(Q28609769)

3 February 2017

title

Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain (English)

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3 February 2017

author

Hediye Erdjument-Bromage

4

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Paul Tempst

5

object named as

Paul Tempst

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Yi Zhang

object named as

Yi Zhang

7

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Huck Hui Ng

3

object named as

Huck Hui Ng

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3 February 2017

Qin Feng

1

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3 February 2017

Hengbin Wang

2

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3 February 2017

Kevin Struhl

6

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3 February 2017

language of work or name

English

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publication date

25 June 2002

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3 February 2017

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3 February 2017

volume

12

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3 February 2017

issue

12

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3 February 2017

page(s)

1052–1058

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The language of covalent histone modifications

3 February 2017

cites work

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Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae

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The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4

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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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Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression.

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S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase

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Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold

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Stem-loop binding protein, the protein that binds the 3' end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms

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The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities

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Tuning of an electrospray ionization source for maximum peptide-ion transmission into a mass spectrometer

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