(Q33195734)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14660634%20AND%20SRC:MED&resulttype=core&format=json

21 December 2019

title

Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription (English)

1 reference

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21 December 2019

1

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21 December 2019

Patrick A Grant

7

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21 December 2019

5

C David Allis

1 reference

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21 December 2019

author name string

Michael S Torok

2

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21 December 2019

Zu-Wen Sun

3

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21 December 2019

David Schieltz

4

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21 December 2019

John R Yates

6

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21 December 2019

language of work or name

English

0 references

publication date

3 December 2003

1 reference

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Journal of Biological Chemistry

21 December 2019

published in

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21 December 2019

volume

279

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21 December 2019

page(s)

1867-1871

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21 December 2019

issue

3

1 reference

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The language of covalent histone modifications

21 December 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Gene silencing: trans-histone regulatory pathway in chromatin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

A conserved RING finger protein required for histone H2B monoubiquitination and cell size control.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Redundant roles for the TFIID and SAGA complexes in global transcription

21 January 2018

1 reference

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Analysis of Spt7 function in the Saccharomyces cerevisiae SAGA coactivator complex.

21 January 2018

1 reference

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Rad6-dependent ubiquitination of histone H2B in yeast

21 January 2018

1 reference

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Active genes are tri-methylated at K4 of histone H3

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

In vivo cross-linking and immunoprecipitation for studying dynamic Protein:DNA associations in a chromatin environment

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Functional organization of the yeast proteome by systematic analysis of protein complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Emerging roles of ubiquitin in transcription regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae

21 January 2018

1 reference

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TOM1p, a yeast hect-domain protein which mediates transcriptional regulation through the ADA/SAGA coactivator complexes.

21 January 2018

1 reference

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The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

SAGA is an essential in vivo target of the yeast acidic activator Gal4p

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

Identification and analysis of yeast nucleosomal histone acetyltransferase complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

In vivo assays to study histone ubiquitylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C300494200

21 January 2018

Identifiers

DOI

10.1074/JBC.C300494200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14660634%20AND%20SRC:MED&resulttype=core&format=json

21 December 2019

1 reference