Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
about
Pharmacogenomics of human P450 oxidoreductaseShedding light on protein folding, structural and functional dynamics by single molecule studiesMolecular view of an electron transfer process essential for iron-sulfur protein biogenesisCytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMRNADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.Research Resource: Correlating Human Cytochrome P450 21A2 Crystal Structure and Phenotypes of Mutations in Congenital Adrenal Hyperplasia.Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles.Identification of six novel P450 oxidoreductase missense variants in Ashkenazi and Moroccan Jewish populations.NADPH-cytochrome P450 reductase is regulated by all-trans retinoic acid and by 1,25-dihydroxyvitamin D3 in human acute myeloid leukemia cells.Real-time analysis of conformational control in electron transfer reactions of human cytochrome P450 reductase with cytochrome cAltered human CYP3A4 activity caused by Antley-Bixler syndrome-related variants of NADPH-cytochrome P450 oxidoreductase measured in a robust in vitro systemMolecular Cloning, Expression Pattern and Polymorphisms of NADPH-Cytochrome P450 Reductase in the Bird Cherry-Oat Aphid Rhopalosiphum padi (L.).Genetic variations in NADPH-CYP450 oxidoreductase in a Czech Slavic cohort.NADPH-cytochrome P450 oxidoreductase: roles in physiology, pharmacology, and toxicology.Human cytochromes P450 in health and diseaseUnusual properties of the cytochrome P450 superfamily.Substrate-modulated cytochrome P450 17A1 and cytochrome b5 interactions revealed by NMR.Mapping of the Allosteric Site in Cholesterol Hydroxylase CYP46A1 for Efavirenz, a Drug That Stimulates Enzyme ActivityMutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN SemiquinonePhosphorylation of human cytochrome P450c17 by p38α selectively increases 17,20 lyase activity and androgen biosynthesis.Intra- and inter-molecular effects of a conserved arginine residue of neuronal and inducible nitric oxide synthases on FMN and calmodulin binding.Correlating structure and function of drug-metabolizing enzymes: progress and ongoing challenges.From cholesterogenesis to steroidogenesis: role of riboflavin and flavoenzymes in the biosynthesis of vitamin D.Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes.Formation of P450 · P450 complexes and their effect on P450 functionDynamic control of electron transfers in diflavin reductases.Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Instability of the Human Cytochrome P450 Reductase A287P Variant Is the Major Contributor to Its Antley-Bixler Syndrome-like Phenotype.Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function.Modeling of Anopheles minimus Mosquito NADPH-cytochrome P450 oxidoreductase (CYPOR) and mutagenesis analysis.A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.Molecular dynamics simulations give insight into the conformational change, complex formation, and electron transfer pathway for cytochrome P450 reductase.Electron transfer by human wild-type and A287P mutant P450 oxidoreductase assessed by transient kinetics: functional basis of P450 oxidoreductase deficiency.Functioning of Microsomal Cytochrome P450s: Murburn Concept Explains the Metabolism of Xenobiotics in Hepatocytes.Coexpression of CPR from various origins enhances biotransformation activity of human CYPs in S. pombe.Kinetic analysis of cytochrome P450 reductase from Artemisia annua reveals accelerated rates of NADH-dependent flavin reduction.The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength.Structural and Kinetic Studies of Asp632 Mutants and Fully Reduced NADPH-Cytochrome P450 Oxidoreductase Define the Role of Asp632 Loop Dynamics in the Control of NADPH Binding and Hydride Transfer.
P2860
Q26998463-8DB2BD27-9ACE-4A29-97EA-F45C70935954Q26999437-AB592ABD-1D60-4A2A-95AC-9D37682FDD6FQ27677438-AD46DE16-CC00-4ABF-A586-2783376B6B2DQ28271636-22C7CFD3-093C-4D76-A766-36F93685191CQ30537968-940B3AD7-C11A-461C-802E-B9ECF87EB005Q33736588-3DADC0D1-06B0-4C43-A919-F14100688282Q34484922-9012E524-FE66-4B65-9B42-E8394D1800C3Q34577168-F8DD4BEE-AC45-4C59-827A-AFF67564A3E0Q34731517-A48FB124-9B6C-4227-AB12-096A864D3082Q35123889-1A0AE68F-A094-4079-92E0-432E7749E851Q35755388-E330D72F-1EBA-48CB-8A47-40FCC27B4833Q35846903-830E25A4-580C-4C45-BBC5-BD39ADFDBD2EQ36001940-E5C3B037-502F-40A9-AB83-3BD9AD2637F3Q36326565-DE08E182-19E3-4472-B361-91CE15E98393Q36497649-ED04E90F-E1FA-4F16-9480-76A3FFFC7E52Q36512912-3FBAFC3C-09A4-4497-84E5-835D981DA3FEQ36512916-C4196BB1-4227-4EE7-9954-0DC104F8CBC8Q36910210-CF1D9658-CDB5-4F6D-9920-5263D09E83F5Q36941138-3B54F4D0-6204-453B-A23B-F729876E2A74Q37078680-F3DC8C31-E63D-4FBA-AA8D-A70865645B91Q37099736-D4587083-D142-4F99-82CF-0001CC79AB4FQ37188160-2E6330AB-ED64-4DB3-887D-885790643D50Q37422674-11BF0DC7-A406-49AE-B83A-9127C59F0501Q37633829-FB2CB72F-1F8A-4C64-9274-6FFDB046302FQ37964804-BE6C5CEF-824A-4EE8-9DCC-EC1BF69B688EQ37966569-DB6E392A-36CB-48BC-A1D2-78FE51BC2E82Q38064332-C441C6EE-DE31-4283-AB24-E44FC2A51050Q38603029-8A2D77EF-7BB4-4535-8644-6EB6BC6DE327Q38753508-D98278EB-A44A-4C02-8A21-F10D9A55D429Q39012305-B30B7C70-56B6-4977-A705-860305FA713AQ39431012-9D3C617D-87BC-4E69-A2AA-B1713E22A2A8Q41159852-7FA7A9A8-C64E-4841-81E7-610C28EBE12AQ41808959-A5AC604E-276D-466E-A546-8B8E36EF4BE1Q42072181-55D8C061-1DBF-4BB3-BE43-32830707D1CDQ42266862-A4B12A70-C91B-4959-BEDF-EC5B65C7DE2EQ42557407-F48DB257-0809-40C9-AE52-E9F11FFC9D43Q43452734-3F9334E8-7935-4F47-B95C-B4936BEABA96Q46964325-7C0A7D24-72FA-49FD-9AF4-0869B7C10DD4Q47104690-162C853C-1D4F-4AC9-8AE1-C8E26DFCDF38Q50140978-9C930E29-CED8-49DE-9E59-29A9F57922DA
P2860
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@ast
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@en
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@nl
type
label
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@ast
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@en
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@nl
prefLabel
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@ast
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@en
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@nl
P2093
P2860
P3181
P356
P1476
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
@en
P2093
Bettie Sue Masters
Christopher C Marohnic
Chuanwu Xia
Jung-Ja P Kim
Satya P Panda
P2860
P304
13486-13491
P3181
P356
10.1073/PNAS.1106632108
P407
P577
2011-08-01T00:00:00Z