Evidence map›Paper›PMID 21440638›Full record

ReviewJournal of structural biology2011

Cells under siege: viral glycoprotein interactions at the cell surface.

Thomas A Bowden, E Yvonne Jones, David I Stuart

Abstract readReview
In one paragraph

Review in Journal of structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. SERINC5 counters retroviruses and non-retroviruses.Frontiers in cellular and infection microbiology · 2024
    Review
  4. Review
  5. Article
  6. Review
  7. A structure-based rationale for sialic acid independent host-cell entry of Sosuga virus.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. Article
  10. Convergent immunological solutions to Argentine hemorrhagic fever virus neutralization.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Molecular recognition of human ephrinB2 cell surface receptor by an emergent African henipavirus.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. Article
  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

3 authors.

Thomas A BowdenDivision of Structural Biology, University of Oxford, Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Oxford OX37BN, United Kingdom. tom@strubi.ox.ac.uk
E Yvonne Jones
David I Stuart

Funding

Cancer Research UKMedical Research Council G1000099Medical Research Council G1100525Wellcome Trust 089026/Z/09/ZWellcome Trust 090532
6 · The paper itself

Abstract

As obligate parasites, viruses are required to enter and replicate within their host, a process which employs many of their proteins to hijack natural cellular processes. High resolution X-ray crystallographic analysis has proven to be an ideal method to visualize the mechanisms by which such virus-host interactions occur and has revealed the innovative capacity of viruses to adapt efficiently to their hosts. In this review, we draw upon recently elucidated paramyxovirus-, arenavirus-, and poxvirus-host protein complex crystal structures to reveal both the capacity of viruses to appropriate one component of a physiological protein-protein binding event (often modifying it to out-compete the host-protein), and the ability to utilize novel binding sites on host cell surface receptors. The structures discussed shed light on a number of biological processes ranging from viral entry to virulence and host antagonism. Drawn together they reveal the common strategies which viruses have evolved to interact with their natural host. The structures also support molecular level rationales for how viruses can be transmitted to unrelated organisms and thus pose severe health risks.

Indexed as

Host-Pathogen InteractionsAnimalsCell MembraneGlycoproteinsHenipavirusHumansImmunologic FactorsProtein ConformationReceptors, TransferrinSemaphorinsViral ProteinsVirus InternalizationGlycoproteinsImmunologic FactorsReceptors, TransferrinSemaphorinsViral Proteins

Identifiers

PMID21440638
PMCPMC3137789

What OpenQuestion holds

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LicenceCC BY
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.