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The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
10490601
retrieved
1 December 2016
title
The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
10490601
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
Chromatin-binding transcription regulator ADA2 YDR448W
1 reference
stated in
GOA release 2020-03-11
Ahc1p YOR023C
1 reference
stated in
GOA release 2020-03-11
Histone acetyltransferase NGG1 YDR176W
1 reference
stated in
GOA release 2020-03-11
Histone acetyltransferase GCN5 YGR252W
1 reference
stated in
GOA release 2020-03-11
author name string
A Eberharter
series ordinal
1
0 references
D E Sterner
series ordinal
2
0 references
D Schieltz
series ordinal
3
0 references
A Hassan
series ordinal
4
0 references
J R Yates
series ordinal
5
0 references
S L Berger
series ordinal
6
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J L Workman
series ordinal
7
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language of work or name
English
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publication date
October 1999
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published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
10490601
retrieved
1 December 2016
volume
19
0 references
issue
10
0 references
page(s)
6621-31
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cites work
An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
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PubMed Central
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The ATM-related cofactor Tra1 is a component of the purified SAGA complex
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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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Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes.
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PubMed Central
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20 March 2017
Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates
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PubMed Central
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20 March 2017
A human SPT3-TAFII31-GCN5-L acetylase complex distinct from transcription factor IID
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PubMed Central
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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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20 March 2017
Histone-like TAFs within the PCAF histone acetylase complex
1 reference
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PubMed Central
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20 March 2017
Function of TAF(II)-containing complex without TBP in transcription by RNA polymerase II
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Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
1 reference
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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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PubMed Central
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ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3.
1 reference
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PubMed Central
reference URL
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Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
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1 reference
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PubMed Central
reference URL
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Gcn5p is involved in the acetylation of histone H3 in nucleosomes.
1 reference
stated in
PubMed Central
reference URL
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The TAF(II)250 subunit of TFIID has histone acetyltransferase activity
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation
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PubMed Central
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1 reference
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PubMed Central
reference URL
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Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4.
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PubMed Central
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1 reference
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PubMed Central
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1 reference
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PubMed Central
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1 reference
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PubMed Central
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1 reference
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1 reference
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PubMed Central
reference URL
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7 April 2017
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1 reference
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PubMed Central
reference URL
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1 reference
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PubMed Central
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1 reference
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PubMed Central
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29 September 2017
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1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
Distinctive patterns of histone H4 acetylation are associated with defined sequence elements within both heterochromatic and euchromatic regions of the human genome
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
Role for ADA/GCN5 products in antagonizing chromatin-mediated transcriptional repression
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p
1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Histone acetylation and chromatin assembly: a single escort, multiple dances?
1 reference
stated in
PubMed Central
reference URL
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1 reference
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PubMed Central
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29 September 2017
Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
ADA3: a gene, identified by resistance to GAL4-VP16, with properties similar to and different from those of ADA2.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
A new class of histone H2A mutations in Saccharomyces cerevisiae causes specific transcriptional defects in vivo
1 reference
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PubMed Central
reference URL
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29 September 2017
Histone acetylation: facts and questions
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PubMed Central
reference URL
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29 September 2017
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1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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29 September 2017
[12] One-step gene disruption in yeast
1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Reversible histone modification and the chromosome cell cycle
1 reference
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PubMed Central
reference URL
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29 September 2017
The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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2 June 2018
Histone acetylation: chromatin in action
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
retrieved
2 June 2018
Transcriptional activation by yeast PDR1p is inhibited by its association with NGG1p/ADA3p.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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27 November 2018
Structure/functional properties of the yeast dual regulator protein NGG1 that are required for glucose repression.
1 reference
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PubMed Central
reference URL
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27 November 2018
Acetylated histone H4 on the male X chromosome is associated with dosage compensation in Drosophila
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=84637
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27 November 2018
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/10490601
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10490601
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
A positive role for histone acetylation in transcription factor access to nucleosomal DNA
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10490601
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Expanded lysine acetylation specificity of Gcn5 in native complexes
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10490601
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Characterization of Physical Interactions of the Putative Transcriptional Adaptor, ADA2, with Acidic Activation Domains and TATA-binding Protein
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10490601
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identification and analysis of yeast nucleosomal histone acetyltransferase complexes
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10490601
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifying the major proteome components of Haemophilus influenzae type-strain NCTC 8143
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10490601
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.19.10.6621
0 references
PMCID
84637
0 references
PubMed ID
10490601
1 reference
stated in
PubMed
PubMed ID
10490601
retrieved
1 December 2016
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