Yuki Okabe
Hokkaido University
9 Papers
81 Citations
Yuki Okabe is an academic researcher from Hokkaido University. The author has contributed to research in topics: Arthritis & Ectodomain. The author has an hindex of 7, co-authored 9 publications. Previous affiliations of Yuki Okabe include Fukuoka University & Kyushu University.
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Papers
Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL.
Atsushi Furukawa,Jun Kamishikiryo,Daiki Mori,Kenji Toyonaga,Yuki Okabe,Aya Toji,R. Kanda,Yasunobu Miyake,Toyoyuki Ose,Sho Yamasaki,Katsumi Maenaka +10 more
TL;DR: In this article, the crystal structures of Mincle, MCL and the Mincle-citric acid complex were reported, showing that these receptors are capable of interacting with sugar in a Ca2+-dependent manner, as observed in other C-type lectins.
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Molecular basis for LLT1 protein recognition by human CD161 protein (NKRP1A/KLRB1).
TL;DR: A new template model for the recognition mode between the KLR family members is revealed and insights are provided into the molecular mechanism underlying Th17/NK/NKT-mediated immune responses are provided.
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The long-term immunosuppressive effects of disulfide-linked HLA-G dimer in mice with collagen-induced arthritis.
Kimiko Kuroki,Kaoru Hirose,Yuki Okabe,Yuko Fukunaga,Ami Takahashi,Mitsunori Shiroishi,Mizuho Kajikawa,Shigekazu Tabata,Seiko Nakamura,Toshiyuki Takai,Satoru Koyanagi,Shigehiro Ohdo,Katsumi Maenaka +12 more
TL;DR: The HLA-G dimer is expected to be quite useful as an anti-rheumatoid arthritis agent, in small amounts with minimal side effects, and binds PIR-B, the mouse homolog of the LILRBs, with higher affinity and avidity than the monomer.
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The immunosuppressive effect of domain-deleted dimer of HLA-G2 isoform in collagen-induced arthritis mice.
Ami Takahashi,Kimiko Kuroki,Yuki Okabe,Yoshiyuki Kasai,Naoki Matsumoto,Chisato Yamada,Toshiyuki Takai,Toyoyuki Ose,Shigeyuki Kon,Tadashi Matsuda,Katsumi Maenaka +10 more
TL;DR: The results suggested that the HLA-G2 protein might be a useful biopharmaceutical for the treatment of rheumatoid arthritis by binding to inhibitory PIR-B.
21
Crystal structure of extracellular domain of human lectin‐like transcript 1 (LLT1), the ligand for natural killer receptor‐P1A
Shunsuke Kita,Haruki Matsubara,Haruki Matsubara,Yoshiyuki Kasai,Takaharu Tamaoki,Yuki Okabe,Hideo Fukuhara,Jun Kamishikiryo,Elena Krayukhina,Susumu Uchiyama,Toyoyuki Ose,Kimiko Kuroki,Katsumi Maenaka +12 more
TL;DR: In this paper, the structure of the ectodomain of the lectin-like transcript 1 (LLT1) was reported and the residues of this face were relatively conserved with another CTLR, keratinocyte-associated C-type lectin, which binds to the CTLr member, NKp65.