Shigeyuki Yokoyama
University of Tokyo
1125 Papers
10.8K Citations
Shigeyuki Yokoyama is an academic researcher from University of Tokyo. The author has contributed to research in topics: Transfer RNA & Thermus thermophilus. The author has an hindex of 107, co-authored 1113 publications. Previous affiliations of Shigeyuki Yokoyama include University of Tsukuba & RIKEN Brain Science Institute.
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Papers
Identification of a Second DNA Binding Site in the Human Rad52 Protein
Wataru Kagawa,Ako Kagawa,Kengo Saito,Shukuko Ikawa,Takehiko Shibata,Hitoshi Kurumizaka,Shigeyuki Yokoyama +6 more
TL;DR: The present study has identified a novel DNA binding site within Rad52 by a structure-based alanine scan mutagenesis that impaired the ability of the Rad52-single-stranded DNA complex to form a ternary complex with double-Stranded DNA and subsequently catalyze the formation of D-loops.
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13-Deoxytedanolide, a marine sponge-derived antitumor macrolide, binds to the 60S large ribosomal subunit.
Shinichi Nishimura,Shigeki Matsunaga,Minoru Yoshida,Hiroshi Hirota,Shigeyuki Yokoyama,Nobuhiro Fusetani +5 more
TL;DR: Results indicate that 13-deoxytedanolide is a potent protein synthesis inhibitor and is the first macrolide to inhibit the eukaryotic ribosome.
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The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.
Akihiko Arakawa,Noriko Handa,Noboru Ohsawa,Meiri Shida,Takanori Kigawa,Fumiaki Hayashi,Mikako Shirouzu,Shigeyuki Yokoyama +7 more
TL;DR: BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding and reduce the affinity of the NBD for ADP.
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Intra- and inter-nucleosomal interactions of the histone H4 tail revealed with a human nucleosome core particle with genetically-incorporated H4 tetra-acetylation.
Masatoshi Wakamori,Yoshifumi Fujii,Noriyuki Suka,Mikako Shirouzu,Kensaku Sakamoto,Takashi Umehara,Shigeyuki Yokoyama +6 more
TL;DR: The present study revealed that the H4 tetra-acetylation impairs NCP self-association by changing the interactions of the H 4 tail with DNA, and is the first demonstration of crystallization quality NCPs reconstituted with genuine PTMs.
Cell Cycle-dependent Phosphorylation, Nuclear Localization, and Activation of Human Condensin
TL;DR: The results suggest that condensin functions in somatic cells are regulated by phosphorylation in two ways during the cell cycle; the phosphorylated of specific sites correlates with the chromosomal targeting of condensIn, and its biochemical activity is stimulated byosphorylation.
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