Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies
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hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cellsLoss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancerApicidin: a novel antiprotozoal agent that inhibits parasite histone deacetylasePeptide mass mapping of acetylated isoforms of histone H4 from mouse lymphosarcoma cells treated with histone deacetylase (HDACs) inhibitors.The transcriptional regulator CBP has defined spatial associations within interphase nuclei.The regulation of gene activity by histones and the histone deacetylase RPD3.A developmental switch in H4 acetylation upstream of Xist plays a role in X chromosome inactivationGlucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1beta-induced histone H4 acetylation on lysines 8 and 12.Histone H4 acetylation of euchromatin and heterochromatin is cell cycle dependent and correlated with replication rather than with transcription.MOF and histone H4 acetylation at lysine 16 are critical for DNA damage response and double-strand break repairDosage compensation regulatory proteins and the evolution of sex chromosomes in Drosophila.Acetylation of core histones in response to HDAC inhibitors is diminished in mitotic HeLa cells.Genes are often sheltered from the global histone hyperacetylation induced by HDAC inhibitors.DNA methylation controls histone H3 lysine 9 methylation and heterochromatin assembly in Arabidopsis.Interphase chromosomes in Arabidopsis are organized as well defined chromocenters from which euchromatin loops emanateNAD+-dependent deacetylation of H4 lysine 16 by class III HDACs.Distinctive patterns of histone H4 acetylation are associated with defined sequence elements within both heterochromatic and euchromatic regions of the human genomeChromosomal localization links the SIN3-RPD3 complex to the regulation of chromatin condensation, histone acetylation and gene expression.Mass spectrometric molecular-weight determination of highly acidic compounds of biological significance via their complexes with basic polypeptides.Histones: at the crossroads of peptide and protein chemistry.Histone H4 lysine 16 acetylation breaks the genome's silenceFinding a balance: how diverse dosage compensation strategies modify histone h4 to regulate transcriptionHistone H4 acetylation and transcription in amphibian chromatinSpatial relationship between transcription sites and chromosome territories.Duplication and maintenance of heterochromatin domains.Distribution of histone H4 modifications as revealed by a panel of specific monoclonal antibodies.Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation patternGenome-wide patterns of histone modifications in yeast.Histone underacetylation is an ancient component of mammalian X chromosome inactivation.Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry.Stage-dependent redistributions of acetylated histones in nuclei of the early preimplantation mouse embryo.Histone H4 N-terminal acetylation in Kasumi-1 cells treated with depsipeptide determined by acetic acid-urea polyacrylamide gel electrophoresis, amino acid coded mass tagging, and mass spectrometry.A CAF-1 dependent pool of HP1 during heterochromatin duplicationHistone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner.Genome-wide mapping of histone modifications and mass spectrometry reveal H4 acetylation bias and H3K36 methylation at gene promoters in fission yeast.Immuno-cytogenetic manifestation of epigenetic chromatin modification marks in plants.A Quantitative Proteomic Analysis of In Vitro Assembled ChromatinHistone acetylation and globin gene switching.Histone H4 hyperacetylation precludes histone H4 lysine 20 trimethylation.Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin.
P2860
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P2860
Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies
description
1989 nî lūn-bûn
@nan
1989 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Histone H4 acetylation in huma ...... with site-specific antibodies
@ast
Histone H4 acetylation in huma ...... with site-specific antibodies
@en
Histone H4 acetylation in huma ...... with site-specific antibodies
@nl
type
label
Histone H4 acetylation in huma ...... with site-specific antibodies
@ast
Histone H4 acetylation in huma ...... with site-specific antibodies
@en
Histone H4 acetylation in huma ...... with site-specific antibodies
@nl
prefLabel
Histone H4 acetylation in huma ...... with site-specific antibodies
@ast
Histone H4 acetylation in huma ...... with site-specific antibodies
@en
Histone H4 acetylation in huma ...... with site-specific antibodies
@nl
P2093
P2860
P1433
P1476
Histone H4 acetylation in huma ...... with site-specific antibodies
@en
P2093
B M Turner
L P O'Neill
P2860
P356
10.1016/0014-5793(89)80947-0
P407
P577
1989-08-14T00:00:00Z