Zobrazeno 1 - 10
of 12
pro vyhledávání: '"K. G. Ravichandran"'
Publikováno v:
Journal of the American Chemical Society. 108(3)
Etude des 2 complexes dinickel (II) anthracene diporphyrine et dicuivre (II) biphenylene diporphyrine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32623a33bb00aaf7a8a3b64c39823de4
https://pubmed.ncbi.nlm.nih.gov/22175456
https://pubmed.ncbi.nlm.nih.gov/22175456
Autor:
Jui Yun Lu, Charles A. Hasemann, Johann Deisenhofer, K. G. Ravichandran, Julian A. Peterson, Elizabeth J. Goldsmith, Sekhar S. Boddupalli
Publikováno v:
Proceedings of the National Academy of Sciences. 89:5567-5571
Cytochromes P450 are members of a superfamily of hemoproteins that are involved in the metabolism of various physiologic and xenobiotic organic compounds. This superfamily of proteins can be divided into two classes based on the electron donor proxim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7648595e7ea8825f479f0c6c26424b6c
https://doi.org/10.1073/pnas.89.12.5567
https://doi.org/10.1073/pnas.89.12.5567
Autor:
K. G. Ravichandran, Ewa Skrzypczak-Jankun, Vasili E. Carperos, Mary L. Westbrook, Alexander Tulinsky, John M. Maraganore
Publikováno v:
Journal of Molecular Biology. 221:1379-1393
The isomorphous structures of the hirugen (N-acetylhirudin 53′-64′ with sulfato-Tyr63′) and hirulog 1 ( d -Phe-Pro-Arg-Pro-(Gly)4 desulfato-Tyr63′-hirugen) complexes of human α-thrombin have been determined and refined at 2.2Aresolution to c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14e56607f31d98d9c446b82bd3d48e83
https://doi.org/10.1016/0022-2836(91)90939-4
https://doi.org/10.1016/0022-2836(91)90939-4
Autor:
Alexander Tulinsky, Wolfram Bode, John W. Fenton, Carolyn Roitsch, Robert Huber, Timothy J. Rydel, K. G. Ravichandran
Publikováno v:
Science. 249:277-280
The crystallographic structure of a recombinant hirudin-thrombin complex has been solved at 2.3 angstrom (A) resolution. Hirudin consists of an NH2-terminal globular domain and a long (39 A) COOH-terminal extended domain. Residues Ile1 to Tyr3 of hir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bea3440ae8560039bdc36e62ffc35c3a
https://doi.org/10.1126/science.2374926
https://doi.org/10.1126/science.2374926
Publikováno v:
Protein science : a publication of the Protein Society. 3(6)
The crystal structure of a monoclinic form of human plasminogen kringle 4 (PGK4) has been solved by molecular replacement using the orthorthombic structure as a model and it has been refined by restrained least-squares methods to an R factor of 16.4%
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2694a7e567bcf53031d4b21fe83daf8f
https://pubmed.ncbi.nlm.nih.gov/8069221
https://pubmed.ncbi.nlm.nih.gov/8069221
Publikováno v:
Journal of molecular biology. 236(4)
Cytochrome P450terp is a class I (mitochondrial/bacterial) P450 that catalyzes the hydroxylation of alpha-terpineol as part of the catabolic assimilation of this compound by a pseudomonad species. Crystals grown from the purified protein have the sym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::405db824073105de1539e585cac62a87
https://pubmed.ncbi.nlm.nih.gov/8120894
https://pubmed.ncbi.nlm.nih.gov/8120894
Autor:
Gour P. Pal, Alexander Tulinsky, Frederick G. Walz, K. G. Ravichandran, Peter Metcalf, Raghuvir K. Arni
Publikováno v:
Biochemistry. 31(12)
The structure of the Gln25 variant of ribonuclease T1 (RNase T1) crystallized at pH 7 and at high ionic strength has been solved by molecular replacement using the coordinates of the Lys25-RNase T1/2'-guanylic acid (2'GMP) complex at pH 5 [Arni et al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::194c8ce015ced5e5125a65a494a73328
https://pubmed.ncbi.nlm.nih.gov/1554699
https://pubmed.ncbi.nlm.nih.gov/1554699
Publikováno v:
Biochemistry. 30(43)
The crystal structure of human plasminogen kringle 4 (PGK4) has been solved by molecular replacement using the bovine prothrombin kringle 1 (PTK1) structure as a model and refined by restrained least-squares methods to an R factor of 14.2% at 1.9-A r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c94e05a640660691792b4d697e792415
https://pubmed.ncbi.nlm.nih.gov/1657148
https://pubmed.ncbi.nlm.nih.gov/1657148
Autor:
E, Skrzypczak-Jankun, V E, Carperos, K G, Ravichandran, A, Tulinsky, M, Westbrook, J M, Maraganore
Publikováno v:
Journal of molecular biology. 221(4)
The isomorphous structures of the hirugen (N-acetylhirudin 53'-64' with sulfato-Tyr63') and hirulog 1 (D-Phe-Pro-Arg-Pro-(Gly)4 desulfato-Tyr63'-hirugen) complexes of human alpha-thrombin have been determined and refined at 2.2 A resolution to crysta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3fd88beca7db10fa9e1282400d96c3f6
https://pubmed.ncbi.nlm.nih.gov/1942057
https://pubmed.ncbi.nlm.nih.gov/1942057
Autor:
K. G. Ravichandran, C.H. Park, Manuel Soriano-Garcia, Alexander Tulinsky, Ewa Skrzypczak-Jankun
Publikováno v:
Biochemistry. 28:6805-6810
The structure of Ca2+ prothrombin fragment 1 has been solved at 2.8-A resolution by X-ray crystallographic methods. Most of the Gla domain of fragment 1 (residues 1-48), which is high homologous with the N-terminal regions of six other blood proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ea2b52b9830a694ba46328c8a7162ab
https://doi.org/10.1021/bi00443a004
https://doi.org/10.1021/bi00443a004