (MLC) and its contribution to the potential pathogenicity of the MLC-producing strains was investigated. Consequently, the treatment with anti-MLC antibody and the mlc gene-knockout significantly reduced the human cell-binding activity of MLC-producing strains. Therefore, the multifunctional MLC was suggested to be important as an adhesion molecule in considering the potential pathogenicity of the MLC-producing strains belonging to MGS, such as SPpn and SM. (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12868 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33331679 ● Search Scopus @ Elsevier (PMID): 33331679 ● Search Scopus @ Elsevier (DOI): 10.1111/1348-0421.12868 (DOI: 10.1111/1348-0421.12868, PubMed: 33331679)
14.	Atsushi Tabata, Hisashi Ohkuni, Yasuhiko Itoh, Yoshitaka Fukunaga, Toshifumi Tomoyasu and Hideaki Nagamune : Complete Genome Sequence of Streptococcus mitis Strain Nm-65, Isolated from a Patient with Kawasaki Disease, Microbiology Resource Announcements, Vol.10, No.1, e01239-20, 2021. (Summary) Nm-65 is a human commensal streptococcal strain of the mitis group that was isolated from the tooth surface of a patient with Kawasaki disease. The complete genome sequence of Nm-65 was obtained by means of hybrid assembly, using two next-generation sequencing data sets. The final assembly size was 2,085,837 bp, with 2,039 coding sequences. (Tokushima University Institutional Repository) ● Metadata: 116462 (Link to Publication Site) ● Publication site (DOI): 10.1128/MRA.01239-20 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33414340 ● Search Scopus @ Elsevier (PMID): 33414340 ● Search Scopus @ Elsevier (DOI): 10.1128/MRA.01239-20 (Tokushima University Institutional Repository: 116462, DOI: 10.1128/MRA.01239-20, PubMed: 33414340)
15.	Keita Hoshi, Yohei Sanagawa, Ryuta Umebayashi, Atsushi Tabata, Hideaki Nagamune, Eiji Hase, Takeo Minamikawa, Takeshi Yasui, Yasushi Yoshida, Keiji Minagawa, Yasuhiko Kawamura, Yasushi Imada and Fumitoshi Yagishita : Synthesis and Optical Property of Quadrupolar Pyridinium Salt and Its Application as Bioimaging Agent, Chemistry Letters, Vol.49, No.12, 1487-1489, 2020. (Link to Publication Site) ● Publication site (DOI): 10.1246/cl.200604 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1246/cl.200604 (DOI: 10.1246/cl.200604)
16.	Eiji Hase, Hiroki Takanari, Keita Hoshi, Masaki Okamoto, Atsushi Tabata, Hideaki Nagamune, Takeo Minamikawa, Takeshi Yasui, Yasushi Yoshida, Keiji Minagawa, Yasuhiko Kawamura, Yasushi Imada and Fumitoshi Yagishita : Two- and three-photon excitable quaternized imidazo[1,2-a]pyridines for mitochondrial imaging and potent cancer therapy agent, Organic & Biomolecular Chemistry, Vol.18, No.38, 7571-7576, 2020. (Link to Publication Site) ● Publication site (DOI): 10.1039/D0OB01585G (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32940324 ● Search Scopus @ Elsevier (PMID): 32940324 ● Search Scopus @ Elsevier (DOI): 10.1039/D0OB01585G (DOI: 10.1039/D0OB01585G, PubMed: 32940324)
17.	Kazuto Ohkura, Atsushi Tabata, Yoshihiro Uto and Hitoshi Hori : Effect of Isomerization of TX-2036 Derivatives on the Interaction With Tyrosine Kinase Domain of EGF Receptor, Anticancer Research, Vol.40, No.8, 4675-4680, 2020. (Summary) From the design and synthesis of enantiomers, we can expect to obtain two compounds with different pharmacokinetics and pharmacological activities at the same time, which is thought to lead to the development of efficient anticancer agents. Chiral-2-nitroimidazole TX-2036 derivatives exhibit stereo-configuration (R- and S-configuration)-dependent tyrosine kinase inhibitory activity, and the activity of the tyrosine kinase domain of EGF receptor (EGFR-tyk) is suppressed. In order to clarify the reason why the effects on EGFR-tyk activity differ depending on stereoisomers, we tried to analyze the interaction between each TX-2036 derivative and EGFR-tyk. The 2-nitroimidazole-based radiosensitizer TX-2036 series were synthesized and their molecular features were examined using protein kinase inhibition assay and molecular structural analysis. R-configured TXs (TX-2043, -2030, and -2036) exhibited more potent protein kinase inhibitory activity than S-configured TXs (TX-2044, - 2031, and -2037), and the IC value of TX-2036 was 1.8 μM. R-configured TXs interacted with Lys and Thr of EGFR-tyk. The combinations of amino acid residues targeted by the S-configured TXs were different from each other (Ile and Thr (TX-2044), Ser, Thr, and Thr (TX-2031), Gly, Cys, and Thr (TX-2037)). Preparing a series of isomers with different target sites was considered beneficial when the target was mutated. (Keyword) EGF receptor / molecular design / TX-2036 derivatives / structure (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.14466 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32727791 ● Search Scopus @ Elsevier (PMID): 32727791 ● Search Scopus @ Elsevier (DOI): 10.21873/anticanres.14466 (DOI: 10.21873/anticanres.14466, PubMed: 32727791)
18.	Daisuke Takamatsu, Kayo Okumura, Atsushi Tabata, Mariko Okamoto and Masatoshi Okura : Transcriptional regulator SpxA1a controls the resistance of the honey bee pathogen Melissococcus plutonius to the antimicrobial activity of royal jelly, Environmental Microbiology, Vol.22, No.7, 2736-2755, 2020. (Summary) Royal jelly (RJ), a brood food of honey bees, has strong antimicrobial activity. Melissococcus plutonius, the causative agent of European foulbrood of honey bees, exhibits resistance to this antimicrobial activity and infects larvae orally. Among three genetically distinct groups (CC3, CC12 and CC13) of M. plutonius, CC3 strains exhibit the strongest RJ resistance. In this study, to identify genes involved in RJ resistance, we generated an RJ-susceptible derivative from a highly RJ-resistant CC3 strain by UV mutagenesis. Genome sequence analysis of the derivative revealed the presence of a frameshift mutation in the putative regulator gene spxA1a. The deletion of spxA1a from a CC3 strain resulted in increased susceptibility to RJ and its antimicrobial component 10-hydroxy-2-decenoic acid. Moreover, the mutant became susceptible to low-pH and oxidative stress, which may be encountered in brood foods. Differentially expressed gene analysis using wild-type and spxA1a mutants revealed that 45 protein-coding genes were commonly upregulated in spxA1a-positive strains. Many upregulated genes were located in a prophage region, and some highly upregulated genes were annotated as universal/general stress proteins, oxidoreductase/reductase, chaperons and superoxide dismutase. These results suggest that SpxA1a is a key regulator to control the tolerance status of M. plutonius against stress in honey bee colonies. (Link to Publication Site) ● Publication site (DOI): 10.1111/1462-2920.15125 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32519428 ● Search Scopus @ Elsevier (PMID): 32519428 ● Search Scopus @ Elsevier (DOI): 10.1111/1462-2920.15125 (DOI: 10.1111/1462-2920.15125, PubMed: 32519428)
19.	Atsushi Tabata, Hisashi Ohkuni, Haruka Hino, Takuya Saigo, Chihiro Kodama, QING TANG, Toshifumi Tomoyasu, Yoshitaka Fukunaga, Yasuhiko Itoh and Hideaki Nagamune : Cytotoxic property of Streptococcus mitis strain producing two different types of cholesterol-dependent cytolysins, Infection, Genetics and Evolution, Vol.85, 104483, 2020. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.meegid.2020.104483 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32731044 ● Summary page in Scopus @ Elsevier: 2-s2.0-85088967403 (DOI: 10.1016/j.meegid.2020.104483, PubMed: 32731044, Elsevier: Scopus)
20.	Ayuko Takao, Toshifumi Tomoyasu, Atsushi Tabata, Hideaki Nagamune and Nobuko Maeda : A photometric pH assay for microplate bacterial cultures., Journal of Microbiological Methods, Vol.172, 1-3, 2020. (Summary) A photometric pH assay for sugar-fermenting bacterial culture on a 96-well plate was developed. This assay can save time and effort in repeat handlings. Its use could decrease the risk of bacterial contamination in measurement devices and leakage into the environment. The assay's pH estimation range was pH 4.2-7.6. (Keyword) chemical indicators / fermentation / pH assay / photometric method / microbial culture (Link to Publication Site) ● Publication site (DOI): 10.1016/j.mimet.2020.105910 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32229266 ● Summary page in Scopus @ Elsevier: 2-s2.0-85082519032 (DOI: 10.1016/j.mimet.2020.105910, PubMed: 32229266, Elsevier: Scopus)
21.	Miho Kobayashi, Madoka Nishimura, Mina Kawamura, Norio Kamemura, Hideaki Nagamune and Atsushi Tabata : Change in membrane potential induced by streptolysin O, a pore-forming toxin: flow cytometric analysis using a voltage-sensitive fluorescent probe and rat thymic lymphocytes, Microbiology and Immunology, Vol.64, No.1, 10-22, 2020. (Summary) Streptolysin O (SLO) is a bacterial pore-forming toxin that is employed to permeabilize cell membranes in some biological experiments. SLO forms various types of pores with different shapes, increasing membrane ion permeability and subsequently inducing changes in membrane potential. To characterize the pores formed by SLO, the changes in membrane potential induced by SLO in rat lymphocytes were considered using flow cytometry with a voltage-sensitive fluorescent probe, bis-(1,3-dibutylbarbituric acid)trimethine oxonol (Oxonol). SLO caused three types of membrane potential responses accessed with Oxonol. One type induces a great decrease in Oxonol fluorescence (large hyperpolarization) that may be elicited via the increase of Ca -dependent K permeability by SLO-induced influx of external Ca . A second type is an increase in Oxonol fluorescence (depolarization) that may be caused by a nonspecific increase in membrane cation permeability. The third type is a small decrease in Oxonol fluorescence (small hyperpolarization), probably via an increase in Cl permeability. That SLO transitionally changes membrane ion permeability may have implications in the pathology of pyogenic group streptococci infections in which SLO is thought to be one of the key virulence factors. (Keyword) Animals / Bacterial Proteins / Bacterial Toxins / Barbiturates / Calcimycin / Calcium / Cell Membrane / Cell Membrane Permeability / Disease Models, Animal / Flow Cytometry / Fluorescent Dyes / Lymphocytes / Male / Membrane Potentials / Rats / Rats, Wistar / Streptolysins (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12748 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31584206 ● Search Scopus @ Elsevier (PMID): 31584206 ● Search Scopus @ Elsevier (DOI): 10.1111/1348-0421.12748 (DOI: 10.1111/1348-0421.12748, PubMed: 31584206)
22.	Fumitoshi Yagishita, Jun-ichi Tanigawa, Chiho Nii, Atsushi Tabata, Hideaki Nagamune, Hiroki Takanari, Yasushi Imada and Yasuhiko Kawamura : Fluorescent Imidazo[1,5-a]pyridinium Salt for a Potential Cancer Therapy Agent, ACS Medicinal Chemistry Letters, Vol.10, No.8, 1110-1114, 2019. (Link to Publication Site) ● Publication site (DOI): 10.1021/acsmedchemlett.9b00034 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1021/acsmedchemlett.9b00034 (DOI: 10.1021/acsmedchemlett.9b00034)
23.	Kazuto Ohkura, Atsushi Tabata, Yoshihiro Uto and Hitoshi Hori : Correlation Between Radiosensitizing Activity and the Stereo-structure of the TX-2036 Series of Molecules, Anticancer Research, Vol.39, No.8, 4479-4483, 2019. (Summary) The stereo-configuration (R-, S-configuration) of chiral-2-nitroimidazole derivatives alters their radiosensitizing activity. This study aimed at examining the molecular features of these enantiomers by molecular simulation techniques. A series of 2-nitroimidazole-based radiosensitizer TX-2036 molecules were synthesized, and their profiles were examined using molecular structural analysis such as conformation analysis, molecular orbital analysis, and electrostatic potential analysis. R-configured TXs (TX-2043, -2030, -2036) had a weaker radiosensitizing activity than S-configured TXs (TX-2044, -2031, -2037), and R-compounds had a small minus electrostatic potential (ESP) field in the cyclopentene-1,3-dione region. S-configured TX-2046 had weaker radiosensitizing activity than R-configured TX-2045, and TX-2046 had a small minus ESP field as well as R-configured TX-2043, -2030, - 2036. The cyclopentene-1,3-dione involved in the small minus ESP field affected the radiosensitizing activity of the TX-2036 series of molecules. (Keyword) molecular design / TX-2036 / radiosensitizing activity / structure (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.13622 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31366548 ● Summary page in Scopus @ Elsevier: 2-s2.0-85070717728 (DOI: 10.21873/anticanres.13622, PubMed: 31366548, Elsevier: Scopus)
24.	Atsushi Tabata, Takuya Yamada, Ohtani Hiromi, Kazuto Ohkura, Toshifumi Tomoyasu and Hideaki Nagamune : β-Hemolytic Streptococcus anginosus subsp. anginosus causes streptolysin S-dependent cytotoxicity to human cell culture lines in vitro, Journal of Oral Microbiology, Vol.11, No.1, 1-11, 2019. (Summary) Streptococcus anginosus subsp. (SAA) is one of the opportunistic pathogens in humans that inhabits the oral cavity. The type strain of SAA, NCTC10713, showed clear β-hemolysis on blood agar plates, and the sole β-hemolytic factor revealed two streptolysin S (SLS) molecules. SLS is well known as the peptide hemolysin produced from the human pathogen and shows not only hemolytic activity on erythrocytes but also cytotoxic activity in cell culture lines and , such as in a mouse infection model. However, no cytotoxic activity of SLS produced from β-hemolytic SAA (β-SAA) has been reported so far. In this study, the SLS-dependent cytotoxicity of the β-SAA strains including the genetically modified strains was investigated . The SLS-producing β-SAA showed cytotoxicity in human cell culture lines under the co-cultivation condition and it was found that this cytotoxicity was caused by the SLS secreted into the extracellular milieu. The results from this study suggest that the SLS produced from β-SAA might indicate the cytotoxic potential similar to that of the SLS from and the SLS-producing β-SAA would be recognized as "a wolf in sheep's clothing" More attention will be paid to the pathogenicity of β-hemolytic Anginosus group streptococci. (Keyword) bacterial toxins / Streptococcus (Tokushima University Institutional Repository) ● Metadata: 113540 (Link to Publication Site) ● Publication site (DOI): 10.1080/20002297.2019.1609839 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31105901 ● Summary page in Scopus @ Elsevier: 2-s2.0-85065585236 (Tokushima University Institutional Repository: 113540, DOI: 10.1080/20002297.2019.1609839, PubMed: 31105901, Elsevier: Scopus)
25.	Toshifumi Tomoyasu, Keigo Tsuruno, Ryosuke Tanatsugu, Aya Miyazaki, Hiroyuki Kondo, Atsushi Tabata, Whiley A. Robert, Kenji Sonomoto and Hideaki Nagamune : Recognizability of heterologous co-chaperones with Streptococcus intermedius DnaK and Escherichia coli DnaK, Microbiology and Immunology, Vol.62, No.11, 681-693, 2018. (Summary) Streptococcus intermedius DnaK complements the temperature-sensitive phenotype of an Escherichia coli dnaK null mutant only when co-chaperones DnaJ and GrpE are co-expressed. Therefore, whether S. intermedius DnaK and E. coli DnaK can recognize heterologous co-chaperones in vitro was examined. Addition of heterologous GrpE to DnaK and DnaJ partially stimulated adenosine triphosphatase (ATPase) activity, and almost completely stimulated luciferase refolding activity. Addition of heterologous DnaJ to GrpE and DnaK also stimulated ATPase activity; however, significant luciferase refolding activity was not observed. Moreover, E. coli DnaJ had a negative effect on the luciferase refolding activity of the S. intermedius DnaK chaperone system. In E. coli chaperone mutants, with the exception of E. coli DnaJ, stronger expression of the heterologous co-chaperones partially or almost completely complemented the temperature-sensitive-phenotype. These results indicate that all heterologous co-chaperones can at least partially recognize DnaK of a distantly related species. A region of the ATPase domain that is present in the DnaK of gram-negative bacteria is absent from the DnaK of gram-positive bacteria. This region is believed to be important for recognition of co-chaperones from gram-negative bacteria. However, insertion of this segment into S. intermedius DnaK failed to increase its ability to recognize E. coli co-chaperones, implying that this region is unnecessary or insufficient for the recognition of E. coli co-chaperones. Thus, our data suggest that a basic structural similarity is conserved among the components of the S. intermedius and E. coli DnaK chaperone systems, allowing weak associations between heterologous components. (Keyword) molecular chaperone / Escherichia coli / Streptococcus (Tokushima University Institutional Repository) ● Metadata: 115748 (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12651 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30239035 ● Summary page in Scopus @ Elsevier: 2-s2.0-85056121796 (Tokushima University Institutional Repository: 115748, DOI: 10.1111/1348-0421.12651, PubMed: 30239035, Elsevier: Scopus)
26.	Fumitoshi Yagishita, Chiho Nii, Yoshihiko Tezuka, Atsushi Tabata, Hideaki Nagamune, Naohiro Uemura, Yasushi Yoshida, Takashi Mino, Masami Sakamoto and Yasuhiko Kawamura : Fluorescent N-Heteroarenes Having Large Stokes Shift and Water Solubility Suitable for Bioimaging, Asian Journal of Organic Chemistry, Vol.7, No.8, 1614-1619, 2018. (Link to Publication Site) ● Publication site (DOI): 10.1002/ajoc.201800250 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1002/ajoc.201800250 (DOI: 10.1002/ajoc.201800250)
27.	Kazuto Ohkura, Y Kawaguchi, Y Tatematsu, Atsushi Tabata, Yoshihiro Uto and Hitoshi Hori : Structure-associated Functional Control of TX-1877 Series by Glyco-conjugation, Anticancer Research, Vol.38, No.7, 4241-4245, 2018. (Summary) Sugar molecules are often used as a tool to structurally modify chemical compounds. The features of synthesized sugar-conjugated TX-1877 derivatives were herein examined. The molecular stabilities (reactivity) and hydrophobicities of sugar (e.g., monosaccharide and tetra-O-acetylated monosaccharide)-conjugated TXs were analyzed using a molecular simulation (e.g. molecular mechanics (MM) and molecular orbital (MO) analysis). The hydrophobicities of TX-1877 derivatives were increased by tetra-O-acetylation, and TX-2244 exhibited the most potent radiosensitizing activity (enhancement ratio: ER=2.30). The conformations and hydrophobicities of chemical compounds may be controlled by adding monosaccharide- and tetra-O-acetyl-conjugated sugars to TX-1877. (Keyword) molecular design / TX-1877 / structure glyco-conjugation (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.12720 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29970557 ● Summary page in Scopus @ Elsevier: 2-s2.0-85049784420 (DOI: 10.21873/anticanres.12720, PubMed: 29970557, Elsevier: Scopus)
28.	Qing Tang, Masayoshi Onitsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Construction of Anti-HER2 Recombinants as Targeting Modules for a Drug-delivery System Against HER2-positive Cells, Anticancer Research, Vol.38, No.7, 4319-4325, 2018. (Summary) Recombinant antibodies have been investigated and used in applications such as targeting modules of drug-delivery systems (DDS) against cancers. This study aimed to prepare recombinant antibodies against HER2, containing sortase A (SrtA) recognition sequence, that are applicable as targeting modules in DDS after linkage with the drug-carrier containing oligoglycine-acceptor peptide by SrtA transpeptidation. The recombinant trastuzumab fragment antibodies (scFvs and Fab) with the SrtA-recognition motif (LPXTG) at their C-terminal were constructed and expressed in Escherichia coli and Chinese hamster ovary (CHO) cells, respectively. The reactivity of the purified recombinant antibodies towards HER2-expressing cells was also evaluated via immunofluorescent staining. Fab demonstrated higher yield and purity and better reactivity towards HER2-expressing cells (HCT-15 and HeLa) when compared to scFvs. The CHO expression system possesses superior yield and purity when compared to the E. coli expression system with respect to the preparation of recombinant antibodies applicable in targeting modules for DDS (DDS-TM). Moreover, a Fab variant prepared in this study demonstrated the potential to be a DDS-TM against HER2-expressing cancer cells. (Keyword) drug delivery system / cancer therapy (Link to Publication Site) ● Publication site (DOI): 10.21873/anticanres.12731 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29970568 ● Summary page in Scopus @ Elsevier: 2-s2.0-85049804969 (DOI: 10.21873/anticanres.12731, PubMed: 29970568, Elsevier: Scopus)
29.	Toshifumi Tomoyasu, Masaki Matoba, Ayuko Takao, Atsushi Tabata, A Robert. Whiley, Nobuko Maeda and Hideaki Nagamune : Rapid screening method for detecting highly pathogenic Streptococcus intermedius strains carrying a mutation in the lacR gene., FEMS Microbiology Letters, Vol.365, No.3, fnx-258, 2018. (Summary) Streptococcus intermedius is a member of the normal human commensal flora and secretes a human-specific cytolysin intermedilysin (ILY) as a major virulence factor. Expression of ily is repressed by LacR and loss-of-function mutations of LacR are observed in many ILY high-producing strains isolated from deep-seated abscesses, suggesting that high ILY production is necessary for increased virulence. However, because ILY exhibits no β-hemolysis on animal blood agar plates, differentiating ILY high- and low-producing strains using conventional laboratory methods is not possible. Interestingly, S. intermedius also produces glycosidases, including MsgA and NanA, which exhibit N-acetyl-β-d-glucosaminidase and neuraminidase activities, respectively. Moreover, MsgA expression, but not NanA, is negatively regulated by LacR. Here we measured the activities of MsgA, NanA and ILY in strains isolated from clinical specimens and dental plaque to determine the correlation between these glycosidase activities and ILY hemolytic activity. Hemolytic activity showed a strong positive correlation with MsgA and a weak negative correlation with NanA activities. Therefore, we calculated the ratio of MsgA and NanA activity (M/N ratio). This value showed a stronger positive correlation (r = 0.81) with ILY hemolytic activity and many strains with high M/N ratios (>2) were ILY-high producers with loss-of-function mutations in LacR. (Keyword) pathogenic microorganism / virulence factor (Tokushima University Institutional Repository) ● Metadata: 115749 (Link to Publication Site) ● Publication site (DOI): 10.1093/femsle/fnx258 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29228148 ● Summary page in Scopus @ Elsevier: 2-s2.0-85056596012 (Tokushima University Institutional Repository: 115749, DOI: 10.1093/femsle/fnx258, PubMed: 29228148, Elsevier: Scopus)
30.	Atsushi Tabata, Douglas Deutsch, Seiya Otsuka, Kathleen Verratti, Toshifumi Tomoyasu, Hideaki Nagamune and A. Vincent Fischetti : A novel plasmid, pSAA0430-08, from Streptococcus anginosus subsp. anginosus strain 0430-08, Plasmid, Vol.95, No.1, 16-27, 2018. (Summary) Mobile genetic elements (MGEs) are the genetic material often involved in the interspecies and intraspecies genetic transduction in bacteria. However, little is known about MGEs in the Anginosus group of streptococci (AGS), one of the streptococcal groups found in the oral cavity of humans. We looked for the presence of MGEs in Streptococcus anginosus subsp. anginosus (SAA), a representative species belonging to AGS, and found a novel plasmid from SAA strain 0430-08. This plasmid was 7038bp and ~31% G/C content which we named pSAA0430-08, and examined its genetic structure and characteristics. Open reading frame (ORF) prediction revealed that pSAA0430-08 was composed of 10 ORFs including a putative plasmid replication protein (ORF1) and a putative toxin-antitoxin system (ORF9 and ORF10). Between ORF10 and ORF 1, four tandem repeats of 22bp each, generally termed as iteron, were also observed. Using variant plasmids of pSAA0430-08, we confirmed that both ORF1 and iteron were necessary for replication in host cells. Interestingly, the region from ORF4 to ORF7 showed homology with a genomic DNA segment of S. gordonii strains. Thus, this plasmid may travel between the different species in Streptococci, i.e., S. gordonii and S. anginosus. (Keyword) pathogenic microorganism / Plasmid (Link to Publication Site) ● Publication site (DOI): 10.1016/j.plasmid.2018.01.002 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29355570 ● Summary page in Scopus @ Elsevier: 2-s2.0-85041495681 (DOI: 10.1016/j.plasmid.2018.01.002, PubMed: 29355570, Elsevier: Scopus)
31.	Tomoko Inubushi, Mayumi Sugimoto, Haruka Kunimi, Haruka Hino, Atsushi Tabata, Naohiro Imura, Shin Abe and Norio Kamemura : Biphenyl increases the intracellular Ca2+ concentration in HL-60 cells, Fundamental Toxicological Sciences, Vol.5, No.3, 99-103, 2018. (Link to Publication Site) ● Publication site (DOI): 10.2131/fts.5.99 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.2131/fts.5.99 (DOI: 10.2131/fts.5.99)
32.	Tatematsu Yohei, Fujita Haruhi, Hayashi Hiroki, Yamamoto Atsushi, Atsushi Tabata, Hideaki Nagamune and Ohkura Kazuto : Effects of the Nonsteroidal Anti-inflammatory Drug Celecoxib on Mitochondrial Function, Biological & Pharmaceutical Bulletin, Vol.41, No.3, 319-325, 2018. (Summary) Nonsteroidal anti-inflammatory drugs (NSAIDs) are widely used to treat inflammation and pain. In the present study, we examined the effects of celecoxib, a cyclooxygenase-2 (COX-2)-selective NSAID, on rat liver mitochondrial function. Celecoxib dose-dependently induced mitochondria swelling, which was not suppressed by cyclosporine A (CsA). The oxygen consumption rate in mitochondria-suspended solution was facilitated by the addition of celecoxib, and its uncoupling activity was observed. Celecoxib also suppressed SF6847-induced uncoupling, and appeared to exert inhibitory effects on the electron transport chain. Celecoxib suppressed the state 3 oxygen consumption rate in the presence of ADP. Protein release from the mitochondrial matrix was detected following the addition of celecoxib, and aldehyde dehydrogenase 2 (ALDH2) and hydroxymethylglutaryl-CoA (HMG-CoA) synthase 2 (HMGCS2) bands were confirmed in a Western blot analysis. On the other hand, protein release of cytochrome C (CytC), which is an inducer of apoptosis, from the intermembrane space was not observed. Celecoxib enhanced the membrane permeability of human erythrocytes and synthesized liposomes dose-dependently. It then induced the membrane-involving mitochondrial swelling and suppressed mitochondrial function. (Keyword) Aldehyde Dehydrogenase, Mitochondrial / Animals / Anti-Inflammatory Agents, Non-Steroidal / Celecoxib / Cell Membrane Permeability / Cyclooxygenase 2 Inhibitors / Dose-Response Relationship, Drug / Electron Transport / Erythrocytes / Hydroxymethylglutaryl-CoA Synthase / In Vitro Techniques / Male / Mitochondria / Mitochondria, Liver / Mitochondrial Swelling / Oxygen Consumption / Rats / Rats, Wistar (Link to Publication Site) ● Publication site (DOI): 10.1248/bpb.b17-00527 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29491208 ● Summary page in Scopus @ Elsevier: 2-s2.0-85050992357 (DOI: 10.1248/bpb.b17-00527, PubMed: 29491208, Elsevier: Scopus)
33.	Toshifumi Tomoyasu, Takahiro Yamasaki, Shinya Chiba, Shingo Kusaka, Atsushi Tabata, Robert A. Whiley and Hideaki Nagamune : Positive- and Negative-Control Pathways by Blood Components for Intermedilysin Production in Streptococcus intermedius., Infection and Immunity, Vol.85, No.9, 1-17, 2017. (Summary) is an opportunistic bacterial pathogen secreting a human-specific cytolysin called intermedilysin (ILY) as a major pathogenic factor. This bacterium can degrade glycans into monosaccharides using two glycosidases, multisubstrate glycosidase A (MsgA) and neuraminidase (NanA). Here, we detected a stronger hemolytic activity mediated by ILY when PC574 was cultured in fetal bovine serum (FBS) than when it was grown in the standard culture medium. FBS-cultured cells also showed higher MsgA and NanA activity, although overproduction of ILY in FBS was undetectable in mutants -null and -null. Addition of purified MsgA and NanA to the FBS resulted in a release of 2.8 mM galactose and 4.3 mM -acetylneuraminic acid; these sugar concentrations were sufficient to upregulate the expression of ILY, MsgA, and NanA. Conversely, when strain PC574 was cultured in human plasma, no similar increase in hemolytic activity was observed. Moreover, addition of human plasma to the culture in FBS appeared to inhibit the stimulatory effect of FBS on ILY, MsgA, and NanA, although there were individual differences among the plasma samples. We confirmed that human plasma contains immunoglobulins that can neutralize ILY, MsgA, and NanA activities. In addition, human plasma had a neutralizing effect on cytotoxicity of toward HepG2 cells in FBS, and a higher concentration of human plasma was necessary to reduce the cytotoxicity of an ILY-high-producing strain than an ILY-low-producing strain. Overall, our data show that blood contains factors that stimulate and inhibit ILY expression and activity, which may affect pathogenicity of . (Keyword) Streptococcus intermedius / intermedilysin / cytolysin / sugar chain / antibody (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.00379-17 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28607101 ● Summary page in Scopus @ Elsevier: 2-s2.0-85027524694 (DOI: 10.1128/IAI.00379-17, PubMed: 28607101, Elsevier: Scopus)
34.	Keiji Murakami, Hiromichi Yumoto, Ayu Murakami, Takashi Amoh, Darija Viducic, Katsuhiko Hirota, Atsushi Tabata, Hideaki Nagamune, Hiroki Kourai, Takashi Matsuo and Yoichiro Miyake : Evaluation of the effectiveness of the potent bis-quaternary ammonium compound, 4,4'-( , -hexametylenedithio) bis (1-octylpyridinium bromide) (4DTBP-6,8) on Pseudomonas aeruginosa., Journal of Applied Microbiology, Vol.122, No.4, 893-899, 2017. (Summary) Quaternary ammonium compounds (QACs), including benzalkonium chloride (BAC) and cetylpyridinium chloride (CPC) are cationic surfactants and have been used widely as general disinfectants in the medical field due to their strong antibacterial effects and low cytotoxicity to human cells. 4,4'-( , -hexametylenedithio) bis (1-octylpyridinium bromide) (4DTBP-6,8) is one of the potent bis-QACs synthesized to improve the antimicrobial activities of mono-QACs such as BAC. This study aimed to assess the effectiveness of 4DTBP-6,8 against Pseudomonas aeruginosa, a prevalent hospital pathogen. The minimum inhibitory concentrations of 4DTBP-6,8, CPC and BAC against P. aeruginosa were measured. 4DTBP-6,8 exhibited strong antibacterial activity. We assessed the bactericidal effects of QACs against P. aeruginosa under certain conditions and their cytotoxicities in human epithelial cells using lactate dehydrogenase (LDH) release. 4DTBP-6,8 exerted excellent bactericidal effects against high concentrations of bacteria, biofilm cells and even in the presence of contaminated proteins. Cellular LDH was not released by the treatment with 4DTBP-6,8. 4DTBP-6,8 exhibited the strongest bactericidal activity against P. aeruginosa among the three QACs tested without any cytotoxicity. The potent bis-QAC, 4DTBP-6,8 has the potential to be an effective disinfectant in preventing hospital infections caused by P. aeruginosa. (Keyword) Anti-Bacterial Agents / Biofilms / Cell Line / Disinfectants / Humans / Niacinamide / Pseudomonas aeruginosa / Pyridinium Compounds (Link to Publication Site) ● Publication site (DOI): 10.1111/jam.13392 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28035713 ● Summary page in Scopus @ Elsevier: 2-s2.0-85013236835 (DOI: 10.1111/jam.13392, PubMed: 28035713, Elsevier: Scopus)
35.	Yuki Kawaguchi, Yohei Tatematsu, Atsushi Tabata, Hideaki Nagamune and Kazuto Ohkura : Cytolytic Activity and Molecular Feature of Cardiotoxin and Cardiotoxin-like Basic Protein: The Electrostatic Potential Field Is an Important Factor for Cell Lytic Activity, Anticancer Research, Vol.35, No.8, 4515-4519, 2015. (Summary) Cardiotoxin (CT) is a well-known cell lytic protein and has been purified from cobra venom. Cardiotoxin-like basic protein (CLBP) has two amino acid insertions and does not exhibit cell lytic activity. The molecular features of these CT family proteins were examined in the present study using molecular modeling and molecular simulation techniques. Molecular models of CT and CLBP were constructed based on the X-ray data of Naja mossambica mossambica CT VII4 (Protein Data Bank ID: 1CDT). The structural features of these models were examined using molecular orbital and electrostatic potential parameters. The stereo-hydrophobicities and molecular torsions of CT and CLBP, which are indexes of structural features, were similar. Electrostatic potential fields (ESP) differed between CT and CLBP and this was considered one of the critical factors in molecular titer. The distribution of ESP fields may affect the cytolytic activity of the CT family. (Keyword) Amino Acid Sequence / Animals / Cobra Cardiotoxin Proteins / Elapidae / Hydrophobic and Hydrophilic Interactions / Models, Molecular / Molecular Sequence Data / Protein Conformation / Sequence Alignment / Static Electricity (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26168495 ● Summary page in Scopus @ Elsevier: 2-s2.0-84939786315 (PubMed: 26168495, Elsevier: Scopus)
36.	Atsushi Tabata, Ohkubo Yukihisa, Natsuki Anyhoji, Keiko Hojo, Toshifumi Tomoyasu, Youhei Tatematsu, Kazuto Ohkura and Hideaki Nagamune : Development of a Sortase A-mediated Peptide-labeled Liposome Applicable to Drug-delivery Systems, Anticancer Research, Vol.35, No.8, 4411-4417, 2015. (Summary) In order to develop an efficient drug-delivery system (DDS), a lipopeptide-loaded liposome that functions as a platform for the transpeptidase reaction mediated by sortase A (SrtA) was constructed and its stability, as well as cell-specific targeting were evaluated in the present study. Several lipopeptides possessing an acceptor peptide sequence (oligoglycine ≥ three residues) or donor peptide sequence (LPETG) for the SrtA-mediated reaction were chemically synthesized and then inserted into the liposome membrane composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and cholesterol (DPPC-Chol-lipo) to obtain the lipopeptide-loaded liposomes. The transpeptidase reaction mediated by recombinant SrtA (His-ΔN59SrtA) was employed to modify the peptide moiety on the liposomal surface using a fluorescently-labeled substrate peptide corresponding to the species of each loaded lipopeptide. Furthermore, lung tumor-binding peptide (LTBP)-labeled liposomes, prepared by this transpeptidase reaction, were investigated for selective targeting to lung cancer cells in vitro. The His-ΔN59SrtA-mediated transpeptidation of fluorescently-labeled peptide on the lipopeptide-loaded DPPC-Chol-lipo was confirmed. The selective targeting of LTBP-labeled liposomes to the lung cancer cell line A549 was also observed in vitro. These results suggest that the labeling of acceptor or donor lipopeptide-loaded liposomes with the transpeptidase SrtA could be a useful method for developing a platform applicable to a cancer-targeting DDS. (Keyword) drug delivery system / liposomes (Tokushima University Institutional Repository) ● Metadata: 117781 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26168480 ● Summary page in Scopus @ Elsevier: 2-s2.0-84939824857 (Tokushima University Institutional Repository: 117781, PubMed: 26168480, Elsevier: Scopus)
37.	Onodera Takefumi, Kuriyama Isoko, Sakamoto Yuka, Kawamura Moe, Kuramochi Kouji, Tsubaki Kazunori, Atsushi Tabata, Hideaki Nagamune and Mizushina Yoshiyuki : 5-O-Acyl plumbagins inhibit DNA polymerase activity and suppress the inflammatory response, Archives of Biochemistry and Biophysics, Vol.573, 100-110, 2015. (Summary) We previously found that vitamin K3 (menadione, 2-methyl-1,4-naphthoquinone) inhibits the activity of human mitochondrial DNA polymerase (pol) γ. In this study, we focused on plumbagin (5-hydroxy-2-methyl-1,4-naphthoquinone), and chemically synthesized novel plumbagins conjugated with C2:0 to C22:6 fatty acids (5-O-acyl plumbagins). These chemically modified plumbagins displayed enhanced mammalian pol inhibition, with plumbagin conjugated to docosahexaenoic acid (C22:6-acyl plumbagin) exhibiting the strongest inhibition of pol λ among the ten 5-O-acyl plumbagins synthesized. C22:6-acyl plumbagin selectively inhibited the activities of mammalian pol species, but did not influence the activities of other pols or DNA metabolic enzymes tested. The inhibition of pol λ, a DNA repair/recombination pol, by these compounds was significantly correlated with both their suppression of lipopolysaccharide (LPS) induced tumor necrosis factor-α (TNF-α) production by mouse RAW264.7 macrophages and the reduction of 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced inflammation in the mouse ear. These data indicate that 5-O-acyl plumbagins act as anti-inflammatory agents by inhibiting mammalian pol λ. These results further suggest that C22:6-acyl plumbagin is a promising anti-inflammatory candidate and that acylation could be an effective chemical modification to improve the anti-inflammatory activity of vitamin K3 derivatives, such as plumbagin. (Keyword) Animals / Anti-Inflammatory Agents / Cell Line / DNA Polymerase beta / Escherichia coli Proteins / Fatty Acids / Gene Knockdown Techniques / Humans / Inflammation / Lipopolysaccharides / Macrophages / Mice / Naphthoquinones / Plant Proteins / Rats / Tetradecanoylphorbol Acetate / Tumor Necrosis Factor-alpha (Link to Publication Site) ● Publication site (DOI): 10.1016/j.abb.2015.02.032 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25748000 ● Summary page in Scopus @ Elsevier: 2-s2.0-84926219634 (DOI: 10.1016/j.abb.2015.02.032, PubMed: 25748000, Elsevier: Scopus)
38.	Kim Hyejin, Atsushi Tabata, Toshifumi Tomoyasu, Ueno Tomomi, Uchiyama Shigeto, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : Estrogen stimuli promote osteoblastic differentiation via the subtilisin-like proprotein convertase PACE4 in MC3T3-E1 cells., Journal of Bone and Mineral Metabolism, Vol.33, No.1, 30-39, 2015. (Summary) Estrogenic compounds include endogenous estrogens such as estradiol as well as soybean isoflavones, such as daidzein and its metabolite equol, which are known phytoestrogens that prevent osteoporosis in postmenopausal women. Indeed, mineralization of MC3T3-E1 cells, a murine osteoblastic cell line, was significantly decreased in medium containing fetal bovine serum treated with charcoal-dextran to deplete endogenous estrogens, but estradiol and these soybean isoflavones dose-dependently restored the differentiation of MC3T3-E1 cells; equal was tenfold more effective than daidzein. These differentiation promoting effects were inhibited by the addition of fulvestrant, which is a selective downregulator of estrogen receptors. Analysis of the expression pattern of bone-related genes by reverse transcription PCR (RT-PCR)/quantitative real-time PCR (qRT-PCR), which focused on responsiveness to the estrogen stimuli, revealed that the transcription of PACE4, a subtilisin-like proprotein convertase, was tightly linked with the differentiation of MC3T3-E1 cells induced by estrogen stimuli. Moreover, treatment with RNAi of PACE4 in MC3T3-E1 cells resulted in a drastic decrease of mineralization in the presence of estrogen stimuli. These results strongly suggest that PACE4 participates in bone formation at least in osteoblast differentiation, and estrogen receptor-mediated stimuli induce osteoblast differentiation through the upregulation of PACE4 expression. (Keyword) osteoblast / PACE4 / Estrogen / Soybean / isoflavone (Link to Publication Site) ● Publication site (DOI): 10.1007/s00774-014-0567-9 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24557631 ● Summary page in Scopus @ Elsevier: 2-s2.0-84893948353 (DOI: 10.1007/s00774-014-0567-9, PubMed: 24557631, Elsevier: Scopus)
39.	Kawaguchi Yuki, Atsushi Tabata, Hideaki Nagamune and Kazuto Ohkura : Molecular Analysis of Streptococcus anginosus-derived SagA Peptides, Anticancer Research, Vol.34, No.8, 4627-4631, 2014. (Summary) SagA1 and SagA2 molecules produced from beta-hemolytic Streptococcus anginosus subsp. anginosus are composed of a leader peptide and a propeptide, and their mature form has hemolytic activity as a well-known Streptococcal peptide toxin, streptolysin. The function of these SagA molecules is thought to be dependent on intra-molecular heterocycle formation. In this study, we examined the heterocycle-involved molecular features of SagA1, SagA2, and S. pyogenes SagA (SPySagA), focusing on their heterocycle formation. Molecular models of SagA1, SagA2, and SPySagA were constructed using a molecular modeling technique. Molecular dynamics and molecular mechanic analyses of the modeled SagA molecules were performed to obtain their energy profiles. Total energy of the modeled SagA1, SagA2, and SPySagA decreased with heterocycle formation, and the border between the leader peptide and propeptide was clearly observed after heterocycle formation. The flexibility of SagA molecules was changed by intramolecular heterocycle formation, and their function (e.g. hemolytic activity) seems to be regulated by structural transition with heterocycle formation. (Keyword) SagA / Streptolysin S / Streptococcus anginosus (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25075110 ● Summary page in Scopus @ Elsevier: 2-s2.0-84908662068 (PubMed: 25075110, Elsevier: Scopus)
40.	Atsushi Tabata, Natsuki Anyoji, Yukimasa Ohkubo, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation on the Reaction Conditions of Staphylococcus aureus Sortase A for Creating Surface-modified Liposomes as a Drug-delivery System Tool, Anticancer Research, Vol.34, No.8, 4521-4527, 2014. (Summary) This study aimed to determine the preferred conditions for the transpeptidase reaction of sortase A from Staphylococcus aureus, for the purpose of creating functional liposomes useful for a drug-delivery system (DDS). His-tagged recombinant sortase A with 59 amino acids deleted from the N-terminus (His-ΔN59SrtA) was prepared using an Escherichia coli expression system. The pH dependency and sorting signal sequence dependency of the transpeptidase reaction of His-ΔN59SrtA were analyzed by monitoring the transfer of model donor-substrates (i.e. His-tagged mutant green fluorescent proteins with a C-terminal LPxTG sorting signal) to model acceptor-beads with a GGGGGC peptide. In addition, using preferred conditions, the sortase A reaction was used to modify liposome surface. The transpeptidase reaction of His-ΔN59SrtA was enhanced under weakly acidic conditions. Transfer efficiency, based on sorting signal recognition by His-ΔN59SrtA, was similar to or higher than that obtained using several substrates with amino acids other than Glu in the sorting signal position "x". Furthermore, liposomes containing GGGGGC peptide-linked dipalmitoylphosphatidylethanolamine were successfully modified using the preferred conditions for His-ΔN59SrtA determined in this study. Preferred conditions for the transpeptidase reaction of His-ΔN59SrtA, especially in a weakly acidic environment to enhance reaction, was established and successfully used to create functional liposomes applicable to DDS. (Keyword) Sortase A (Tokushima University Institutional Repository) ● Metadata: 117782 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25075095 ● Summary page in Scopus @ Elsevier: 2-s2.0-84908660909 (Tokushima University Institutional Repository: 117782, PubMed: 25075095, Elsevier: Scopus)
41.	Hidenori Imaki, Toshifumi Tomoyasu, Naoki Yamamoto, Chiharu Taue, Sachiko Masuda, Ayuko Takao, Nobuko Maeda, Atsushi Tabata, Robert A. Whiley and Hideaki Nagamune : Identification and Characterization of a Novel Secreted Glycosidase with Multiple Glycosidase Activities in Streptococcus intermedius, Journal of Bacteriology, Vol.196, No.15, 2817-2826, 2014. (Summary) Streptococcus intermedius is a known human pathogen and belongs to the anginosus group (S. anginosus, S. intermedius, and S. constellatus) of streptococci (AGS). We found a large open reading frame (6,708 bp) in the lac operon, and bioinformatic analysis suggested that this gene encodes a novel glycosidase that can exhibit β-d-galactosidase and N-acetyl-β-d-hexosaminidase activities. We, therefore, named this protein "multisubstrate glycosidase A" (MsgA). To test whether MsgA has these glycosidase activities, the msgA gene was disrupted in S. intermedius. The msgA-deficient mutant no longer showed cell- and supernatant-associated β-d-galactosidase, β-d-fucosidase, N-acetyl-β-d-glucosaminidase, and N-acetyl-β-d-galactosaminidase activities, and all phenotypes were complemented in trans with a recombinant plasmid carrying msgA. Purified MsgA had all four of these glycosidase activities and exhibited the lowest Km with 4-methylumbelliferyl-linked N-acetyl-β-d-glucosaminide and the highest kcat with 4-methylumbelliferyl-linked β-d-galactopyranoside. In addition, the purified LacZ domain of MsgA had β-d-galactosidase and β-d-fucosidase activities, and the GH20 domain exhibited both N-acetyl-β-d-glucosaminidase and N-acetyl-β-d-galactosaminidase activities. The β-d-galactosidase and β-d-fucosidase activities of MsgA are thermolabile, and the optimal temperature of the reaction was 40°C, whereas almost all enzymatic activities disappeared at 49°C. The optimal temperatures for the N-acetyl-β-d-glucosaminidase and N-acetyl-β-d-galactosaminidase activities were 58 and 55°C, respectively. The requirement of sialidase treatment to remove sialic acid residues of the glycan branch end for glycan degradation by MsgA on human α1-antitrypsin indicates that MsgA has exoglycosidase activities. MsgA and sialidase might have an important function in the production and utilization of monosaccharides from oligosaccharides, such as glycans for survival in a normal habitat and for pathogenicity of S. intermedius. (Keyword) Streptococcus intermedius / glycosidase / multi-substrates glycosidase (Link to Publication Site) ● Publication site (DOI): 10.1128/JB.01727-14 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24858187 ● Summary page in Scopus @ Elsevier: 2-s2.0-84903904703 (DOI: 10.1128/JB.01727-14, PubMed: 24858187, Elsevier: Scopus)
42.	Atsushi Tabata, Yuji Sato, Kentaro Maya, Kota Nakano, Ken Kikuchi, Robert A. Whiley, Kazuto Ohkura, Toshifumi Tomoyasu and Hideaki Nagamune : A streptolysin S homologue is essential for beta-haemolytic Streptococcus constellatus subsp. constellatus cytotoxicit, Microbiology, Vol.160, No.5, 980-991, 2014. (Summary) Streptococcus constellatus is a member of the Anginosus group streptococci (AGS) and primarily inhabits the human oral cavity. S. constellatus is composed of three subspecies: S. constellatus subsp. constellatus (SCC), S. constellatus subsp. pharyngis and the newly described subspecies S. constellatus subsp. viborgensis. Although previous studies have established that SCC contains β-haemolytic strains, the factor(s) responsible for β-haemolysis in β-haemolytic SCC (β-SCC) has yet to be clarified. Recently, we discovered that a streptolysin S (SLS) homologue is the β-haemolytic factor of β-haemolytic Streptococcus anginosus subsp. anginosus (β-SAA), another member of the AGS. Furthermore, because previous studies have suggested that other AGS species, except for Streptococcus intermedius, do not possess a haemolysin(s) belonging to the family of cholesterol-dependent cytolysins, we hypothesized that, as with β-SAA, the SLS homologue is the β-haemolytic factor of β-SCC, and therefore aimed to investigate and characterize the haemolytic factor of β-SCC in the present study. PCR amplification revealed that all of the tested β-SCC strains were positive for the sagA homologue of SCC (sagA(SCC)). Further investigations using β-SCC strain W277 were conducted to elucidate the relationship between sagA(SCC) and β-haemolysis by constructing sagA(SCC) deletion mutants, which completely lost β-haemolytic activity. This loss of β-haemolytic activity was restored by trans-complementation of sagA(SCC). Furthermore, a co-cultivation assay established that the cytotoxicity of β-SCC was clearly dependent on the presence of sagA(SCC). These results demonstrate that sagA(SCC) is the factor responsible for β-SCC β-haemolysis and cytotoxicity. (Keyword) Streptolysin S / Streptococcus constellatus / beta-hemolytic / cytotoxicity (Link to Publication Site) ● Publication site (DOI): 10.1099/mic.0.075580-0 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24600025 ● Search Scopus @ Elsevier (PMID): 24600025 ● Search Scopus @ Elsevier (DOI): 10.1099/mic.0.075580-0 (DOI: 10.1099/mic.0.075580-0, PubMed: 24600025)
43.	Atsushi Tabata, Kazuto Ohkura, Ohkubo Yukimasa, Toshifumi Tomoyasu, Ohkuni Hisashi, Whiley A. Robert and Hideaki Nagamune : The diversity of receptor recognition in cholesterol-dependent cytolysins, Microbiology and Immunology, Vol.58, No.3, 155-171, 2014. (Summary) Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming toxins secreted mainly by pathogenic Gram-positive bacteria. CDCs generally recognize and bind to membrane cholesterol to create pores and lyse target cells. However, in contrast to typical CDCs such as streptolysin O, several atypical CDCs have been reported. The first of these was intermedilysin, which is secreted by Streptococcus intermedius and has human cell-specificity, human CD59 (huCD59) being its receptor. In the study reported here, the diversity of receptor recognition among CDCs was investigated and multi-receptor recognition characteristics were identified within this toxin family. Streptococcus mitis-derived human platelet aggregation factor (Sm-hPAF) secreted by S. mitis strain Nm-65 isolated from a patient with Kawasaki disease was previously shown to hemolyze erythrocytes in a species-dependent manner, its maximum activity being in human cells. In the present study, it was found that Sm-hPAF recognizes both membrane cholesterol and huCD59 as receptors for triggering pore-formation. Moreover, vaginolysin (VLY) of Gardnerella vaginalis showed similar characteristics to Sm-hPAF regarding receptor recognition. On the basis of the results presented here, the mode of receptor recognition of CDCs can be categorized into the following three groups: (i) Group I, comprising typical CDCs with high affinity to cholesterol and no or very little affinity to huCD59; (ii) Group II, including atypical CDCs such as ILY, with no or very little affinity to cholesterol and high affinity to huCD59; and (iii) Group III, which contains atypical CDCs such as Sm-hPAF and VLY with affinity to both cholesterol and huCD59. (Keyword) cytolysin / cholesterol-dependet cytolysin / diversity (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12131 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24401114 ● CiNii @ National Institute of Informatics (CRID): 1520291853530158464 ● Summary page in Scopus @ Elsevier: 2-s2.0-84895562361 (DOI: 10.1111/1348-0421.12131, PubMed: 24401114, CiNii: 1520291853530158464, Elsevier: Scopus)
44.	Toshifumi Tomoyasu, Hidenori Imaki, Sachiko Masuda, Ayumi Okamoto, HyeJin Kim, Richard Waite, Robert Whiley, Ken Kikuchi, Keiichi Hiramatsu, Atsushi Tabata and Hideaki Nagamune : LacR mutations are frequently observed in Streptococcus intermedius and are responsible for increased intermedilysin production and virulence., Infection and Immunity, Vol.81, No.9, 3276-3286, 2013. (Summary) Streptococcus intermedius secretes a human-specific cytolysin, intermedilysin (ILY), which is considered to be the major virulence factor of this pathogen. We screened for a repressor of ily expression by using random gene disruption in a low-ILY-producing strain (PC574). Three independent high-ILY-producing colonies that had plasmid insertions within a gene that has high homology to lacR were isolated. Validation of these observations was achieved through disruption of lacR in strain PC574 with an erythromycin cassette, which also led to higher hemolytic activity, increased transcription of ily, and higher cytotoxicity against HepG2 cells, compared to the parental strain. The direct binding of LacR within the ily promoter region was shown by a biotinylated DNA probe pulldown assay, and the amount of ILY secreted into the culture supernatant by PC574 cells was increased by adding lactose or galactose to the medium as a carbon source. Furthermore, we examined lacR nucleotide sequences and the hemolytic activity of 50 strains isolated from clinical infections and 7 strains isolated from dental plaque. Of the 50 strains isolated from infections, 13 showed high ILY production, 11 of these 13 strains had one or more point mutations and/or an insertion mutation in LacR, and almost all mutations were associated with a marked decline in LacR function. These results strongly suggest that mutation in lacR is required for the overproduction of ILY, which is associated with an increase in pathogenicity of S. intermedius. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / gene expression (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.00638-13 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23798532 ● Summary page in Scopus @ Elsevier: 2-s2.0-84884217618 (DOI: 10.1128/IAI.00638-13, PubMed: 23798532, Elsevier: Scopus)
45.	Kawaguchi Yuki, Atsushi Tabata, Hideaki Nagamune and Kazuto Ohkura : Profiles of ILY, VLY and Sm-hPAF interaction with human CD59, Anticancer Research, Vol.33, No.7, 2901-2904, 2013. (Summary) The molecular features of a new member of the bacterially -derived cytolysin family were examined. In particular, the interactive mechanisms of intermedilysin (ILY), vaginolysin (VLY), and Streptococcus mitis-derived human platelet aggregation factor (Sm-hPAF) with human CD59 (hCD59) were analyzed. Molecular models of VLY and Sm-hPAF were constructed based on X-ray data of ILY (protein data bank ID=1S3R), and their interactive profiles with hCD59 were examined using molecular simulation. Non-binding (NB) energy between ILY and hCD59 was three orders of magnitude higher than the energy between VLY and hCD59. NB energy between Sm-hPAF and hCD59 was similar to that between VLY and hCD59. A hydrogen bond (ILY Arg432-hCD59 Glu76) was observed between ILY and hCD59, and a stronger interaction was formed by flexible adjustment between them. (Keyword) cytolysin / cholesterol / human-specific / intermedilysin / CD59 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23780977 ● Search Scopus @ Elsevier (PMID): 23780977 (PubMed: 23780977)
46.	Atsushi Tabata, Yukimasa Ohkubo, Masato Tamura, Toshifumi Tomoyasu, Kazuto Ohkura and Hideaki Nagamune : Construction of an improved drug delivery system tool with enhanced versatility in cell-targeting., Anticancer Research, Vol.33, No.7, 2905-2910, 2013. (Summary) His-Z-CDC(ss)(IS) was revealed to be an improved DDS tool with enhanced versatility in cell targeting. (Keyword) Carcinoembryonic Antigen / Cell Membrane / Cells, Cultured / cholesterol / Drug Delivery Systems / Fibroblasts / Fluorouracil / Hemolysis / Hep G2 Cells / Humans / Immunoglobulin G / liposomes / Perforin / Protein Transport / Recombinant Fusion Proteins / Staphylococcus aureus (Tokushima University Institutional Repository) ● Metadata: 117783 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23780978 ● Search Scopus @ Elsevier (PMID): 23780978 (Tokushima University Institutional Repository: 117783, PubMed: 23780978)
47.	Atsushi Tabata, Kota Nakano, Kazuto Ohkura, Toshifumi Tomoyasu, Ken Kikuchi, Robert Whiley and Hideaki Nagamune : Novel Twin Streptolysin S-Like Peptides Encoded in the sag Operon Homologue of Beta-Hemolytic Streptococcus anginosus., Journal of Bacteriology, Vol.195, No.5, 1090-1099, 2013. (Summary) Streptococcus anginosus is a member of the anginosus group streptococci, which form part of the normal human oral flora. In contrast to the pyogenic group streptococci, our knowledge of the virulence factors of the anginosus group streptococci, including S. anginosus, is not sufficient to allow a clear understanding of the basis of their pathogenicity. Generally, hemolysins are thought to be important virulence factors in streptococcal infections. In the present study, a sag operon homologue was shown to be responsible for beta-hemolysis in S. anginosus strains by random gene knockout. Interestingly, contrary to pyogenic group streptococci, beta-hemolytic S. anginosus was shown to have two tandem sagA homologues, encoding streptolysin S (SLS)-like peptides, in the sag operon homologue. Gene deletion and complementation experiments revealed that both genes were functional, and these SLS-like peptides were essential for beta-hemolysis in beta-hemolytic S. anginosus. Furthermore, the amino acid sequence of these SLS-like peptides differed from that of the typical SLS of S. pyogenes, especially in their propeptide domain, and an amino acid residue indicated to be important for the cytolytic activity of SLS in S. pyogenes was deleted in both S. anginosus homologues. These data suggest that SLS-like peptides encoded by two sagA homologues in beta-hemolytic S. anginosus may be potential virulence factors with a different structure essential for hemolytic activity and/or the maturation process compared to the typical SLS present in pyogenic group streptococci. (Keyword) Streptococcus / Streptolysin S (Tokushima University Institutional Repository) ● Metadata: 117785 (Link to Publication Site) ● Publication site (DOI): 10.1128/JB.01344-12 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23292771 ● Search Scopus @ Elsevier (PMID): 23292771 ● Search Scopus @ Elsevier (DOI): 10.1128/JB.01344-12 (Tokushima University Institutional Repository: 117785, DOI: 10.1128/JB.01344-12, PubMed: 23292771)
48.	Toshifumi Tomoyasu, Atsushi Tabata, Yoko Ishikawa, Robert Whiley and Hideaki Nagamune : Small heat shock protein AgsA: an effective stabilizer of enzyme activities., Journal of Bioscience and Bioengineering, Vol.115, No.1, 15-19, 2013. (Summary) A small heat shock protein, AgsA, possesses chaperone activity that can reduce the amount of heat-aggregated protein in vivo, and suppress the aggregation of chemical- and heat-denatured proteins in vitro. Therefore, we examined the ability of AgsA to stabilize the activity of several enzymes by using this chaperone activity. We observed that AgsA can stabilize the enzymatic activities of Renilla (Renilla reniformis) luciferase, firefly (Photinus pyralis) luciferase, and β-galactosidase, and showed comparable or greater stabilization of these enzymes than bovine serum albumin (BSA), a well-known stabilizer of enzyme activities. In particular, AgsA revealed better stabilization of Renilla luciferase and β-galactosidase than BSA under disulfide bond-reducing conditions with dithiothreitol. In addition, AgsA also increased the enzymatic performance of β-galactosidase and various restriction enzymes to a comparable or greater extent than BSA. These data indicate that AgsA may be useful as a general stabilizer of enzyme activities. (Keyword) Small heat shock protein / HSP / enzyme (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jbiosc.2012.08.001 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22929984 ● Search Scopus @ Elsevier (PMID): 22929984 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jbiosc.2012.08.001 (DOI: 10.1016/j.jbiosc.2012.08.001, PubMed: 22929984)
49.	Kazuto Ohkura, Yuki Kawaguchi, Atsushi Tabata, Atsushi Yamamoto, Yasuo Shinohara, Hideaki Nagamune and Hitoshi Hori : Molecular Profiles of Cholesterol-dependent Cytolysin Family-derived 11mer Regions, Anticancer Research, Vol.32, No.6, 2343-2346, 2012. (Summary) Cholesterol-dependent cytolysins (CDCs) are secreted from various types of bacteria and are involved in various diseases (e.g. abscess formation). Traditional CDCs has a conserved 11mer region, which is a key structure in membrane recognition. Based on the X-ray data of traditional CDC perfringolysin O (PFO), molecular models of intermedilysin (ILY), pyolysin (PLO), vaginolysin (VLY), and Streptococcus mitis-derived human platelet aggregation factor (Sm-hPAF) were constructed. The 11mer regions of these models were extracted, and their molecular features were analyzed. The dipole moments of these 11mer regions were classified into four types, and their stereo-hydrophobicity (dGW) was different. It was thought that these results influenced the species specificity and membrane recognition of each cytolysin. Traditional CDCs, ILY, PLO, and VLY consisted of four domains (domains 1 to 4). Domain 0 existed on the N-terminal side in Sm-hPAF in addition to these four domains. The 11mer sequence of Sm-hPAF is the same as that of VLY, but Sm-hPAF has slightly different characteristics (e.g. species specificity, membrane recognition, cholesterol dependency) compared to VLY. Dynamic structure analysis of domain 0 might clarify these differences. (Keyword) Amino Acid Sequence / Cytotoxins / Humans / Models, Molecular / Molecular Sequence Data / X-Ray Diffraction (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22641672 ● Search Scopus @ Elsevier (PMID): 22641672 (PubMed: 22641672)
50.	Atsushi Tabata, Yukimasa Ohkubo, Eriko Sakakura, Toshifumi Tomoyasu, Kazuto Ohkura and Hideaki Nagamune : Investigation of a Bacterial Pore-forming Chimera Toxin for Application as a Novel Drug-delivery System Tool, Anticancer Research, Vol.32, No.6, 2323-2330, 2012. (Summary) Cholesterol-dependent cytolysins (CDCs) are pore-forming toxins from Gram-positive bacteria. The aim of this study was to investigate the potential of a CDC, intermedilysin, as a drug-delivery system (DDS) for clinical application. Intermedilysin was modified by the addition of a disulfide bridge to regulate pore formation, by swapping domain 4 to provide cholesterol-binding capacity, and by the introduction of a targeting domain. The resultant chimera protein, His-LTBP-CDC(ss)(IP), was investigated for its use as a DDS tool in vitro. His-LTBP-CDC(ss)(IP) exhibited a regulated pore-forming capacity under reducing conditions. This chimera protein was able to deliver a drug-carrier liposome specifically to the target cell, to be endocytosed into the cell with subsequent release of the components into the cytoplasm. A chimera protein derived from the bacterial pore-forming toxin intermedilysin (His-LTBP-CDC(ss)(IP)) forms the basis for a novel DDS tool. (Keyword) Bacteriocins / Cell Line, Tumor / Drug Delivery Systems / Electrophoresis, Polyacrylamide Gel / Humans / Liposomes / Microscopy, Fluorescence / Recombinant Fusion Proteins (Tokushima University Institutional Repository) ● Metadata: 117784 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22641669 ● Summary page in Scopus @ Elsevier: 2-s2.0-84864557140 (Tokushima University Institutional Repository: 117784, PubMed: 22641669, Elsevier: Scopus)
51.	Toshifumi Tomoyasu, Atsushi Tabata, Hidenori Imaki, Keigo Tsuruno, Aya Miyazaki, Kenji Sonomoto, Robert Whiley and Hideaki Nagamune : Role of Streptococcus intermedius DnaK chaperone system in stress tolerance and pathogenicity, Cell Stress & Chaperones, Vol.17, No.1, 41-55, 2012. (Summary) Streptococcus intermedius is a facultatively anaerobic, opportunistic pathogen that causes purulent infections and abscess formation. The DnaK chaperone system has been characterized in several pathogenic bacteria and seems to have important functions in stress resistance and pathogenicity. However, the role of DnaK in S. intermedius remains unclear. Therefore, we constructed a dnaK knockout mutant that exhibited slow growth, thermosensitivity, accumulation of GroEL in the cell, and reduced cytotoxicity to HepG2 cells. The level of secretion of a major pathogenic factor, intermedilysin, was not affected by dnaK mutation. We further examined the function and property of the S. intermedius DnaK chaperone system by using Escherichia coli ΔdnaK and ΔrpoH mutant strains. S. intermedius DnaK could not complement the thermosensitivity of E. coli ΔdnaK mutant. However, the intact S. intermedius DnaK chaperone system could complement the thermosensitivity and acid sensitivity of E. coli ΔdnaK mutant. The S. intermedius DnaK chaperone system could regulate the activity and stability of the heat shock transcription factor ς(32) in E. coli, although S. intermedius does not utilize ς(32) for heat shock transcription. The S. intermedius DnaK chaperone system was also able to efficiently eliminate the aggregated proteins from ΔrpoH mutant cells. Overall, our data showed that the S. intermedius DnaK chaperone system has important functions in quality control of cellular proteins but has less participation in the modulation of expression of pathogenic factors. (Keyword) Streptococci / molecular chaperone / 病原性 (Link to Publication Site) ● Publication site (DOI): 10.1007/s12192-011-0284-4 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21822788 ● Search Scopus @ Elsevier (PMID): 21822788 ● Search Scopus @ Elsevier (DOI): 10.1007/s12192-011-0284-4 (DOI: 10.1007/s12192-011-0284-4, PubMed: 21822788)
52.	Hisashi Ohkuni, Hideaki Nagamune, Nana Ozaki, Atsushi Tabata, Yuko Todome, Yukino Watanabe, Hidemi Takahashi, Kazuto Ohkura, Hiroki Kourai, Hiromi Ohtsuka, Vincent A. Fischetti and John B. Zabriskie : Characterization of recombinant Streptococcus mitis-derived human platelet aggregation factor, APMIS, Vol.120, No.1, 56-71, 2012. (Summary) We previously purified Streptococcus mitis-derived human platelet aggregation factor (Sm-hPAF) from the culture supernatant of S. mitis strain Nm-65, isolated from the tooth surface of a patient with Kawasaki disease. Here we produced recombinant Sm-hPAF protein (rSm-hPAF) in Escherichia coli, to determine whether rSm-hPAF conserves its platelet aggregation activity. rSm-hPAF precursor (665 amino acids) shows up to 36-56% identity with the family of cholesterol-dependent cytolysins (CDCs), and rSm-hPAF displayed potent hemolytic activity toward mammalian erythrocytes, including human erythrocytes with platelet aggregation activity. The 162-amino acid amino-terminal domain of rSm-hPAF was found in no other CDCs except lectinolysin; this domain is homologous to a portion of pneumococcal fucolectin-related protein. Interestingly, suilysin (SLY) and pneumolysin (PLY) of CDCs also exhibit substantial human platelet aggregation activity, similar to rSm-hPAF, and the platelet aggregation by rSm-hPAF, SLY, and PLY was morphologically confirmed using light and electron microscopy. (Keyword) Adult / Amino Acid Sequence / Animals / Antibodies, Monoclonal / Bacterial Proteins / bacterial toxins / Base Sequence / Blood Platelets / Cell Adhesion Molecules / cholesterol / Cytotoxins / DNA, Bacterial / Female / Genes, Bacterial / Hemolysin Proteins / Humans / L-Lactate Dehydrogenase / Mice / Mice, Inbred BALB C / transmission electron microscopy / Molecular Sequence Data / Mucocutaneous Lymph Node Syndrome / Phylogeny / Platelet Aggregation / Recombinant Proteins / Sequence Homology, Amino Acid / Streptococcus mitis / Streptolysins (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1600-0463.2011.02813.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22151309 ● Search Scopus @ Elsevier (PMID): 22151309 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1600-0463.2011.02813.x (DOI: 10.1111/j.1600-0463.2011.02813.x, PubMed: 22151309)
53.	Heni Susilowati, Hirohiko Okamura, Katsuhiko Hirota, Masayuki Shono, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake : Intermedilysin induces EGR-1 expression through calcineurin/NFAT pathway in human cholangiocellular carcinoma cells., Biochemical and Biophysical Research Communications, Vol.404, No.1, 57-61, 2011. (Summary) (Intermedilysin (ILY) is a cholesterol-dependent cytolysin produced by Streptococcus intermedius, which is associated with human brain and liver abscesses. Although intrahepatic bile duct cells play a valuable role in the pathogenesis of liver abscess, the molecular mechanism of ILY-treated intrahepatic bile duct cells remains unknown. In this study, we report that ILY induced a nuclear accumulation of intracellular calcium ([Ca(2+)]i) in human cholangiocellular cells HuCCT1. We also demonstrate that 10 ng/ml ILY induced NFAT1 dephosphorylation and its nuclear translocation in HuCCT1 cells. In contrast to the result that ILY induced NF-B translocation in human hepatic HepG2 cells, ILY did not affect NF-B localization in HuCCT1 cells. Dephosphorylation and nuclear translocation of NFAT1 caused by ILY were prevented by [Ca(2+)]i calcium chelator, BAPTA/AM, and calcineurin inhibitors, cyclosporine A and tacrolimus. ILY induced early growth response-1 (EGR-1) expression and it was inhibited by the pre-treatment with cyclosporine A, indicating that the calcineurin/NFAT pathway was involved in EGR-1 expression in response to ILY. ILY-induced calcineurin/NFAT1 activation and sequential EGR-1 expression might be related to the pathogenesis of S. intermedius in human bile duct cells.) (Keyword) Bacteriocins / Bile Ducts, Intrahepatic / Calcineurin / calcium / Cell Line, Tumor / Cell Nucleus / Early Growth Response Protein 1 / Humans / NFATC Transcription Factors (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbrc.2010.11.057 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21094139 ● Summary page in Scopus @ Elsevier: 2-s2.0-78650872240 (DOI: 10.1016/j.bbrc.2010.11.057, PubMed: 21094139, Elsevier: Scopus)
54.	Toshifumi Tomoyasu, Atsushi Tabata, Hiroshima Riki, Imaki Hidenori, Masuda Sachiko, Whiley A. Robert, Aduse-Opoku Joseph, Kikuchi Ken, Hiramatsu Keiichi and Hideaki Nagamune : Role of catabolite control protein A in the regulation of intermedilysin production by Streptococcus intermedius., Infection and Immunity, Vol.78, No.9, 4012-4021, 2010. (Summary) Streptococcus intermedius is an opportunistic pathogen of humans that causes purulent infections, including brain and liver abscesses. This pathogen secretes a human-specific cytolysin, intermedilysin, which has been recognized as a major virulence factor. However, most of the expressional control mechanisms of ily are still unknown. To determine these mechanisms, we analyzed the nucleotide sequence of the ily promoter region. We found a highly homologous region to the catabolite-repressible element (cre) in the ily promoter region and observed a considerable decrease in the amount of secreted intermedilysin when cells were grown in a culture medium containing high concentrations of glucose/utilizable carbohydrates. Disruption of the ccpA gene, which encodes catabolite control protein A, did not induce catabolite repression of ily by glucose/utilizable carbohydrates. In cre mutants, catabolite repression of ily was partially restored, and purified catabolite control protein A bound to an oligonucleotide containing the cre consensus sequence in the ily promoter region. In addition, a prolonged lag phase and slower doubling time of the ccpA mutant cells were observed. Our data show that S. intermedius can modulate ily expression and growth rate through catabolite control protein A-mediated monitoring of the extracellular glucose/utilizable carbohydrate concentration. (Keyword) virulence factor (Link to Publication Site) ● Publication site (DOI): 10.1128/IAI.00113-10 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20624907 ● Search Scopus @ Elsevier (PMID): 20624907 ● Search Scopus @ Elsevier (DOI): 10.1128/IAI.00113-10 (DOI: 10.1128/IAI.00113-10, PubMed: 20624907)
55.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Investigation of the chaperone function of the small heat shock protein AgsA., BMC Biochemistry, Vol.11, 27, 2010. (Summary) A small heat shock protein AgsA was originally isolated from Salmonella enterica serovar Typhimurium. We previously demonstrated that AgsA was an effective chaperone that could reduce the amount of heat-aggregated proteins in an Escherichia coli rpoH mutant. AgsA appeared to promote survival at lethal temperatures by cooperating with other chaperones in vivo. To investigate the aggregation prevention mechanisms of AgsA, we constructed N- or C-terminal truncated mutants and compared their properties with wild type AgsA. AgsA showed significant overall homology to wheat sHsp16.9 allowing its three-dimensional structure to be predicted. Truncations of AgsA until the N-terminal 23rd and C-terminal 11th amino acid (AA) from both termini preserved its in vivo chaperone activity. Temperature-controlled gel filtration chromatography showed that purified AgsA could maintain large oligomeric complexes up to 50 degrees C. Destabilization of oligomeric complexes was observed for N-terminal 11- and 17-AA truncated AgsA; C-terminal 11-AA truncated AgsA could not form large oligomeric complexes. AgsA prevented the aggregation of denatured lysozyme, malate dehydrogenase (MDH) and citrate synthase (CS) but did not prevent the aggregation of insulin at 25 degrees C. N-terminal 17-AA truncated AgsA showed no chaperone activity towards MDH. C-terminal 11-AA truncated AgsA showed weak or no chaperone activity towards lysozyme, MDH and CS although it prevented the aggregation of insulin at 25 degrees C. When the same amount of AgsA and C-terminal 11-AA truncated AgsA were mixed (half of respective amount required for efficient chaperone activities), good chaperone activity for all substrates and temperatures was observed. Detectable intermolecular exchanges between AgsA oligomers at 25 degrees C were not observed using fluorescence resonance energy transfer analysis; however, significant exchanges between AgsA oligomers and C-terminal truncated AgsA were observed at 25 degrees C. Our data demonstrate that AgsA has several regions necessary for efficient chaperone activity: region(s) important for lysozyme chaperone activity are located outer surface of the oligomeric complex while those region(s) important for insulin are located inside the oligomeric complex and those for MDH are located within the N-terminal arm. In addition, the equilibrium between the oligomer and the dimer structures appears to be important for its efficient chaperone activity. (Keyword) chaperone (Tokushima University Institutional Repository) ● Metadata: 114744 (Link to Publication Site) ● Publication site (DOI): 10.1186/1471-2091-11-27 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20653971 ● Search Scopus @ Elsevier (PMID): 20653971 ● Search Scopus @ Elsevier (DOI): 10.1186/1471-2091-11-27 (Tokushima University Institutional Repository: 114744, DOI: 10.1186/1471-2091-11-27, PubMed: 20653971)
56.	Fumihiko Namba, Hiroyuki Kitajima, Atsushi Tabata, Masahiro Nakayama, Noriyuki Suehara, Katsura Matsunami, Keiko Yanagihara, Masahiro Nishihara, Akihiro Morita, Minoru Yamada, Akihito Kimoto, Shinya Hirano, Kiyotoshi Sekiguchi, Masanori Fujimura and Itaru Yanagihara : Anti-Annexin A2 IgM Antibody in Preterm Infants: Its Association with Chorioamnionitis, Pediatric Research, Vol.60, No.6, 699-704, 2006. (Summary) Intrauterine infection is associated with chorioamnionitis (CAM), which can lead to preterm delivery. We previously reported that the levels of IgM and the incidence of CAM were elevated in preterm infants with neonatal pulmonary emphysema. The pathogen and target of this IgM remain unclear. By using Western blot and amino acid sequences, we have determined one of the target proteins: annexin A2. Immunohistochemical analysis showed that annexin A2 was expressed at fetal chorion and amnion membranes. Among very low birth weight (VLBW) infants with hyper-IgM (> or = 30 mg/dL), 58.8% showed a high titer against annexin A2 (more than x 16), which accounted for about 20%-40% of the total IgM. Anti-annexin A2 IgM antibody inhibited plasmin generation. Furthermore, the median of anti-annexin A2 IgM titer from preterm infants who were delivered with high-grade (grade III) CAM was significantly higher than those from preterm infants without CAM (p = 0.011) and with low-grade CAM (grade I and II) (p = 0.010). Here, we indicate the fetal autoimmunoreactivity against the fetomaternal interface in preterm infants. (Keyword) Amino Acid Sequence / Annexin A2 / Chorioamnionitis / Female / Fibrinolysin / Humans / Immunoglobulin M / Infant, Newborn / Infant, Premature / Infant, Very Low Birth Weight / Molecular Sequence Data / Placenta / Pregnancy / Pregnancy Complications (Link to Publication Site) ● Publication site (DOI): 10.1203/01.pdr.0000245910.10929.a6 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17065584 ● Search Scopus @ Elsevier (PMID): 17065584 ● Search Scopus @ Elsevier (DOI): 10.1203/01.pdr.0000245910.10929.a6 (DOI: 10.1203/01.pdr.0000245910.10929.a6, PubMed: 17065584)
57.	Atsushi Tabata, Fumihiko Namba, Minoru Yamada, Taeko Hasegawa, Kumiko Nakahira, Daizo Hamada, Hiroyuki Kitajima, Eiichiro Fukusaki and Itaru Yanagihara : Expression and purification of recombinant human annexin A2 in Pichia pastoris and utility of expression product for detecting annexin A2 antibody, Journal of Bioscience and Bioengineering, Vol.101, No.2, 190-197, 2006. (Summary) Annexin A2, a Ca2+-dependent phospholipid binding protein, is abundantly expressed in various human organs, which exists as either a membrane-associated, cytosolic or soluble form in serum. We constructed expression systems for recombinant human annexin A2 (rhA2) using Pichia pastoris. The systems are designed to secrete rhA2 as either the N- or C-terminally His6-tagged form to facilitate purification. Both types of rhA2 were overexpressed, but in the N-terminal-truncated form as revealed from the results of N-terminal amino acid sequencing and Western blotting. Therefore, further purification of N-terminally His6-tagged rhA2 was not feasible because of the removal of the N-terminal His6-tag sequence. C-terminally His6-tagged rhA2 was expressed as either a glycosylated or a nonglycosylated form, and the nonglycosylated form was purified using the combination of nickel-immobilized affinity, concanavalin A and cation exchanged column chromatographies. The solid-phase binding of rhA2 was examined by enzyme-linked immunosorbent assay (ELISA), which revealed the specific reactivity of rhA2 against an anti-annexin A2 monoclonal antibody. These results suggest that the expression system using P. pastoris is useful for the preparation of rhA2 that is applicable to the ELISA detection of the anti-annexin A2 antibody. (Keyword) Amino Acid Sequence / Annexin A2 / Antibodies, Monoclonal / Enzyme-Linked Immunosorbent Assay / Gene Expression Regulation / Histidine / Humans / Molecular Sequence Data / Pichia / Protein Engineering / Recombinant Proteins (Link to Publication Site) ● Publication site (DOI): 10.1263/jbb.101.190 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16569618 ● Search Scopus @ Elsevier (PMID): 16569618 ● Search Scopus @ Elsevier (DOI): 10.1263/jbb.101.190 (DOI: 10.1263/jbb.101.190, PubMed: 16569618)
58.	Atsushi Tabata, Hideaki Nagamune, Takuya Maeda, Keiji Murakami, Yoichiro Miyake and Hiroki Kourai : Correlation between resistance of Pseudomonas aeruginosa to quaternary ammonium compounds and expression of outer membrane protein OprR, Antimicrobial Agents and Chemotherapy, Vol.47, No.7, 2093-2099, 2003. (Summary) 論文題目:緑膿菌の細胞膜タンパク質OprRの発現と第四アンモニウム塩に対する耐性化の相関第四アンモニウム塩系消毒剤に耐性化した緑膿菌において顕著に発現量が増加する約25.6kDaの蛋白質を2次元電気泳動で分離し，そのN末端アミノ酸配列の解析によって，それが外膜蛋白質のOprRであることを明らかとした．またその耐性化株でOprRのノックアウト株を作成したところ，第四アンモニウム塩系消毒剤に対する感受性が野生株と同程度まで上昇することから，OprRがこの消毒薬耐性に重要な役割を果たしていることを示した． (Keyword) Adaptation, Physiological / Amino Acid Sequence / Bacterial Outer Membrane Proteins / Drug Resistance, Bacterial / Gene Deletion / Genes, Bacterial / Molecular Sequence Data / Mutagenesis / Pseudomonas aeruginosa / Quaternary Ammonium Compounds (Tokushima University Institutional Repository) ● Metadata: 117786 (Link to Publication Site) ● Publication site (DOI): 10.1128/AAC.47.7.2093-2099.2003 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12821452 ● Search Scopus @ Elsevier (PMID): 12821452 ● Search Scopus @ Elsevier (DOI): 10.1128/AAC.47.7.2093-2099.2003 (Tokushima University Institutional Repository: 117786, DOI: 10.1128/AAC.47.7.2093-2099.2003, PubMed: 12821452)
59.	Atsushi Tabata, Daxin Zhang, Takuya Maeda, Hideaki Nagamune and Hiroki Kourai : Microbial Contamination in Home Laundry Operations in Japan, Biocontrol Science, Vol.8, No.1, 9-18, 2003. (Summary) 論文題目:日本における家庭洗濯の微生物汚染．家庭洗濯中の衛生レベルは生活様式の変化と共に変遷してきた．諸外国では洗濯中に微生物汚染や感染が報告されている．そこで日本における洗濯中の汚染について様々な着用後の繊維製品に付着している微生物種の同定，洗濯物間の微生物転移による感染の危険性の実態について明らかにした．さらに除菌洗剤と非除菌洗剤を用いて検討し，除菌洗剤の汚染や感染防止効果が高いことを明らかにした． (Keyword) Home laundry / Japan / Microbial contamination / Microbial transmission / Bath water (Tokushima University Institutional Repository) ● Metadata: 117799 (Link to Publication Site) ● Publication site (DOI): 10.4265/bio.8.9 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390001204464267648 ● Search Scopus @ Elsevier (DOI): 10.4265/bio.8.9 (Tokushima University Institutional Repository: 117799, DOI: 10.4265/bio.8.9, CiNii: 1390001204464267648)
60.	Atsushi Tabata, Takuya Maeda, Hideaki Nagamune and Hiroki Kourai : The Properties of Bacterial Adaptation to Mono-and Bis-Quaternary Ammonium Compounds, Biocontrol Science, Vol.8, No.1, 37-42, 2003. (Summary) 論文題目:モノ型およびビス型第四アンモニウム塩に対する細菌の適応の性質．モノ型(デシルピリジニウム塩)およびビス型第四アンモニウム塩(架橋構造がチオール，エステル，カルバモイルおよびアミド)に対する細菌の適応について検討した．最小発育阻止濃度(MIC)測定法により検討した結果，モノ型ではMIC値が上昇し，抵抗性化が見受けられたが，ビス型第四アンモニウム塩では全く耐性化が見られなかった．抵抗性菌の表面疎水性を解析した結果，モノ型の抵抗性化は細胞表面の疎水性が低下したためであるとした． (Keyword) Quaternary ammonium compound / Bis-QAC / Bacterial adaptation / Resistance to disinfectant / Cell surface hydrophobicity (Tokushima University Institutional Repository) ● Metadata: 117798 (Link to Publication Site) ● Publication site (DOI): 10.4265/bio.8.37 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390282679441002368 ● Search Scopus @ Elsevier (DOI): 10.4265/bio.8.37 (Tokushima University Institutional Repository: 117798, DOI: 10.4265/bio.8.37, CiNii: 1390282679441002368)
61.	Atsushi Tabata, Takuya Maeda, Hideaki Nagamune and Hiroki Kourai : Characterization of Pseudomonas aeruginosa Resistant to a Quaternary Ammonium Compound, Biocontrol Science, Vol.7, No.3, 147-153, 2002. (Summary) 論文題目:第四アンモニウム塩化合物に対して薬剤耐性を示す緑膿菌の特徴 N-ドデシルピリジニウムアイオダイドに対する薬剤耐性化を最小濃度測定法である培地希釈法を用いて行うことに成功した．その結果，感受性菌よりも8倍高い耐性化細菌を得ることができた．電子顕微鏡で観察した結果，耐性化細胞は感受性細胞には見られないバイオフィルム様の凝集が観察された．さらに，耐性化した細胞の表面疎水性について測定した結果，感受性細胞よりも親水性化していることがわかった． (Keyword) Quaternary ammonium compound / Pseudomonas aeruginosa / Disinfectant resistance / Cell surface hydrophobicity / Biofilm (Tokushima University Institutional Repository) ● Metadata: 117800 (Link to Publication Site) ● Publication site (DOI): 10.4265/bio.7.147 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390001204463971328 ● Search Scopus @ Elsevier (DOI): 10.4265/bio.7.147 (Tokushima University Institutional Repository: 117800, DOI: 10.4265/bio.7.147, CiNii: 1390001204463971328)

Academic Paper (Unrefereed Paper):

1.	Ogawa Itsuki, Atsushi Tabata, Yukihiro Arakawa, Keiji Minagawa and Fumitoshi Yagishita : Blue Luminescent Boron Complexes Based on N,N-type Bidentate Imidazo[1,2-a]pyridine Ligands, 次世代光フォーラム 2024 in 徳島論文集, Vol.2024, 127-128, 2024.
2.	abe sota, Atsushi Tabata, Yukihiro Arakawa, Keiji Minagawa and Fumitoshi Yagishita : Naphthalene-fused Imidazo[1,2-a]pyridinium Salts Showing Green Emission with High Quantum Yields and Large Stokes Shift, 次世代光フォーラム 2024 in 徳島論文集, Vol.2024, 125-126, 2024.
3.	Fumitoshi Yagishita, Keita Hoshi, Atsushi Tabata, Hideaki Nagamune, Keiji Minagawa and Yasushi Imada : Fluorescent Imidazo[1,2-a]pyridinium Salt for Potent Cancer Therapeutic Agent, Proceedings of the LED General Forum 2021 Tokushima, 155-156, 2021.
4.	Fumitoshi Yagishita, Tanigawa Junichi, Sanagawa Yohei, Okamoto Masaki, Ishihara Kaito, Atsushi Tabata, Hideaki Nagamune, Yasushi Imada and Yasuhiko Kawamura : Fluorescent N-Heteroarene as a DNA Photo-cleaving Agent under the LED Irradiation, LED総合フォーラム2019 in 徳島論文集, Vol.2019, 71-72, 2019.

Proceeding of International Conference:

1.	Mikito Yasuzawa, Sato Yusuke, KIDO Takanari, Zhao Yumeng, Masashi Kurashina, Masao Nagase, Tomoyuki Ueki and Atsushi Tabata : Preparation of Platinum Nanoelectrodes Using Tapered Tungsten Probes and Their Application to a Single Cell Measurement, PRiME 2024 (Pacific rim meeting on electrochemisty and solid state science 2024) , Hawaii, M02-4340, Honolulu, Oct. 2024. (Summary) Platinum nanoelectrodes, which the electroactive region is located on the tip, were prepared in two steps. First, an insulating film was formed on the tapered tungsten probe by electrodeposition coating using the cationic electrodeposition paint, and then platinum nanopillars with a diameter of about 200 nm were formed on the tip using Focused-Ion-Beam Chemical-Vapor-Deposition (FIB-CVD). The conditions for forming an insulating film on tungsten surface with low thickness and excellent insulation properties were investigated and were evaluated by electrochemical measurements and SEM observations, and an appropriate insulating film was successfully produced. After the formation of a platinum pillar on the tip of an insulating film-coated tungsten probe, a platinum nanoelectrode was obtained and confirmed to function as an electrode. Using automatic micro manipulation system, repeated insertion of platinum nanoelectrode into HeLa cell was attempted. The results showed that the insertion of platinum nanoelectrodes into HeLa cells appeared to be successful.
2.	Nakano Kiichi, Zhao Yumeng, Masashi Kurashina, Atsushi Tabata, Hitoshi Matsuki and Mikito Yasuzawa : Preparation of zwitterionic polymer brush surface using optical ATRP method and its inhibitory effect on protein adsorption, International Conference on Advanced Materials Development and Performance 2024 (AMDP 2024), PE59, Tokushima, Sep. 2024. (Summary) Medical devices that are implanted in the body are subject to adsorption reactions of various components, such as proteins and blood cells, by the body's immune defense system. Therefore, it is essential for medical devices that come into contact with bodily fluids to have a surface that inhibits the adsorption of proteins such as fibrinogen, which occurs in the early stages of the immune response. For this purpose, materials with the ability to retain water are considered useful, and polymers such as sulfobetaine methacrylate (SBMA) and phosphorylcholine methacrylate (MPC), which are zwitterionic polymers, are used [1]. On the other hand, the surface-initiated atom transfer radical polymerization (SI-ATRP) method is interesting because it can form dense polymer brushes (PB) on the substrate surface, and furthermore, photo-ATRP, in which the catalyst is regenerated by UV irradiation, can be fabricated in a simple environment because it proceeds even in the presence of oxygen [2]. In this study, zwitterionic PB was prepared on the substrate surface using Photo-ATRP. SBMA and methacrylate 2-(methacryloyloxy)ethyl choline hydrogen phosphate (MCHP), a novel phosphobetaine methacrylate in which the polar groups of MPC is reversed, were used as zwitterionic monomers. Quartz crystal with SiO2 surface (QCM-SiO2) was used as substrate and fibrinogen adsorption behavior was evaluated using the flow quartz crystal microbalance system. Successful PB modification of SBMA and MCHP on QCM-SiO2 were confirmed by XPS. PBS containing fibrinogen was flowed through the system and the change in mass per unit area of the modified surface was measured. The unmodified SiO2 cell adsorbed 240 ng/cm2, while the SBMA-PB-modified surface adsorbed 118 ng/cm2 and the MCHP-PB-modified surface 20 ng/cm2. Thus, protein adsorption was significantly inhibited by both PB modifications, but the inhibitory effect of MCHP-PB modification was superior to that of SBMA-PB modification. [1] S. Nishimura et al., Bull. Chem. Soc. Jpn. 96, 1052 (2023) [2] W.-Q. Yan et al., Macromolecules 53, 8, 2801 (2020)
3.	Tsai YuanChih, SHIMAHARA Hisui, Zhao Yumeng, Nakano Kiichi, Masashi Kurashina, Atsushi Tabata, Hitoshi Matsuki, Mikito Yasuzawa and Bai MengYi : The in vitro evaluations of photo-curing 2-(methacryloyloxy)ethyl choline hydrogen phosphate bio-printing scaffold, International Conference on Advanced Materials Development and Performance 2024 (AMDP 2024), PE58, Tokushima, Sep. 2024. (Summary) Patients who require tooth extraction due to trauma, severe periodontal disease, or caries often have the bone defect repaired before receiving future restorations or dental implants. However, such procedures frequently need the use of bone graft powder and/or other materials to promote bone cell proliferation and prevent epithelial cells from migrating prematurely into the defect, putting physicians' skills and techniques to the test. Medical imaging and bioprinting technologies enable the customization of bone scaffolds prior to surgery, which is anticipated to reduce the surgery time and help with estimating the quantity of implant material necessary. 2-methacryloyloxyethyl phosphorylcholine (MPC) is a biocompatible phosphocholine structure with minimal cytotoxicity. Based on the abovementioned features, we further modified its structures to synthesize a novel chemical, i.e., 2-(methacryloyloxy)ethyl choline hydrogen phosphate (MCHP), which phosphocholine structure is translocated, allowing for a wider range of uses. In this study, we combined this material with calcium triphosphate and a photoinitiator to produce a photocurable bioink. In vitro investigations using various bioinks with varying formula ratios revealed that this material is also showing biocompatible and has no significant cytotoxic properties toward cell lines. It also demonstrated a plausible microenvironment for cultured osteoblasts (OB) to differentiation growth, indicating promise for bone regeneration and therapeutic uses in patients with bone abnormalities in the future.
4.	OGAWA Itsuki, Shoko Ueta, Tetsuro Katayama, Akihiro Furube, Atsushi Tabata, Keiji Minagawa and Fumitoshi Yagishita : Synthesis of Boron Complexes Based on N,N-Type Bidentate Imidazopyridine Ligands and Evaluation of Their Photophysical Properties, 10th International Conference on Advanced Materials Development and Performance, Sep. 2024.
5.	Akihiro Shirai, Ami Tanaka and Atsushi Tabata : Influences of light-irradiation wavelength and irradiance on growth and deoxynivalenol production in Fusarium graminearum, ASM Microbe 2024, Vol.4247, No.MBP-FRIDAY-610, Atlanta, Jun. 2024.
6.	Nakai Hiroki, Akiyama Daiu, Taniguchi Yoshiaki, Kishinobu Iori, Ikeda Takuya, Atsushi Tabata, Hideaki Nagamune, Yasuhide Ohno and Masao Nagase : Protein detection by electron donor using epitaxial graphene film on SiC substrate, 33rd International Microprocesses and Nanotechnology Conference (MNC2020), No.2020-21-12, Online, Nov. 2020.
7.	Fumitoshi Yagishita, Sanagawa Yohei, Tanigawa Jun-ichi, Nii Chiho, Atsushi Tabata, Hideaki Nagamune, Yasushi Imada and Yasuhiko Kawamura : Synthesis of Water-Soluble Fluorescent N-Heteroarenes And Its Applications, 18th International Symposium on Novel Aromatic Compounds (ISNA-18), Jul. 2019.
8.	Yamada Takuya, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Response of human cells against peptide type hemolysin Streptolysin S derived from Streptococcus anginosus subsp. anginosus, International Peptide Symposium, Dec. 2018. (Keyword) Streptococcus / cytolysin / peptide
9.	Tang Qing, Masayoshi Onitsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Characterizatio of anti-HER2 scFv and Fab as a targeting module for novel drug-delivery system against HER2-positive cancer, 24th IUBMB congress & 15th FAOBMB congress, Seoul, Korea, Jun. 2018.
10.	Toshifumi Tomoyasu, Atsushi Tabata, Chiba Shinya, Yamasaki Takahiro, Kusaka Shingo, Takeda Nozomi, Tamaoka Masaaki, Kazuto Ohkura, Whiley A. Robert and Hideaki Nagamune : Positive and negative control mechanisms of pathogenicity expression in Streptococcus intermedius, Lancefield International Symposium on Streptococci and Streptococcal Diseases, Denarau Island Fiji, Oct. 2017. (Keyword) pathogenic microorganism / bacterial toxins / immunity
11.	Atsushi Tabata, Deutsch Douglas, Otsuka Seiya, Verratti Kathleen, Toshifumi Tomoyasu, Hideaki Nagamune and Fischetti A. Vincent : Characterization of a novel plasmid discovered in a clinical isolate of Streptococcus anginosus subsp. anginosus, Lancefield International Symposium on Streptococci and Streptococcal Diseases, Denarau Island Fiji, Oct. 2017. (Keyword) pathogenic microorganism / plasmid
12.	Toshifumi Tomoyasu, Shinya Chiba, Takahiro Yamasaki, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Expression control pathways of ily by blood components in Streptococcus intermedius, The 13th Korea - Japan International Symposium on Microbiology (XIII-KJISM), May 2016. (Keyword) cytolysin / sugar / antibody / Streptococcus
13.	Hideaki Nagamune, Atsushi Tabata, Yoshitoshi Ogura and Tetsuya Hayashi : Diversity in genome structure showing the genomic dynamism of human-derived Streptococcus mitis, International Symposium on Genome Science 2015: Expanding Frontiers of Genome Science II, Jan. 2015. (Keyword) Streptococcus mitis / genome science
14.	Hideaki Nagamune, Toshifumi Tomoyasu, Hidenori Imaki, Naoki Yamamoto, Chiharu Taue, 増田早智子, 高尾亞由子, 前田伸子, Atsushi Tabata and Whiley A. Robert : CHARACTERIZATION OF A NOVEL SECRETED GLYCOSIDASE WITH MULTIPLE GLYCOSIDASE ACTIVITIES, MSGA: A CANDIDATE KEY ENZYME REGULATING GROWTH AND PATHOGENICITY OF STREPTOCOCCUS INTERMEDIUS, XIX Lancefield International Symposium on Streptococci and Streptococcal Diseases, Nov. 2014. (Keyword) Streptococcus / enzyme / gene expression / cytolysin
15.	Atsushi Tabata, Kota Nakano, Yuji Sato, Kentaro Maya, Hiromi Ohtani, Yukimasa Ohkubo, Kazuto Ohkura, Ken Kikuchi, Robert A Whiley, Toshifumi Tomoyasu and Hideaki Nagamune : STREPTOLYSIN S HOMOLOGUES OF PEPTIDE HEMOLYSIN: NOVEL BETA-HEMOLYTIC FACTORS DISTRIBUTED AMONG BETA-HEMOLYTIC ANGINOSUS GROUP STREPTOCOCCI, XIX Lancefield International Symposium on Streptococci and Streptococcal Diseases, Buenos Aires, Argentina, Nov. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor
16.	Yukihiro Nishikawa, Atsushi Tabata, Toshifumi Tomoyasu, Momoyo Azuma, Yasuhiko Nishioka, Saburo Sone and Hideaki Nagamune : Triple fusion PCR immunochromatography for a rapid and simple diagnosis of penicillin-resistant Streptococcus pneumoniae, IUMS 2011 Sapporo Congress, Sapporo, Japan, Sep. 2011. (Keyword) Streptococci / antibiotics / clinical laboratory testing
17.	Kota Nakano, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation of the novel cytotoxic factor secreted from streptococcus anginosus, IUMS 2011 Sapporo Congress, Sapporo, Sep. 2011.
18.	Hidenori Imaki, Toshifumi Tomoyasu, Sachiko Masuda, Atsushi Tabata and Hideaki Nagamune : Molecular and phenotypic analysis of mutants of ily expressional control factors in Streptococcus intermedius, IUMS 2011 Sapporo Congress, Palermo, Italy, Sep. 2011. (Keyword) Streptococci / cytolysin / gene expression
19.	Atsushi Tabata, Yasuhiro Yamamoto, Ayuko Takao, Toshifumi Tomoyasu, Ayako Nakayama, Nobuko Maeda, Hisashi Ohkuni and Hideaki Nagamune : Investigation of pathogenic properties of cholesterol-dependent cytolysin producing Streptococcus mitis, XVIII Lancefield International Symposium, Palermo, Italy, Sep. 2011. (Keyword) Streptococci / cytolysin
20.	Toshifumi Tomoyasu, Sachiko Masuda, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : Genetic screening of ily expression control factors in Streptococcus intermedius, XVIII Lancefield International Symposium, Palermo, Italy, Sep. 2011. (Keyword) Streptococci / cytolysin / gene expression
21.	Susilowati Heni, Hirohiko Okamura, Katsuhiko Hirota, Kaya Yoshida, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake : Nuclear Translocation of NF-kB induced by Streptococcus intermedius intermedilysin, International Conference of Indonesian Society for Microbiology: Recent advances of Microbiology in Health, Agriculture, Bioindustry, Surabayai, Nov. 2009.
22.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functions of DnaK chaperone system in Streptococcus intermedius, Cell Stress Society International, Sapporo, Oct. 2009. (Keyword) pathogenic microorganism / virulence factor
23.	Susilowati Heni, Hirohiko Okamura, Katsuhiko Hirota, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake : The molecular mechanism for Streptococcus intermedius intermedilysin-induced cell death inhuman cholangiocellular carcinoma cells, International Joint Symposium Frontier in Biomedical Sciences: From Genes to Applications, Yogyakarta, Nov. 2008.
24.	Atsushi Tabata, Shizuka Saito, Eriko Sakakura, Yuki Shinohara, Soichiro Miyoshi, Kou Fukushima, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : Streptococcus mitis-derived human platelet aggregation factor is a novel type of cholesterol-dependent cytolysin that recognizes dual receptors, cholesterol and human CD59., XVII Lancefield International Symposium on Streptococci & Streptococcal Diseases, Porto Heli, Greece, Jun. 2008.
25.	Heni Susilowati, Katsuhiko Hirota, Hirohiko Okamura, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake : Intermedilysin induces cell death in HepG2 cells, 21st International Association for Dental Research - South East Asia Division, Bali, Indonesia, Sep. 2007.
26.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Function of DnaK in Streptococcus intermedius, Cell Stress Society International, Budapest, Aug. 2007. (Keyword) Streptococcus / Chaperon / DnaK
27.	Heni Susilowati, Katsuhiko Hirota, Hirohiko Okamura, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake : The mechanisms of Intermedilysin to induce cell death on HepG2 and HuCCT1 cell lines, The 1st international symposium and workshop ''The Future Direction of Oral Sciences in the 21st century'', Awajishima, Mar. 2007.
28.	Atsushi Tabata, Akiko Inubushi, Toshifumi Tomoyasu and Hideaki Nagamune : Immunochemical analysis of a human specific cytolysin, intermedilysin, for elucidation of its mode of action to human cells, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
29.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Small heat shock protein ``AgsA'' suppresses aggregation of heat denatured proteins., 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.

Proceeding of Domestic Conference:

1.	YUMENG ZHAO, NAKANO Kiichi, Masashi Kurashina, Atsushi Tabata, Hitoshi Matsuki and Mikito Yasuzawa : Preparation of biocompatible surface using a new phosphobetaine monomer, 日本バイオマテリアル学会シンポジウム2024, 2P-002, Oct. 2024.
2.	細野小次郎, 田中彩水, Atsushi Tabata and Akihiro Shirai : Gibberella zeaeのデオキシニバレノール生合成およびその関連遺伝子に及ぼす光照射の影響, 日本防菌防黴学会第51回年次大会要旨集, No.2P-Ca18, 139, Sep. 2024.
3.	ABE Sota, Shoko Ueta, Tetsuro Katayama, Akihiro Furube, Atsushi Tabata, Keiji Minagawa and Fumitoshi Yagishita : ナフタレン縮環イミダゾ[1,2-a]ピリジニウム塩の合成と光機能性評価, 2024年光化学討論会, Sep. 2024.
4.	OGAWA Itsuki, Shoko Ueta, Tetsuro Katayama, Akihiro Furube, Atsushi Tabata, Keiji Minagawa and Fumitoshi Yagishita : Photophysical Properties of Boron Complexes Based on N,N-Type Imidazopyridine-Indole Ligands and Their Application as Photofunctional Materials, 2024年光化学討論会, Sep. 2024.
5.	Hiroshi Takashima, Hiromu Matsumura, Yasuhide Ohno, Masao Nagase, Atsushi Tabata and Hideaki Nagamune : 抗体配向修飾SiC上グラフェン膜を用いた蛍光・電気測定による標的検出, 2024年度応用物理・物理系学会中国四国支部合同学術講演会, Vol.Fp-7, Jul. 2024.
6.	Hiromu Matsumura, Yusuke Mori, Hiroshi Takashima, Yasuhide Ohno, Masao Nagase, Tung Anh Hoang, Atsushi Tabata and Hideaki Nagamune : HisタグB-domainを用いたSiC上グラフェンへの抗体配向修飾法, 2024年第71回応用物理学会春季学術講演会, Vol.24a-1BM-7, Mar. 2024.
7.	ABE Sota, Shoko Ueta, Atsushi Tabata, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : ナフタレン縮環イミダゾ[1,2-a]ピリジニウム塩の合成と光物性評価, 日本化学会第104春季年会, Mar. 2024.
8.	PARK SOJEONG, Ryuta Umebayashi, Atsushi Tabata, Yukihiro Arakawa, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : サブフタロシアニン誘導体の合成と光細胞傷害性評価, 2023年日本化学会中国四国支部大会山口大会, Nov. 2023.
9.	YAMAMORI Yugo, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Streptococcus anginosusが産生するStreptolysin Sに対する宿主細胞応答のメカニズム, 第96回日本生化学会大会, Nov. 2023. (Keyword) レンサ球菌 / cytolysin
10.	AOYAMA Rina, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有する新規細胞壁アンカータンパク質の機能解析, 第76回日本細菌学会支部総会, Oct. 2023. (Keyword) レンサ球菌 / extracellular matrix
11.	Atsushi Tabata, YOKOHATA Shuto, Kazuto Ohkura, Toshifumi Tomoyasu and Hideaki Nagamune : レンサ球菌が産生するペプチド溶血毒素ストレプトリジンSの血清アルブミンによる活性保護, 第69回トキシンシンポジウム, Sep. 2023. (Keyword) レンサ球菌 / cytolysin
12.	YAMAMORI Yugo, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Streptococcus anginosus が産生する Streptolysin S に対する宿主細胞応答のメカニズム, 第69回トキシンシンポジウム, Sep. 2023. (Keyword) レンサ球菌 / cytolysin / 宿主細胞応答
13.	松本愛理, 大貝悠一, Atsushi Tabata, Tomoko Sumitomo and 中田匡宣 : ミティス群レンサ球菌における細胞外小胞の産生とその作用特性, 第75回九州微生物研究フォーラム2023, Sep. 2023.
14.	田中彩水, Atsushi Tabata and Akihiro Shirai : Fusarium graminearumの生育とデオキシニバレノール生合成に及ぼす光波長と照度の影響, 日本防菌防黴学会第50回年次大会要旨集, No.2P-Dp05, 200, Aug. 2023.
15.	Yoshihiko Ueno, Yosuke Seki, Takefumi Hattori, Atsushi Tabata, Rie Mukai, Naohiro Oka and Yoshihiro Uto : B学部における学校推薦型選抜Ⅰ地方創生型(地域産業振興枠)の設計と実施 ―入試業務効率化に向けた新たな取り組みを踏まえて―, 令和5年度全国大学入学者選抜研究連絡協議会大会(第18回), May 2023.
16.	OHOKA Keichiroh, Atsushi Tabata, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : Induction of cytokine gene expression in human cell line depending on N-terminal domain of Sm-hPAF, 第96回日本細菌学会総会, Mar. 2023. (Keyword) レンサ球菌 / ヒト血小板凝集因子 / cytolysin / 細胞応答
17.	YOKOHATA Shuto, Kazuto Ohkura, Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Human serum albumin stabilizes streptolysin S secreted by streptolysin S-producing streptococci, 第96回日本細菌学会総会, Mar. 2023. (Keyword) ヒト血清アルブミン / 細胞傷害 / cytolysin
18.	OKAMOTO Ryota, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functional analysis of DnaK chaperone system in Brevibacillus brevis, 第96回日本細菌学会総会, Mar. 2023. (Keyword) Brevibacillus / molecular chaperone / DnaK / グラム陽性菌
19.	Atsushi Tabata, Airi Matsumoto, Ai Fujimoto, Toshifumi Tomoyasu, 髙尾亜由子, Hisashi Ohkuni and Hideaki Nagamune : Molecular characteristics of novel 5-domain type cholesterol-dependent cytolysin, discoidinolysin, 第96回日本細菌学会総会, Mar. 2023. (Keyword) レンサ球菌 / cytolysin / 分子特性
20.	YAMAMORI Yugo, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Mechanism of cellular response to Streptolysin S produced by Streptococcus anginosus, 第96回日本細菌学会総会, Mar. 2023. (Keyword) レンサ球菌 / cytolysin / 細胞応答
21.	TAKESHITA Ryoya, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 肺がん細胞指向性DDS ツールの作製に向けたリガンド分子の構築, 第146回徳島生物学会, Jan. 2023. (Keyword) 肺がん / DDS ツール / cancer therapy
22.	Yusuke Mori, Hiromu Matsumura, Keita Murayama, Ryoya Takeshita, Anh Hoang Tung, Yasuhide Ohno, Masao Nagase, Atsushi Tabata and Hideaki Nagamune : His-tag 法を用いた SiC 上グラフェンへの抗体配向修飾技術, 第39回「センサ・マイクロマシンと応用システム」シンポジウム, Vol.16P2-P-52, Nov. 2022.
23.	TAKEZAWA Kohji, Atsushi Tabata, Hideaki Nagamune and Toshifumi Tomoyasu : Development and evaluation of a novel micelle-based DDS tool for cancer therapy, 第95回日本生化学会大会, Nov. 2022. (Keyword) ミセル / DDS / cancer therapy
24.	Atsushi Tabata, Airi Matsumoto, Ai Fujimoto, IKEDA Takuya, Toshifumi Tomoyasu, 髙尾亜由子, Hisashi Ohkuni and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の分子特性と病原性への寄与, 第52回レンサ球菌研究会, Jul. 2022. (Keyword) レンサ球菌 / コレステロール依存性細胞溶解毒素 / 病原性
25.	SHIMIZU Tohya, Toshifumi Tomoyasu, TADA Yuya, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有する細胞壁アンカー型エンド-β-N-アセチルグルコサミニダーゼの機能解析, 第52回レンサ球菌研究会, Jul. 2022. (Keyword) レンサ球菌 / 糖鎖 / エンド-β-N-アセチルグルコサミニダーゼ
26.	Atsushi Tabata, YOKOHATA Shuto, Toshifumi Tomoyasu and Hideaki Nagamune : レンサ球菌が産生するペプチド溶血毒素ストレプトリジンSに対するTHP-1の応答反応, 第63回日本生化学会中国四国支部例会, May 2022. (Keyword) レンサ球菌 / 溶血毒素 / 病原性
27.	Atsushi Tabata : Diversity of β-hemolysins produced by opportunistic streptococci and their pathogenic contribution, 第95回日本細菌学会総会, Mar. 2022.
28.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functional analysis of a novel cell wall-anchored glycosidase of Streptococcus intermedius, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / グリコシダーゼ / 糖タンパク質 / 糖鎖
29.	ODA Hiroki, Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : Production and molecular characterization of mitilectin homolog derived from S. mitis, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / cytolysin / 宿主細胞定着因子
30.	YOKOHATA Shuto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Characterization of β-hemolysin produced by Streptococcus phocae, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / cytolysin / ストレプトリジンS / 細胞障害性
31.	KUBO Momoka, Atsushi Tabata, IKEDA Takuya, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : Response of human macrophage-like cells to pore-forming toxin produced by S. mitis clinical isolate, 第95回細菌学会総会, Mar. 2022. (Keyword) Streptococci / 川崎病 / cytolysin / inflammatory cytokine
32.	YOKOHATA Shuto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus phocae が産生するβ溶血因子の作用特性と病原性への寄与, 第74回⽇本細菌学会中国・四国⽀部総会, Oct. 2021. (Keyword) Streptococci / cytolysin / ストレプトリジンS / コレステロール依存性細胞溶解毒素
33.	Kohki Tahara, Masami Itaya, Atsushi Tabata, Hideaki Nagamune, Tetsuro Katayama, Akihiro Furube, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : イミダゾ[1,5-a]ピリジン三座配位子-ホウ素錯体の合成および構造と光物性評価, 2021年光化学討論会, Sep. 2021.
34.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Genetic analysis of the type VII secretion system of Streptococcus intermedius, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / Type VII輸送装置 / 病原性
35.	MIKI Haruka, Atsushi Tabata, 菊池賢, LIU HANYU, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation on the cytotoxicity of a cholesterol-dependent cytolysin derived from Gemella bergeri, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / cytolysin / 細胞障害性
36.	Atsushi Tabata, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : Potential pathogenicity of S. mitis strain Nm-65 based on the complete genomic information, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / virulence factor / ゲノム情報
37.	ICHIJOH Ayu, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Purification of cell wall-anchored proteins of Streptococcus intermedius, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / extracellular matrix / 細胞壁アンカータンパク質
38.	IKEDA Takuya, Atsushi Tabata, Toshifumi Tomoyasu, 高尾亜由子, Hisashi Ohkuni and Hideaki Nagamune : Dual host cell-binding characteristics of the 5-domain-type CDC with N-terminal extra-domain derived from S. mitis, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / cytolysin / N末追加ドメイン
39.	SHIRAI Rina, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Investigation of the cellular response in THP-1 against Streptolysin S produced by S. anginosus, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / cytolysin / 免疫担当細胞
40.	Airi Matsumoto, Atsushi Tabata, Kazuto Ohkura, Chihiro Kodama, Hisashi Ohkuni, 高尾亞由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : Molecular characteristics of an adhesion molecule containing cholesterol-dependent cytolysin-motif produced by Mitis group streptococci, 第94回日本細菌学会総会, Mar. 2021. (Keyword) レンサ球菌 / 細胞接着分子
41.	Fumitoshi Yagishita, Shota Kunimi, Keita Hoshi, Masaki Okamoto, Atsushi Tabata, Hideaki Nagamune, Eiji Hase, Keiji Minagawa and Yasushi Imada : 多光子励起可能なイミダゾ[1,2-a]ピリジニウム塩の合成と光細胞傷害性, 日本化学会第101春季年会, Mar. 2021.
42.	Kazuma Kusumoto, Hiroki Takanari, Atsushi Tabata, Hideaki Nagamune, Yukihiro Arakawa, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : D-π-A型ベンゾチアゾール誘導体の合成と光機能性, 2020年日本化学会中国四国支部大会島根大会, Nov. 2020.
43.	Airi Matsumoto, Atsushi Tabata, 高尾亜由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : ミチス群レンサ球菌が産生するコレステロール依存性細胞溶解毒素様の細胞接着分子の特性, 第73回日本細菌学会中国・四国支部総会, Oct. 2020.
44.	Kazuma Kusumoto, Yohei Sanagawa, Eiji Hase, Hiroki Takanari, Atsushi Tabata, Hideaki Nagamune, Yukihiro Arakawa, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : 多光子励起を目指したA-D-A型N-へテロアレーン類のデザインと応用, 2020年web光化学討論会, Sep. 2020.
45.	Ryuta Umebayashi, Masaki Okamoto, Eiji Hase, Hiroki Takanari, Atsushi Tabata, Hideaki Nagamune, Yukihiro Arakawa, Keiji Minagawa, Yasushi Imada and Fumitoshi Yagishita : 多光子励起可能な水溶性イミダゾ[1,2-a]ピリジニウム塩の合成とミトコンドリアイメージング, 2020年web光化学討論会, Sep. 2020.
46.	Airi Matsumoto, Atsushi Tabata, Kazuto Ohkura, Chihiro Kodama, Hisashi Ohkuni, 高尾亞由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : ミチス群レンサ球菌が産生するコレステロール依存性細胞溶解毒素モチーフを持つ細胞接着分子の特性, 第15回細菌学若手コロッセウム, Aug. 2020. (Keyword) レンサ球菌 / 細胞接着分子
47.	Atsushi Tabata, Kazuto Ohkura, Hisashi Ohkuni, Miho Kobayashi, Airi Matsumoto, Toshifumi Tomoyasu and Hideaki Nagamune : The structural and functional diversity of cholesterol-dependent cytolysin produced from Streptococci, 第20回日本蛋白質科学会年会, Jul. 2020.
48.	Airi Matsumoto, Atsushi Tabata, 高尾亞由子, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : Cholesterol-dependent cytolysin-like adhesion protein of Mitis group streptococci, 第20回日本蛋白質科学会年会, Jul. 2020.
49.	Fumitoshi Yagishita, Junichi Tanigawa, Masaki Okamoto, Eiji Hase, Hiroki Takanari, Atsushi Tabata, Hideaki Nagamune, Takeo Minamikawa, Takeshi Yasui, Yasushi Imada and Yasuhiko Kawamura : Synthesis of Imidazopyridinium Salts Having Potential Application as Image-guided Photodynamic Therapy Agents, The 100th CSJ Annual Meeting, Mar. 2020.
50.	Atsushi Tabata : アンギノーサス群レンサ球菌が産生するペプチド溶血毒素Streptolysin Sの特徴と細胞障害性, 第93回日本細菌学会総会, Feb. 2020.
51.	Toshifumi Tomoyasu, Mari Deguchi, Atsushi Tabata, 髙尾亞由子, 前田伸子 and Hideaki Nagamune : Streptococcus intermediusのヒアルロニダーゼ発現制御機構についての解析, 第93回日本細菌学会総会, Feb. 2020. (Keyword) ヒアルロニダーゼ / gene expression / Streptococci
52.	Airi Matsumoto, Atsushi Tabata, 髙尾亞由子, 菊池賢, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : ミチス群レンサ球菌が産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第93回日本細菌学会総会, Feb. 2020. (Keyword) 細胞接着因子 / Streptococci / cytolysin
53.	Chihiro Kodama, Atsushi Tabata, Toshifumi Tomoyasu, 髙尾亞由子, 前田伸子 and Hideaki Nagamune : S. infantisが産生するコレステロール依存性細胞溶解毒素infantilysinの特性解析, 第93回日本細菌学会総会, Feb. 2020. (Keyword) cytolysin / cholesterol / Streptococci
54.	Fumitoshi Yagishita, Masaki Okamoto, Hiroki Takanari, Eiji Hase, Atsushi Tabata, Hideaki Nagamune, Yasushi Imada, Takeshi Yasui and Yasuhiko Kawamura : ミトコンドリアイメージングを可能とするイミダゾ[1,2-a]ピリジニウム塩の合成, 2019年日本化学会中国四国支部大会徳島大会, Nov. 2019.
55.	Fumitoshi Yagishita, Junichi Tanigawa, Chiho Nii, Atsushi Tabata, Hideaki Nagamune, Hiroki Takanari, Yasushi Imada and Yasuhiko Kawamura : 光線力学療法への応用を狙いとしたイミダゾ[1,5-a]ピリジニウム塩の合成, 2019年日本化学会中国四国支部大会徳島大会, Nov. 2019.
56.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第92回日本生化学会大会, Sep. 2019. (Keyword) 細胞接着 / レンサ球菌 / virulence factor
57.	Toshifumi Tomoyasu, Akiko Tominaga, Mari Deguchi, Eri Arimoto, Atsushi Tabata, 高尾亞由子, 前田伸子 and Hideaki Nagamune : Streptococcus intermedius が分泌する病原因子の特性解析, 第66回トキシンシンポジウム, Sep. 2019. (Keyword) cytolysin / ヒアルロニダーゼ / レンサ球菌
58.	Fumitoshi Yagishita, Ryuta Umebayashi, Masaki Okamoto, Atsushi Tabata, Hideaki Nagamune, Hiroki Takanari, Yasushi Imada and Yasuhiko Kawamura : D-π-A 型イミダゾ [1,2-a] ピリジニウム塩の合成とミトコンドリアイメージングへの応用, 2019年光化学討論会, Sep. 2019.
59.	立松三千子, 萩原純孝, Atsushi Tabata, 服部正也, 小谷はるる, 水野靖也, 澤木正孝, 石黒淳子, 吉村章代, 片岡愛弓, 肱岡範, 清水淳市 and 岩田広治 : エベロリムス服用患者におけるステロイド含有含嗽薬使用時の口腔内微生物叢の変動についての検討, 第4回日本がんサポーティブケア学会学術集会, Sep. 2019.
60.	Chihiro Kodama, QING TANG, Atsushi Tabata, 髙尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus infantisが産生する新規コレステロール依存性細胞溶解毒素infantilysinの作用特性の解明, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) Streptococci / cytolysin
61.	Ayu Ichijoh, Toshifumi Tomoyasu, Eri Arimoto, Mari Deguchi, Atsushi Tabata, 高尾亞由子, 前田伸子 and Hideaki Nagamune : Streptococcus intermediusのヒアルロニダーゼ発現制御機構の解析, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) 連鎖球菌 / ヒアルロン酸分解酵素 / extracellular matrix
62.	Rina Shirai, Miho Kobayashi, Atsushi Tabata, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitisが産生する非典型CDCに対する細胞の応答反応, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) Streptococci / cytolysin
63.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第13回細菌学若手コロッセウム, Aug. 2019. (Keyword) Streptococci / 細胞接着分子 / cytolysin
64.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様の細胞接着分子, 第51回レンサ球菌研究会, Jun. 2019. (Keyword) Streptococcus / cytolysin / 細胞接着分子
65.	Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus subsp. anginosus由来溶原性ファージの遺伝子的特性, 第51回レンサ球菌研究会, Jun. 2019. (Keyword) Streptococcus / bacteriophage
66.	Toshifumi Tomoyasu, Mari Deguchi, 高尾亞由子, Atsushi Tabata, 前田伸子 and Hideaki Nagamune : Streptococcus intermediusが保有する分泌型グリコシダーゼの局在性, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / グリコシダーゼ / 局在性
67.	Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus由来溶原性ファージの特性, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / bacteriophage
68.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. pseudopneumoniaeが産生するコレステロール依存性細胞溶解毒素様分子の特性解析, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / cytolysin / evolution
69.	Chihiro Kodama, QING TANG, Atsushi Tabata, 高尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus infantisが産生するinfantilysinの分子特性, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / cytolysin
70.	Miho Kobayashi, Atsushi Tabata, Hisashi Ohkuni, 高尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisが産生する5ドメイン型CDCに対するヒト好中球様細胞の応答反応, 第92回日本細菌学会総会, Apr. 2019. (Keyword) Streptococcus / cytolysin
71.	Fumitoshi Yagishita, Junichi Tanigawa, Chiho Nii, Atsushi Tabata, Hideaki Nagamune, Yasushi Imada and Yasuhiko Kawamura : 水溶性N-へテロアレーンを用いたHeLa細胞の蛍光イメージングと光細胞毒性, 日本化学会第99春季年会, Mar. 2019.
72.	Atsushi Tabata, Yoshihiro Uto, Hitoshi Hori and 大倉一人 : Chiral-2-nitroimidazole骨格を有するTX-2036 誘導体の開発:放射線増感能の修飾に関わる分子特性の検証, 第22回バイオ治療法研究会学術集会, Dec. 2018.
73.	Yurina Nishihira, Atsushi Tabata, Toshifumi Tomoyasu, Kazuto Ohkura and Hideaki Nagamune : 薬剤キャリアのミセルが示す癌細胞障害性, 第22回バイオ治療法研究会学術集会, Dec. 2018. (Keyword) drug delivery system / cancer therapy
74.	Fumitoshi Yagishita, Junichi Tanigawa, Chiho Nii, Atsushi Tabata, Hideaki Nagamune, Yasushi Imada and Yasuhiko Kawamura : 光照射をトリガーとした水溶性N-ヘテロアレーンによるDNA損傷, 2018年日本化学会中国四国支部大会, Nov. 2018.
75.	Mari Deguchi, Toshifumi Tomoyasu, 高尾亞由子, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが保有するグリコシダーゼの局在性についての解析, 第71回日本細菌学会中国・四国支部総会, Oct. 2018. (Keyword) Streptococcus / グリコシダーゼ / 局在性
76.	山田拓矢, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Response of host human cells against SLS-homolog derived from S. anginosus subsp. anginosus, 第91回日本生化学会大会, Sep. 2018.
77.	Junichi Tanigawa, Fumitoshi Yagishita, Chiho Nii, Atsushi Tabata, Hideaki Nagamune, Yasushi Imada and Yasuhiko Kawamura : 水溶性N-ヘテロアレーンの蛍光バイオイメージングへの応用とDNA損傷, 2018年光化学討論会, Sep. 2018.
78.	Junichi Tanigawa, Fumitoshi Yagishita, Chiho Nii, Atsushi Tabata, Hideaki Nagamune, Yasushi Imada and Yasuhiko Kawamura : 蛍光発光性N-ヘテロアレーンのバイオイメージングへの応用とDNA損傷, 第48回複素環化学討論会, Sep. 2018.
79.	Fumitoshi Yagishita, Shota Unesaki, Yoshihiko Tezuka, Atsushi Tabata, Hideaki Nagamune and Yasuhiko Kawamura : スチリル基を有するイミダゾ[1,5-a]ピリジン二量体の金属イオン存在下における発光挙動, 第48回複素環化学討論会, Sep. 2018.
80.	Yohhei Sanagawa, Fumitoshi Yagishita, Atsushi Tabata, Hideaki Nagamune and Yasuhiko Kawamura : A-π-D-π-A システムに基づく新規対称発光分子のデザインと合成，及び光物性, 第48回複素環化学討論会, Sep. 2018.
81.	児玉千紘, 唐卿, Atsushi Tabata, 髙尾亞由子, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus infantisが産生するInfantilysinの作用特性を明らかにする, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
82.	藤本あい, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性に関する研究, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
83.	松本愛理, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus pseudopneumoniaeが保有するコレステロール依存性細胞溶解毒素様分子の解析, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
84.	Atsushi Tabata, 松本愛理, 藤本あい, 児玉千紘, Toshifumi Tomoyasu and Hideaki Nagamune : 咽頭口腔レンサ球菌が産生する溶血毒素とその多様性, 第12回細菌学若手コロッセウム in OKAYAMA, Aug. 2018.
85.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. pseudopneumoniaeが保有するコレステロール依存性細胞溶解毒素様分子の解析, 第65回トキシンシンポジウム, Jul. 2018. (Keyword) Streptococcus / cytolysin
86.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性, 第65回トキシンシンポジウム, Jul. 2018. (Keyword) Streptococcus / cytolysin / cholesterol
87.	Akiko Tominaga, Toshifumi Tomoyasu, Tatsuma Kusaka, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子 and Hideaki Nagamune : グループ3に属するコレステロール依存性細胞溶解毒素のCD59認識性の比較, 第65回トキシンシンポジウム, Jul. 2018. (Keyword) Streptococcus / cytolysin / cholesterol
88.	Atsushi Tabata, Seiya Otsuka, Deutsch Douglas, 菊池賢, Fischetti A. Vincent, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus subsp. anginosusが保有するプラスミドとその特徴, 第50回レンサ球菌研究会, Jun. 2018. (Keyword) Streptococcus / プラスミド
89.	Toshifumi Tomoyasu, Masaki Matoba, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのグリコシダーゼとインターメディリシン産生との関連について, 第50回レンサ球菌研究会, Jun. 2018. (Keyword) Streptococcus / virulence factor / cytolysin / sugar
90.	立松洋平, Atsushi Tabata, Hideaki Nagamune and 大倉一人 : 非ステロイド性抗炎症薬セレコキシブの細胞膜障害メカニズムの解析, 第91回日本細菌学会総会, Mar. 2018.
91.	Haruka Hino, Tatsuya Okahata, Atsushi Tabata, 髙尾亞由子, 大國寿士, 小椋義俊, Toshifumi Tomoyasu, 林哲也, 前田伸子 and Hideaki Nagamune : Streptococcus mitisにおけるコレステロール依存性細胞溶解毒素の遺伝子分布パターンと細胞障害性との関連性, 第91回日本細菌学会総会, Mar. 2018.
92.	Risako Araki, Atsushi Tabata, 村上漱, 髙尾亞由子, Hisashi Ohkuni, 小椋義俊, Toshifumi Tomoyasu, 林哲也, 前田伸子 and Hideaki Nagamune : タンデム型末追加ドメインを持つコレステロール依存性細胞溶解毒素の特性解析, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
93.	Takuya Yamada, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Transcriptional response of host cells induced by SLS-producing S. anginosus subsp. anginosus, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
94.	高尾亞由子, Toshifumi Tomoyasu, Atsushi Tabata, Hideaki Nagamune and 前田伸子 : グリコシダーゼ活性が Streptococcus intermedius の実験的バイオフィルム量に及ぼす影響, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
95.	Yayoi Iwasa, Asuka Fukutomi, Atsushi Tabata, 村上漱, Toshifumi Tomoyasu and Hideaki Nagamune : Multiplex-PCR による高病原性 S. mitis 検出系の実用化に向けた検討, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
96.	Atsushi Tabata, Seiya Otsuka, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : S. anginosus subsp. anginosusにおけるプラスミドの保有状況とそれらの特性, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / virulence factor
97.	Toshifumi Tomoyasu, Akiko Tominaga, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子 and Hideaki Nagamune : DTT処理赤血球を用いたコレステロール依存性細胞溶解毒素の CD59認識性の比較, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
98.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : S. mitis由来の新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性に関する研究, 第91回日本細菌学会総会, Mar. 2018. (Keyword) pathogenic microorganism / bacterial toxins
99.	谷脇竜弥, 杉田知世, Keiji Murakami, Takashi Amoh, Atsushi Tabata, Yoshiko Yamamura, Tetsuya Tamatani, Hideaki Nagamune, Youji Miyamoto and Hideki Fujii : 幼児口腔内創部より検出された多剤耐性レンサ球菌について, 四国歯学会第52回例会, Mar. 2018.
100.	Fumitoshi Yagishita, Chiho Nii, Yoshihiko Tezuka, Atsushi Tabata, Hideaki Nagamune, Shoko Ueta and Yasuhiko Kawamura : Synthesis and Evaluation of Photophysical Properties of Dimeric Imidazo[1,5-a]pyridinium Salts, 日本化学会第98春季年会, Mar. 2018.
101.	Akiko Tominaga, Toshifumi Tomoyasu, Tatsuma Kusaka, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子 and Hideaki Nagamune : グループ3に属するコレステロール依存性細胞溶解毒素のCD59認識性の比較, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) pathogenic microorganism / bacterial toxins
102.	Shingo Kusaka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : シアリダーゼ阻害剤がStreptococcus intermediusのシアリダーゼ活性や溶血活性に及ぼす効果, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) pathogenic microorganism / virulence factor
103.	Kazuki Hatta, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ナノ粒子表面加工システムの構築に用いる細菌由来ペプチド転移酵素Sortase A組換え体の作製とその特性, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) cancer therapy
104.	Chiho Okada, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : DDS用エフェクター分子としての細菌毒素組換え体の効率的な調製システムの構築, 2017年度生命科学系学会合同年次大会, Dec. 2017. (Keyword) cancer therapy
105.	立松洋平, 川口遊喜, Atsushi Tabata, Yoshihiro Uto, 堀均 and 大倉一人 : 糖付加によるTX-1877系列化合物の機能制御:放射線増感能との相関解析, 第21回バイオ治療法研究会, Dec. 2017.
106.	Qing Tang, Masayoshi Onitsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 癌治療用新規DDSツール作製に用いるリガンド分子の調製とその機能評価, 第21回バイオ治療法研究会, Dec. 2017. (Keyword) cancer therapy
107.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitis由来新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性を規定する構造領域の探索, 第70回日本細菌学会中国・四国支部総会, Oct. 2017. (Keyword) pathogenic microorganism / bacterial toxins
108.	Toshifumi Tomoyasu, Shingo Kusaka, Shinya Chiba, Takahiro Yamasaki, Atsushi Tabata and Hideaki Nagamune : ヒト血漿によるStreptococcus intermediusの病原性発現抑制機構の解析, 第70回日本細菌学会中国・四国支部総会, Oct. 2017. (Keyword) pathogenic microorganism / virulence factor
109.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. mitis由来5ドメイン型コレステロール依存性細胞溶解毒素のN末追加ドメインが示す細胞障害作用, 第11回細菌学若手コロッセウム, Aug. 2017. (Keyword) pathogenic microorganism / bacterial toxins
110.	Ai Fujimoto, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitis が産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性に関する研究, 第11回細菌学若手コロッセウム, Aug. 2017. (Keyword) pathogenic microorganism / bacterial toxins
111.	Toshifumi Tomoyasu, Atsushi Tabata, Shinya Chiba, Takahiro Yamasaki, Nozomi Takeda, Masaaki Tamaoka, Kazuto Ohkura and Hideaki Nagamune : 糖によるStreptococcus intermediusの病原性制御機構, 第64回トキシンシンポジウム, Jul. 2017. (Keyword) pathogenic microorganism / virulence factor
112.	Tatsuya Okahata, Atsushi Tabata, 小椋義俊, 林哲也, 高尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitis におけるコレステロール依存性細胞溶解毒素遺伝子の周辺遺伝子配座の多様性とその特徴, 第58回日本生化学会中国・四国支部例会, May 2017. (Keyword) bacterial toxins / gene
113.	Seiya Ohtsuka, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosus subsp. anginosusが保有する新規Extra-chromosomal DNAの分子特性, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / プラスミド / 可動遺伝子
114.	Masaki Matoba, Toshifumi Tomoyasu, Ayuko Takao, Atsushi Tabata, nobuko Maeda and Hideaki Nagamune : Streptococcus intermediusの高病原性株スクリーニングシステムの開発, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / virulence factor / cytolysin
115.	Tatsuya Okahata, Syu Murakami, Atsushi Tabata, Yoshitoshi Ogura, Tetsuya Hayashi, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Streptococcus mitisが保有するコレステロール依存性細胞溶解毒素遺伝子周辺における遺伝子配座の多様性, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / cytolysin / genome
116.	Airi Matsumoto, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : S. mitis由来5ドメイン型コレステロール依存性細胞溶解毒素のN末追加ドメインが示す細胞障害作用, 第90回日本細菌学会総会, Mar. 2017. (Keyword) Streptococcus / cytolysin
117.	Tatsuma Kusaka, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : ウマ赤血球に存在するExD-CDCレセプターの探索, 第3回日本生物工学会西日本支部講演会, Dec. 2016. (Keyword) Streptococcus / cytolysin / CD59
118.	Ai Fujimoto, Atsushi Tabata, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitisが産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性の多様性, 第3回日本生物工学会西日本支部講演会, Dec. 2016. (Keyword) Streptococcus / cytolysin
119.	Takuya Saigoh, Atsushi Tabata, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus mitisにおける効果的な形質転換法の検討, 第3回日本生物工学会西日本支部講演会, Dec. 2016. (Keyword) Streptococcus / 形質転換法 / プラスミド / DNA断片
120.	Atsushi Tabata, Kazuto Ohkura, Youhei Tatematsu, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞障害性を示す細菌毒素に対する糖の阻害作用, 第20回バイオ治療法研究会, Dec. 2016. (Keyword) Streptococcus / cytolysin / sugar
121.	Shingo Kusaka, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が産生するシアリダーゼの発現制御機構の解析, 第69回日本細菌学会中国・四国支部総会, Oct. 2016. (Keyword) Streptococcus / cytolysin / sugar
122.	Ikumi Tamura, Atsushi Tabata, Syu Murakami, Ayuko Takao, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Streptococcus infantis が産生する新規コレステロール依存性細胞溶解毒素Infantilysin, 第63回トキシンシンポジウム, Jul. 2016. (Keyword) Streptococcus / cytolysin
123.	Toshifumi Tomoyasu, Shinya Chiba, Takahiro Yamasaki, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius の血液成分による病原性亢進とヒト血液成分によるその防御, 第48回レンサ球菌研究会, Jul. 2016. (Keyword) Streptococcus / cytolysin / sugar / antibody
124.	Ikumi Tamura, Atsushi Tabata, Shu Murakami, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Cytotoxic properties of a novel cholesterol-dependent cytolysin from Streptococcus infantis, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / function
125.	Hiromi Ohtani, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptolysin S homolog-dependent cytotoxicity of betahemolytic S. anginosus subsp. anginosus, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / function / gene expression
126.	Toshifumi Tomoyasu, Shinya Kusaka, Masaki Matoba, Yukihiro Kaneko, Atsushi Tabata and Hideaki Nagamune : Wide upstream region of ily is involved in its repression in Streptococcus intermedius, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / gene expression
127.	Shinya Chiba, Toshifumi Tomoyasu, Takahiro Yamasaki, Shingo Kusaka, Atsushi Tabata and Hideaki Nagamune : Positive and negative control of ily expression by blood components, 第89回日本細菌学会総会, Mar. 2016. (Keyword) Streptococcus / cytolysin / blood / sugar
128.	Qing Tang, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : A trial for development of effective drug delivery system using small targeting module against CEA-positive cancer, Joint Meeting of the 38th Annual Meeting of the Molecular Biology Society of Japan and the 88th Annual Meeting of the Japanese Biochemical Society, Dec. 2015. (Keyword) drug delivery system / antibody
129.	Ryosuke Tanatsugu, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Functional analysis of a gram-negative characteristic segment of DnaK using Streptococcus intermedius DnaK, 第38回日本分子生物学会年会, Dec. 2015. (Keyword) Streptococcus / molecular chaperone / protein
130.	Shinya Kusaka, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Investigation of transcriptional regulation elements in ily promoter region of Streptococcus intermedius, 第38回日本分子生物学会年会, Dec. 2015. (Keyword) Streptococcus / cytolysin / gene expression
131.	Shinya Chiba, Toshifumi Tomoyasu, Takahiro Yamasaki, Atsushi Tabata and Hideaki Nagamune : 血液成分によるインターメディリシン発現調節機構の解析, 第68回日本細菌学会中国・四国支部総会, Oct. 2015. (Keyword) Streptococcus / cytolysin / sugar / blood
132.	Ikumi Tamura, Atsushi Tabata, Shu Murakami, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu, Nobuko Maeda and Hideaki Nagamune : Streptococcus infantis由来の新規コレステロール依存性細胞溶解毒素の作用特性, 第68回日本細菌学会中国・四国支部総会, Oct. 2015. (Keyword) Streptococcus / cytolysin / virulence factor
133.	Toshifumi Tomoyasu, Shinya Chiba, Takahiro Yamasaki, 甲斐瑛之, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのグリコシダーゼによるインターメディリシン発現調節機構の解析, 第56回日本生化学会中国四国支部例会, May 2015. (Keyword) Streptococci / enzyme / sugar / cytolysin / gene expression
134.	Kentaro Maya, Atsushi Tabata, Kazuto Ohkura, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : S. anginosus subsp. whileyi およびS. constellatus subsp. viborgensis が保有するβ溶血因子の特性解析, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / cytolysin / function
135.	Atsushi Morishita, Atsushi Tabata, Shu Murakami, 高尾亞由子, Hisashi Ohkuni, 小椋義俊, 林哲也, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : S. mitis におけるコレステロール依存性細胞溶解毒素遺伝子の分布とβ-ラクタム系薬剤耐性の関連性, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / antibiotics / cytolysin
136.	Takahiro Yamasaki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : S. intermedius が保有するグリコシダーゼがインターメディリシン発現制御に果たす役割についての解析, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / gene expression / enzyme / sugar
137.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有するシアリダーゼの精製とその性状の解析, 第88回日本細菌学会総会, Mar. 2015. (Keyword) Streptococci / protein / sugar
138.	Hajime Yoshida, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Inerolysin (INY) の pH 依存的な膜孔形成活性と立体構造変化, 第133回徳島生物学会総会, Dec. 2014. (Keyword) pathogenic microorganism / Streptococci / cytolysin / pH
139.	Yukimasa Okubo, Natsuki Anyohji, Atsushi Tabata, 北條恵子, Toshifumi Tomoyasu, 立松洋平, Kazuto Ohkura and Hideaki Nagamune : ドラッグデリバリーシステム創成を目指したSortase Aによるペプチド修飾化リポソーム作製技術の開発, 第18回バイオ治療法研究会, Dec. 2014. (Keyword) drug delivery system / Sortase A / liposomes
140.	Yukimasa Okubo, Natsuki Anyohji, Atsushi Tabata, 北條恵子, Toshifumi Tomoyasu and Hideaki Nagamune : 新規ドラッグデリバリーシステムツール作製法としてのペプチド修飾化リポソームの作製, 第87回日本生化学会大会, Oct. 2014. (Keyword) drug delivery system / liposomes / ガン治療
141.	Masaaki Tamaoka, Nozomi Takeda, Atsushi Tabata, Kazuto Ohkura, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の膜孔形成活性に対する糖の抑制効果, 第87回日本生化学会大会, Oct. 2014. (Keyword) pathogenic microorganism / Streptococcus / virulence factor / sugar / cytolysin
142.	Natsuki Anyohji, Atsushi Tabata, Yukimasa Okubo, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来ペプチド転移酵素Sortase Aの由来菌種依存的な基質認識特性, 第87回日本生化学会大会, Oct. 2014. (Keyword) グラム陽性菌 / ブドウ球菌 / Streptococcus / Sortase A / 基質特異性
143.	Atsushi Morishita, Atsushi Tabata, Shu Murakami, 高尾亞由子, 勝部康弘, Hisashi Ohkuni, Toshifumi Tomoyasu, 前田伸子 and Hideaki Nagamune : Streptococcus mitisにおける膜孔形成毒素遺伝子の保有とβ-ラクタム薬耐性の関連性, 第67回日本細菌学会中国四国支部総会, Oct. 2014. (Keyword) pathogenic microorganism / Streptococcus / virulence factor / 溶血因子 / 薬剤耐性
144.	Takahiro Yamasaki, Toshifumi Tomoyasu, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusの病原性とグリコシダーゼとの関連性, 第67回日本細菌学会中国四国支部総会, Oct. 2014. (Keyword) pathogenic microorganism / Streptococcus / sugar / グリコシダーゼ
145.	Toshifumi Tomoyasu, 今木英統, Chiharu Taue, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius が保有するグリコシダーゼの病原性に果たす役割について, 第61 回トキシンシンポジウム ∼鳴門渦潮カンファレンス∼, Sep. 2014. (Keyword) Streptococcus / pathogenic microorganism / sugar / グリコシダーゼ
146.	Atsushi Tabata, Kentaro Maya, 大谷浩美, Yuji Sato, Kota Nakano, Kazuto Ohkura, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : β溶血性アンギノーサス群レンサ球菌が保有するストレプトリジンSホモログの多様性, 第46回レンサ球菌研究会, Jun. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / 溶血因子
147.	Atsushi Tabata, Nozomi Takeda, Masaaki Tamaoka, Toshifumi Tomoyasu, 高尾亞由子, 前田伸子, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の膜孔形成活性に及ぼす糖の影響, 第55回日本生化学会中国・四国支部例会, Jun. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / sugar
148.	Toshifumi Tomoyasu, 今木英統, Chiharu Taue, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが保有する多基質酵素``MsgA''の性状解析, 第55回日本生化学会中国・四国支部例会, Jun. 2014. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / 糖鎖 / グリコシダーゼ
149.	Toshifumi Tomoyasu, Yukihiro Kaneko, Atsushi Tabata and Hideaki Nagamune : Identification and study of the binding region of ily transcriptional repressive element, 第87回日本細菌学会総会, Mar. 2014. (Keyword) Streptococci / 転写抑制因子結合部位 / gene expression / cytolysin
150.	Shu Murakami, Atsushi Tabata, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : 高病原性Streptococcus mitisの検出・同定を目的とした新規検査システムの開発, 第87回日本細菌学会総会, Mar. 2014. (Keyword) Streptococci / identification / PCR / cytolysin
151.	Naoki Yamamoto, Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : Characterization of a novel secreted glycosidase (MsgA) of Streptococcus intermedius, 第87回日本細菌学会総会, Mar. 2014. (Keyword) Streptococci / グリコシダーゼ / 糖鎖 / decomposition
152.	Natsuki Anyohji, Atsushi Tabata, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : Comparison of the transition activity of Sortase A using GFP-substrate panel, 第87回日本細菌学会総会, Mar. 2014. (Keyword) enzyme / ペプチド転位酵素 / GFP
153.	金惠珍, Atsushi Tabata, Toshifumi Tomoyasu, 上野友美, 内山成人, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : エストロゲン作用物質が示す骨芽細胞分化促進作用の解析, 徳島生物学会, Dec. 2013. (Keyword) エストロゲン / 骨芽細胞分化
154.	大倉一人, 川口遊喜, Atsushi Tabata and Hideaki Nagamune : Streptococcus anginosus由来ストレプトリジンSホモログの分子内環形成による活性制御, 第17回バイオ治療法研究会学術集会, Dec. 2013. (Keyword) bacteria / ストレプトリジンS / Streptococcus anginosus
155.	Atsushi Tabata, 安養寺夏希, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来ペプチド転移酵素Sortase Aを用いたDDS用新規機能性リポソームの創成に関する検討, 第17回バイオ治療法研究会学術集会, Dec. 2013. (Keyword) bacteria / drug delivery system / liposomes / ペプチド転移酵素 / GFP
156.	Toshifumi Tomoyasu, Hidenori Imaki, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Identification and characterization of MsgA, a novel secreted glycosidase of Streptococcus intermedius, 第36回日本分子生物学会年会, Dec. 2013. (Keyword) Streptococcus / pathogenic microorganism / sugar / enzyme
157.	Shu Murakami, Atsushi Tabata, 髙尾亞由子, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : 高病原性Streptococcus mitis検出・同定システムの構築, 第66回日本細菌学会中国・四国支部総会, Oct. 2013. (Keyword) Streptococcus / pathogenic microorganism / identification / PCR
158.	Naoki Yamamoto, Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが分泌する新規グリコシダーゼの発見と性状解析, 第66回日本細菌学会中国・四国支部総会, Oct. 2013. (Keyword) Streptococcus / pathogenic microorganism / sugar / enzyme
159.	Natsuki Anyohji, Atsushi Tabata, Yukimasa Okubo, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来ペプチド転移酵素Sortase Aの比較解析 -新規DDS開発への応用を目指して-, 日本生化学会, Sep. 2013. (Keyword) bacteria / drug delivery system / 蛍光タンパク質 / ペプチド転移酵素
160.	Nozomi Takeda, Atsushi Tabata, Asuka Nogami, 髙尾亞由子, Hisashi Ohkuni, 前田伸子, Toshifumi Tomoyasu and Hideaki Nagamune : N末に追加ドメインを有するコレステロール依存性細胞溶解毒素の作用特性, 日本生化学会, Sep. 2013. (Keyword) cytolysin / protein / cholesterol / sugar
161.	Atsushi Tabata, Kazuto Ohkura, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の受容体認識および作用特性における多様性, 第60回毒素シンポジウム, Jul. 2013. (Keyword) Streptococcus / pathogenic microorganism / gene expression / virulence factor
162.	Toshifumi Tomoyasu, Hidenori Imaki, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius の主要病原因子であるインターメディリシンの発現調節機構の解析, 第60回毒素シンポジウム, Jul. 2013. (Keyword) Streptococcus / pathogenic microorganism / gene expression / virulence factor
163.	Atsushi Tabata, 中野晃太, Kazuto Ohkura, 菊池賢, Toshifumi Tomoyasu and Hideaki Nagamune : β溶血性 Streptococcus anginosus が保有するストレプトリジンS ホモログの特徴と細胞障害性への寄与, 第22回 Lancefieldレンサ球菌研究会, Jun. 2013. (Keyword) Streptococcus / pathogenic microorganism / virulence factor
164.	Hidenori Imaki, Toshifumi Tomoyasu, 増田早智子, Naoki Yamamoto, Atsushi Tabata and Hideaki Nagamune : 糖タンパク質によるStreptococcus intermediusのily発現促進機構の解析, 第22回 Lancefieldレンサ球菌研究会, Jun. 2013. (Keyword) Streptococcus / pathogenic microorganism / virulence factor / gene expression
165.	Toshifumi Tomoyasu, Hiroyuki Kondo, Masanori Oisugi, Atsushi Tabata and Hideaki Nagamune : グラム陽性菌と陰性菌のDnaKシャペロンシステムの比較, 第54回日本生化学会中国・四国支部例会, Jun. 2013. (Keyword) DnaK / ClpB / Gram-Positive Bacteria / Gram-Negative Bacteria / molecular chaperone
166.	Asuka Nogami, Atsushi Tabata, Nozomi Takeda, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : β溶血性の高病原性Streptococcus mitisサブグループの特性, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / clinical laboratory testing
167.	Yukihiro Kaneko, Toshifumi Tomoyasu, Hidenoro Imaki, Atsushi Tabata and Hideaki Nagamune : ily転写抑制因子の結合領域の探索, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / gene expression
168.	Atsushi Tabata, Yuji Sato, Kota Nakano, Kazuto Ohkura, Ken Kikuti, Toshifumi Tomoyasu and Hideaki Nagamune : S. constellatus subsp. constellatusが保有するβ溶血因子の探索, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / enzyme
169.	Nozomi Takeda, Atsushi Tabata, Asuka Nogami, Ayuko Takao, Hisashi Ohkuni, Nobuko Maeda, Toshifumi Tomoyasu and Hideaki Nagamune : 新規5ドメイン型コレステロール依存性細胞溶解毒素の分子特性, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / enzyme
170.	Miku Ishikawa, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な膜孔形成毒素インターメディリシンにより好中球に誘導される応答反応, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / 細胞感染
171.	Hidenori Imaki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Identification of an expressionpromoting factor for ily of Streptococcus intermedius, 第86回日本細菌学会総会, Mar. 2013. (Keyword) Streptococci / cytolysin / gene expression
172.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Does DnaK from Gram-positive Bacterium recognize ClpB of E.coli?, 第86回日本細菌学会総会, Mar. 2013. (Keyword) molecular chaperone / Streptococcus / enzyme
173.	Kenji Nagataki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Investigation on the procedure for enhancement of cellulase activity and its application, 日本生化学会, Dec. 2012. (Keyword) molecular chaperone / セルラーゼ / バイオエタノール / application
174.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Small heat shock protein AgsA is an effective stabilizer of enzyme activities, 日本生化学会, Dec. 2012. (Keyword) molecular chaperone / sHSP / enzyme
175.	Hyejin Kim, Atsushi Tabata, Toshifumi Tomoyasu, Tomomi Ueno, Naruhito Uchiyama, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : A study on the mechanism of osteoblast differentiation induced by estrogen-stimuli, 日本生化学会, Dec. 2012. (Keyword) osteoblast / エストロゲン / イソフラボン
176.	大倉一人, 川口遊喜, Atsushi Tabata, 篠原康雄 and Hideaki Nagamune : 細菌由来細胞溶解毒素のヒト側受容体との相互作用, 第16回バイオ治療法研究会学術集会, Dec. 2012.
177.	Manami Aoyagi, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシンの細胞膜結合能と分子集合メカニズムの解析, 徳島生物学会, Dec. 2012. (Keyword) Streptococci / cytolysin / 細胞膜
178.	Yasunori Iwano, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシン刺激が単球系細胞THP-1の遺伝子発現に及ぼす影響, 徳島生物学会, Dec. 2012. (Keyword) Streptococci / cytolysin / gene expression
179.	Masanori Oisugi, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 大腸菌のClpBは連鎖球菌のDnaKシャペロンシステムを認識するのか, 徳島生物学会, Dec. 2012. (Keyword) molecular chaperone / Hsp70 / Hsp104 / DnaK / ClpB
180.	Nozomi Takeda, Atsushi Tabata, Ayuko Takao, Hisashi Ohkuni, Toshifumi Tomoyasu and Atsushi Tabata : Streptococcus mitis が産生する新規5ドメイン型コレステロール依存性細胞溶解毒素の作用特性, 日本細菌学会, Oct. 2012. (Keyword) Streptococci / Streptococcus mitis / コレステロール依存性細胞溶解毒素
181.	Yukihiro Kaneko, Toshifumi Tomoyasu, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : ily 発現抑制因子が認識するコンセンサス配列の探索, 日本細菌学会, Oct. 2012. (Keyword) Streptococci / gene expression / コンセンサス配列
182.	Atsushi Tabata, 中野晃太, Kazuto Ohkura, Toshifumi Tomoyasu and 菊池賢 : アンギノーサス群連鎖球菌が保有するβ溶血因子の探索とその特性, 第59回毒素シンポジウム, Aug. 2012.
183.	Atsushi Tabata, 中野晃太, 大倉一人, Toshifumi Tomoyasu, 菊池賢 and Hideaki Nagamune : β溶血性Streptococcus anginosusが保有するペプチド性溶血因子の分子特性, 第6回細菌学若手コロッセウム, Aug. 2012.
184.	金惠珍, Atsushi Tabata, Toshifumi Tomoyasu, 上野友美, 内山成人 and Hideaki Nagamune : Effect of Equol, an Enterobacterial Metabolite of Soybean Isoflavones on Osteoblast Differentiation., 第16回腸内細菌学会, Jun. 2012.
185.	今木英統, Toshifumi Tomoyasu, 増田早智子, Atsushi Tabata and Hideaki Nagamune : LacRはStreptococcus intermediusのily発現の主要な制御因子である, 第21回 Lancefieldレンサ球菌研究会, Jun. 2012.
186.	Atsushi Tabata, 野上明日香, 竹田望, 髙尾亞由子, Hisashi Ohkuni, Toshifumi Tomoyasu and Hideaki Nagamune : コレステロール依存性細胞溶解毒素遺伝子を保有するStreptococcus mitis株の毒素産生特性とヒト細胞障害性, 第21回 Lancefieldレンサ球菌研究会, Jun. 2012.
187.	金惠珍, Atsushi Tabata, Toshifumi Tomoyasu, 上野友美, 内山成人, Keizo Yuasa, Akihiko Tsuji and Hideaki Nagamune : エストロゲン作用物質が示す骨芽細胞の分化促進作用, 第53回日本生化学会中国・四国支部例会, May 2012.
188.	Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : グラム陽性菌と陰性菌のコシャペロンによるDnaK活性化機構の比較, 第85回日本細菌学会総会, Mar. 2012. (Keyword) Streptococci / molecular chaperone / protein
189.	今木英統, Toshifumi Tomoyasu, 増田早智子, Atsushi Tabata and Hideaki Nagamune : ILYを高産生するStreptococcus intermediusの臨床分離株の多くがLacRに変異を持つ, 第85回日本細菌学会総会, Mar. 2012. (Keyword) Streptococci / cytolysin / gene expression
190.	Atsushi Tabata, 中野晃太, Toshifumi Tomoyasu, 大倉一人, 菊池賢 and Hideaki Nagamune : TOMM family peptides decide the hemolytic character of Streptococcus anginosus, 第85回日本細菌学会総会, Mar. 2012. (Keyword) Streptococci / bacterial toxins
191.	福居孝之, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の膜孔形成反応における分子動態の解析, 第127回徳島生物学会, Dec. 2011. (Keyword) Streptococci / cytolysin
192.	Atsushi Tabata, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : 膜孔形成性キメラ毒素の新規DDSツールとしての応用性に関する検討, 第15回バイオ治療法研究会学術集会, Dec. 2011. (Keyword) cancer therapy
193.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが保有するDnaKシャペロンシステムの機能解析, 第64回日本細菌学会中国・四国支部総会, Oct. 2011. (Keyword) Streptococci / molecular chaperone
194.	中野晃太, Atsushi Tabata, Toshifumi Tomoyasu, 大倉一人, 菊池賢, 平松啓一 and Hideaki Nagamune : β溶血性Streptococcus anginosusで見出された新規ペプチド性溶血因子, 第64回日本細菌学会中国・四国支部総会, Oct. 2011. (Keyword) Streptococci / bacterial toxins
195.	今木英統, Toshifumi Tomoyasu, 増田早智子, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのily発現調節因子の探索, 第64回日本細菌学会中国・四国支部総会, Oct. 2011. (Keyword) Streptococci / cytolysin / gene expression
196.	大久保行将, Atsushi Tabata, 田村仁人, Toshifumi Tomoyasu and Hideaki Nagamune : 細胞標的化キメラ細菌毒素を用いた新規DDSツールの開発, 第84回日本生化学会大会, Sep. 2011. (Keyword) cancer therapy
197.	岡久奈緒美, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : キノコβ-グルカンによるマクロファージ様THP-1の活性化作用, 第84回日本生化学会大会, Sep. 2011. (Keyword) cancer immunotherapy
198.	Atsushi Tabata, 中野晃太, Toshifumi Tomoyasu and Hideaki Nagamune : アンギノーサス群連鎖球菌が保有する溶血因子に関する検討, 第5回細菌学若手コロッセウム, Aug. 2011. (Keyword) Streptococci / bacterial toxins
199.	Toshifumi Tomoyasu, 今木英統, 増田早智子, Atsushi Tabata and Hideaki Nagamune : コレステロール依存性細胞溶解毒素intermedilysinの発現調節因子がStreptococcus intermediusの病原性に果たす役割の解析, 第58回トキシンシンポジウム, Jul. 2011. (Keyword) Streptococci / cytolysin
200.	Atsushi Tabata, 中野晃太, Toshifumi Tomoyasu and Hideaki Nagamune : アンギノーサス群連鎖球菌が保有する溶血因子の探索, 第20回Lancefieldレンサ球菌研究会/第43回レンサ球菌感染症研究会, Jun. 2011.
201.	Toshifumi Tomoyasu, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : カタボライト抑制因子CcpAによるStreptococcus intermediusのヒト特異的細胞溶解毒素intermedilysinの発現調節, 第33回日本分子生物学会年会第83回日本生化学会大会合同大会, Dec. 2010.
202.	Atsushi Tabata, 山本泰裕, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : 2種のコレステロール依存性細胞溶解毒素を産生するStreptococcus mitis Nm-65株の細胞障害性に関する検討, 第33回日本分子生物学会年会第83回日本生化学会大会合同大会, Dec. 2010.
203.	田村仁人, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 細菌由来タンパク質をベースとしたDDSツールの開発-標的細胞に対する選択的送達能に関する検討-, 第125回徳島生物学会, Dec. 2010.
204.	村田貴洋, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : コレステロール依存性細胞溶解毒素による宿主細胞の応答反応の検討, 第125回徳島生物学会, Dec. 2010.
205.	Atsushi Tabata, Kota Nakano, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus anginosusが保有する細胞傷害因子に関する検討, 第63回日本細菌学会中国・四国支部総会, Oct. 2010.
206.	増田早智子, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 血液成分によるily遺伝子の発現調節, 第63回日本細菌学会中国・四国支部総会, Oct. 2010.
207.	山本泰裕, Atsushi Tabata, Toshifumi Tomoyasu, Katsuhiko Hirota, 大国寿士 and Hideaki Nagamune : 川崎病患児由来Streptococcus mitis Nm-65株が産生する2種類のコレステロール依存性細胞溶解毒素遺伝子の発現とその病原性への寄与, 第57回トキシンシンポジウム, Jul. 2010.
208.	Atsushi Tabata, 鈴木圭祐, Toshifumi Tomoyasu and Hideaki Nagamune : 細胞膜構造に依存したインターメディリシンの作用特性, 第51回日本生化学会中国・四国支部例会, May 2010.
209.	今木英統, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius ccpA破壊株とcre変異株の細胞毒性の解析, 第83回日本細菌学会総会, Mar. 2010. (Keyword) virulence factor
210.	Toshifumi Tomoyasu, 今木英統, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermedius dnaK破壊相補株の表現型の解析, 第83回日本細菌学会総会, Mar. 2010. (Keyword) virulence factor
211.	山本泰裕, Atsushi Tabata, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake, Hideaki Nagamune and 大國寿士 : Analysis of a novel S.mitis strain possessing two distinct cholesterol-dependent cytolysin genes, 第83回日本細菌学会総会, Mar. 2010.
212.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Dissection of the chaperone function of the small heat shock protein AgsA, 第32回日本分子生物学会年会, Dec. 2009.
213.	Atsushi Tabata, 金惠珍, Toshifumi Tomoyasu, Hiroki Kourai, 澤田千恵子, 下野生世, Motoyuki Sugai, 赤松優 and Hideaki Nagamune : 融合PCRイムノクロマトグラフィーによる迅速微生物検査系の構築, 日本防菌防黴学会 2009年度若手の会, Dec. 2009.
214.	Atsushi Tabata, 三好宗一郎, 天河崇, Toshifumi Tomoyasu and Hideaki Nagamune : 脂質ラフトを反応場とするStreptococcus intermediusのヒト細胞感染機構, 第82回日本生化学会大会, Oct. 2009.
215.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的細胞溶解毒素の膜貫入領域が膜孔形成反応において果たす機能の解析, 第82回日本生化学会大会, Oct. 2009.
216.	鈴木圭祐, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 多様な受容体認識性を示すコレステロール依存性細胞溶解毒素の細胞膜構造に依存した作用特性, 第62回日本細菌学会中国・四国支部総会, Oct. 2009.
217.	伊藤貴洋, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 蛍光性Streptococcus intermedius株の作製, 第62回日本細菌学会中国・四国支部総会, Oct. 2009.
218.	Atsushi Tabata, Keisuke Suzuki, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : 標的細胞膜構造がコレステロール依存性細胞溶解毒素の受容体認識多様性に及ぼす影響, 若手研究者育成のためのワークショップ若手コロセウム(III), Oct. 2009.
219.	Toshifumi Tomoyasu, Atsushi Tabata, 菊池賢, 佐々木崇, 馬場理, 平松啓一 and Hideaki Nagamune : Streptococcus intermediusが産生するヒト特異的細胞溶解毒素インターメディリシンの発現調節機構の解析, 第56回トキシンシンポジウム, 106-109, Aug. 2009.
220.	Toshifumi Tomoyasu, 廣島理樹, 今木英統, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusのily発現調節機構の解析, 第18回 Lancefield レンサ球菌研究会, Jun. 2009.
221.	Atsushi Tabata, 篠原由樹, 鈴木圭祐, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシンの膜孔形成に携わる分子構造と機能に関する解析, 第18回 Lancefieldレンサ球菌研究会, Jun. 2009.
222.	Atsushi Tabata, 篠原由樹, Toshifumi Tomoyasu and Hideaki Nagamune : インターメディリシンの分子間相互作用に寄与する部分構造の解析, 第50回日本生化学会中国・四国支部例会, May 2009.
223.	Toshifumi Tomoyasu, Atsushi Tabata, 菊池賢, 佐々木崇, 馬場理, 平松啓一 and Hideaki Nagamune : カタボライト抑制因子CcpAによるヒト特異的細胞溶解毒素インターメディリシンの発現調節機構の解析, 第82回日本細菌学会総会, Mar. 2009.
224.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞溶解毒素インターメディリシン(ILY)の膜孔形成を誘導する構造変化領域の解析, 第82回日本日本細菌学会総会, Mar. 2009.
225.	金惠珍, Toshifumi Tomoyasu, Atsushi Tabata, 菅井基行, 赤松優 and Hideaki Nagamune : 融合PCRイムノクロマトグラフィーによる迅速細菌検査, 第82回日本細菌学会総会, Mar. 2009.
226.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptooccus intermediusのストレス誘導型シャペロンDnaKの機能解析, 第82回日本日本細菌学会総会, Mar. 2009.
227.	Katsuhiko Hirota, Shizuo Kayama, Hiromichi Yumoto, Atsushi Tabata, Hideaki Nagamune, Tsuneko Ono and Yoichiro Miyake : Intermedilysinにより誘導される小胞体異常とgp210の細胞内分布の変動, 第82回日本日本細菌学会総会, Mar. 2009.
228.	齋藤静香, Atsushi Tabata, 坂倉永里子, 鈴木圭祐, 垣口貴沙, 篠原由樹, 福島江, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール依存性細胞溶解毒素の受容体認識特性に関する検討, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
229.	坂倉永里子, Atsushi Tabata, 齋藤静香, Toshifumi Tomoyasu and Hideaki Nagamune : 癌標的化毒素を用いた癌療法のための効果的DDSの開発, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
230.	廣島理樹, Toshifumi Tomoyasu, 小南章, Atsushi Tabata, 菊池賢, 佐々木崇, 馬場理, 平松啓一 and Hideaki Nagamune : Streptococcus intermediusが保有するヒト特異的細胞溶解毒素インターメディリシンをコードするily遺伝子のプロモーター領域の解析, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
231.	石川洋子, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : サルモネラ属細菌が保有する小型分子シャペロンAgsAのN末端とC末端領域の機能解析, 第31回日本分子生物学会年会第81回日本生化学会大会合同大会, Dec. 2008.
232.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞溶解毒素インターメディリシンの膜孔形成に関与する分子構造の解析, 第120回徳島生物学会, Nov. 2008.
233.	Katsuhiko Hirota, Shizuo Kayama, Atsushi Tabata, Hideaki Nagamune, Tsuneko Ono and Yoichiro Miyake : Intermedilysinにより誘導されるヒト培養胆管上皮細胞死とgp210の細胞内分布の変動, 第61回日本細菌学会中国・四国支部総会, Oct. 2008.
234.	Atsushi Tabata, 齋藤静香, 坂倉永里子, 鈴木圭祐, 篠原由樹, 福島江, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : コレステロール及びヒト型CD59を受容体とするCholesterol-dependent cytolysin:Sm-hPAFのコレステロール認識特性に関する検討, 第61回日本細菌学会中国・四国支部総会, Oct. 2008.
235.	三好宗一郎, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Streptococcus intermediusのヒト細胞感染現象におけるインターメディリシンと宿主細胞膜構造の役割, 第61回日本細菌学会中国・四国支部総会, Oct. 2008.
236.	Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : 連鎖球菌属が産生するコレステロール依存性細胞溶解毒素の受容体認識における多様性, 第2回細菌学若手コロッセウム, Aug. 2008.
237.	廣島理樹, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : ヒト特異的細胞溶解毒素インターメディリシンの発現調節機構の解析, 第17回 Lancefieldレンサ球菌研究会, Jul. 2008.
238.	Atsushi Tabata, 齋藤静香, 坂倉永里子, 鈴木圭祐, 山本泰裕, 篠原由樹, 福島江, Toshifumi Tomoyasu, Hisashi Ohkuni and Hideaki Nagamune : ヒトCD59指向性コレステロール依存性細胞溶解毒素の受容体認識特性に関する検討, 第17回 Lancefieldレンサ球菌研究会, Jul. 2008.
239.	Katsuhiko Hirota, Heni Susilowati, Hirohiko Okamura, Kaya Yoshida, Atsushi Tabata, Shizuo Kayama, Hiromichi Yumoto, Tatsuji Haneji, Hideaki Nagamune, Tsuneko Ono and Yoichiro Miyake : Intermedilysinにより誘導されるカルシウム振動と胆管上皮細胞死, 第17回Lancefielfレンサ球菌研究会 2008, Jul. 2008.
240.	石川洋子, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : サルモネラ属細菌が保有する小型分子シャペロンAgsAの機能解析, 第49回日本生化学会中国・四国支部例会, May 2008.
241.	垣口貴沙, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : ヒト特異的な細胞溶解毒素インターメディリシン(ILY)の膜孔形成に関わる部分構造に関する解析, 第49回日本生化学会中国・四国支部例会, May 2008.
242.	Atsushi Tabata, Souichirou Miyoshi, Toshifumi Tomoyasu and Hideaki Nagamune : 宿主細胞膜構造がStreptococcus intermediusのヒト細胞感染に及ぼす影響, 第81回日本細菌学会総会, Mar. 2008. (Keyword) Streptococcus / Lipid raft / infection
243.	Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : ヒト特異的な細胞溶解毒素インターメディリシンの発現調節の遺伝学的解析, 第81回日本細菌学会総会, Mar. 2008.
244.	Katsuhiko Hirota, Shizuo Kayama, Atsushi Tabata, Hideaki Nagamune, Tsuneko Ono and Yoichiro Miyake : Intermedilysinにより誘導される非アポトーシス型細胞死と細胞内Ca²⁺濃度の変動, 第81回日本細菌学会総会, Mar. 2008.
245.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 連鎖球菌(S. intermedius)ClpP破壊株の作成とその表現型の解析, 第81回日本細菌学会総会, Mar. 2008. (Keyword) Streptococcus / protease / ClpP
246.	Atsushi Tabata, Souichirou Miyoshi, Ayuha Kadota, Kou Fukushima, Akiko Sukeno, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake, Hisashi Ohkuni and Hideaki Nagamune : 細菌感染反応場としてのヒト型CD59:ヒト細胞指向性コレステロール依存性細胞溶解毒素の受容体及びStreptococcus intermedius感染の宿主側トリガー因子としての役割, 第80回日本生化学会大会-第30回日本分子生物学会年会合同大会, Dec. 2007. (Keyword) Streptococcus / CD59 / Infection
247.	Hiroshima Riki, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusが生産するヒト特異的細胞溶解毒素インターメディシンの発現調節, 第80回日本生化学会大会-第30回日本分子生物学会年会合同大会, Dec. 2007. (Keyword) Streptococcus / gene expression
248.	Toshifumi Tomoyasu, Syunsuke Azuma, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : 腸管出血性大腸菌のGrlAによるLEE1オペロンの新規発現調節機構, 第30回日本分子生物学会年会, Dec. 2007. (Keyword) EHEC / LEE pathgenisity island
249.	Katsuhiko Hirota, Susilowati Heni, 劉大力, Shizuo Kayama, Atsushi Tabata, Hideaki Nagamune, Tsuneko Ono and Yoichiro Miyake : Intermedilysinにより誘導されるヒト培養胆管上皮細胞死の分子機構の解明, 第60回日本細菌学会中国四国支部総会, Oct. 2007.
250.	Shinohara Yuki, Takumi Ishida, Atsushi Tabata, Toshifumi Tomoyasu and Hideaki Nagamune : Analysis of intermolecular interaction site of intermedilysin, 第60回日本細菌学会中国四国支部総会, Oct. 2007. (Keyword) Streptococcus / Cytolysin
251.	Atsushi Tabata, Miyoshi Souichirou, Kadota Ayuha, Akiko Sukeno, Katsuhiko Hirota, Toshifumi Tomoyasu, Yoichiro Miyake and Hideaki Nagamune : Streptococcus intermedius が分泌する細胞溶解毒素インターメディリシンが関与するヒト細胞特異的な感染現象, 第54回毒素シンポジウム, Sep. 2007. (Keyword) cytotoxicity / Streptococcus
252.	Toshifumi Tomoyasu, Riki Hiroshima, Syunsuke Ishida, Akira Kominami, Atsushi Tabata and Hideaki Nagamune : Streptococcus intermediusの病原性発現調節機構の解析, 第16回Lancefieldレンサ球菌研究会, Jun. 2007. (Keyword) Streptococcus / Pathogenisity / Chaperon
253.	Atsushi Tabata, 三好宗一郎, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake and Hideaki Nagamune : 細胞溶解毒素インターメディリシンのヒト細胞特異的感染因子としての役割, 第80回日本細菌学会総会, Mar. 2007.
254.	今木英統, Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : GrlR，GrlAによる腸管出血性大腸菌(EHEC)のLEE領域発現制御機構の解析, 第80回日本細菌学会総会, Mar. 2007.
255.	Toshifumi Tomoyasu, Atsushi Tabata and Hideaki Nagamune : 腸管出血性大腸菌(EHEC)のLEE領域発現制御機構の解析, 第59回日本細菌学会中国・四国支部総, Oct. 2006.
256.	福島江, Atsushi Tabata, Toshifumi Tomoyasu, 大倉一人, 大国壽士 and Hideaki Nagamune : Sm-hPAFの受容体多様性:コレステロール依存性細胞溶解毒素の分子進化, 第59回日本細菌学会中国・四国支部総, Oct. 2006.

Products:

1.	Atsushi Tabata : 細胞膜に障害を及ぼすレンサ球菌由来溶血毒素の構造的および機能的な多様性, 生化学6, Vol.95, No.6, 757-764, Dec. 2023.
2.	Atsushi Tabata : Cytotoxin producing Anginosus group streptococci and their potential pathogenicity, 月刊「細胞」, Vol.54, No.10, 54(588)-57(591), Sep. 2022.

Et cetera, Workshop:

1.	Atsushi Tabata, Yoshihiro Uto and 大倉一人 : UTX-114ファミリーとEGFR-tykとの相互作用解析:アセチルグルコース付加によるゲフィチニブ機能の修飾, 第27回バイオ治療法学会, Dec. 2023.
2.	Atsushi Tabata, YOKOHATA Shuto, 大倉一人, Toshifumi Tomoyasu and Hideaki Nagamune : ペプチド溶血毒素ストレプトリジンSの血液成分による安定化と病原性への寄与, 第53回レンサ球菌研究会, Jul. 2023.
3.	Atsushi Tabata and 大倉一人 : C-配糖体型SGLT2阻害剤の分子特性:ヒトSGLT2モデルとの相互作用解析, 第26回日本バイオ治療法学会学術集会, Dec. 2022.
4.	Atsushi Tabata, Yoshihiro Uto and 大倉一人 : UTX-51誘導体とモデル標的タンパク質との相互作用:中性子照射による終末糖化産物破壊に寄与するボロントレース化合物の開発, 第25回バイオ治療法研究会学術集会, Dec. 2021.
5.	Atsushi Tabata, 立松洋平 and 大倉一人 : リアルタイム薬剤検出システムの構築試行:ミトコンドリア酸素消費速度を利用した担体からの薬剤放出特性の解析, 第24回バイオ治療法研究会学術集会, Dec. 2020.
6.	Atsushi Tabata, Yoshihiro Uto, Hitoshi Hori and Kazuto Ohkura : Chiral-2-nitroimidazole骨格を足場としたTX-2036誘導体の特性:EGF受容体キナーゼドメインとの相互作用, 第23回バイオ治療法研究会学術集会, Dec. 2019.
7.	Takashi Amoh, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Katsuhiko Hirota, Yoichiro Miyake and Hideki Fujii : 幼児口腔内から検出された多剤耐性レンサ球菌について, 第71回日本細菌学会中国，四国支部総会, Oct. 2018.
8.	Atsushi Tabata, 安養寺夏希, 大久保行将, 北條恵子, 水品善之, Toshifumi Tomoyasu and Hideaki Nagamune : Development of surface-processing systems as targeting technology of nano-particles, --- Optimization of the transpeptidase reaction of bacterial sortase A using GFP-substrate panel and investigation for its applications ---, 神戸学院大学ライフサイエンス産学連携研究センター, Mar. 2014.
9.	Atsushi Tabata, 大久保行将, 安養寺夏希, Toshifumi Tomoyasu and Hideaki Nagamune : Development of surface-processing systems as targeting technology of nano-particles, --- Development and investigation of SrtA substrate-producing system for surface processing ---, 神戸学院大学ライフサイエンス産学連携研究センター, Mar. 2013.
10.	Atsushi Tabata, 大久保行将, Toshifumi Tomoyasu and Hideaki Nagamune : 標的細胞に対する汎用性を高めたDDSツールの構築とその機能に関する評価, 第16回バイオ治療法研究会学術集会, Dec. 2012.
11.	Toshifumi Tomoyasu, Ayumi Okamoto, Hidenori Imaki, Atsushi Tabata and Hideaki Nagamune : ラクトースリプレッサーLacRによるインターメディリシン遺伝子の発現抑制, 第19回Lancefieldレンサ球菌研究会, Jun. 2010.
12.	Atsushi Tabata, 山本泰裕, Toshifumi Tomoyasu, Katsuhiko Hirota, Yoichiro Miyake, 大国寿士 and Hideaki Nagamune : 2種のコレステロール依存性細胞溶解毒素を産生する川崎病患児由来Streptococcus mitis Nm-65株の病原性に関する検討, 第19回Lancefieldレンサ球菌研究会, Jun. 2010.

Report:

1.	Atsushi Tabata : 川崎病児由来レンサ球菌が産生するコレステロール依存性細胞溶解毒素による血管炎症惹起メカニズムの解明, 公益財団法人大山健康財団 2023年度年報, Vol.49, 19-22, Dec. 2023.

Patent:

1.	Hideaki Nagamune, Toshifumi Tomoyasu and Atsushi Tabata : Cholesterol-dependent cytolysin variant and use thereof in DDS, WO2012/121395 A1 (Sep. 2012), .
2.	佐々木健二, 綿矢有佑, 金惠淑, 高麗寛紀, Atsushi Tabata, 難波哲人, 清武義弘, 田村卓二 and 吉田宗弘 : 新規抗マラリア剤, 2003-419719 (Dec. 2003), 2005-179212 (Jul. 2005), .

Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)

バイオマス由来の低分子化リグニンを活用したカビの次世代型光殺菌技術の開発 (Project/Area Number: 23K27041 )
Molecular characteristics specific for streptolysin S produced by human opportunistic Anginosus group streptococci (Project/Area Number: 23K09139 )
病原性連鎖球菌に由来する細胞傷害因子の構造機能解析と感染制御への応用 (Project/Area Number: 21K06655 )
The environmental determinant for Anginosus group streptococci to be the human pathogen. (Project/Area Number: 20K09919 )
Molecular evolution of hemolysins involved in oral streptococcal pathogenicity (Project/Area Number: 18K09552 )
Functional analysis of streptococcal toxins (Project/Area Number: 18K06764 )
Importance for the existence of mobile-genetic elements in cytotoxic Anginosus group streptococci (Project/Area Number: 17K11615 )
Characterization of the molecular properties of streptolysin S homolog secreted from Anginosus group streptococci (Project/Area Number: 15K20361 )
Pathogenicity acquisition mechanism of oral streptococci via gene transfer and expression of cytolysin genes (Project/Area Number: 15K11012 )
Role of a novel secreted glycosidase for pathogenicity of a human-specific pathogenic streptococci. (Project/Area Number: 26460528 )
Investigation for the pathogenic potential of streptolysin S homolog secreted from beta-hemolytic oral streptococci (Project/Area Number: 25861746 )
Highly pathogenic Streptococcus mitis exists: A study on its pathogenicity and epidemiology (Project/Area Number: 24592769 )
Investigation of the regulatory mechanism for the production of a human specific cytolysin, a crucial factor for the infectivity of Streptococcus intermedius (Project/Area Number: 23590510 )
Development of a cancer treatment technique using intracellular collapsing liposomes directed to cancer with double safety systems (Project/Area Number: 21590115 )
Regulation of pathogenicity by the heat shock chaperone and the protease in streptococci (Project/Area Number: 19590449 )
連鎖球菌が持つCD59指向性コレステロール依存性細胞溶解毒素の作用機構 (Project/Area Number: 18890127 )
Molecular mechanism of human-specific infection by an oral streptococcus, Streptococcusintermedius (Project/Area Number: 18592004 )
Expression control mechanisms of LEE pathogenic factors by AAA proteases in Enterohaemorrhagic and Enteropathogenic Eschericha coli (Project/Area Number: 17590387 )
Search by Researcher Number (10432767)

Professor : Tabata, Atsushi

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Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)