Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kayoko Fuchimura"'
Autor:
Yasunori Tawaragi, Shoji Tanaka, Mayumi Furuya, Yasuo Kitajima, Yoshiharu Minamitake, Kayoko Fuchimura, Kenji Kangawa, Naoto Minamino, Hisayuki Matsuo
Publikováno v:
Biochemical and Biophysical Research Communications. 183:964-969
Summary C-type natriuretic peptide (CNP), which was recently found to be a selective ligand for one of the two known natriuretic peptide receptor guanylyl cyclases (NPR-B), potently stimulates cGMP production in cultured rat vascular smooth muscle ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e82d0d2f8b9b199deed18ad19b24eb3f
https://doi.org/10.1016/s0006-291x(05)80284-0
https://doi.org/10.1016/s0006-291x(05)80284-0
Autor:
Kayoko Fuchimura, Hisayuki Matsuo, Naoto Minamino, Yasunori Tawaragi, Shoji Tanaka, Kenji Kangawa
Publikováno v:
Biochemical and Biophysical Research Communications. 175:645-651
We have isolated the gene for human C-type natriuretic peptide (CNP) from a human genomic library using a cloned porcine CNP genomic DNA fragment as probe. Human CNP gene consists of at least two coding blocks and an intron, and encodes a 126-residue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a339dc6bb19404dc98eff7a5793f405
https://doi.org/10.1016/0006-291x(91)91614-i
https://doi.org/10.1016/0006-291x(91)91614-i
Autor:
Kayoko Fuchimura, Yasunori Tawaragi, Naoto Minamino, Hiroshi Nakazato, Shoji Tanaka, Kenji Kangawa, Hisayuki Matsuo
Publikováno v:
Biochemical and Biophysical Research Communications. 172:627-632
Recently we isolated from porcine brain two related peptides, a 22-residue peptide (CNP-22) and its N-terminally elongated peptide (CNP-53; 53-residue), which belong to the third type of mammalian natriuretic peptide designated C-type natriuretic pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5cd7413f1699bf94a1918402b457c4e
https://doi.org/10.1016/0006-291x(90)90720-8
https://doi.org/10.1016/0006-291x(90)90720-8
Autor:
Morio Ikehara, Shigetoshi Sugio, Shoji Toda, Hiroshi Morioka, Eiko Ohtsuka, Satoshi Nishikawa, Toshio Hakoshima, Seiichi Uesugi, Tsuyoshi Kimura, Kayoko Fuchimura, Ken Ichi Tomita
Publikováno v:
"Protein Engineering, Design and Selection". 2:55-61
Recognition by ribonuclease T1 of guanine bases via multidentate hydrogen bonding and stacking interactions appears to be mediated mainly by a short peptide segment formed by one stretch of a heptapeptide, Tyr42-Asn43-Asn44-Tyr45-Glu46-Gly47- Phe48.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45c990c55e875d3a98c3a9c999e4d9e3
https://doi.org/10.1093/protein/2.1.55
https://doi.org/10.1093/protein/2.1.55
Autor:
Eiko Ohtsuka, Jeanne Adiwinata, Kayoko Fuchimura, Seiichi Uesugi, Satoshi Nishikawa, Hiroshi Morioka, Tsuyoshi Kimura, Morio Ikehara, Hyo Joon Kim, Toshiyuki Tanaka
Publikováno v:
Pure and Applied Chemistry. 59:965-968
Ribonuclease Tl (RNase Tl) specifically hydrolyzed the phosphodiester linkages of guanosine 3'-phosphate of single—stranded RNA and the cleavage occurs in a two—step reaction mechanism. It is considered that in the first step Glu 58 abstracts a p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15103aed4d757db8d219af1bf3709b6d
https://doi.org/10.1351/pac198759080965
https://doi.org/10.1351/pac198759080965
Autor:
Morio Ikehara, Satoshi Nishikawa, Eiko Ohtsuka, Toshio Hakoshima, Hiroshi Morioka, Kayoko Fuchimura, Seiichi Uesugi, Hyo Joon Kim, Ken Ichi Tomita, Toshiki Tanaka
Publikováno v:
Biochemistry. 26:8620-8624
Ribonuclease T1 (RNase T1, EC 3.1.27.3) is a guanosine-specific ribonuclease that cleaves the 3',5'-phosphodiester linkage of single-stranded RNA. It is assumed that the reaction is generated by concerted acid-base catalysis between residues Glu-58 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5bca447001f5522ebdff509e8120bac
https://doi.org/10.1021/bi00400a019
https://doi.org/10.1021/bi00400a019
Autor:
Kayoko Fuchimura, Kazuhiro Ohsuye, Yayoi Wada, Shoji Tanaka, Katsuhiko Kitano, Kensaku Mizuno, Hisayuki Matsuo
Publikováno v:
Biochemical and biophysical research communications. 150(3)
A cDNA clone encoding a precursor of a peptide C-terminal alpha-amidating enzyme (AE-I) from Xenopus laevis skin was recently isolated and sequenced in our laboratory. In this study, by using the restriction fragment of this clone as a hybridization
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f9efdb117a18107573e6e56a34ce036
https://pubmed.ncbi.nlm.nih.gov/2829895
https://pubmed.ncbi.nlm.nih.gov/2829895
Publikováno v:
Biochemical and biophysical research communications. 148(2)
The C-terminal alpha-amide formation of the peptides is one of the most important events of prohormone processing. We have recently isolated an alpha-amidating enzyme, AE-I, from Xenopus laevis skin, which is the only enzyme ever purified to homogene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa54c956cab375da7e8a0743d7d75108
https://pubmed.ncbi.nlm.nih.gov/3689360
https://pubmed.ncbi.nlm.nih.gov/3689360