Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. (Q54027019)

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scientific article published in November 1997

Language	Label	Description	Also known as
English	Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators.	scientific article published in November 1997

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. (English)

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

author name string

Ikonen T

1

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

Palvimo JJ

2

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

Jänne OA

3

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

language of work or name

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publication date

1 November 1997

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

272

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

47

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

29821-29828

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

Androgen receptor defects: historical, clinical, and molecular perspectives

1 reference

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The nuclear receptor superfamily: the second decade

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Steroid hormone receptors: many actors in search of a plot

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Regulation of gene expression by retinoic acid receptors

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Androgen-specific gene activation via a consensus glucocorticoid response element is determined by interaction with nonreceptor factors

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21 January 2018

Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element

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The N-terminal region of the chicken progesterone receptor specifies target gene activation

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A and B forms of the androgen receptor are present in human genital skin fibroblasts

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Cloning and characterization of a specific coactivator, ARA70, for the androgen receptor in human prostate cells

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A transcriptional co-repressor that interacts with nuclear hormone receptors

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A nuclear hormone receptor-associated protein that inhibits transactivation by the thyroid hormone and retinoic acid receptors

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Nuclear receptor coactivators and corepressors

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Sequence and characterization of a coactivator for the steroid hormone receptor superfamily

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Molecular cloning and properties of a full-length putative thyroid hormone receptor coactivator

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GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors

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

1 reference

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21 January 2018

The nuclear hormone receptor coactivator SRC-1 is a specific target of p300.

1 reference

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21 January 2018

Versatile molecular glue. Transcriptional control

1 reference

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Role of CBP/P300 in nuclear receptor signalling

1 reference

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21 January 2018

Androgen receptor-mediated transcriptional regulation in the absence of direct interaction with a specific DNA element

1 reference

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21 January 2018

Domains of the Human Androgen Receptor Involved in Steroid Binding, Transcriptional Activation, and Subcellular Localization

1 reference

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21 January 2018

Identification of two transcription activation units in the N-terminal domain of the human androgen receptor

1 reference

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21 January 2018

Structural analysis of complementary DNA and amino acid sequences of human and rat androgen receptors

1 reference

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21 January 2018

Effects of mitogens on androgen receptor-mediated transactivation

1 reference

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21 January 2018

Mutual transcriptional interference between RelA and androgen receptor

1 reference

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21 January 2018

Characterization of cell-specific modulatory element in the murine ornithine decarboxylase promoter

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21 January 2018

Phosphorylated CREB binds specifically to the nuclear protein CBP

1 reference

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21 January 2018

Stimulation of androgen-regulated transactivation by modulators of protein phosphorylation

1 reference

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21 January 2018

The rat androgen receptor: primary structure, autoregulation of its messenger ribonucleic acid, and immunocytochemical localization of the receptor protein

1 reference

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21 January 2018

Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy

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Meiotic stability and genotype-phenotype correlation of the trinucleotide repeat in X-linked spinal and bulbar muscular atrophy

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21 January 2018

Delineation of two distinct type 1 activation functions in the androgen receptor amino-terminal domain

1 reference

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21 January 2018

Multiple and cooperative trans-activation domains of the human glucocorticoid receptor

1 reference

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21 January 2018

Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor

1 reference

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21 January 2018

Three amino acid substitutions selectively disrupt the activation but not the repression function of the glucocorticoid receptor N terminus.

1 reference

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21 January 2018

The human estrogen receptor has two independent nonacidic transcriptional activation functions

1 reference

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21 January 2018

Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer

1 reference

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21 January 2018

Functional in vivo interaction between the amino-terminal, transactivation domain and the ligand binding domain of the androgen receptor

1 reference

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21 January 2018

Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor

1 reference

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21 January 2018

Analysis of estrogen receptor transcriptional enhancement by a nuclear hormone receptor coactivator

1 reference

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21 January 2018

The CBP co-activator is a histone acetyltransferase

1 reference

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21 January 2018

The transcriptional coactivators p300 and CBP are histone acetyltransferases

1 reference

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21 January 2018

CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription

1 reference

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RIP-140 interacts with multiple nuclear receptors by means of two distinct sites

1 reference

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The killing fields

1 reference

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A growing coactivator network

1 reference

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21 January 2018

Identifiers

10.1074/JBC.272.47.29821

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

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https://api.fatcat.wiki/v0/release/xv7jfn4bfzg7zkb5o4k3ar5zqe

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1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9368054

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