Evidence map›Paper›PMID 23393263›Full record

ArticleScience (New York, N.Y.)2013

Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins.

Katia Zanier, Sebastian Charbonnier, Abdellahi Ould M'hamed Ould Sidi, Alastair G McEwen, Maria Giovanna Ferrario, Pierre Poussin-Courmontagne, Vincent Cura, Nicole Brimer, Khaled Ould Babah, Tina Ansari and 5 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

120 citing papers in PubMed, 211 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Targeted degradation of the HPV oncoprotein E6 reduces tumor burden in cervical cancer.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  10. The multi-kingdom cancer microbiome.Nature microbiology · 2025
    Review
  11. Article
  12. Article
  13. DARPin-induced reactivation of p53 in HPV-positive cells.Nature structural & molecular biology · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

60 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

15 authors at 2 institutions in 1 country.

Katia ZanierBiotechnologie et Signalisation Cellulaire UMR 7242, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, BP 10413, F-67412 Illkirch, France.
Sebastian Charbonnier
Abdellahi Ould M'hamed Ould Sidi
Alastair G McEwen
Maria Giovanna Ferrario
Pierre Poussin-Courmontagne
Vincent Cura
Nicole Brimer
Khaled Ould Babah
Tina Ansari
Isabelle Muller
Roland H Stote
Jean Cavarelli
Scott Vande Pol
Gilles Travé
École Supérieure de Biotechnologie de Strasbourg · FRBiotechnologie et Signalisation Cellulaire · FR

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Thomas P. Loughran · 1987 to 2026
$72.1M
Papillomavirus E6 Structural ConsortiumR01CA134737 · NCI · UNIVERSITY OF VIRGINIA · PI VANDE POL, SCOTT BRIAN · 2010 to 2019
$4.2M
E6 Interaction with Cellular PDZ ProteinsR01CA120352 · NCI · UNIVERSITY OF VIRGINIA · PI VANDE POL, SCOTT BRIAN · 2007 to 2010
$1.2M
NCI NIH HHS CA08093NCI NIH HHS CA120352NCI NIH HHS CA134737NCI NIH HHS P30 CA044579NCI NIH HHS R01 CA120352NCI NIH HHS R01 CA134737NCI NIH HHS R01CA134737
6 · The paper itself

Abstract

E6 viral oncoproteins are key players in epithelial tumors induced by papillomaviruses in vertebrates, including cervical cancer in humans. E6 proteins target many host proteins by specifically interacting with acidic LxxLL motifs. We solved the crystal structures of bovine (BPV1) and human (HPV16) papillomavirus E6 proteins bound to LxxLL peptides from the focal adhesion protein paxillin and the ubiquitin ligase E6AP, respectively. In both E6 proteins, two zinc domains and a linker helix form a basic-hydrophobic pocket, which captures helical LxxLL motifs in a way compatible with other interaction modes. Mutational inactivation of the LxxLL binding pocket disrupts the oncogenic activities of both E6 proteins. This work reveals the structural basis of both the multifunctionality and the oncogenicity of E6 proteins.

Indexed as

Protein Interaction Domains and MotifsAmino Acid MotifsAmino Acid SequenceBovine papillomavirus 1Crystallography, X-RayHuman papillomavirus 16HumansHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataOncogene Proteins, ViralPaxillinPeptide FragmentsPoint MutationProtein Structure, SecondaryE6 protein, Human papillomavirus type 16Oncogene Proteins, ViralPaxillinPeptide Fragmentsprotein E6, Bovine papillomavirusRepressor ProteinsUBE3A protein, humanUbiquitin-Protein Ligases

Identifiers

PMID23393263
PMCPMC3899395
OpenAlexW1993568759

What OpenQuestion holds

Textmetadata
LicenceTDM
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.