Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2.

PloS one - 1 Jan 2017

Reinke Lennart Michel, Spiegel Martin, Plegge Teresa, Hartleib Anika, Nehlmeier Inga, Gierer Stefanie, Hoffmann Markus, Hofmann-Winkler Heike, Winkler Michael, Pöhlmann Stefan

Abstract excerpt

The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) mediates viral entry into target cells. Cleavage and activation of SARS S by a host cell protease is essential for infectious viral entry and the responsible enzymes are potential targets for antiviral intervention. The type II transmembrane serine protease TMPRSS2 cleaves and activates SARS S in cell culture and potentially also in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to TMPRSS2 gene
Share to HEK293 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Host-Pathogen Interactions

Share to Mutation

Share to Protein Transport

Share to Serine Endopeptidases

Share to Spike Glycoprotein, Coronavirus

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 28636671
DOI: 10.1371/journal.pone.0179177
PMCID: PMC5479546

Genes

TMPRSS2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2.PMID 28636671Read ↗

Different host cell proteases activate the SARS-coronavirus spike-protein for cell-cell and virus-cell fusion.Semantic proximity Read ↗

Proteolytic activation of SARS-CoV-2 spike at the S1/S2 boundary: potential role of proteases beyond furinSemantic proximity Read ↗

Insight towards the effect of the multibasic cleavage site of SARS-CoV-2 spike protein on cellular proteasesSemantic proximity Read ↗

Impact of SARS-CoV-2 Spike Mutations on Its Activation by TMPRSS2 and the Alternative TMPRSS13 Protease.Semantic proximity Read ↗

A Review on Expression, Pathological Roles, and Inhibition of TMPRSS2, the Serine Protease Responsible for SARS-CoV-2 Spike Protein ActivationSemantic proximity Read ↗

Sequential Glycosylations at the Multibasic Cleavage Site of SARS-CoV-2 Spike Protein Regulate Viral Activation, Assembly, and InfectionSemantic proximity Read ↗

TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target CellsSemantic proximity Read ↗

Effect of SARS-CoV-2 spike mutations on its activation by TMPRSS2 and TMPRSS13Semantic proximity Read ↗

Structure of Human TMPRSS2 in Complex with SARS-CoV-2 Spike Glycoprotein and Implications for Potential TherapeuticsSemantic proximity Read ↗

Elastase-mediated activation of the severe acute respiratory syndrome coronavirus spike protein at discrete sites within the S2 domain.Semantic proximity Read ↗

Sequential glycosylations at the multibasic cleavage site of SARS-CoV-2 spike protein regulate viral activity.Semantic proximity Read ↗

Genome-wide Bioinformatics Analysis of Human Protease Specificity Identified Potential Cathepsin L Cleavage Site at K790 Position of the SARS-CoV-2 Spike GlycoproteinSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.