S
Sho Yamasaki
Researcher at Osaka University
Publications - 195
Citations - 11586
Sho Yamasaki is an academic researcher from Osaka University. The author has contributed to research in topics: C-type lectin & Immune system. The author has an hindex of 45, co-authored 156 publications receiving 9894 citations. Previous affiliations of Sho Yamasaki include Chiba University & National Institute for Medical Research.
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Journal ArticleDOI
Essential role of Rap signal in pre-TCR–mediated β-selection checkpoint in αβ T-cell development
Kohei Kometani,Masaki Moriyama,Yasuhiro Nakashima,Yoshinori Katayama,Shu Fang Wang,Sho Yamasaki,Takashi Saito,Masakazu Hattori,Nagahiro Minato +8 more
TL;DR: The results suggest that endogenous Rap GTPases downstream of pre-TCR play an essential role in rescuing pre-T cells from the p53-mediated checkpoint response, thus allowing Notch-mediated expansion and differentiation.
Journal ArticleDOI
Involvement of Rap-1 activation and early termination of immune synapse in CTLA-4-mediated negative signal.
Satoru Hara,Chiaki Nakaseko,Sho Yamasaki,Masakazu Hattori,Johannes L. Bos,Yasushi Saito,Nagahiro Minato,Takashi Saito +7 more
TL;DR: It is found that CTLA-4 specifically up-regulates cell motility and suppresses prolonged accumulation of Talin at the contact area with antigen presenting cells upon antigen stimulation, and suggests that Rap-1 is activated upon CT LA-4 ligation and mediates inhibitory signals through prevention of IS formation.
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Agonistic or antagonistic mucosal-associated invariant T (MAIT) cell activity is determined by the 6-alkylamino substituent on uracil MR1 ligands
Chriselle D. Braganza,Chihiro Motozono,Koh Hei Sonoda,Sho Yamasaki,Kensuke Shibata,Kensuke Shibata,Kensuke Shibata,Mattie S. M. Timmer,Bridget L. Stocker +8 more
TL;DR: It is demonstrated that changes to the 6-aminoalkyl chain on uracil agonist 5-OP-RU can determine agonistic or antagonistic MAIT cell activity.
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C-Type Lectin Receptor Dectin-2 Binds to an Endogenous Protein β-Glucuronidase on Dendritic Cells.
TL;DR: This study suggests that a glycosylated protein with mannose-related structure is recognized by Dectin-2, and Overexpression of Gusb in a macrophage cell line conferred an ability to stimulate DectIn-2-expressing reporter cells.
Journal ArticleDOI
Lipid structure influences the ability of glucose monocorynomycolate to signal through Mincle
Phillip L. van der Peet,Masahiro Nagata,Sayali Shah,Jonathan M. White,Sho Yamasaki,Spencer J. Williams +5 more
TL;DR: This work suggests that Mincle has the ability to survey mycolate-derived glycolipids from actinomycetes, distinguishing non-pathogenic and pathogenic species on the basis of α-chain length.