Evidence map›Paper›PMID 7799971›Full record

ArticleMolecular and cellular biology1995

The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing.

A Baniahmad, X Leng, T P Burris, S Y Tsai, M J Tsai, B W O'Malley

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
26.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

76 citing papers in PubMed, 247 citations in OpenAlex.

  1. Article
  2. Review
  3. Origins of the Field of Molecular Endocrinology: A Personal Perspective.Molecular endocrinology (Baltimore, Md.) · 2016
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
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  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. A novel 1297-1304delGCCTGCCA mutation in the exon 10 of the thyroid hormone receptor β gene causes resistance to thyroid hormone.Molecular diagnosis : a journal devoted to the understanding of human disease through the clinical application of molecular biology · 2004
    Article
  17. Article
  18. Nuclear receptor corepressors.Nuclear receptor signaling · 2003
    Article
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

A BaniahmadDepartment of Cell Biology, Baylor College of Medicine, Houston, Texas 77030.
X Leng
T P Burris
S Y Tsai
M J Tsai
B W O'Malley
Baylor College of Medicine · US

Funding

COACTIVATORS OF THE HUMAN PROGESTERONE RECEPTORF32HD007738 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI BURRIS, THOMAS P · 1993 to 1993
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NICHD NIH HHS HD-07738NICHD NIH HHS HD-08188
6 · The paper itself

Abstract

The C terminus of nuclear hormone receptors is a complex structure that contains multiple functions. We are interested in the mechanism by which thyroid hormone converts its receptor from a transcriptional silencer to an activator of transcription. Both regulatory functions are localized in the ligand binding domain of this receptor superfamily member. In this study, we have identified and characterized several functional domains within the ligand binding domain of the human thyroid hormone receptor (TR beta) conferring transactivation. Interestingly, these domains are localized adjacent to hormone binding sites. One activation domain, designated tau 4, is only 17 amino acids in length and is localized at the extreme C terminus of TR. Deletion of six amino acids of tau 4 resulted in a receptor that could still bind hormone but acted as a constitutive silencer, indicating that tau 4 is required for both transactivation and relief of the silencing functions. In addition, we performed in vivo competition experiments, the results of which suggest that in the absence of tau 4 or hormone, TR is bound by a corepressor protein(s) and that one role of hormone is to release corepressor from the receptor. We propose a general model in which the role of hormone is to induce a conformational change in the receptor that subsequently affects the action of tau 4, leading to both relief of silencing and transcriptional activation.

Indexed as

Gene Expression RegulationBase SequenceBinding SitesDNA Mutational AnalysisHumansMolecular Sequence DataOligodeoxyribonucleotidesReceptors, Thyroid HormoneRepressor ProteinsSequence AlignmentSequence Homology, Amino AcidStructure-Activity RelationshipTranscription, GeneticTriiodothyronineOligodeoxyribonucleotidesReceptors, Thyroid HormoneRepressor ProteinsTriiodothyronine

Identifiers

PMID7799971
PMCPMC231910
OpenAlexW2157063922

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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 Socratic graph.