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Volumn 513, Issue 2, 2011, Pages 110-118

Formation of raloxifene homo-dimer in CYP3A4, evidence for multi-substrate binding in a single catalytically competent P450 active site

(5) Davis, John A a Greene, Robert J a Han, Sean a,b Rock, Dan A a Wienkers, Larry C a

a AMGEN INC (United States)

b PFIZER INC (United States)

Author keywords

Binding sites; CYP3A4; Homo dimer; Metabolism; Phenoxy radical; Raloxifene

Indexed keywords

CYTOCHROME P450 3A4; HOMODIMER; PEROXIDASE; RALOXIFENE; REACTIVE OXYGEN METABOLITE;

ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; ENZYME SUBSTRATE COMPLEX; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HISTOGRAM; MASS SPECTROMETRY; NUCLEOPHILICITY; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; ULTRAVIOLET RADIATION;

CATALYTIC DOMAIN; CYTOCHROME P-450 CYP3A; DEUTERIUM EXCHANGE MEASUREMENT; DIMERIZATION; ELECTROCHEMICAL TECHNIQUES; HORSERADISH PEROXIDASE; HUMANS; MASS SPECTROMETRY; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; RALOXIFENE;

ARMORACIA RUSTICANA;

EID: 80051789386 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2011.06.016 Document Type: Article

Times cited : (13)

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