Zobrazeno 1 - 10
of 89
pro vyhledávání: '"Ikuo Matsui"'
Autor:
Hideshi Yokoyama, Ikuo Matsui
Publikováno v:
FEBS Open Bio, Vol 13, Iss 5, Pp 926-937 (2023)
Currently, information on the higher‐order structure of Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH)‐domain proteins is limited. Briefly, the coordinate information (Refined PH1511.pdb) of the stomatin ortholog, PH1511 monomer, was obtained
Externí odkaz:
https://doaj.org/article/b3fba002d8bc4564a01f5ac052efdf8c
Publikováno v:
Biochemistry and Biophysics Reports, Vol 32, Iss , Pp 101384- (2022)
Stomatin is a major integral membrane protein in human erythrocytes. In a form of hemolytic anemia known as hereditary stomatocytosis, stomatin is deficient in the erythrocyte membrane due to mis-trafficking. It is a member of stomatin, prohibitin, f
Externí odkaz:
https://doaj.org/article/ab2311124b6a46bf98e29bf45959a377
Autor:
Hideshi Yokoyama, Ikuo Matsui
Publikováno v:
FEBS Open Bio, Vol 4, Iss C, Pp 804-812 (2014)
Stomatin, prohibitin, flotillin, and HflK/C (SPFH) domain proteins are found in the lipid raft microdomains of various cellular membranes. Stomatin/STOPP (stomatin operon partner protein) gene pairs are present in both archaeal and bacterial species,
Externí odkaz:
https://doaj.org/article/fdb8ccedd2454a4eb0b4e02e5c5462f7
Publikováno v:
Life, Vol 3, Iss 3, Pp 375-385 (2013)
Archaea-specific D-family DNA polymerase (PolD) forms a dimeric heterodimer consisting of two large polymerase subunits and two small exonuclease subunits. According to the protein-protein interactions identified among the domains of large and small
Externí odkaz:
https://doaj.org/article/7c7415998a0a4865b584b99e78300834
Autor:
Hideshi Yokoyama, Ikuo Matsui
Publikováno v:
FEBS Open Bio. 13:926-937
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b2853b360948f5e9992220ad66c99cb
https://doi.org/10.1002/2211-5463.13593
https://doi.org/10.1002/2211-5463.13593
Autor:
Hideshi, Yokoyama, Nanami, Kamei, Keijiro, Konishi, Kodai, Hara, Yoshinobu, Ishikawa, Ikuo, Matsui, Patrick, Forterre, Hiroshi, Hashimoto
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 90:1434-1442
Oligopeptide permease A (OppA) plays an important role in the nutrition of cells and various signaling processes. In archaea, OppA is a major protein present in membrane vesicles of Thermococcales. Because there being no crystal structures of archaea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb3ff8686474cff3c324f7e8f73f3ba8
https://doi.org/10.1002/prot.26324
https://doi.org/10.1002/prot.26324
Publikováno v:
Acta Crystallographica Section D Structural Biology. 76:515-520
The N-terminal region of the stomatin operon partner protein (STOPP) PH1510 (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser–Lys dyad (Ser97 and Lys138) and specifically cleaves the C-term
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f784445b68065aeafe3a591fc7666083
https://doi.org/10.1107/s2059798320005021
https://doi.org/10.1107/s2059798320005021
Autor:
Ikuo Matsui, Hideshi Yokoyama
Publikováno v:
Critical reviews in microbiology. 46(1)
SPFH-domain proteins are found in almost all organisms across three domains: archaea, bacteria, and eukaryotes. In eukaryotic organelles, their subfamilies exhibit overlapping distribution and functions; thus, the rationality of annotation to discrim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4e33abf0a068d97458dc1c348d89b81
https://pubmed.ncbi.nlm.nih.gov/31983249
https://pubmed.ncbi.nlm.nih.gov/31983249
Publikováno v:
Journal of Data Mining in Genomics & Proteomics.
Stomatin is a membrane protein in human red blood cells. The crystal structure, in which the monomeric stomatin from the hyperthermophilic archaeon Pyrococcus horikoshii consists of the α/β domain and the C-terminal α-helical segment, forms a homo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::850405c11195f91d8b77a38caa4ef730
https://doi.org/10.4172/2153-0602.1000216
https://doi.org/10.4172/2153-0602.1000216
Autor:
Ikuo Matsui, Hideshi Yokoyama
Publikováno v:
FEBS Open Bio, Vol 4, Iss C, Pp 804-812 (2014)
FEBS Open Bio
FEBS Open Bio
Highlights • The structure of C-terminal domain of stomatin operon partner protein PH1510 was determined. • C-terminal domain of PH1510 (1510-C) forms a five-stranded β-barrel known as an OB-fold. • 1510-C could assemble into multimers based o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f003980d7bd7d8bae92eb001979a3672
https://doi.org/10.1016/j.fob.2014.09.002
https://doi.org/10.1016/j.fob.2014.09.002