Tokushima University / Educator and Researcher Directory --- Fukui, Kiyoshi

Personal Web Page

https://researchmap.jp/read0002644 (researchmap)

https://orcid.org/0000-0002-7438-4938 (ORCID)

Field of Study

○	Vitaminology
○	Molecular Biology
○	Biochemistry

Subject of Study

○	ビタミンB関連酵素の疾患酵素学
○	Molecular Mechanism of apoptosis regulating development and cell differentiation
○	Molecular Eznymology on D-amino acid biosystems in the neural network regulation, Structure proteomics of proteins in D-amino acid metabolism and apoptosis

Book / Paper

Book:

1.	Kiyoshi Fukui : ビタミン・バイオファクター総合事典, 朝倉書店, Tokyo, Jul. 2021.
2.	Yusuke Kato, Diem Hong Tran, Huong Thi Thanh Trinh and Kiyoshi Fukui : Chapter 19: D-Amino Acid Oxidase and D-Aspartate Oxidase, Springer, Sep. 2016.
3.	Kiyoshi Fukui : ビタミン総合事典, 朝倉書店, Tokyo, Nov. 2010.
4.	Kiyoshi Fukui : タンパク質・アミノ酸の新栄養学, 株式会社講談社サイエンティフィク, Tokyo, Mar. 2007.
5.	Hwan Ki Park, Yoshiteru Urai, Osamu Jinnouchi, Atsuhiko Suzue, Tokujiro Kanamori, Kyung Tak Kwak, Oded-Ben Yoseph, Shinji Nagahiro and Kiyoshi Fukui : 6-12 Astroglial expression of D-amino acid oxidase, --- regional and cell-type specific expression ---, Nova Science Publishers, New York, Jan. 2007.
6.	Yoshihiro Miyake and Kiyoshi Fukui : 第15章 D-アミノ酸オキシダーゼ, 株式会社廣川書店, Tokyo, Feb. 2000.
7.	Kiyoshi Fukui : 第2章病気の分子生物学第2節循環器系, 朝倉書店, Tokyo, Nov. 1997.
8.	Yoshihiro Miyake and Kiyoshi Fukui : XIII-ビタミン·カルシウムとその異常 c.ビタミンC, Nakayama-Shoten Co., Ltd., Tokyo, Nov. 1995.
9.	Kiyoshi Fukui : Southern Blotting, Nankodo, Tokyo, Mar. 1995.

Academic Paper (Judged Full Paper):

1.	Hirofumi Sogabe, Yuji Shishido, Hayato Miyazaki, SooHyeon Kim, Wanitcha Rachadech and Kiyoshi Fukui : Dynamics of D-amino acid oxidase in kidney epithelial cells under amino acid starvation, The Journal of Biochemistry, Vol.170, No.1, 119-129, 2021. (Summary) D-amino acid oxidase (DAO) is a flavoenzyme catalyzing the oxidation of D-amino acid (AA)s. In the kidney, its expression is detected in proximal tubules, and DAO is considered to play a role in the conversion of D-form AAs to α-keto acids. LLC-PK1 cells, a pig renal proximal tubule cell line, were used to elucidate the regulation of DAO protein synthesis and degradation. In this study, we showed that trypsinization of LLC-PK1 cells in culture system rapidly reduced the intracellular DAO protein level to approximately 33.9% of that before treatment, even within 30 min. Furthermore, we observed that the DAO protein level was decreased when LLC-PK1 cells were subjected to AA starvation. To determine the degradation pathway, we treated the cells with chloroquine and MG132. DAO degradation was found to be inhibited by chloroquine, but not by MG132 treatment. We next examined whether or not DAO was degraded by autophagy. We found that AA starvation led to an increased accumulation of LC3-II, suggesting that DAO protein is degraded by autophagy due to AA starvation conditions. Furthermore, treatment with cycloheximide inhibited DAO protein degradation. Taken together, DAO protein is degraded by autophagy under starvation. The present study revealed the potential dynamics of DAO correlated with renal pathophysiology. (Tokushima University Institutional Repository) ● Metadata: 116073 (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvab029 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33725110 ● Search Scopus @ Elsevier (PMID): 33725110 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvab029 (Tokushima University Institutional Repository: 116073, DOI: 10.1093/jb/mvab029, PubMed: 33725110)
2.	Yusuke Kato, Kazuhiro Takahashi, Fuyu Ito, Shoichi Suzuki, Kiyoshi Fukui, Masakazu Mimaki and Kazuo Suzuki : Novel oseltamivir-resistant mutations distant from the active site of influenza B neuraminidase, Journal of Biomolecular Structure & Dynamics, Vol.39, No.10, 3491-3500, 2021. (Summary) We performed a neuraminidase sequence analysis of thirty-two pediatric patients with influenza B who visited Teikyo University Hospital from January 2016 to March 2017, and found oseltamivir-resistant samples belonging to the Yamagata and Victoria lineages. Comparison with the neuraminidase sequence of oseltamivir-susceptible B/Brisbane/60/2008 revealed 5 common amino acid substitutions in many of these samples. According to the binding free energy calculation, the N340D and E358K substitutions reduced the affinity of oseltamivir to neuraminidase. Unexpectedly, these substitutions were located distant from the oseltamivir-binding site in neuraminidase. According to the molecular dynamics simulations, the N340D substitution rearranged complicated hydrogen bond networks in an extensive surface region of neuraminidase. The E358K substitution extensively altered the electrostatic potential map of the overall neuraminidase structure. Through these novel mechanisms, the N340D and E358K substitutions indirectly influenced the affinity reduction. These results may be useful for designing drugs for the treatment of oseltamivir-resistant virus infections.Communicated by Ramaswamy H. Sarma. (Link to Publication Site) ● Publication site (DOI): 10.1080/07391102.2020.1765872 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32406800 ● Summary page in Scopus @ Elsevier: 2-s2.0-85086049154 (DOI: 10.1080/07391102.2020.1765872, PubMed: 32406800, Elsevier: Scopus)
3.	Wanitcha Rachadech, Yusuke Kato, Rabab Magd El Abou Mohamed Ahmed, Yuji Shishido, SooHyeon Kim, Hirofumi Sogabe, Nobuo Maita, Kazuko YORITA and Kiyoshi Fukui : P219L substitution in human D-amino acid oxidase impacts the ligand binding and catalytic efficiency, The Journal of Biochemistry, Vol.168, No.5, 557-567, 2020. (Summary) Human D-amino acid oxidase (DAO) is a flavoenzyme that is implicated in neurodegenerative diseases. We investigated the impact of replacement of proline with leucine at Position 219 (P219L) in the active site lid of human DAO on the structural and enzymatic properties, because porcine DAO contains leucine at the corresponding position. The turnover numbers (kcat) of P219L were unchanged, but its Km values decreased compared with wild-type, leading to an increase in the catalytic efficiency (kcat/Km). Moreover, benzoate inhibits P219L with lower Ki value (0.7-0.9 µM) compared with wild-type (1.2-2.0 µM). Crystal structure of P219L in complex with flavin adenine dinucleotide (FAD) and benzoate at 2.25 Å resolution displayed conformational changes of the active site and lid. The distances between the H-bond-forming atoms of arginine 283 and benzoate and the relative position between the aromatic rings of tyrosine 224 and benzoate were changed in the P219L complex. Taken together, the P219L substitution leads to an increase in the catalytic efficiency and binding affinity for substrates/inhibitors due to these structural changes. Furthermore, an acetic acid was located near the adenine ring of FAD in the P219L complex. This study provides new insights into the structure-function relationship of human DAO. (Keyword) Amino Acid Sequence / Amino Acid Substitution / Catalysis / Catalytic Domain / Crystallography, X-Ray / D-Amino-Acid Oxidase / Humans / Ligands / Models, Molecular / Neurodegenerative Diseases / Protein Conformation / Structure-Activity Relationship (Tokushima University Institutional Repository) ● Metadata: 116051 (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvaa083 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32730563 ● CiNii @ National Institute of Informatics (CRID): 1523669555785559936 ● Search Scopus @ Elsevier (PMID): 32730563 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvaa083 (Tokushima University Institutional Repository: 116051, DOI: 10.1093/jb/mvaa083, PubMed: 32730563, CiNii: 1523669555785559936)
4.	Soo Hyeon Kim, Yuji Shishido, Hirofumi Sogabe, Wanitcha Rachadech, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : Age- and gender-dependent D-amino acid oxidase activity in mouse brain and peripheral tissues: implication for aging and neurodegeneration, The Journal of Biochemistry, Vol.166, No.2, 187-196, 2019. (Summary) D-amino acid oxidase (DAO) is a flavoenzyme, catalysing oxidative deamination of D-amino acids to produce corresponding α-keto acids, ammonia and hydrogen peroxide. In our search for DAO activity among various tissues, we developed a sensitive assay based on hydrogen peroxide production involving enzyme-coupled colorimetric assay with peroxidase. We first optimized buffer components to extract DAO protein from mouse tissues. Here we show that DAO activity was detected in kidney, cerebellum, medulla oblongata, midbrain and spinal cord, but not in liver. In addition, we observed that DAO activity and expression were decreased in thoracic and lumbar regions of spinal cord in aged mice when compared with young mice, indicating that decreased DAO is involved in motoneuron degeneration during senescence. We also found gender difference in DAO activity in the kidney, suggesting that DAO activity is influenced by sexual dimorphism. We newly detected DAO activity in the epididymis, although undetected in testis. Furthermore, DAO activity was significantly higher in the caput region than corpus and cauda regions of epididymis, indicating that D-amino acids present in the testis are eliminated in epididymis. Taken together, age- and gender-dependent DAO activity in each organ may underlie the human pathophysiology regulated by D-amino acid metabolism. (Tokushima University Institutional Repository) ● Metadata: 113627 (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvz025 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30938755 ● Search Scopus @ Elsevier (PMID): 30938755 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvz025 (Tokushima University Institutional Repository: 113627, DOI: 10.1093/jb/mvz025, PubMed: 30938755)
5.	Yusuke Kato, Niyada Hin, Nobuo Maita, Ajit G. Thomas, Sumire Kurosawa, Camilo Rojas, Kazuko YORITA, Barbara S. Slusher, Kiyoshi Fukui and Takashi Tsukamoto : Structural basis for potent inhibition of d-amino acid oxidase by thiophene carboxylic acids, European Journal of Medicinal Chemistry, Vol.159, 23-34, 2018. (Summary) A series of thiophene-2-carboxylic acids and thiophene-3-carboxylic acids were identified as a new class of DAO inhibitors. Structure-activity relationship (SAR) studies revealed that small substituents are well-tolerated on the thiophene ring of both the 2-carboxylic acid and 3-carboxylic acid scaffolds. Crystal structures of human DAO in complex with potent thiophene carboxylic acids revealed that Tyr224 was tightly stacked with the thiophene ring of the inhibitors, resulting in the disappearance of the secondary pocket observed with other DAO inhibitors. Molecular dynamics simulations of the complex revealed that Tyr224 preferred the stacked conformation irrespective of whether Tyr224 was stacked or not in the initial state of the simulations. MM/GBSA indicated a substantial hydrophobic interaction between Tyr244 and the thiophene-based inhibitor. In addition, the active site was tightly closed with an extensive network of hydrogen bonds including those from Tyr224 in the stacked conformation. The introduction of a large branched side chain to the thiophene ring markedly decreased potency. These results are in marked contrast to other DAO inhibitors that can gain potency with a branched side chain extending to the secondary pocket due to Tyr224 repositioning. These insights should be of particular importance in future efforts to optimize DAO inhibitors with novel scaffolds. (Keyword) Carboxylic Acids / X-ray crystallography / D-amino acid oxidase / Dose-Response Relationship, Drug / Enzyme Inhibitors / Humans / Models, Molecular / molecular structure / structureactivity relationship / Thiophenes (Tokushima University Institutional Repository) ● Metadata: 112839 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.ejmech.2018.09.040 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30265959 ● Summary page in Scopus @ Elsevier: 2-s2.0-85053806498 (Tokushima University Institutional Repository: 112839, DOI: 10.1016/j.ejmech.2018.09.040, PubMed: 30265959, Elsevier: Scopus)
6.	Yusuke Kato, Hiroshi Kihara, Kiyoshi Fukui and Masaki Kojima : A ternary complex model of Sirtuin4-NAD⁺-Glutamate dehydrogenase, Computational Biology and Chemistry, Vol.74, 94-104, 2018. (Keyword) Sirtuin / Metabolism / Homology modeling / Cancer / Docking / Ischemic heart disease (Tokushima University Institutional Repository) ● Metadata: 112024 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.compbiolchem.2018.03.006 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/j.compbiolchem.2018.03.006 (Tokushima University Institutional Repository: 112024, DOI: 10.1016/j.compbiolchem.2018.03.006)
7.	Akira Nishi, Shusuke Numata, Atsushi Tajima, Xiaolei Zhu, Koki Ito, Atsushi Saito, Yusuke Kato, Makoto Kinoshita, Shinji Shimodera, Shinji Ono, Shinichiro Ochi, Akira Imamura, Naohiro Kurotaki, Shu-Ichi Ueno, Nakao Iwata, Kiyoshi Fukui, Issei Imoto, Atsushi Kamiya and Tetsuro Ohmori : De novo non-synonymous TBL1XR1 mutation alters Wnt signaling activity., Scientific Reports, Vol.7, No.1, 2887, 2017. (Summary) Here we report de novo non-synonymous single-nucleotide variants (SNVs) by conducting whole exome sequencing of 18 trios consisting of Japanese patients with sporadic schizophrenia and their parents. Among nine SNVs, we explored the functional impact of the de novo mutation in TBL1XR1 [c.30 C > G (p.Phe10Leu)], a gene previously found to be associated with autism spectrum disorder and epilepsy. Protein structural analysis revealed that Phe10Leu mutation may decrease the structural stability of the TBL1XR1 protein. We demonstrate that Phe10Leu mutation alters the interaction of TBL1XR1 with N-CoR and β-catenin, which play critical roles in regulation of Wnt-mediated transcriptional activity. Consistently, TBL1XR1-mediated activation of Wnt signaling was up-regulated by Phe10Leu mutation. These results suggest that a de novo TBL1XR1 point mutation could alter Wnt/β-catenin signaling activity. Further studies are required to clarify the involvement of TBL1XR1 mutations in neuropsychiatric conditions. (Tokushima University Institutional Repository) ● Metadata: 110165 (Link to Publication Site) ● Publication site (DOI): 10.1038/s41598-017-02792-z (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28588275 ● Summary page in Scopus @ Elsevier: 2-s2.0-85020428321 (Tokushima University Institutional Repository: 110165, DOI: 10.1038/s41598-017-02792-z, PubMed: 28588275, Elsevier: Scopus)
8.	Taiki Kohiki, Yusuke Kato, Yusuke Nishikawa, Kazuko YORITA, Ikuko Sagawa, Masaya Denda, Tsubasa Inokuma, Akira Shigenaga, Kiyoshi Fukui and Akira Otaka : Inside Front Cover: Elucidation of inhibitor-binding pocket of D-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology, Organic & Biomolecular Chemistry, Vol.15, 5240, 2017. (Link to Publication Site) ● Publication site (DOI): 10.1039/C7OB90109G (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1039/C7OB90109G (DOI: 10.1039/C7OB90109G)
9.	Taiki Kohiki, Yusuke Kato, Yusuke Nishikawa, Kazuko YORITA, Ikuko Sagawa, Masaya Denda, Tsubasa Inokuma, Akira Shigenaga, Kiyoshi Fukui and Akira Otaka : Elucidation of inhibitor-binding pocket of D-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology, Organic & Biomolecular Chemistry, Vol.15, No.25, 5289-5297, 2017. (Tokushima University Institutional Repository) ● Metadata: 111927 (Link to Publication Site) ● Publication site (DOI): 10.1039/C7OB00633K (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1039/C7OB00633K (Tokushima University Institutional Repository: 111927, DOI: 10.1039/C7OB00633K)
10.	Do Youn Jun, Hyejin Kim, Won Young Jang, Ji Young Lee, Kiyoshi Fukui and Young Ho Kim : Ectopic overexpression of LAPTM5 results in lysosomal targeting and induces Mcl-1 down-regulation, Bak activation, and mitochondria-dependent apoptosis in human HeLa cells, PLoS ONE, Vol.12, No.5, e0176544, 2017. (Summary) Human lysosomal-associated protein multispanning membrane 5 (LAPTM5) was identified by an ordered differential display-polymerase chain reaction (ODD-PCR) as an up-regulated cDNA fragment during 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced differentiation of U937 cells into monocytes/macrophages. After TPA-treatment, the levels of LAPTM5 mRNA and protein increased and reached a maximum at 18-36 h. In healthy human tissues, LAPTM5 mRNA was expressed at high levels in hematopoietic cells and tissues, at low levels in the lung and fetal liver, and was not detected in other non-hematopoietic tissues. LAPTM5 mRNA was detected in immature malignant cells of myeloid lineage, such as K562, HL-60, U937, and THP-1 cells, and in unstimulated peripheral T cells, but was absent or barely detectable in lymphoid malignant or non-hematopoietic malignant cells. The LAPTM5 level in HL-60 cells increased more significantly during TPA-induced monocyte/macrophage differentiation than during DMSO-induced granulocyte differentiation. Ectopic expression of GFP-LAPTM5 or LAPTM5 in HeLa cells exhibited the localization of LAPTM5 to the lysosome. In HeLa cells overexpressing LAPTM5, the Mcl-1 and Bid levels declined markedly and apoptosis was induced via Bak activation, Δψm loss, activation of caspase-9, -8 and -3, and PARP degradation without accompanying necrosis. However, these LAPTM5-induced apoptotic events except for the decline of Bid level were completely abrogated by concomitant overexpression of Mcl-1. The pan-caspase inhibitor (z-VAD-fmk) could suppress the LAPTM5-induced apoptotic sub-G1 peak by ~40% but failed to block the induced Δψm loss, whereas the broad-range inhibitor of cathepsins (Cathepsin Inhibitor I) could suppress the LAPTM5-induced apoptotic sub-G1 peak and Δψm loss, by ~22% and ~23%, respectively, suggesting that the LAPTM5-mediated Δψm loss was exerted at least in part in a cathepsin-dependent manner. Together, these results demonstrate that ectopic overexpression of LAPTM5 in HeLa cells induced apoptosis via cleavage of Mcl-1 and Bid by a LAPTM5-associated lysosomal pathway, and subsequent activation of the mitochondria-dependent caspase cascade. (Keyword) Apoptosis / Down-Regulation / Ectopic Gene Expression / HeLa Cells / Humans / Lysosomes / Membrane Proteins / Mitochondria / Myeloid Cell Leukemia Sequence 1 Protein / bcl-2 Homologous Antagonist-Killer Protein (Tokushima University Institutional Repository) ● Metadata: 112313 (Link to Publication Site) ● Publication site (DOI): 10.1371/journal.pone.0176544 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28464033 ● Search Scopus @ Elsevier (PMID): 28464033 ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0176544 (Tokushima University Institutional Repository: 112313, DOI: 10.1371/journal.pone.0176544, PubMed: 28464033)
11.	Yusuke Kato and Kiyoshi Fukui : Structure models of G72, the product of a susceptibility gene to schizophrenia, The Journal of Biochemistry, Vol.161, No.2, 223-230, 2017. (Summary) The G72 gene is one of the most susceptible genes to schizophrenia and is contained exclusively in the genomes of primates. The product of the G72 gene modulates the activity of D-amino acid oxidase (DAO) and is a small protein prone to aggregate, which hampers its structural studies. In addition, lack of a known structure of a homologue makes it difficult to use the homology modelling method for the prediction of the structure. Thus, we first developed a hybrid ab initio approach for small proteins prior to the prediction of the structure of G72. The approach uses three known ab initio algorithms. To evaluate the hybrid approach, we tested our prediction of the structure of the amino acid sequences whose structures were already solved and compared the predicted structures with the experimentally solved structures. Based on these comparisons, the average accuracy of our approach was calculated to be ∼5 Å. We then applied the approach to the sequence of G72 and successfully predicted the structures of the N- and C-terminal domains (ND and CD, respectively) of G72. The predicted structures of ND and CD were similar to membrane-bound proteins and adaptor proteins, respectively. (Keyword) Algorithms / Amino Acid Sequence / Carrier Proteins / Computational Biology / Genetic Predisposition to Disease / Genetic Variation / Humans / Intracellular Signaling Peptides and Proteins / Molecular Dynamics Simulation / Protein Domains / Protein Structure, Secondary / Reproducibility of Results / Schizophrenia (Tokushima University Institutional Repository) ● Metadata: 110891 (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvw064 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27815320 ● Summary page in Scopus @ Elsevier: 2-s2.0-85015838860 (Tokushima University Institutional Repository: 110891, DOI: 10.1093/jb/mvw064, PubMed: 27815320, Elsevier: Scopus)
12.	Shohei Toguchi, Tomoyasu Hirose, Kazuko YORITA, Kiyoshi Fukui, Barry K Sharpless, Satoshi Ōmura and Toshiaki Sunazuka : In Situ Click Chemistry for the Identification of a Potent D-Amino Acid Oxidase Inhibitor., Chemical & Pharmaceutical Bulletin, Vol.64, No.7, 695-703, 2016. (Summary) In situ click chemistry is a target-guided synthesis approach for discovering novel lead compounds by assembling organic azides and alkynes into triazoles inside the affinity site of target biogenic molecules such as proteins. We report in situ click chemistry screening with human D-amino acid oxidase (hDAO), which led to the identification of a more potent hDAO inhibitor. The hDAO inhibitors have chemotherapeutic potential as antipsychotic agents. The new inhibitor displayed competitive inhibition of hDAO and showed significantly increased inhibitory activity against hDAO compared with that of an anchor molecule of in situ click chemistry. (Tokushima University Institutional Repository) ● Metadata: 115431 (Link to Publication Site) ● Publication site (DOI): 10.1248/cpb.c15-00867 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26686243 ● Summary page in Scopus @ Elsevier: 2-s2.0-84977529588 (Tokushima University Institutional Repository: 115431, DOI: 10.1248/cpb.c15-00867, PubMed: 26686243, Elsevier: Scopus)
13.	Yusuke Kato, Kiyoshi Fukui and Kazuo Suzuki : Mechanism of a Mutation in Non-Structural Protein 1 Inducing High Pathogenicity of Avian Influenza Virus H5N1., Protein and Peptide Letters, Vol.23, No.4, 372-378, 2016. (Summary) Avian influenza H5N1 has shown high mortality rate in human. Non-structural protein 1 (NS1) is a virulence factor of H5N1. Mutation at the 42nd residue within the RNA-binding domain (RBD) of NS1 dramatically changes the degree of pathogenicity of H5N1 in mice. We here studied the impact of this mutation on the function of RBD, and found that RBD with serine at the 42th residue binds double-stranded RNA (dsRNA), whereas that with proline at the 42th residue does not. Analysis of structural models of the RBD proteins with S42 and P42 suggested remarkable difference in the structure of the dsRNA-binding interface, whereas structural analysis by analytical gel filtration and CD measurements did not indicate difference between those RBD proteins. Our results suggest that the single amino acid replacement induces a minor, but global structural change leading to the loss of function of NS1 thereby the change in the degree of pathogenicity. (Tokushima University Institutional Repository) ● Metadata: 110030 (Link to Publication Site) ● Publication site (DOI): 10.2174/0929866523666160204124406 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26845765 ● Summary page in Scopus @ Elsevier: 2-s2.0-84961707855 (Tokushima University Institutional Repository: 110030, DOI: 10.2174/0929866523666160204124406, PubMed: 26845765, Elsevier: Scopus)
14.	Diem Hong Tran, Yuji Shishido, Seongpil Chung, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Identification of DNA-binding proteins that interact with the 5-flanking region of the human d-amino acid oxidase gene by pull-down assay coupled with two-dimensional gel electrophoresis and mass spectrometry, Journal of Pharmaceutical and Biomedical Analysis, Vol.116, 94-100, 2015. (Summary) d-Amino acid oxidase (DAO) is a flavoenzyme that metabolizes d-amino acids and is expected to be a promising therapeutic target of schizophrenia and glioblastoma. The study of DNA-binding proteins has yielded much information in the regulation of transcription and other biological processes. However, proteins interacting with DAO gene have not been elucidated. Our assessment of human DAO promoter activity using luciferase reporter system indicated the 5'-flanking region of this gene (-4289bp from transcription initiation site) has a regulatory sequence for gene expression, which is regulated by multi-protein complexes interacting with this region. By using pull-down assay coupled with two-dimensional gel electrophoresis and mass spectrometry, we identified six proteins binding to the 5'-flanking region of the human DAO gene (zinc finger C2HC domain-containing protein 1A; histidine-tRNA ligase, cytoplasmic; molybdenum cofactor biosynthesis protein; 60S ribosomal protein L37; calponin-1; calmodulin binding protein and heterogeneous nuclear ribonucleoprotein A2/B1). These preliminary results will contribute to the advance in the understanding of the potential factors associated with the regulatory mechanism of DAO expression. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jpba.2015.02.031 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25749303 ● Search Scopus @ Elsevier (PMID): 25749303 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jpba.2015.02.031 (DOI: 10.1016/j.jpba.2015.02.031, PubMed: 25749303)
15.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : Nucling, a Novel Apoptosis-associated Protein, Controls Mammary Gland Involution by Regulating NF-B and STAT3, The Journal of Biological Chemistry, Vol.290, No.40, 24626-24635, 2015. (Summary) Postpartum mammary gland involution is the physiological process by which the lactating gland returns to its pre-pregnant state. In rodent models, the microenvironment of mammary gland involution is sufficient to induce enhanced tumor cell growth, local invasion, and metastasis. Therefore, a deeper understanding of the physiological regulation of involution may provide in-depth information on breast cancer therapy. We herein identified Nucling as an important regulator of involution of the mammary gland. A knock-out mouse model was generated and revealed that postpartum involution were impaired in mice lacking Nucling. Involution is normally associated with an increase in the activation of NF-B and STAT3, which is required for the organized regulation of involution, and was observed in WT glands, but not in the absence of Nucling. Furthermore, the loss of Nucling led to the suppression of Calpain-1, IL-6, and C/EBP factors, which are known to be essential for normal involution. The number of M2 macrophages, which are crucial for epithelial cell death and adipocyte repopulation after weaning, was also reduced in Nucling-KO glands. Taken together, the results of the present study demonstrated that Nucling played an important role in mammary gland involution by regulating NF-B and STAT3 signaling pathways. (Tokushima University Institutional Repository) ● Metadata: 109502 (Link to Publication Site) ● Publication site (DOI): 10.1074/jbc.M115.673848 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26269594 ● Search Scopus @ Elsevier (PMID): 26269594 ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M115.673848 (Tokushima University Institutional Repository: 109502, DOI: 10.1074/jbc.M115.673848, PubMed: 26269594)
16.	Diem Hong Tran, Yuji Shishido, Seongpil Chung, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Identification of two promoters for human D-amino acid oxidase gene: implication for the differential promoter regulation mediated by PAX5/PAX2, The Journal of Biochemistry, Vol.157, No.5, 377-387, 2015. (Summary) D-amino acid oxidase (DAO) is a flavoenzyme that metabolizes d-amino acids. Until now, the DAO expression mechanism is still unclear. Our assessment of human DAO (hDAO) promoter activity using luciferase reporter system indicated the proximal upstream region of exon1 (-237/+1) has promoter activity (P1). Interestingly, we identified an alternative promoter in the proximal upstream region of exon2 (+4,126/+4,929) (P2). This alternative promoter has stronger activity than that of P1. Our results also revealed a negative regulatory segment (+1,163/+1,940) in intron1; that would act in concert with P1 and P2. Bioinformatics analyses elucidated the conservation of transcription factor PAX5 family binding sites among species. These sites (-60/-31) and (+4,464/+4,493), locate in P1 and P2 of hDAO, respectively. Gel shift assays demonstrated P1 contains a site (-60/-31) for PAX5 binding while P2 has three sites for both paired box gene 2 (PAX2) and paired box gene 5 (PAX5) binding. The dual roles of PAX5 family in regulating hDAO transcription by modulating promoter activity of P1 and activating promoter activity of P2 were implicated based on the site-directed mutagenesis experiment. Altogether, our data suggested the differential regulation of hDAO expression by two promoters whose activities may be modulated by the binding of PAX2 and PAX5. (Keyword) D-amino acid oxidase / promoter / transcription factor / PAX5 / PAX2 (Tokushima University Institutional Repository) ● Metadata: 106442 (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvu084 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25500505 ● Summary page in Scopus @ Elsevier: 2-s2.0-84944457818 (Tokushima University Institutional Repository: 106442, DOI: 10.1093/jb/mvu084, PubMed: 25500505, Elsevier: Scopus)
17.	Miho Shishikura, Hitomi Hakariya, Sumiko Iwasa, Takashi Yoshio, Hideaki Ichiba, Kazuko YORITA, Kiyoshi Fukui and Takeshi Fukushima : Evaluation of human D-amino acid oxidase inhibition by anti-psychotic drugs in vitro, Bioscience Trends, Vol.8, No.3, 149-154, 2014. (Summary) It is of importance to determine whether antipsychotic drugs currently prescribed for schizophrenia exert D-amino acid oxidase (DAO)-inhibitory effects. We first investigated whether human (h)DAO can metabolize D-kynurenine (D-KYN) to produce the fluorescent compound kynurenic acid (KYNA) by using high-performance liquid chromatography with mass spectrometry, and fluorescence spectrometry. After confirmation of KYNA production from D-KYN by hDAO, 8 first- and second-generation antipsychotic drugs, and 6 drugs often prescribed concomitantly, were assayed for hDAO-inhibitory effects by using in vitro fluorometric methods with D-KYN as the substrate. DAO inhibitors 3-methylpyrazole-5-carboxylic acid and 4H-thieno[3,2-b]pyrrole-5-carboxylic acid inhibited KYNA production in a dose-dependent manner. Similarly, the second-generation antipsychotics blonanserin and risperidone were found to possess relatively strong hDAO-inhibitory effects in vitro (5.29 ± 0.47 M and 4.70 ± 0.17 M, respectively). With regard to blonanserin and risperidone, DAO-inhibitory effects should be taken into consideration in the context of their in vivo pharmacotherapeutic efficacy. (Keyword) Antipsychotic Agents / D-Amino-Acid Oxidase / Enzyme Activation / Humans / Piperazines / Piperidines / Risperidone (Link to Publication Site) ● Publication site (DOI): 10.5582/bst.2014.01034 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25030849 ● CiNii @ National Institute of Informatics (CRID): 1390001205737899008 ● Summary page in Scopus @ Elsevier: 2-s2.0-84904859965 (DOI: 10.5582/bst.2014.01034, PubMed: 25030849, CiNii: 1390001205737899008, Elsevier: Scopus)
18.	Sayuri Ishiwata, Asami Umino, Masakazu Umino, Kazuko YORITA, Kiyoshi Fukui and Toru Nishikawa : Modulation of extracellular d-serine content by calcium permeable AMPA receptors in rat medial prefrontal cortex as revealed by in vivo microdialysis, The International Journal of Neuropsychopharmacology, Vol.16, No.6, 1395-1406, 2013. (Summary) In mammalian brains, d-serine has been shown to be required for the regulation of glutamate neurotransmission as an endogenous co-agonist for the N-methyl-d-aspartate type glutamate receptor that is essential for the expression of higher-order brain functions. The exact control mechanisms for the extracellular d-serine dynamics, however, await further elucidation. To obtain an insight into this issue, we have characterized the effects of agents acting at the α-amino-3-hydroxy-5-methyl-4-isoxazolepropioinic acid (AMPA) type glutamate receptor on the extracellular d-serine contents in the medial prefrontal cortex of freely moving rats by an in vivo microdialysis technique in combination with high-performance liquid chromatography with fluorometric detection. In vivo experiments are needed in terms of a crucial role of d-serine in the neuron-glia communications despite the previous in vitro studies on AMPA receptor-d-serine interactions using the separated preparations of neurons or glial cells. Here, we show that the intra-cortical infusion of (S)-AMPA, an active enantiomer at the AMPA receptor, causes a significant and concentration-dependent reduction in the prefrontal extracellular contents of d-serine, which is reversed by an AMPA/kainate receptor antagonist, 2,3-dioxo-6-nitro-1,2,3,4-tetrahydrobenzo[f]quinoxaline-7-sulfonamide disodium salt, and a calcium permeable AMPA receptor antagonist, 1-naphthyl acetyl spermine. The d-serine reducing effects of (S)-AMPA are augmented by co-infusion of cyclothiazide that prevents AMPA receptor desensitization. Our data support the view that a calcium permeable AMPA receptor subtype may exert a phasic inhibitory control on the extracellular d-serine release in the mammalian prefrontal cortex in vivo. (Link to Publication Site) ● Publication site (DOI): 10.1017/S1461145712001484 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23298512 ● Search Scopus @ Elsevier (PMID): 23298512 ● Search Scopus @ Elsevier (DOI): 10.1017/S1461145712001484 (DOI: 10.1017/S1461145712001484, PubMed: 23298512)
19.	Norihiro Shibuya, Shin Koike, Makiko Tanaka, Mari Ishigami-Yuasa, Yuka Kimura, Yuki Ogasawara, Kiyoshi Fukui, Noriyuki Nagahara and Hideo Kimura : A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells, Nature Communications, Vol.4, No.1366, 2013. (Summary) In eukaryotes, hydrogen sulphide acts as a signalling molecule and cytoprotectant. Hydrogen sulphide is known to be produced from L-cysteine by cystathionine -synthase, cystathionine -lyase and 3-mercaptopyruvate sulfurtransferase coupled with cysteine aminotransferase. Here we report an additional biosynthetic pathway for the production of hydrogen sulphide from D-cysteine involving 3-mercaptopyruvate sulfurtransferase and D-amino acid oxidase. Unlike the L-cysteine pathway, this D-cysteine-dependent pathway operates predominantly in the cerebellum and the kidney. Our study reveals that administration of D-cysteine protects primary cultures of cerebellar neurons from oxidative stress induced by hydrogen peroxide and attenuates ischaemia-reperfusion injury in the kidney more than L-cysteine. This study presents a novel pathway of hydrogen sulphide production and provides a new therapeutic approach to deliver hydrogen sulphide to specific tissues. (Keyword) Animals / Biosynthetic Pathways / Brain / Cells, Cultured / Cysteine / Cytoprotection / D-Amino-Acid Oxidase / Hydrogen Sulfide / Kidney / Male / Mammals / Mice / Mice, Inbred C57BL / Neurons / Organ Specificity / Oxidative Stress / Reperfusion Injury / Substrate Specificity / Sulfurtransferases (Link to Publication Site) ● Publication site (DOI): 10.1038/ncomms2371 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23340406 ● Search Scopus @ Elsevier (PMID): 23340406 ● Search Scopus @ Elsevier (DOI): 10.1038/ncomms2371 (DOI: 10.1038/ncomms2371, PubMed: 23340406)
20.	Sun Mi Kim, Takashi Sakai, Huy Van Dang, HoangNam Tran, Koji Ono, Kazunori Ishimura and Kiyoshi Fukui : Nucling, a novel protein associated with NF-B, regulates endotoxin-induced apoptosis in vivo, The Journal of Biochemistry, Vol.153, No.1, 93-101, 2013. (Summary) Nucling is a proapoptotic protein that regulates the apoptosome and nuclear factor-kappa B (NF-B) signalling pathways. Strong stimuli, such as Gram-negative bacterial lipopolysaccharide (LPS), induce the simultaneous secretion of cytokines following the activation of NF-B. Proinflammatory cytokines can induce liver damage through several mechanisms such as increases in oxidative stress and apoptotic reactions leading to tissue necrosis. Herein, we show that Nucling-knockout (KO) mice are resistant to LPS that consistently caused mortality in wild-type (WT) counterparts. Although serum levels of cytokines such as tumour necrosis factor (TNF)-, interleukin (IL)-1 and IL-6 did not differ significantly between WT and Nucling-KO mice after the LPS challenge, hepatocytes of Nucling-KO mice were refractory to LPS- or TNF--induced cell death. These results were consistent with the decreased expression of proapoptotic proteins including apoptosis-inducing factor and cleaved form of poly (ADP-ribose) polymerase and terminal deoxynucleotidyl transferase dUTP nick end-labelling positive cells in the liver of Nucling-KO mice after the administration of a lethal dose of LPS. Moreover, the upregulation of NF-B-regulated anti-apoptotic molecules including cellular inhibitor of apoptosis (cIAP) 1 and cIAP2 was observed in the liver of Nucling-KO mice after LPS treatment. These findings indicate that the Nucling deficiency leads to resistance to apoptosis in liver. We propose that Nucling is important for the induction of apoptosis in cells damaged by cytotoxic stressors through the NF-B signalling pathway. (Keyword) Animals / apoptosis / Apoptosis Regulatory Proteins / Cells, Cultured / cytokinesis / Disease Resistance / Down-Regulation / Endotoxins / Hepatocytes / Kupffer Cells / Male / Membrane Proteins / Mice / knockout mice / NF-kappa B / Shock, Septic / signal transduction / Specific Pathogen-Free Organisms / Survival Analysis / Survival Rate / Up-Regulation (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvs119 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23071121 ● Summary page in Scopus @ Elsevier: 2-s2.0-84871630704 (DOI: 10.1093/jb/mvs119, PubMed: 23071121, Elsevier: Scopus)
21.	Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Kazuko YORITA, Seongpil Chung, Diem Hong Tran, Takashi Sakai, Hiroyoshi Watanabe, Shoji Kagami and Kiyoshi Fukui : D-Amino acid oxidase-induced oxidative stress, 3-bromopyruvate and citrate inhibit angiogenesis, exhibiting potent anticancer effects, Journal of Bioenergetics and Biomembranes, Vol.44, No.5, 513-523, 2012. (Summary) Angiogenesis is critical for cancer growth and metastasis. Steps of angiogenesis are energy consuming, while vascular endothelial cells are highly glycolytic. Glioblastoma multiforme (GBM) is a highly vascular tumor and this enhances its aggressiveness. D-amino acid oxidase (DAO) is a promising therapeutic protein that induces oxidative stress upon acting on its substrates. Oxidative stress-energy depletion (OSED) therapy was recently reported (El Sayed et al., Cancer Gene Ther, 19, 1-18, 2012). OSED combines DAO-induced oxidative stress with energy depletion caused by glycolytic inhibitors such as 3-bromopyruvate (3BP), a hexokinase II inhibitor that depleted ATP in cancer cells and induced production of hydrogen peroxide. 3BP disturbs the Warburg effect and antagonizes effects of lactate and pyruvate (El Sayed et al., J Bioenerg Biomembr, 44, 61-79, 2012). Citrate is a natural organic acid capable of inhibiting glycolysis by targeting phosphofructokinase. Here, we report that DAO, 3BP and citrate significantly inhibited angiogenesis, decreased the number of vascular branching points and shortened the length of vascular tubules. OSED delayed the growth of C6/DAO glioma cells. 3BP combined with citrate delayed the growth of C6 glioma cells and decreased significantly the number and size of C6 glioma colonies in soft agar. Human GBM cells (U373MG) were resistant to chemotherapy e.g. cisplatin and cytosine arabinoside, while 3BP was effective in decreasing the viability and disturbing the morphology of U373MG cells. (Keyword) Adenosine Triphosphate / Animals / Antineoplastic Agents / Cell Line, Tumor / Chelating Agents / Cisplatin / Citric Acid / Cytarabine / D-Amino-Acid Oxidase / Drug Resistance, Neoplasm / Energy Metabolism / Enzyme Inhibitors / Glioblastoma / Hexokinase / Human Umbilical Vein Endothelial Cells / Humans / Hydrogen Peroxide / Mice / Neovascularization, Pathologic / Oxidative Stress / Pyruvates (Link to Publication Site) ● Publication site (DOI): 10.1007/s10863-012-9455-y (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22802136 ● Search Scopus @ Elsevier (PMID): 22802136 ● Search Scopus @ Elsevier (DOI): 10.1007/s10863-012-9455-y (DOI: 10.1007/s10863-012-9455-y, PubMed: 22802136)
22.	Kaori Kiso, Satoko Ueno, Mana Fukuda, Ikuyo Ichi, Keiko Kobayashi, Takashi Sakai, Kiyoshi Fukui and Shousuke Kojo : The Role of Kupffer Cells in Carbon Tetrachloride Intoxication in Mice, Biological & Pharmaceutical Bulletin, Vol.35, No.6, 980-983, 2012. (Summary) Carbon tetrachloride (CCl(4))-induced acute hepatitis is assumed to involve two phases. The initial phase, initiated within 2 h after CCl(4) administration, involves the generation of reactive oxygen species. The second phase is assumed to start about 8 h subsequent to CCl(4) administration and involves the oxidant-induced activation of Kupffer cells, which release various pro-inflammatory mediators such as tumor necrosis factor- (TNF-) and interleukin-6 (IL-6). We investigated the role of Kupffer cells during CCl(4) intoxication using Nucling-knockout mice (the KO group), in which the number of Kupffer cells is largely reduced. Plasma alanine transaminase and aspartate transaminase levels demonstrated that the liver necrosis during the second phase was significantly alleviated in the KO group compared with that in the wild-type mice (the WT group). Plasma TNF- concentrations in the WT group significantly increased 24 h after CCl(4) intoxication, whereas those in the KO group did not significantly increase. Plasma IL-6 levels also significantly increased in the WT group 24 h after CCl(4) administration, but those in the KO group did not increase at any time point. These results indicated that excess reactions of Kupffer cells, once primed by oxidants, were involved in the exacerbation of oxidative stress and liver damage during the second phase of CCl(4) intoxication. (Keyword) carbon tetrachloride / Kupffer / nucling / interleukin / tumor necrosis factor / oxidative stress (Link to Publication Site) ● Publication site (DOI): 10.1248/bpb.35.980 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22687543 ● Search Scopus @ Elsevier (PMID): 22687543 ● Search Scopus @ Elsevier (DOI): 10.1248/bpb.35.980 (DOI: 10.1248/bpb.35.980, PubMed: 22687543)
23.	Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Diem Hong Tran, Takashi Sakai, Hiroyoshi Watanabe, Shoji Kagami and Kiyoshi Fukui : 3-Bromopyruvate antagonizes effects of lactate and pyruvate, synergizes with citrate and exerts novel anti-glioma effects, Journal of Bioenergetics and Biomembranes, Vol.44, No.1, 61-79, 2012. (Summary) Oxidative stress-energy depletion therapy using oxidative stress induced by D-amino acid oxidase (DAO) and energy depletion induced by 3-bromopyruvate (3BP) was reported recently (El Sayed et al., Cancer Gene Ther., 19, 1-18, 2012). Even in the presence of oxygen, cancer cells oxidize glucose preferentially to produce lactate (Warburg effect) which seems vital for cancer microenvironment and progression. 3BP is a closely related structure to lactate and pyruvate and may antagonize their effects as a novel mechanism of its action. Pyruvate exerted a potent H(2)O(2) scavenging effect to exogenous H(2)O(2), while lactate had no scavenging effect. 3BP induced H(2)O(2) production. Pyruvate protected against H(2)O(2)-induced C6 glioma cell death, 3BP-induced C6 glioma cell death but not against DAO/D-serine-induced cell death, while lactate had no protecting effect. Lactate and pyruvate protected against 3BP-induced C6 glioma cell death and energy depletion which were overcome with higher doses of 3BP. Lactate and pyruvate enhanced migratory power of C6 glioma which was blocked by 3BP. Pyruvate and lactate did not protect against C6 glioma cell death induced by other glycolytic inhibitors e.g. citrate (inhibitor of phosphofructokinase) and sodium fluoride (inhibitor of enolase). Serial doses of 3BP were synergistic with citrate in decreasing viability of C6 glioma cells and spheroids. Glycolysis subjected to double inhibition using 3BP with citrate depleted ATP, clonogenic power and migratory power of C6 glioma cells. 3BP induced a caspase-dependent cell death in C6 glioma. 3BP was powerful in decreasing viability of human glioblastoma multiforme cells (U373MG) and C6 glioma in a dose- and time-dependent manner. (Keyword) Antineoplastic Agents, Alkylating / apoptosis / Cell Survival / Citric Acid / D-amino acid oxidase / Electrophoresis, Polyacrylamide Gel / Glioblastoma / Glioma / Glycolysis / Humans / hydrogen peroxide / Immunoblotting / Lactic Acid / oxidative stress / Pyruvates / Pyruvic Acid / Tetrazolium Salts / Thiazoles (Link to Publication Site) ● Publication site (DOI): 10.1007/s10863-012-9409-4 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22318356 ● Summary page in Scopus @ Elsevier: 2-s2.0-84858749705 (DOI: 10.1007/s10863-012-9409-4, PubMed: 22318356, Elsevier: Scopus)
24.	Kiyoshi Fukui : Disease-targeted enzymology on the function and structure of D-Amino Acid Metabolic System, Vitamins, Vol.86, No.2, 63-73, 2012. (Summary) D-Amino acid oxidase (DAO) has been proposed to be involved in the decreased glutamatergic neurotransmission in schizophrenia and the modulation of its activity is expected to be therapeutic. Here we show the inhibitory effect of antipsychotic drugs, chlorpromazine and risperidone, on human DAO activity. In search of the pathophysiological role of DAO, we analyzed its distribution in brain. The immunoreactivity for DAO was detected in glial cells of rhombencephalon and in choroid plexus (CP) in the human brain. Furthermore, higher level of DAO expression was observed in schizophrenic CP epithelial cells. These results suggest that DAO expression level is altered in schizophrenia and the increase in DAO expression is involved in aberrant D-amino acid metabolism. In particular, gene expression of DAO in CP suggests that DAO may regulate D-amino acid concentration by modulating the cerebrospinal fluid, and may be regarded as a potential therapeutic target for schizophrenia. (Keyword) D-Amino acid oxidase / glutamatergic neurotransmission / schizophrenia / glial cells / choroid plexus (Link to Publication Site) ● Publication site (DOI): 10.20632/vso.86.2_63 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390282680678553472 ● Search Scopus @ Elsevier (DOI): 10.20632/vso.86.2_63 (DOI: 10.20632/vso.86.2_63, CiNii: 1390282680678553472)
25.	Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Takashi Sakai, Hiroyoshi Watanabe, Shoji Kagami and Kiyoshi Fukui : D-amino acid oxidase gene therapy sensitizes glioma cells to the antiglycolytic effect of 3-bromopyruvate, Cancer Gene Therapy, Vol.19, No.1, 1-18, 2012. (Summary) Glioma tumors are refractory to conventional treatment. Glioblastoma multiforme is the most aggressive type of primary brain tumors in humans. In this study, we introduce oxidative stress-energy depletion (OSED) therapy as a new suggested treatment for glioblastoma. OSED utilizes D-amino acid oxidase (DAO), which is a promising therapeutic protein that induces oxidative stress and apoptosis through generating hydrogen peroxide (H2O2). OSED combines DAO with 3-bromopyruvate (3BP), a hexokinase II (HK II) inhibitor that interferes with Warburg effect, a metabolic alteration of most tumor cells that is characterized by enhanced aerobic glycolysis. Our data revealed that 3BP induced depletion of energetic capabilities of glioma cells. 3BP induced H2O2 production as a novel mechanism of its action. C6 glioma transfected with DAO and treated with D-serine together with 3BP-sensitized glioma cells to 3BP and decreased markedly proliferation, clonogenic power and viability in a three-dimensional tumor model with lesser effect on normal astrocytes. DAO gene therapy using atelocollagen as an in vivo transfection agent proved effective in a glioma tumor model in Sprague-Dawley (SD) rats, especially after combination with 3BP. OSED treatment was safe and tolerable in SD rats. OSED therapy may be a promising therapeutic modality for glioma. (Keyword) Adenosine Triphosphate / Animals / Cell Line, Tumor / D-Amino-Acid Oxidase / Disease Models, Animal / Enzyme Inhibitors / Female / Gene Therapy / Glioblastoma / Glioma / Glycolysis / Humans / Hydrogen Peroxide / Mice / Neoplastic Stem Cells / Oxidative Stress / Pyruvates / Rats / Rats, Sprague-Dawley / Transfection (Link to Publication Site) ● Publication site (DOI): 10.1038/cgt.2011.59 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21921941 ● Search Scopus @ Elsevier (PMID): 21921941 ● Search Scopus @ Elsevier (DOI): 10.1038/cgt.2011.59 (DOI: 10.1038/cgt.2011.59, PubMed: 21921941)
26.	Seongpil Chung, Sogabe Kimiko, Hwan Ki Park, Ying Song, Koji Ono, Rabab Mohamed Abou El-Magd, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Potential cytotoxic effect of hydroxypyruvate produced from D-serine by astroglial D-amino acid oxidase, The Journal of Biochemistry, Vol.148, No.6, 743-753, 2010. (Summary) D-amino acid oxidase (DAO) is a flavoenzyme that exists in the kidney, liver and brain of mammals. This enzyme catalyzes the oxidation of D-amino acids to the corresponding -keto acid, hydrogen peroxide and ammonia. Recently D-serine, one of the substrates of DAO, has been found in the mammalian brain, and shown to be a co-agonist of the N-methyl-D-aspartate (NMDA) receptor in glutamate neurotransmission. In this study, we investigated the metabolism of extracellular D-serine and the effects of D-serine metabolites to study the pathophysiological role of DAO. Treatment with a high dose of D-serine induced the cell death in dose-dependent manner in DAO-expressing cells. Moreover, overexpression of DAO in astroglial cells induced the enhanced cytotoxicity. The treatment with 1 mM beta-hydroxypyruvate (HPA), uniquely produced from the D-serine metabolism by DAO activity, also induced cell death, comprising apoptosis, in the astroglial cell, but not in the other cells derived from liver and kidney. Taken together, we consider that high dose of extracellular D-serine induced cell death by the production of not only hydrogen peroxide but also HPA as a result of DAO catalytic activity in astroglial cell. Furthermore, this cytotoxicity of HPA is observed uniquely in astroglial cells expressing DAO. (Keyword) D-amino acid oxidase / cytotoxicity / beta-hydroxypyruvate / oxidative stress / D-serine (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvq112 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20876609 ● Search Scopus @ Elsevier (PMID): 20876609 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvq112 (DOI: 10.1093/jb/mvq112, PubMed: 20876609)
27.	Rabab Mohamed Abou El-Magd, Chizuru Sasaki, Tomoya Kawazoe, Salah Mohamed El-Sayed, Kazuko YORITA, Yuji Shishido, Takashi Sakai, Yoshitoshi Nakamura and Kiyoshi Fukui : Bioprocess development of the production of the mutant P-219-L human D-amino acid oxidase for high soluble fraction expression in recombinant Escherichia coli, Biochemical Engineering Journal, Vol.52, No.2-3, 236-247, 2010. (Keyword) human D-amino acid oxidase / structureactivity relationship / bioprocess development / Fed-batch culture / Chaperon inducer (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bej.2010.08.016 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/j.bej.2010.08.016 (DOI: 10.1016/j.bej.2010.08.016)
28.	HoangNam Tran, Takashi Sakai, Mi Sun Kim and Kiyoshi Fukui : NF-κB regulates the expression of Nucling, a novel apoptosis regulator, with involvement of proteasome and caspase for its degradation, The Journal of Biochemistry, Vol.148, No.5, 573-580, 2010. (Summary) Nucling is identified as a novel regulator of apoptosis. In this study, we investigated the nuclear factor-B (NF-B)-dependent mechanism of Nucling expression, as well as the degradation pathways mediated by proteasome system and caspase activation. Using chromatin immunoprecipitation assay in wild-type mouse embryonic fibroblasts (WT MEFs), we found that NF-B p65 could bind to the B motifs in the promoter regions of Nucling gene at four putative-binding sites. By real-time PCR and immunoblot, we confirmed that Nucling expression was up-regulated by tumour necrosis factor- (TNF-) stimulation in WT MEFs, but not in NF-B p50 knockout MEFs. On the other hand, we investigated the degradation of Nucling in connection with proteasome and caspase by using cycloheximide chase. The results showed that Nucling is a short-lived protein, and its degradation was recovered by proteasome inhibitor MG132. Moreover, under TNF- stimulation, degradation of Nucling was recovered by pan-caspase inhibitor zVAD-fmk. Taken together, we propose a mechanism of Nucling intracellular metabolism. Nucling expression is induced by canonical NF-B signalling pathway, whereas Nucling is undergoing proteasome degradation, as well as being cleaved by caspase system under stress conditions. This opens a new perspective for studying the NF-B dependent regulation mechanism of cell death and survival. (Keyword) apoptosis / caspase / nuclear factor κB / nucling / tumor necrosis factor-α / proteasome (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvq089 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20702393 ● Summary page in Scopus @ Elsevier: 2-s2.0-78049486202 (DOI: 10.1093/jb/mvq089, PubMed: 20702393, Elsevier: Scopus)
29.	Rabab Mohamed Abou El-Magd, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Seongpil Chung, Motoshige Miyano, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : The Effect of Risperidone on D-Amino Acid Oxidase Activity as a Hypothesis for a Novel Mechanism of Action in the Treatment of Schizophrenia, Journal of Psychopharmacology, Vol.24, No.7, 1055-1067, 2010. (Summary) D-Amino acid oxidase (DAO) has been established to be involved in the oxidation of D-serine, an allosteric activator of the N-methyl-D-aspartate-type glutamate receptor in the brain, and to be associated with the onset of schizophrenia. The effect of risperidone, a benzisoxazole derivative, atypical antischizophrenic drug, on the activity of human DAO was tested using an in-vitro oxygraph system and rat C6, stable C6 transformant cells overexpressing mouse DAO (designated as C6/DAO) and pig kidney epithelial cells (LLC-PK1). Risperidone has a hyperbolic mixed-type inhibition, designated as `partial uncompetitive inhibition effect', with Ki value of 41 M on human DAO. Risperidone exhibited a protective effect from D-amino acid induced cell death in both C6/DAO and LLC-PK1 cells with 10% increase in viability. These data indicate the involvement of DAO activity in D-serine metabolism and also suggest a new mechanism of action to risperidone as antischizophrenic drug. (Keyword) D-amino acid oxidase / D-serine / NMDA-receptors / risperidone (Link to Publication Site) ● Publication site (DOI): 10.1177/0269881109102644 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19329549 ● Search Scopus @ Elsevier (PMID): 19329549 ● Search Scopus @ Elsevier (DOI): 10.1177/0269881109102644 (DOI: 10.1177/0269881109102644, PubMed: 19329549)
30.	Takashi Sakai, Li Liu, Xichuan Teng, Naozumi Ishimaru, Rika Mukai-Sakai, HoangNam Tran, Sun Mi Kim, Nobuya Sano, Yoshio Hayashi, Ryuji Kaji and Kiyoshi Fukui : Inflammatory disease and cancer with a decrease in Kupffer cell numbers in Nucling-knockout mice., International Journal of Cancer, Vol.126, No.5, 1079-1094, 2010. (Summary) Nucling is a stress-inducible protein associated with apoptosomes. The cytochrome c-triggered formation of apoptosomes represents a key-initiating event in apoptosis. We have recently reported that Nucling regulates the apoptotic pathway by controlling the activation of NF-kappaB as well. Here we show that hepatocellular carcinoma (HCC) arising spontaneously against a background of hepatitis occurred more frequently in Nucling-knockout (KO) mice than wild-type (WT) mice. Biochemical serum testing revealed potential liver dysfunction with hypercholesterolemia in Nucling-KO males. In the background of Nucling-KO mice, we observed the up-regulation of TNFalpha, spontaneous NF-kappaB-activation and the induction of galectin-3 expression in liver. In addition, we observed a decrease in the number of Kupffer cells (KCs) in the KO mice. KCs are important for the hepatic immune system, acting as phagocytes or antigen-presenting cells (APCs). We found that KCs in Nucling-KO mice were apoptotic possibly through the up-regulation of TNFalpha. These observations indicate that Nucling is important for the regulation of NF-kappaB signals in liver. We propose that Nucling deficiency could be a powerful tool to reveal the NF-kappaB-related molecular networks leading to hepatitis and HCC development. (Keyword) Animals / apoptosis / Blotting, Western / carbon tetrachloride / Carcinogens / Carcinoma, Hepatocellular / Electrophoretic Mobility Shift Assay / Flow Cytometry / Hepatitis / immunohistochemistry / inflammation / Kupffer Cells / Liver Neoplasms / Membrane Proteins / Mice / knockout mice / NF-kappa B / Precancerous Conditions / Reverse Transcriptase Polymerase Chain Reaction / Signal Transduction / Tumor Necrosis Factor-alpha (Link to Publication Site) ● Publication site (DOI): 10.1002/ijc.24789 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19637241 ● Summary page in Scopus @ Elsevier: 2-s2.0-74049095937 (DOI: 10.1002/ijc.24789, PubMed: 19637241, Elsevier: Scopus)
31.	Koji Ono, Yuji Shishido, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Seongpil Chung, Rabab Mohamed Abou El-Magd, Kazuko YORITA, Mai Okano, Takeshi Watanabe, Nobuya Sano, Yoshimi Bando, Kunimasa Arima, Takashi Sakai and Kiyoshi Fukui : Potential pathophysiological role of D-amino acid oxidase in schizophrenia: immunohistochemical and in situ hybridization study of the expression in human and rat brain, Journal of Neural Transmission, Vol.116, No.10, 1335-1347, 2009. (Summary) D-Amino acid oxidase (DAO) is a peroxisomal flavoenzyme that catalyzes oxidative deamination of a wide range of D-amino acids. Among the possible substrates of DAO in vivo, D-serine is proposed to be a neuromodulator of the N-methyl-D-aspartate (NMDA) type glutamate receptor. The gene for DAO was reported to be associated with schizophrenia. Since DAO is expected to be one of the key enzymes in the regulation of NMDA neurotransmission, the modulation of the enzyme activity is expected to be therapeutical for neuronal disorders. In search of the pathophysiological role of DAO, we analyzed the distribution of DAO mRNA and protein in the rat and human brain. In rat, the distribution of DAO mRNA was newly detected in choroid plexus (CP) epithelial cells in addition to glial cells of pons, medulla oblongata, and especially Bergmann glia of cerebellum. Moreover, to investigate how DAO expression level is altered in schizophrenia, we performed immunohistochemistry in the human brain. In agreement with the results in the rat brain, the immunoreactivity for DAO was detected in glial cells of rhombencephalon and in CP. Furthermore, higher level of DAO expression was observed in schizophrenic CP epithelial cells than that in non-schizophrenic cases. These results suggest that an increase in DAO expression in parts of the brain is involved in aberrant D-amino acid metabolism. In particular, gene expression of DAO in CP suggests that DAO may regulate D-amino acid concentration by modulating the cerebrospinal fluid and may be regarded as a potential therapeutic target for schizophrenia. (Keyword) D-amino acid oxidase / D-Serine metabolism / gene expression / schizophrenia / choroid plexus / glutamatergic neurotransmission (Link to Publication Site) ● Publication site (DOI): 10.1007/s00702-009-0289-7 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19685198 ● Search Scopus @ Elsevier (PMID): 19685198 ● Search Scopus @ Elsevier (DOI): 10.1007/s00702-009-0289-7 (DOI: 10.1007/s00702-009-0289-7, PubMed: 19685198)
32.	Li Liu, Takashi Sakai, HoangNam Tran, Rika Mukai-Sakai, Ryuji Kaji and Kiyoshi Fukui : Nucling interacts with nuclear factor-B, regulating its cellular distribution, The FEBS Journal, Vol.276, No.5, 1459-1470, 2009. (Summary) Nucling is an Apaf1-binding proapoptotic protein involved in apoptosome-mediated apoptosis. Luciferase assays have revealed that the activation of nuclear factor-kappaB induced by tumor necrosis factor-alpha, interleukin-1beta and lipopolysaccharide is downregulated by the overexpression of Nucling in HEK293 cells. Moreover, the expression of endogenous cyclooxygenase 2, tumor necrosis factor-alpha and galectin-3, the end-point molecules in the pathway for the activation of nuclear factor-kappaB, as well as nuclear factor-kappaB (p65) itself, is upregulated in Nucling gene-deficient mouse embryonic fibroblasts, suggesting that nuclear factor-kappaB is a target of Nucling. Subsequent study has revealed that Nucling physically interacts with nuclear factor-kappaB (p65 and p50) and that the binding domain of Nucling is its amino-terminal region (amino acids 1-466) containing ankyrin repeats. Overexpression of Nucling prevents the translocation of nuclear factor-kappaB into the nucleus. In addition, the cytoplasmic retention of endogenous nuclear factor-kappaB in resting cells is not observed in Nucling gene-deficient mouse embryonic fibroblasts. These results reveal a novel function of Nucling as a suppressor of nuclear factor-kappaB, mediated by its cytoplasmic retention through physical interaction. (Keyword) IκBα / nuclear factor κB / nuclear translocation / nucling / tumor necrosis factor-α (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1742-4658.2009.06888.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19187222 ● Summary page in Scopus @ Elsevier: 2-s2.0-60349104730 (DOI: 10.1111/j.1742-4658.2009.06888.x, PubMed: 19187222, Elsevier: Scopus)
33.	Sanae Iwana, Tomoya Kawazoe, Hwan Ki Park, Koichiro Tsuchiya, Koji Ono, Kazuko YORITA, Takashi Sakai, Takenori Kusumi and Kiyoshi Fukui : Chlorpromazine oligomer is a potentially active substance that inhibits human D-amino acid oxidase, product of a susceptibility gene for schizophrenia, Journal of Enzyme Inhibition and Medicinal Chemistry, Vol.23, No.6, 901-911, 2008. (Summary) D-amino acid oxidase (DAO), a potential risk factor for schizophrenia, has been proposed to be involved in the decreased glutamatergic neurotransmission in schizophrenia. Here we show the inhibitory effect of an antipsychotic drug, chlorpromazine, on human DAO, which is consistent with previous reports using porcine DAO, although human DAO was inhibited to a lesser degree (K(i) = 0.7 mM) than porcine DAO. Since chlorpromazine is known to induce phototoxic or photoallergic reactions and also to be transformed into various metabolites, we examined the effects of white light-irradiated chlorpromazine on the enzymatic activity. Analytical methods including high-resolution mass spectrometry revealed that irradiation triggered the oligomerization of chlorpromazine molecules. The oligomerized chlorpromazine showed a mixed type inhibition with inhibition constants of low micromolar range, indicative of enhanced inhibition. Taken together, these results suggest that oligomerized chlorpromazine could act as an active substance that might contribute to the therapeutic effects of this drug. (Keyword) D-amino acid oxidase / schizophrenia / chlorpromazine / oligomer / glutamatergic neurotransmission / inhibition (Link to Publication Site) ● Publication site (DOI): 10.1080/14756360701745478 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18615285 ● Search Scopus @ Elsevier (PMID): 18615285 ● Search Scopus @ Elsevier (DOI): 10.1080/14756360701745478 (DOI: 10.1080/14756360701745478, PubMed: 18615285)
34.	Do Youn Jun, Hae Sun Park, Ji Young Lee, Joo Youn Baek, Hwan Ki Park, Kiyoshi Fukui and Young Ho Kim : Positive regulation of promoter activity of human 3-phosphoglycerate dehydrogenase (PHGDH) gene is mediated by transcription factors Sp1 and NF-Y, Gene, Vol.414, No.1-2, 106-114, 2008. (Summary) The PHGDH gene encodes the 3-phosphoglycerate dehydrogenase that catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxy pyruvate for the phosphorylated pathway of serine biosynthesis. To understand transcriptional regulation of the human PHGDH promoter, a genomic clone containing the 5'-flanking region of the PHGDH gene was isolated from a human genomic library. The 1192-bp PHGDH promoter region was cloned by PCR using the genomic DNA isolated from the PHGDH genomic clone. Sequence analysis of the promoter region exhibited several putative transcription factor binding sites for NF-Y, Sp1, GATA-1, p53, AP2, and AP1, with no TATA-box motif at an appropriate position. Transfection of a series of deletion constructs of the promoter region into HeLa cells revealed that the core positive promoter activity resided in the -276 to +1, which contains two GC-motifs for binding Sp1 and one CCAAT-motif for NF-Y. Mutational analysis and electrophoretic mobility shift assay indicated that both the proximal GC-motif and CCAAT-motif were crucial for full induction of the promoter activity. Chromatin immunoprecipitation analysis confirmed the recruitment of Sp1 and NF-Y to the promoter region in vivo. These results demonstrated that the promoter activity of the human PHGDH gene was positively regulated by the action of transcription factors Sp1 and NF-Y. (Keyword) Human 3-phosphoglycerate dehydrogenase promoter / Transcriptional regulation / GC-motif / CCAAT-motif / HeLa cells / Jurkat T cells (Link to Publication Site) ● Publication site (DOI): 10.1016/j.gene.2008.02.018 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18378410 ● Search Scopus @ Elsevier (PMID): 18378410 ● Search Scopus @ Elsevier (DOI): 10.1016/j.gene.2008.02.018 (DOI: 10.1016/j.gene.2008.02.018, PubMed: 18378410)
35.	Tomoya Kawazoe, Hwan Ki Park, Sanae Iwana, Hideaki Tsuge and Kiyoshi Fukui : Human D-amino acid oxidase: an update and review, Chemical Record, Vol.7, No.5, 305-315, 2007. (Summary) The flavoprotein D-amino acid oxidase (DAO) degrades the gliotransmitter D-Ser, a potent activator of N-methyl-D-aspartate-type glutamate receptors. A body of evidence suggests that DAO, together with its activator, G72 protein, may play a key role in the pathophysiology of schizophrenia. It has also been suggested that 3,4-dihydroxy-D-phenylalanine (D-DOPA), the stereoisomer of 3,4-dihydroxy-L-phenylalanine (L-DOPA), is oxidized by DAO and converted to dopamine via an alternative biosynthetic pathway. We determined the crystal structures of human DAO in complex with the reaction products of two clinically important substrates, D-Ser and D-DOPA. Kinetic data show that the maximum velocity is much greater for D-DOPA than that for D-Ser, which strongly supports the proposed alternative pathway for dopamine biosynthesis in the treatment of Parkinson's disease. In addition, biochemical characterization of human DAO indicates that it binds FAD more weakly than does porcine D-amino acid oxidase (pDAO) and exists as a stable homodimer, even in the apoprotein form. Determination of the structures of human DAO in various states reveals that, in contrast to pDAO, the hydrophobic-Val-Ala-Ala-Gly-Leu (VAAGL) stretch (residues 47-51, structurally ambivalent peptide) located at the si-face of the flavin ring assumes a uniquely stable conformation, which provides a structural basis for the unique kinetic features of human DAO. (Keyword) D-amino acid oxidase / D-serine / schizophrenia / D-DOPA / Parkinson's disease (Link to Publication Site) ● Publication site (DOI): 10.1002/tcr.20129 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17924443 ● Search Scopus @ Elsevier (PMID): 17924443 ● Search Scopus @ Elsevier (DOI): 10.1002/tcr.20129 (DOI: 10.1002/tcr.20129, PubMed: 17924443)
36.	Jie Shu Li, Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Akiko Kita, Kiyoshi Fukui and Yukio Morimoto : Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9Å resolution, Biochemical and Biophysical Research Communications, Vol.358, No.4, 1002-1007, 2007. (Summary) L-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of L-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent L-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 Angstrom. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265. The alpha-carbon of pyruvate is found to be 3.13 Angstrom from the N5 atom of FMN at an angle of 105.4 degrees from the flavin N5-N10 axis. (Keyword) flavoenzyme / pyruvate / lactate oxidase / crystal structure / interaction (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbrc.2007.05.021 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17517371 ● Search Scopus @ Elsevier (PMID): 17517371 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2007.05.021 (DOI: 10.1016/j.bbrc.2007.05.021, PubMed: 17517371)
37.	Tomoya Kawazoe, Hideaki Tsuge, Mirella S. Pilone and Kiyoshi Fukui : Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis, Biochemical and Biophysical Research Communications, Vol.355, No.2, 385-391, 2007. (Summary) D-amino acid oxidase (DAO) degrades the gliotransmitter D-serine, a potent endogenous ligand of N-methyl-D-aspartate type glutamate receptors. It also has been suggested that D-DOPA, the stereoisomer of L-DOPA, is oxidized by DAO and then converted to dopamine via an alternative biosynthetic pathway. Here, we provide direct crystallographic evidence that D-DOPA is readily fitted into the active site of human DAO, where it is oxidized by the enzyme. Moreover, our kinetic data show that the maximal velocity for oxidation of D-DOPA is much greater than for D-serine, which strongly supports the proposed alternative pathway for dopamine biosynthesis in the treatment of Parkinson's disease. In addition, determination of the structures of human DAO in various states revealed that the conformation of the hydrophobic VAAGL stretch (residues 47-51) to be uniquely stable in the human enzyme, which provides a structural basis for the unique kinetic features of human DAO. (Keyword) D-amino acid oxidase / X-ray crystallography / D-DOPA / D-serine / dopamine / Parkinson's disease (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbrc.2007.01.181 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17303072 ● Search Scopus @ Elsevier (PMID): 17303072 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2007.01.181 (DOI: 10.1016/j.bbrc.2007.01.181, PubMed: 17303072)
38.	Nagisa Kozuka, Asami Umino, Dai Shimazu, Tetsuro Kubota, Reiji Semba, Tomoya Kawazoe, Kiyoshi Fukui, Naoki Yamamoto and Toru Nishikawa : Immunohistochemical and biochemical determination of D-serine in the cultured astrocytes and neurons from the rat neocortex, Neuroscience Research, Vol.58, No.Supplement 1, S137, 2007. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.neures.2007.06.1376 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/j.neures.2007.06.1376 (DOI: 10.1016/j.neures.2007.06.1376)
39.	Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : 生体不斉アミノ酸分子の存在とその代謝酵素の病態生理学的意義, 日本応用酵素協会誌, Vol.41, 21-31, 2007.
40.	Tomoya Kawazoe, Hideaki Tsuge, Mirella S. Pilone and Kiyoshi Fukui : Crystal structure of human D-amino acid oxidase, --- Context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring ---, Protein Science, Vol.15, No.12, 2708-2717, 2006. (Summary) In the brain, the extensively studied FAD-dependent enzyme D-amino acid oxidase (DAO) degrades the gliotransmitter D-serine, a potent activator of N-methyl-D-aspartate type glutamate receptors, and evidence suggests that DAO, together with its activator G72 protein, may play a key role in the pathophysiology of schizophrenia. Indeed, its potential clinical importance highlights the need for structural and functional analyses of human DAO. We recently succeeded in purifying human DAO, and found that it weakly binds FAD and shows a significant slower rate of flavin reduction compared with porcine DAO. However, the molecular basis for the different kinetic features remains unclear because the active site of human DAO was considered to be virtually identical to that of porcine DAO, as would be expected from the 85% sequence identity. To address this issue, we determined the crystal structure of human DAO in complex with a competitive inhibitor benzoate, at a resolution of 2.5 Angstrom. The overall dimeric structure of human DAO is similar to porcine DAO, and the catalytic residues are fully conserved at the re-face of the flavin ring. However, at the si-face of the flavin ring, despite the strict sequence identity, a hydrophobic stretch (residues 47-51, VAAGL) exists in a significantly different conformation compared with both of the independently determined porcine DAO-benzoate structures. This suggests that a context-dependent conformational variability of the hydrophobic stretch accounts for the low affinity for FAD as well as the slower rate of flavin reduction, thus highlighting the unique features of the human enzyme. (Keyword) D-amino acid oxidase / Homo sapiens / X-ray crystallography / structurally ambivalent peptides / conformational variability (Link to Publication Site) ● Publication site (DOI): 10.1110/ps.062421606 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17088322 ● Search Scopus @ Elsevier (PMID): 17088322 ● Search Scopus @ Elsevier (DOI): 10.1110/ps.062421606 (DOI: 10.1110/ps.062421606, PubMed: 17088322)
41.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Akiko Kita, Kiyoshi Fukui and Yukio Morimoto : The Crystal structure of L-Lactate oxidase from Aerococcus viridans at 2.1Å resolution reveals the mechanism of strict substrate recognition, Biochemical and Biophysical Research Communications, Vol.350, No.2, 249-256, 2006. (Summary) L-Lactate oxidase (LOX) from Aerococcus viridans is a member of the alpha-hydroxyacid-oxidase flavoenzyme family. We have determined the three-dimensional structure of LOX and revealed the mechanism of substrate recognition. The LOX monomer structure has a typical alpha(8)/beta(8) motif commonly found in other flavin family proteins. A related enzyme, glycolate oxidase, catalyzes the oxidation of glycolate rather than lactate. Comparison of the two enzyme structures highlights the importance of five residues around the FMN prosthetic group of LOX, which act synergistically to discriminate between the l/d configurations of lactate. X-ray crystallography of LOX gave a space group I422 of unit-cell parameters a=b=191.096A, c=194.497A and alpha=beta=gamma=90 degrees with four monomers per asymmetric unit. The four independent monomers display slight structural differences around the active site. Diffraction data were collected, under cryogenic conditions to 2.1A resolution at the synchrotron facilities in Japan. (Keyword) X-ray structure analysis / lactate oxidase / flavoenzyme / substrate recognition (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bbrc.2006.09.025 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17007814 ● Search Scopus @ Elsevier (PMID): 17007814 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2006.09.025 (DOI: 10.1016/j.bbrc.2006.09.025, PubMed: 17007814)
42.	Xichuan Teng, Takashi Sakai, Li Liu, Rika Sakai, Ryuji Kaji and Kiyoshi Fukui : Attenuation of MPTP-induced neurotoxicity and locomotor dysfunction in Nucling-deficient mice via suppression of the apoptosome pathway, Journal of Neurochemistry, Vol.97, No.4, 1126-1135, 2006. (Summary) 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced neurotoxicity is one of the experimental models most commonly used to study the pathogenesis of Parkinson's disease (PD). Although the biochemical mechanisms underlying the cell death induced by MPTP remain to be clarified, it has been found that the mitochondrial apoptotic signaling pathway plays an important role in the neurotoxicity of MPTP. Nucling is a novel type of apoptosis-associated molecule, essential for cytochrome c, apoptosis protease activating factor 1 (Apaf-1), pro-caspase-9 apoptosome induction and caspase-9 activation following pro-apoptotic stress. Here we found that Nucling-deficient mice treated with MPTP did not exhibit locomotor dysfunction in an open-field test. The substantia nigra dopaminergic neurons of Nucling-deficient mice were resistant to the damaging effects of the neurotoxin MPTP. Up-regulated expression of apoptosome was attenuated in Nucling-deficient mice treated with MPTP. These results indicate an important role for Nucling in MPTP-induced neuronal degeneration and suggest that the suppression of Nucling would be of therapeutic benefit for the treatment of neurodegeneration in PD. (Keyword) apoptosis / apoptosome / MPTP / nucling / Parkinson's disease (Link to Publication Site) ● Publication site (DOI): 10.1111/j.1471-4159.2006.03833.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16686692 ● Search Scopus @ Elsevier (PMID): 16686692 ● Search Scopus @ Elsevier (DOI): 10.1111/j.1471-4159.2006.03833.x (DOI: 10.1111/j.1471-4159.2006.03833.x, PubMed: 16686692)
43.	Gianluca Molla, Silvia Sacchi, Mariagrazia Bernasconi, Mirella S. Pilone, Kiyoshi Fukui and Loredano Pollegioni : Characterization of human D-amino acid oxidase, FEBS Letters, Vol.580, No.9, 2358-2364, 2006. (Summary) D-Amino acid oxidase (DAAO) has been proposed to be involved in the oxidation of D-serine, an allosteric activator of the NMDA-type glutamate receptor in the brain, and to be associated with the onset of schizophrenia. The recombinant human DAAO was expressed in Escherichia coli and was isolated as an active homodimeric flavoenzyme. It shows the properties of the dehydrogenase-oxidase class of flavoproteins, possesses a low kinetic efficiency, and follows a ternary complex (sequential) kinetic mechanism. In contrast to the other known DAAOs, the human enzyme is a stable homodimer even in the apoprotein form and weakly binds the cofactor in the free form. (Keyword) schizophrenia / flavoenzyme / neurotransmission (Link to Publication Site) ● Publication site (DOI): 10.1016/j.febslet.2006.03.045 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16616139 ● Search Scopus @ Elsevier (PMID): 16616139 ● Search Scopus @ Elsevier (DOI): 10.1016/j.febslet.2006.03.045 (DOI: 10.1016/j.febslet.2006.03.045, PubMed: 16616139)
44.	Hwan Ki Park, Yuji Shishido, Sayaka Ichise-Shishido, Tomoya Kawazoe, Koji Ono, Sanae Iwana, Yumiko Tomita, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Potential Role for Astroglial D-Amino Acid Oxidase in Extracelluar D-Serine Metabolism and Cytotoxicity, The Journal of Biochemistry, Vol.139, No.2, 295-304, 2006. (Summary) D-amino acid oxidase (DAO) is a flavoenzyme that catalyzes the oxidation of D-amino acids. In the brain, gene expression of DAO is detected in astrocytes. Among the possible substrates of DAO in vivo, D-serine is proposed to be a neuromodulator of the N-methyl-D-aspartate (NMDA) receptor. In a search for the physiological role of DAO in the brain, we investigated the metabolism of extracellular D-serine in glial cells. Here we show that after D-serine treatment, rat primary type-1 astrocytes exhibited increased cell death. In order to enhance the enzyme activity of DAO in cells, we established stable rat C6 glial cells overexpressing mouse DAO designated as C6/DAO. Treatment with a high dose of D-serine led to the production of hydrogen peroxide (H(2)O(2)) followed by apoptosis in C6/DAO cells. Among the amino acids tested, D-serine specifically exhibited a significant cell death-inducing effect. DAO inhibitors, i.e., sodium benzoate and chlorpromazine, partially prevented the death of C6/DAO cells treated with D-serine, indicating the involvement of DAO activity in d-serine metabolism. Overall, we consider that extracellular D-serine can gain access to intracellular DAO, being metabolized to produce H(2)O(2). These results support the proposal that astroglial DAO plays an important role in metabolizing a neuromodulator, D-serine. (Keyword) D-amino acid oxidase / astrocyte / chlorpromazine / hydrogen peroxide / D-serine (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvj036 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16452318 ● Search Scopus @ Elsevier (PMID): 16452318 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvj036 (DOI: 10.1093/jb/mvj036, PubMed: 16452318)
45.	Kiyoshi Fukui, Hwan Ki Park, Tomoya Kawazoe, Koji Ono, Sanae Iwana, Yumiko Tomita, Kazuko YORITA, Takashi Sakai and Young Ho Kim : Functional Roles and Pathophysiology of Brain D-Amino Acid Oxidase, Flavins and Flavoproteins 2005, 853-860, 2005. (Summary) D-Amino acid oxidase (D-amino acid: O2 oxidoreductase, DAO; EC 1.4.3.3) is a flavoenzyme with noncovalently bound FAD as its prosthetic group, that catalyzes the oxidative deamination of wide range of D-amino acids to the corresponding imino acids, whereas molecular oxygen undergoes reduction to hydrogen peroxide (H2O2) . The imino acid is nonenzymatically hydrolyzed to α-keto acid and ammonia. H2O2, a type of reactive oxygen species (ROS), is known to damage DNA, proteins and lipids, thereby leading to stress-induced apoptosis. In mammals, DAO is found at highest concentration in kidney proximal tubules, liver and granules of neutrophilic leukocyte as well as certain parts of the brain. This enzyme is intracellularly localized in peroxisomes, and DAO is regarded as a characteristic marker enzyme of the peroxisomes. Since the initial characterization of this enzyme, many attempts have been made to clarify the physicochemical properties and reaction mechanism.
46.	Gianluca Molla, Mirella S. Pilone, Silvia Sacchi, Mariagrazia Bernasconi, Kiyoshi Fukui and Loredano Pollegioni : Molecular Basis of Schizophrenia: Characterization of Human D-Amino Acid Oxidase, Flavins and Flavoproteins 2005, 861-866, 2005.
47.	Tomoya Kawazoe, Sanae Iwana, Koji Ono, Hwan Ki Park, Kazuko YORITA, Yumiko Tomita, Hideaki Tsuge and Kiyoshi Fukui : Purification and Crystal Structure of Human D-Amino Acid Oxidase, Flavins and Flavoproteins 2005, 33-36, 2005.
48.	Kazuko YORITA, Takeshi Matsukoa, David P. Ballou and Kiyoshi Fukui : H265Q L-Lactate Oxidase from Aerococcus viridans, Flavins and Flavoproteins 2005, 37-41, 2005.
49.	Kazuko YORITA, Yasufumi Umena, Takeshi Matsuoka, David P. Ballou, Makoto Abe, Akiko Kita, Tomitake Tsukihara, Yukio Morimoto and Kiyoshi Fukui : Crystal Structures of Wild-type and R181M L-Lactate Oxidase from Aerococcus viridans, Flavins and Flavoproteins 2005, 43-48, 2005.
50.	Sanae Iwana and Kiyoshi Fukui : D-アミノ酸代謝システムによる脳機能制御の医化学, Farumashia, Vol.41, No.9, 857-861, 2005.
51.	Kiyoshi Fukui, Hwan Ki Park, Tomoya Kawazoe, Koji Ono, Sanae Iwana, Kazuko YORITA and Takashi Sakai : Astroglial D-amino acid oxidase is the key enzyme to metabolize extracellular D-serine, a neuromodulator of N-methyl-D-aspartate receptor, Amino Acids, Vol.29, No.1, 61-62, 2005.
52.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui, Tomitake Tsukihara and Yukio Morimoto : Crystallization and preliminary X-ray diffraction study of L-lactate oxidase (LOX), R18M mutant from Aerococcus viridans, Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, Vol.61, No.4, 439-441, 2005. (Summary) L-Lactate oxidase (LOX) from Aerococcus viridans is a member of the alpha-hydroxyacid oxidase flavoenzyme family. An X-ray crystallographic study of a LOX mutant in which Arg181 is replaced by Met was initiated in order to understand the functions of the conserved amino-acid residues around the FMN in the enzyme active site. LOX-R181M crystals belong to the tetragonal space group I422, with unit-cell parameters a = b = 192.632, c = 200.263 A, alpha = beta = gamma = 90 degrees. There are four monomers in the asymmetric unit. Diffraction data were collected under cryogenic conditions to 2.44 A resolution from LOX-R181M crystals at BL41XU, SPring-8. (Keyword) lactate oxidase (Link to Publication Site) ● Publication site (DOI): 10.1107/S1744309105009152 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16511063 ● Search Scopus @ Elsevier (PMID): 16511063 ● Search Scopus @ Elsevier (DOI): 10.1107/S1744309105009152 (DOI: 10.1107/S1744309105009152, PubMed: 16511063)
53.	Tomoya Kawazoe, Koji Ono, Ki Hwan Park, Kazuko YORITA, Yumiko Tomita and Kiyoshi Fukui : D-アミノ酸バイオシステムによる哺乳類の中枢神経機能の制御, 化学と生物, Vol.42, No.7, 426-428, 2004. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1520853833415702784 (CiNii: 1520853833415702784)
54.	Takashi Sakai, Li Liu, Xichuan Teng, Rika Mukai-Sakai, Hidenori Shimada, Ryuji Kaji, Tasuku Mitani, Mitsuru Matsumoto, Kazunori Toida, Kazunori Ishimura, Yuji Shishido, Tak W. Mak and Kiyoshi Fukui : Nucling Recruits Apaf-1/Pro-caspase-9 Complex for the Induction of Stress-Induced Apoptosis, The Journal of Biological Chemistry, Vol.279, No.39, 41131-41140, 2004. (Summary) Nucling is a novel protein isolated from murine embryonal carcinoma cells with an up-regulated expression during cardiac muscle differentiation. We show here that Nucling was up-regulated by proapoptotic stimuli and important for the induction of apoptosis after cytotoxic stress. We further demonstrated that overexpressed Nucling was able to induce apoptosis. In Nucling-deficient cells, the expression levels of Apaf-1 and cytochrome c, which are the major components of an apoptosis-promoting complex named apoptosome, were both down-regulated under cellular stress. A deficiency of Nucling also conferred resistance to apoptotic stress on the cell. After UV irradiation, Nucling was shown to reside in an Apaf-1/pro-caspase-9 complex, suggesting that Nucling might be a key molecule for the formation and maintenance of this complex. Nucling induced translocation of Apaf-1 to the nucleus, thereby distributing the Nucling/Apaf-1/pro-caspase-9 complex to the nuclear fraction. These findings suggest that Nucling recruits and transports the apoptosome complex during stress-induced apoptosis. (Keyword) Alleles / Amino Acid Chloromethyl Ketones / Animals / Apoptosis / Apoptotic Protease-Activating Factor 1 / Blotting, Northern / Blotting, Western / COS Cells / Caspase 9 / Caspases / Cell Death / Cell Line / Cysteine Proteinase Inhibitors / Cytochromes c / Dose-Response Relationship, Drug / Down-Regulation / Electrophoresis, Gel, Two-Dimensional / Electrophoresis, Polyacrylamide Gel / Genetic Vectors / HeLa Cells / Humans / Hydrogen Peroxide / In Situ Nick-End Labeling / Membrane Proteins / Mice / Mice, Transgenic / Microscopy, Confocal / Mitochondria / Models, Genetic / Plasmids / Proteins / RNA / Reverse Transcriptase Polymerase Chain Reaction / Transfection / Transgenes / Ultraviolet Rays / Up-Regulation (Link to Publication Site) ● Publication site (DOI): 10.1074/jbc.M402902200 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15271982 ● CiNii @ National Institute of Informatics (CRID): 1364233268616555648 ● Search Scopus @ Elsevier (PMID): 15271982 ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M402902200 (DOI: 10.1074/jbc.M402902200, PubMed: 15271982, CiNii: 1364233268616555648)
55.	Li Liu, Takashi Sakai, Nobuya Sano and Kiyoshi Fukui : Nucling mediates apoptosis by inhibiting expression of galectin-3 through interference with nuclear factor B signalling, The Biochemical Journal, Vol.380, No.1, 31-41, 2004. (Keyword) anoikis / apoptosis / galectin-3 / nucling / nuclear factor κB / preputial gland (Link to Publication Site) ● Publication site (DOI): 10.1042/BJ20031300 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14961764 ● Search Scopus @ Elsevier (PMID): 14961764 ● Search Scopus @ Elsevier (DOI): 10.1042/BJ20031300 (DOI: 10.1042/BJ20031300, PubMed: 14961764)
56.	Takashi Sakai, Li Liu, Yuji Shishido and Kiyoshi Fukui : Identification of a Novel, Embryonal Carcinoma Cell-Associated Molecule, Nucling, That Is Up-regulated during Cardiac Muscle Differentiation, The Journal of Biochemistry, Vol.133, No.4, 429-436, 2003. (Summary) EC cells are characterized by their potent capacity to differentiate into several cell types, such as mesoderm-like cells, endoderm-like cells, or ectoderm-like cells. By subtracting the mRNAs expressed by one EC cell clone, F9 cells, with the mRNAs expressed by another EC cell clone, P19 cells, we identified six novel genes that are expressed selectively by F9 cells. One of these genes (Nucling) encodes a polypeptide of 1411 amino acids containing an ankyrin repeat, aspartyl protease motif, a leucine zipper motif, and two t-SNARE coiled-coil domains. Northern blot analyses revealed the Nucling mRNA to be detected predominantly in heart, liver, kidney and testis, but not in brain or spleen. Immunostaining analyses revealed a unique feature of Nucling that the transiently expressed protein forms aggregates exclusively around nuclear membranes. Moreover, the expression level of the Nucling gene transcript increases progressively during the early developmental stages in mice, and specifically at cardiomuscular differentiation in vitro and in vivo. These results suggest that Nucling may play some role in the gene regulation of cell differentiation during embryonal development. (Keyword) cardiomuscular differentiation / cDNA subtractive screening / cell differentiation / EC cells / embryonal development (Link to Publication Site) ● Publication site (DOI): 10.1093/jb/mvg056 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12761289 ● Search Scopus @ Elsevier (PMID): 12761289 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvg056 (DOI: 10.1093/jb/mvg056, PubMed: 12761289)
57.	Atsuhiko Suzue, Shinji Nagahiro, Yoshiteru Urai, Osamu Jinnouchi, Tokujiro Kanamori, Kyung Tak Kwak, Hwan Ki Park, Tomoya Kawazoe, Sayaka Ichise, Yuji Shishido, Yumiko Tomita, Takashi Sakai and Kiyoshi Fukui : Astroglial expression of D-amino acid oxidase gene, Flavins and Flavoproteins 2002, 853-856, 2002.
58.	Yoshiteru Urai, Atsuhiko Suzue, Osamu Jinnouchi, Kyung Tak Kwak, Shinji Nagahiro and Kiyoshi Fukui : Gene expression of D-amino Acid oxidase in cultured rat astrocytes, Neuroscience Letters, Vol.324, No.2, 101-104, 2002. (Summary) Neuromodulative free D-serine is present in mammalian brain, and localized to type-2 astrocytes in culture. D-amino acid oxidase (DAO) is a flavoenzyme that catalyzes D-amino acids. We examined the DAO gene expression in cultured rat astrocytes by reverse transcriptase-polymerase chain reaction. We established a method to prepare highly purified culture of type-1 and type-2 astrocytes from any brain region. This method utilizes combination of cell type specific separation by shaking and subsequent purification by immunopanning or treatment with cytosine arabinoside. We detected higher DAO gene expression in type-1 astrocyte cultures from cerebellum than that from cerebral cortex. In cerebellum, we observed higher DAO expression in type-1 astrocyte cultures than that in type-2. We also revealed that DAO expression in C6, corresponding to type-1 astrocyte, was higher than that in CG-4 derived type-2 astrocytes. (Keyword) D-amino acid oxidase / astrocyte / D-serine / NMDA-receptors / Reverse transcriptase-polymerase chain reaction / cell separation / CG-4 / C6 (Link to Publication Site) ● Publication site (DOI): 10.1016/S0304-3940(02)00184-2 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11988337 ● Summary page in Scopus @ Elsevier: 2-s2.0-0037123710 (DOI: 10.1016/S0304-3940(02)00184-2, PubMed: 11988337, Elsevier: Scopus)
59.	Ming Li, Azusa Marubayashi, Yutaka Nakaya, Kiyoshi Fukui and Seiji Arase : Minoxidil-Induced hair growth is mediated by adenosine in cultured dermal papilla cells: possible involvement of sulfonylurea receptor 2B as a target of minoxidil, The Journal of Investigative Dermatology, Vol.117, No.6, 1594-1600, 2001. (Summary) The mechanism by which minoxidil, an adenosine-triphosphate-sensitive potassium channel opener, induces hypertrichosis remains to be elucidated. Minoxidil has been reported to stimulate the production of vascular endothelial growth factor, a possible promoter of hair growth, in cultured dermal papilla cells. The mechanism of production of vascular endothelial growth factor remains unclear, however. We hypothesize that adenosine serves as a mediator of vascular endothelial growth factor production. Minoxidil-induced increases in levels of intracellular Ca(2+) and vascular endothelial growth factor production in cultured dermal papilla cells were found to be inhibited by 8-sulfophenyl theophylline, a specific antagonist for adenosine receptors, suggesting that dermal papilla cells possess adenosine receptors and sulfonylurea receptors, the latter of which is a well-known target receptor for adenosine-triphosphate-sensitive potassium channel openers. The expression of sulfonylurea receptor 2B and of the adenosine A1, A2A, and A2B receptors was detected in dermal papilla cells by means of reverse transcription polymerase chain reaction analysis. In order to determine which of the adenosine receptor subtypes contribute to minoxidil-induced hair growth, the effects of subtype-specific antagonists for adenosine receptors were investigated. Significant inhibition in increase in intracellular calcium level by minoxidil or adenosine was observed as the result of pretreatment with 8-cyclopentyl-1,3-dipropylxanthine, an antagonist for adenosine A1 receptor, but not by 3,7-dimethyl-1-propargyl-xanthine, an antagonist for adenosine A2 receptor, whereas vascular endothelial growth factor production was blocked by both adenosine A1 and A2 receptor antagonists. These results indicate that the effect of minoxidil is mediated by adenosine, which triggers intracellular signal transduction via both adenosine A1 and A2 receptors, and that the expression of sulfonylurea receptor 2B in dermal papilla cells might play a role in the production of adenosine. (Keyword) adenosine receptor / ATP-sensitive potassium channel / hypertrichosis / intracellular calcium / vascular endothelial growth factor (Link to Publication Site) ● Publication site (DOI): 10.1046/j.0022-202x.2001.01570.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11886528 ● Summary page in Scopus @ Elsevier: 2-s2.0-0035675210 (DOI: 10.1046/j.0022-202x.2001.01570.x, PubMed: 11886528, Elsevier: Scopus)
60.	Yoshihisa Shimizu, Tomohiro Akashi, Asuko Okuda, Akihiko Kikuchi and Kiyoshi Fukui : NBP1 (Nap1 Binding Protein 1), an essential gene for G2/M transition of Saccharomyces cerevisiae, encodes a protein of distinct sub-nuclear localization, Gene, Vol.246, No.1-2, 395-404, 2000. (Summary) Nap1p is identified in mammalian cell extract by its intrinsic activity to facilitate nucleosome assembly in vitro in the physiological ionic condition. The homologous proteins are present in most eukaryotes, and their functional analyses in vitro have suggested that they are necessary to keep proper nucleosome structures in transcription and replication. This protein is also identified for its interaction with Clb2p in vitro. To address the function of Nap1p in vivo, we have surveyed for proteins to interact with Nap1p by two-hybrid system and obtained two genes, NBP1 and NBP2 (Nap1 Binding Protein 1 and 2). NBP1 is an essential gene and encodes a novel protein consisting of 319 amino acids, with a coiled-coil structure in the center of the predicted amino acid sequence. Several A-kinase dependent phosphorylation sites and Cdc28p kinase-dependent sites are also observed. By isolating the temperature-sensitive mutant, we demonstrate that the nuclear division at a non-permissive temperature is delayed and that the population of cells with a large bud carrying a single nucleus with a short spindle are increased. This mutant also confers resistance against benomyl, a microtubule-destabilizing agent. Judging from the green fluorescent protein (GFP) signal fused with Nbp1p, this protein localizes in the nucleus as one or two tiny dots. (Keyword) cell cycle / coiled-coil motif / mitotic apparatus (Link to Publication Site) ● Publication site (DOI): 10.1016/S0378-1119(00)00067-6 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10767562 ● Summary page in Scopus @ Elsevier: 2-s2.0-0034603853 (DOI: 10.1016/S0378-1119(00)00067-6, PubMed: 10767562, Elsevier: Scopus)
61.	Andrei A. Raibekas, Kiyoshi Fukui and Vincent Massey : Design and properties of human D-amino acid oxidase with covalently attached flavin, Proceedings of the National Academy of Sciences of the United States of America, Vol.97, No.7, 3089-3093, 2000. (Summary) An "artificial flavinylation" approach was developed to replace a native noncovalent flavin prosthetic group with a covalently attached flavin analogue in recombinant human d-amino acid oxidase. The protein residue Gly-281 was replaced with Cys by site-directed mutagenesis, followed by reaction between mutated apoenzyme and the thiol-reactive flavin analogue, 8-methylsulfonyl FAD. The stoichiometric process of flavin attachment was accompanied by gain in enzymatic activity, reaching up to 26% activity of the recombinant native enzyme. The steady-state kinetic data together with the results of limited proteolysis and benzoate-binding studies suggest that, although mutation perturbs protein structural and catalytic properties, the flavinylation alone does not have any negative impact. We conclude that, despite the implemented restraints on its mobility, the covalently attached flavin is properly positioned within the protein active site and acts efficiently during d-amino acid oxidase catalytic turnover. (Keyword) Base Sequence / Benzoates / Catalysis / D-Amino-Acid Oxidase / DNA Primers / Flavins / Humans / Hydrolysis / Kinetics / Mutagenesis, Site-Directed / Oxidation-Reduction / Spectrum Analysis (Link to Publication Site) ● Publication site (DOI): 10.1073/pnas.040559597 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10716694 ● Summary page in Scopus @ Elsevier: 2-s2.0-0034724295 (DOI: 10.1073/pnas.040559597, PubMed: 10716694, Elsevier: Scopus)
62.	Chie Yuasa, Osamu Miyoshi, Kiyoshi Fukui and Toshinori Oka : Hyperlipemia and Early Pancreatic Injury Induced by Ethanol Intake in Rats, Journal of Nutritional Science and Vitaminology, Vol.46, No.6, 297-301, 2000. (Summary) The pathogenesis of alcoholic pancreatitis is unknown, and even though hyperlipemia has been hypothesized to be a risk factor for alcoholic pancreatitis, no studies directly investigating whether there is a relationship between the two have ever been reported. Therefore, to determine if a relationship exists between hyperlipemia and alcoholic pancreatitis, especially the early stage of alcoholic pancreatic injury, we administered a regular liquid Lieber-DeCarli diet, with and without ethanol as 35% of total calories, to rats for 2 wk. Thereafter we measured their plasma lipid concentrations, pancreatic zymogen granule fragility, and plasma lipase activity and subsequently investigated the correlations between these parameters. Significant increases in plasma triglyceride, total cholesterol, phospholipid, nonesterified fatty acid, pancreatic zymogen granule fragility, and plasma lipase activity were observed in the ethanol liquid diet group, compared with the values of the control liquid diet group, and pancreatic zymogen granule fragility was correlated with plasma triglyceride (r=0.62), total cholesterol (r=0.77), phospholipid (r=0.76), nonesterified fatty acid concentrations (r=0.62), and lipase activity (r=0.63). These results show a possible relationship between hyperlipemia and the early stage of alcoholic pancreatic injury, and they may support the hypothesis that hyperlipemia contributes to the etiology of alcoholic pancreatitis. (Keyword) early stage / ethanol intake / rat / hyperlipemia / pancreatic injury (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11227801 ● Summary page in Scopus @ Elsevier: 2-s2.0-0034519163 (PubMed: 11227801, Elsevier: Scopus)
63.	Tokujiro Kanamori, Mariko Obayashi, Osamu Jinnouchi, Kazuya Kanda, Yoshiteru Urai, Yuji Shishido, Atsuhiko Suzue, Takashi Sakai and Kiyoshi Fukui : Gene Expression of D-Amino Acid Oxidase in Nervous System, Flavins and Flavoproteins 1999, 887-890, 1999.
64.	Chie Yuasa, Kenji Irimura, Minoru Oda, Kiyoshi Fukui and Toshinori Oka : Oral Administration of Sepimostat Mesilate Prevents Acute Alcohol Pancreatic Injury in Rats, The Journal of Pharmacy and Pharmacology, Vol.51, No.7, 867-871, 1999.
65.	Osamu Jinnouchi, Yasuo Koike and Kiyoshi Fukui : Glutamatergic Neurotransmission in the Inner Ear, Practica Oto-Rhino-Laryngologica. Suppl., Vol.101, 1-6, 1999. (Keyword) neurotransmission / ionotroic glutamate receptor / δ1 subunit / D-amino acid oxidase (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390001205526942848 (CiNii: 1390001205526942848)
66.	Osamu Jinnouchi, Yasuo Koike and Kiyoshi Fukui : D-セリンの聴覚に対する影響, Audiology Japan, Vol.41, 359-360, 1998.
67.	Masatsugu Nakai, Jun Ogata, Kiyoshi Fukui, Yasuo Nakai and Michiyuki Maeda : Basal forebrain and cerebral cortical muscarinic receptors mediate in crease in cortical blood flow provoked by periaqueductal gray matter, Neuroscience, Vol.79, No.2, 571-579, 1997. (Keyword) basal forebrain / central gray / cerebral blood flow / defence reaction / muscarinic receptor / nucleus basalis of Meynert
68.	Ryuichi Konno, Masato Sasaki, Setsuko Asakura, Kiyoshi Fukui, Jumpei Enami and Akira Niwa : D-Amino acid oxidase is not present in the mouse liver, Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.1335, No.1-2, 173-181, 1997. (Summary) Since there are conflict reports on the presence of D-amino-acid oxidase in the mouse liver, this problem was examined. D-Amino-acid oxidase activity was not detected in the homogenates of the mouse liver, lung, or heart, whereas it was detected in the homogenates of the mouse kidney and brain. Western blotting showed that a protein which reacted with the antiserum against pig D-amino-acid oxidase was present in the homogenates of the mouse kidney and brain but not in those of the liver or heart. Northern hybridization using a D-amino-acid oxidase cDNA probe detected a hybridizing signal in poly(A)+ RNAs extracted from the mouse kidney and brain but not in those from the liver, heart, or lung. Reverse transcription-polymerase chain reaction using three primer pairs always amplified D-amino-acid oxidase cDNA fragments of expected sizes in the mouse kidney and brain but very rarely did so in the liver, heart, or lung. The results indicate that D-amino-acid oxidase is not present in the mouse liver in a measurable amount. (Keyword) Animals / Blotting, Northern / Blotting, Western / Brain / D-Amino-Acid Oxidase / Kidney / Liver / Lung / Mice / Mice, Inbred Strains / Myocardium / Polymerase Chain Reaction (Link to Publication Site) ● Publication site (DOI): 10.1016/S0304-4165(96)00136-5 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9133654 ● Search Scopus @ Elsevier (PMID): 9133654 ● Search Scopus @ Elsevier (DOI): 10.1016/S0304-4165(96)00136-5 (DOI: 10.1016/S0304-4165(96)00136-5, PubMed: 9133654)
69.	Ryuichi Konno, Akira Niwa, Masato Sasaki, Jumpei Enami, Setsuko Asakura and Kiyoshi Fukui : Is There D-Amino acid oxidase in the Mouse Liver?, Flavins and Flavoproteins 1996, 203-206, 1997.
70.	Kiyoshi Fukui, Tokujiro Kanamori, Osamu Jinnouchi and Oded Ben-Yoseph : Tissue Specific Expression of the D-Amino Acid Oxidase Gene, Flavins and Flavoproteins 1996, 199-202, 1997.
71.	中井正継, 緒方絢, 玉城欣也, 山本仁, Kiyoshi Fukui, 松井征男 and 前田正信 : 脳循環調節中枢, Advances in Neurological Sciences, Vol.40, No.4, 527-539, 1996.
72.	Shunji Yamazaki, Kiyoshi Fukui, Hidefumi Kawashima, Yuji Kuge, Yoshihiro Miyake and Kenji Kangawa : Uptake of radioactive octanoate in astrocytoma cells: Basic Studies for application of [11C] octanoate as a PET tracer, Annals of Nuclear Medicine, Vol.10, No.4, 395-399, 1996.
73.	中井正継, 緒方絢, 玉城欣也, 山本仁, Kiyoshi Fukui, 松井征男 and 前田正信 : 大脳皮質循環を拡張性に調節する中枢神経領域, Recent Advances in Cardiovascular Disease, Vol.16, 95-113, 1995.
74.	Loredano Pollegioni, Kiyoshi Fukui and Vincent Massey : Studies on the Kinetic Mechanism of Pig Kidney D-Amino Acid Oxidase by Site-directed Mutagenesis of Tyrosine 224 and Tyrosine 228, The Journal of Biological Chemistry, Vol.269, No.50, 31666-31673, 1994.
75.	Saori Takahashi, Hiroyasu Inoue, Kiyoshi Fukui and Yoshihiro Miyake : Structure and function of renin binding protein, Kidney International, Vol.46, No.6, 1525-1527, 1994.
76.	Kiyoshi Fukui : 組織レニン·アンジオテンシン系と高血圧遺伝子研究, Recent Advances in Cardiovascular Disease, Vol.15, 83-91, 1994.
77.	Kiyoshi Fukui : Structure of Human D-Amino Acid Oxidase Gene, Flavins and Flavoproteins 1993, 159-162, 1994.
78.	Kiyoshi Fukui and Yoshihiro Miyake : Molecular Cloning and Chromosomal Localization of a Human Gene Encoding D-Amino Acid Oxidase, The Journal of Biological Chemistry, Vol.267, No.26, 18631-18638, 1992.
79.	Hiroyasu Inoue, Saori Takahashi, Kiyoshi Fukui and Yoshihiro Miyake : Genetic and Molecular Properties of Human and Rat Renin-Binding Proteins with Reference to the Function of the Leucine Zipper Motif, The Journal of Biochemistry, Vol.110, No.4, 493-500, 1991.
80.	Hiroyasu Inoue, Saori Takahashi, Kiyoshi Fukui and Yoshihiro Miyake : Leucine Zipper Motif in Porcine Renin-binding Protein (RnBP) and Its Relationship to the Formation of an RnBP-Renin Heterodimer and an RnBP Homodimer, The Journal of Biological Chemistry, Vol.266, No.18, 11896-11900, 1991.
81.	Motoshige Miyano, Kiyoshi Fukui, Fusao Watanabe, Saori Takahashi, Masazumi Tada, Masaru Kanashiro and Yoshihiro Miyake : Studies on Phe-228 and Leu-307 Recombinant Mutants of Porcine Kidney D-Amino Acid Oxidases, --- Expression, Purification, and Characterization ---, The Journal of Biochemistry, Vol.109, No.1, 171-177, 1991.
82.	Masazumi Tada, Kiyoshi Fukui, Motoshige Miyano and Yoshihiro Miyake : Expression of Mouse Kidney D-Amino Acid Oxidase in Escherichia Coli, --- Purification and Characterization of the Recombinant Protein ---, Flavins and Flavoproteins 1990, 147-150, 1991.
83.	Motoshige Miyano, Kiyoshi Fukui, Fusao Watanabe, Masazumi Tada, Saori Takahashi and Yoshihiro Miyake : Purification of Recombinant Mutant Porcine D-Amino Acid Oxidases, Flavins and Flavoproteins 1990, 151-154, 1991.
84.	Yoshihiro Miyake, Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe, Masazumi Tada, Motoshige Miyano and Saori Takahashi : Molecular Biological Studies on Structure-Function Relationship of D-Amino Acid Oxidase, Flavins and Flavoproteins 1990, 135-142, 1991.
85.	Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe, Masazumi Tada, Motoshige Miyano and Yoshihiro Miyake : Genomic Organization and Expression of D-Amino Acid Oxidase Gene, Flavins and Flavoproteins 1990, 143-146, 1991.
86.	Kiyoshi Fukui and Yoshihiro Miyake : D-アミノ酸酸化酵素の分子生物学的研究, Vitamins, Vol.64, No.9, 546-548, 1990.
87.	Kyoko Momoi, Kiyoshi Fukui, Masazumi Tada and Yoshihiro Miyake : Gene Expression of D-Amino Acid Oxidase in Rabbit Kidney, The Journal of Biochemistry, Vol.108, No.3, 406-413, 1990.
88.	Masazumi Tada, Kiyoshi Fukui, Kyoko Momoi and Yoshihiro Miyake : Cloning and Expression of a cDNA Encoding Mouse Kidney D-Amino Acid Oxidase, Gene, Vol.90, No.2, 293-297, 1990.
89.	Hiroyasu Inoue, Kiyoshi Fukui, Saori Takahashi and Yoshihiro Miyake : Molecular Cloning and Sequence Analysis of a cDNA Encoding a Porcine Kidney Renin-binding Protein, The Journal of Biological Chemistry, Vol.265, No.12, 6556-6561, 1990.
90.	Fusao Watanabe, Kiyoshi Fukui, Kyoko Momoi and Yoshihiro Miyake : Expression of Normal and Abnormal Porcine Kidney D-Amino Acid Oxidases in Escherichia Coil, --- Purification and Characterization of the Enzymes ---, Biochemical and Biophysical Research Communications, Vol.165, No.3, 1422-1427, 1989.
91.	Kiyoshi Fukui, Hiroyasu Inoue, Saori Takahashi and Yoshihiro Miyake : Biosynthesis of a Renin Binding Protein, Biochemical and Biophysical Research Communications, Vol.164, No.1, 265-270, 1989.
92.	Fusao Watanabe, Kiyoshi Fukui, Kyoko Momoi and Yoshihiro Miyake : Site-specific Mutagenesis of Lysine-204, Tyrosine-224, Tyrosine-228, and Histidine-307 of Porcine Kidney D-Amino Acid Oxidase and the Implications as to Its Catalytic Function, The Journal of Biochemistry, Vol.105, No.6, 1024-1029, 1989.
93.	Hiroyasu Inoue, Kiyoshi Fukui and Yoshihiro Miyake : Identification and Structure of the Rat True Tissue Kallikrein Gene Expressed in the Kidney., The Journal of Biochemistry, Vol.105, No.5, 834-840, 1989.
94.	Fusao Watanabe, Kiyoshi Fukui, Kyoko Momoi and Yoshihiro Miyake : Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function, FEBS Letters, Vol.238, No.2, 269-272, 1988.
95.	Kyoko Momoi, Kiyoshi Fukui, Fusao Watanabe and Yoshihiro Miyake : Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase, FEBS Letters, Vol.238, No.1, 180-184, 1988.
96.	Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe and Yoshihiro Miyake : In Vivo and in Vitro Expression of Porcine D-Amino Acid Oxidase, --- In Vitro System for the Synthesis of a Functional Enzyme ---, Biochemistry, Vol.27, No.18, 6693-6697, 1988.
97.	Yoshihiro Miyake, Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe and Toshihiro Shibata : Biological and Medical Aspects of D-Amino Acid Oxidase, --- Biogenesis and in vivo reaction with D-Propargylglycine ---, Flavins and Flavoproteins 1987, 501-508, 1988.
98.	Kiyoshi Fukui, Fusao Watanabe, Toshihiro Shibata, Kyoko Momoi and Yoshihiro Miyake : Molecular and Cellular Biology of D-Amino Acid Oxidase, Flavins and Flavoproteins 1987, 509-512, 1988.
99.	James R. Panuska, Kiyoshi Fukui and Charles W. Parker : Secreted Proteins of Human Monocytes, --- Analysis by Two-dimensional Gel Electrophoresis and Effect of Lipopolysaccharide ---, The Biochemical Journal, Vol.249, No.2, 501-511, 1988.
100.	Kiyoshi Fukui, Fusao Watanabe, Toshihiro Shibata and Yoshihiro Miyake : Molecular Cloning and Sequence Analysis of cDNA Encoding Porcine Kidney D-Amino Acid Oxidase., Biochemistry, Vol.26, No.12, 3612-3618, 1987.
101.	Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe and Yoshihiro Miyake : Biosynthesis of porcine kidney D-amino acid oxidase, Biochemical and Biophysical Research Communications, Vol.141, No.3, 1222-1228, 1986.
102.	Kyoko Momoi, Kiyoshi Fukui, Toshio Yamano and Yoshihiro Miyake : Nephrotoxicity of D-Propargylglycine, a Suicide Inhibitor of D-Amino Acid Oxidase, Toxicology Letters, Vol.31, 34, 1986.
103.	Junji Yodoi, Masafumi Okada, Yutaka Tagaya, Keisuke Teshigawara, Kiyoshi Fukui, Norio Ishida, Koh-ichi Ikuta, Michiyuki Maeda, Tasuku Honjo, Hisao Osawa, Tibor Diamantstein, Masatoshi Tateno and Takashi Yoshiki : Rat Lymphoid Cell Lines Producing Human T Cell Leukemia Virus., --- II. Constitutive Expression of Rat Interleukin 2 Receptor ---, The Journal of Experimental Medicine, Vol.161, No.5, 924-934, 1985.
104.	Junji Yodoi, Keisuke Teshigawara, Toshio Nikaido, Kiyoshi Fukui, Takafumi Noma, Tasuku Honjo, Masahiro Takigawa, Masao Sasaki, Nagahiro Minato, Mitsuru Tsudo, Takashi Uchiyama and Michiyuki Maeda : TCGF (IL-2)-Receptor Inducing Factor(s)., --- I. Regulation of IL 2 Receptor on a Natural Killer-like Cell Line (YT Cells). ---, The Journal of Immunology, Vol.134, No.3, 1623-1630, 1985.
105.	Yuji Wano, Takashi Uchiyama, Kiyoshi Fukui, Michiyuki Maeda, Haruto Uchino and Junji Yodoi : Characterization of Human Interleukin 2 Receptor ( Tac Antigen ) in Normal and Leukemic T cells, --- Co-expression of Normal and Aberrant Receptors on HUT-102 Cells. ---, The Journal of Immunology, Vol.132, No.6, 3005-3010, 1984.
106.	Kiyoshi Fukui, Yasushi Hamaguchi, Akira Shimizu, Sumiko Nakai, Kazuo Moriwaki, Hai Wang Cheng and Tasuku Honjo : Duplicated Immunoglobulin Gamma 2a Genes in Wild Mice, The Journal of Molecular and Cellular Immunology, Vol.1, 321-330, 1984.
107.	Kiyoshi Fukui, 矢尾板芳郎 and Tasuku Honjo : Southern Blotting, 免疫実験操作法, Vol.12, 4007-4013, 1983.
108.	Kiyoshi Fukui, Takafumi Noma, Kaoru Takeuchi, Nobuyuki Kobayashi, Masakazu Hatanaka and Tasuku Honjo : Origin of Adult T-Cell Leukemia Virus, --- Implication for Its Zoonosis ---, Molecular Biology & Medicine, Vol.1, 447-456, 1983.
109.	Kiyoshi Fukui and Charles W. Parker : Binding of a 37k MW protein Produced by human monocytes to lymphocytes, Federation Proceedings, Vol.41, No.3, 318, 1982.

Academic Paper (Unrefereed Paper):

1.	Taiki Kohiki, Yusuke Kato, Masaya Denda, Yusuke Nishikawa, Kazuko YORITA, Ikuko Sagawa, Tsubasa Inokuma, Akira Shigenaga, Kiyoshi Fukui and Akira Otaka : Development and application of novel protein labeling reagent "SEAL", Peptide Science 2018, 104, 2019.
2.	Kiyoshi Fukui : ビタミンB群が担う脳内D-アミノ酸代謝システムの疾患酵素学研究, Vitamins, Vol.88, No.10, 524-529, 2014. (Link to Publication Site) ● Publication site (DOI): 10.20632/vso.88.10_524 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390001205700169472 ● Search Scopus @ Elsevier (DOI): 10.20632/vso.88.10_524 (DOI: 10.20632/vso.88.10_524, CiNii: 1390001205700169472)
3.	Kiyoshi Fukui, Yuji Shishido, Kazuko YORITA and Takashi Sakai : Pathophysiological Basis of D-Amino Acid Metabolizing Enzyme : Susceptibility to Schizophrenia and D-Amino Acid Oxidase, BIO INDUSTRY, Vol.31, No.3, 11-16, 2014. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1520854804832558080 (CiNii: 1520854804832558080)
4.	Koji Ono, Yuji Shishido, Hwan Ki Park, Rabab Mohamed Abou EL-Magd, Seongpil Chung, Kazuko YORITA, Nobuya Sano, Arima Kunimasa, Takashi Sakai, Kazunori Ishimura and Kiyoshi Fukui : 統合失調症におけるD-アミノ酸酸化酵素の病態生理学的役割:ヒトおよびラット脳内における組織化学的発現解析, Vitamins, Vol.86, No.7, 395-397, 2012. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1390282680677137280 (CiNii: 1390282680677137280)
5.	Kiyoshi Fukui, Yumiko Tomita, Takashi Sakai, Yoshihisa Shimizu and Kazuya Kanda : Molecular biological study on the function and signal transduction of novel vasoactive mediator, Research Report of Takeda Medical Research Foundation, Vol.25, 61-65, 1998.

Academic Letter:

1.	Yusuke Kato, Kiyoshi Fukui and Kazuo Suzuki : トリインフルエンザH5N1を高病原性化するNon-structural protein 1における変異のタンパク質分子機構, バイオイメージング, Vol.25, No.1, 30-31, 2016. (Tokushima University Institutional Repository) ● Metadata: 112840 (Tokushima University Institutional Repository: 112840)
2.	Norihiro Shibuya, Mari Ishigami, Mariko Tanaka, Yuka Kimura, Yuki Ogasawara, Kiyoshi Fukui and Hideo Kimura : Another Pathway to produce hydrogen sulfide in the brain, Journal of Pharmacological Sciences, Vol.118, No.Suppl.1, 104, 2012.
3.	Kiyoshi Fukui : Disease-oriented enzymology on D-amino acid metabolism, Seikagaku, Vol.80, No.4, 344-351, 2008. (Keyword) Amino Acids / Animals / Antipsychotic Agents / Astrocytes / Cloning, Molecular / Crystallization / D-Amino-Acid Oxidase / Drug Design / Gene Expression Regulation, Enzymologic / Humans / Isomerism / Mental Disorders / Nervous System Diseases / Protein Modification, Translational / RNA, Messenger / Serine (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18516914 ● CiNii @ National Institute of Informatics (CRID): 1520572358857347584 ● Summary page in Scopus @ Elsevier: 2-s2.0-48049092051 (PubMed: 18516914, CiNii: 1520572358857347584, Elsevier: Scopus)
4.	Takashi Sakai and Kiyoshi Fukui : Nucling, a novel mediator for cell death pathway, Seikagaku, Vol.78, No.9, 867-871, 2006. (Keyword) Animals / Apoptosis / Apoptotic Protease-Activating Factor 1 / Caspase 9 / Cytochromes c / Galectin 3 / Humans / Liver Neoplasms / Membrane Proteins / NF-kappa B / Parkinson Disease / Signal Transduction (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17052022 ● CiNii @ National Institute of Informatics (CRID): 1520009409491028352 ● Search Scopus @ Elsevier (PMID): 17052022 (PubMed: 17052022, CiNii: 1520009409491028352)
5.	Suzana Gispert, Astrid Lunkes, Nieves Santos, Guillermo Orozco, Duc Ha-Hao, Tim Ratzlaff, Jorge Aguiar, Isis Torrens, Luis Heredero, Alexis Brice, Geraldine Cancel, Giovanni Stevanin, Jean-Claude Vernant, Alexandra Durr, Agnes Lepage-Lezin, Samir Belal, Mongi Ben-Hamida, Stephan Pulst, Guy Rouleau, Jean Weissenbach, Denis LePaslier, Raju Kucherlapati, Kate Montgomery, Kiyoshi Fukui and Georg Auburger : Localization of the candidate gene D-Amino Acid Oxidase outside the refined 1-cM region of Spinocerebellar Ataxia 2 (SCA2), American Journal of Human Genetics, Vol.57, No.4, 972-975, 1995. (Keyword) Base Sequence / D-Amino-Acid Oxidase / DNA, Satellite / Haplotypes / Humans / Molecular Sequence Data / Pedigree / Spinocerebellar Degenerations (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 7573064 ● Search Scopus @ Elsevier (PMID): 7573064 (PubMed: 7573064)

Proceeding of International Conference:

1.	Hyeon Soo Kim, Hirofumi Sogabe, Wanitcha Rachadech, Yuji Shishido, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : Spatiotemporal distribution of D-amino acid oxidase in central neurons system and kidney, 5th International Conference on D-Amino Acid Research -- IDAR2022, Urbana, Illinois, Jul. 2022.
2.	Yuji Shishido, Soo Hyeon Kim, Hirofumi Sogabe, Wanitcha Rachadech, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : AGE- AND GENDER-DEPENDENT D-AMINO ACID OXIDASE ACTIVITY IN MOUSE NERVOUS SYSTEM AND PERIPHERAL TISSUES: IMPLICATION FOR AGING AND NEURODEGENERATION, The 4th International Conference of D-Amino Acid Research, Tokyo, Sep. 2019.
3.	Taiki Kohiki, Yusuke Kato, Masaya Denda, Yusuke Nishikawa, Kazuko YORITA, Ikuko Sagawa, Tsubasa Inokuma, Akira Shigenaga, Kiyoshi Fukui and Akira Otaka : Development and application of novel protein labeling reagent "SEAL", 10th International Peptide Symposium, Kyoto, Dec. 2018.
4.	Yusuke Kato, Nobuo Maita, Taiki Kohiki, Sumire Kurosawa, Yusuke Nishikawa, Ikuko Sagawa, Masaya Denda, Tsubasa Inokuma, Yuji Shishido, Kazuko YORITA, Akira Shigenaga, Akira Otaka and Kiyoshi Fukui : Combined approach of computation and enzymology to investigate novel D-amino acid oxidase inhibitors, The 13th International Symposium of the Institute Network for Biomedical Sciences joint with the 3rd Symposium of the Inter-University Research Network for Trans-Omics Medicine and the 28th Hot Spring Harbor Symposium, Fukuoka, Oct. 2018.
5.	Yusuke Kato, Taiki Kohiki, Yusuke Nishikawa, Ikuko Sagawa, Masaya Denda, Tsubasa Inokuma, Yuji Shishido, Akira Shigenaga, Akira Otaka and Kiyoshi Fukui : Studies on binding molecules to D-amino acid oxidase using computational approaches, The 12th International Symposium of the Institute Network, Tokyo, Nov. 2017.
6.	Kiyoshi Fukui, Hong Diem Tran, Hirofumi Sogabe, Hyeon Soo Kim, Trinh Thanh Thi Huong, Anh Tuan Pham, Yuji Shishido, Kazuko YORITA and Yusuke Kato : Translational enzymology on D-amino acid metabolism, The 3rd International Conference of D-Amino Acid Research, Varese, Jul. 2017.
7.	Hirofumi Sogabe, Yuji Shishido, SooHyeon Kim, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : Regulation of D-amino acid oxidase expression and metabolism in mammalian cells, The 3rd International Conference of D-Amino Acid Research, Varese, Jul. 2017.
8.	Kazuko YORITA, Sumire Kurosawa, Yuri Yoshida, Yoshiki Kashiwada, Shigeki Sano, Akira Otaka and Kiyoshi Fukui : Screening of the effectors for human D-amino acid oxidase and the analyses of structure-activity relationships, The 19th triennial International Symposium on Flavins and Flavoproteins, Groningen, Jul. 2017.
9.	Hirofumi Sogabe, Yuji Shishido and Kiyoshi Fukui : Regulation of D-amino acid oxidase expression in mammalian cells, 11th International Symposium of The Institute Network Frontiers in Biomedical Sciences, Tokushima, Jan. 2017.
10.	Kiyoshi Fukui, Hirofumi Sogabe, Soo Hyeon Kim, Hung Thi Thanh Trinh, Tuan Anh Pham, Diem Hong Tran, Yuji Shishido, Kazuko YORITA and Yusuke Kato : Medical aspects and chiral science of amino acid metabolism: regulation of human D-amino acid oxidase gene expression and implication for translation to neuropsychiatric disorders, The Fifth International Conference on Cofactors and Active Enzyme Molecule 2016, Kurobe, Sep. 2016.
11.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : A novel apoptosis associated protein, Nucling Controls Mammary Gland Involution by Regulating NF-B and STAT3: Implication for the pathogenesis of breast cancer, Inaugural Symposium Biochemistry: Towards Academic Excellence, Boralesgamuwa, Jun. 2016.
12.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : Nucling, a Novel Apoptosis-associated Protein, Controls Mammary Gland Involution by Regulating NF-B and STAT3, 1st International Symposium on Molecular Medicine in Tokushima University, Tokushima, Dec. 2015.
13.	Kiyoshi Fukui, Diem Hong Tran, Huy Van Dang, Huong Thi Thanh Trinh, Tuan Anh Pham, Hirofumi Sogabe, Soo Hyeon Kim, Takanaga Ako, Yuji Shishido, Kazuko YORITA, Yusuke Kato and Takashi Sakai : Chiral Science and Pathophysiology of Amino Acid Metabolism: regulation of human D-amino acid oxidase gene expression and implication for human psychiatric disorders., 14th FAOBMB Congress and 84th Annual Meeting of SBC (I), Hyderabad, Nov. 2015.
14.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : Nucling, a novel apoptosis-associated protein, controls postlactational involution of mammary gland through regulation of NF-B and STAT3, The 2nd GENE AND IMMUNOTHERAPY CONFERENCE in VIETNAM, Ho Chi Minh, Sep. 2015.
15.	Diem Hong Tran, Yuji Shishido, Seongpil Chung, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Search for the regulation of human D-amino acid oxidase gene, a potential risk factor of schizophrenia, The 2nd GENE AND IMMUNOTHERAPY CONFERENCE in VIETNAM, Ho Chi Minh, Sep. 2015.
16.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : Nucling, an apoptosis-associated novel protein, controls mammary gland involution through regulation of NF-B and STAT3, The 10th International Symposium of the Institute Network, Sapporo, Jul. 2015. (Link to Publication Site) ● Publication site (DOI): 10.1074/jbc.M115.673848 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26269594 ● Search Scopus @ Elsevier (PMID): 26269594 ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M115.673848 (DOI: 10.1074/jbc.M115.673848, PubMed: 26269594)
17.	Yusuke Kato and Kiyoshi Fukui : In silico approach to elucidate the regulatory mechanism of D-amino acid oxidase, The 10th International Symposium of the Institute Network, Sapporo, Jul. 2015.
18.	Kiyoshi Fukui, Diem Hong Tran, Huy Van Dang, Huong Thi Thanh Trinh, Tuan Anh Pham, Hirofumi Sogabe, Soo Hyeon Kim, Takanaga Ako, Yuji Shishido, Kazuko YORITA, Yusuke Kato and Takashi Sakai : Chiral science of amino acid metabolism and implication to pathophysiology of schizophrenia, 40th Annual Conference of the Malaysian Society for Biochemistry & Molecular Biology, Kuala Lumpur, Jun. 2015.
19.	Kiyoshi Fukui, Yoshiteru Urai, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Rabab Mohamed Abou El-Magd, Seongpil Chung, Salah Mohamed El-Sayed, Diem Hong Tran, Hirofumi Sogabe, Takanaga Ako, Yuji Shishido, Kazuko YORITA and Takashi Sakai : D-AMINO ACID METABOLISM IN HEALTH AND DISEASES: PATHOPHYSIOLOGICAL BASES FOR SCHIZOPHRENIA AND CANCER GENE THERAPY, The 2nd International Conference of D-Amino Acid Research, Utsunomiya, Sep. 2014.
20.	Diem Hong Tran, Yuji Shishido, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Identification of promoter region of human D-amino acid oxidase (hDAO) gene and its interacting proteins - Search for the regulation of hDAO expression, The 9th International Symposium of the Institute Network, Suita, Jun. 2014.
21.	Kiyoshi Fukui : Pathophysiological Basis of D-Amino Acid Metabolizing System in Brain for Susceptibility to Schizophrenia, FAOBMB/HKSBMB Mini-Symposium 2014 Perspectives and Challenges in Biochemistry and Molecular Biology, Hong Kong, Jun. 2014.
22.	Kiyoshi Fukui, Yoshiteru Urai, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Rabab Mohamed Abou El-Magd, Seongpil Chung, Salah Mohamed El-Sayed, Diem Hong Tran, Yuji Shishido, Kazuko YORITA and Takashi Sakai : Medical Aspects of D-Amino Acid Metabolism: Molecular Target for Cancer Gene Therapy and Schizophrenia, FAOBMB Mini-Symposium Molecular Bases for Medical and Pharmaceutical Sciences, Yahaba, Apr. 2013.
23.	Kiyoshi Fukui, Yoshiteru Urai, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Rabab Mohamed Abou El-Magd, Seongpil Chung, Salah Mohamed El-Sayed, Diem Hong Tran, Yuji Shishido, Kazuko YORITA and Takashi Sakai : Medical Aspects of D-Amino Acid Metabolism: Molecular Target for Cancer Gene Therapy and Schizophrenia, The 1st GENE AND IMMUNOTHERAPY CONFERENCE, Ho Chi Minh, Mar. 2013.
24.	Kiyoshi Fukui, Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Diem Hong Tran and Takashi Sakai : Oxidative Stress-Energy Deplation Therapy as a New Treatment Modality for Glioma, Miami 2013 Winter Symposium: The Molecular Basis of Metabolism and Nutrition, Miami, Feb. 2013.
25.	Kiyoshi Fukui, Tomoya Kawazoe, Sanae Iwana, Rabab Mohamed Abou El-Magd, Koji Ono, Seongpil Chung, Salah Mohamed El-Sayed, Kumiko Shinohara, Diem Hong Tran, Yuji Shishido, Kazuko YORITA and Takashi Sakai : Modulation of D-amino acid oxidase activity as a novel strategy for the treatment of psychiatric disorders, Function and dysfunction of D-amino acids in the central nervous system, Tokyo, Sep. 2011.
26.	Kiyoshi Fukui : Enzyme Pathophysiology on D-Amino Acid Metabolism and Apoptosis: Molecular Targets for Schizophrenia and Neurodegeneration, Enzyme Research Forum 2011 in Nantong University, 南通市, Mar. 2011.
27.	Takashi Sakai, Li Liu, HoangNam Tran, Sun Mi Kim and Kiyoshi Fukui : Nucling a novel apoptosis-associating protein, regulates NF-B pathway, the 12th IUBMB Conference, the 21st FAOBMB Conference and the ComBio2010 meeting, Melbourne, Sep. 2010.
28.	Kiyoshi Fukui, Koji Ono, Rabab Mohamed Abou El-Magd, Sanae Iwana, Tomoya Kawazoe, Seongpil Chung, Ying Song, Yuji Shishido, Kazuko YORITA and Takashi Sakai : D-amino acid oxidase: pathophysiological basis and molecular target for schizophrenia, the 12th IUBMB Conference, the 21st FAOBMB Conference and the ComBio2010 meeting, Melbourne, Sep. 2010.
29.	Sun Mi Kim, Takashi Sakai, HoangNam Tran and Kiyoshi Fukui : Physiological Function of a Novel NF-B-Regulating Molecule, Nucling, in Immune System, the 12th IUBMB Conference, the 21st FAOBMB Conference and the ComBio2010 meeting, Melbourne, Sep. 2010.
30.	Kiyoshi Fukui, Sanae Iwana, Rabab Mohamed Abou El-Magd, Tomoya Kawazoe, Koji Ono, Seongpil Chung, Yuji Shishido, Kazuko YORITA and Takashi Sakai : Modulation of D-Amino Acid Oxidase Activity as a Novel Strategy for the Treatment of Schizophrenia, The 1st Meeting of the Asian College of Neuropsychopharmacology, Kyoto, Nov. 2009.
31.	Takashi Sakai, HoangNam Tran, Sun Mi Kim, Li Liu, Xichuan Teng, Yuji Shishido, Mukai-Sakai Rika, Mitsuru Matsumoto, Kazunori Ishimura, Yoshio Hayashi, Ryuji Kaji and Kiyoshi Fukui : Nucling, a novel stress-sensitive protein, regulates NF-kappa B activation, The 4th International Congress on Stress Responses in Biology and Medicine, The 4th Annual Meeting of the Biomedical Society for Stress Response, Sapporo, Oct. 2009.
32.	Kiyoshi Fukui, Sanae Iwana, Rabab Mohamed Abou El-Magd, Tomoya Kawazoe, Koji Ono, Seongpil Chung, Yuji Shishido, Kazuko YORITA and Takashi Sakai : Modulation of D-amino acid oxidase activity as a novel strategy for the treatment of schinophrenia, The 1st International Conference of D-amino Acid Research, Awaji, Jul. 2009.
33.	Takashi Sakai, Li Liu, Xichuan Teng, Naozumi Ishimaru, Rika Sakai, HoangNam Tran, Nobuya Sano, Yoshio Hayashi, Ryuji Kaji and Kiyoshi Fukui : Inflammatory disease and cancer with a decrease in Kupffer cell numbers in Nucling-konckout mouse, 20th FAOBMB Taipei Conference, Taipei, Oct. 2008.
34.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Akiko Kita, Kiyoshi Fukui, Tomitake Tsukihara and Yukio Morimoto : Substrate recognition mechanism of L-lactate oxidase from Aerococcus viridans at 2.0Å resolution, Joint Conference of the Asian Crystallographic Association and the Crystallographic Society of Japan (AsCA '06/CrSJ), Tsukuba, Nov. 2007.
35.	Kiyoshi Fukui : Potential Role for Astroglial D-amino Acid Oxidase in Extracellular D-Serine Metabolism and Pathogenesis of Schizophrenia, The 14th Symposium of Dongguk University Medical Research Institute, Gyounju, Sep. 2006.
36.	Kiyoshi Fukui : Potential Role for Astroglial D-amino Acid Oxidase in Extracellular D-Serine Metabolism and Pathogenesis of Schizophrenia, The 47th International Symposium of Korean Society of Life Science, Daegu, Sep. 2006.
37.	Tomoya Kawazoe, Hideaki Tsuge, Mirella S. Pilone and Kiyoshi Fukui : Crystal structure of human D-amino acid oxidase: Implications for a Hypothetical Activation Mechanism, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
38.	Sanae Iwana, Kazuko YORITA, Tomoya Kawazoe, Koji Ono, Akiko Kita, Seongpil Chung, Rabab Mohamed Abou El-Magd, Hwan Ki Park and Kiyoshi Fukui : Inhibitory effect of an antipsychotic, chlorpromazine, and its derivative on D-amino acid oxidase, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
39.	Kazuko YORITA, Yasufumi Umena, Takeshi Matsuoka, David P. Ballou, Akiko Kita, Yukio Morimoto and Kiyoshi Fukui : Active Site Topology of L-Lactate Oxidase from Aerococcus Viridans, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
40.	Koji Ono, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Seongpil Chung, Rabab Mohamed Abou El-Magd, Yumiko Tomita, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Gene Expression of D-Amino Acid Oxidase in the brain, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
41.	Li Liu, Takashi Sakai, Xichuan Teng, Rika Mukai-Sakai, Ryuji Kaji and Kiyoshi Fukui : Nucling inhibits nuclear translocation and activation of NF-B through interaction with NF-B-p50, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
42.	Xichuan Teng, Takashi Sakai, Li Liu, Rika Sakai, Ryuji Kaji and Kiyoshi Fukui : Attenuation of MPTP-induced neurotoxicity and locomotor dysfunction in Nucling-deficient mice via suppression of the apoptosome pathway, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
43.	Takashi Sakai, Li Liu, Rika Mukai-Sakai, Nobuya Sano, Ryuji Kaji and Kiyoshi Fukui : Pro-inflammatory stress promotes carcinogenesis through NF-B-activation and inactivation pathway, 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress, Kyoto, Jun. 2006.
44.	Kiyoshi Fukui, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Kazuko YORITA, Takashi Sakai and Hideaki Tsuge : Potential roles for astroglial D-amino acid oxidase in extracellular D-serine metabolism and cytotoxicity: Molecular approach to schizophrenia, IUBMB Symposium 344 International Interdisciplinary Conference on Vitamins, Coenzymes, and Biofactors 2005, Higashiura, Nov. 2005.
45.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui, Tomitake Tsukihara and Yukio Morimoto : Structures of Arg-181 mutant and wild type of L-lactate oxidase from Aerococcus viridans., 20th Congress of the International Union of Crystallography, Florence, Aug. 2005.
46.	Kiyoshi Fukui, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Kazuko YORITA and Takashi Sakai : Potential roles for astroglial D-amino acid oxidase in extracellular D-serine metabolism and cytotoxicity: Molecular approach to schizophrenia, 9th International Congress on Amino Acids and Ptoteins, Wien, Aug. 2005.
47.	Kazuko YORITA, Takeshi Matsukoa, David P. Ballou and Kiyoshi Fukui : H265Q L-Lactate Oxidase from Aerococcus viridans, 15th International Symposium on Flavins and Flavoproteins, Hayama, Apr. 2005.
48.	Kazuko YORITA, Yasufumi Umena, Takeshi Matsukoa, David P. Ballou, Makoto Abe, Akiko Kita, Tomitake Tsukihara, Yukio Morimoto and Kiyoshi Fukui : Crystal Structures of Wild-type and R181M L-Lactate Oxidase from Aerococcus viridans, 15th International Symposium on Flavins and Flavoproteins, Hayama, Apr. 2005.
49.	Kiyoshi Fukui, Hwan Ki Park, Tomoya Kawazoe, Koji Ono, Sanae Iwana, Yumiko Tomita, Kazuko YORITA, Takashi Sakai and Young Ho Kim : Functional Roles and Pathophysiology of Brain D-Amino Acid Oxidase, 15th International Symposium of Flavins and Flavoproteins, Hayama, Apr. 2005.
50.	Gianluca Molla, Mirella S. Pilone, Silvia Sacchi, Mariagrazia Bernasconi, Kiyoshi Fukui and Loredano Pollegioni : Molecular Basis of Schizophrenia: Characterization of Human D-Amino Acid Oxidase, 15th International Symposium of Flavins and Flavoproteins, Hayama, Apr. 2005.
51.	Tomoya Kawazoe, Sanae Iwana, Koji Ono, Hwan Ki Park, Kazuko YORITA, Yumiko Tomita, Hideaki Tsuge and Kiyoshi Fukui : Purification and Crystal Structure of Human D-Amino Acid Oxidase, 15th International Symposium of Flavins and Flavoproteins, Hayama, Apr. 2005.
52.	Kiyoshi Fukui, Yoshiteru Urai, Osamu Jinnouchi, Tokujiro Kanamori, Kyung Tak Kwak, Hwan Ki Park, Atsuhiko Suzue, Shinji Nagahiro, Yumiko Tomita and Takashi Sakai : Astroglial expression of D-amino acid oxidase gene, The 14th International Congress on Flavins and Flavoproteins, Cambridge, Jul. 2002.
53.	Kiyoshi Fukui, Tokujiro Kanamori, Mariko Obayashi, Osamu Jinnouchi, Kazuya Kanda, Yoshiteru Urai, Yuji Shishido, Atsuhiko Suzue and Takashi Sakai : Gene Expression of D-Amino Acid Oxidase in Nervous System, The 13th International Congress on Flavins and Flavoproteins, Konstanz, Aug. 1999.
54.	Ryuichi Konno, Akira Niwa, Masato Sasaki, Jumpei Enami, Setsuko Asakura and Kiyoshi Fukui : Is There D-Amino acid oxidase in the Mouse Liver?, The 12th International Symposium on Flavins and Flavoproteins, Calgary, Jun. 1996.
55.	Kiyoshi Fukui, Tokujiro Kanamori, Osamu Jinnouchi and Oded Ben-Yoseph : Tissue Specific Expression of the D-Amino Acid Oxidase Gene, The 12th International Symposium on Flavins and Flavoproteins, Calgary, Jun. 1996.
56.	Kiyoshi Fukui : Structure of Human D-Amino Acid Oxidase Gene, The 11th International Symposium on Flavins and Flavoproteins, Nagoya, Jul. 1993.
57.	Masazumi Tada, Kiyoshi Fukui, Motoshige Miyano and Yoshihiro Miyake : Expression of Mouse Kidney D-Amino Acid Oxidase in Escherichia Coli, --- Purification and Characterization of the Recombinant Protein ---, The 10th International Symposium on Flavins and Flavoproteins, Como, Jul. 1990.
58.	Motoshige Miyano, Kiyoshi Fukui, Fusao Watanabe, Masazumi Tada, Saori Takahashi and Yoshihiro Miyake : Purification of Recombinant Mutant Porcine D-Amino Acid Oxidases, The 10th International Symposium on Flavins and Flavoproteins, Como, Jul. 1990.
59.	Yoshihiro Miyake, Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe, Masazumi Tada, Motoshige Miyano and Saori Takahashi : Molecular Biological Studies on Structure-Function Relationship of D-Amino Acid Oxidase, The 10th International Symposium on Flavins and Flavoproteins, Como, Jul. 1990.
60.	Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe, Masazumi Tada, Motoshige Miyano and Yoshihiro Miyake : Genomic Organization and Expression of D-Amino Acid Oxidase Gene, The 10th International Symposium on Flavins and Flavoproteins, Como, Jul. 1990.
61.	Yoshihiro Miyake, Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe and Toshihiro Shibata : Biological and Medical Aspects of D-Amino Acid Oxidase, --- Biogenesis and in vivo reaction with D-Propargylglycine ---, The 9th International Symposium on Flavins & Flavoproteins, Atlanta, Jun. 1987.
62.	Kiyoshi Fukui, Fusao Watanabe, Toshihiro Shibata, Kyoko Momoi and Yoshihiro Miyake : Molecular and Cellular Biology of D-Amino Acid Oxidase, The 9th International Symposium on Flavins & Flavoproteins, Atlanta, Jun. 1987.

Proceeding of Domestic Conference:

1.	Wanitcha Rachadech, Yusuke Kato, Rabab Magd El Abou Mohamed Ahmed, Yuji Shishido, SooHyeon Kim, Hirofumi Sogabe, Nobuo Maita, Kazuko YORITA and Kiyoshi Fukui : Structural and catalytic properties of P219L human D-amino acid oxidase: implications for the ligand binding and catalytic efficiency, The 93rd Annual Meeting of the Japanese Biochemical Society, Sep. 2020.
2.	SooHyeon Kim, Yuji Shishido, Hirofumi Sogabe, Wanitcha Rachadech, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : マウス脳および末梢組織における年齢および性別依存的D-アミノ酸酸化酵素活性:加齢および神経変性への影響について, The 92nd Annual Meeting of the Japanese Biochemical Society, Sep. 2019.
3.	Bunrin Rin, Hirofumi Sogabe, Yuji Shishido, Kiyoshi Fukui and Takashi Sakai : 新規NF-κB制御分子ヌクリングはインスリンの発現制御に関与している, The 91st Annual Meeting of the Japanese Biochemical Society, Sep. 2018.
4.	SooHyeon Kim, Yuji Shishido, Hirofumi Sogabe, Rachadech Wanitcha, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : Distribution of D-amino acid oxidase activity in mouse brain regions and peripheral tissues examined by enzyme-coupled colorimetric assay, The 91st Annual Meeting of the Japanese Biochemical Society, Sep. 2018.
5.	Yuji Shishido, Hirofumi Sogabe, SooHyeon Kim, Rachadech Wanitcha, Yusuke Kato and Kiyoshi Fukui : アストログリアにおける自然免疫系によるD-アミノ酸酸化酵素遺伝子の発現調節, The 91st Annual Meeting of the Japanese Biochemical Society, Sep. 2018.
6.	Yuji Shishido, Hirofumi Sogabe, Hyeon Soo Kim, Rachadech Wanitcha, Yusuke Kato and Kiyoshi Fukui : 自然免疫とヒト D-アミノ酸酸化酵素遺伝子の発現調節機構, 第14回 D-アミノ酸研究会学術講演会, Sep. 2018.
7.	Yusuke Kato, 伊藤吹夕, 高橋和浩, 菅又龍一, Sumire Kurosawa, Kazuko YORITA, 鈴木章一, 山本友子, 河内正治, 三牧正和, Kazuo Suzuki and Kiyoshi Fukui : 計算科学による酵素活性制御分子の解析, 日本バイオイメージング学会, Sep. 2018.
8.	西晃, Shusuke Numata, Atsushi Tajima, Xiaolei Zhu, 伊藤候輝, 斎藤淳, Yusuke Kato, Makoto Kinoshita, 下寺信次, 小野慎治, 越智紳一郎, 今村明, 黒滝直弘, Shu-ichi Ueno, 岩田仲生, Kiyoshi Fukui, Issei Imoto, 神谷篤 and Tetsuro Ohmori : 統合失調症におけるde novo変異(突然変異)研究, 第13回日本統合失調症学会, Mar. 2018.
9.	Hirofumi Sogabe, Yuji Shishido, SooHyeon Kim, Wanitcha Rachadech, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : 哺乳動物細胞におけるD-アミノ酸酸化酵素タンパク質の代謝経路の解析, 2017年度生命科学系学会合同年次大会, Dec. 2017.
10.	Yuji Shishido, Hirofumi Sogabe, SooHyeon Kim, Wanitcha Rachadech, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : ミクログリアにおけるD-アミノ酸酸化酵素遺伝子の発現調節機構の解明, 2017年度生命科学系学会合同年次大会, Dec. 2017.
11.	渋谷典広, 小池伸, 宮本亮, 湯浅磨里, 田中真紀子, 木村由佳, 高野陽子, 花岡健二郎, 永原則之, Kiyoshi Fukui, 浦野泰照, 小笠原祐樹 and 木村英雄 : 生理活性物質硫化水素とポリサルファイドの産生機構, 2017年度生命科学系学会合同年次大会, Dec. 2017.
12.	Yusuke Kato, Taiki Kohiki, Yusuke Nishikawa, Ikuko Sagawa, Masaya Denda, Tsubasa Inokuma, Yuji Shishido, Akira Shigenaga, Akira Otaka and Kiyoshi Fukui : DAO分子表面に結合する阻害分子の計算科学的解析, 2017年度生命科学系学会合同年次大会, Dec. 2017.
13.	Yusuke Kato, 伊藤吹夕, 髙橋和浩, 菅又龍一, 鈴木章一, 山本友子, 河内正治, Kiyoshi Fukui, 三牧正和 and Kazuo Suzuki : B型インフルエンザノイラミニダーゼの薬物耐性機構の解析に向けて, 第23回MPO研究会, Dec. 2017.
14.	Kiyoshi Fukui : 脳内D-アミノ酸代謝システムをターゲットとした疾患酵素学研究, 第28回フォーラム・イン・ドージン「D-アミノ酸生物学-右と左からみた生命の世界」, Nov. 2017.
15.	Taiki Kohiki, Yusuke Kato, Yusuke Nishikawa, Kazuko YORITA, Ikuko Sagawa, Masaya Denda, Tsubasa Inokuma, Akira Shigenaga, Kiyoshi Fukui and Akira Otaka : N-Sアシル基転移を基盤としたタンパク質ラベル化法を用いたD-アミノ酸酸化酵素阻害剤の結合サイト解明研究, 第56回日本薬学会・日本薬剤師会・日本大学病院薬剤師会中国四国支部学術大会, Oct. 2017.
16.	Yusuke Kato and Kiyoshi Fukui : D-アミノ酸酸化酵素の相互作用分子に関する計算科学的解析, Japanese Bioimaging Society Symposium, Sep. 2017.
17.	伊藤吹夕, Yusuke Kato, 髙橋和浩, 菅又龍一, 鈴木章一, 山本友子, 河内正治, Kiyoshi Fukui, 三牧正和 and Kazuo Suzuki : 抗インフルエンザ薬の効果が不良な小児のノイラミニダーゼ(NA)解析, 第26回日本バイオイメージング学会学術集会, Sep. 2017.
18.	Hirofumi Sogabe, Yuji Shishido, Soo Hyeon Kim, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : 哺乳動物細胞におけるD-アミノ酸酸化酵素タンパク質の代謝経路の解析, 日本ビタミン学会第69回大会, Jun. 2017.
19.	Wenling Lin, Tuan Anh Pham, Kiyoshi Fukui and Takashi Sakai : 新規NF-κB制御分子ヌクリングはインスリンの発現制御に関与している, 第39回日本分子生物学会年会, Dec. 2016.
20.	Yusuke Kato and Kiyoshi Fukui : Structure and function prediction of the G72 protein, 第54回日本生物物理学会年会, Nov. 2016.
21.	渋谷典広, 小池伸, 田中真紀子, 湯浅磨里, 木村由佳, 小笠原祐樹, Kiyoshi Fukui, 永原則之 and 木村英雄 : D-システインからの硫化水素産生, 第89回日本生化学会大会, Sep. 2016.
22.	Yuji Shishido, Huong Thi Thanh Trinh, Soo Hyeong Kim, Hirofumi Sogabe, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : グリア細胞におけるヒトD-アミノ酸酸化酵素遺伝子の発現誘導機構の解明, 第89回日本生化学会大会, Sep. 2016.
23.	Yusuke Kato, 早田海渡 and Kiyoshi Fukui : D-アミノ酸酸化酵素の相互作用分子に関する計算科学的解析, 第89回日本生化学会大会, Sep. 2016.
24.	Yuji Shishido, Yuta Isomura, Hiroya Matsuda, Huong Thi Thanh Trinh, Soo Hyeong Kim, Hirofumi Sogabe, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : ヒトD-アミノ酸酸化酵素遺伝子の発現調節機構と炎症反応, 第12回D-アミノ酸学会学術講演会, Sep. 2016.
25.	Yusuke Kato, Kiyoshi Fukui and Kazuo Suzuki : トリインフルエンザ劇症化における NS1 ダイマーの分子機構, 第25回日本バイオイメージング学会学術集会, Sep. 2016.
26.	Kazuko YORITA, Sumire Kurosawa, Yuuri Yoshida, Akira Otaka, Yoshiki Kashiwada, Shigeki Sano, Noriaki Minakawa and Kiyoshi Fukui : ヒトD-アミノ酸酸化酵素のエフェクター探索と構造活性相関, 日本ビタミン学会第68回大会, Jun. 2016.
27.	Huong Thi Thanh Trinh, Yuji Shishido, Diem Hong Tran, Hirofumi Sogabe, Soo Hyeon Kim and Kiyoshi Fukui : Regulation of gene expression of mouse D-amino acid oxidase, 第57回日本生化学会中国四国支部例会, May 2016.
28.	Hirofumi Sogabe, Takanaga Ako, Yuji Shishido, Diem Hong Tran, Huong Thi Thanh Trinh, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : 低栄養ストレスによる D-アミノ酸酸化酵素タンパク質の動的変化, 第57回日本生化学会中国四国支部例会, May 2016.
29.	Shohei Toguchi, Tomoyasu Hirose, Kazuko YORITA, Kiyoshi Fukui, Barry K Sharpless, Satoshi Ōmura and Toshiaki Sunazuka : In situ click chemistryを利用したD-アミノ酸酸化酵素阻害剤の探索研究, 日本薬学会第136年会, Mar. 2016.
30.	渋谷典広, 小池伸, 田中真紀子, 湯浅磨里, 木村由佳, 小笠原裕樹, Kiyoshi Fukui, 永原則之 and 木村英雄 : 生理活性物質硫化水素の産生経路, 第38回日本分子生物学会年会,第88回日本生化学会大会合同大会, Dec. 2015.
31.	Yuji Shishido, Diem Hong Tran, Soo Hyeon Kim, Huong Thi Thanh Trinh, Hirofumi Sogabe, Takanaga Ako, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : ヒト細胞におけるD-アミノ酸酸化酵素遺伝子の発現調節機構, 第38回日本分子生物学会年会,第88回日本生化学会大会合同大会, Dec. 2015.
32.	Kiyoshi Fukui, Diem Hong Tran, Yuji Shishido, Huong Thi Thanh Trinh, Tuan Anh Pham, Hirofumi Sogabe, Soo Hyeon Kim, Takanaga Ako, Kazuko YORITA and Yusuke Kato : アミノ酸代謝のキラルサイエンスと統合失調症病態システム酵素学, 第38回日本分子生物学会年会,第88回日本生化学会大会合同大会, Dec. 2015.
33.	Yusuke Kato and Kiyoshi Fukui : D-アミノ酸酸化酵素調節因子 G72 のドメインモデリング, 第24回日本バイオイメージング学会学術集会, Sep. 2015.
34.	Yuji Shishido, Diem Hong Tran, Huong Thi Thanh Trinh, Soo Hyoen Kim, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : 哺乳動物における D-アミノ酸酸化酵素遺伝子の発現誘導機構の解析, 第 11 回 D-アミノ酸学会学術講演会, Aug. 2015.
35.	Diem Hong Tran, Yuji Shishido, Seongpil Chung, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : ヒトD-アミノ酸酸化酵素遺伝子の発現調節機構:2つのプロモーター領域の同定とその調節, 日本ビタミン学会第67回大会, Jun. 2015.
36.	Kazuko YORITA, Sumire Kurosawa, Yuji Shishido, Shigeki Sano, Yoshiki Kashiwada, Noriaki Minakawa and Kiyoshi Fukui : ヒト由来D-アミノ酸酸化酵素のエフェクター探索のためのハイスループットクリーニングと構造機能相関, 第56回日本生化学会中国四国支部例会, May 2015.
37.	Hirofumi Sogabe, Takanaga Ako, Yuji Shishido, Diem Hong Tran, Huong Thi Thanh Trinh, Kazuko YORITA, Yusuke Kato and Kiyoshi Fukui : 腎臓近位尿細管様細胞におけるD-アミノ酸酸化酵素の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.
38.	渋谷典広, 小池伸, 田中真紀子, 湯浅磨里, 木村由佳, 小笠原裕樹, Kiyoshi Fukui, 永原則之 and 木村英雄 : D-システインからの生理活性物質硫化水素の生産, The 87th Annual Meeting of the Japanese Biochemical Society, Oct. 2014.
39.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : Nucling an apoptosis-associated novel protein, controls the postlactational involution of mammary gland through regulation of NF-B and STAT3, The 87th Annual Meeting of the Japanese Biochemical Society, Oct. 2014.
40.	Yuji Shishido, Kana Morimoto, Diem Hong Tran, Huong Thi Thanh Trinh, Hirofumi Sogabe, Takanaga Ako, Kazuko YORITA and Kiyoshi Fukui : 哺乳動物の中枢神経系におけるDーアミノ酸酸化酵素遺伝子発現誘導機構, The 87th Annual Meeting of the Japanese Biochemical Society, Oct. 2014.
41.	Bukasa Kalubi, Omar Maningo Rodis, Masashi Akaike and Kiyoshi Fukui : Communication Know-how course: A practical approach to improving professional communication skills in graduate and post-graduate education, 17th JASMEE Academic Meeting, Jul. 2014.
42.	Diem Hong Tran, Yuji Shishido, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Induction and regulation of gene expression of D-amino acid oxidase in glial and kidney cells, 日本ビタミン学会第66回大会, Jun. 2014.
43.	Takashi Sakai, Yukiya Sako, Yuki Honjo, Kota Nakajima, Huy Van Dang, Tuan Anh Pham, Yuji Shishido, Kazuko YORITA and Kiyoshi Fukui : 新規アポトーシス誘導因子ヌクリングのホモシステイン代謝系及び神経精神疾患への関与の検討, 日本ビタミン学会第66回大会, Jun. 2014.
44.	Kana Morimoto, Yuji Shishido, Diem Hong Tran, Huong Thi Thanh Trinh, Hirofumi Sogabe, Kazuko YORITA and Kiyoshi Fukui : 中枢神経系におけるD-アミノ酸酸化酵素遺伝子の発現誘導機構の解析, 第55回日生化学会中国四国支部例会, Jun. 2014.
45.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : Loss of Nucling promotes delayed mammary gland involution through suppression of NF-B and STAT3, 第55回日生化学会中国四国支部例会, Jun. 2014.
46.	宍倉美穂, 柏熊快之, 秤屋瞳, 岩佐澄子, 一場秀章, 吉尾隆, Kazuko YORITA, Kiyoshi Fukui and 福島健 : 統合失調症治療薬のヒトDAO活性阻害作用の評価:in vitro実験による検討, 日本薬学会第134年会, Mar. 2014.
47.	Kiyoshi Fukui : ビタミン B 群が担う脳内 D-アミノ酸代謝システムの疾患酵素学研究, ビタミンB研究委員会平成25年度シンポジウム, Jan. 2014.
48.	Takashi Sakai, Yukiya Sako, Huy Van Dang, Tuan Anh Pham and Kiyoshi Fukui : Nonalcoholic fatty liver disease (NAFLD) and altered insulin expression in mice lacking Nucling, The 86th Annual Meeting of the Japanese Biochemical Society, Sep. 2013.
49.	Yuji Shishido, Kana Morimoto, Diem Hong Tran, Huong Thi Thanh Trinh, Hirofumi Sogabe, Kazuko YORITA and Kiyoshi Fukui : Analysis of the regulatory mechanism of mammalian D-amino acid oxidase gene expression, The 86th Annual Meeting of the Japanese Biochemical Society, Sep. 2013.
50.	Huy Van Dang, Takashi Sakai, Tuan Anh Pham, Diem Hong Tran, Kazuko YORITA, Yuji Shishido and Kiyoshi Fukui : Delayed mammary gland involution in Nucling-KO mice, The 86th Annual Meeting of the Japanese Biochemical Society, Sep. 2013.
51.	Diem Hong Tran, Yuji Shishido, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Induction and regulation of gene expression of D-amino acid oxidase in LLC-PK1 cells, The 86th Annual Meeting of the Japanese Biochemical Society, Sep. 2013.
52.	Diem Hong Tran, Yuji Shishido, Huong Thi Thanh Trinh, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Induction and regulation of gene expression of D-amino acid oxidase in LLC-PK1 cells, 第9回 D-アミノ酸研究会学術講演会, Sep. 2013.
53.	Diem Hong Tran, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Induction and regulation of gene expression of in LLC-PK1 cells, 第54回日本生化学会中国四国支部例会, Jun. 2013.
54.	Kiyoshi Fukui : D-アミノ酸代謝システムをターゲットとした疾患酵素学研究, 第65回日本ビタミン学会大会, May 2013.
55.	Kaori Kiso, 上野聡子, 福田麻菜, 市育代, 小林慧子, Takashi Sakai, Kiyoshi Fukui and 小城勝相 : 四塩化炭素中毒におけるKupffer細胞による肝炎拡大機構, The 85th Annual Meeting of the Japanese Biochemical Society, Dec. 2012.
56.	Shibuya Norihiro, Mari Ishigami, Makiko Tanaka, Yuka Kimura, Yuki Ogasawara, Kiyoshi Fukui and Hideo Kimura : Another pathway to produce H2S in the brain, The 85th Annual Meeting of the Japanese Biochemical Society, Dec. 2012.
57.	Sun Mi Kim, Takashi Sakai, HoangNam Tran, Sako Yukiya, Huy Van Dang and Kiyoshi Fukui : Nucling, a novel protein associated with NF-kappaB, Regulates endotoxin-induced apoptosis in vivo, The 85th Annual Meeting of the Japanese Biochemical Society, Dec. 2012.
58.	Diem Hong Tran, Yuji Shishido, Seongpil Chung, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Induction and regulation of gene expression of D-amino acid oxidase in LLC-PK1 cells, The 85th Annual Meeting of the Japanese Biochemical Society, Dec. 2012.
59.	Yuji Shishido, Diem Hong Tran, Kana Morimoto, Seongpil Chung, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Regulation of gene expression of D-amino acid oxidase in glial cells, The 85th Annual Meeting of the Japanese Biochemical Society, Dec. 2012.
60.	Takashi Sakai, Yukiya Sako, Seongpil Chung, Sun Mi Kim, Huy Van Dang, Rieko Nakata and Kiyoshi Fukui : 新規NF-κB制御分子ヌクリングは非アルコール性脂肪肝及び糖尿病発症抑制に重要である, 第16回日本心血管内分泌代謝学会学術総会, Nov. 2012.
61.	Kiyoshi Fukui : 統合失調症の疾患酵素学:D-アミノ酸酸化酵素の活性制御による新規治療戦略, 第64回シグナル伝達医学グローバルCOE学術講演会, Aug. 2012.
62.	Yukiya Sako, Seongpil Chung, Sun Mi Kim, Huy Van Dang, Nakata Rieko, Takashi Sakai and Kiyoshi Fukui : ホモシステイン代謝系における新規NF-κB制御因子ヌクリングの関与, 日本ビタミン学会第64回大会, Jun. 2012.
63.	Kiyoshi Fukui, Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Diem Hong Tran and Takashi Sakai : Oxidative stress-energy depletion therapy as a new treatment modality for cancer, 日本ビタミン学会第64回大会, Jun. 2012.
64.	Seongpil Chung, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : D-アミノ酸酸化酵素関連遺伝子の発現に関するマイクロアレイ並びにプロテオミクス解析, 日本ビタミン学会第64回大会, Jun. 2012.
65.	Seongpil Chung, Diem Hong Tran, Kazuko YORITA, Yuji Shishido, Takashi Sakai and Kiyoshi Fukui : アストログリア細胞におけるD-セリン代謝産物ヒドロキシピルビン酸の細胞死誘導活性, 第53回日本生化学会中国・四国支部例会, May 2012.
66.	Mi Sun Kim, Takashi Sakai, Huy Van Dang, Yukiya Sako and Kiyoshi Fukui : 新規 NF-kB 制御分子ヌクリングの炎症性病態への関与についての検討, 第53回日本生化学会中国・四国支部例会・シンポジウム, May 2012.
67.	Norihiro Shibuya, Mari Ishigami, Mariko Tanaka, Yuka Kimura, Yuki Ogasawara, Kiyoshi Fukui and Hideo Kimura : Another Pathway to produce hydrogen sulfide in the brain, 第85回日本薬理学会年会, Mar. 2012.
68.	Kiyoshi Fukui : D-アミノ酸代謝酵素システムの活性制御による新規精神神経疾患治療薬の開発戦略, 第3回共同利用・共同研究「酵素学研究拠点」シンポジウム, Oct. 2011.
69.	Kiyoshi Fukui, rabab Mohamed Abou El-Magd, Seongpil Chung, Salah Mohamed El-Sayed, Diem Hong Tran, Kumiko Shinohara, Yuji Shishido, Kazuko YORITA and Takashi Sakai : D-アミノ酸代謝システムの活性制御による新規精神神経疾患治療戦略, The 84th Annual Meeting of the Japanese Biochemical Society, Sep. 2011.
70.	Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Kazuko YORITA, Takashi Sakai, Hiroyoshi Watanabe, Shoji Kagami and Kiyoshi Fukui : Combination of oxidative stress and energy depletion induced significant glioma cell death, The 84th Annual Meeting of the Japanese Biochemical Society, Sep. 2011.
71.	Yuji Shishido, Ying Song, Kumiko Shinohara, Diem Hong Tran, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : ヒトD-アミノ酸酸化酵素のグリア細胞内における機能解析, The 84th Annual Meeting of the Japanese Biochemical Society, Sep. 2011.
72.	Takashi Sakai, Sun Mi Kim, HoangNam Tran and Kiyoshi Fukui : 新規アポトーシス/NF-κB制御分子ヌクリングの機能解析, The 84th Annual Meeting of the Japanese Biochemical Society, Sep. 2011.
73.	Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Takashi Sakai, Hiroyoshi Watanabe, Shoji Kagami and Kiyoshi Fukui : D-アミノ酸酸化酵素の遺伝子導入により，グリオーマ細胞では，3-ブロモピルビン酸の解糖系への阻害作用が増強される, 第7回 D-アミノ酸研究会学術講演会, Sep. 2011.
74.	Seongpil Chung, Ying Song, Hwan Ki Park, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : アストログリア細胞内の D-アミノ酸酸化酵素により D-セリンから産生されるヒドロキシピルビン酸の細胞死誘導活性, 第7回 D-アミノ酸研究会学術講演会, Sep. 2011.
75.	Yuji Shishido, Ying Song, Kumiko Shinohara, Rabab Mohamed Abou El-Magd, Diem Hong Tran, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : グリア細胞における D‒アミノ酸酸化酵素の機能解析, 第7回 D-アミノ酸研究会学術講演会, Sep. 2011.
76.	Kiyoshi Fukui, Tomoya Kawazoe, Sanae Iwana, Rabab Mohamed Abou El-Magd, Koji Ono, Seongpil Chung, Salah Mohamed EL-Sayed, Kumiko Shinohara, Yuji Shishido, Kazuko YORITA and Takashi Sakai : D-アミノ酸酸化酵素の活性制御による新規精神神経疾患治療戦略, 第7回 D-アミノ酸研究会学術講演会, Sep. 2011.
77.	Salah Mohamed El-Sayed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Kazuko YORITA, Takashi Sakai, Hiroyoshi Watanabe, Shoji Kagami and Kiyoshi Fukui : D-amino acid oxidase gene therapy sensitizes glioma cells to the anti-glycolytic effect of 3-bromopyruvate, 第52回日本生化学会中国・四国支部例会・シンポジウム, May 2011.
78.	Mi Sun Kim, Takashi Sakai, Yukiya Sako and Kiyoshi Fukui : 新規 NF-kB 制御分子ヌクリングの免疫系における役割の検討, 第52回日本生化学会中国・四国支部例会・シンポジウム, May 2011.
79.	Salah El-Sayed Mohamed, Rabab Mohamed Abou El-Magd, Yuji Shishido, Seongpil Chung, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : DAO gene therapy sensitizes glioma cell selectively to anti-glycolytic effect of 3-bromopyruvate, 日本農芸化学会中四国支部第29回講演会日本ビタミン学会中国・四国地区第1回講演会合同講演会, Jan. 2011.
80.	Seongpil Chung, Ying Song, Ki Hwan Park, Kazuko YORITA, Yuji Shishido, Takashi Sakai and Kiyoshi Fukui : D-セリン代謝産物ヒドロキシピルビン酸の細胞死誘導活性, 日本農芸化学会中四国支部第29回講演会日本ビタミン学会中国・四国地区第1回講演会合同講演会, Jan. 2011.
81.	Kiyoshi Fukui : D-アミノ酸酸化酵素をターゲットとした疾患酵素学研究とその方法論, 第1回酵素学講習会(酵素学ウインタースクール), Jan. 2011.
82.	Seongpil Chung, Kimiko Sogabe, Hwan Ki Park, Ying Song, Koji Ono, Rabab Mohamed Abou El-Magd, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Potential cytotoxic effect of hydroxypyruvate produced from D-serine by astroglial D-amino acid oxidase, 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.
83.	HoangNam Tran, Takashi Sakai, Sun Mi Kim and Kiyoshi Fukui : Intracellular metabolism of Nucling, a novel apoptosis regulator, 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.
84.	Sun Mi Kim, Takashi Sakai, HoangNam Tran and Kiyoshi Fukui : Physiological Function of a novel NF-B-regulating molecule, NUCLING, in Immune system, 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.
85.	Salah El-Sayed M., Rabab Abou El-Magd Mohamed, Yuji Shishido, Seongpil Chung, Kazuko YORITA, Takashi Sakai, Hiroyoshi Watanabe, Shoji Kagami and Kiyoshi Fukui : D-amino acid oxidase gene therapy sensitizes glioma cells selectively to the anti-glycolytic effect of 3-bromopyruvate, 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.
86.	Yukiya Sako, Seongpil Chung, Takashi Sakai and Kiyoshi Fukui : 新規アポトーシス誘導因子Nuclingのホモシステイン代謝系における関与, 日本ビタミン学会第62回大会, Jun. 2010.
87.	Koji Ono, Yuji Shishido, Hwan Ki Park, Rabab Mohamed Abou El-Magd, Seongpil Chung, Kazuko YORITA, Nobuya Sano, Arima Kunimasa, Takashi Sakai, Kazunori Ishimura and Kiyoshi Fukui : 脈絡叢におけるD-アミノ酸酸化酵素発現の病態生理学的役割:ヒトおよびラット脳におけるRNA並びにタンパク質レベルでの解析, 日本ビタミン学会第62回大会, Jun. 2010.
88.	Seongpil Chung, Ying Song, Hwan Ki Park, Sogabe Kimiko, Koji Ono, Mohamed Abou El-Magd Rabab, Kazuko YORITA, Yuji Shishido, Takashi Sakai and Kiyoshi Fukui : アストログリア細胞内のD-セリン代謝システムにおけるD-アミノ酸酸化酵素の役割及び代謝産物の細胞死誘導活性, 日本ビタミン学会第62回大会, Jun. 2010.
89.	Ying Song, Seongpil Chung, Rabab Mohamed Abou El-Magd, Kazuko YORITA, Yuji Shishido, Takashi Sakai and Kiyoshi Fukui : D-セリン代謝システムにおける D-アミノ酸酸化酵素の役割及び代謝産物の細胞毒性, 第51回日本生化学会中国四国支部例会, May 2010.
90.	HoangNam Tran, Takashi Sakai, Sun Mi Kim and Kiyoshi Fukui : The novel apoptosis regulator, Nucling, is regulated by NF-B, proteasome and caspase, 第51回日本生化学会中国四国支部例会, May 2010.
91.	Takashi Sakai, HoangNam Tran, Li Liu, Rika Sakai, Sun Mi Kim, Ryuji Kaji and Kiyoshi Fukui : Nucling, a novel apoptosis-regulatory molecule, regulates NF-kappa B signal, The 82nd annual meeting of the Japanese Biochemical Society, Oct. 2009.
92.	HoangNam Tran, Takashi Sakai, Kim Sun Mi and Kiyoshi Fukui : Nucling expression is regulated by NF-kappa B signaling, The 82nd annual meeting of the Japanese Biochemical Society, Oct. 2009.
93.	Kazuko YORITA and Kiyoshi Fukui : Stability of TIM barrel enzyme L-Lactate oxidase from Aerococcus viridans, The 82nd annual meeting of the Japanese Biochemical Society, Oct. 2009.
94.	Koji Ono, Yuji Shishido, Hwan Ki Park, Rabab Mohamed Abou EL-Magd, Seongpil Chung, Kazuko YORITA, Nobuya Sano, Arima Kunimasa, Takashi Sakai and Kiyoshi Fukui : Potential pathophysiological role of D-amino acid oxidase in schizophrenia: immunohistochemical and in situ hybridization studies on the expression in human and rat brain, The 82nd annual meeting of the Japanese Biochemical Society, Oct. 2009.
95.	Kiyoshi Fukui, Sanae Iwana, Rabab Mohamed abou El-Magd, Tomoya Kawazoe, Koji Ono, Seongpil Chung, Yuji Shishido, Kazuko YORITA and Takashi Sakai : Modulation of D-amino acid oxidase: novel mechanism for the action of anti-schizophrenic drugs, The 82nd annual meeting of the Japanese Biochemical Society, Oct. 2009.
96.	Kiyoshi Fukui : D-アミノ酸とその代謝酵素による脳機能制御に関する疾患酵素学研究, 日本アミノ酸学会第3回学術大会, Sep. 2009.
97.	Koji Ono, Yuji Shishido, Park Ki Hwan, El-Magd Mohamed Abou Rabab, Seongpil Chung, Kazuko YORITA, Nobuya Sano, Arima Kunimasa, Takashi Sakai, Kazunori Ishimura and Kiyoshi Fukui : 免疫組織化学と in situ hybridization 法を用いたヒトおよびラット脳における D-アミノ酸酸化酵素の発現解析, 第50回日本組織細胞化学会総会・学術集会, Sep. 2009.
98.	Koji Ono, Yuji Shishido, 朴煥埼, Rabab Mohamed Abou El-Magd, Seongpil Chung, Kazuko YORITA, Nobuya Sano, 有馬邦正, Takashi Sakai, Kazunori Ishimura and Kiyoshi Fukui : 免疫組織化学とin situ hybridization法を用いたヒトおよびラット脳におけるD- アミノ酸酸化酵素の発現解析, 第50回日本組織細胞化学会総会・学術集会, Sep. 2009.
99.	Seongpil Chung, Hwan Ki Park, Koji Ono, Rabab Mohamed Abou El-Magd, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Genomic and proteomic analysis of rat glioma cells overexpressing D-amino acid oxidase and stimulated with D-serine, 日本ビタミン学会第61回大会, May 2009.
100.	Rabab Mohamed Abou El-Magd, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Seongpil Chung, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : The Effect of Risperidone on D-Amino Acid Oxidase Activity as a Hypothesis for a Novel Mechanism of Action in the Treatment of Schizophrenia, 日本ビタミン学会第61回大会, May 2009.
101.	Yuji Shishido, Seongpil Chung, Hwan Ki Park, Takashi Sakai and Kiyoshi Fukui : D-アミノ酸酸化酵素のグリア細胞特異的発現, 50回日本生化学会中国四国支部例会, May 2009.
102.	Takashi Sakai, Hoang Nam Tran, Li Liu, Rika -Mukai Sakai, Sun Mi Kim, Ryuji Kaji and Kiyoshi Fukui : 炎症性肝疾患におけるヌクリング-NF-κB経路の働き, 50回日本生化学会中国四国支部例会, May 2009.
103.	Koji Ono, Hwan Ki Park, Rabab Mohamed Abou El-Magd, Seongpil Chung, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : 脳内におけるD-アミノ酸酸化酵素遺伝子の発現:ヒトおよびラット脳におけるRNA並びにタンパク質レベルでの解析, 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.
104.	Seongpil Chung, Hwan Ki Park, Koji Ono, Rabab M. Abou El-Magd, Yuji Shishido, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Proteomic and genomic analyses of rat glioma cells overexpressing D-amino acid oxidase, 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.
105.	Rabab M. Abou El-Magd, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Seongpil Chung, Kazuko YORITA and Kiyoshi Fukui : The Effect of Risperidone on D-Amino Acid Oxidase Activity as a Hypothesis for Treatment of Schizophrenia, 第4回D-アミノ酸研究会学術講演会, Sep. 2008.
106.	Seongpil Chung, Hwan Ki Park, Koji Ono, Rabab Mohamed Abou El-Magd, Kazuko YORITA, Yuji Shishido, Takashi Sakai and Kiyoshi Fukui : 脳内D-セリン代謝システムにおけるD-アミノ酸酸化酵素の役割及び代謝産物の細胞死誘導活性, 第4回D-アミノ酸研究会学術講演会, Sep. 2008.
107.	Kiyoshi Fukui : D-アミノ酸代謝酵素システムの機能と構造に関する疾患酵素学的研究, 日本ビタミン学会第60回大会, Jun. 2008.
108.	Hwan Ki Park, Seongpil Chung, Rabab Abou El-Magd, Koji Ono, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : 脳内D-セリン代謝システムにおけるD-アミノ酸酸化酵素役割及び代謝産物の細胞毒性, 日本ビタミン学会第60回大会, Jun. 2008.
109.	Hoang Nam Tran, Takashi Sakai, Salah M. El-Sayed, Li Liu, Rika Sakai, Naozumi Ishimaru, Yoshio Hayashi, Ryuji Kaji and Kiyoshi Fukui : 新規アポトーシス制御分子ヌクリングはNF-κB の制御に関与する, 第49回日本生化学会中国四国支部例会, May 2008.
110.	Rabab Mohamed Abou El-Magd, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Koji Ono, Seongpil Chung, Kazuko YORITA and Kiyoshi Fukui : The Effect of Risperidone on D-Amino Acid Oxidase Activity as a Hypothesis for Treatment of Schizophrenia, 第49回日本生化学会中国四国支部例会, May 2008.
111.	Takashi Sakai, HoangNam Tran, Li Liu, Xichuan Teng, Naozumi Ishimaru, Rika Sakai, Nobuya Sano, Ryuji Kaji, Yoshio Hayashi and Kiyoshi Fukui : Nucling is essential for the maintenance of Kupffer cells related to tumorgenesis in liver, The 30th Annual Meetings of the Molecular Biology Society of Japan/The 80th Annual Meeting of the Japanese Biochemical Society, Dec. 2007.
112.	Tomoya Kawazoe, Hideaki Tsuge and Kiyoshi Fukui : ヒトD-アミノ酸酸化酵素の結晶構造解析, The 30th Annual Meetings of the Molecular Biology Society of Japan/The 80th Annual Meeting of the Japanese Biochemical Society, Dec. 2007.
113.	Seongpil Chung, Hwan Ki Park, Koji Ono, Tomoya Kawazoe, Sanae Iwana, Rabab Mohamed Abou El-Magd, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Proteomics analysis of the rat C6 glioma cells: comparison with DAO-overexpressing cells, The 30th Annual Meetings of the Molecular Biology Society of Japan/The 80th Annual Meeting of the Japanese Biochemical Society, Dec. 2007.
114.	Koji Ono, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Seongpil Chung, Rabab Mohamed Abou El-Magd, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Gene expression of D-amino acid oxidase in rat brain, The 30th Annual Meetings of the Molecular Biology Society of Japan/The 80th Annual Meeting of the Japanese Biochemical Society, Dec. 2007.
115.	Seongpil Chung, Hwan Ki Park, Koji Ono, Tomoya Kawazoe, Sanae Iwana, Rabab Mohamed Abou El-Magd, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : D-アミノ酸酸化酵素を過剰発現させたラットC6グリオーマ細胞株のプロテオミクス解析, 第3回D-アミノ酸研究会学術講演会, Sep. 2007.
116.	Koji Ono, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Seongpil Chung, Rabab Mohamed Abou El-Magd, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : ラット脳内におけるD-アミノ酸酸化酵素の遺伝子発現解析, 第3回D-アミノ酸研究会学術講演会, Sep. 2007.
117.	Kazuko YORITA, Yasufumi Umena, Yukio Morimoto and Kiyoshi Fukui : X線結晶構造解析に基づいたL-乳酸酸化酵素の基質結合様式, 日本ビタミン学会第59回大会, May 2007.
118.	Sanae Iwana, Tomoya Kawazoe, Hwan Ki Park, Koji Ono, Seongpil Chung, Rabab Mohamed Abou El-Magd, Kazuko YORITA and Kiyoshi Fukui : 向精神薬クロルプロマジンの光反応産物によるD-アミノ酸酸化酵素の活性阻害, 日本ビタミン学会第59回大会, May 2007.
119.	Takashi Sakai, Li Liu, Xichuan Teng, Naozumi Ishimaru, Rika Sakai, Nobuya Sano, Ryuji Kaji, Hoang Nam Tran, Yoshio Hayashi and Kiyoshi Fukui : 新規アポトーシス制御分子ヌクリングの肝癌発症機構における役割の解明, 第48回日本生化学会中国四国支部例会, May 2007.
120.	Kiyoshi Fukui : D-アミノ酸とその代謝酵素による中枢神経制御システム, 第3回公開シンポジウム多因子疾患克服に向けた分子的戦略, Nov. 2006.
121.	Tomoya Kawazoe, Hideaki Tsuge and Kiyoshi Fukui : ヒトD-アミノ酸酸化酵素のX線結晶構造解析および活性化機構への仮説, 第2回D-アミノ酸研究会学術講演会, Sep. 2006.
122.	Kazuko YORITA, Yasufumi Umena, Takeshi Matsuoka, Akiko Kita, Yukio Morimoto and Kiyoshi Fukui : 結晶X線回折法によるL-乳酸酸化酵素の活性中心の構造, 日本ビタミン学会第58回大会, May 2006.
123.	Tomoya Kawazoe, Sanae Iwana, Koji Ono, Hwan Ki Park, Kazuko YORITA, Hideaki Tsuge and Kiyoshi Fukui : ヒトD-アミノ酸酸化酵素の構造および活性化機構への仮説モデル, 日本ビタミン学会第58回大会, May 2006.
124.	Sanae Iwana, Kazuko YORITA, Tomoya Kawazoe, Koji Ono, Seongpil Chung, Rabab Mohamed Abou El-Magd, Hwan Ki Park and Kiyoshi Fukui : 向精神薬クロルプロマジンとその光反応産物によるD-アミノ酸酸化酵素の活性阻害, 日本ビタミン学会第58回大会, May 2006.
125.	Koji Ono, Hwan Ki Park, Tomoya Kawazoe, Sanae Iwana, Seongpil Chung, Rabab Abou EL-Magd, Yumiko Tomita, Kazuko YORITA and Kiyoshi Fukui : 脳内におけるD-アミノ酸酸化酵素の遺伝子発現, 第47回日本生化学会中四国支部例会, May 2006.
126.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Akiko Kita, Kiyoshi Fukui, Tomitake Tsukihara and Yukio Morimoto : The crystal structure of L-lactate oxidase H265Q mutant, 第6回日本蛋白質科学会年会, Apr. 2006.
127.	Li Liu, Takashi Sakai, Xichuan Teng, Rika Sakai, Ryuji Kaji and Kiyoshi Fukui : Nucling mediates NF-B nuclear translocation and activation through interaction with NF-B-p50, 28th Annual meeting of the molecular biology society of Japan, Dec. 2005.
128.	Takashi Sakai, Xichuan Teng, Li Liu, Rika Sakai, Ryuji Kaji and Kiyoshi Fukui : 新規Apoptosome制御因子Nuclingに関するノックアウトマウスを用いた機能解析, Nucling mediates NF-B nuclear translocation and activation through interaction with NF-B-p50, Dec. 2005.
129.	Takashi Sakai, Xichuan Teng, Li Liu, Rika Sakai, Nobuya Sano, Ryuji Kaji and Kiyoshi Fukui : Nucling controls NF-B-associated tumorgenesis by regulating inflammation and apoptosis, The 78th Annual Meeting of the Japanese Biochemical Society, Oct. 2005.
130.	Xichuan Teng, Takashi Sakai, Li Liu, Rika Sakai, Ryuji Kaji and Kiyoshi Fukui : Nucling mediates the induction of apoptosome and the expression of cyclooxygenase 2 in a mouse model of Parkinson's, The 78th Annual Meeting of the Japanese Biochemical Society, Oct. 2005.
131.	Tomoya Kawazoe, Sanae Iwana, Koji Ono, Hwan Ki Park, Kazuko YORITA, Hideaki Tsuge and Kiyoshi Fukui : Crystal structure of human D-amino acid oxidase in complex with benzoate, The 78th Annual Meeting of the Japanese Biochemical Society, Oct. 2005.
132.	Hwan Ki Park, Tomoya Kawazoe, Koji Ono, Sanae Iwana, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : Potential role for astroglial D-amino acid oxidase in extracellular D-serine metabolism and cytotoxicity, The 78th Annual Meeting of the Japanese Biochemical Society, Oct. 2005.
133.	Kazuko YORITA, Yasufumi Umena, Takeshi Matsuoka, Makoto Abe, Akiko Kida, Kiyoshi Fukui and Yukio Morimoto : Crystal structure of the wild type, R181M, and R268M L-lactate oxidase from Aerococcus viridans, The 78th Annual Meeting of the Japanese Biochemical Society, Oct. 2005.
134.	Kiyoshi Fukui : 生命世界の左右非対称性, 日本理科教育学会第55回全国大会, Aug. 2005.
135.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui, Miki Kunio and Yukio Morimoto : Aerococcus viridans由来L-乳酸酸化酵素(LOX)のArg-181変異体と野生体のX線結晶構造解析, 第5回日本蛋白質科学会年会, Jul. 2005.
136.	Sanae Iwana, Kazuko YORITA, Tomoya Kawazoe, Koji Ono, Hwan Ki Park, Yumiko Tomita and Kiyoshi Fukui : 向精神薬クロルプロマジンによるD-アミノ酸酸化酵素の活性阻害, 日本ビタミン学会第57回大会, May 2005.
137.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui and Yukio Morimoto : 放射光による乳酸酸化酵素4量体の結晶構造解析, 第18回日本放射光学会年会・放射光科学合同シンポジウム, Jan. 2005.
138.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui and Yukio Morimoto : 乳酸酸化酵素変異体のX線結晶構造解析, 日本生物物理学会第42回年会, Dec. 2004.
139.	Yasufumi Umena, Kazuko YORITA, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui and Yukio Morimoto : 乳酸酸化酵素4量体の結晶構造解析, 第16回日本結晶学会年会, Nov. 2004.
140.	Takashi Sakai, Li Liu, Rika Sakai, Ryuji Kaji, Tasuku Mitani, Mitsuru Matsumoto, Kazunori Toida, Yuji Shishido and Kiyoshi Fukui : Nucling is important for the upregulation of Apaf-1/procaspase-9cytochrome c apoptosome following cellular stress in vivo, The 77th Annual Meeting of the Japanese Biochemical Society, Oct. 2004.
141.	Li Liu, Takashi Sakai, Nobuya Sano, Xichuan Teng and Kiyoshi Fukui : Nuclig Mediates apoptosis by inhibiting expression of galectin-3 through interfence with NF-B signaling, The 77th Annual Meeting of the Japanese Biochemical Society, Oct. 2004.
142.	Xichuan Teng, Takashi Sakai, Li Liu, Rika Sakai, Ryuji Kaji and Kiyoshi Fukui : Attenuation of MPTP-induced neurotoxicity and motor dysfunction in Nucling deficient mice, The 77th Annual Meeting of the Japanese Biochemical Society, Oct. 2004.
143.	Takashi Sakai, Li Liu, Yuji Shishido, Ryuji Kaji and Kiyoshi Fukui : Identification of a Novel, Embryonal Carcinoma Cell-Associated Molecule, Nucling, That is Up-regulated during Cardiac Muscle Differentiation, The 77th Annual Meeting of the Japanese Biochemical Society, Oct. 2004.
144.	Tomoya Kawazoe, Kazuko YORITA, Koji Ono, Sanae Iwana, Hwan Ki Park, Yumiko Tomita and Kiyoshi Fukui : Purification and Characterization of recombinant human D-amino acid oxidase, The 77th Annual Meeting of the Japanese Biochemical Society, Oct. 2004.
145.	Kiyoshi Fukui : 脳におけるD-アミノ酸酸化酵素の機能的・病態生理学的意義, 第27回日本神経科学大会・第47回日本神経化学会大会合同大会, Sep. 2004.
146.	Kiyoshi Fukui : 脳におけるD-セリンとその代謝酵素の生理機能と神経疾患における意義, 日本ビタミン学会第56回大会, May 2004.
147.	Tomoya Kawazoe, Kazuko YORITA, Koji Ono, Park Hwan Ki, Yumiko Tomita and Kiyoshi Fukui : ヒト組換え型D-アミノ酸酸化酵素の大腸菌からの精製と酵素化学的解析, 日本ビタミン学会第56回大会, May 2004.
148.	Kazuko YORITA, Misaki Hideo, Vincent Massey and Kiyoshi Fukui : 8-Formyl-flavinで活性中心を標識したフラビン酵素のスペクトル特性, 第45回日本生化学会中国・四国支部例会徳島, May 2004.

Et cetera, Workshop:

1.	SooHyeon Kim, Yuji Shishido, Hirofumi Sogabe, Wanitcha Rachadech, Yusuke Kato and Kiyoshi Fukui : 生体内各組織におけるD-アミノ酸酸化酵素活性の検出とその生理的意義の考察, 第454回研究協議会, Oct. 2018.
2.	Yusuke Kato, 伊藤吹夕, 髙橋和浩, 菅又龍一, 鈴木章一, 山本友子, 河内正治, Kiyoshi Fukui, 三牧正和 and Kazuo Suzuki : 薬物耐性B型インフルエンザのin silico 機構解析, 第24回MPO研究会, 札幌, Sep. 2018.
3.	Kiyoshi Fukui : 阻害剤開発を目指したD-アミノ酸坂酵素阻害作用分子の解析, 第450回ビタミンB研究協議会, Oct. 2017.
4.	Kiyoshi Fukui, Yuji Shishido, Diem Hong Tran, Huong Thi Thanh Trinh, Soo Hyeon Kim, Hirofumi Sogabe, Kazuko YORITA and Yusuke Kato : D-アミノ酸酸化酵素遺伝子の発現調節機構の解析による統合失調症胎児期起源仮説の考察, 第444回ビタミンB研究協議会, Jun. 2016.
5.	Shohei Toguchi, Tomoyasu Hirose, Kazuko YORITA, Kiyoshi Fukui, Satoshi Ōmura and Toshiaki Sunazuka : In Situ Click Chemistryを利用したD-アミノ酸酸化酵素阻害剤の探索研究, AKPS集会第9回北里化学シンポジウム, Sep. 2015.
6.	Yuji Shishido, Diem Hong Tran, Kana Morimoto, Huong Thi Thanh Trinh, Hirofumi Sogabe, Kazuko YORITA, Takashi Sakai and Kiyoshi Fukui : 遺伝子発現調節から探るグリア・ニューロン連関の病態システム酵素学, 第433回ビタミンB研究協議会, Aug. 2013.
7.	Kiyoshi Fukui : 酸化ストレス誘導系と解糖系を分子標的としたD-アミノ酸酸化酵素遺伝子によるグリオーマ治療法, 第427回ビタミンB研究協議会, Feb. 2012.
8.	Kiyoshi Fukui : D-アミノ酸代謝システムの活性制御による新規精神神経疾患治療薬の開発戦略, 日本応用酵素協会第37回研究発表会, Nov. 2011.
9.	Kiyoshi Fukui : D―アミノ酸酸化酵素を用いたグリオーマの遺伝子治療戦略, 第426回ビタミンB研究協議会, Nov. 2011.
10.	Kiyoshi Fukui : D-AMINO ACID OXIDASE : PATHOPHYSIOLOGICAL BASIS AND MOLECULAR TARGET FOR SCHIZOPHRENIA, 26th KITASATO MICROBIAL CHEMISTRY (KMC) FRONTIER SEMINAR, Jul. 2011.
11.	Kiyoshi Fukui : D-アミノ酸代謝の病態システム酵素学:D-アミノ酸酸化酵素と精神神経疾患, 第32回日本トリプトファン研究会学術集会, Dec. 2010.
12.	Kiyoshi Fukui : D-アミノ酸代謝システムによる脳機能制御に関する医学応用酵素学研究, 日本応用酵素協会第36回研究発表会, Nov. 2010.
13.	Kiyoshi Fukui : ヒトD-アミノ酸代謝システムの制御と疾患, ビタミンB研究委員会シンポジウム「B群ビタミンのシステムバイオロジー-新機能タンパク質の発見から病気との関連まで-」, Feb. 2010.
14.	Kiyoshi Fukui : D-アミノ酸による細胞死誘導, 第416回ビタミンB研究協議会, May 2009.
15.	Kiyoshi Fukui : D-アミノ酸代謝システムの疾患酵素学, ビタミンB研究委員会シンポジウム「B群ビタミン酵素構造機能解析の新展開」, Feb. 2008.
16.	Kiyoshi Fukui : D- アミノ酸代謝と細胞死制御の疾患酵素学, 第5回徳島大学疾患酵素学研究センターシンポジウム「疾患酵素学研究の最前線と新展開」, Sep. 2007.
17.	Sanae Iwana, Tomoya Kawazoe, Hwan Ki Park, Koji Ono, Seongpil Chung, Rabab Mohamed Abou El-Magd, Kazuko YORITA and Kiyoshi Fukui : 向精神薬クロルプロマジンの光反応産物によるD-アミノ酸酸化酵素の活性阻害, 第408回ビタミンB研究協議会, May 2007.
18.	Kiyoshi Fukui : レニン結合蛋白質とD-アミノ酸酸化酵素の構造と機能, 第20回蛋白質と酵素の構造と機能に関する九州シンポジウム, Jul. 1996.
19.	Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe, Masazumi Tada, Motoshige Miyano and Yoshihiro Miyake : D-アミノ酸酸化酵素の遺伝子構造とその発現, 第63回日本生化学会大会ミニシンポジウム, Sep. 1990.
20.	三宅可浩, Kiyoshi Fukui, 桃井京子 and 渡邊房男 : フラビン酵素-D-アミノ酸酸化酵素の遺伝子構造と発現制御, ビタミンB研究委員会シンポジウム「ビタミン研究における遺伝子工学の応用」, Feb. 1989.
21.	Kiyoshi Fukui, Kyoko Momoi, Fusao Watanabe and Yoshihiro Miyake : D-プロパルギルグリシンとD-アミノ酸酸化酵素のin vivoにおける反応, 第303回ビタミンB研究協議会, May 1988.

Report:

1.	Ri-ichi Murakami, Toshihisa Ohshima, Kiyoshi Fukui, Hideyuki Nakagawa, Haruhiko Sakuraba and Daisuke Yonekura : ダイヤモンドなど炭素系薄膜を利用した新規高度耐久性バイオ基材の開発, 文部科学省科学研究費補助金(基盤研究(C)(2))成果報告書, Mar. 2004.

Patent:

1.	Kiyoshi Fukui and Takashi Sakai : 新規アポトーシス誘導タンパク質及びそれをコードする遺伝子, 2001-326784 (Oct. 2001), 3985131 (Jul. 2007).

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

分子表面の有用構造を標的としたD-アミノ酸酸化酵素阻害剤の創出 (Project/Area Number: 18K06580 )
Study of a novel NF-kappaB-regulating protein, Nucling, in the development of non-alcoholic fatty liver diseases (Project/Area Number: 25460388 )
Studies on signaling pathways mediated by Nucling, a novel apoptosis-associating protein, in the development of inflammatory disorders and tumors (Project/Area Number: 22590286 )
Elucidation of the mechanism of Nuoling, a novel NF-Kb-regulatory factor, for the development of inflammatory diseases (Project/Area Number: 19590310 )
D-アミノ酸酸化酵素は統合失調症の疾患感受性を規定し、その病態制御に関与するか? (Project/Area Number: 17659094 )
統合失調症病態のD-アミノ酸酸化酵素による制御機構の解明 (Project/Area Number: 16659304 )
ダイヤモンドなど炭素系薄膜を利用した新規硬度耐久性バイオ基材の開発 (Project/Area Number: 14655047 )
Molecular Enzymological Studies on the Pathophysiological Significance of Brain Endogeneous D-amino Acids and Their Metabolizing Enzyme (Project/Area Number: 13670143 )
哺乳類におけるD-アミノ酸の生理機能に関する総合的研究 (Project/Area Number: 12897002 )
神経細胞死の防御に関与するD-アミノ酸酸化酵素の機能解析 (Project/Area Number: 10176224 )
Molecular Biological Analysis of function and signal transduction of renin-binding protein (Project/Area Number: 09671631 )
Molecular Biological Studies on the Function and Signal Transduction of Novel Brain and Cardiovascular Regulatory Factors (Project/Area Number: 09470033 )
Joint Study on the Function of Brain D-Amino Acid Oxidase (Project/Area Number: 09044315 )
Joint Study on the Function of Renin-binding Protein (Project/Area Number: 08044297 )
循環調節系の新しい因子の機能と情報伝達に関する分子生物学的研究 (Project/Area Number: 07680705 )
Molecular Biological Studies on new regulatory factors in the control of blood pressure and body fluid with reference to the pathogenesis of hypertension (Project/Area Number: 05670159 )
Biochemical and Molecular Biological Studies on Factors Related to Kidney Transport and Homeostasis under Normal and Pathological States (Project/Area Number: 63570137 )
Studies on moiecular and cellular transporting mechanism of nephrons under pathological states (Project/Area Number: 61570151 )
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Professor Emeritus / Vice president : Fukui, Kiyoshi

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