Evidence map›Paper›PMID 10871399›Full record

ArticleNucleic acids research2000

Expression and function of the homeodomain-containing protein Hex in thyroid cells.

L Pellizzari, A D'Elia, A Rustighi, G Manfioletti, G Tell, G Damante

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Defining theThyroid : official journal of the American Thyroid Association · 2024
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Homeobox protein Hhex negatively regulates Treg cells by inhibiting Foxp3 expression and function.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. The role of thyroglobulin in thyroid hormonogenesis.Nature reviews. Endocrinology · 2019
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Clinical review: The emerging cell biology of thyroid stem cells.The Journal of clinical endocrinology and metabolism · 2011
    Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

L PellizzariDipartimento di Scienze e Tecnologie Biomediche, Università di Udine, Italy.
A D'Elia
A Rustighi
G Manfioletti
G Tell
G Damante
University of Udine · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The homeodomain-containing protein Hex (also named Prh) is expressed in primitive endoderm (during the early phases of development), in some endoderm-derived tissues and in endothelial and hematopoietic precursors. Hex expression is exting-uished during terminal differentiation of endothelial and hematopoietic cells as well as in adult lung. Previous investigations have demonstrated that Hex is expressed during early thyroid gland development. No information has been reported on Hex expression in adult thyroid gland or on the function of this protein in follicular thyroid cells. These issues represent the focus of the present study. We demonstrate that Hex mRNA is present in rat and human adult thyroid gland as well as in differentiated follicular thyroid cell lines. In FRTL-5 cells TSH reduces Hex expression. In thyroid cell lines transformed by several oncogenes Hex expression is completely abolished. By using co-transfection assays we demonstrate that Hex is a repressor of the thyroglobulin promoter and that it is able to abolish the activating effects of both TTF-1 and Pax8. These data would suggest that Hex may play an important role in thyroid cell differentiation. Protein-DNA interaction experiments indicate that Hex is able to bind sites of the thyroglobulin promoter containing either the core sequence 5'-TAAT-3' or 5'-CAAG-3'. The DNA binding specificity of the Hex homeodomain, therefore, is more 'relaxed' than that observed in the majority of other homeo-domains.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesCell DifferentiationCell LineCell Transformation, NeoplasticDNADNA-Binding ProteinsGene Expression RegulationHomeodomain ProteinsHumansMiceMolecular Sequence DataNuclear ProteinsPaired Box Transcription FactorsDNADNA-Binding ProteinsHHEX protein, humanHhex protein, mouseHhex protein, ratHomeodomain ProteinsNKX2-1 protein, humanNkx2-1 protein, mouseNkx2-1 protein, ratNuclear ProteinsPaired Box Transcription FactorsPAX8 protein, humanPax8 protein, mousePax8 protein, ratPAX8 Transcription FactorRepressor ProteinsRNA, MessengerThyroglobulinThyroid Nuclear Factor 1ThyrotropinTrans-ActivatorsTranscription Factors

Identifiers

PMID10871399
PMCPMC102703
OpenAlexW2154697123

What OpenQuestion 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 OpenQuestion graph.