(Q51023875)

27 March 2018

title

Purification of histone methyltransferases from HeLa cells. (English)

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27 March 2018

author name string

Jia Fang

series ordinal

1

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27 March 2018

Hengbin Wang

series ordinal

2

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27 March 2018

Yi Zhang

series ordinal

3

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27 March 2018

language of work or name

English

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publication date

1 January 2004

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27 March 2018

published in

Methods in Enzymology

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27 March 2018

volume

377

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27 March 2018

page(s)

213-226

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27 March 2018

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

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The language of covalent histone modifications

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Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase

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Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association

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Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase.

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Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

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Requirement of RSF and FACT for transcription of chromatin templates in vitro

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Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor

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Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

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Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase

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PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin

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Role of histone H3 lysine 27 methylation in Polycomb-group silencing

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Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation

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Regulation of chromatin structure by site-specific histone H3 methyltransferases

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Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor

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SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins

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

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mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression

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A murine ATFa-associated factor with transcriptional repressing activity

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Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein

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Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites

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Histone methyltransferase activity of a Drosophila Polycomb group repressor complex

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7 January 2021

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Identifiers

DOI

1 reference

27 March 2018

PubMed ID

14979027

1 reference

27 March 2018