Stimulation of histone deacetylase activity by metabolites of intermediary metabolism

Journal of Biological Chemistry

Volumn 287, Issue 38, 2012, Pages 32006-32016

  Vogelauer, Maria ^a   Krall, Abigail S ^a   McBrian, Matthew A ^a,b   Li, Jing Yu ^a   Kurdistani, Siavash K ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL-COA; ACTIVATION KINETICS; ALLOSTERIC ACTIVATOR; BUTYRYL-COA; COENZYME A; ENZYMATIC ACTIVITIES; GLOBAL LEVELS; GLUCOSE-6-PHOSPHATE DEHYDROGENASE; HDAC INHIBITORS; HISTONE ACETYLATION; HISTONE DEACETYLASES; HISTONE H3; IN-VITRO; IN-VIVO; INTERMEDIARY METABOLISM; MALONYL-COA; MOLECULAR PROCESS; NATIVE COMPLEX; PHARMACOLOGICAL INHIBITION; RECRUITMENT MECHANISM; SUBCELLULAR LOCALIZATIONS; THERAPEUTIC TARGETS;

ACETYLATION; BIOMOLECULES; CHEMICAL ACTIVATION; GENE EXPRESSION; METABOLITES;

PROTEINS;

3 HYDROXY 3 METHYLGLUTARYL COENZYME A; ACETYL COENZYME A; BUTYRYL COENZYME A; COENZYME A; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE INHIBITOR; HISTONE H3; HISTONE H4; MALONYL COENZYME A; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CELL METABOLISM; CHEMICAL STRUCTURE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; HISTONE ACETYLATION; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; METABOLITE; PRIORITY JOURNAL;

ALLOSTERIC SITE; ANIMALS; CELL NUCLEUS; CHROMATIN; COENZYME A; EPIGENESIS, GENETIC; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HELA CELLS; HISTONE DEACETYLASE 1; HISTONE DEACETYLASES; HISTONES; HUMANS; INSECTS; KINETICS; MUTATION; RECOMBINANT PROTEINS; SIRTUINS; SUBCELLULAR FRACTIONS;

EID: 84866375559     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.362467     Document Type: Article

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