ArticleNucleic acids research1997
Binding of type II nuclear receptors and estrogen receptor to full and half-site estrogen response elements in vitro.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 74 citations in OpenAlex.
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- 17β-Estradiol induces sulfotransferase 2A1 expression through estrogen receptor α.Drug metabolism and disposition: the biological fate of chemicals · 2014Article
- Small-molecule hormones: molecular mechanisms of action.International journal of endocrinology · 2013Article
- Achieving CNS axon regeneration by manipulating convergent neuro-immune signaling.Cell and tissue research · 2012Review
- Nuclear receptors as therapeutic targets for Alzheimer's disease.Expert opinion on therapeutic targets · 2011Review
- Expanding the paradigm for estrogen receptor binding and transcriptional activation.Molecular endocrinology (Baltimore, Md.) · 2011Article
- The Peroxisomal 3-keto-acyl-CoA thiolase B Gene Expression Is under the Dual Control of PPARα and HNF4α in the Liver.PPAR research · 2010Article
- Revealing genes associated with vitellogenesis in the liver of the zebrafish (Danio rerio) by transcriptome profiling.BMC genomics · 2009Article
- Augmentation of estrogen receptor-mediated transcription by steroid and xenobiotic receptor.Endocrine · 2008Article
- Estrogen signaling multiple pathways to impact gene transcription.Current genomics · 2006Article
- Positive and negative regulation of chicken anemia virus transcription.Journal of virology · 2005Article
- Increases in mouse uterine heat shock protein levels are a sensitive and specific response to uterotrophic agents.Environmental health perspectives · 2002Article
- Estrogen receptor interaction with estrogen response elements.Nucleic acids research · 2001Review
- Strategies for assessing the implications of malformed frogs for environmental health.Environmental health perspectives · 2000Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The mechanism by which retinoids, thyroid hormone (T3) and estrogens modulate the growth of breast cancer cells is unclear. Since nuclear type II nuclear receptors, including retinoic acid receptor (RAR), retinoid X receptor (RXR) and thyroid hormone receptor (TR), bind direct repeats (DR) of the estrogen response elements (ERE) half-site (5'-AGGTCA-3'), we examined the ability of estrogen receptor (ER) versus type II nuclear receptors, i.e. RARalpha, beta and gamma, RXRbeta, TRalpha and TRbeta, to bind various EREs in vitro . ER bound a consensus ERE, containing a perfectly palindromic 17 bp inverted repeat (IR), as a homodimer. In contrast, ER did not bind to a single ERE half-site. Likewise, ER did not bind two tandem (38 bp apart) half-sites, but low ER binding was detected to three tandem copies of the same half-site. RARalpha,beta or gamma bound both ERE and half-site constructs as a homodimer. RXRbeta did not bind full or half-site EREs, nor did RXRbeta enhance RARalpha binding to a full ERE. However, RARalpha and RXRbeta bound a half-site ERE cooperatively forming a dimeric complex. The RARalpha-RXRbeta heterodimer bound the Xenopus vitellogenin B1 estrogen responsive unit, with two non-consensus EREs, with higher affinity than one or two copies of the full or half-site ERE. Both TRalpha and TRbeta bound the full and the half-site ERE as monomers and homodimers and cooperatively as heterodimers with RXRbeta. We suggest that the cellular concentrations of nuclear receptors and their ligands, and the nature of the ERE or half-site sequence and those of its flanking sequences determine the occupation of EREs in estrogen-regulated genes in vivo .
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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.