Tokushima University / Educator and Researcher Directory --- Kondo, Hiroyuki

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Tokushima University ⟩ Graduate School of Biomedical Sciences ⟩ 医学域 ⟩ 先端医学教育研究プロジェクト ⟩
Tokushima University ⟩ Graduate School of Biomedical Sciences ⟩ 医学域 ⟩ Medical Science ⟩ Pathological Sciences ⟩ Department of Immunology and Parasitology ⟩
Tokushima University ⟩ Faculty of Medicine ⟩ School of Medicine ⟩ Course of Microbiology and Immunology ⟩ Immunology and Parasitology ⟩

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Research

Field of Study

Subject of Study

Book / Paper

Academic Paper (Judged Full Paper):

1.	Thiranut Jaroonwitchawan, Hideki Arimochi, Yuki Sasaki, Chieko Ishifune, Hiroyuki Kondo, Kunihiro Otsuka, Shin-ichi Tsukumo and Koji Yasutomo : Stimulation of the farnesoid X receptor promotes M2 macrophage polarization., Frontiers in Immunology, Vol.14, 2023. (Summary) This skewed polarization towards M2 macrophages by an FXR agonist was accompanied by increased expression of signaling molecules related to the retinoic acid receptor. Inhibition of the retinoic acid receptor suppressed FXR agonist-mediated M2 macrophage polarization, indicating that this polarization was, at least, partly dependent on the retinoic acid receptor pathway. These data demonstrate that FXR has a role in polarization toward M2 macrophages and suggest a possible therapeutic potential of FXR agonists in M2 macrophage-related conditions. (Keyword) Receptors, Cytoplasmic and Nuclear (Tokushima University Institutional Repository) ● Metadata: 118291 (Link to Publication Site) ● Publication site (DOI): 10.3389/fimmu.2023.1065790 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36776885 ● Search Scopus @ Elsevier (PMID): 36776885 ● Search Scopus @ Elsevier (DOI): 10.3389/fimmu.2023.1065790 (Tokushima University Institutional Repository: 118291, DOI: 10.3389/fimmu.2023.1065790, PubMed: 36776885)
2.	Hiroyuki Kondo, Takahiro Kageyama, Shigeru Tanaka, Kunihiro Otsuka, Shin-ichi Tsukumo, Yoichi Mashimo, Yoshihiro Onouchi, Hiroshi Nakajima and Koji Yasutomo : Markers of Memory CD8 T Cells Depicting the Effect of the BNT162b2 mRNA COVID-19 Vaccine in Japan., Frontiers in Immunology, Vol.13, 2022. (Summary) BNT162b2, a nucleoside-modified mRNA vaccine for SARS-CoV-2 spike glycoprotein (S), provides approximately 95% efficacy for preventing COVID-19. However, it remains unclear how effectively memory CD8+ T cells are generated and which genetic and environmental factors affect the generation and function of memory CD8+ T cells elicited by this vaccine. Here, we investigated the frequency and functions of memory CD8+ T cells 3 weeks after the second vaccination in the Japanese population. Using a peptide-MHC pentamer, we detected an increased number of memory CD8+ T cells together with increased serum anti-S protein antibody in females compared with that in males, but the frequency of pentamer-positive cells was not positively correlated with antibody titers. Memory precursor effector cells (KLRG1-CD127+) among both CD8+ cells and pentamer+ cells and effector cells (CD38-HLA-DR+) among pentamer+ cells were more abundant in females than in males. Upon S protein-mediated stimulation of T cells, the intensity of CD107a and granzyme B expression was increased in females compared with that in males, indicating stronger memory CD8+ T cell responses in females than in males. Our studies showed that the BNT162b2 vaccine elicits increased memory CD8+ T cell proliferation and secondary CTL responses in females compared with those in males in the Japanese population. These findings provide an important basis for the distinct sex difference in cellular immune responses to mRNA vaccination and suggest that memory precursor effector cells can be one of markers to evaluate and boost cellular immunity induced by BNT162b2. (Tokushima University Institutional Repository) ● Metadata: 117815 (Link to Publication Site) ● Publication site (DOI): 10.3389/fimmu.2022.836923 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35572546 ● Search Scopus @ Elsevier (PMID): 35572546 ● Search Scopus @ Elsevier (DOI): 10.3389/fimmu.2022.836923 (Tokushima University Institutional Repository: 117815, DOI: 10.3389/fimmu.2022.836923, PubMed: 35572546)
3.	Yuki Sasaki, Hideki Arimochi, Kunihiro Otsuka, Hiroyuki Kondo, Shin-ichi Tsukumo and Koji Yasutomo : Blockade of the CXCR3/CXCL10 axis ameliorates inflammation caused by immunoproteasome dysfunction., JCI Insight, Vol.7, No.7, 2022. (Summary) Immunoproteasomes regulate the degradation of ubiquitin-coupled proteins and generate peptides that are preferentially presented by MHC class I. Mutations in immunoproteasome subunits lead to immunoproteasome dysfunction, which causes proteasome-associated autoinflammatory syndromes (PRAAS) characterized by nodular erythema and partial lipodystrophy. It remains unclear, however, how immunoproteasome dysfunction leads to inflammatory symptoms. Here, we established mice harboring a mutation in Psmb8 (Psmb8-KI mice) and addressed this question. Psmb8-KI mice showed higher susceptibility to imiquimod-induced skin inflammation (IMS). Blockade of IL-6 or TNF-α partially suppressed IMS in both control and Psmb8-KI mice, but there was still more residual inflammation in the Psmb8-KI mice than in the control mice. DNA microarray analysis showed that treatment of J774 cells with proteasome inhibitors increased the expression of the Cxcl9 and Cxcl10 genes. Deficiency in Cxcr3, the gene encoding the receptor of CXCL9 and CXCL10, in control mice did not change IMS susceptibility, while deficiency in Cxcr3 in Psmb8-KI mice ameliorated IMS. Taken together, these findings demonstrate that this mutation in Psmb8 leads to hyperactivation of the CXCR3 pathway, which is responsible for the increased susceptibility of Psmb8-KI mice to IMS. These data suggest the CXCR3/CXCL10 axis as a new molecular target for treating PRAAS. (Tokushima University Institutional Repository) ● Metadata: 117226 (Link to Publication Site) ● Publication site (DOI): 10.1172/jci.insight.152681 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35393946 ● Search Scopus @ Elsevier (PMID): 35393946 ● Search Scopus @ Elsevier (DOI): 10.1172/jci.insight.152681 (Tokushima University Institutional Repository: 117226, DOI: 10.1172/jci.insight.152681, PubMed: 35393946)
4.	Yohei Yamamoto, Naoko Matsui, Akiyuki Uzawa, Yukiko Ozawa, Tetsuya Kanai, Fumiko Oda, Hiroyuki Kondo, Izumi Ohigashi, Hiromitsu Takizawa, Kazuya Kondo, Mikio Sugano, Takashi Kitaichi, Hiroki Hata, Ryuji Kaji, Satoshi Kuwabara, Takashi Yamamura and Yuishin Izumi : Intrathymic Plasmablasts Are Affected in Patients With Myasthenia Gravis With Active Disease., Neurology® Neuroimmunology & Neuroinflammation, Vol.8, No.6, e1087, 2021. (Summary) Our findings confirmed a correlation between increased frequency of intrathymic plasmablasts and disease activity before thymectomy. We postulate that activated intrathymic plasmablasts endow pathogenic capacity in MG. (Keyword) Adolescent / adult / Aged / B-Lymphocytes / children / Child, Preschool / female / Humans / Leukocytes, Mononuclear / Lymphopoiesis / male / Middle Aged / Myasthenia Gravis / Stem Cells / T lymphocytes / Thymectomy / Thymoma / Thymus Neoplasms / Young Adult (Tokushima University Institutional Repository) ● Metadata: 116884 (Link to Publication Site) ● Publication site (DOI): 10.1212/NXI.0000000000001087 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34561276 ● Summary page in Scopus @ Elsevier: 2-s2.0-85117018419 (Tokushima University Institutional Repository: 116884, DOI: 10.1212/NXI.0000000000001087, PubMed: 34561276, Elsevier: Scopus)
5.	M Lachén-Montes, N Mendizuri, K Ausín, A Pérez-Mediavilla, M Azkargorta, I Iloro, F Elortza, Hiroyuki Kondo, Izumi Ohigashi, I Ferrer, R la Torre de, P Robledo, J Fernández-Irigoyen and E Santamaría : Smelling the Dark Proteome: Functional Characterization of PITH Domain-Containing Protein 1 (C1orf128) in Olfactory Metabolism, Journal of Proteome Research, Vol.19, No.12, 4826-4843, 2020. (Summary) The Human Proteome Project (HPP) consortium aims to functionally characterize the dark proteome. On the basis of the relevance of olfaction in early neurodegeneration, we have analyzed the dark proteome using data mining in public resources and omics data sets derived from the human olfactory system. Multiple dark proteins localize at synaptic terminals and may be involved in amyloidopathies such as Alzheimer's disease (AD). We have characterized the dark PITH domain-containing protein 1 (PITHD1) in olfactory metabolism using bioinformatics, proteomics, in vitro and in vivo studies, and neuropathology. PITHD1 mice exhibit olfactory bulb (OB) proteome changes related to synaptic transmission, cognition, and memory. OB PITHD1 expression increases with age in wild-type (WT) mice and decreases in Tg2576 AD mice at late stages. The analysis across 6 neurological disorders reveals that olfactory tract (OT) PITHD1 is specifically upregulated in human AD. Stimulation of olfactory neuroepithelial (ON) cells with PITHD1 alters the ON phosphoproteome, modifies the proliferation rate, and induces a pro-inflammatory phenotype. This workflow applied by the Spanish C-HPP and Human Brain Proteome Project (HBPP) teams across the ON-OB-OT axis can be adapted as a guidance to decipher functional features of dark proteins. Data are available via ProteomeXchange with identifiers PXD018784 and PXD021634. (Tokushima University Institutional Repository) ● Metadata: 116206 (Link to Publication Site) ● Publication site (DOI): 10.1021/acs.jproteome.0c00452 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33185454 ● Summary page in Scopus @ Elsevier: 2-s2.0-85096567671 (Tokushima University Institutional Repository: 116206, DOI: 10.1021/acs.jproteome.0c00452, PubMed: 33185454, Elsevier: Scopus)
6.	Hiroyuki Kondo, Takafumi Matsumura, Mari Kaneko, Kenichi Inoue, Hidetaka Kosako, Masahito Ikawa, Yousuke Takahama and Izumi Ohigashi : PITHD1 is a proteasome-interacting protein essential for male fertilization, The Journal of Biological Chemistry, Vol.295, No.6, 1658-1672, 2020. (Summary) The proteasome is a protein-degrading molecular complex that is necessary for protein homeostasis and various biological functions, including cell cycle regulation, signal transduction, and immune response. Proteasome activity is finely regulated by a variety of proteasome-interacting molecules. PITHD1 is a recently described molecule that has a domain putatively capable of interacting with the proteasome. However, it is unknown whether PITHD1 can actually bind to proteasomes and what it does Here we report that PITHD1 is detected specifically in the spermatids in the testis and the cortical thymic epithelium in the thymus. Interestingly, PITHD1 associates with immunoproteasomes in the testis, but not with thymoproteasomes in the thymus. Mice deficient in PITHD1 exhibit severe male infertility accompanied with morphological abnormalities and impaired motility of spermatozoa. Furthermore, PITHD1 deficiency reduces proteasome activity in the testis and alters the amount of proteins that are important for fertilization capability by the sperm. However, the PITHD1-deficient mice demonstrate no detectable defects in the thymus, including T cell development. Collectively, our results identify PITHD1 as a proteasome-interacting protein that plays a nonredundant role in the male reproductive system. (Tokushima University Institutional Repository) ● Metadata: 114611 (Link to Publication Site) ● Publication site (DOI): 10.1074/jbc.RA119.011144 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31915251 ● Search Scopus @ Elsevier (PMID): 31915251 ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.RA119.011144 (Tokushima University Institutional Repository: 114611, DOI: 10.1074/jbc.RA119.011144, PubMed: 31915251)
7.	Izumi Ohigashi, Yu Tanaka, Kenta Kondou, Sayumi Fujimori, Hiroyuki Kondo, Amy Palin, Victoria Hoffmann, Mina Kozai, Yosuke Matsushita, Shinsuke Uda, Ryo Motosugi, Jun Hamazaki, Hiroyuki Kubota, Shigeo Murata, Keiji Tanaka, Toyomasa Katagiri, Hidetaka Kosako and Yousuke Takahama : Trans-omics Impact of Thymoproteasome in Cortical Thymic Epithelial Cells., Cell Reports, Vol.29, No.9, 2901-2916.e6, 2019. (Tokushima University Institutional Repository) ● Metadata: 115049 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.celrep.2019.10.079 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31775054 ● Search Scopus @ Elsevier (PMID): 31775054 ● Search Scopus @ Elsevier (DOI): 10.1016/j.celrep.2019.10.079 (Tokushima University Institutional Repository: 115049, DOI: 10.1016/j.celrep.2019.10.079, PubMed: 31775054)
8.	Toshifumi Tomoyasu, Keigo Tsuruno, Ryosuke Tanatsugu, Aya Miyazaki, Hiroyuki Kondo, Atsushi Tabata, Whiley A. Robert, Kenji Sonomoto and Hideaki Nagamune : Recognizability of heterologous co-chaperones with Streptococcus intermedius DnaK and Escherichia coli DnaK, Microbiology and Immunology, Vol.62, No.11, 681-693, 2018. (Summary) Streptococcus intermedius DnaK complements the temperature-sensitive phenotype of an Escherichia coli dnaK null mutant only when co-chaperones DnaJ and GrpE are co-expressed. Therefore, whether S. intermedius DnaK and E. coli DnaK can recognize heterologous co-chaperones in vitro was examined. Addition of heterologous GrpE to DnaK and DnaJ partially stimulated adenosine triphosphatase (ATPase) activity, and almost completely stimulated luciferase refolding activity. Addition of heterologous DnaJ to GrpE and DnaK also stimulated ATPase activity; however, significant luciferase refolding activity was not observed. Moreover, E. coli DnaJ had a negative effect on the luciferase refolding activity of the S. intermedius DnaK chaperone system. In E. coli chaperone mutants, with the exception of E. coli DnaJ, stronger expression of the heterologous co-chaperones partially or almost completely complemented the temperature-sensitive-phenotype. These results indicate that all heterologous co-chaperones can at least partially recognize DnaK of a distantly related species. A region of the ATPase domain that is present in the DnaK of gram-negative bacteria is absent from the DnaK of gram-positive bacteria. This region is believed to be important for recognition of co-chaperones from gram-negative bacteria. However, insertion of this segment into S. intermedius DnaK failed to increase its ability to recognize E. coli co-chaperones, implying that this region is unnecessary or insufficient for the recognition of E. coli co-chaperones. Thus, our data suggest that a basic structural similarity is conserved among the components of the S. intermedius and E. coli DnaK chaperone systems, allowing weak associations between heterologous components. (Keyword) molecular chaperone / Escherichia coli / Streptococcus (Tokushima University Institutional Repository) ● Metadata: 115748 (Link to Publication Site) ● Publication site (DOI): 10.1111/1348-0421.12651 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30239035 ● Summary page in Scopus @ Elsevier: 2-s2.0-85056121796 (Tokushima University Institutional Repository: 115748, DOI: 10.1111/1348-0421.12651, PubMed: 30239035, Elsevier: Scopus)
9.	Mina Kozai, Yuki Kubo, Tomoya Katakai, Hiroyuki Kondo, Hiroshi Kiyonari, Karin Schaeuble, Sanjiv A. Luther, Naozumi Ishimaru, Izumi Ohigashi and Yousuke Takahama : Essential role of CCL21 in establishment of central self-tolerance in T cells, The Journal of Experimental Medicine, Vol.214, No.7, 1925-1935, 2017. (Summary) The chemokine receptor CCR7 directs T cell relocation into and within lymphoid organs, including the migration of developing thymocytes into the thymic medulla. However, how three functional CCR7 ligands in mouse, CCL19, CCL21Ser, and CCL21Leu, divide their roles in immune organs is unclear. By producing mice specifically deficient in CCL21Ser, we show that CCL21Ser is essential for the accumulation of positively selected thymocytes in the thymic medulla. CCL21Ser-deficient mice were impaired in the medullary deletion of self-reactive thymocytes and developed autoimmune dacryoadenitis. T cell accumulation in the lymph nodes was also defective. These results indicate a nonredundant role of CCL21Ser in the establishment of self-tolerance in T cells in the thymic medulla, and reveal a functional inequality among CCR7 ligands in vivo. (Keyword) Animals / Autoimmune Diseases / Central Tolerance / Chemokine CCL21 / Dacryocystitis / Flow Cytometry / gene expression / Lymph Nodes / Mice, Inbred C57BL / knockout mice / Mice, Nude / Mice, Transgenic / Microscopy, Confocal / Receptors, CCR7 / Reverse Transcriptase Polymerase Chain Reaction / Self Tolerance / T lymphocytes / Thymocytes / Thymus Gland (Tokushima University Institutional Repository) ● Metadata: 110168 (Link to Publication Site) ● Publication site (DOI): 10.1084/jem.20161864 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28611158 ● Search Scopus @ Elsevier (PMID): 28611158 ● Search Scopus @ Elsevier (DOI): 10.1084/jem.20161864 (Tokushima University Institutional Repository: 110168, DOI: 10.1084/jem.20161864, PubMed: 28611158)
10.	Katsuhiro Sasaki, Kensuke Takada, Yuki Ohte, Hiroyuki Kondo, Hiroyuki Sorimachi, Keiji Tanaka, Yousuke Takahama and Shigeo Murata : Thymoproteasomes produce unique peptide motifs for positive selection of CD8(+) T cells., Nature Communications, Vol.6, 7484, 2015. (Summary) Positive selection in the thymus provides low-affinity T-cell receptor (TCR) engagement to support the development of potentially useful self-major histocompatibility complex class I (MHC-I)-restricted T cells. Optimal positive selection of CD8(+) T cells requires cortical thymic epithelial cells that express 5t-containing thymoproteasomes (tCPs). However, how tCPs govern positive selection is unclear. Here we show that the tCPs produce unique cleavage motifs in digested peptides and in MHC-I-associated peptides. Interestingly, MHC-I-associated peptides carrying these tCP-dependent motifs are enriched with low-affinity TCR ligands that efficiently induce the positive selection of functionally competent CD8(+) T cells in antigen-specific TCR-transgenic models. These results suggest that tCPs contribute to the positive selection of CD8(+) T cells by preferentially producing low-affinity TCR ligand peptides. (Tokushima University Institutional Repository) ● Metadata: 115643 (Link to Publication Site) ● Publication site (DOI): 10.1038/ncomms8484 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 26099460 ● Summary page in Scopus @ Elsevier: 2-s2.0-84934975580 (Tokushima University Institutional Repository: 115643, DOI: 10.1038/ncomms8484, PubMed: 26099460, Elsevier: Scopus)

Review, Commentary:

1.	Hiroyuki Kondo and Koji Yasutomo : BNT162b2 mRNA COVID-19ワクチン後の効果に関連するメモリーCD8T細胞マーカー, Clinical Immunology & Allergology, Vol.79, No.1, 44-48, Jan. 2023.
2.	Hiroyuki Kondo and Yousuke Takahama : Tリンパ球の分化と胸腺の役割, 病理と臨床, Vol.33, 696-702, 2015.

Proceeding of International Conference:

1.	Kunihiro Otsuka, Hiroyuki Kondo, Shin-ichi Tsukumo and Koji Yasutomo : The interplay between CD4 T cells and fibroblasts in salivary glands drives autoimmune pathology in Sjögrens syndrome, 11th International Conference on Autoimmunity: Mechanisms and NovelTreatments; Aegean Conference, Oct. 2024.
2.	Izumi Ohigashi, Yu Tanaka, Kenta Kondou, Sayumi Fujimori, Amy C. Palin, Hiroyuki Kondo, Hidetaka Kosako and Yousuke Takahama : Trans-omics impact of thymoproteasome in cortical thymic epithelial cells, ThymE: T cell and thymus biology, May 2019.

Proceeding of Domestic Conference:

1.	Kunihiro Otsuka, Hiroyuki Kondo, Naozumi Ishimaru and Koji Yasutomo : 線維芽細胞を介した自己免疫病変の増悪機構, 第32回日本シェーグレン症候群学会学術集会, Sep. 2024.
2.	Erkhembayar Shinebaatar, Junko Morimoto, Hiroyuki Kondo and Koji Yasutomo : Dysfunction of proteasomes in T cells causes immunodeficiency, 第52回日本免疫学会学術集会, Jan. 2024.
3.	Kunihiro Otsuka, Hiroyuki Kondo, Shin-ichi Tsukumo, Aya Ushio, Naozumi Ishimaru and Koji Yasutomo : CD153+ CD4+ T cells and CD30+ cells exacerbate the autoimmune pathology in salivary glands of Sjögren's syndrome, 第52回日本免疫学会学術集会, Jan. 2024.
4.	Hiroyuki Kondo, OKABE Katsuki, KAWASAKA Yasuto, Kunihiro Otsuka and Koji Yasutomo : インフルエンザウイルス肺炎の免疫応答におけるマルチプレックス時空間解析とそこから発見した組織修復性CD4陽性T細胞の解析, 第46回日本分子生物学会年会, Dec. 2023.
5.	Kunihiro Otsuka, Hiroyuki Kondo, Shin-ichi Tsukumo, Aya Ushio, RUKA Nagao, Keiko Aota, Naozumi Ishimaru and Koji Yasutomo : シングルセル解析を基盤としたシェーグレン症候群の病態解明, 第31回日本シェーグレン症候群学会学術集会, Sep. 2023.
6.	OKABE Katsuki, Kunihiro Otsuka, Hiroyuki Kondo and Koji Yasutomo : インフルエンザウイルス肺炎の免疫応答に関するマルチプレックス時空間解析, 第112回日本病理学会総会, Apr. 2023.
7.	Kunihiro Otsuka, Hiroyuki Kondo, Shin-ichi Tsukumo, Rieko Arakaki, Ruka Nagao, Mami Sato, Aya Ushio, Naozumi Ishimaru and Koji Yasutomo : CD153-CD30相互反応を介したシェーグレン症候群の病態形成機構の解明, 第112回日本病理学会総会, Apr. 2023.
8.	Hiroyuki Kondo, Shin-ichi Tsukumo, Kunihiro Otsuka and Koji Yasutomo : Markers of memory CD8 T cells depicting the effect of the BNT162b2 mRNA COVID-19 vaccine in Japan, 第45回日本分子生物学会年会, Nov. 2022.
9.	Kunihiro Otsuka, Hiroyuki Kondo, Shin-ichi Tsukumo, Rieko Arakaki, Mami Sato, Takaaki Tsunematsu, Naozumi Ishimaru and Koji Yasutomo : シングルセルRNA-seqとマルチプレックスSpatial解析を基盤としたシェーグレン症候群の標的臓器微小環境変化の解明, 第33回日本臨床口腔病理学会, Sep. 2022.
10.	Kunihiro Otsuka, Shin-ichi Tsukumo, Hiroyuki Kondo, Mami Sato, Hiroaki TAWARA, Takaaki Tsunematsu, Naozumi Ishimaru and Koji Yasutomo : シングルセルRNA-seqで紐解くシェーグレン症候群モデルに特徴的に出現するT細胞集団の解析, 第64回歯科基礎医学会学術大会, Sep. 2022.
11.	Hiroyuki Kondo, Kunihiro Otsuka, Shin-ichi Tsukumo and Koji Yasutomo : 日本における新型SARS-CoV-2 mRNAワクチンBNT162b2の効果を示すメモリーCD8T細胞マーカー, 第20回四国免疫フォーラム, Jun. 2022.
12.	Kunihiro Otsuka, Shin-ichi Tsukumo, Hiroyuki Kondo, Rieko Arakaki, Naozumi Ishimaru and Koji Yasutomo : シングルセルRNA-seqで紐解くシェーグレン症候群モデルに特徴的に出現するT細胞集団の解析, 第111回日本病理学会総会, Apr. 2022.
13.	Yuki Sasaki, Hideki Arimochi, Kunihiro Otsuka, Hiroyuki Kondo, Shin-ichi Tsukumo and Koji Yasutomo : Blockade of the CXCR3-CXCL10 axis ameliorates inflammatory responses caused by immunoproteasome dysfunctions, 第50回日本免疫学会学術集会, Dec. 2021.
14.	Hiroyuki Kondo, 松村貴史, Hidetaka Kosako, 伊川正人, Yousuke Takahama and Izumi Ohigashi : 新規プロテアソーム会合因子PITHD1は精子形成を制御する, 第42回日本分子生物学学会年会, Dec. 2019.
15.	Yohhei Yamamoto, Naoko Matsui, 織田史子, 小澤由希子, 金井哲也, 鵜沢顕之, Izumi Ohigashi, Hiroyuki Kondo, Kazuya Kondo, Tetsuya Kitagawa, 桑原聡, 山村隆, Yuishin Izumi and Ryuji Kaji : 重症筋無力症患者の胸腺におけるB細胞分画と濾胞性ヘルパーT細胞の解析, 第31回日本神経免疫学会学術集会, Vol.24, No.1, 140, Sep. 2019.
16.	Yohei Yamamoto, Naoko Matsui, Fumiko Oda, Yukiko Ozawa, Tetsuya Kanai, Akiyuki Uzawa, Izumi Ohigashi, Hiroyuki Kondo, Kazuya Kondo, Tetsuya Kitagawa, Takashi Yamamura, Satoshi Kuwabara, Yuishin Izumi and Ryuji Kaji : B cell subsets and T follicular helper cells in myasthenia gravis thymus, 第60回日本神経学会学術大会, May 2019.
17.	Hiroyuki Kondo, 松村貴史, Hidetaka Kosako, 伊川正人, Yousuke Takahama and Izumi Ohigashi : プロテアソームに会合する新規分子PITHD1の機能解析, 第41回日本分子生物学会年会, Nov. 2018.
18.	Toshifumi Tomoyasu, Hiroyuki Kondo, Masanori Oisugi, Atsushi Tabata and Hideaki Nagamune : グラム陽性菌と陰性菌のDnaKシャペロンシステムの比較, 第54回日本生化学会中国・四国支部例会, Jun. 2013. (Keyword) DnaK / ClpB / Gram-Positive Bacteria / Gram-Negative Bacteria / molecular chaperone

Et cetera, Workshop:

1.	Hiroyuki Kondo, Yousuke Takahama and Izumi Ohigashi : 胸腺皮質上皮細胞で高発現する新規分子の機能解析, 第28回 Kyoto T cell Conference, Jun. 2018.
2.	Hiroyuki Kondo, Izumi Ohigashi and Yousuke Takahama : CCL21Ser欠損マウスにおけるT細胞異常, 第16回四国免疫フォーラム, Jun. 2017.
3.	Hiroyuki Kondo, Izumi Ohigashi and Yousuke Takahama : 胸腺皮質上皮細胞で高発現される機能未知新規遺伝子の研究, 2015感染免疫クラスター・ミニリトリート, Nov. 2015.
4.	Hiroyuki Kondo, Izumi Ohigashi and Yousuke Takahama : 胸腺皮質上皮細胞で高発現される機能未知新規遺伝子の研究:ノックアウトマウスと特異的抗体の作製によるアプローチ, 2014感染免疫クラスター・ミニリトリート, Oct. 2014.

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

メモリーCD8+T細胞で発現するDMRTA1の機能解析 (Project/Area Number: 22K15495 )
Search by Researcher Number (60935047)