Evidence map›Paper›PMID 29463763›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies.

Kirby N Swatek, Martina Aumayr, Jonathan N Pruneda, Linda J Visser, Stephen Berryman, Anja F Kueck, Paul P Geurink, Huib Ovaa, Frank J M van Kuppeveld, Tobias J Tuthill and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.2field-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

51 citing papers in PubMed, 78 citations in OpenAlex.

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  15. An expanded lexicon for the ubiquitin code.Nature reviews. Molecular cell biology · 2023
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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

12 authors at 5 institutions in 3 countries.

Kirby N SwatekProtein and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, CB2 0QH Cambridge, United Kingdom.
Martina AumayrDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Vienna Biocenter, Medical University of Vienna, A-1030 Vienna, Austria.
Jonathan N PrunedaProtein and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, CB2 0QH Cambridge, United Kingdom.
Linda J VisserDepartment of Infectious Diseases & Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, 3584CL Utrecht, The Netherlands.
Stephen BerrymanThe Pirbright Institute, GU24 0NF Pirbright, Surrey, United Kingdom.
Anja F KueckProtein and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, CB2 0QH Cambridge, United Kingdom.
Paul P GeurinkDepartment of Chemical Immunology, Leiden University Medical Centre, 2333 ZC Leiden, The Netherlands.
Huib OvaaDepartment of Chemical Immunology, Leiden University Medical Centre, 2333 ZC Leiden, The Netherlands.
Frank J M van KuppeveldDepartment of Infectious Diseases & Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, 3584CL Utrecht, The Netherlands.
Tobias J TuthillThe Pirbright Institute, GU24 0NF Pirbright, Surrey, United Kingdom.
Tim SkernDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Vienna Biocenter, Medical University of Vienna, A-1030 Vienna, Austria.ORCID 0000-0001-8865-5500
David KomanderProtein and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, CB2 0QH Cambridge, United Kingdom; dk@mrc-lmb.cam.ac.uk.ORCID 0000-0002-8092-4320
MRC Laboratory of Molecular Biology · GBLeiden University · NLMax Perutz Labs · ATThe Pirbright Institute · GBUtrecht University · NL

Funding

Biotechnology and Biological Sciences Research Council BBS/E/I/00007034Biotechnology and Biological Sciences Research Council BBS/E/I/00007037Biotechnology and Biological Sciences Research Council BBS/E/I/00007039European Research Council 309756Medical Research Council MC_U105192732
6 · The paper itself

Abstract

In response to viral infection, cells mount a potent inflammatory response that relies on ISG15 and ubiquitin posttranslational modifications. Many viruses use deubiquitinases and deISGylases that reverse these modifications and antagonize host signaling processes. We here reveal that the leader protease, Lb

Indexed as

CytokinesEndopeptidasesUbiquitinsCrystallographyHeLa CellsHost-Pathogen InteractionsHumansModels, MolecularProtein BindingSubstrate SpecificityUbiquitinCytokinesEndopeptidasesISG15 protein, humanleader proteinase, foot-and-mouth disease virusUbiquitinUbiquitinsFMDVISG15structureubiquitinviral signaling

Identifiers

PMID29463763
PMCPMC5877979
OpenAlexW2790472448

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.