Structure of the spt16 middle domain reveals functional features of the Histone chaperone FACT

Journal of Biological Chemistry

Volumn 288, Issue 15, 2013, Pages 10188-10194

  Kemble, David J ^a   Whitby, Frank G ^a   Robinson, Howard ^b   McCullough, Laura L ^a   Formosa, Tim ^a   Hill, Christopher P ^a  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FUNCTIONAL FEATURES; GENETIC DATA; HETERO DIMERS; PHYSIOLOGICAL FUNCTIONS; PLECKSTRIN HOMOLOGY; PLECKSTRIN HOMOLOGY DOMAINS; SMALL SUBUNITS;

BIOCHEMISTRY; BIOLOGY;

PROTEINS;

CARBOXY TERMINAL TELOPEPTIDE; CHAPERONE; HISTONE CHAPERONE FACT; HISTONE CHAPERONE RTT106; HISTONE H3; HISTONE H4; PLECKSTRIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; HIGH MOBILITY GROUP PROTEINS; HUMANS; MOLECULAR CHAPERONES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSCRIPTION FACTORS; TRANSCRIPTIONAL ELONGATION FACTORS;

EUKARYOTA;

EID: 84876275605     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C113.451369     Document Type: Article

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