S
Shizuo Akira
Researcher at Osaka University
Publications - 1330
Citations - 344469
Shizuo Akira is an academic researcher from Osaka University. The author has contributed to research in topics: Innate immune system & Immune system. The author has an hindex of 261, co-authored 1308 publications receiving 320561 citations. Previous affiliations of Shizuo Akira include University of California, Berkeley & Wakayama Medical University.
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Journal ArticleDOI
BS69, a specific adaptor in the latent membrane protein 1-mediated c-Jun N-terminal kinase pathway
Jun Wan,Wei Zhang,Liming Wu,Ting Bai,Mingjie Zhang,Kwok Wai Lo,Yiu Ioon Chui,Yan Cui,Qian Tao,Masahiro Yamamoto,Shizuo Akira,Zhenguo Wu +11 more
TL;DR: It is shown that BS69, a MYND domain-containing cellular protein, is the missing adaptor that bridges LMP1 and TRAF6, as the MyND domain and a separate region of BS69 bind to the carboxyl termini of LMP 1 and TRAf6, respectively.
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Introduction of Human γ1 Immunoglobulin Genes into Fertilized Mouse Eggs
Ken Ichi Yamamura,Hitoshi Kikutani,Naoki Takahashi,Tetsuya Taga,Shizuo Akira,Kazuhiko Kawai,Ken-ichiro Fukuchi,Yuichi Kumahara,Tasuku Honjo,Tadamitsu Kishimoto +9 more
TL;DR: The presence of the human gamma 1 immunoglobulin gene appeared to have no effect on the expression of endogenous mouse immunoglOBulin genes, as judged by the Southern blotting patterns for several restriction enzymes.
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Neutrophils alleviate fibrosis in the CCl4-induced mouse chronic liver injury model.
Eiko Saijou,Yutaka Enomoto,Michitaka Matsuda,Cindy Kok,Shizuo Akira,Minoru Tanaka,Atsushi Miyajima +6 more
TL;DR: A beneficial role of neutrophils is demonstrated in chronic liver injury by promoting fibrolysis while neutrophil depletion by infusion of Ly6G antibody significantly enhanced CCl4‐induced fibrosis.
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Antigenic epitopes fused to cationic peptide bound to oligonucleotides facilitate Toll-like receptor 9-dependent, but CD4+ T cell help-independent, priming of CD8+ T cells
TL;DR: Oligodeoxynucleotides (ODN) with immune-stimulating sequences (ISS) containing CpG motifs facilitate the priming of MHC class I-restricted CD8+ T cell responses to proteins or peptides, and are potent Th1-promoting adjuvants when bound to cationic peptides covalently linked to antigenic epitopes.
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Proteolytic Processing of Stat6 Signaling in Mast Cells as a Negative Regulatory Mechanism
Kotaro Suzuki,Hiroshi Nakajima,Shin-ichiro Kagami,Akira Suto,Kei Ikeda,Koichi Hirose,Takaki Hiwasa,Kiyoshi Takeda,Yasushi Saito,Shizuo Akira,Itsuo Iwamoto +10 more
TL;DR: The results indicate that the proteolytic processing of Stat 6 functions as a lineage-specific negative regulator of Stat6-dependent signaling in mast cells, and thus suggest that it may account for the limited role of stat6 in IL-4 signaling inmast cells.