Evidence map›Paper›PMID 27145174›Full record

ReviewReviews in medical virology2016

Enteroviral proteases: structure, host interactions and pathogenicity.

Olli H Laitinen, Emma Svedin, Sebastian Kapell, Anssi Nurminen, Vesa P Hytönen, Malin Flodström-Tullberg

Open access · bronzeAbstract readReview
In one paragraph

Review in Reviews in medical virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed, 1 pooled it
4.5field-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

68 citing papers in PubMed, 1 synthesis or guideline pooled it, 113 citations in OpenAlex.

  1. Pooled it
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  17. Crystal structures of the 3C proteases from Coxsackievirus B3 and B4.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
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  20. An efficientJournal of virology · 2024
    Article

8 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 3 institutions in 2 countries.

Olli H LaitinenBioMediTech, Finland and Fimlab Laboratories, University of Tampere, Tampere, Finland.
Emma SvedinThe Center for Infectious Medicine, Department of Medicine HS, Karolinska Institutet, Stockholm, Sweden.
Sebastian KapellThe Center for Infectious Medicine, Department of Medicine HS, Karolinska Institutet, Stockholm, Sweden.
Anssi NurminenBioMediTech, Finland and Fimlab Laboratories, University of Tampere, Tampere, Finland.
Vesa P HytönenBioMediTech, Finland and Fimlab Laboratories, University of Tampere, Tampere, Finland.
Malin Flodström-TullbergBioMediTech, Finland and Fimlab Laboratories, University of Tampere, Tampere, Finland.
Fimlab (Finland) · FIKarolinska Institutet · SETampere University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enteroviruses are common human pathogens, and infections are particularly frequent in children. Severe infections can lead to a variety of diseases, including poliomyelitis, aseptic meningitis, myocarditis and neonatal sepsis. Enterovirus infections have also been implicated in asthmatic exacerbations and type 1 diabetes. The large disease spectrum of the closely related enteroviruses may be partially, but not fully, explained by differences in tissue tropism. The molecular mechanisms by which enteroviruses cause disease are poorly understood, but there is increasing evidence that the two enteroviral proteases, 2A(pro) and 3C(pro) , are important mediators of pathology. These proteases perform the post-translational proteolytic processing of the viral polyprotein, but they also cleave several host-cell proteins in order to promote the production of new virus particles, as well as to evade the cellular antiviral immune responses. Enterovirus-associated processing of cellular proteins may also contribute to pathology, as elegantly demonstrated by the 2A(pro) -mediated cleavage of dystrophin in cardiomyocytes contributing to Coxsackievirus-induced cardiomyopathy. It is likely that improved tools to identify targets for these proteases will reveal additional host protein substrates that can be linked to specific enterovirus-associated diseases. Here, we discuss the function of the enteroviral proteases in the virus replication cycle and review the current knowledge regarding how these proteases modulate the infected cell in order to favour virus replication, including ways to avoid detection by the immune system. We also highlight new possibilities for the identification of protease-specific cellular targets and thereby a way to discover novel mechanisms contributing to disease. Copyright © 2016 John Wiley & Sons, Ltd.

Indexed as

Host-Pathogen InteractionsVirus ReplicationCysteine EndopeptidasesEnterovirusHumansImmune EvasionProtein ConformationProtein Processing, Post-TranslationalSequence AlignmentViral ProteinsCysteine EndopeptidasesViral Proteins

Identifiers

PMID27145174
PMCPMC7169145
OpenAlexW2345602871

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.