Suppression of sterol 12α-hydroxylase transcription by the short heterodimer partner: Insights into the repression mechanism

Nucleic Acids Research

Volumn 29, Issue 19, 2001, Pages 4035-4042

  Del Castillo Olivares, A ^a   Gil, G ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BILE ACID; CHENODEOXYCHOLIC ACID; CHOLESTEROL; CHOLIC ACID; CYTOCHROME P450 8B1; CYTOCHROME P450 ISOENZYME; FETOPROTEIN; HEPATIC NUCLEAR FACTOR 4; NUCLEAR FACTOR; OXYGENASE; STEROL 12ALPHA HYDROXYLASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; CELL RECEPTOR; CYTOCHROME P450; DNA BINDING PROTEIN; FETOPROTEIN TRANSCRIPTION FACTOR; HEPATOCYTE NUCLEAR FACTOR 4; MLX PROTEIN, HUMAN; PHOSPHOPROTEIN; REPRESSOR PROTEIN; SMALL HETERODIMER PARTNER PROTEIN; STEROID 12ALPHA MONOOXYGENASE; STEROID MONOOXYGENASE;

ANIMAL CELL; ARTICLE; BILE ACID METABOLISM; BINDING SITE; BIOSYNTHESIS; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME REGULATION; ENZYME REPRESSION; ENZYME SPECIFICITY; ENZYME SYNTHESIS; FEEDBACK SYSTEM; GENETIC CODE; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; HYDROPHOBICITY; LABORATORY TEST; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BINDING; REGULATORY MECHANISM; TRANSCRIPTION REGULATION; CELL LINE; CHEMISTRY; GENETICS; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; REPORTER GENE;

BASIC HELIX-LOOP-HELIX LEUCINE ZIPPER TRANSCRIPTION FACTORS; BILE ACIDS AND SALTS; BINDING SITES; CELL LINE; CYTOCHROME P-450 ENZYME SYSTEM; DNA-BINDING PROTEINS; DOWN-REGULATION; GENES, REPORTER; HEPATOCYTE NUCLEAR FACTOR 4; HUMANS; PHOSPHOPROTEINS; PROMOTER REGIONS (GENETICS); PROTEIN STRUCTURE, TERTIARY; RECEPTORS, CYTOPLASMIC AND NUCLEAR; REPRESSOR PROTEINS; STEROID 12-ALPHA-HYDROXYLASE; STEROID HYDROXYLASES; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 0035470833     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/29.19.4035     Document Type: Article

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