Evidence map›Paper›PMID 22474346›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Structure of p73 DNA-binding domain tetramer modulates p73 transactivation.

Abdul S Ethayathulla, Pui-Wah Tse, Paola Monti, Sonha Nguyen, Alberto Inga, Gilberto Fronza, Hector Viadiu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Structural diversity of p63 and p73 isoforms.Cell death and differentiation · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
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

7 authors at 2 institutions in 2 countries.

Abdul S EthayathullaLaboratory of Structural Biochemistry, Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive 0378, La Jolla, CA 92093, USA.
Pui-Wah Tse
Paola Monti
Sonha Nguyen
Alberto Inga
Gilberto Fronza
Hector Viadiu
University of California, San Diego · USOspedale Policlinico San Martino · IT

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
NCRR NIH HHS (P41RR001209NCRR NIH HHS P41 RR001209
6 · The paper itself

Abstract

The transcription factor p73 triggers developmental pathways and overlaps stress-induced p53 transcriptional pathways. How p53-family response elements determine and regulate transcriptional specificity remains an unsolved problem. In this work, we have determined the first crystal structures of p73 DNA-binding domain tetramer bound to response elements with spacers of different length. The structure and function of the adaptable tetramer are determined by the distance between two half-sites. The structures with zero and one base-pair spacers show compact p73 DNA-binding domain tetramers with large tetramerization interfaces; a two base-pair spacer results in DNA unwinding and a smaller tetramerization interface, whereas a four base-pair spacer hinders tetramerization. Functionally, p73 is more sensitive to spacer length than p53, with one base-pair spacer reducing 90% of transactivation activity and longer spacers reducing transactivation to basal levels. Our results establish the quaternary structure of the p73 DNA-binding domain required as a scaffold to promote transactivation.

Indexed as

Protein MultimerizationProtein Structure, TertiaryTranscriptional ActivationAmino Acid SequenceBase SequenceBinding SitesCrystallography, X-RayDNADNA-Binding ProteinsHumansModels, MolecularMolecular Sequence DataNuclear ProteinsNucleic Acid ConformationProtein BindingProtein Structure, QuaternaryDNADNA-Binding ProteinsNuclear ProteinsTP73 protein, humanTumor Protein p73Tumor Suppressor Proteins

Identifiers

PMID22474346
PMCPMC3341074
OpenAlexW2123267727

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.