The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
about
Hydrocarbon hydroxylation by cytochrome P450 enzymesA novel type of allosteric regulation: functional cooperativity in monomeric proteinsRedox potential control by drug binding to cytochrome P450 3A4Spectroscopic characterization of the oxyferrous complex of prostacyclin synthase in solution and in trapped sol-gel matrix.Spin equilibrium and O₂-binding kinetics of Mycobacterium tuberculosis CYP51 with mutations in the histidine-threonine dyadCYP3A4-Mediated carbamazepine (CBZ) metabolism: formation of a covalent CBZ-CYP3A4 adduct and alteration of the enzyme kinetic profile.Lipid-protein correlations in nanoscale phospholipid bilayers determined by solid-state nuclear magnetic resonance.Cytochromes P450 in nanodiscs.Defining CYP3A4 structural responses to substrate binding. Raman spectroscopic studies of a nanodisc-incorporated mammalian cytochrome P450.Cytochrome P450 7A1 cholesterol 7alpha-hydroxylation: individual reaction steps in the catalytic cycle and rate-limiting ferric iron reductionInteractions of cytochrome P450s with their ligands.Magic-angle spinning solid-state NMR spectroscopy of nanodisc-embedded human CYP3A4.Screening of type I and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy.Membrane protein assembly into Nanodiscs.Chapter 11 - Reconstitution of membrane proteins in phospholipid bilayer nanodiscsTemperature derivative spectroscopy to monitor the autoxidation decay of cytochromes P450Mechanism of drug-drug interactions mediated by human cytochrome P450 CYP3A4 monomerThe ferrous-oxy complex of human aromataseCharacterization of the physiological turnover of native and inactivated cytochromes P450 3A in cultured rat hepatocytes: a role for the cytosolic AAA ATPase p97?The use of isomeric testosterone dimers to explore allosteric effects in substrate binding to cytochrome P450 CYP3A4Oxygen activation by cytochrome P450 monooxygenaseSpectroscopic features of cytochrome P450 reaction intermediatesAdvances in predicting CYP-mediated drug interactions in the drug discovery setting.Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4Nanodiscs in Membrane Biochemistry and Biophysics.Cytochrome P450 is present in both ferrous and ferric forms in the resting state within intact Escherichia coli and hepatocytes.Spectroscopic studies of the cytochrome P450 reaction mechanisms.Small-angle scattering determination of the shape and localization of human cytochrome P450 embedded in a phospholipid nanodisc environment.Mechanism-Based Inhibition of CYP3A4 by Podophyllotoxin: Aging of an Intermediate Is Important for in Vitro/in Vivo Correlations.Liver microsomal lipid enhances the activity and redox coupling of colocalized cytochrome P450 reductase-cytochrome P450 3A4 in nanodiscs.Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein.Functional reconstitution of monomeric CYP3A4 with multiple cytochrome P450 reductase molecules in Nanodiscs.Kinetics of electron transfer between NADPH-cytochrome P450 reductase and cytochrome P450 3A4.Cryoradiolysis and cryospectroscopy for studies of heme-oxygen intermediates in cytochromes p450.Oxidase uncoupling in heme monooxygenases: human cytochrome P450 CYP3A4 in Nanodiscs.Nanodiscs in the studies of membrane-bound cytochrome P450 enzymes.Mass spectrometric detection of CYP450 adducts following oxidative desulfuration of methyl parathion.Drug-Drug Interactions between Atorvastatin and Dronedarone Mediated by Monomeric CYP3A4.Cooperativity in Cytochrome P450 3A4The One-electron Autoxidation of Human Cytochrome P450 3A4
P2860
Q24649665-3BBFC6DF-838F-4B62-AC02-D2D7A641C71DQ27011182-0A98F892-13D1-416E-95F1-2F2222E335ECQ28757148-1C486433-42CB-4CF3-8239-75AB9EF2E50FQ33775642-F9D92F64-C1A9-400D-873A-D2EE5952F10BQ33859424-10995FA9-D868-4E64-88B7-11EC9AF8E3CEQ33898107-B9FD0778-B3FA-421F-BFC4-93AFBE54B21BQ34134824-C6825BF6-EB13-41A4-8E45-6F2386510876Q34284199-0F534C0F-A964-4553-A50D-2D72D7DB27A4Q34551011-53836B83-371F-4F7D-B9A6-2E0D0BA6B81BQ34575691-E8131F4A-E9DA-45B5-BFA0-24DA23BCB3FCQ34586606-479E4C00-0C41-40B4-A0E3-D2D8B295DEA3Q34710847-0ED4BB47-8761-4A44-B2A4-CCAA9303BD95Q34975426-58454703-D996-4385-83F2-7ABDC137F607Q35008328-0CF64C4D-561D-4DE3-B9C8-C02F95D45D6AQ35012211-7DB49FA0-F8E6-4C51-9DD2-5AEDC7D957BBQ35186919-E47DD1F3-8331-41CC-8C32-6326C39F2D81Q36590427-4AD99379-F681-42D7-BFE9-D2D67AB41503Q36782111-8BF5EA2F-0735-4780-91DE-EAC0566425CFQ36876654-FE525B9F-4C29-497E-9E32-88E9A7940242Q36952271-514A3BB7-58C8-4855-A822-F9F18EB33980Q37207087-FF5F1D2D-0D13-4C73-923A-84C118402354Q37822069-B91564C9-EA7B-4490-A7E9-48B1D79A052EQ38089823-8B621FDD-4DEE-40B0-89A1-66441C325F66Q38393619-33946757-B860-4BF1-AC8C-D668EE0E1D2CQ39126044-8E9E63AF-071B-42CB-9417-6B03CB795892Q39243009-F8F2D8EC-1C26-483D-BEE0-44D5514DEC58Q39409036-8CECBDB7-C159-4A7F-B3BD-24C441A2C4B0Q40252259-E3922561-8113-4396-B1FD-A6754F79812FQ41432197-59A447E9-72D5-44AB-9000-99FE6D447B1FQ41551984-5C6C85F9-0314-4E59-8694-845F383FCA7BQ41904468-A57E262B-E6E3-480A-89A2-3E50844585AFQ42233562-2CA93CC4-65B3-4926-BA6B-437179106A2BQ42873685-B2357CCD-D388-4A00-BBF1-3EF9A9FC141CQ42921523-A7771DCB-3065-4E57-9F8D-B0169BD1B8C0Q42937681-683B51F6-C0FC-4C0B-BFF3-D2CE9FD89D95Q42945187-E234EA50-105E-4E5B-95E5-7D73C21D0BCFQ46148544-A86AC0AE-090C-4EE6-8019-78E6E55EAE3BQ48188313-8492E3D1-82EE-4980-8CBB-CE80D19D594EQ58035710-2338B5AE-63FD-4F5A-90AA-6FDC55D5288FQ58035712-DC9F72BE-2950-4E9D-A90F-BC1F67FB5C32
P2860
The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im Juni 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в червні 2006
@uk
name
The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
@en
The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
@nl
type
label
The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
@en
The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
@nl
prefLabel
The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
@en
The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
@nl
P2093
P2860
P356
P1476
The ferrous-dioxygen intermedi ...... f formation and decay kinetics
@en
P2093
Bradley J Baas
Stephen G Sligar
Yelena V Grinkova
P2860
P304
23313-23318
P356
10.1074/JBC.M605511200
P407
P577
2006-06-08T00:00:00Z