Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4 - Wikidata - wikimedia - TriplyDB

Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4

Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4

http://www.wikidata.org/entity/Q38393619

about

A novel type of allosteric regulation: functional cooperativity in monomeric proteins Optimization of the bacterial cytochrome P450 BM3 system for the production of human drug metabolites Cytochromes P450 in nanodiscs.Defining CYP3A4 structural responses to substrate binding. Raman spectroscopic studies of a nanodisc-incorporated mammalian cytochrome P450.Analysis of heterotropic cooperativity in cytochrome P450 3A4 using alpha-naphthoflavone and testosterone.Interactions of cytochrome P450s with their ligands.Current Approaches for Investigating and Predicting Cytochrome P450 3A4-Ligand Interactions Mechanism of drug-drug interactions mediated by human cytochrome P450 CYP3A4 monomer Nanodiscs in Membrane Biochemistry and Biophysics.Spectroscopic studies of the cytochrome P450 reaction mechanisms.Nanodiscs in the studies of membrane-bound cytochrome P450 enzymes.Drug-Drug Interactions between Atorvastatin and Dronedarone Mediated by Monomeric CYP3A4.Membrane-embedded substrate recognition by cytochrome P450 3A4.

P2860

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P2860

Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4

http://www.wikidata.org/entity/Q38393619

description

2009 nî lūn-bûn

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

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2009年论文

@zh-cn

name

Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4

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type

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Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4

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Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4

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J.ABB.2009.06.013

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Archives of Biochemistry and Biophysics

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Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4

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Stephen G Sligar

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P2860

Redox potential control by drug binding to cytochrome P450 3A4

Predicting in vivo drug interactions from in vitro drug discovery data.

A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4.

Enzyme kinetics of cytochrome P450-mediated reactions.

Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions.

Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians.

Diazepam metabolism by human liver microsomes is mediated by both S-mephenytoin hydroxylase and CYP3A isoforms.

A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase.

Structural basis for ligand promiscuity in cytochrome P450 3A4.

Non-Michaelis-Menten kinetics in cytochrome P450-catalyzed reactions.

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146-152

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