ArticleThe EMBO journal1993
The patterns of binding of RAR, RXR and TR homo- and heterodimers to direct repeats are dictated by the binding specificites of the DNA binding domains.
Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
65 citing papers in PubMed, 217 citations in OpenAlex.
- Retinoic acid receptor structures: the journey from single domains to full-length complex.Journal of molecular endocrinology · 2022Article
- A coregulator shift, rather than the canonical switch, underlies thyroid hormone action in the liver.Genes & development · 2021Article
- Nuclear Receptors, Ligands and the Mammalian B Cell.International journal of molecular sciences · 2020Review
- Ameliorating effect of lipo-ATRA treatment on the expression of TIG3 and its suppressing effect on PPARγ gene expression in lung cancer animal model.Molecular and cellular biochemistry · 2019Article
- Comprehensive study of nuclear receptor DNA binding provides a revised framework for understanding receptor specificity.Nature communications · 2019Article
- Conservation of DNA and ligand binding properties of retinoid X receptor from the placozoan Trichoplax adhaerens to human.The Journal of steroid biochemistry and molecular biology · 2018Review
- Regulation of type 1 iodothyronine deiodinase by LXRα.PloS one · 2017Article
- Transcriptional Factors Mediating Retinoic Acid Signals in the Control of Energy Metabolism.International journal of molecular sciences · 2015Review
- Understanding nuclear receptor form and function using structural biology.Journal of molecular endocrinology · 2013Review
- The role of retinoic acid in hepatic lipid homeostasis defined by genomic binding and transcriptome profiling.BMC genomics · 2013Article
- Genome-wide analysis of thyroid hormone receptors shared and specific functions in neural cells.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Xenobiotic-sensing nuclear receptors involved in drug metabolism: a structural perspective.Drug metabolism reviews · 2013Review
- Small-molecule hormones: molecular mechanisms of action.International journal of endocrinology · 2013Article
- Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings.Nature structural & molecular biology · 2011Article
- The eccentric cleavage product of β-carotene, β-apo-13-carotenone, functions as an antagonist of RXRα.Archives of biochemistry and biophysics · 2010Article
- Research resource: transcriptome profiling of genes regulated by RXR and its permissive and nonpermissive partners in differentiating monocyte-derived dendritic cells.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Hif1α down-regulation is associated with transposition of great arteries in mice treated with a retinoic acid antagonist.BMC genomics · 2010Article
- Structure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response element.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Retinoids regulate human amniotic tissue-type plasminogen activator gene by a two-step mechanism.Journal of cellular and molecular medicine · 2010Article
- DNA recognition by thyroid hormone and retinoic acid receptors: 3,4,5 rule modified.Molecular and cellular endocrinology · 2010Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We show here that, in addition to generating an increase in DNA binding efficiency, heterodimerization of retinoid X receptor (RXR) with either retinoic acid receptor (RAR) or thyroid hormone receptor (TR) alters the binding site repertoires of RAR, RXR and TR homodimers. The binding site specificities of both homo- and heterodimers appear to be largely determined by their DNA binding domains (DBDs), and are dictated by (i) homocooperative DNA binding of the RXR DBD, (ii) heterocooperative DNA binding of RXR/RAR and RXR/TR DBDs, and (iii) steric hindrance. No homodimerization domain exists in the DBDs of TR and RAR. The dimerization function which is located in the ligand binding domain further stabilizes, but in general does not change, the repertoire dictated by the corresponding DBD(s). The binding repertoire can be further modified by the actual sequence of the binding site. We also provide evidence supporting the view that the cooperative binding of the RXR/RAR and RXR/TR DBDs to directly repeated elements is anisotropic, with interactions between the dimerization interfaces occurring only with RXR bound to the 5' located motif. This polarity, which appears to be maintained in the full-length receptor heterodimers, may constitute a novel parameter in promoter-specific transactivation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.