Evidence map›Paper›PMID 24121034›Full record

ReviewAntiviral research2013

Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.

Graham Simmons, Pawel Zmora, Stefanie Gierer, Adeline Heurich, Stefan Pöhlmann

Open access · greenAbstract readReview
In one paragraph

Review in Antiviral research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 240 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
240citing papers in PubMed, 4 pooled it
5.0field-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

240 citing papers in PubMed, 4 syntheses or guidelines pooled it, 441 citations in OpenAlex.

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180 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

5 authors at 2 institutions in 2 countries.

Graham SimmonsBlood Systems Research Institute, 270 Masonic Ave, San Francisco, CA 94118, United States. Electronic address: gsimmons@bloodsystems.org.
Pawel Zmora
Stefanie Gierer
Adeline Heurich
Stefan Pöhlmann
German Primate Center · DEBlood Systems Research Institute · US

Funding

Modeling viral entry and its inhibition using SARS-CoVR01AI074986 · NIAID · VITALANT · PI SIMMONS, GRAHAM · 2008 to 2012
$2.0M
Broad spectrum antivirals targeting envelope proteolysis and viral uncoatingR21AI107165 · NIAID · VITALANT · PI SIMMONS, GRAHAM · 2013 to 2014
$499k
NIAID NIH HHS R01 AI074986NIAID NIH HHS R01AI074986NIAID NIH HHS R21 AI107165NIAID NIH HHS R21AI107165
6 · The paper itself

Abstract

The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10years of research on highly pathogenic human coronaviruses.''

Indexed as

Angiotensin-Converting Enzyme 2CathepsinsCommunicable Diseases, EmergingCoronavirus InfectionsEndosomesHumansLungMembrane ProteinsModels, BiologicalPeptidyl-Dipeptidase AProteolysisSerine EndopeptidasesSerine ProteasesSevere Acute Respiratory SyndromeSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2CathepsinsMembrane ProteinsPeptidyl-Dipeptidase ASerine EndopeptidasesSerine ProteasesSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVTMPRSS2 protein, humanCathepsin LMERSProteaseSARSSpike proteinTMPRSS2

Identifiers

PMID24121034
PMCPMC3889862
OpenAlexW2044139515

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.