Organization of cytochrome P450 enzymes involved in sex steroid synthesis: Protein-protein interactions in lipid membranes

Journal of Biological Chemistry

Volumn 284, Issue 48, 2009, Pages 33224-33232

  Praporski, Slavica ^a   Ng, Su May ^a   Nguyen, Ann D ^b   Corbin, C Jo ^b   Mechler, Adam ^a   Zheng, Jie ^c   Conley, Alan J ^b   Martin, Lisandra L ^a  

^a MONASH UNIVERSITY   (Australia)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AFM IMAGE; AROMATASE; BIOMIMETIC MEMBRANE; CYTOCHROME P450; ELECTRON DONORS; FLUORESCENCE RESONANCE ENERGY TRANSFER; FUNCTIONAL REGULATION; HIGH RESOLUTION; HIGHER ORDER; HOMODIMERIZATION; HOMODIMERIZE; HOMODIMERS; IN-VITRO; IN-VIVO; LIPID MEMBRANES; LIVE CELL; LIVING CELL; MEMBRANE ASSOCIATION; OXIDOREDUCTASES; PHOSPHATIDYL CHOLINE; PROTEIN-PROTEIN INTERACTIONS; SATURATED SURFACES; SEX STEROIDS; TRANS-MEMBRANE DOMAINS; WILD TYPES;

ACTIVATION ANALYSIS; ATOMIC FORCE MICROSCOPY; BIOMIMETICS; CATALYSTS; DRUG INTERACTIONS; ENERGY TRANSFER; ENZYMES; FLUORESCENCE; LAWS AND LEGISLATION; LIPID BILAYERS; MAMMALS; OLIGOMERS; OXIDE MINERALS; QUARTZ; QUARTZ CRYSTAL MICROBALANCES;

MEMBRANES;

AROMATASE; CYTOCHROME P450; PHOSPHATIDYLCHOLINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE; SEX HORMONE; STEROID 17ALPHA MONOOXYGENASE;

ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; ENZYME BINDING; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HUMAN CELL; LIPID MEMBRANE; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN PROTEIN INTERACTION; QUARTZ CRYSTAL MICROBALANCE; STEROIDOGENESIS;

AROMATASE; BACTERIAL PROTEINS; CELL LINE; CELL LINE, TUMOR; FLUORESCENCE RESONANCE ENERGY TRANSFER; GREEN FLUORESCENT PROTEINS; HUMANS; LIPID BILAYERS; LUMINESCENT PROTEINS; MICROSCOPY, ATOMIC FORCE; NADPH-FERRIHEMOPROTEIN REDUCTASE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; RECOMBINANT FUSION PROTEINS; STEROID 17-ALPHA-HYDROXYLASE; TRANSFECTION;

MAMMALIA;

EID: 70450248395     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.006064     Document Type: Article

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