Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Koshiki Mino"'
Autor:
Yusuke Toda, Hiroaki Fujita, Koshiki Mino, Takuto Koyama, Seiji Matsuoka, Toshie Kaizuka, Mari Agawa, Shigeyuki Matsumoto, Akiko Idei, Momoko Nishikori, Yasushi Okuno, Hiroyuki Osada, Minoru Yoshida, Akifumi Takaori-Kondo, Kazuhiro Iwai
Publikováno v:
Cell Death and Disease, Vol 15, Iss 11, Pp 1-11 (2024)
Abstract The linear ubiquitin chain assembly complex (LUBAC) plays crucial roles in NF-κB signaling and protection against cell death by generating linear ubiquitin chains. Its accessory subunits, HOIL-1L and SHARPIN, regulate LUBAC function by bind
Externí odkaz:
https://doaj.org/article/13dabb45ace449559ee44638c104dbd5
Autor:
Akihiro Ito, Minoru Yoshida, Koshiki Mino, Yasumasa Matsumori, Eishin Mitsui, Hiroshi Tsujii, Shogo Yoshida, Tetsuo Onuki, Makoto Hasegawa, Mie Tsuchida, Yui Shinoda, Ryuzo Sasaki, Shuichi Wada, Tamio Mizukami
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
Scientific Reports
Scientific Reports
KDM5 family members (A, B, C and D) that demethylate H3K4me3 have been shown to be involved in human cancers. Here we performed screening for KDM5A inhibitors from chemical libraries using the AlphaScreen method and identified a battery of screening
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60cde6cebec0014218aefbf6bd56c7a5
http://link.springer.com/article/10.1038/s41598-019-46346-x
http://link.springer.com/article/10.1038/s41598-019-46346-x
Autor:
Koshiki Mino, Angie Rizzino, Nigar D. Babayeva, Tahir H. Tahirov, Tripti Shrivastava, Oxana I.Baranovskaya
Publikováno v:
Leukemia
Runx1 is required for definitive hematopoiesis and is well known for its frequent chromosomal translocations and point mutations in leukemia. Runx1 regulates a variety of genes via Ets1 activation on an Ets1•Runx1 composite DNA sequence. The struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc07fd100f4f74c9d7d46a1e5917346b
http://europepmc.org/articles/PMC4169772
http://europepmc.org/articles/PMC4169772
Autor:
Tetsuo Yoshida, Minoru Yoshida, Makoto Hasegawa, Koshiki Mino, Ryuzo Sasaki, Koichi Koseki, Tamio Mizukami, Kouji Kuzuya, Ayu Inoue, Tatsuki Kunoh, Tatsuhiro Miura, Sueharu Horinouchi, Se Won Ki
Publikováno v:
ACS Chemical Biology. 6:229-233
GEX1A is a microbial product with antitumor activity. HeLa cells cultured with GEX1A accumulated p27(Kip) and its C-terminally truncated form p27*. GEX1A inhibited the pre-mRNA splicing of p27, producing p27* from the unspliced mRNA containing the fi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6becab3842805207a7e0c3cd714ca270
https://doi.org/10.1021/cb100248e
https://doi.org/10.1021/cb100248e
Publikováno v:
Biochemical Engineering Journal. 48:315-322
Proposal of the archaea as a discrete domain shed new light on the central problems of early evolution of life and prokaryotic systematics. Recently new amino acid synthesis pathways and new amino acid synthases have been found in archaea from its ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af3fc3c41a9ae910ab0dbf6812bb7eef
https://doi.org/10.1016/j.bej.2009.10.015
https://doi.org/10.1016/j.bej.2009.10.015
Publikováno v:
Journal of Molecular Biology. 351:334-344
O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine synthetic reaction from O-phospho-l-serine and sulfide. The crystal structure of the enzyme was determine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e55681e127085ebfa6a841c64de7528
https://doi.org/10.1016/j.jmb.2005.05.064
https://doi.org/10.1016/j.jmb.2005.05.064
Autor:
Kazuhiko Ishikawa, Koshiki Mino
Publikováno v:
FEBS Letters. 551:133-138
O-Acetylserine sulfhydrylase (OASS), a pyridoxal 5'-phosphate (PLP)-dependent enzyme, catalyzes the synthesis of L-cysteine from O-acetyl-L-serine and sulfide. O-Acetyl-L-serine is labile at high temperatures at which hyperthermophilic archaea live.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f11d5ad941c070b94040c1a54cf4714f
https://doi.org/10.1016/s0014-5793(03)00913-x
https://doi.org/10.1016/s0014-5793(03)00913-x
Autor:
Kazuhiko Ishikawa, Koshiki Mino
Publikováno v:
Journal of Bacteriology. 185:2277-2284
An O -acetylserine sulfhydrylase (OASS) from the hyperthermophilic archaeon Aeropyrum pernix K1, which shares the pyridoxal 5′-phosphate binding motif with both OASS and cystathionine β-synthase (CBS), was cloned and expressed by using Escherichia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9df30c1709e74bcf4b790ce82ef9303d
https://doi.org/10.1128/jb.185.7.2277-2284.2003
https://doi.org/10.1128/jb.185.7.2277-2284.2003
Autor:
Satoshi Nishimura, Miho Hosoi, Koshiki Mino, Naoki Miyata, Shuichi Wada, Tamio Mizukami, Yukie Murakami-Yamaguchi, Shogo Ninomiya, Ryuzo Sasaki, Hiroshi Tujii, Hiroshi Narita, Yasumasa Matsumori, Takayoshi Suzuki, Koichi Koseki, Makoto Hasegawa, Mie Tsuchida
Publikováno v:
Bioscience, biotechnology, and biochemistry. 78(6)
Tissue factor pathway inhibitor-2 (TFPI-2) is a major inhibitor of extracellular matrix degradation. Decreases in TFPI-2 contribute to malignant tumor cell production, and TFPI-2 is a presumed tumor suppressor. TFPI-2 gene transcription is regulated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::876e4d8c4983148af8c7cfe5003122f4
https://pubmed.ncbi.nlm.nih.gov/25036127
https://pubmed.ncbi.nlm.nih.gov/25036127
Autor:
Naoki Eisaki, Takaharu Sakiyama, Tsuyoshi Yamanoue, Koshiki Mino, Katsuhiro Ohno, Asahi Matsuyama, Kazuhiro Nakanishi
Publikováno v:
Biotechnology Letters. 23:2051-2055
β-(Pyrazol-1-yl)-l-alanine (β-PA) was produced from l-serine and pyrazol using recombinant Escherichia coli cells expressing serine acetyltransferase and O-acetylserine sulfhydrylase-A. The amount of β-PA increased with increasing l-serine concent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7cfbb1e9e222597c46ab620a81ddab28
https://doi.org/10.1023/a:1013799915951
https://doi.org/10.1023/a:1013799915951