Evidence map›Paper›PMID 21775458›Full record

ReviewJournal of virology2011

Emerging theme: cellular PDZ proteins as common targets of pathogenic viruses.

Ronald T Javier, Andrew P Rice

Abstract readReview
In one paragraph

Review in Journal of virology, 2011. 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
–field-weighted citation impact
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.

  1. International journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Evolutionarily divergent nidovirus with an exceptionally large genome identified in Pacific oysters undergoing mass mortality.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

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

2 authors.

Ronald T JavierDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA. rjavier@bcm.edu
Andrew P Rice

Funding

ROLE OF THE AD9 E4 REGION IN MAMMARY GLAND ONCOGENESISR01CA058541 · NCI · BAYLOR COLLEGE OF MEDICINE · PI JAVIER, RONALD T. · 1993 to 2013
$3.9M
Structure and function of influenza A virus PDZ-binding motifR21AI083396 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI RICE, ANDREW P · 2010 to 2011
$420k
NCI NIH HHS R01 CA058541NCI NIH HHS R01CA058541NIAID NIH HHS R21 AI083396NIAID NIH HHS R21AI083396
6 · The paper itself

Abstract

More than a decade ago, three viral oncoproteins, adenovirus type 9 E4-ORF1, human T-lymphotropic virus type 1 Tax, and high-risk human papillomavirus E6, were found to encode a related carboxyl-terminal PDZ domain-binding motif (PBM) that mediates interactions with a select group of cellular PDZ proteins. Recent studies have shown that many other viruses also encode PBM-containing proteins that bind to cellular PDZ proteins. Interestingly, these recently recognized viruses include not only some with oncogenic potential (hepatitis B virus, rhesus papillomavirus, cottontail rabbit papillomavirus) but also many without this potential (influenza virus, Dengue virus, tick-borne encephalitis virus, rabies virus, severe acute respiratory syndrome coronavirus, human immunodeficiency virus). Examination of the cellular PDZ proteins that are targets of viral PBMs reveals that the viral proteins often interact with the same or similar types of PDZ proteins, most notably Dlg1 and other members of the membrane-associated guanylate kinase protein family, as well as Scribble. In addition, cellular PDZ protein targets of viral PBMs commonly control tight junction formation, cell polarity establishment, and apoptosis. These findings reveal a new theme in virology wherein many different virus families encode proteins that bind and perturb the function of cellular PDZ proteins. The inhibition or perturbation of the function of cellular PDZ proteins appears to be a widely used strategy for viruses to enhance their replication, disseminate in the host, and transmit to new hosts.

Indexed as

Host-Pathogen InteractionsAnimalsHumansProtein BindingProtein Interaction Domains and MotifsViral ProteinsVirusesViral Proteins

Identifiers

PMID21775458
PMCPMC3209276

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.