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Cluster analysis of mass spectrometry data reveals a novel component of SAGA
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scholarly article
1 reference
stated in
PubMed
PubMed ID
15282323
retrieved
1 December 2016
title
Cluster analysis of mass spectrometry data reveals a novel component of SAGA
(English)
1 reference
stated in
PubMed
PubMed ID
15282323
retrieved
1 December 2016
main subject
cell biology
0 references
SAGA histone acetyltransferase complex subunit SGF11 YPL047W
1 reference
stated in
GOA release 2020-03-11
mass spectrometry
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cluster analysis
1 reference
based on heuristic
inferred from title
author name string
David W Powell
series ordinal
1
0 references
Connie M Weaver
series ordinal
2
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Jennifer L Jennings
series ordinal
3
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K Jill McAfee
series ordinal
4
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Yue He
series ordinal
5
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P Anthony Weil
series ordinal
6
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Andrew J Link
series ordinal
7
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language of work or name
English
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publication date
August 2004
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published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
15282323
retrieved
1 December 2016
volume
24
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page(s)
7249-59
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issue
16
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cites work
Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.
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The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.
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Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo
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SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription
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Analysis of Spt7 function in the Saccharomyces cerevisiae SAGA coactivator complex.
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Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry
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Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
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Functional organization of the yeast proteome by systematic analysis of protein complexes
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Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation
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The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4.
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Acetylation of histones and transcription-related factors
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PubMed Central
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The language of covalent histone modifications
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Inhibition of TATA-binding protein function by SAGA subunits Spt3 and Spt8 at Gcn4-activated promoters
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20 March 2017
The ATM-related cofactor Tra1 is a component of the purified SAGA complex
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PubMed Central
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20 March 2017
Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.
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PubMed Central
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20 March 2017
Cluster analysis and display of genome-wide expression patterns
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PubMed Central
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20 March 2017
Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes.
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A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation
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PubMed Central
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Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex
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20 March 2017
Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
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20 March 2017
ADR1 activation domains contact the histone acetyltransferase GCN5 and the core transcriptional factor TFIIB.
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Dissecting the regulatory circuitry of a eukaryotic genome
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Open source clustering software
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Cooperation between complexes that regulate chromatin structure and transcription
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Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
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Direct analysis of protein complexes using mass spectrometry
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Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor
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Components of the SAGA histone acetyltransferase complex are required for repressed transcription of ARG1 in rich medium
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29 September 2017
Redundant roles for the TFIID and SAGA complexes in global transcription
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29 September 2017
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29 September 2017
Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo
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29 September 2017
Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf/Swi and Srb/mediator complexes
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29 September 2017
Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo.
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29 September 2017
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29 September 2017
Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones
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29 September 2017
Chromatin structure and transcription
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29 September 2017
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2 June 2018
The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes.
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2 June 2018
Inhibition of transcription selectively reduces the level of ubiquitinated histone H2B in chromatin
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2 June 2018
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27 November 2018
SWI/SNF complexes and facilitation of TATA binding protein:nucleosome interactions.
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27 November 2018
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15282323
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ADA3 and ADA2
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15282323
retrieved
12 December 2020
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Identifiers
DOI
10.1128/MCB.24.16.7249-7259.2004
1 reference
stated in
PubMed
PubMed ID
15282323
retrieved
1 December 2016
PMCID
479721
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PubMed ID
15282323
1 reference
stated in
PubMed
PubMed ID
15282323
retrieved
1 December 2016
ResearchGate publication ID
8428301
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