(Q44286566)

English

Hierarchical affinities and a bipartite interaction model for estrogen receptor isoforms and full-length steroid receptor coactivator (SRC/p160) family members

scientific article published on 22 January 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 December 2017

Hierarchical affinities and a bipartite interaction model for estrogen receptor isoforms and full-length steroid receptor coactivator (SRC/p160) family members (English)

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Europe PubMed Central

PubMed publication ID

1 December 2017

2

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1 December 2017

Bert W. O'Malley

7

object named as

Bert W O'Malley

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1 December 2017

author name string

Boris J Cheskis

1

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Europe PubMed Central

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1 December 2017

Chi-Wai Wong

3

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Europe PubMed Central

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1 December 2017

Jiemin Wong

4

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Europe PubMed Central

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1 December 2017

Barry Komm

5

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Europe PubMed Central

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1 December 2017

C Richard Lyttle

6

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1 December 2017

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publication date

22 January 2003

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1 December 2017

Journal of Biological Chemistry

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1 December 2017

278

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1 December 2017

15

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1 December 2017

13271-13277

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1 December 2017

Molecular mechanisms of action of steroid/thyroid receptor superfamily members

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Role of CBP/P300 in nuclear receptor signalling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex in embryonic development and thyroid hormone action

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Structure and specificity of nuclear receptor-coactivator interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Nuclear receptor conformation, coregulators, and tamoxifen-resistant breast cancer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Combinatorial control of gene expression by nuclear receptors and coregulators

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Nuclear receptor coregulators: multiple modes of modification

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Estrogen receptor (ER) modulators each induce distinct conformational changes in ER alpha and ER beta.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Structure-function evaluation of ER alpha and beta interplay with SRC family coactivators. ER selective ligands

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Peptide antagonists of the human estrogen receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

An additional region of coactivator GRIP1 required for interaction with the hormone-binding domains of a subset of nuclear receptors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Molecular determinants of the estrogen receptor-coactivator interface

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and receptor-dependent cell-free transcription of chromatin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

p300 requires its histone acetyltransferase activity and SRC-1 interaction domain to facilitate thyroid hormone receptor activation in chromatin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Estrogen receptor activation function 1 works by binding p160 coactivator proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Distinct steady-state nuclear receptor coregulator complexes exist in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

A transcriptional coactivator, steroid receptor coactivator-3, selectively augments steroid receptor transcriptional activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M211031200

21 January 2018

Identifiers

10.1074/JBC.M211031200

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

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