Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Barbara T. Hsu"'
Autor:
Pinak Chakrabarti, Barbara T. Hsu
Publikováno v:
Inorganic Chemistry. 33:1165-1170
The geometry of interactions of metal ions with the phenolate group in proteins and small molecules has been examined using coordinates listed in structural databases. Cations are found to avoid the sp^2 lone pair directions of the ligand oxygen; in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::179766ff637c64a9b446918132580766
https://doi.org/10.1021/ic00084a032
https://doi.org/10.1021/ic00084a032
Autor:
Zhi Hao Zhou, Leemor Joshua-Tor, Douglas C. Rees, Barbara T. Hsu, Jae-Bum Park, Michael W. W. Adams, Michael W. Day
Publikováno v:
Protein Science. 1:1494-1507
The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 degrees C, have been determined by X-ray crystallography to a resolution of 1.8 A. Crystals of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15705462620c184b9d2b6d54b4450931
https://doi.org/10.1002/pro.5560011111
https://doi.org/10.1002/pro.5560011111
Autor:
Tina M. Iverson, Douglas C. Rees, Barbara T. Hsu, Alan B. Hooper, David M. Arciero, Michael S.P. Logan
Publikováno v:
Nature structural biology. 5(11)
Cytochrome c554 (cyt c554), a tetra-heme cytochrome from Nitrosomonas europaea, is an essential component in the biological nitrification pathway. In N. europaea, ammonia is converted to hydroxylamine, which is then oxidized to nitrite by hydroxylami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad8c51bb5ed01abbd4133b601e705a25
https://pubmed.ncbi.nlm.nih.gov/9808046
https://pubmed.ncbi.nlm.nih.gov/9808046
Publikováno v:
Biochemistry. 35(13)
The structure of a ternary complex of the R65Q mutant of yeast 3-phosphoglycerate kinase (PGK) with magnesium 5'-adenylylimidodiphosphate (Mg-AMP-PNP) and 3-phospho-D-glycerate (3-PG) has been determined by X-ray crystallography to 2.4 angstrom resol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b212beda1440fc6e4898662238c46bf
https://pubmed.ncbi.nlm.nih.gov/8672447
https://pubmed.ncbi.nlm.nih.gov/8672447
Autor:
Michael W. Day, Arthur J. Chirino, Herbert L. Axelrod, Barbara T. Hsu, Douglas C. Rees, George Feher, James P. Allen
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 50(Pt 4)
Cytochrome c(2) serves as the secondary electron donor that reduces the photo-oxidized bacteriochlorophyll dimer in photosynthetic bacteria. Cytochrome c(2) from Rhodobacter sphaeroides has been crystallized in three different forms. At high ionic st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14496cfc75c54d27b58cfe5078132b26
https://pubmed.ncbi.nlm.nih.gov/15299423
https://pubmed.ncbi.nlm.nih.gov/15299423
Publikováno v:
Structure (London, England : 1993). 1(1)
Background: The anti-ulcer drug sucrose octasulfate (SOS) binds to fibroblast growth factors (FGFs), proteins which stimulate the growth and differentiation of several cell types, including stomach epithelial cells. It is believed that SOS stabilizes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ad5cafc5950754691bbe20801ce5253
https://pubmed.ncbi.nlm.nih.gov/7520817
https://pubmed.ncbi.nlm.nih.gov/7520817
Autor:
D. Woo, J. Schlessman, Jongsun Kim, Arthur J. Chirino, Michael K. Chan, Douglas C. Rees, Millie M. Georgiadis, H. Komiya, Barbara T. Hsu
Publikováno v:
New Horizons in Nitrogen Fixation ISBN: 9789048142552
The biological conversion of dinitrogen to ammonia is catalyzed by the nitrogenase enzyme system found in nitrogen-fixing bacteria (Burgess, 1984; Orme-Johnson, 1985; Smith and Eady, 1992). The conventional nitrogenase consists of two component prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1217c0665c108ed2ef1a1286020b6cd0
https://doi.org/10.1007/978-94-017-2416-6_9
https://doi.org/10.1007/978-94-017-2416-6_9
Autor:
Douglas C. Rees, Jae-Bum Park, Michael W. W. Adams, Dennis R. Hare, Paul R. Blake, Michael W. Day, Barbara T. Hsu, Leemor Joshua-Tor, Michael F. Summers
The three-dimensional X-ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at -161 degrees C, and the NMR structure of the zinc-substituted protein, determined in solution at 45 degrees C, are compared
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ea1ec5d55c9631e81109aa6a8167c09
https://resolver.caltech.edu/CaltechAUTHORS:20150209-101846134
https://resolver.caltech.edu/CaltechAUTHORS:20150209-101846134
Autor:
Arthur J. Chirino, Xiaotian Zhu, H. Komiya, Salem Faham, Tsutomu Arakawa, Douglas C. Rees, Gary M. Fox, Barbara T. Hsu
Publikováno v:
Science (New York, N.Y.). 251(4989)
Members of the fibroblast growth factor (FGF) family of proteins stimulate the proliferation and differentiation of a variety of cell types through receptor-mediated pathways. The three-dimensional structures of two members of this family, bovine aci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3740c27351479fc649f2e27cfe899732
https://pubmed.ncbi.nlm.nih.gov/1702556
https://pubmed.ncbi.nlm.nih.gov/1702556