Zobrazeno 1 - 10 of 10 pro vyhledávání: '"B C, Crews"'
1
Spatial requirements for 15-(R)-hydroxy-5Z,8Z,11Z, 13E-eicosatetraenoic acid synthesis within the cyclooxygenase active site of murine COX-2. Why acetylated COX-1 does not synthesize 15-(R)-hete
Autor: S W, Rowlinson, B C, Crews, D C, Goodwin, C, Schneider, J K, Gierse, L J, Marnett
Publikováno v: The Journal of biological chemistry. 275(9)
The two isoforms of cyclooxygenase, COX-1 and COX-2, are acetylated by aspirin at Ser-530 and Ser-516, respectively, in the cyclooxygenase active site. Acetylated COX-2 is essentially a lipoxygenase, making 15-(R)-hydroxyeicosatetraenoic acid (15-HET
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0a16d00677dd3ac38f40b585f20180f2
https://pubmed.ncbi.nlm.nih.gov/10692466
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3
Thromboxane A2 is a mediator of cyclooxygenase-2-dependent endothelial migration and angiogenesis
Autor: T O, Daniel, H, Liu, J D, Morrow, B C, Crews, L J, Marnett
Publikováno v: Cancer research. 59(18)
Cyclooxygenase-2 (COX-2) inhibitors reduce angiogenic responses to a variety of stimuli, suggesting that products of COX-2 may mediate critical steps. Here, we show that thromboxane A2 (TXA2) is one of several eicosanoid products generated by activat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4a4f74f32434e7ade1a214064de99196
https://pubmed.ncbi.nlm.nih.gov/10493510
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4
The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (COX-2). A putative L-shaped binding conformation utilizing the top channel region
Autor: S W, Rowlinson, B C, Crews, C A, Lanzo, L J, Marnett
Publikováno v: The Journal of biological chemistry. 274(33)
The chemical mandates for arachidonic acid conversion to prostaglandin G(2) within the cyclooxygenase (COX) active site predict that the substrate will orient in a kinked or L-shaped conformation. Molecular modeling of arachidonic acid in sheep COX-1
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::69b98fc00166e1748619ef6480fa254c
https://pubmed.ncbi.nlm.nih.gov/10438506
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5
Nitric oxide trapping of tyrosyl radicals generated during prostaglandin endoperoxide synthase turnover. Detection of the radical derivative of tyrosine 385
Autor: D C, Goodwin, M R, Gunther, L C, Hsi, B C, Crews, T E, Eling, R P, Mason, L J, Marnett
Publikováno v: The Journal of biological chemistry. 273(15)
Tyrosyl radicals have been detected during turnover of prostaglandin endoperoxide H synthase (PGHS), and they are speculated to participate in cyclooxygenase catalysis. Spectroscopic approaches to elucidate the identity of the radicals have not been
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e8712c8e004af27150353482606af1e0
https://pubmed.ncbi.nlm.nih.gov/9535872
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7
Alpha 2-macroglobulin bait region variants. A role for the bait region in tetramer formation
Autor: P G, Gettins, K H, Hahn, B C, Crews
Publikováno v: The Journal of biological chemistry. 270(23)
To test the hypothesis that a large portion of the bait region of human alpha 2-macroglobulin (alpha 2M) can be removed without adversely affecting the protein's structural and functional properties, we expressed two human alpha 2M variants with trun
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7da02a83b1762e19c129e11659dfe3a4
https://pubmed.ncbi.nlm.nih.gov/7539801
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8
Heterogeneity of recombinant human antithrombin III expressed in baby hamster kidney cells. Effect of glycosylation differences on heparin binding and structure
Autor: B, Fan, B C, Crews, I V, Turko, J, Choay, G, Zettlmeissl, P, Gettins
Publikováno v: The Journal of biological chemistry. 268(23)
To determine the effects of differences in glycosylation on the structure and functional properties of recombinant human antithrombin (rHAT), we have characterized the properties of the recombinant protein overexpressed by baby hamster kidney cells.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ec5f61321eefa7cbcf62074ac2dbe947
https://pubmed.ncbi.nlm.nih.gov/8349638
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9
Role of tryptophan 49 in the heparin cofactor activity of human antithrombin III
Autor: P, Gettins, J, Choay, B C, Crews, G, Zettlmeiss
Publikováno v: The Journal of biological chemistry. 267(30)
To probe the functional role of tryptophan 49 in human antithrombin III, a mutant antithrombin, W49K, has been expressed in baby hamster kidney cells. The mutation reduces the affinity for heparin pentasaccharide by 1.8 kcal mol-1 but does not alter
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6bfc445ceb330557a8efbdb6b1c421c1
https://pubmed.ncbi.nlm.nih.gov/1400504
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10
77Se NMR characterization of 77Se-labeled ovine erythrocyte glutathione peroxidase
Autor: P, Gettins, B C, Crews
Publikováno v: The Journal of biological chemistry. 266(8)
Lambs, maintained on a selenium-deficient diet supplemented with 94 atom % Na2 27SeO3, have been used as a source of 77Se-enriched erythrocyte glutathione peroxidase. After 5 months on this diet, the percentage of selenium in the enzyme derived from
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a51671182ffc77160415ddeafb587bc6
https://pubmed.ncbi.nlm.nih.gov/2002027
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