Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Yoshikazu Tomisugi"'
Publikováno v:
Journal of Biological Chemistry. 279:47320-47325
CooA is a homodimeric transcriptional activator from Rhodospirillum rubrum containing one heme in each subunit. CO binding to the heme in its sensor domain activates CooA, facilitating the binding to DNA by its DNA-binding domain. The C-helix links t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc2f8cd76c9924c891cb1416054b0b3a
https://doi.org/10.1074/jbc.m407766200
https://doi.org/10.1074/jbc.m407766200
Autor:
Daisuke Ryu, Hiroko Tsutsumi, Yoshikazu Tomisugi, Anthony J. Wilkinson, Tadayuki Uno, Yoshinobu Ishikawa, Hideaki Sato, Takashi Hayashi
Publikováno v:
Journal of Biological Chemistry. 279:5886-5893
Amino acid residues in the ligand binding pocket of human neuroglobin have been identified by site-directed mutagenesis and their properties investigated by resonance Raman and flash photolysis methods. Wild-type neuroglobin has been shown to have si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::382a3e482dd4689d2ee6f74580fe914c
https://doi.org/10.1074/jbc.m311748200
https://doi.org/10.1074/jbc.m311748200
Publikováno v:
Chemical and Pharmaceutical Bulletin. 51:899-903
A series of tentacle porphyrins having four aminoalkyl groups at the periphery was synthesized, and the DNA binding properties were investigated by absorption and circular dichroism (CD) spectroscopic methods. The aminopropyl chain was found to facil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ea11d8444a120ff170a35565cfc01d3
https://doi.org/10.1248/cpb.51.899
https://doi.org/10.1248/cpb.51.899
Autor:
Tadayuki Uno, Yoshikazu Tomisugi, Tomoko Shikimi, Yoshinobu Ishikawa, Katsumasa Aoki, Yumi Hiranuma
Publikováno v:
Biochemistry. 41:13059-13066
The binding of the copper(II) complex of water-soluble meso-tetrakis(N-methylpyridinium-4-yl)porphyrin (TMPyP) to double-helical polynucleotides has been studied by optical absorption, circular dichroism (CD), and resonance Raman spectroscopic method
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b3400effdfb38b0975a3873f58d012d
https://doi.org/10.1021/bi026139z
https://doi.org/10.1021/bi026139z
Autor:
Keiji Tanaka, Noritake Yasuoka, Yukio Morimoto, Yoshikazu Tomisugi, Masaki Unno, Tomitake Tsukihara, Tsunehiro Mizushima
Publikováno v:
Structure. 10(5):609-618
The 20S proteasome is the catalytic portion of the 26S proteasome. Constitutively expressed mammalian 20S proteasomes have three active subunits, beta 1, beta 2, and beta 5, which are replaced in the immunoproteasome by interferon-gamma-inducible sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3119ede9f7e524022f9e3e1430d4a689
Autor:
Yoshikazu Tomisugi, Tomitake Tsukihara, Masaki Unno, Noritake Yasuoka, Keiji Tanaka, Yukio Morimoto, Tsunehiro Mizushima, Nobuyuki Tanahashi
Publikováno v:
Journal of Biochemistry. 127:941-943
20S proteasomes from higher eukaryotes have immunological functions rather than those from archibacteria or yeast. To clarify the mechanism of the sorting and production of antigen-presenting peptides, it is important and worthwhile to determine the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfa1ba953318b5bc7b21068311b286cd
https://doi.org/10.1093/oxfordjournals.jbchem.a022709
https://doi.org/10.1093/oxfordjournals.jbchem.a022709
Publikováno v:
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme. 50
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::73f6ec32e424c207b6881683b14bc7ed
https://pubmed.ncbi.nlm.nih.gov/16104584
https://pubmed.ncbi.nlm.nih.gov/16104584
Autor:
Yoshikazu Tomisugi, Kimiko Watanabe, Yohei Hoashi, Tadayuki Uno, Yoshinobu Ishikawa, Taku Yamashita
Publikováno v:
The Journal of biological chemistry. 279(20)
CooA is a CO-dependent transcription factor of the bacterium Rhodospirillum rubrum that contains a six-coordinate heme. It has as its heme axial ligands Pro(2) and Cys(75) in the ferric state and Pro(2) and His(77) in the ferrous state. To probe the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::006b5769ffafa8b75e01c63d7f5b1749
https://pubmed.ncbi.nlm.nih.gov/15026411
https://pubmed.ncbi.nlm.nih.gov/15026411
Autor:
Tadayuki, Uno, Daisuke, Ryu, Hiroko, Tsutsumi, Yoshikazu, Tomisugi, Yoshinobu, Ishikawa, Anthony J, Wilkinson, Hideaki, Sato, Takashi, Hayashi
Publikováno v:
The Journal of biological chemistry. 279(7)
Amino acid residues in the ligand binding pocket of human neuroglobin have been identified by site-directed mutagenesis and their properties investigated by resonance Raman and flash photolysis methods. Wild-type neuroglobin has been shown to have si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bc3007e01522b038ef8df44fc1671025
https://pubmed.ncbi.nlm.nih.gov/14645216
https://pubmed.ncbi.nlm.nih.gov/14645216
Autor:
Rikiharu Sakamoto, Yoshikazu Tomisugi, Tadayuki Uno, Anthony J. Wilkinson, Yoshinobu Ishikawa
Publikováno v:
Biochemistry. 42(34)
A ligand binding pocket has been created on the proximal side of the heme in porcine myoglobin by site-directed mutagenesis. Our starting point was the H64V/V68H double mutant which has been shown to have bis-histidine (His68 and His93) heme coordina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c07fb5a4fdc91c99c599b75782f7757
https://pubmed.ncbi.nlm.nih.gov/12939147
https://pubmed.ncbi.nlm.nih.gov/12939147