Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation

Molecular and Cellular Biology

Volumn 21, Issue 24, 2001, Pages 8371-8384

  Li, D ^a   Wang, F ^a   Samuels, H H ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; PROTEIN NRIF3; UNCLASSIFIED DRUG;

ALTERNATIVE RNA SPLICING; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DIMERIZATION; GENE EXPRESSION REGULATION; MOLECULAR MODEL; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; TRANSACTIVATION; TRANSCRIPTION REGULATION;

ALTERNATIVE SPLICING; AMINO ACID SEQUENCE; AMINO ACIDS; DIMERIZATION; DNA; FUNGAL PROTEINS; GENE DELETION; GENE EXPRESSION REGULATION; HELA CELLS; HUMANS; MICROSCOPY, FLUORESCENCE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEAR PROTEINS; PLASMIDS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; TIME FACTORS; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC; TRANSFECTION; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 0035192927     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.24.8371-8384.2001     Document Type: Article

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