Discover Community Create You

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

Effect of clinical isolate or cleavage site mutations in the SARS-CoV-2 spike protein on protein stability, cleavage, and cell–cell fusion

20 Jun 2021

Abstract excerpt

The trimeric severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein (S) is the sole viral protein responsible for both viral binding to a host cell and the membrane fusion event needed for cell entry. In addition to facilitating fusion needed for viral entry, S can also drive cell-cell fusion, a pathogenic effect observed in the lungs of SARS-CoV-2-infected patients. While several studies have...

Read the complete abstract on PubMed

Topics

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

Share to Animal Virus Infections Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34157282
DOI: 10.1016/j.jbc.2021.100902

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 20 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of clinical isolate or cleavage site mutations in the SARS-CoV-2 spike protein on protein stability, cleavage, and cell–cell fusionPMID 34157282Read ↗

Effect of mutations in the SARS-CoV-2 spike protein on protein stability, cleavage, and cell-cell fusion functionSemantic proximity Read ↗

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

Spike glycoprotein and host cell determinants of SARS-CoV-2 entry and cytopathic effectsSemantic proximity Read ↗

Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein.Semantic proximity Read ↗

Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusionSemantic proximity Read ↗

Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusionSemantic proximity Read ↗

Proteolytic processing of Middle East respiratory syndrome coronavirus spikes expands virus tropism.Semantic proximity Read ↗

D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction.Semantic proximity Read ↗

Domains and Functions of Spike Protein in Sars-Cov-2 in the Context of Vaccine Design.Semantic proximity Read ↗

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

Coronavirus entry: how we arrived at SARS-CoV-2Semantic proximity Read ↗

SARS-CoV-2 variants with mutations at the S1/S2 cleavage site are generated in vitro during propagation in TMPRSS2-deficient cells.Semantic proximity Read ↗

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