Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
about
Accessing DNA damage in chromatin: Preparing the chromatin landscape for base excision repairPost-translational modifications of histones that influence nucleosome dynamicsMechanisms of Histone Deacetylase Inhibitor-Regulated Gene Expression in Cancer CellsThe CENP-A nucleosome: a battle between Dr Jekyll and Mr HydeStructural characterization of H3K56Q nucleosomes and nucleosomal arraysStructural basis for high-affinity binding of LEDGF PWWP to mononucleosomesStructure and organization of chromatin fiber in the nucleusChromatin-to-nucleoprotamine transition is controlled by the histone H2B variant TH2BChemical and biological tools for the preparation of modified histone proteinsApplication of the protein semisynthesis strategy to the generation of modified chromatinChemical and semisynthesis of posttranslationally modified proteins.Internal modifications in the CENP-A nucleosome modulate centromeric dynamics.Synthesis of histone H3 proteins by a thioacid capture ligation strategy.Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localizationPreparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes.Chemical and biochemical approaches in the study of histone methylation and demethylationA structural perspective on the where, how, why, and what of nucleosome positioning.Scratching the (lateral) surface of chromatin regulation by histone modifications.Local geometry and elasticity in compact chromatin structure.Differential contributions of histone H3 and H4 residues to heterochromatin structure.Histone fold modifications control nucleosome unwrapping and disassembly.Histones: at the crossroads of peptide and protein chemistry.A quantitative model of nucleosome dynamics.Histone core phosphorylation regulates DNA accessibility.Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF.Autoacetylation of the MYST lysine acetyltransferase MOF proteinRegulation of the nucleosome unwrapping rate controls DNA accessibility.Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamicsDivergent Residues Within Histone H3 Dictate a Unique Chromatin Structure in Saccharomyces cerevisiaeA reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-Acylurea approach.Site-specific acetylation of the proteasome activator REGγ directs its heptameric structure and functions.ATP-dependent nucleosome unwrapping catalyzed by human RAD51Histone tails: ideal motifs for probing epigenetics through chemical biology approaches.Dynamics of histone H3 acetylation in the nucleosome core during mouse pre-implantation development.Mechanism(s) of SWI/SNF-induced nucleosome mobilizationSequence-dependent thymine dimer formation and photoreversal rates in double-stranded DNAEvidence that nucleosomes inhibit mismatch repair in eukaryotic cellsChemical approaches for studying histone modifications.Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.Spreading chromatin into chemical biology.
P2860
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P2860
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 11 June 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
@en
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
@nl
type
label
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
@en
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
@nl
prefLabel
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
@en
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.
@nl
P2093
P2860
P356
P1476
Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding
@en
P2093
Alex M Mooney
Annick Edon
Jonathan W Picking
Justin A North
Michael G Poirier
Mridula Manohar
Richard Fishel
Robin J Nakkula
P2860
P304
23312-23321
P356
10.1074/JBC.M109.003202
P407
P577
2009-06-11T00:00:00Z