Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Ronald T. Ogata"'
Autor:
Chuong-Thu Thai, Carla Clark, Dušan Uhrín, Ronald T. Ogata, Paul N. Barlow, Juraj Bella, Marie M. Phelan, Janice Bramham
Publikováno v:
Biomolecular NMR Assignments. 7:285-288
Human C7 is one of four homologous complement proteins that self-assemble on the nascent activation-specific fragment, C5b, thus forming the cytolytic membrane attack complex (MAC). In addition to the conserved modular core of the MAC/perforin protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d60e9f8e8c2d92655935d409bbaca388
https://doi.org/10.1007/s12104-012-9429-3
https://doi.org/10.1007/s12104-012-9429-3
Autor:
Juraj Bella, Ronald T. Ogata, Chuong-Thu Thai, Dušan Uhrín, Andrew P. Herbert, Paul N. Barlow, Marie M. Phelan, Janice Bramham
Publikováno v:
Biomolecular NMR Assignments. 3:49-52
The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23ebbf65e4c70e6b2f4be57362decfb7
https://doi.org/10.1007/s12104-008-9139-z
https://doi.org/10.1007/s12104-008-9139-z
Autor:
Ronald T. Ogata, Chuong-Thu Thai
Publikováno v:
The Journal of Immunology. 174:6227-6232
Complement component C5 binds to components C6 and C7 in reversible reactions that are distinct from the essentially nonreversible associations that form during assembly of the complement membrane attack complex (MAC). We previously reported that the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a56de3967b9bb639116dcab710e4b32e
https://doi.org/10.4049/jimmunol.174.10.6227
https://doi.org/10.4049/jimmunol.174.10.6227
Autor:
Dinesh C. Soares, Ronald T. Ogata, Paul N. Barlow, Dušan Uhrín, Janice Bramham, Chuong-Thu Thai
Publikováno v:
Journal of Biological Chemistry. 280:10636-10645
The complement protein C5 initiates assembly of the membrane attack complex. This remarkable process results in lysis of target cells and is fundamental to mammalian defense against infection. The 150-amino acid residue domain at the C terminus of C5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08e1ffabe053c1e746195e70fac2b051
https://doi.org/10.1074/jbc.m413126200
https://doi.org/10.1074/jbc.m413126200
Autor:
Chuong-Thu Thai, Ronald T. Ogata
Publikováno v:
The Journal of Immunology. 171:6565-6573
Complement components C3, C4, and C5 are members of the thioester-containing α-macroglobulin protein superfamily. Within this superfamily, a unique feature of the complement proteins is a 150-residue-long C-terminal extension of their α-subunits th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3462bcf58c77a2acc9289d0434fa680e
https://doi.org/10.4049/jimmunol.171.12.6565
https://doi.org/10.4049/jimmunol.171.12.6565
Publikováno v:
The Journal of Immunology. 165:1066-1073
Previous studies focused on indels in the complement C345 protein family identified a number of potential protein-protein interaction sites in components C3 and C5. Here, one of these sites in C5, near the α-chain C terminus, was examined by alanine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57e164df203eb090ab077209d0e258cb
https://doi.org/10.4049/jimmunol.165.2.1066
https://doi.org/10.4049/jimmunol.165.2.1066
Fatty Acid Binding Proteins from Different Tissues Show Distinct Patterns of Fatty Acid Interactions
Autor:
Ronald T. Ogata, Alan M. Kleinfeld, Jacques H. Veerkamp, Aukje W. Zimmerman, Gary V. Richieri
Publikováno v:
Biochemistry, 39, 7197-7204
Biochemistry, 39, pp. 7197-7204
Biochemistry, 39, pp. 7197-7204
Fatty acid binding proteins (FABP) form a family of proteins displaying tissue-specific expression. These proteins are involved in fatty acid (FA) transport and metabolism by mechanisms that also appear to be tissue-specific. Cellular retinoid bindin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9ab7f3d0db103943c8065d3da40d981
https://doi.org/10.1021/bi000314z
https://doi.org/10.1021/bi000314z
Publikováno v:
The Journal of Immunology. 162:6580-6588
We recently suggested that sites of length polymorphisms in protein families (indels) might serve as useful guides for locating protein:protein interaction sites. This report describes additional site-specific mutagenesis and synthetic peptide inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd9f403af8f01c91fa80e486ab24d951
https://doi.org/10.4049/jimmunol.162.11.6580
https://doi.org/10.4049/jimmunol.162.11.6580
Publikováno v:
The Journal of Immunology. 161:4785-4794
Engineered mutants of human complement component C3 were used to test the idea that sites of length polymorphisms in protein families (indels) can guide a search for protein:protein interaction sites. Sequence changes were introduced at each of the 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::492856ca1800a443db585a29a2c1cf1d
https://doi.org/10.4049/jimmunol.161.9.4785
https://doi.org/10.4049/jimmunol.161.9.4785
Publikováno v:
Journal of Biological Chemistry. 273:7397-7405
We constructed 18 single amino acid mutants of the adipocyte fatty acid-binding protein (A-FABP) and 17 of the intestinal fatty acid-binding protein (I-FABP), at locations in the fatty acid (FA) binding sites. For each mutant protein, we measured the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d3787af6c49831947d0b9a949d808fb
https://doi.org/10.1074/jbc.273.13.7397
https://doi.org/10.1074/jbc.273.13.7397