Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Kyouhei Arita"'
Autor:
Kyouhei Arita
Publikováno v:
Nihon Kessho Gakkaishi. 57:53-58
Autor:
Mayuko Akaboshi, Toshiyuki Shimizu, Kyouhei Arita, Kumiko Igari, Shinsuke Kutsuna, Mamoru Sato, Hiroshi Hashimoto
Publikováno v:
Journal of Biological Chemistry. 282:1128-1135
Circadian clocks are self-sustained biochemical oscillators. The oscillator of cyanobacteria comprises the products of three kai genes (kaiA, kaiB, and kaiC). The autophosphorylation cycle of KaiC oscillates robustly in the cell with a 24-h period an
Autor:
Youngho Lee, Mamoru Sato, Bryan Knuckley, Yuan Luo, Paul R. Thompson, Michael R. Stallcup, Kyouhei Arita, Monica Bhatia
Publikováno v:
Biochemistry. 45:11727-11736
Protein arginine deiminase 4 (PAD4) is a transcriptional coregulator that catalyzes the calcium-dependent conversion of specific arginine residues in proteins to citrulline. Recently, we reported the synthesis and characterization of F-amidine, a pot
Autor:
Mamoru Sato, Yuji Hidaka, Michiyuki Yamada, Toshiyuki Shimizu, Hiroshi Hashimoto, Kyouhei Arita
Publikováno v:
Proceedings of the National Academy of Sciences. 103:5291-5296
Histone arginine methylation is a posttranslational modification linked to the regulation of gene transcription. Unlike other posttranslational modifications, methylation has generally been regarded as stable, and enzymes that demethylate histone arg
Autor:
Mamoru Sato, Kyouhei Arita
Publikováno v:
Nihon Kessho Gakkaishi. 47:268-273
Peptidylarginine deimianse 4 (PAD4) is a Ca2+-dependent enzyme that catalyzes the conversion of both arginine and mono-methyl arginine in histones into citrullines, and regulates both histone argininine methylation level and gene activity. Its gene i
Autor:
Toshiyuki Shimizu, Hiroshi Hashimoto, Katsuhiko Nakashima, Michiyuki Yamada, Mamoru Sato, Kyouhei Arita
Publikováno v:
Nature Structural & Molecular Biology. 11:777-783
Peptidylarginine deiminase 4 (PAD4) is a Ca(2+)-dependent enzyme that catalyzes the conversion of protein arginine residues to citrulline. Its gene is a susceptibility locus for rheumatoid arthritis. Here we present the crystal structure of Ca(2+)-fr
Crystal structure of the ubiquitin-associated (UBA) domain of p62 and its interaction with ubiquitin
Autor:
Masaaki Komatsu, Yu-shin Sou, Satoru Unzai, Hidehito Tochio, Kyouhei Arita, Shin Isogai, Masahiro Shirakawa, Daichi Morimoto, Keiji Tanaka, Jun Hasegawa, Takeshi Tenno
Publikováno v:
The Journal of biological chemistry. 286(36)
p62/SQSTM1/A170 is a multimodular protein that is found in ubiquitin-positive inclusions associated with neurodegenerative diseases. Recent findings indicate that p62 mediates the interaction between ubiquitinated proteins and autophagosomes, leading
Autor:
Hiroshi Kanazawa, Mamoru Sato, Kyouhei Arita, Youichi Naoe, Toshiyuki Shimizu, Hiroshi Hashimoto
Publikováno v:
The Journal of biological chemistry. 280(37)
Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding EF-hand protein that plays a role in membrane trafficking. It binds to multiple effector proteins, including Na(+)/H(+) exchangers, a serine/threonine kinase, and calc
Autor:
Takayuki Kobayashi, Yuji Obana, Naoyuki Kuboi, Yohko Kitayama, Shingo Hayashi, Masataka Oka, Naomichi Wada, Kyouhei Arita, Toshiyuki Shimizu, Mamoru Sato, Kanaly, Robert A., Shinsuke Kutsuna
Publikováno v:
Plant & Cell Physiology; Jan2016, Vol. 57 Issue 1, p105-114, 10p
Autor:
Mamoru Sato, Kyouhei Arita, Youichi Naoe, Toshiyuki Shimizu, Hiroshi Kanazawa, Hiroshi Hashimoto
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:612-613
Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na+/H+ exchangers, serine/threonine protein kinase and calcineurin