NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC. (Q28567527)

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English	NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC.	scientific article

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scholarly article

1 reference

Europe PubMed Central

6 July 2017

NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC. (English)

1 reference

Europe PubMed Central

6 July 2017

author name string

Audrey Murray

2

1 reference

Europe PubMed Central

6 July 2017

Muktar A Mahajan

1

1 reference

Europe PubMed Central

6 July 2017

Herbert H Samuels

3

1 reference

Europe PubMed Central

6 July 2017

language of work or name

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publication date

1 October 2002

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Europe PubMed Central

6 July 2017

Molecular and Cellular Biology

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Europe PubMed Central

6 July 2017

22

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Europe PubMed Central

6 July 2017

19

1 reference

Europe PubMed Central

6 July 2017

6883-6894

1 reference

Europe PubMed Central

6 July 2017

Combinatorial control of gene expression by nuclear receptors and coregulators

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=134037

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Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors

1 reference

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Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function

1 reference

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Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)

1 reference

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Nuclear hormone receptors and gene expression

1 reference

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The USA-derived transcriptional coactivator PC2 is a submodule of TRAP/SMCC and acts synergistically with other PCs

1 reference

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A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein

1 reference

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19 March 2017

Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator

1 reference

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Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR

1 reference

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Cloning and characterization of RAP250, a novel nuclear receptor coactivator

1 reference

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A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo

1 reference

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NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors

1 reference

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Regulation of transcription by a protein methyltransferase

1 reference

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Purification of transcription cofactor complex CRSP

1 reference

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Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein

1 reference

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Composite co-activator ARC mediates chromatin-directed transcriptional activation

1 reference

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

1 reference

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Molecular determinants of the estrogen receptor-coactivator interface

1 reference

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

1 reference

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Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation

1 reference

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19 March 2017

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

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

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A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis

1 reference

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

1 reference

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

1 reference

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1 reference

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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

1 reference

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

1 reference

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

1 reference

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Binding and modulation of p53 by p300/CBP coactivators

1 reference

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Two contact regions between Stat1 and CBP/p300 in interferon gamma signaling

1 reference

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Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex

1 reference

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A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A

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TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors

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1 reference

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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

1 reference

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

1 reference

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1 reference

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1 reference

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Nuclear receptor coregulators: cellular and molecular biology

1 reference

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

1 reference

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Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor

1 reference

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Role of CBP/P300 in nuclear receptor signalling

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=134037

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Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities

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1 reference

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29 September 2017

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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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3 June 2018

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/12215545

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Half-site spacing and orientation determines whether thyroid hormone and retinoic acid receptors and related factors bind to DNA response elements as monomers, homodimers, or heterodimers

1 reference

https://pubmed.ncbi.nlm.nih.gov/12215545

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/MCB.22.19.6883-6894.2002

1 reference

Europe PubMed Central

6 July 2017

1 reference

Europe PubMed Central

6 July 2017

1 reference

Europe PubMed Central

6 July 2017

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