ArticleMolecular endocrinology (Baltimore, Md.)2011
A mechanism for pituitary-resistance to thyroid hormone (PRTH) syndrome: a loss in cooperative coactivator contacts by thyroid hormone receptor (TR)beta2.
Article in Molecular endocrinology (Baltimore, Md.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- A case of thyroid hormone resistance with thyroid regrowth: implications of misdiagnosis on patient care.JCEM case reports · 2026Article
- Transport, Metabolism, and Function of Thyroid Hormones in the Developing Mammalian Brain.Frontiers in endocrinology · 2019Review
- Pituitary resistance to thyroid hormone caused by a novel mutation (H435A) in the thyroid hormone receptor beta: A case report.Medicine · 2018Article
- Naturally Occurring Amino Acids in Helix 10 of the Thyroid Hormone Receptor Mediate Isoform-Specific TH Gene Regulation.Endocrinology · 2017Article
- Homeostatic Control of the Thyroid-Pituitary Axis: Perspectives for Diagnosis and Treatment.Frontiers in endocrinology · 2015Review
- The ability of thyroid hormone receptors to sense t4 as an agonist depends on receptor isoform and on cellular cofactors.Molecular endocrinology (Baltimore, Md.) · 2014Article
- Cloning and identification of a novel thyroid hormone receptor β isoform expressed in the pituitary gland.Molecular and cellular biochemistry · 2014Article
- A rare thyroid hormone receptor beta (THRβ) gene mutation in a 15-year-old girl with thyroid hormone resistance syndrome: a case report.Journal of medical case reports · 2014Article
- The syndromes of reduced sensitivity to thyroid hormone.Biochimica et biophysica acta · 2013Review
- RTHα, a newly recognized phenotype of the resistance to thyroid hormone (RTH) syndrome in patients with THRA gene mutations.The Journal of clinical endocrinology and metabolism · 2013Article
- Research resource: identification of novel coregulators specific for thyroid hormone receptor-β2.Molecular endocrinology (Baltimore, Md.) · 2013Article
- TSH and Thyrotropic Agonists: Key Actors in Thyroid Homeostasis.Journal of thyroid research · 2012Article
- TSH Measurement and Its Implications for Personalised Clinical Decision-Making.Journal of thyroid research · 2012Article
- Review
- RESISTANCE TO THYROID HORMONES: A NOVEL MUTATION OF THE THYROID HORMONE RECEPTOR β GENE IN AN ALGERIAN FAMILY.Acta endocrinologica (Bucharest, Romania : 2005)Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Thyroid hormone receptors (TR) are hormone-modulated transcription factors that regulate overall metabolic rate, lipid utilization, heart rate, and development. TR are expressed as a mix of interrelated receptor isoforms. The TRβ2 isoform is expressed in the hypothalamus and pituitary, where it plays an important role in the feedback regulation of thyroid hormone levels. TRβ2 exhibits unique transcriptional properties that parallel the ability of this isoform to bind to certain coactivators cooperatively through multiple contact surfaces. The more peripherally expressed TRβ1 isoform, in contrast, appears to recruit these coactivators through a single contact mechanism. We report here that clusters of charged amino acids in the TR hormone-binding domain are required for this enhanced mode of coactivator recruitment and that mutations in these charge clusters, by disrupting TRβ2 coactivator binding, are a molecular basis for pituitary resistance to thyroid hormone, a disease characterized by inappropriate thyroid hormone feedback regulation. We propose that the charge clusters allow wild-type TRβ2 to assume a conformation compatible with its mode of multiple contact coactivator recruitment, whereas disruption of these charge clusters disrupts normal T(3) homeostasis by reducing TRβ2 to a TRβ1-like, single contact mode of coactivator binding.
Indexed as
Identifiers
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.