(Q24554276)

English

The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes

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The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes (English)

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Lynn P. Freedman

6

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L P Freedman

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author name string

C Rachez

1

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M Gamble

2

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C P Chang

3

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G B Atkins

4

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M A Lazar

5

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publication date

April 2000

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Molecular and Cellular Biology

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20

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8

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2718-26

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1 reference

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Coactivators for the orphan nuclear receptor RORalpha

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Composite co-activator ARC mediates chromatin-directed transcriptional activation

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Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex

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Molecular determinants of the estrogen receptor-coactivator interface

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Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators

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A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation

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The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1

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Distinct steady-state nuclear receptor coregulator complexes exist in vivo

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Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways

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The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion

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A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system

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Transcriptional activation and repression by RORalpha, an orphan nuclear receptor required for cerebellar development

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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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Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex

1 reference

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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

1 reference

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Structure and specificity of nuclear receptor-coactivator interactions

1 reference

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Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma

1 reference

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A signature motif in transcriptional co-activators mediates binding to nuclear receptors

1 reference

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The transcriptional coactivators p300 and CBP are histone acetyltransferases

1 reference

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Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase

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Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein

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NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription

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Steroid receptor coactivator-1 is a histone acetyltransferase

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Competition between thyroid hormone receptor-associated protein (TRAP) 220 and transcriptional intermediary factor (TIF) 2 for binding to nuclear receptors. Implications for the recruitment of TRAP and p160 coactivator complexes

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Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation

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The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function

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1 reference

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p300 stimulates transcription instigated by ligand-bound thyroid hormone receptor at a step subsequent to chromatin disruption

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Stoichiometric and steric principles governing repression by nuclear hormone receptors

1 reference

https://pubmed.ncbi.nlm.nih.gov/10733574

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/MCB.20.8.2718-2726.2000

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