About: Histone Deacetylases (HDACs): Evolution, Specificity, Role in Transcriptional Complexes, and Pharmacological Actionability

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About: Histone Deacetylases (HDACs): Evolution, Specificity, Role in Transcriptional Complexes, and Pharmacological Actionability Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Histone Deacetylases (HDACs): Evolution, Specificity, Role in Transcriptional Complexes, and Pharmacological Actionability
Creator	Giorgi, Federico Mercatelli, Daniele De Rosa, Piergiuseppe Milazzo, Giorgio Perini, Giovanni Triboli, Luca Muzio, Giulia
Source	Medline; PMC
abstract	Histone deacetylases (HDACs) are evolutionary conserved enzymes which operate by removing acetyl groups from histones and other protein regulatory factors, with functional consequences on chromatin remodeling and gene expression profiles. We provide here a review on the recent knowledge accrued on the zinc-dependent HDAC protein family across different species, tissues, and human pathologies, specifically focusing on the role of HDAC inhibitors as anti-cancer agents. We will investigate the chemical specificity of different HDACs and discuss their role in the human interactome as members of chromatin-binding and regulatory complexes.
has issue date	2020-05-15(xsd:dateTime)
bibo:doi	10.3390/genes11050556
bibo:pmid	32429325
has license	cc-by
sha1sum (hex)	6586847495a654336f7b57200bcd5a1808e6cc98
schema:url	https://doi.org/10.3390/genes11050556
resource representing a document's title	Histone Deacetylases (HDACs): Evolution, Specificity, Role in Transcriptional Complexes, and Pharmacological Actionability
has PubMed Central identifier	PMC7288346
has PubMed identifier	32429325
schema:publication	Genes (Basel)
resource representing a document's body	covid:6586847495a654336f7b57200bcd5a1808e6cc98#body_text
is schema:about of	named entity 'ACETYL' named entity 'chromatin remodeling' named entity 'interactome' named entity 'protein' named entity 'Actionability' named entity 'Pharmacological' named entity 'Transcriptional Complexes' named entity 'p27' named entity 'MLL' named entity 'RuvBL1' named entity 'breast cancer' named entity 'Unicellular eukaryotes' named entity 'DNA replication' named entity 'nematode' named entity 'protein' named entity 'mammals' named entity 'histone deacetylases' named entity 'Experimental evidence' named entity 'adipose tissue' named entity 'Entinostat' named entity 'RARα' named entity 'hydroxamates' named entity 'liver' named entity 'phenotypically' named entity 'Belinostat' named entity 'SIRT2' named entity 'HDACs' named entity 'Crebbp' named entity 'HDAC4' named entity 'cis' named entity 'biological function' named entity 'HDAC6' named entity 'Cdc6' named entity 'Aquifex aeolicus' named entity 'model organisms' named entity 'Aquifex aeolicus' named entity 'gene' named entity 'cytokine' named entity 'CoREST' named entity 'naturally derived' named entity 'chromatin' named entity 'HDAC8' named entity 'embryonic development' named entity 'HDACs' named entity 'binding activity' named entity 'H3K9me3' named entity 'lungs' named entity 'Arabidopsis thaliana' named entity 'HDAC' named entity 'Rag1' named entity 'corepressors' named entity 'depsipeptide' named entity 'Lysine' named entity 'exogenous' named entity 'deacetylation' named entity 'HDAC9' named entity 'nuclear localization signal' named entity 'prostate carcinoma' named entity 'thyroid hormone' named entity 'HDAC' named entity 'recombinant' named entity 'N-terminal region' named entity 'HDAC' named entity 'HDAC1' named entity 'HDACs' named entity 'Lysine' named entity 'ataxia telangiectasia' named entity 'transcription factors' named entity 'HDAC' named entity 'HDAC' named entity 'deacetylate' named entity 'HDACi' named entity 'PCNA' named entity 'bladder' named entity 'HDAC'

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