(Q33937627)

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H-2RIIBP (RXR beta) heterodimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive genes

scientific article published on April 1, 1992

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PubMed publication ID

30 July 2017

H-2RIIBP (RXR beta) heterodimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive genes (English)

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30 July 2017

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based on heuristic

inferred from title

protein heterodimerization activity

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based on heuristic

inferred from title

regulation of gene expression

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12 September 2022

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J. H. Segars

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M. S. Marks

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P. L. Hallenbeck

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T. Nagata

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V. M. Nikodem

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K. Ozato

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1 April 1992

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https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/j.1460-2075.1992.tb05187.x

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https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fj.1460-2075.1992.tb05187.x

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10.1002/J.1460-2075.1992.TB05187.X

https://api.crossref.org/works/10.1002/J.1460-2075.1992.TB05187.X

3 December 2023

http://onlinelibrary.wiley.com/wol1/doi/10.1002/j.1460-2075.1992.tb05187.x/fullpdf

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10.1002/J.1460-2075.1992.TB05187.X

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3 December 2023

The EMBO Journal

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30 July 2017

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30 July 2017

4

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30 July 2017

1419-1435

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30 July 2017

Retinoic acid induces neuronal differentiation of a cloned human embryonal carcinoma cell line in vitro

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Binding of multiple nuclear factors to the 5' upstream regulatory element of the murine major histocompatibility class I gene

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1 reference

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DNA binding activities of three murine Jun proteins: stimulation by Fos.

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Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene

1 reference

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Retinoic acid and thyroid hormone induce gene expression through a common responsive element.

1 reference

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Cloning and expression of full-length cDNA encoding human vitamin D receptor

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Identification of a receptor for the morphogen retinoic acid

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A human retinoic acid receptor which belongs to the family of nuclear receptors

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COUP transcription factor is a member of the steroid receptor superfamily

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Gene regulation by steroid hormones

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A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors

1 reference

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Retinoic acid receptor expression vector inhibits differentiation of F9 embryonal carcinoma cells

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Positive and negative regulation of gene transcription by a retinoic acid-thyroid hormone receptor heterodimer

1 reference

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H-2RIIBP, a member of the nuclear hormone receptor superfamily that binds to both the regulatory element of major histocompatibility class I genes and the estrogen response element

1 reference

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Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity

1 reference

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Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence

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The DNA binding domain of the rat liver nuclear protein C/EBP is bipartite

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A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins

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Characterization of a third human thyroid hormone receptor coexpressed with other thyroid hormone receptors in several tissues

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A human beta-actin expression vector system directs high-level accumulation of antisense transcripts

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Human estrogen receptor forms multiple protein-DNA complexes.

1 reference

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Identification of a thyroid hormone response element in the malic enzyme gene.

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Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor

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Thyroid hormone receptors form distinct nuclear protein-dependent and independent complexes with a thyroid hormone response element

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The C'-terminal interaction domain of the thyroid hormone receptor confers the ability of the DNA site to dictate positive or negative transcriptional activity

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Commitment and activation at pol II promoters: a tail of protein-protein interactions

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Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model

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Multiple cell type-specific proteins differentially regulate target sequence recognition by the alpha retinoic acid receptor

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Ligand-activated thyroid hormone and retinoic acid receptors inhibit growth factor receptor promoter expression.

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A steroid/thyroid hormone receptor superfamily member in Drosophila melanogaster that shares extensive sequence similarity with a mammalian homologue

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Nuclear receptor that identifies a novel retinoic acid response pathway

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=556591

29 October 2018

I-POU: a POU-domain protein that inhibits neuron-specific gene activation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=556591

29 October 2018

The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer

1 reference

https://pubmed.ncbi.nlm.nih.gov/1314168

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Thyroid hormone receptor mutations that interfere with transcriptional activation also interfere with receptor interaction with a nuclear protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/1314168

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification of nuclear factors that enhance binding of the thyroid hormone receptor to a thyroid hormone response element

1 reference

https://pubmed.ncbi.nlm.nih.gov/1314168

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Molecular interactions of steroid hormone receptor with its enhancer element: evidence for receptor dimer formation

1 reference

https://pubmed.ncbi.nlm.nih.gov/1314168

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/J.1460-2075.1992.TB05187.X

1 reference

National Center for Biotechnology Information

PubMed publication ID

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1314168

12 September 2022

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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