Histone chaperone specificity in Rtt109 activation (Q27931083)

H3 histone acetyltransferase RTT109 YLL002W

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Karolin Luger

1 reference

ORCID Public Data File 2021

author name string

Young-Jun Park

1

0 references

Keely B Sudhoff

2

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Andrew J Andrews

3

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Laurie A Stargell

Nature Structural & Molecular Biology

4

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language of work or name

English

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publication date

September 2008

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published in

1 reference

1 December 2016

15

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page(s)

957-64

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describes a project that uses

ImageQuant

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2680711/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

cites work

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Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae

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Type B histone acetyltransferase Hat1p participates in telomeric silencing

20 March 2017

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Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein

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20 March 2017

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Histone chaperones: an escort network regulating histone traffic

7 April 2017

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29 September 2017

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29 September 2017

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29 September 2017

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Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes

2 June 2018

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2 June 2018

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New applications of simulated annealing in X-ray crystallography and solution NMR.

2 June 2018

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The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3

2 June 2018

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The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase.

27 November 2018

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Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding.

27 November 2018

1 reference

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Extraction, purification and analysis of histones

27 November 2018

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FNSMB.1480

31 March 2020

Identifiers

DOI

10.1038/NSMB.1480

1 reference

Dimensions Publication ID

4943490

1035842823

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4943490

1 reference

1 reference

1 reference