About: Acetylation and deacetylation of non-histone proteins

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scientific article (publication date: 19 December 2005)

Attributes	Values
rdf:type	Item
description	article scientifique publié en 2005 (fr) artículu científicu espublizáu en 2005 (ast) 2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված (hy) 2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в грудні 2005 (uk) مقالة علمية (نشرت في 19-12-2005) (ar) wetenschappelijk artikel (gepubliceerd op 2005/12/19) (nl) im Dezember 2005 veröffentlichter wissenschaftlicher Artikel (de) scientific article (publication date: 19 December 2005) (en)
publication date	wds:Q29619636-35327DC4-0E1A-4AB4-8EDD-C37C4854A394
publication date	2005-12-19 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q29619636-CFA88B2D-F1B2-4D5C-BBDF-FC9A45E2A01E
language of work or name	English
author name string	wds:Q29619636-2C96B56B-0F3F-4B21-A58B-7D410E07E953 wds:Q29619636-B51A80A2-AAF9-4622-A69D-45E02837BA32 wds:Q29619636-BEABDAD6-FC12-4EAD-927B-DAA6DBA6064D wds:Q29619636-C3C608A1-42D9-460F-8A64-EDF90493AF5F
OpenCitations bibliographic resource ID	wds:Q29619636-53AACF36-5B2F-4218-A672-71EFBB93F824
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/229796
author name string	Zhang X Seto E Sengupta N Glozak MA
OpenCitations bibliographic resource ID	229796
rdfs:label	Acetylation and deacetylation of non-histone proteins (en) Acetylation and deacetylation of non-histone proteins (ast)
skos:prefLabel	Acetylation and deacetylation of non-histone proteins (en) Acetylation and deacetylation of non-histone proteins (ast)
name	Acetylation and deacetylation of non-histone proteins (en) Acetylation and deacetylation of non-histone proteins (ast)
title	wds:Q29619636-2DB6F075-1254-4F6D-A75A-D1485B3BBFEE
title	Acetylation and deacetylation of non-histone proteins (en)
page(s)	wds:Q29619636-342B2592-46A1-440A-8F49-72DD03C09A60
page(s)	15-23
instance of	wds:Q29619636-4D4372FC-3E36-4785-9A2B-B81E61F41F31 wds:Q29619636-713cac28-f075-43fd-a6b2-7ea05b0359c7
instance of	review article scholarly article
PubMed ID	wds:Q29619636-29DCAA0C-E9EE-4ED5-8BB1-8F228C23AE12
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16289629
PubMed ID	16289629
published in	wds:Q29619636-EAC71C0A-FDBB-43FB-9C50-AE60D8F9BA1F
published in	Gene
volume	wds:Q29619636-915CA1A2-AE10-4CB1-A745-9E8FC9EA168E
volume	363
DOI	wds:Q29619636-BA372251-3B66-41E3-B1BF-41B95524F6BF
DOI	http://dx.doi.org/10.1016/J.GENE.2005.09.010
DOI	10.1016/J.GENE.2005.09.010
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q29619636
is cites work of	Metabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon - and O-acetylation HDAC4 represses p21(WAF1/Cip1) expression in human cancer cells through a Sp1-dependent, p53-independent mechanism Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases Histone deacetylase inhibitors: molecular mechanisms of action Caspase-8 cleaves histone deacetylase 7 and abolishes its transcription repressor function Myelin basic protein undergoes a broader range of modifications in mammals than in lower vertebrates Significant enhancement of hPrx1 chaperone activity through lysine acetylation. HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics Small changes, big impact: posttranslational modifications and function of huntingtin in Huntington disease. Deacetylation of the DNA-binding domain regulates p53-mediated apoptosis Transcriptional regulation by the Set7 lysine methyltransferase Enhanced deacetylation of p53 by the anti-apoptotic protein HSCO in association with histone deacetylase 1. Belinostat: clinical applications in solid tumors and lymphoma Expression level of histone deacetylase 2 correlates with occurring of chronic obstructive pulmonary diseases Acetylation of glucokinase regulatory protein decreases glucose metabolism by suppressing glucokinase activity. Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation. HDAC inhibitors in cancer biology: emerging mechanisms and clinical applications Enhanced histone deacetylase enzyme activity in primary myelofibrosis. Valproic acid as a potential inhibitor of Plasmodium falciparum histone deacetylase 1 (PfHDAC1): an in silico approach. Mitochondrial protein acetylation regulates metabolism Site-specific acetylation of p53 directs selective transcription complex assembly. Histone deacetylase inhibitors suppress rheumatoid arthritis fibroblast-like synoviocyte and macrophage IL-6 production by accelerating mRNA decay Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain Histone deacetylase inhibitors as novel anticancer therapeutics. Histone deacetylase inhibitor romidepsin enhances anti-tumor effect of erlotinib in non-small cell lung cancer (NSCLC) cell lines Chromatin remodeling and circadian control: master regulator CLOCK is an enzyme. Structure and mechanism of non-histone protein acetyltransferase enzymes Histone deacetylase 3 is required for maintenance of bone mass during aging Selective boosting of transcriptional and behavioral responses to drugs of abuse by histone deacetylase inhibition. Histone deacetylase inhibitors prevent apoptosis following lethal hemorrhagic shock in rodent kidney cells N-Myc down regulation induced differentiation, early cell cycle exit, and apoptosis in human malignant neuroblastoma cells having wild type or mutant p53. miR-93 suppresses proliferation and colony formation of human colon cancer stem cells Class IIa histone deacetylases: regulating the regulators HDAC4 promotes growth of colon cancer cells via repression of p21. The cyclin-dependent kinase inhibitor p21 is a crucial target for histone deacetylase 1 as a regulator of cellular proliferation. CBP knockdown inhibits angiotensin II-induced vascular smooth muscle cells proliferation through downregulating NF-kB transcriptional activity Histone deacetylase inhibitor (HDACI) PCI-24781 potentiates cytotoxic effects of doxorubicin in bone sarcoma cells HDAC1 and HDAC2 control the transcriptional program of myelination and the survival of Schwann cells. Hopx and Hdac2 interact to modulate Gata4 acetylation and embryonic cardiac myocyte proliferation SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination Acetylation of Smad2 by the co-activator p300 regulates activin and transforming growth factor beta response Lysine acetylation: codified crosstalk with other posttranslational modifications Regulation of P-TEFb elongation complex activity by CDK9 acetylation CLOCK-mediated acetylation of BMAL1 controls circadian function Epigenetic changes induced by curcumin and other natural compounds. The role of epigenetic regulation in stem cell and cancer biology Deacetylase inhibition promotes the generation and function of regulatory T cells. Posttranslational modification of p53: cooperative integrators of function

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