ArticleThe Journal of biological chemistry2009
Direct interdomain interactions can mediate allosterism in the thyroid receptor.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 41 citations in OpenAlex.
- Conformational transition of a polycationic hinge domain contributes to DNA binding.Biophysical chemistry · 2026Article
- Structural basis for the asymmetric binding of coactivator SRC1 to FXR-RXRα and allosteric communication within the complex.Communications biology · 2025Article
- Bridging prediction and reality: Comprehensive analysis of experimental and AlphaFold 2 full-length nuclear receptor structures.Computational and structural biotechnology journal · 2025Article
- Hormone response elements for the thyroid receptor-α include specific distal 5'-flanking DNA.Science advances · 2024Article
- Targeting Androgen, Thyroid Hormone, and Vitamin A and D Receptors to Treat Prostate Cancer.International journal of molecular sciences · 2024Review
- Revealing a Mutant-Induced Receptor Allosteric Mechanism for the Thyroid Hormone Resistance.iScience · 2019Article
- Allosteric pathways in nuclear receptors - Potential targets for drug design.Pharmacology & therapeutics · 2018Review
- Interaction of the phosphorylated DNA-binding domain in nuclear receptor CAR with its ligand-binding domain regulates CAR activation.The Journal of biological chemistry · 2018Article
- Synergistic Regulation of Coregulator/Nuclear Receptor Interaction by Ligand and DNA.Structure (London, England : 1993) · 2017Article
- DNA-induced unfolding of the thyroid hormone receptor α A/B domain through allostery.FEBS open bio · 2017Article
- Visualizing the Architectures and Interactions of Nuclear Receptors.Endocrinology · 2016Review
- Mapping allostery through computational glycine scanning and correlation analysis of residue-residue contacts.Biochemistry · 2015Article
- RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment.Molecular endocrinology (Baltimore, Md.) · 2015Article
- Nuclear corepressors mediate the repression of phospholipase A2 group IIa gene transcription by thyroid hormone.The Journal of biological chemistry · 2013Article
- Evidence for DNA-binding domain--ligand-binding domain communications in the androgen receptor.Molecular and cellular biology · 2012Article
- Structural basis for negative cooperativity within agonist-bound TR:RXR heterodimers.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Endocrine reviews · 2012Review
- Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The retinoid X receptors and their ligands.Biochimica et biophysica acta · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The thyroid (TR) and retinoid X receptors (RXR) belong to the nuclear receptor (NR) superfamily of ligand-mediated transcription factors. At the molecular level, TR activity is specifically modulated by interactions with the ligand 3,3',5 triiodo-l-thyronine (T3), RXR, DNA, and co-activators such as SRC1, occurring in concert or sequentially. Although binding sites for DNA and coregulators such as SRC1 are distinct and at distal regions of these receptors, cell-based and EMSA studies have suggested that these molecules can regulate binding of each other to the receptor. We present evidence of direct, DNA-dependent, communication between the DNA and ligand binding domains (DBD and LBD) that can allosterically regulate interactions with SRC1 and DNA, respectively, using isothermal titration calorimetry (ITC) and cell-based assays. Additionally, we note that interdomain communication is affected by RXR in RXR:TR. We also noticed a DNA-dependent cross-talk between RXR and TR within RXR:TR. Finally, we suggest that differences in transactivation on different TRE may be the consequence of different affinities between TRE and RXR:TR.
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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.