(Q28609779)

3 February 2017

title

Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains (English)

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3 February 2017

Jeffrey Shabanowitz

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Charles David Allis

object named as

C. David Allis

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3 February 2017

Scott D. Briggs

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Judd C. Rice

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3 February 2017

Beatrix Ueberheide

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3 February 2017

Cynthia M. Barber

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3 February 2017

Donald F. Hunt

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3 February 2017

Yoichi Shinkai

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3 February 2017

publication date

1 December 2003

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3 February 2017

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3 February 2017

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3 February 2017

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3 February 2017

page(s)

1591–1598

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Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation

3 February 2017

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Crystal structure of the nucleosome core particle at 2.8 A resolution

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Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component

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Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression

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BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias

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Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly

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Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries

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Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression

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A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells

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Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability

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Partitioning and plasticity of repressive histone methylation states in mammalian chromatin

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Histone methylation versus histone acetylation: new insights into epigenetic regulation

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Epigenetic codes for heterochromatin formation and silencing: rounding up the usual suspects

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7 January 2021

Active genes are tri-methylated at K4 of histone H3

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Gene-specific targeting of H3K9 methylation is sufficient for initiating repression in vivo.

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The language of covalent histone modifications

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Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3

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7 January 2021

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis

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Cellular memory and the histone code

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Chromatin disruption and modification

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Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails

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Analysis of core histones by liquid chromatography-mass spectrometry and peptide mapping

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7 January 2021

10.1016/S1097-2765(03)00479-9

Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017