Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Seiko Shimamoto"'
Autor:
Hiroshi Tokumitsu, Kiyohito Kato, Kohji Moriishi, Seiko Shimamoto, Yoshiharu Matsuura, Ryoji Kobayashi, Kyoko Mori, Hisaaki Miyoshi, Joji Tani, Mitsumasa Tsuchiya, Tsutomu Masaki, Tomohito Fujimoto, Nobuyuki Kato
Publikováno v:
Liver International. 33:1008-1018
Background & Aim FKBP8/FKBP38 is a unique FK506-binding protein with a C-terminal membrane anchor and localizes at the outer membranes of mitochondria and the endoplasmic reticulum. Similar to some immunophilins, such as FKBP51, FKBP52 and Cyclophili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::853157bbf2b15e541c66ef706659df0c
https://doi.org/10.1111/liv.12151
https://doi.org/10.1111/liv.12151
Publikováno v:
Journal of Biological Chemistry. 288:7158-7168
The U-box E3 ubiquitin ligase CHIP (C terminus of Hsc70-interacting protein) binds Hsp90 and/or Hsp70 via its tetratricopeptide repeat (TPR), facilitating ubiquitination of the chaperone-bound client proteins. Mechanisms that regulate the activity of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18d3ab90c5f31c8dbd4d21e6f6d09f90
https://doi.org/10.1074/jbc.m112.436758
https://doi.org/10.1074/jbc.m112.436758
Autor:
Hiroshi Tokumitsu, Masaaki Tokuda, Fuminori Yamaguchi, Seiko Shimamoto, Mitsumasa Tsuchiya, Tomohito Fujimoto, Ryoji Kobayashi
Publikováno v:
The Tohoku journal of experimental medicine. 240(1)
Oxidative stress is the consequence of an imbalance between the production of harmful reactive oxygen species and the cellular antioxidant system for neutralization, and it activates multiple intracellular signaling pathways, including apoptosis sign
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0ec6ec087d12bb851ad4115e6e52e72
https://pubmed.ncbi.nlm.nih.gov/27600583
https://pubmed.ncbi.nlm.nih.gov/27600583
Autor:
Seiko Shimamoto, Hiroshi Tokumitsu, Fuminori Yamaguchi, Masaaki Tokuda, Ryoji Kobayashi, Yoshinori Umeda, Mitsumasa Tsuchiya
Publikováno v:
Journal of Biological Chemistry. 287:13787-13798
PP5 is a unique member of serine/threonine phosphatases comprising a regulatory tetratricopeptide repeat (TPR) domain and functions in signaling pathways that control many cellular responses. We reported previously that Ca2+/S100 proteins directly as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c465b382b621ada125649236f7f35d8
https://doi.org/10.1074/jbc.m111.329771
https://doi.org/10.1074/jbc.m111.329771
Publikováno v:
FEBS Letters. 584:1119-1125
S100 proteins are a subfamily of the EF-hand type calcium sensing proteins, the exact biological functions of which have not been clarified yet. In this work, we have identified Cyclophilin 40 (CyP40) and FKBP52 (called immunophilins) as novel target
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f2b623d65feaa3178bf6d6d8d498542
https://doi.org/10.1016/j.febslet.2010.02.055
https://doi.org/10.1016/j.febslet.2010.02.055
Autor:
Hiroshi Tokumitsu, Fumikazu Oohira, Ryoji Kobayashi, Seiko Shimamoto, Maki Takata, Masaaki Tokuda
Publikováno v:
Journal of Biological Chemistry. 283:28246-28258
S100A2 and S100A6 interact with several target proteins in a Ca2+-regulated manner. However, the exact intracellular roles of the S100 proteins are unclear. In this study we identified Hsp70/Hsp90-organizing protein (Hop) and kinesin light chain (KLC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13067b1873ea7f5cd1839efb4a95f7cb
https://doi.org/10.1074/jbc.m801473200
https://doi.org/10.1074/jbc.m801473200
Autor:
Michie Moriyama, Shiro Kato, Kenji Urakami, Keishi Hamasaki, Atsushi Masayama, Ryuichi Moriyama, Seiko Shimamoto, Tohru Yoshimura, Shio Makino
Publikováno v:
Genes & Genetic Systems. 81:227-234
In Clostridium perfringens S40, spore germination-specific enzymes are synthesized during sporulation. Previous reports have demonstrated that two cortex-lytic enzymes, SleC and SleM, and a component of germination-specific protease, CspC, are locate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::155f1eab9598b093a0ef96fb982b3f6d
https://doi.org/10.1266/ggs.81.227
https://doi.org/10.1266/ggs.81.227
Publikováno v:
European Journal of Biochemistry. 271:3765-3775
In this report, we have focused our attention on identifying intracellular mammalian proteins that bind S100A12 in a Ca2+-dependent manner. Using S100A12 affinity chromatography, we have identified cytosolic NADP+-dependent isocitrate dehydrogenase (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abe7661e504fde2c65c9dd1f991fbf4e
https://doi.org/10.1111/j.1432-1033.2004.04318.x
https://doi.org/10.1111/j.1432-1033.2004.04318.x
Autor:
Masato Kaji, Osamu Matsushita, Shigeru Miyata, Akinobu Okabe, Akihisa Takamizawa, Seiko Shimamoto, Eiji Tamai, Yuki Taniguchi
Publikováno v:
Protein Expression and Purification. 36:70-75
A “large” sialidase isozyme (NanI) from Clostridium perfringens is a representative microbial sialidase with broad substrate specificity, being used for the analysis of sialoglycoconjugates. It is also a possible virulence factor. However, purifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74b2d6c06cf615abcee157169f668554
https://doi.org/10.1016/j.pep.2004.03.004
https://doi.org/10.1016/j.pep.2004.03.004
Autor:
Seiko Shimamoto, Masaaki Tokuda, Mitsumasa Tsuchiya, Ryoji Kobayashi, Hiroshi Tokumitsu, Fuminori Yamaguchi, Tomohito Fujimoto
Publikováno v:
International journal of molecular medicine. 34(6)
S100 proteins bind to numerous target proteins, as well as other S100 proteins and activate signaling cascades. S100 proteins can be modified by various post-translational modifications, such as phosphorylation, methylation and acetylation. In additi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65a67bd16f5b8447c6ca6f7e1c5ce2b9
https://pubmed.ncbi.nlm.nih.gov/25269953
https://pubmed.ncbi.nlm.nih.gov/25269953