Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1 (Q24291436)

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9 November 2019

title

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

1 reference

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Protein arginine methyltransferase 1

9 November 2019

main subject

1 reference

histone methyltransferase activity (H4-R3 specific)

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Brian D Strahl

1

1 reference

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9 November 2019

Scott D Briggs

2

1 reference

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9 November 2019

11

C D Allis

1 reference

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9 November 2019

author name string

C J Brame

3

1 reference

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9 November 2019

J A Caldwell

4

1 reference

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9 November 2019

S S Koh

5

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9 November 2019

H Ma

6

1 reference

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9 November 2019

R G Cook

7

1 reference

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9 November 2019

J Shabanowitz

8

1 reference

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9 November 2019

D F Hunt

9

1 reference

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9 November 2019

M R Stallcup

10

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9 November 2019

language of work or name

English

0 references

publication date

1 June 2001

1 reference

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9 November 2019

number of pages

5

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inferred from page(s)

published in

Current Biology

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9 November 2019

volume

11

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9 November 2019

issue

12

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9 November 2019

page(s)

996-1000

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The language of covalent histone modifications

9 November 2019

cites work

1 reference

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7 January 2021

Acetylation and chromosomal functions.

1 reference

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7 January 2021

Histone methylation versus histone acetylation: new insights into epigenetic regulation

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7 January 2021

Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena

1 reference

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7 January 2021

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

1 reference

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7 January 2021

Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Regulation of transcription by a protein methyltransferase

1 reference

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7 January 2021

Role of protein methylation in chromatin remodeling and transcriptional regulation

1 reference

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7 January 2021

Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities

1 reference

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7 January 2021

RNA and protein interactions modulated by protein arginine methylation.

1 reference

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7 January 2021

PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells

1 reference

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7 January 2021

Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3

1 reference

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7 January 2021

Signaling to chromatin through histone modifications

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7 January 2021

Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation

1 reference

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7 January 2021

Regulation of chromatin structure by site-specific histone H3 methyltransferases

1 reference

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7 January 2021

Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14.

1 reference

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7 January 2021

10.1016/S0960-9822(01)00294-9

Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11448779 AND SRC:MED&resulttype=core&format=json

9 November 2019

1 reference

Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017