CYP2C8 exists as a dimer in natural membranes. - Wikidata - wikimedia - TriplyDB

CYP2C8 exists as a dimer in natural membranes.

CYP2C8 exists as a dimer in natural membranes.

http://www.wikidata.org/entity/Q34257489

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Progesterone receptor membrane component 1 inhibits the activity of drug-metabolizing cytochromes P450 and binds to cytochrome P450 reductase Membrane position of ibuprofen agrees with suggested access path entrance to cytochrome P450 2C9 active site A novel type of allosteric regulation: functional cooperativity in monomeric proteins Structure and dynamics of the membrane-bound cytochrome P450 2C9 Identifying cytochrome p450 functional networks and their allosteric regulatory elements Cytochrome P450 system proteins reside in different regions of the endoplasmic reticulum.Interactions among cytochromes P450 in microsomal membranes: oligomerization of cytochromes P450 3A4, 3A5, and 2E1 and its functional consequences Drug metabolism by CYP2C8.3 is determined by substrate dependent interactions with cytochrome P450 reductase and cytochrome b5.CYP2R1 Mutations Impair Generation of 25-hydroxyvitamin D and Cause an Atypical Form of Vitamin D Deficiency.Identification of cytochrome P450 2C2 protein complexes in mouse liver.Effect of homomeric P450-P450 complexes on P450 function.Immobilized Cytochrome P450 for Monitoring of P450-P450 Interactions and Metabolism Interactions between cytochromes P450 2B4 (CYP2B4) and 1A2 (CYP1A2) lead to alterations in toluene disposition and P450 uncoupling Correlating structure and function of drug-metabolizing enzymes: progress and ongoing challenges.Physical Studies of P450-P450 Interactions: Predicting Quaternary Structures of P450 Complexes in Membranes from Their X-ray Crystal Structures.Microsomal monooxygenase as a multienzyme system: the role of P450-P450 interactions.Formation of P450 · P450 complexes and their effect on P450 function Role of Cytochrome P450 2C8 in Drug Metabolism and Interactions.Characterization of interactions among CYP1A2, CYP2B4, and NADPH-cytochrome P450 reductase: Identification of specific protein complexes.Protein-protein and protein-membrane associations in the lignin pathway.Effects of polymorphic variation on the thermostability of heterogenous populations of CYP3A4 and CYP2C9 enzymes in solution

P2860

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P2860

CYP2C8 exists as a dimer in natural membranes.

http://www.wikidata.org/entity/Q34257489

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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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

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name

CYP2C8 exists as a dimer in natural membranes.

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CYP2C8 exists as a dimer in natural membranes.

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CYP2C8 exists as a dimer in natural membranes.

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type

label

CYP2C8 exists as a dimer in natural membranes.

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CYP2C8 exists as a dimer in natural membranes.

@en

CYP2C8 exists as a dimer in natural membranes.

@nl

prefLabel

CYP2C8 exists as a dimer in natural membranes.

@ast

CYP2C8 exists as a dimer in natural membranes.

@en

CYP2C8 exists as a dimer in natural membranes.

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Drug Metabolism and Disposition

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CYP2C8 exists as a dimer in natural membranes.

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P2093

Byron Kemper

http://www.w3.org/2001/XMLSchema#string

Eric F Johnson

http://www.w3.org/2001/XMLSchema#string

Gang Hu

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P2860

CYP2D6-CYP2C9 protein-protein interactions and isoform-selective effects on substrate binding and catalysis

Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum

Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity

Crystal structure of human cytochrome P450 2C9 with bound warfarin

Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site

Determinants of Cytochrome P450 2C8 Substrate Binding: STRUCTURES OF COMPLEXES WITH MONTELUKAST, TROGLITAZONE, FELODIPINE, AND 9-CIS-RETINOIC ACID

Cysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interface

X-ray structure of human aromatase reveals an androgen-specific active site

Functional interactions between cytochromes P450 1A2 and 2B4 require both enzymes to reside in the same phospholipid vesicle: evidence for physical complex formation.

CYP2C9-CYP3A4 protein-protein interactions: role of the hydrophobic N terminus.

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1976-1983

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scholarly article

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10.1124/DMD.110.034942

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11

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38

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2010-08-10T00:00:00Z

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20699412

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2967391

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