about
Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1An H3K36 methylation-engaging Tudor motif of polycomb-like proteins mediates PRC2 complex targetingSet2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression.Opposing roles for Set2 and yFACT in regulating TBP binding at promotersPolymerase IV occupancy at RNA-directed DNA methylation sites requires SHH1Molecular basis for chromatin binding and regulation of MLL5Dido3 PHD Modulates Cell Differentiation and DivisionStructures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologueThe language of covalent histone modificationsThe histone methylase Set2p and the histone deacetylase Rpd3p repress meiotic recombination at the HIS4 meiotic recombination hotspot in Saccharomyces cerevisiaeCotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex.A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions.BUR kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the PAF elongation complex.Histone H2B ubiquitylation is associated with elongating RNA polymerase IIRoles for Ctk1 and Spt6 in regulating the different methylation states of histone H3 lysine 36.Identification of lysine 37 of histone H2B as a novel site of methylationThe Ccr4-Not complex interacts with the mRNA export machineryChromatin condensation and recruitment of PHD finger proteins to histone H3K4me3 are mutually exclusiveHemi-methylated DNA regulates DNA methylation inheritance through allosteric activation of H3 ubiquitylation by UHRF1Gene silencing: trans-histone regulatory pathway in chromatin.Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification.Organismal differences in post-translational modifications in histones H3 and H4.A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation.Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor.Neuronal Stress Pathway Mediating a Histone Methyl/Phospho Switch Is Required for Herpes Simplex Virus Reactivation.The Set2/Rpd3S pathway suppresses cryptic transcription without regard to gene length or transcription frequencyA histone methylation network regulates transgenerational epigenetic memory in C. elegans.Influence of combinatorial histone modifications on antibody and effector protein recognition.Thermodynamic stability of histone H3 is a necessary but not sufficient driving force for its evolutionary conservationCatalysis-dependent stabilization of Bre1 fine-tunes histone H2B ubiquitylation to regulate gene transcription.Histone H3 K36 methylation is associated with transcription elongation in Schizosaccharomyces pombe.Methylation of histone H3 lysine 36 is required for normal development in Neurospora crassa.Peptide microarrays to interrogate the "histone code".The Taf14 YEATS domain is a reader of histone crotonylation.The nature of FSH induction by GnRH.Recombinant antibodies to histone post-translational modificationsProduct binding enforces the genomic specificity of a yeast polycomb repressive complex.An acetyl-methyl switch drives a conformational change in p53.Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1From histones to ribosomes: a chromatin regulator tangoes with translation.
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Brian D Strahl
@ast
Brian D Strahl
@en
Brian D Strahl
@es
Brian D Strahl
@nl
Brian D Strahl
@sl
type
label
Brian D Strahl
@ast
Brian D Strahl
@en
Brian D Strahl
@es
Brian D Strahl
@nl
Brian D Strahl
@sl
altLabel
Brian Strahl
@en
prefLabel
Brian D Strahl
@ast
Brian D Strahl
@en
Brian D Strahl
@es
Brian D Strahl
@nl
Brian D Strahl
@sl
P1053
C-7601-2012
P106
P108
P21
P2798
P31
P3829
P496
0000-0002-4947-6259