Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Miho Manzoku"'
Autor:
Rihito Morita, Ryoji Masui, Miho Manzoku, Seiki Kuramitsu, Kenji Fukui, Akio Ebihara, Atsuhiro Shimada
Publikováno v:
Extremophiles. 19:775-785
Hydrogen peroxide (H2O2) produces hydroxyl radicals that directly attack a variety of biomolecules and cause severe cellular dysfunction. An extremely thermophilic bacterium, Thermus thermophilus HB8, possesses at least three enzymes that can scaveng
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e60389ee95db5933828942b9490ec102
https://doi.org/10.1007/s00792-015-0753-2
https://doi.org/10.1007/s00792-015-0753-2
Publikováno v:
Journal of Biological Chemistry. 285:10777-10785
ComA of Streptococcus is a member of the bacteriocin-associated ATP-binding cassette transporter family and is postulated to be responsible for both the processing of the propeptide ComC and secretion of the mature quorum-sensing signal. The 150-amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8acda7009f0c90d390706dddfe79ba39
https://doi.org/10.1074/jbc.m109.093781
https://doi.org/10.1074/jbc.m109.093781
Autor:
Akio Ebihara, Mayumi Kanagawa, Seiki Kuramitsu, Akeo Shinkai, Hitoshi Iino, Miho Manzoku, Shigeyuki Yokoyama
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 71:2097-2101
Crystal structure of uncharacterized protein TTHA1756 from Thermus thermophilus HB8: Structural variety in UPF0150 family proteins Akio Ebihara, Miho Manzoku, Hitoshi Iino, Mayumi Kanagawa, Akeo Shinkai, Shigeyuki Yokoyama, and Seiki Kuramitsu* 1 RIK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90642108c603631d6517a2f1493bbd22
https://doi.org/10.1002/prot.22018
https://doi.org/10.1002/prot.22018
Publikováno v:
Biochemical and biophysical research communications. 399(3)
A rapid temperature downshift induces the expression of many proteins termed ‘cold-induced’ proteins. Although some of these proteins are known to participate in metabolism, transcription, translation and protein folding, processes that are affec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e9729eb3a77739fafd3ed781229ccaf
https://pubmed.ncbi.nlm.nih.gov/20655297
https://pubmed.ncbi.nlm.nih.gov/20655297
Publikováno v:
Biochemistry. 46(44)
Monofunctional histidinol phosphate phosphatase from Thermus thermophilus HB8, which catalyzes the dephosphorylation of l-histidinol phosphate, belongs to the PHP family, together with the PHP domain of bacterial DNA polymerase III and family X DNA p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eba419b0e80118f999bd42fe32076ea
https://pubmed.ncbi.nlm.nih.gov/17929834
https://pubmed.ncbi.nlm.nih.gov/17929834
Autor:
Lirong Chen, Kazutaka Murayama, Chie Takemoto, Mikako Shirouzu, Akio Ebihara, Zhi-Jie Liu, Miho Manzoku, Seiki Kuramitsu, S. Kishishita, Tomomi Uchikubo-Kamo, Yong Xie, Bi-Cheng Wang, Shigeyuki Yokoyama
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 63(Pt 12)
The gene encoding TTHA1544 is a singleton found in the Thermus thermophilus HB8 genome and encodes a 131-amino-acid protein. The crystal structure of TTHA1544 has been determined at 2.0 A resolution by the single-wavelength anomalous dispersion metho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e93f8a2b2da5536d0af2b685b13f8e5
https://pubmed.ncbi.nlm.nih.gov/18084077
https://pubmed.ncbi.nlm.nih.gov/18084077
Autor:
Nobuo Okazaki, Shigeyuki Yokoyama, Miho Manzoku, Akeo Shinkai, Maki Kumei, Mikako Shirouzu, Seiki Kuramitsu
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 63(Pt 3)
TTHA0281 is a hypothetical protein from Thermus thermophilus HB8 that belongs to an uncharacterized protein family, UPF0150, in the Pfam database and to COG1598 in the National Center for Biotechnology Information Database of Clusters of Orthologous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ef43324a5714c0b4e63b98a60078770
https://pubmed.ncbi.nlm.nih.gov/17329807
https://pubmed.ncbi.nlm.nih.gov/17329807
Autor:
Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, Yoshitaka Bessho, Kazutaka Murayama, Motoyuki Hattori, Shigeyuki Yokoyama, Eiichi Mizohata, Miho Manzoku
Publikováno v:
Proteins. 61(4)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c467b6f80ad9aea979d8bedef27dd51f
https://pubmed.ncbi.nlm.nih.gov/16250002
https://pubmed.ncbi.nlm.nih.gov/16250002