ArticleProceedings of the National Academy of Sciences of the United States of America1995
A nuclear hormone receptor-associated protein that inhibits transactivation by the thyroid hormone and retinoic acid receptors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 99 citations in OpenAlex.
- Rev-Erb co-regulates muscle regeneration via tethered interaction with the NF-Y cistrome.Molecular metabolism · 2017Trial
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- Extra-Ribosomal Roles for Ribosomal Proteins and Their Relevance to Tumour Suppression, Carcinogenesis and Cancer Progression.Cancers · 2025Review
- Experimental upregulation of developmentally downregulated ribosomal protein large subunits 7 and 7A promotes axon regeneration after injury in vivo.Experimental neurology · 2023Article
- The Hippocampal Response to Acute Corticosterone Elevation Is Altered in a Mouse Model for Angelman Syndrome.International journal of molecular sciences · 2022Article
- Bioinformatics Analysis Reveals the Potential Diagnostic Biomarkers for Abdominal Aortic Aneurysm.Frontiers in cardiovascular medicine · 2021Article
- Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of human ribosomal protein L7a (RPL7a).Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Down-regulation of ribosomal protein L7A in human osteosarcoma.Journal of cancer research and clinical oncology · 2009Article
- Molecular cloning and characterization of the human PED/PEA-15 gene promoter reveal antagonistic regulation by hepatocyte nuclear factor 4alpha and chicken ovalbumin upstream promoter transcription factor II.The Journal of biological chemistry · 2008Article
- The extracellular domain of the growth hormone receptor interacts with coactivator activator to promote cell proliferation.Molecular endocrinology (Baltimore, Md.) · 2008Article
- Article
- A complex role for the progesterone receptor in the response to vascular injury.The Journal of clinical investigation · 2001Article
- CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant.Molecular and cellular biology · 2001Article
- Proteasome-dependent degradation of the human estrogen receptor.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily.Molecular and cellular biology · 1999Article
- High-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cells.Molecular and cellular biology · 1998Article
- Mutations in the conserved C-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity.Molecular and cellular biology · 1997Article
- Protein kinase A-dependent phosphorylation modulates DNA-binding activity of hepatocyte nuclear factor 4.Molecular and cellular biology · 1997Article
- Chicken ovalbumin upstream promoter transcription factors act as auxiliary cofactors for hepatocyte nuclear factor 4 and enhance hepatic gene expression.Molecular and cellular biology · 1997Article
- GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors.Molecular and cellular biology · 1997Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear hormone receptors are transcription factors that require multiple protein-protein interactions to regulate the expression of their target genes. Using the yeast two-hybrid system, we identified a protein, thyroid hormone receptor uncoupling protein (TRUP), that specifically interacts with a region of the human thyroid hormone receptor (TR) consisting of the hinge region and the N-terminal portion of the ligand binding domain in a hormone-independent manner. Interestingly, TRUP inhibits transactivation by TR and the retinoic acid receptor but has no effect on the estrogen receptor or the retinoid X receptor in mammalian cells. We also demonstrate that TRUP exerts its action on TR and retinoic acid receptor by interfering with their abilities to interact with their DNA. TRUP represents a type of regulatory protein that modulates the transcriptional activity of a subclass of the nuclear hormone receptor superfamily by preventing interaction with their genomic response elements.
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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.