ArticleMolecular and cellular biology1997
A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 84 citations in OpenAlex.
- Repurposing nuclear receptors for ligand-responsive liquid condensate formation and gene regulation.Nature communications · 2026Article
- ZNF143 binds DNA and stimulates transcription initiation to activate and repress direct target genes.Nucleic acids research · 2025Article
- ZNF143 binds DNA and stimulates transcripstion initiation to activate and repress direct target genes.bioRxiv : the preprint server for biology · 2024Article
- Structure-Guided Approach to Relieving Transcriptional Repression in Resistance to Thyroid Hormone α.Molecular and cellular biology · 2022Article
- Multiple mechanisms regulate H3 acetylation of enhancers in response to thyroid hormone.PLoS genetics · 2020Article
- Effects of hyperthyroidism in the development of the appendicular skeleton and muscles of zebrafish, with notes on evolutionary developmental pathology (Evo-Devo-Path).Scientific reports · 2019Article
- Novel Insight Into the Epigenetic and Post-transcriptional Control of Cardiac Gene Expression by Thyroid Hormone.Frontiers in endocrinology · 2019Review
- Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors and modulate transcriptional activity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Transcriptional activation by the thyroid hormone receptor through ligand-dependent receptor recruitment and chromatin remodelling.Nature communications · 2015Article
- Defining the communication between agonist and coactivator binding in the retinoid X receptor α ligand binding domain.The Journal of biological chemistry · 2014Article
- Research resource: identification of novel coregulators specific for thyroid hormone receptor-β2.Molecular endocrinology (Baltimore, Md.) · 2013Article
- Mutant thyroid hormone receptors (TRs) isolated from distinct cancer types display distinct target gene specificities: a unique regulatory repertoire associated with two renal clear cell carcinomas.Molecular endocrinology (Baltimore, Md.) · 2011Article
- The interaction between nuclear receptor corepressor and histone deacetylase 3 regulates both positive and negative thyroid hormone action in vivo.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Direct interdomain interactions can mediate allosterism in the thyroid receptor.The Journal of biological chemistry · 2009Article
- The p160 coactivator PAS-B motif stabilizes nuclear receptor binding and contributes to isoform-specific regulation by thyroid hormone receptors.The Journal of biological chemistry · 2009Article
- Vitamin D-dependent recruitment of corepressors to vitamin D/retinoid X receptor heterodimers.Molecular and cellular biology · 2008Article
- Article
- Isotype-restricted corepressor recruitment: a constitutively closed helix 12 conformation in retinoic acid receptors beta and gamma interferes with corepressor recruitment and prevents transcriptional repression.Molecular and cellular biology · 2003Article
- A dominant negative PPARgamma mutant shows altered cofactor recruitment and inhibits adipogenesis in 3T3-L1 cells.Diabetologia · 2003Article
- Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia.Molecular and cellular biology · 2001Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Nuclear hormone receptors are ligand-regulated transcription factors that modulate gene expression in response to small, hydrophobic hormones, such as retinoic acid and thyroid hormone. The thyroid hormone and retinoic acid receptors typically repress transcription in the absence of hormone and activate it in the presence of hormone. Transcriptional repression is mediated, in part, through the ability of these receptors to physically associate with ancillary polypeptides called corepressors. We wished to understand the mechanism by which corepressors are recruited to unliganded nuclear hormone receptors and are released on the binding of hormone. We report here that an alpha-helical domain located at the thyroid hormone receptor C terminus appears to undergo a hormone-induced conformational change required for release of corepressor and that amino acid substitutions that abrogate this conformational change can impair or prevent corepressor release. In contrast, retinoid X receptors appear neither to undergo an equivalent conformational alteration in their C termini nor to release corepressor in response to cognate hormone, consistent with the distinct transcriptional regulatory properties displayed by this class of receptors.
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What OpenQuestion holds
Registered trials
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.