Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Tomoharu Gomi"'
Autor:
Takahiro Shimizu, Tomoharu Gomi, Kazuhiro Tsukada, Hideki Sakai, Yuji Takahashi, Hiroshi Tsuji, Shun-ya Awaka, Kyosuke Fujita, Takuto Fujii
Publikováno v:
FEBS Letters. 587:3898-3905
ERp57 is a ubiquitous ER chaperone that has disulfide isomerase activity. Here, we found that both ERp57 and gastric H(+),K(+)-ATPase are expressed in a sample derived from the apical canalicular membranes of parietal cells. Overexpression of ERp57 i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::789124ef4a5204a3f62ab8bcba5f011c
https://doi.org/10.1016/j.febslet.2013.10.030
https://doi.org/10.1016/j.febslet.2013.10.030
Autor:
Hiroki Mano, Oliver Vugrek, Masaharu Urakaze, Hirofumi Ogawa, Tomoharu Gomi, Hirofumi Taki, Kouichiro Shinoda, Isao Usui, Bryan Knuckley, Tatsurou Miyahara, Hisashi Mori, Eiji Sugiyama, Ayumi Tanaka, Hiroyuki Hounoki, Tetsuya Ishimoto, Paul R. Thompson, Kazuyuki Tobe, Ran Inoue, Kazuya Hirata
Publikováno v:
Advances in Bioscience and Biotechnology
The murine peptidylarginine deiminase (PAD) has five isoforms encoded by different genes and partici- pates in a variety of cellular functions through the citrullination of target proteins. The crystal structure of human PAD4 with a dimeric form was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b6673b95ea6df01e6735d1f7306ef7d
https://doi.org/10.4236/abb.2011.24044
https://doi.org/10.4236/abb.2011.24044
Autor:
H Oda, Kyoko Hayashi, Ikuo Saiki, Hiroshi Ochiai, Toshiro Miwa, Tomoharu Gomi, Masashi Kobayashi, Hisashi Mori, Fusao Takusagawa, Takashi Fujishita, Shunro Endo, Henry C. Pitot, Mikio Nishizawa, Keiichi Koizumi, Yumiko Hayakawa, Muneharu Maruyama, Hiroaki Sakurai, Hirofumi Ogawa
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764:961-971
A cDNA clone similar to human serine dehydratase (SDH) is deposited in the GenBank/EMBL databases, but its structural and functional bases remain unknown. Despite the occurrence of mRNA, the expected protein level was found to be low in cultured cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4266cddb9626eca574c3efab06fcada
https://doi.org/10.1016/j.bbapap.2006.02.010
https://doi.org/10.1016/j.bbapap.2006.02.010
Autor:
Hirofumi Ogawa, Junichi Komoto, Tomoharu Gomi, Fusao Takusagawa, Taro Yamada, Yoshimi Takata, Motoji Fujioka
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 37:2417-2435
S-adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the hydrolysis of S-adenosylhomocysteine (AdoHcy) to form adenosine and homocysteine. The crystal structure of the K185N mutated enzyme, which has weak catalytic activity (0.1%), has been determi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5efeee89a5fca249edb0766b6ee9d4ad
https://doi.org/10.1016/j.biocel.2005.06.009
https://doi.org/10.1016/j.biocel.2005.06.009
Autor:
Junichi Komoto, Taro Yamada, Kiyoshi Konishi, Tomoharu Gomi, Fusao Takusagawa, Yoshimi Takata, Hirofumi Ogawa, Motoji Fujioka
Publikováno v:
Biochemistry. 43:14385-14394
Guanidinoacetate methyltransferase (GAMT) is the enzyme that catalyzes the last step of creatine biosynthesis. The enzyme is found in abundance in the livers of all vertebrates. The intact GAMT from recombinant rat liver has been crystallized with an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b385737ee4aa7f0442ad3b8e025fa09e
https://doi.org/10.1021/bi0486785
https://doi.org/10.1021/bi0486785
Autor:
Taro Yamada, Fusao Takusagawa, Hirofumi Ogawa, Kiyoshi Konishi, Junichi Komoto, Yoshimi Takata, Yafei Huang, Motoji Fujioka, Tomoharu Gomi
Publikováno v:
Biochemistry. 42:8394-8402
Methyltransfer reactions are some of the most important reactions in biological systems. Glycine N-methyltransferase (GNMT) catalyzes the S-adenosyl-l-methionine- (SAM-) dependent methylation of glycine to form sarcosine. Unlike most SAM-dependent me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f2b331f954a50704e75e08d91b7bb6e
https://doi.org/10.1021/bi034245a
https://doi.org/10.1021/bi034245a
Autor:
Taro Yamada, Fusao Takusagawa, Tomoharu Gomi, Kiyoshi Konishi, Yafei Huang, Hirofumi Ogawa, Yoshimi Takata, Junichi Komoto, Motoji Fujioka
Publikováno v:
Journal of Molecular Biology. 320:223-235
Guanidinoacetate methyltransferase (GAMT) is the enzyme that catalyzes the last step of creatine biosynthesis. The enzyme is found in abundance in the livers of all vertebrates. Recombinant rat liver GAMT has been crystallized with S-adenosylhomocyst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5a482f9d5c6ec4b8bdb4a9e9b585fa0
https://doi.org/10.1016/s0022-2836(02)00448-5
https://doi.org/10.1016/s0022-2836(02)00448-5
Autor:
Yafei Huang, Motoji Fujioka, Taro Yamada, Tomoharu Gomi, Hirofumi Ogawa, Yoshimi Takata, Junichi Komoto, Fusao Takusagawa
Publikováno v:
Journal of Biological Chemistry. 277:22670-22676
S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the hydrolysis ofS-adenosylhomocysteine to form adenosine and homocysteine. On the bases of crystal structures of the wild type enzyme and the D244E mutated enzyme complexed with 3′-keto-adenos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09388a28833d2deeb33884b7d1ca2077
https://doi.org/10.1074/jbc.m201116200
https://doi.org/10.1074/jbc.m201116200
Autor:
Hirofumi Ogawa, Junichi Komoto, Fusao Takusagawa, Douglas R. Powell, Yoshimi Takata, Yafei Huang, Tomoharu Gomi, Motoji Fujioka
Publikováno v:
Journal of Biological Chemistry. 277:7477-7482
d-Eritadenine (DEA) is a potent inhibitor (IC50 = 7 nm) ofS-adenosyl-l-homocysteine hydrolase (AdoHcyase). Unlike cyclic sugar Ado analogue inhibitors, including mechanism-based inhibitors, DEA is an acyclic sugar Ado analogue, and the C2′ and C3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55253f098e37c1acb611bffcd2c2ac53
https://doi.org/10.1074/jbc.m109187200
https://doi.org/10.1074/jbc.m109187200
Publikováno v:
Microbiology and Immunology. 45:497-506
Cytolethal distending toxin (CDT) has been found in various pathogenic bacterial species and causes a cell distending and a G2 arrest against eukaryotic cells. All the cdtABC genes, which encode CDT, are known to be required for the CDT activities al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5a87ec79c3313d095d7f4c306ad75b2
https://doi.org/10.1111/j.1348-0421.2001.tb02650.x
https://doi.org/10.1111/j.1348-0421.2001.tb02650.x