Zobrazeno 1 - 10
of 222
pro vyhledávání: '"Ronald W. Estabrook"'
Publikováno v:
Archives of biochemistry and biophysics. 726
Autor:
Institute of Medicine, Division of Health Sciences Policy, Roundtable on Research and Development of Drugs, Biologics, and Medical Devices, Jonathan R. Davis, Sarah Pitluck, Peter Bouxsein, Ronald W. Estabrook, Sumner Yaffe, M.D
The Institute of Medicine's (IOM's) Roundtable on Research and Development of Drugs, Biologics, and Medical Devices evolved from the Forum on Drug Development, which was established in 1986. Sponsor representatives and IOM determined the importance o
Autor:
Institute of Medicine, Roundtable on Research and Development of Drugs, Biologics, and Medical Devices, Ronald W. Estabrook, Janet Woodcock, Vivian P. Nolan, Jonathan R. Davis
In an effort to increase knowledge and understanding of the process of assuring data quality and validity in clinical trials, the IOM hosted a workshop to open a dialogue on the process to identify and discuss issues of mutual concern among industry,
Publikováno v:
Biochemical Pharmacology. 84:374-382
The NADPH-dependent consumption of O(2) by cytochrome P450 BM3 was stimulated by either laurate or perfluorolaurate, but the NADPH/O(2) molar consumption ratios were approximately 1 and 2, respectively, indicating that perfluorolaurate does not becom
Autor:
Ronald W. Estabrook
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814:6-13
Autor:
Ronald W. Estabrook
Publikováno v:
Xenobiotica. 39:558-564
Steroid hydroxylations: A paradigm for cytochrome P450 catalyzed mammalian monooxygenation reactions
Autor:
Ronald W. Estabrook
Publikováno v:
Biochemical and Biophysical Research Communications. 338:290-298
The present article reviews the history of research on the hydroxylation of steroid hormones as catalyzed by enzymes present in mammalian tissues. The report describes how studies of steroid hormone synthesis have played a central role in the discove
Publikováno v:
Biochemistry (Moscow). 70:357-365
NADPH-cytochrome P450 reductase (CPR) is a membrane-bound flavoprotein that interacts with the membrane via its N-terminal hydrophobic sequence (residues 1-56). CPR is the main electron transfer component of hydroxylation reactions catalyzed by micro
Publikováno v:
Biochemistry (Moscow). 69:364-375
Cytochrome P45017alpha is a key enzyme in steroid hormone biosynthesis. It catalyzes the reaction of 17alpha-hydroxylation of progesterone (P4) and pregnenolone (P5) and the 17,20-lyase reaction resulting in side chain cleavage of C21 steroids to for
Publikováno v:
Proceedings of the National Academy of Sciences. 100:14754-14759
Metabolites of vitamin D 3 (D3) (cholecalciferol) are recognized as enzymatically formed chemicals in humans that can influence a wide variety of reactions that regulate a large number of cellular functions. The metabolism of D3 has been extensively