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Yoshiki Yamaguchi
Researcher at Tohoku Pharmaceutical University
Publications - 270
Citations - 7268
Yoshiki Yamaguchi is an academic researcher from Tohoku Pharmaceutical University. The author has contributed to research in topics: Glycan & Glycosylation. The author has an hindex of 41, co-authored 247 publications receiving 6186 citations. Previous affiliations of Yoshiki Yamaguchi include University of Tokyo & Max Planck Society.
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NIRF/UHRF2 occupies a central position in the cell cycle network and allows coupling with the epigenetic landscape
TL;DR: It is proposed the new paradigm that NIRF produces the extreme diversity in the network wiring that helps the diversity of Waddington's canals.
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Structural diversity and changes in conformational equilibria of biantennary complex-type N-glycans in water revealed by replica-exchange molecular dynamics simulation.
TL;DR: These simulations show that an N-glycan modification like the bisecting GlcNAc selects a certain "key" (or group of "keys") within the framework of the "bunch of keys" mechanism.
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Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain.
Masato Akutsu,Masato Akutsu,Masato Kawasaki,Yohei Katoh,Tomoo Shiba,Yoshiki Yamaguchi,Ryuichi Kato,Ryuichi Kato,Koichi Kato,Kazuhisa Nakayama,Soichi Wakatsuki,Soichi Wakatsuki +11 more
TL;DR: It is demonstrated that the three‐helix bundle of Tom1‐GAT has two ubiquitin‐binding sites recognizing the hydrophobic Ile44 surface of Ubiquitin.
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Ultra-high field NMR studies of antibody binding and site-specific phosphorylation of alpha-synuclein.
Hiroaki Sasakawa,Eri Sakata,Yoshiki Yamaguchi,Masami Masuda,Tetsuya Mori,Eiji Kurimoto,Takeshi Iguchi,Shin-ichi Hisanaga,Takeshi Iwatsubo,Masato Hasegawa,Koichi Kato,Koichi Kato +11 more
TL;DR: An ultra-high field NMR study ofalpha-synuclein, an intrinsically disordered protein identified as the major component of the Lewy bodies, and characterized conformational effects of phosphorylation at Ser129 of alpha- synuclein.
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An Alkynyl-Fucose Halts Hepatoma Cell Migration and Invasion by Inhibiting GDP-Fucose-Synthesizing Enzyme FX, TSTA3.
Yasuhiko Kizuka,Miyako Nakano,Yoshiki Yamaguchi,Kazuki Nakajima,Ritsuko Oka,Keiko Sato,Chien-Tai Ren,Tsui-Ling Hsu,Chi-Huey Wong,Naoyuki Taniguchi +9 more
TL;DR: The glycan analysis using lectin and mass spectrometry demonstrated that 6-Alk-Fuc is a potent and general inhibitor of cellular fucosylation, with much higher potency than the existing inhibitor, 2-fluoro-fucose (2-F-Fuk).