Increased acetylation in the DNA-binding domain of TR4 nuclear receptor by the coregulator ARA55 leads to suppression of TR4 transactivation

Journal of Biological Chemistry

Volumn 286, Issue 24, 2011, Pages 21129-21136

  Xie, Shaozhen ^a   Ni, Jing ^a   Lee, Yi Fen ^a   Liu, Su ^a   Li, Gonghui ^a   Shyr, Chih Rong ^b   Chang, Chawnshang ^a,b  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

^b CHINA MEDICAL UNIVERSITY HOSPITAL   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL TRANSFERASE; ANDROGEN RECEPTORS; COACTIVATORS; COREPRESSORS; DIFFERENT DOMAINS; DNA BINDING ACTIVITY; DNA-BINDING DOMAIN; FUNCTIONAL MECHANISMS; KEY REGULATORS; MUTATION ANALYSIS; NUCLEAR RECEPTORS; PHYSIOLOGICAL PROCESS; RECEPTOR TRANSACTIVATION; SMALL MOLECULES; THERAPEUTIC APPLICATION; TRANSACTIVATION; TRANSCRIPTIONAL ACTIVITY;

AMINO ACIDS; BINDING SITES; DNA; PHYSIOLOGY; TRANSCRIPTION FACTORS;

ACETYLATION;

ANDROGEN RECEPTOR; CELL NUCLEUS RECEPTOR; DNA; HISTONE ACETYLTRANSFERASE; LYSINE; NUCLEAR RECEPTOR TR4; PROTEIN ARA55; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

ACETYLATION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DNA BINDING; ENZYME ACTIVITY; GENETIC TRANSFECTION; IN VITRO STUDY; MOLECULAR MECHANICS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

ANIMALS; CELL LINE, TUMOR; DNA; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LIGANDS; LYSINE; MICE; MUTAGENESIS, SITE-DIRECTED; NUCLEAR RECEPTOR SUBFAMILY 2, GROUP C, MEMBER 2; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; TRANSCRIPTIONAL ACTIVATION; TREATMENT OUTCOME;

EID: 79958721153     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.208181     Document Type: Article

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