Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Masae Taniguchi"'
Autor:
Atsushi Nakagawa, Harumi Hosaka, Makoto Kimura, Masae Taniguchi, Takashi Nakashima, Isao Tanaka
Publikováno v:
The Ribosome
This chapter focuses on the crystal structure of the RNA binding domain of BstL2, and discusses its structure from functional and evolutionary points of view. Site-directed mutagenesis of Arg86 or Arg155 significantly diminished RNA binding affinity,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0276295457364611f093c038252849db
https://doi.org/10.1128/9781555818142.ch9
https://doi.org/10.1128/9781555818142.ch9
Autor:
Harumi Hosaka, Makoto Kimura, Takashi Nakashima, Masae Taniguchi, Atsushi Nakagawa, Isao Tanaka
Publikováno v:
The EMBO Journal. 18:1459-1467
Ribosomal protein L2 is the largest protein component in the ribosome. It is located at or near the peptidyl transferase center and has been a prime candidate for the peptidyl transferase activity. It binds directly to 23S rRNA and plays a crucial ro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcf2fddb93bfa16724cdb09715c568f4
https://doi.org/10.1093/emboj/18.6.1459
https://doi.org/10.1093/emboj/18.6.1459
Autor:
Hiroshi Sugimoto, Masae Taniguchi, Masaki Suzuki, Jun Nishihira, Isao Tanaka, Atsushi Nakagawa
Publikováno v:
Journal of Structural Biology. 120:105-108
D-Dopachrome tautomerase catalyzes the conversion of D-dopachrome to 5,6-dihydroxyindole. This protein has amino acid sequence homology with that of macrophage migration inhibitory factor (MIF), suggesting a pathophysiological role of this protein in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2ef2af9af56cba01d41a196a481c56f
https://doi.org/10.1006/jsbi.1997.3904
https://doi.org/10.1006/jsbi.1997.3904
Autor:
Masaki Suzuki, Isao Tanaka, Hiroshi Sugimoto, Masae Taniguchi, Jun Nishihira, Atsushi Nakagawa
Publikováno v:
Biochemistry. 38(11)
D-Dopachrome tautomerase shares a low homologous amino acid sequence (33% homology) with the macrophage migration inhibitory factor (MIF) and possesses similar tautomerase activity as well. MIF is a cytokine involved in inflammatory reactions and imm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cc4e512bfbaaeb802aad1310c9b9fb7
https://pubmed.ncbi.nlm.nih.gov/10079069
https://pubmed.ncbi.nlm.nih.gov/10079069
Autor:
ISAO TANAKA, ATSUSHI NAKAGAWA, TAKASHI NAKASHIMA, MASAE TANIGUCHI, HARUMI HOSAKA, MAKOTO KIMURA
Publikováno v:
Ribosome; 2000, p85-92, 8p