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cytochrome P450 3A4 protein, human

Known as: Cytochrome P450 HLp, P450, FAMILY III, EC 1.14.13.67 
Cytochrome P450 3A4 (503 aa, ~57 kDa) is encoded by the human CYP3A4 gene. This protein is involved in the oxidation of steroids, fatty acids and… 
National Institutes of Health

Related topics

Related topics

50 relations
Alfentanil hydrochlorideBetamethasone benzoateCarbamazepineCortisone

Broader (3)

Cytochrome P-450 CYP3A4Cytochrome P450cytochrome P450 3A

Papers overview

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Highly Cited
2011
Highly Cited
2011
Conversion of 7-Dehydrocholesterol to 7-Ketocholesterol Is Catalyzed by Human Cytochrome P450 7A1 and Occurs by Direct Oxidation without an Epoxide Intermediate
7-Ketocholesterol is a bioactive sterol, a potent competitive inhibitor of cytochrome P450 7A1, and toxic in liver cells… 
Highly Cited
1999
Highly Cited
1999
Studies on cytochrome P-450-mediated bioactivation of diclofenac in rats and in human hepatocytes: identification of glutathione conjugated metabolites.
The nonsteroidal anti-inflammatory drug diclofenac causes a rare but potentially fatal hepatotoxicity that may be associated with… 
Highly Cited
1999
Highly Cited
1999
Prediction of human liver microsomal oxidations of 7-ethoxycoumarin and chlorzoxazone with kinetic parameters of recombinant cytochrome P-450 enzymes.
Different roles of individual forms of human cytochrome P-450 (CYP) in the oxidation of 7-ethoxycoumarin and chlorzoxazone were… 
Highly Cited
1999
Highly Cited
1999
In vitro metabolism of quinidine: the (3S)-3-hydroxylation of quinidine is a specific marker reaction for cytochrome P-4503A4 activity in human liver microsomes.
The aim of this study was to evaluate the (3S)-3-hydroxylation and the N-oxidation of quinidine as biomarkers for cytochrome P… 
Review
1996
Review
1996
Cytochrome P450, the arachidonic acid cascade, and hypertension: new vistas for an old enzyme system
As a participant of the endogenous arachidonic acid metabolic cascade, microsomal cy‐tochrome P450 metabolizes the fatty acid to… 
Highly Cited
1989
Highly Cited
1989
Evidence for cytochrome P-450NF, the nifedipine oxidase, being the principal enzyme involved in the bioactivation of aflatoxins in human liver.
In vitro studies with human liver indicate that the major catalyst involved in the bioactivation of the hepato-carcinogen… 
Highly Cited
1989
Highly Cited
1989
Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity.
P-450NF is the major enzyme in human liver involved in the metabolism of the calcium-channel blocker nifedipine. By screening a… 
Highly Cited
1988
Highly Cited
1988
Human P450PCN1: sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase.
P450PCN protein levels and nifedipine oxidase activities were quantitated in 12 human livers and were shown to be highly… 
Highly Cited
1986
Highly Cited
1986
Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase.
Human liver cytochrome P-450NF is the form of cytochrome P-450 responsible for the oxidation of the calcium-channel blocker… 
Highly Cited
1980
Highly Cited
1980
Plasma high-density lipoprotein cholesterol and hepatic cytochrome P-450 concentrations in epileptics undergoing anticonvulsant treatment.
Relation of plasma high-density lipoprotein (HDL) cholesterol concentration to hepatic microsomal enzyme activity in eighteen… 
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