The interaction of microsomal cytochrome P450 2B4 with its redox partners, cytochrome P450 reductase and cytochrome b(5).
about
Structural diversity of eukaryotic membrane cytochrome p450sThe Role of Protein-Protein and Protein-Membrane Interactions on P450 FunctionCytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMREffect of Cytochrome b5 Content on the Activity of Polymorphic CYP1A2, 2B6, and 2E1 in Human Liver MicrosomesNADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data.Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.Role of protein-protein interactions in cytochrome P450-mediated drug metabolism and toxicityCatalytically relevant electrostatic interactions of cytochrome P450c17 (CYP17A1) and cytochrome b5.Effects of membrane mimetics on cytochrome P450-cytochrome b5 interactions characterized by NMR spectroscopy.Differences in Methadone Metabolism by CYP2B6 VariantsCross-linking mass spectrometry and mutagenesis confirm the functional importance of surface interactions between CYP3A4 and holo/apo cytochrome b(5).The action of cytochrome b(5) on CYP2E1 and CYP2C19 activities requires anionic residues D58 and D65.Substrate-modulated cytochrome P450 17A1 and cytochrome b5 interactions revealed by NMR.Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN SemiquinoneNADH:Cytochrome b5 Reductase and Cytochrome b5 Can Act as Sole Electron Donors to Human Cytochrome P450 1A1-Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene.CB5C affects the glucosinolate profile in Arabidopsis thalianaCorrelating structure and function of drug-metabolizing enzymes: progress and ongoing challenges.Another look at the interaction between mitochondrial cytochrome c and flavocytochrome b (2).Dynamic control of electron transfers in diflavin reductases.Gene duplication leads to altered membrane topology of a cytochrome P450 enzyme in seed plants.The catalytic function of cytochrome P450 is entwined with its membrane-bound nature.Transmembrane Interactions of Full-length Mammalian Bitopic Cytochrome-P450-Cytochrome-b5 Complex in Lipid Bilayers Revealed by Sensitivity-Enhanced Dynamic Nuclear Polarization Solid-state NMR Spectroscopy.Kinetic and Structural Characterization of the Effects of Membrane on the Complex of Cytochrome b 5 and Cytochrome c.Genome-guided investigation of plant natural product biosynthesis.Evidence that cytochrome b5 acts as a redox donor in CYP17A1 mediated androgen synthesis.Knockdown of several components of cytochrome P450 enzyme systems by RNA interference enhances the susceptibility of Helicoverpa armigera to fenvalerate.Molecular dynamics simulations give insight into the conformational change, complex formation, and electron transfer pathway for cytochrome P450 reductase.Quantum chemical calculations of amide-15N chemical shift anisotropy tensors for a membrane-bound cytochrome-b5.Determination of 15N chemical shift anisotropy from a membrane-bound protein by NMR spectroscopyCytochrome b5 Activates the 17,20-Lyase Activity of Human Cytochrome P450 17A1 by Increasing the Coupling of NADPH Consumption to Androgen Production.Cytochrome-P450-cytochrome-b5 interaction in a membrane environment changes 15N chemical shift anisotropy tensors.Insights into the role of substrates on the interaction between cytochrome b5 and cytochrome P450 2B4 by NMR.Use of phenoxyaniline analogs to generate biochemical insights into polybrominated diphenyl ether interaction with CYP2B enzymes.Membrane topology and search for potential redox partners of colon cancer-specific cytochrome P450 2W1.High warfarin sensitivity in carriers of CYP2C9*35 is determined by the impaired interaction with P450 oxidoreductase.Approaches and Recent Developments for the Commercial Production of Semi-synthetic Artemisinin.A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.Properties of purified CYP2R1 in a reconstituted membrane environment and its 25-hydroxylation of 20-hydroxyvitamin D3.Interactions of uranyl ion with cytochrome b₅ and its His39Ser variant as revealed by molecular simulation in combination with experimental methods.
P2860
Q27025716-9EE86D77-E5FE-439D-9E00-2DC4715DECA1Q27345454-C56C0758-F1C3-407D-8118-BC9F1AD64AB3Q28271636-65120F2C-453D-4A9D-9AC5-BF51358ECBABQ28547950-388383D1-13D5-4DF6-80EF-42266BCA8C5DQ30537968-A9672D0A-09B4-4E47-BBD7-93A5D963BC66Q30633058-6AD894F9-07B1-4A3C-85D5-18ABC2785C69Q33736588-99270E88-BE58-46B0-A0FE-DF63F2480711Q34181972-13B5225F-EF7C-441B-A7D1-DE576B5878DCQ34634130-AECC1C64-FBB4-422E-9BAF-F8292908E8E4Q35608108-52B7A4FC-87C6-4F25-B9F7-43EA164385A2Q35745266-248E38FB-C6BA-49D4-85C5-13C99420C609Q36598930-71501701-8BBC-4DC6-B217-CC13C9B4DFCFQ36680194-EE4F277D-B687-4684-9543-64E6EB500CD7Q36910210-6D2C0CCF-3B30-4502-A916-8FD089DA8F5CQ37078680-0A2623C1-5476-4CC0-87A0-F2C08FD3368FQ37182024-AB7E25C4-9DDA-47A4-8E7F-A30B83B3CCDCQ37255152-E9CFC981-8D87-4BBC-BA4D-F6D31A72DAF8Q37422674-35D5D79F-1D02-41A1-9A8C-2880ADBBC867Q37866680-FEF713E6-C735-4CDA-A56F-893C7B25A7C1Q38064332-2166DA6B-8CBC-4F1B-89B2-39A11C6BE73DQ38785709-DEC69412-DD98-4D4E-9D9B-1463EA1F3F71Q39321457-7F593B3C-18AF-430B-80E5-FDD3C4CB3F6FQ41054539-EC9011A0-5835-42E2-8261-8F64D2DB388BQ41353184-5DBE91A4-C314-4A9D-8C30-A51A4C9128C3Q41378077-16CCE08A-AF61-4FC4-805F-FE6F1E2E00E5Q41913564-28F4A4D6-4A72-4DB8-B185-492DBCECAD29Q42012833-783A85EE-A308-4561-BD4E-CC0C40E25D2FQ42072181-1459DC3B-E6AE-4F8C-8A1C-226043DEA96BQ42137311-2A43744D-0693-47D2-BF74-CACB1C6E9160Q42211095-2458C45B-3A7D-41CA-BBDF-45B021F4C9A1Q42324882-E3375929-FEE6-4638-9C78-93F3A4DC76C0Q42555411-84BE56F9-8FBC-45A8-95E4-3837C082679DQ43149378-54879142-EE8E-4C49-A4FD-A4E16C9025FAQ46246116-8C7ECAF6-462F-4110-8793-197AE04BB543Q48258823-B27C06BC-F79E-4D69-92BD-82F772531297Q48336005-1390EF21-296D-41CC-AA4E-C2D3E5803BE5Q49291649-67C67DEB-78C3-496F-A3B2-A26EE633E5CAQ50134156-3473BA17-0EE8-46FD-B98D-9BEB828A0898Q50885385-39500A9F-B7C0-44E4-BF0D-9F86F10DD838Q52612278-5117D98E-32E6-4B95-BC07-C95F4B41D7E3
P2860
The interaction of microsomal cytochrome P450 2B4 with its redox partners, cytochrome P450 reductase and cytochrome b(5).
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The interaction of microsomal ...... reductase and cytochrome b(5).
@ast
The interaction of microsomal ...... reductase and cytochrome b(5).
@en
The interaction of microsomal ...... reductase and cytochrome b(5).
@nl
type
label
The interaction of microsomal ...... reductase and cytochrome b(5).
@ast
The interaction of microsomal ...... reductase and cytochrome b(5).
@en
The interaction of microsomal ...... reductase and cytochrome b(5).
@nl
prefLabel
The interaction of microsomal ...... reductase and cytochrome b(5).
@ast
The interaction of microsomal ...... reductase and cytochrome b(5).
@en
The interaction of microsomal ...... reductase and cytochrome b(5).
@nl
P2860
P1476
The interaction of microsomal ...... reductase and cytochrome b(5).
@en
P2093
Lucy Waskell
Sang-Choul Im
P2860
P304
P356
10.1016/J.ABB.2010.10.023
P407
P577
2010-11-03T00:00:00Z