2001 - Fellow of the American Association for the Advancement of Science (AAAS)
Her primary areas of investigation include Biochemistry, Nitric oxide synthase, Reductase, Heme and Microsome. Her study in Cytochrome c, Tetrahydrobiopterin, Enzyme, Calmodulin and Hemeprotein is carried out as part of her studies in Biochemistry. Her research integrates issues of Molecular biology, Superoxide and Cell biology in her study of Nitric oxide synthase.
In her study, Oxidoreductase, Flavin adenine dinucleotide and Flavoprotein is strongly linked to Flavin group, which falls under the umbrella field of Reductase. Bettie Sue Siler Masters has researched Heme in several fields, including Stereochemistry, Cofactor and Citrulline. Her work on Cytochrome c reductase as part of general Microsome research is frequently linked to Mechanism, thereby connecting diverse disciplines of science.
Her main research concerns Biochemistry, Microsome, Reductase, Nitric oxide synthase and Cytochrome. Her study in Heme, Enzyme, Cytochrome c, Hydroxylation and Cytochrome P450 is done as part of Biochemistry. In her study, which falls under the umbrella issue of Microsome, Isozyme is strongly linked to Kidney.
She usually deals with Reductase and limits it to topics linked to Flavoprotein and Amine oxidase. Her Nitric oxide synthase research focuses on subjects like Biophysics, which are linked to Electron transport chain. Her Cytochrome research incorporates elements of Drug metabolism and Cytochrome P450 reductase.
Her primary areas of study are Biochemistry, Nitric oxide, Nitric oxide synthase, Reductase and Heme. Her work deals with themes such as Substrate, Catalysis and Oxygen, which intersect with Nitric oxide. The concepts of her Nitric oxide synthase study are interwoven with issues in Biophysics, Insulin, Stereochemistry, Phosphorylation and Skeletal muscle.
She has included themes like Monooxygenase and Heme oxygenase in her Reductase study. Her Heme study also includes fields such as
Her scientific interests lie mostly in Biochemistry, Nitric oxide synthase, Nitric oxide, Mutant and Heme. Her work is connected to Reductase, Flavin adenine dinucleotide, FAD binding, NADPH-Ferrihemoprotein Reductase and Tetrahydrobiopterin, as a part of Biochemistry. The study incorporates disciplines such as Oxidoreductase, Molecular biology and Cytochrome c in addition to Flavin adenine dinucleotide.
In her study, Endothelial NOS is inextricably linked to Insulin resistance, which falls within the broad field of Nitric oxide synthase. Her Nitric oxide research is multidisciplinary, relying on both NADPH Cytochrome P450 Oxidoreductase, Molecular oxygen and Organic molecules. Bettie Sue Siler Masters combines subjects such as Wild type and Stereochemistry with her study of Heme.
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Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
Jeannette Vásquez-Vivar;B. Kalyanaraman;Pavel Martásek;Neil Hogg.
Proceedings of the National Academy of Sciences of the United States of America (1998)
Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography.
Y Yasukochi;B S Masters.
Journal of Biological Chemistry (1976)
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.
Proceedings of the National Academy of Sciences of the United States of America (1997)
Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the nos caveolin binding domain in vivo
Guillermo Garcı́a-Cardeña;Pavel Martasek;Bettie Sue Siler Masters;Phillip M. Skidd.
Journal of Biological Chemistry (1997)
[92] The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver
Bettie Sue Siler Masters;Charles H. Williams;Henry Kamin.
Methods in Enzymology (1967)
Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.
C.S Raman;Huiying Li;Pavel Martásek;Vladimir Král.
Cell (1998)
Inducible nitric-oxide synthase generates superoxide from the reductase domain
Yong Xia;Linda J. Roman;Bettie Sue S. Masters;Jay L. Zweier.
Journal of Biological Chemistry (1998)
Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide.
Kirk Mcmillan;David S. Bredt;David J. Hirsch;Solomon H. Snyder.
Proceedings of the National Academy of Sciences of the United States of America (1992)
Neuronal nitric oxide synthase and dystrophin-deficient muscular dystrophy
Wen Jinn Chang;Susan T. Iannaccone;Kim S. Lau;Bettie Sue S Masters.
Proceedings of the National Academy of Sciences of the United States of America (1996)
ENDOTHELIAL NITRIC OXIDE SYNTHASE-DEPENDENT SUPEROXIDE GENERATION FROM ADRIAMYCIN
Jeannette Vásquez-Vivar;Pavel Martasek;Neil Hogg;Bettie Sue Siler Masters.
Biochemistry (1997)
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