SMRT recruitment by PPARγ is mediated by specific residues located in its carboxy-terminal interacting domain (DOI:10.1016/j.mce.2006.08.004)

Molecular and Cellular Endocrinology

Volumn 267, Issue 1-2, 2007, Pages 138-143

  Sutanto, Maria M ^a   Symons, Melissa S ^a   Cohen, Ronald N ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

Adipogenesis; Corepressors; Peroxisome proliferator activated receptor; Silencing mediator of retinoid and thyroid hormone receptors; Transcriptional regulation

Indexed keywords

ERRATUM; ERROR; PRIORITY JOURNAL; ANIMAL; ARTICLE; CELL STRAIN 3T3; CERCOPITHECUS; CHEMICAL STRUCTURE; DIMERIZATION; METABOLISM; MOUSE; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; TRANSACTIVATION;

DNA BINDING PROTEIN; ISOPROTEIN; MUTANT PROTEIN; NUCLEAR RECEPTOR CO REPRESSOR 2; NUCLEAR RECEPTOR CO-REPRESSOR 2; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; REPRESSOR PROTEIN; RETINOID X RECEPTOR; UNCLASSIFIED DRUG;

3T3-L1 CELLS; ANIMALS; CERCOPITHECUS AETHIOPS; DIMERIZATION; DNA-BINDING PROTEINS; MICE; MODELS, MOLECULAR; MUTANT PROTEINS; PPAR GAMMA; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; RETINOID X RECEPTORS; TRANS-ACTIVATION (GENETICS);

EID: 33847326835     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2006.10.015     Document Type: Erratum

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