Evidence map›Paper›PMID 26321473›Full record

ReviewArchives of virology2015

Beyond RGD: virus interactions with integrins.

Hosni A M Hussein, Lia R Walker, Usama M Abdel-Raouf, Sayed A Desouky, Abdel Khalek M Montasser, Shaw M Akula

Open access · bronzeAbstract readReview
In one paragraph

Review in Archives of virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

115 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
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  4. Cell entry mechanisms of porcine enteric coronaviruses.The Journal of biological chemistry · 2026
    Review
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  19. LangerinClinical, cosmetic and investigational dermatology · 2025
    Review
  20. Article

55 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

6 authors at 2 institutions in 3 countries.

Hosni A M HusseinDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, 27834, USA.
Lia R WalkerDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, 27834, USA.
Usama M Abdel-RaoufFaculty of Science, Al Azhar University, Assiut Branch, Assiut, 71524, Egypt.
Sayed A DesoukyFaculty of Science, Al Azhar University, Assiut Branch, Assiut, 71524, Egypt.
Abdel Khalek M MontasserBrucellosis Research Department, Animal Health Research Institute, Dokki, Egypt.
Shaw M AkulaDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, NC, 27834, USA. akulas@ecu.edu.ORCID http://orcid.org/0000-0001-7990-7307
East Carolina University · USAl-Azhar University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viruses successfully infect host cells by initially binding to the surfaces of the cells, followed by an intricate entry process. As multifunctional heterodimeric cell-surface receptor molecules, integrins have been shown to usefully serve as entry receptors for a plethora of viruses. However, the exact role(s) of integrins in viral pathogen internalization has yet to be elaborately described. Notably, several viruses harbor integrin-recognition motifs displayed on viral envelope/capsid-associated proteins. The most common of these motifs is the minimal peptide sequence for binding integrins, RGD (Arg-Gly-Asp), which is known for its role in virus infection via its ability to interact with over half of the more than 20 known integrins. Not all virus-integrin interactions are RGD-dependent, however. Non-RGD-binding integrins have also been shown to effectively promote virus entry and infection as well. Such virus-integrin binding is shown to facilitate adhesion, cytoskeleton rearrangement, integrin activation, and increased intracellular signaling. Also, we have attempted to discuss the role of carbohydrate moieties in virus interactions with receptor-like host cell surface integrins that drive the process of internalization. As much as possible, this article examines the published literature regarding the role of integrins in terms of virus infection and virus-encoded glycosylated proteins that mediate interactions with integrins, and it explores the idea of targeting these receptors as a therapeutic treatment option.

Indexed as

Amino Acid MotifsAnimalsHumansIntegrinsProtein BindingViral Envelope ProteinsVirus DiseasesVirusesIntegrinsViral Envelope Proteins

Identifiers

PMID26321473
PMCPMC7086847
OpenAlexW1237762235

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.