(Q34489597)

2 August 2017

title

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

1 reference

2 August 2017

Hong H

1

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2 August 2017

Darimont BD

2

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2 August 2017

Ma H

3

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2 August 2017

Yang L

4

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2 August 2017

Yamamoto KR

5

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2 August 2017

Stallcup MR

6

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2 August 2017

language of work or name

English

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publication date

1 February 1999

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Journal of Biological Chemistry

2 August 2017

published in

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2 August 2017

volume

274

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2 August 2017

issue

6

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2 August 2017

page(s)

3496-3502

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The steroid and thyroid hormone receptor superfamily

2 August 2017

cites work

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

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Differential ligand activation of estrogen receptors ERalpha and ERbeta at AP1 sites

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

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Steroid-dependent interaction of transcription factors with the inducible promoter of mouse mammary tumor virus in vivo

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

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Co-activators and co-repressors in the integration of transcriptional responses

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

21 January 2018

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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

21 January 2018

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GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors

21 January 2018

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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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RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2

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AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer

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TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1

21 January 2018

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

21 January 2018

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Transcription factor-specific requirements for coactivators and their acetyltransferase functions

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Structure and specificity of nuclear receptor-coactivator interactions

21 January 2018

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

21 January 2018

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The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways

21 January 2018

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21 January 2018

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Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor

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Estrogen receptor activation function 1 works by binding p160 coactivator proteins

21 January 2018

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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.

21 January 2018

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The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily

21 January 2018

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A structural role for hormone in the thyroid hormone receptor.

21 January 2018

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Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid

21 January 2018

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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

21 January 2018

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Molecular basis of agonism and antagonism in the oestrogen receptor

21 January 2018

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Atomic structure of progesterone complexed with its receptor

21 January 2018

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Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor

21 January 2018

1 reference

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A splicing variant of Steroid Receptor Coactivator-1 (SRC-1E): the major isoform of SRC-1 to mediate thyroid hormone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.6.3496

21 January 2018

Identifiers

DOI

10.1074/JBC.274.6.3496

1 reference

release_5c66u5oyjfh7jp6avuhdyzoeny

2 August 2017

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/5c66u5oyjfh7jp6avuhdyzoeny

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference