ArticleMolecular and cellular biology1996
Activation and repression by nuclear hormone receptors: hormone modulates an equilibrium between active and repressive states.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
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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
33 citing papers in PubMed, 134 citations in OpenAlex.
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- Regulation of RXR-RAR Heterodimers by RXR- and RAR-Specific Ligands and Their Combinations.Cells · 2019Article
- Ligand-Dependent Corepressor (LCoR) Is a Rexinoid-Inhibited Peroxisome Proliferator-Activated Receptor γ-Retinoid X Receptor α Coactivator.Molecular and cellular biology · 2018Article
- Flow signaling and atherosclerosis.Cellular and molecular life sciences : CMLS · 2017Review
- Functional diversification of vitamin D receptor paralogs in teleost fish after a whole genome duplication event.Endocrinology · 2014Article
- Novel mechanisms of endothelial mechanotransduction.Arteriosclerosis, thrombosis, and vascular biology · 2014Review
- Nuclear receptor Rev-erbalpha: a heme receptor that coordinates circadian rhythm and metabolism.Nuclear receptor signaling · 2010Review
- Vitamin D-dependent recruitment of corepressors to vitamin D/retinoid X receptor heterodimers.Molecular and cellular biology · 2008Article
- The RXRalpha C-terminus T462 is a NMR sensor for coactivator peptide binding.Biochemical and biophysical research communications · 2008Article
- The hinge-helix 1 region of peroxisome proliferator-activated receptor gamma1 (PPARgamma1) mediates interaction with extracellular signal-regulated kinase 5 and PPARgamma1 transcriptional activation: involvement in flow-induced PPARgamma activation in endothelial cells.Molecular and cellular biology · 2004Article
- Article
- Thyroid hormone actions on neural cells.Cellular and molecular neurobiology · 2002Review
- Segmentation gene product Fushi tarazu is an LXXLL motif-dependent coactivator for orphan receptor FTZ-F1.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Ligand-dependent degradation of retinoid X receptors does not require transcriptional activity or coactivator interactions.Molecular and cellular biology · 2001Article
- PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors.Molecular and cellular biology · 2001Article
- The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II).Molecular and cellular biochemistry · 2001Article
- Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors.Molecular and cellular biology · 2001Article
- CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant.Molecular and cellular biology · 2001Article
- Transcriptional anti-repression. Thyroid hormone receptor beta-2 recruits SMRT corepressor but interferes with subsequent assembly of a functional corepressor complex.The Journal of biological chemistry · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Transactivation-defective retinoid X and thyroid hormone receptors have been used to examine mechanisms of hormonal activation. Activation and repression of transcription by retinoid X and thyroid hormone receptors are shown to be mediated by physically distinct and functionally independent regions of the hormone binding domain. Nevertheless, the ability of receptors to respond to hormone requires communication between both functional domains. Deletion of the hormone-dependent transactivation function of the retinoid X receptor, the common subunit of heterodimeric nuclear receptors, significantly impairs hormone-dependent transcription by retinoic acid, thyroid hormone, and vitamin D receptors. The results indicate that receptors do not exist in static off and on conformations but that hormone alters an equilibrium between inactive and active states.
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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.