Evidence map›Paper›PMID 30647130›Full record

ArticleThe Journal of biological chemistry2019

Polyprotein processing and intermolecular interactions within the viral replication complex spatially and temporally control norovirus protease activity.

Edward Emmott, Alexis de Rougemont, Myra Hosmillo, Jia Lu, Timothy Fitzmaurice, Jürgen Haas, Ian Goodfellow

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Edward EmmottFrom the Division of Virology, Department of Pathology, University of Cambridge, Addenbrookes Hospital, Hills Road, Cambridge CB2 0QQ, United Kingdom, e.emmott@northeastern.edu.ORCID 0000-0002-3239-8178
Alexis de Rougemontthe National Reference Centre for Gastroenteritis Viruses, Labology of Biology and Pathology, University Hospital Dijon Bourgogne, Dijon 21700, France.ORCID 0000-0002-3084-9414
Myra HosmilloFrom the Division of Virology, Department of Pathology, University of Cambridge, Addenbrookes Hospital, Hills Road, Cambridge CB2 0QQ, United Kingdom.
Jia LuFrom the Division of Virology, Department of Pathology, University of Cambridge, Addenbrookes Hospital, Hills Road, Cambridge CB2 0QQ, United Kingdom.ORCID 0000-0003-3995-324X
Timothy FitzmauriceFrom the Division of Virology, Department of Pathology, University of Cambridge, Addenbrookes Hospital, Hills Road, Cambridge CB2 0QQ, United Kingdom.
Jürgen Haasthe Division of Infection and Pathway Medicine, University of Edinburgh Medical School, Edinburgh EH16 4SB, United Kingdom.
Ian GoodfellowFrom the Division of Virology, Department of Pathology, University of Cambridge, Addenbrookes Hospital, Hills Road, Cambridge CB2 0QQ, United Kingdom, ig299@cam.ac.uk.ORCID 0000-0002-9483-510X
University of Cambridge · GBProcédés Alimentaires et Microbiologiques · FRUniversity of Edinburgh · GB

Funding

Medical Research Council G0501453Medical Research Council MR/P011349/1
6 · The paper itself

Abstract

Norovirus infections are a major cause of acute viral gastroenteritis and a significant burden on global human health. A vital process for norovirus replication is the processing of the nonstructural polyprotein by a viral protease into the viral components required to form the viral replication complex. This cleavage occurs at different rates, resulting in the accumulation of stable precursor forms. Here, we characterized how precursor forms of the norovirus protease accumulate during infection. Using stable forms of the protease precursors, we demonstrated that all of them are proteolytically active

Indexed as

Virus ReplicationAnimalsCaliciviridae InfectionsCell LineHeLa CellsHumansMiceNorovirusPeptide HydrolasesPolyproteinsProtein BindingPeptide HydrolasesPolyproteinsCalicivirusfluorescence resonance energy transfer (FRET)Norovirusplus-stranded RNA virusPrecursorproteaseRNA virusviral replication

Identifiers

PMID30647130
PMCPMC6422069
OpenAlexW2908982806

What OpenQuestion holds

Textmetadata
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.