How the flexibility of human histone deacetylases influences ligand binding: An overview

Drug Discovery Today

Volumn 20, Issue 6, 2015, Pages 736-742

  Deschamps, Nathalie ^a   Simões Pires, Claudia Avello ^a   Carrupt, Pierre Alain ^a   Nurisso, Alessandra ^a  

^a UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 10; HISTONE DEACETYLASE 11; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE 7; HISTONE DEACETYLASE 8; ISOPROTEIN; UBIQUITIN; HISTONE DEACETYLASE INHIBITOR; ISOENZYME; LIGAND; PROTEIN BINDING;

ALLOSTERISM; BINDING AFFINITY; BIOLOGICAL FUNCTIONS; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTALLOGRAPHY; DRUG BINDING; ENZYME STRUCTURE; HUMAN; LIGAND BINDING; MOLECULAR DYNAMICS; NONHUMAN; PLASTICITY; PROTEIN PROTEIN INTERACTION; REVIEW; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DESIGN; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; METABOLISM; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

ANIMALS; BINDING SITES; CATALYTIC DOMAIN; DRUG DESIGN; HISTONE DEACETYLASE INHIBITORS; HISTONE DEACETYLASES; HUMANS; ISOENZYMES; LIGANDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84934958844     PISSN: 13596446     EISSN: 18785832     Source Type: Journal    
DOI: 10.1016/j.drudis.2015.01.004     Document Type: Review

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