Splicing regulates NAD metabolite binding to histone macroH2A.
about
Immunopositivity for histone macroH2A1 isoforms marks steatosis-associated hepatocellular carcinomaThe histone variant macroH2A1 marks repressed autosomal chromatin, but protects a subset of its target genes from silencingThe histone variant macroH2A is an epigenetic regulator of key developmental genesPoly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1The atypical histone macroH2A1.2 interacts with HER-2 protein in cancer cellsOrphan macrodomain protein (human C6orf130) is an O-acyl-ADP-ribose deacylase: solution structure and catalytic propertiesA family of macrodomain proteins reverses cellular mono-ADP-ribosylationDeficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative diseaseIdentification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylasesChromatin affinity-precipitation using a small metabolic molecule: its application to analysis of O-acetyl-ADP-riboseCalorie restriction and the exercise of chromatinAnalysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolitesNuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylasesStructural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domainsFunctions of PARylation in DNA Damage Repair PathwaysSpliceosomal gene mutations in myelodysplasia: molecular links to clonal abnormalities of hematopoiesisChromatin Dynamics in Vivo: A Game of Musical ChairsThe Structural Determinants behind the Epigenetic Role of Histone VariantsSirtuins as regulators of metabolism and healthspanStructure and function of the ARH family of ADP-ribosyl-acceptor hydrolasesExpression and functionality of histone H2A variants in cancerThe nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in miceThe Crystal Structures of Chikungunya and Venezuelan Equine Encephalitis Virus nsP3 Macro Domains Define a Conserved Adenosine Binding PocketCrystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved propertyThe SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-QuadruplexesA macrodomain-containing histone rearranges chromatin upon sensing PARP1 activationThe structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolaseStructural and functional insights into alphavirus polyprotein processing and pathogenesisVisualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activitiesControl of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domainsDisruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolorHydrolase regulates NAD+ metabolites and modulates cellular redox.Loss of ATRX Suppresses Resolution of Telomere Cohesion to Control Recombination in ALT Cancer CellsSplicing switch of an epigenetic regulator by RNA helicases promotes tumor-cell invasivenessB-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.A phosphorylated subpopulation of the histone variant macroH2A1 is excluded from the inactive X chromosome and enriched during mitosis.N-lysine propionylation controls the activity of propionyl-CoA synthetase.Epigenetic responses to environmental change and their evolutionary implicationsGlobal analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells
P2860
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P2860
Splicing regulates NAD metabolite binding to histone macroH2A.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Splicing regulates NAD metabolite binding to histone macroH2A.
@ast
Splicing regulates NAD metabolite binding to histone macroH2A.
@en
Splicing regulates NAD metabolite binding to histone macroH2A.
@nl
type
label
Splicing regulates NAD metabolite binding to histone macroH2A.
@ast
Splicing regulates NAD metabolite binding to histone macroH2A.
@en
Splicing regulates NAD metabolite binding to histone macroH2A.
@nl
prefLabel
Splicing regulates NAD metabolite binding to histone macroH2A.
@ast
Splicing regulates NAD metabolite binding to histone macroH2A.
@en
Splicing regulates NAD metabolite binding to histone macroH2A.
@nl
P2093
P356
P1476
Splicing regulates NAD metabolite binding to histone macroH2A
@en
P2093
Andreas G Ladurner
Céline Pugieux
Klaus Scheffzek
P2888
P304
P356
10.1038/NSMB956
P577
2005-06-19T00:00:00Z