B. Strahl

Publications225
h-index67
Citations29,912
Highly Influential Citations1,578
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The language of covalent histone modifications
TLDR
It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
View on Nature
Regulation of chromatin structure by site-specific histone H3 methyltransferases
TLDR
A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
View on Nature
Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
TLDR
In vivo evidence is provided that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast, defining a conserved pathway wherein sequential histone modifications establish a “histone code” essential for the epigenetic inheritance of heterochROMatin assembly.
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Cotranscriptional Set2 Methylation of Histone H3 Lysine 36 Recruits a Repressive Rpd3 Complex
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Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor
TLDR
A mutation in theS-adenosyl-l-methionine–binding site of PRMT1 substantially crippled its nuclear receptor coactivator activity and indicates that Arg 3 methylation plays an important role in transcriptional regulation.
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Evidence for nucleosome depletion at active regulatory regions genome-wide
TLDR
Evidence is presented that the basic repeating units of eukaryotic chromatin, nucleosomes, are depleted from active regulatory elements throughout the Saccharomyces cerevisiae genome in vivo and the level of nucleosome occupancy is inversely proportional to the transcriptional initiation rate at the promoter.
View on Nature
Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae.
TLDR
Chromatin immunoprecipitation assays show that H3 Lys4 methylation is present at the rDNA locus and that Set1-mediated H3 lysine 4 (Lys4)methylation is required for repression of RNA polymerase II transcription within rDNA, and suggest that Set 1-mediatedH3 Lys 4 methylation are required for normal cell growth and transcriptional silencing.
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Gene silencing: Trans-histone regulatory pathway in chromatin
TLDR
It is suggested that H2B ubiquitination acts as a master switch that controls the site-selective histone methylation patterns responsible for this silencing.
View on Springer
A Novel Domain in Set2 Mediates RNA Polymerase II Interaction and Couples Histone H3 K36 Methylation with Transcript Elongation
TLDR
It is determined that deletion of SET2, its SRI domain, or amino acid substitutions at K36 result in an alteration of RNAPII occupancy levels over transcribing genes, which indicates K36 methylation, established by the Sri domain-mediated association of Set2 with RNAP II, plays an important role in the transcription elongation process.
View on ASMUSA
Set2 Is a Nucleosomal Histone H3-Selective Methyltransferase That Mediates Transcriptional Repression
TLDR
The biochemical purification and characterization of Set2 are described, a novel HMT that is site-specific for lysine 36 (Lys36) of the H3 tail and it is suggested that Set2 and methylation at H3 Lys36 play a role in the repression of gene transcription.
View on ASMUSA
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