Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Yasufumi Minami"'
Autor:
Yasufumi Minami, Koichi Kato, Keiji Tanaka, Eri Sakata, Shin-ichi Takata, Eiji Kurimoto, Keita Kanai, Masaaki Sugiyama, Hirokazu Yagi, Hiroki Sahashi
Publikováno v:
Biochemical and Biophysical Research Communications. 432:141-145
A major form of proteasome activator PA28 is a heteroheptamer composed of interferon-γ-inducible α and β subunits, which share approximately 50% amino acid identity and possess distinct insert loops. This activator forms a complex with the 20S pro
Publikováno v:
Human Molecular Genetics. 17:602-616
Mutations in the ubiquitously expressed gene PTEN-induced kinase 1 (Pink1) cause autosomal recessive Parkinson's disease. Pink1 encodes a putative serine/threonine kinase with an N-terminal mitochondrial targeting sequence. The mechanism that leads t
Autor:
Yasufumi Emori, Akira Nakai, Tomohiro Kurosaki, Kazuya Terasawa, Ken Matsumoto, Yasufumi Minami, Katsuhiko Yoshimatsu, Fumika Shinozaki, Miho Suzuki, Keiji Tanaka, Yoshimasa Ichikawa, Michiko Minami, Tomoki Chiba
Publikováno v:
Journal of Biological Chemistry. 281:16361-16369
Hsp90 participates in many distinct aspects of cellular functions and accomplishes these roles by interacting with multiple client proteins. To gain insight into the interactions between Hsp90 and its clients, here we have reduced the protein level o
Autor:
Katsuhiko Yoshimatsu, Yoshimasa Ichikawa, Michiko Minami, Fumika Shinozaki, Miho Suzuki, Yasufumi Minami
Publikováno v:
Biochemical and Biophysical Research Communications. 344:1315-1319
We have previously shown that the proteasome activator PA28 is essential to Hsp90-dependent protein refolding in vitro, where PA28 mediates transfer of the Hsp90-bound substrate protein to the Hsc70/Hsp40 chaperone machine for its correct refolding.
Autor:
Yasufumi Minami, Kazuya Terasawa, Keiji Tanaka, Tohru Natsume, Katsuhiko Yoshimatsu, Shun-ichiro Iemura
Publikováno v:
Molecular and Cellular Biology. 26:3378-3389
Recently, we identified a client-binding site of Cdc37 that is required for its association with protein kinases. Phage display technology and liquid chromatography-tandem mass spectrometry (which identifies a total of 33 proteins) consistently ident
Publikováno v:
European Journal of Biochemistry. 268:2520-2524
Hsp90 is able to bind partially unfolded firefly luciferase and maintain it in a refoldable state; the subsequent successive action of the 20S proteasome activator PA28, Hsc70 and Hsp40 enables its refolding. Hsp90 possesses two chaperone sites in th
Autor:
Keiji Tanaka, Yasuko Murakami, Naoki Shimbara, Nobuyuki Tanahashi, Yasufumi Minami, Klavs B. Hendil
Publikováno v:
Journal of Biological Chemistry. 275:14336-14345
Eukaryotic cells contain various types of proteasomes. Core 20 S proteasomes (abbreviated 20 S below) have two binding sites for the regulatory particles, PA700 and PA28. PA700–20 S-PA700 complexes are known as 26 S proteasomes and are ATP-dependen
Publikováno v:
Annals of the New York Academy of Sciences. 851:54-60
Publikováno v:
Journal of Biological Chemistry. 271:2641-2645
The 90-kDa stress protein, HSP90, is a major cytosolic protein ubiquitously distributed in all species. Using two substrate proteins, dihydrofolate reductase (DHFR) and firefly luciferase, we demonstrate here that HSP90 newly acquires a chaperone act
Autor:
Shogo Matsumoto, Ken Matsumoto, Fumika Shinozaki, Michiko Minami, Yukari Suzuki, Yasufumi Minami, Keiko Abe, Shuhei Zenno
Publikováno v:
Biochemical and biophysical research communications. 407(4)
Previously, we found that treatment of cells with the Hsp90 inhibitor geldanamycin (GA) leads to a substantial reduction in the number of processing bodies (P-bodies), and also alters the size and subcellular localization of stress granules. These fi