H
Hiroyuki Kawahara
Researcher at Tokyo Metropolitan University
Publications - 71
Citations - 2013
Hiroyuki Kawahara is an academic researcher from Tokyo Metropolitan University. The author has contributed to research in topics: Proteasome & Ubiquitin. The author has an hindex of 25, co-authored 69 publications receiving 1848 citations. Previous affiliations of Hiroyuki Kawahara include University of Tokyo & Hokkaido University.
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Journal ArticleDOI
Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
Eri Sakata,Yoshiki Yamaguchi,Eiji Kurimoto,Jun Kikuchi,Shigeyuki Yokoyama,Shingo Yamada,Hiroyuki Kawahara,Hideyoshi Yokosawa,Nobutaka Hattori,Yoshikuni Mizuno,Keiji Tanaka,Koichi Kato +11 more
TL;DR: The findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10‐binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR‐JP.
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Growth Retardation in Mice Lacking the Proteasome Activator PA28γ
Shigeo Murata,Hiroyuki Kawahara,Shigeto Tohma,Kazuhiko Yamamoto,Masanori Kasahara,Yo-ichi Nabeshima,Keiji Tanaka,Tomoki Chiba +7 more
TL;DR: PA28γ functions as a regulator of cell proliferation and body growth in mice and it is suggested that neither PA28α nor PA28β compensates for the PA28γ deficiency.
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BAG-6 is essential for selective elimination of defective proteasomal substrates.
Ryosuke Minami,Atsuko Hayakawa,Hiroki Kagawa,Hiroki Kagawa,Yuko Yanagi,Hideyoshi Yokosawa,Hiroyuki Kawahara,Hiroyuki Kawahara +7 more
TL;DR: The ubiquitin-like protein BAG-6 protects cells from newly synthesized misfolded proteins by tethering them to the proteasome.
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Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse development.
Jun Hamazaki,Katsuhiro Sasaki,Hiroyuki Kawahara,Shin-ichi Hisanaga,Keiji Tanaka,Shigeo Murata +5 more
TL;DR: It is demonstrated that Rpn10-mediated degradation of ubiquitinated proteins, catalyzed by UIMs, is indispensable for mammalian life.
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Intracellular Calcium Mobilization Regulates the Activity of 26 S Proteasome during the Metaphase-Anaphase Transition in the Ascidian Meiotic Cell Cycle
TL;DR: Examination of changes in the activities and in the amounts of proteasomes during progression of the ascidian meiotic division cycle suggests that 26 S proteasome activity is regulated through interconversion between the 26 S and 20 S prote asomes induced by intracellular calcium mobilization during the meiotic metaphase-anaphase transition.