Evidence map›Paper›PMID 24512893›Full record

ReviewVirus research2014

Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities.

Anna M Mielech, Yafang Chen, Andrew D Mesecar, Susan C Baker

Open access · greenAbstract readReview
In one paragraph

Review in Virus research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

121 citing papers in PubMed, 184 citations in OpenAlex.

  1. Role of HWorld journal of clinical cases · 2022
    Trial
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. ISG-15, beyond its functions in the cell: a mini review.Cellular and molecular life sciences : CMLS · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Consensus Pharmacophore Strategy For Identifying Novel SARS-Cov-2 MJournal of chemical information and modeling · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Unlocking STING as a Therapeutic Antiviral Strategy.International journal of molecular sciences · 2023
    Review

61 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

4 authors at 2 institutions in 1 country.

Anna M MielechDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States.
Yafang ChenDepartment of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States.
Andrew D MesecarDepartment of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States.
Susan C BakerDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States. Electronic address: sbaker1@lumc.edu.
Loyola University Chicago · USPurdue University West Lafayette · US

Funding

Mechanisms of viral proteases in coronavirus replication and pathogenesisR01AI085089 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI BAKER, SUSAN C., MESECAR, ANDREW D · 2010 to 2019
$6.8M
NIAID NIH HHS R01 AI085089
6 · The paper itself

Abstract

Coronaviruses and arteriviruses, members of the order Nidovirales, are positive strand RNA viruses that encode large replicase polyproteins that are processed by viral proteases to generate the nonstructural proteins which mediate viral RNA synthesis. The viral papain-like proteases (PLPs) are critical for processing the amino-terminal end of the replicase and are attractive targets for antiviral therapies. With the analysis of the papain-like protease of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV), came the realization of the multifunctional nature of these enzymes. Structural and enzymatic studies revealed that SARS-CoV PLpro can act as both a protease to cleave peptide bonds and also as a deubiquitinating (DUB) enzyme to cleave the isopeptide bonds found in polyubiquitin chains. Furthermore, viral DUBs can also remove the protective effect of conjugated ubiquitin-like molecules such as interferon stimulated gene 15 (ISG15). Extension of these studies to other coronaviruses and arteriviruses led to the realization that viral protease/DUB activity is conserved in many family members. Overexpression studies revealed that viral protease/DUB activity can modulate or block activation of the innate immune response pathway. Importantly, mutations that alter DUB activity but not viral protease activity have been identified and arteriviruses expressing DUB mutants stimulated higher levels of acute inflammatory cytokines after infection. Further understanding of the multifunctional nature of the Nidovirus PLP/DUBs may facilitate vaccine development. Here, we review studies describing the PLPs' enzymatic activity and their role in virus pathogenesis.

Indexed as

Multifunctional EnzymesNidoviralesPeptide HydrolasesUbiquitin-Specific ProteasesMultifunctional EnzymesPeptide HydrolasesUbiquitin-Specific ProteasesArterivirusCoronavirusDeISGylating activityDeubiquitinating enzymeMERS-CoVPapain-like protease

Identifiers

PMID24512893
PMCPMC4125544
OpenAlexW2053473486

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.