K
Kazuo Yamamoto
Researcher at University of Tokyo
Publications - 33
Citations - 1153
Kazuo Yamamoto is an academic researcher from University of Tokyo. The author has contributed to research in topics: Lectin & Receptor. The author has an hindex of 16, co-authored 28 publications receiving 1047 citations.
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Journal ArticleDOI
Killer cell lectin-like receptor G1 binds three members of the classical cadherin family to inhibit NK cell cytotoxicity
TL;DR: KLRG1 ligation by E-, N-, or R-cadherins may regulate the cytotoxicity of killer cells to prevent damage to tissues expressing the cadherins.
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The Macrophage C-type Lectin Specific for Galactose/N-Acetylgalactosamine Is an Endocytic Receptor Expressed on Monocyte-derived Immature Dendritic Cells
Nobuaki Higashi,Kouki Fujioka,Kaori Denda-Nagai,Shin-ichi Hashimoto,Shigenori Nagai,Taku J. Sato,Yuko Fujita,Akiko Morikawa,Makoto Tsuiji,Megumi Miyata-Takeuchi,Yoshihiko Sano,Noriko Suzuki,Kazuo Yamamoto,Kouji Matsushima,Tatsuro Irimura +14 more
TL;DR: It is proposed that hMGL is a marker of imDCs and that it functions as an endocytic receptor for glycosylated antigens, which was significantly inhibited by pretreatment of the cells with an anti-hMGL monoclonal antibody.
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Modulation of Heat-shock Protein 27 (Hsp27) Anti-apoptotic Activity by Methylglyoxal Modification
Hiroshi Sakamoto,Hiroshi Sakamoto,Tetsuo Mashima,Kazuo Yamamoto,Takashi Tsuruo,Takashi Tsuruo +5 more
TL;DR: Heat-shock protein 27 (Hsp27) is identified as a major MG-modified protein in cells that causes sensitization of the cells to anti-tumor drug-induced apoptosis and is a novel modulator of cell survival by directly incorporating with the specific protein residue.
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The inhibitory NK cell receptor CD94/NKG2A and the activating receptor CD94/NKG2C bind the top of HLA‐E through mostly shared but partly distinct sets of HLA‐E residues
TL;DR: The results suggest that CD94/NKG2A binds a HLA‐E surface equivalent to a NKG2D binding site on MICA, and indicate that a mostly shared, but partly distinct set of Hla‐E residues is discriminated by the two receptors.
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Sugar-binding Properties of VIP36, an Intracellular Animal Lectin Operating as a Cargo Receptor
Yukiko Kamiya,Yoshiki Yamaguchi,Noriko Takahashi,Yoichiro Arata,Ken-ichi Kasai,Yoshito Ihara,Ichiro Matsuo,Yukishige Ito,Kazuo Yamamoto,Koichi Kato +9 more
TL;DR: It is suggested that VIP36 binds glycoproteins that retain the intact D1 mannosyl branch in the cis-Golgi network and recycles to the endoplasmic reticulum where, due to higher pH, it releases its cargos, thereby contributing to the quality control of glyCoproteins.