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Bettie Sue Siler Masters
Researcher at University of Texas Health Science Center at San Antonio
Publications - 204
Citations - 15591
Bettie Sue Siler Masters is an academic researcher from University of Texas Health Science Center at San Antonio. The author has contributed to research in topics: Nitric oxide synthase & Reductase. The author has an hindex of 59, co-authored 203 publications receiving 15324 citations. Previous affiliations of Bettie Sue Siler Masters include Federation of American Societies for Experimental Biology & Duke University.
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Journal ArticleDOI
Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
Jeannette Vasquez-Vivar,Balaraman Kalyanaraman,Pavel Martásek,Neil Hogg,Bettie Sue Siler Masters,Hakim Karoui,Paul Tordo,Kirkwood A. Pritchard +7 more
TL;DR: The mechanism of superoxide generation by endothelial nitric oxide synthase (eNOS) was investigated by the electron spin resonance spin-trapping technique using 5-diethoxyphosphoryl-5-methyl-1-pyrroline N-oxide as discussed by the authors.
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Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography.
TL;DR: Titration of these purified preparations aerobically with both NADPH and potassium ferricyanide demonstrated unequivocally that the air-stable, reduced form of NADPH-cytochrome c (P-450) reductase contains 2 electron equivalents, confirming recent results obtained.
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Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the nos caveolin binding domain in vivo
Guillermo García-Cardeña,Pavel Martásek,Bettie Sue Siler Masters,Phillip M. Skidd,Jacques Couet,Shengwen Li,Michael P. Lisanti,William C. Sessa +7 more
TL;DR: The data demonstrate a novel functional role for Caveolin-1 in mammalian cells as a potential molecular chaperone that directly inactivates NOS and the inactivation of eNOS and nNOS by the scaffolding domain of caveolin-3 suggests that eN OS in cardiac myocytes and n NOS in skeletal muscle are likely subject to negative regulation by this muscle-specific caveolin isoform.
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Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.
Ming Wang,David L. Roberts,Rosemary Paschke,Thomas M. Shea,Bettie Sue Siler Masters,Jung-Ja P. Kim +5 more
TL;DR: The structure of rat liver CPR, expressed in Escherichia coli and solubilized by limited trypsinolysis, has been determined by x-ray crystallography at 2.6 A resolution.
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Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.
Chander Raman,Huiying Li,Pavel Martásek,Vladimír Král,Bettie Sue Siler Masters,Thomas L. Poulos +5 more
TL;DR: The unexpected recognition of the substrate, L-arginine, at the H4B site indicates that this site is poised to stabilize a positively charged pterin ring and suggests a model involving a cationic pterIn radical in the catalytic cycle.