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A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen
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scholarly article
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stated in
PubMed
PubMed ID
10713165
retrieved
15 November 2016
title
A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen
(English)
1 reference
stated in
PubMed
PubMed ID
10713165
retrieved
15 November 2016
main subject
PPARG coactivator 1 alpha
1 reference
stated in
GOA release 2020-03-11
DNA binding
1 reference
stated in
GOA release 2020-03-11
author name string
D Knutti
series ordinal
1
author given names
D
author last names
Knutti
1 reference
stated in
PubMed
PubMed ID
10713165
retrieved
8 February 2023
A Kaul
series ordinal
2
author given names
A
author last names
Kaul
1 reference
stated in
PubMed
PubMed ID
10713165
retrieved
8 February 2023
A Kralli
series ordinal
3
author given names
A
author last names
Kralli
1 reference
stated in
PubMed
PubMed ID
10713165
retrieved
8 February 2023
language of work or name
English
0 references
publication date
April 2000
0 references
published in
Molecular and Cellular Biology
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volume
20
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issue
7
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page(s)
2411-22
0 references
cites work
Composite co-activator ARC mediates chromatin-directed transcriptional activation
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Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction
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A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex
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High-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cells
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Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor
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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
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A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
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Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors
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A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor
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Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor
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Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations
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Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma
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A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
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A signature motif in transcriptional co-activators mediates binding to nuclear receptors
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Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
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Predicting coiled coils from protein sequences
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Essential role of Swp73p in the function of yeast Swi/Snf complex
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One-step gene disruption in yeast
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19 March 2017
The CBP co-activator is a histone acetyltransferase
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Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1
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Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein
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Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex
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TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors
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Steroid receptor coactivator-1 is a histone acetyltransferase
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The signal-dependent coactivator CBP is a nuclear target for pp90RSK
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A transcriptional co-repressor that interacts with nuclear hormone receptors
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Isolation of three novel human cyclins by rescue of G1 cyclin (cln) function in yeast
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Human D-type cyclin
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Mechanistic principles in NR box-dependent interaction between nuclear hormone receptors and the coactivator TIF2
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A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
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The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins
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The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
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Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
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Coactivator and corepressor complexes in nuclear receptor function
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Transcriptional activators direct histone acetyltransferase complexes to nucleosomes
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Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2
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Increasing the complexity of coactivation in nuclear receptor signaling
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HMG-1 stimulates estrogen response element binding by estrogen receptor from stably transfected HeLa cells
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27 September 2017
An additional region of coactivator GRIP1 required for interaction with the hormone-binding domains of a subset of nuclear receptors
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27 September 2017
CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV.
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27 September 2017
DA-complex assembly activity required for VP16C transcriptional activation
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27 September 2017
Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes
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27 September 2017
TLS (Translocated-in-Liposarcoma) Is a High-Affinity Interactor for Steroid, Thyroid Hormone, and Retinoid Receptors
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27 September 2017
Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.
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27 September 2017
Three amino acid substitutions selectively disrupt the activation but not the repression function of the glucocorticoid receptor N terminus.
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27 September 2017
Estradiol-inducible squelching and cell growth arrest by a chimeric VP16-estrogen receptor expressed in Saccharomyces cerevisiae: suppression by an allele of PDR1
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27 September 2017
The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences
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27 September 2017
LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones
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27 September 2017
[12] One-step gene disruption in yeast
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27 September 2017
Signal transduction and transcriptional regulation by glucocorticoid receptor-LexA fusion proteins
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27 September 2017
A novel cyclin gene from Drosophila complements CLN function in yeast
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27 September 2017
An evolutionarily conserved cyclin homolog from Drosophila rescues yeast deficient in G1 cyclins.
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27 September 2017
Identification of a negative regulatory function for steroid receptors
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27 September 2017
Determinants of promoter-specific activity by glucocorticoid receptor
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27 September 2017
Thyroid hormone export regulates cellular hormone content and response
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27 September 2017
An FK506-sensitive transporter selectively decreases intracellular levels and potency of steroid hormones
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27 September 2017
The coupling of multiple signal transduction pathways with steroid response mechanisms
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27 September 2017
Latent agonist activity of the steroid antagonist, RU486, is unmasked in cells treated with activators of protein kinase A.
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30 May 2018
Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element
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30 May 2018
Modulation of cell signaling pathways can enhance or impair glucocorticoid-induced gene expression without altering the state of receptor phosphorylation.
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30 May 2018
Tamoxifen activation of the estrogen receptor/AP-1 pathway: potential origin for the cell-specific estrogen-like effects of antiestrogens
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30 May 2018
Mammalian glucocorticoid receptor derivatives enhance transcription in yeast
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30 May 2018
Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene.
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30 May 2018
Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors
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30 May 2018
Role of the beta(3)-adrenergic receptor and/or a putative beta(4)-adrenergic receptor on the expression of uncoupling proteins and peroxisome proliferator-activated receptor-gamma coactivator-1.
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29 November 2018
The nuclear receptor ligand-binding domain: structure and function.
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29 November 2018
Co-activators and co-repressors in the integration of transcriptional responses
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=85422
retrieved
29 November 2018
The human oestrogen receptor functions in yeast
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=85422
retrieved
29 November 2018
Nerve growth factor up-regulates the transcriptional activity of CBP through activation of the p42/p44(MAPK) cascade
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10713165
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
A shared but complex bridge
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10713165
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10713165
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Negative effect of the transcriptional activator GAL4
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10713165
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.20.7.2411-2422.2000
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
566641
OpenCitations bibliographic resource ID
566641
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
566641
PMCID
85422
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
566641
PubMed ID
10713165
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
566641
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