Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Mari Ohmura-Hoshino"'
Publikováno v:
Heliyon, Vol 8, Iss 8, Pp e10231- (2022)
Human diarrhea-causing strains of Escherichia coli are referred to as diarrheagenic E. coli (DEC). DEC can be divided into five main categories based on distinct epidemiological and clinical features, specific virulence determinants, and association
Externí odkaz:
https://doaj.org/article/4e37a36da89e47a5b2bd6e38abc13628
Autor:
Eiji Goto, Mari Mito-Yoshida, Mika Uematsu, Masami Aoki, Yohei Matsuki, Mari Ohmura-Hoshino, Hak Hotta, Makoto Miyagishi, Satoshi Ishido
Publikováno v:
PLoS ONE, Vol 3, Iss 1, p e1490 (2008)
BACKGROUND: At present, it is difficult to visualize the internalization of surface receptors induced by ubiquitination that is taken place at the plasma membrane in mammals. This problem makes it difficult to reveal molecular basis for ubiquitinatio
Externí odkaz:
https://doaj.org/article/fa42557ca9af45a7b0d0aed9a5ade5dc
Autor:
Katsuaki Hoshino, Hai Ying Fu, Atsushi Tobiume, Mari Ohmura-Hoshino, Masahiro Moritoki, Tadashi Sofue, Hiroyuki Saiga, Tetsuo Minamino, Keisuke Onishi
Publikováno v:
Clinical and Experimental Nephrology. 26:226-233
Galectin-9 (Gal-9) is a multifunctional lectin that moderates inflammation and organ damage. In this study, we tested whether Gal-9 has a protective role in the pathogenesis of endotoxemic acute kidney injury. We examined the levels of Gal-9 in contr
Publikováno v:
Heliyon. 8(8)
Human diarrhea-causing strains of
Autor:
Keisuke, Onishi, Hai Ying, Fu, Tadashi, Sofue, Atsushi, Tobiume, Masahiro, Moritoki, Hiroyuki, Saiga, Mari, Ohmura-Hoshino, Katsuaki, Hoshino, Tetsuo, Minamino
Publikováno v:
Clinical and experimental nephrology. 26(3)
Galectin-9 (Gal-9) is a multifunctional lectin that moderates inflammation and organ damage. In this study, we tested whether Gal-9 has a protective role in the pathogenesis of endotoxemic acute kidney injury.We examined the levels of Gal-9 in contro
Autor:
Debbie R. Howard, Satoshi Ishido, Carla M. Roots, Christopher C. Goodnow, Keisuke Horikawa, Christopher E. Andoniou, Heather Domaschenz, Robert J. Rigby, Mari Ohmura-Hoshino, Mariapia A. Degli-Esposti, David A. Way, Lina E. Tze
Publikováno v:
The Journal of Experimental Medicine
By opposing IL-10–driven, MARCH1-mediated ubiquitination and degradation of MHC class II, CD83 may boost the immunogenicity of dendritic cells.
Effective vaccine adjuvants must induce expression of major histocompatability (MHC) class II prote
Effective vaccine adjuvants must induce expression of major histocompatability (MHC) class II prote
Autor:
Mari Ohmura-Hoshino, Adele M. Mount, Jose A Villadangos, Ken Shortman, Nicholas S. Wilson, Satoshi Ishido, Yohei Matsuki, Willem Stoorvogel, William R. Heath, Anna I Proietto, Meredith O'Keeffe, Gabrielle T. Belz, Petra Schnorrer, Toine ten Broeke, Louise J. Young
Publikováno v:
Nature Immunology. 9:1244-1252
The importance of conventional dendritic cells (cDCs) in the processing and presentation of antigen is well established, but the contribution of plasmacytoid dendritic cells (pDCs) to these processes, and hence to T cell immunity, remains unclear. He
Autor:
Mari Mito-Yoshida, Hak Hotta, Haruhiko Koseki, Osamu Ohara, Akitsugu Yamamoto, Takanori Hasegawa, Yohei Matsuki, Kiminori Toyooka, Mika Uematsu, Masami Aoki, Satoshi Ishido, Eiji Goto, Ken Matsuoka, Mari Ohmura-Hoshino, Manabu Nakayama
Publikováno v:
The EMBO Journal. 26:846-854
The presence of post-translational regulation of MHC class II (MHC II) under physiological conditions has been demonstrated recently in dendritic cells (DCs) that potently function as antigen-presenting cells (APCs). Here, we report that MARCH-I, an
Autor:
Eiji Goto, Hak Hotta, Mari Mito, Yohei Matsuki, Masami Aoki, Satoshi Ishido, Mika Uematsu, Mari Ohmura-Hoshino
Publikováno v:
The Journal of Biochemistry. 140:147-154
A novel E3 ubiquitin ligase family that consists of viral E3 ubiquitin ligases (E3s) and their mammalian homologues was recently discovered. These novel E3s are membrane-bound molecules that share the secondary structure and catalytic domain for E3 a
Autor:
Mika Uematsu, Terutaka Kakiuchi, Mari Mito, Hak Hotta, Satoshi Ishido, Yohei Matsuki, Masami Aoki, Mari Ohmura-Hoshino, Eiji Goto
Publikováno v:
The Journal of Immunology. 177:341-354
We previously reported a novel E3 ubiquitin ligase (E3), designated as c-MIR, which targets B7-2 to lysosomal degradation and down-regulates the B7-2 surface expression through ubiquitination of its cytoplasmic tail. B7-2 is well known as a costimula