Class I HDACs share a common mechanism of regulation by inositol phosphates

Molecular Cell

Volumn 51, Issue 1, 2013, Pages 57-67

  Millard, Christopher J ^a   Watson, Peter J ^a   Celardo, Ivana ^a   Gordiyenko, Yuliya ^b   Cowley, Shaun M ^a   Robinson, Carol V ^b   Fairall, Louise ^a   Schwabe, John W R ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; INOSITOL PHOSPHATE; INOSITOL TETRAKISPHOSPHATE; METASTASIS ASSOCIATED PROTEIN 1; NUCLEAR HORMONE RECEPTOR COREPRESSOR; PROTEIN; PROTEIN ELM2; PROTEIN NURD; PROTEIN SANT; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR; UNCLASSIFIED DRUG; HISTONE DEACETYLASE; MTA1 PROTEIN, HUMAN; REPRESSOR PROTEIN;

ARTICLE; CELL STRAIN HEK293; COMPLEX FORMATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HUMAN; MOLECULAR BIOLOGY; NUCLEOSOME; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYME SPECIFICITY; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; HEK293 CELL LINE;

AMINO ACID SEQUENCE; DIMERIZATION; HEK293 CELLS; HISTONE DEACETYLASE 1; HISTONE DEACETYLASES; HUMANS; INOSITOL PHOSPHATES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84891720942     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2013.05.020     Document Type: Article

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