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

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

Cell reports - 12 Jan 2021

Gobeil Sophie M-C, Janowska Katarzyna, McDowell Shana, Mansouri Katayoun, Parks Robert, Manne Kartik, Stalls Victoria, Kopp Megan F, Henderson Rory, Edwards Robert J, Haynes Barton F, Acharya Priyamvada

Abstract excerpt

The severe acute respiratory coronavirus 2 (SARS-CoV-2) spike (S) protein is the target of vaccine design efforts to end the coronavirus disease 2019 (COVID-19) pandemic. Despite a low mutation rate, isolates with the D614G substitution in the S protein appeared early during the pandemic and are now the dominant form worldwide. Here, we explore S conformational changes and the effects of the D614G mutation on a...

Read the complete abstract on PubMed

Topics

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

Share to Protein Structure, Quaternary
Share to Cryoelectron Microscopy

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

Share to Immunogenicity, Vaccine

Share to Peptide Hydrolases

Share to Protein Domains

Share to Protein Stability

Share to Proteolysis

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 33417835
DOI: 10.1016/j.celrep.2020.108630
PMCID: PMC7762703

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 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

D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction.PMID 33417835Read ↗

Structural impact on SARS-CoV-2 spike protein by D614G substitutionSemantic proximity Read ↗

Structural impact on SARS-CoV-2 spike protein by D614G substitutionSemantic proximity Read ↗

Structural effects of spike protein D614G mutation in SARS-CoV-2.Semantic proximity Read ↗

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

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

The Spike-Stabilizing D614G Mutation Interacts with S1/S2 Cleavage Site Mutations To Promote the Infectious Potential of SARS-CoV-2 Variants.Semantic proximity Read ↗

Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein VariantSemantic proximity Read ↗

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

Conformational dynamics of SARS-CoV-2 spike on a membrane reveals the allosteric effects of furin cleavage and the D614G mutation.Semantic proximity Read ↗

The spike-stabilizing D614G mutation interacts with S1/S2 cleavage site mutations to promote the infectious potential of SARS-CoV-2 variantsSemantic proximity Read ↗

Structure of Furin Protease Binding to SARS-CoV-2 Spike Glycoprotein and Implications for Potential Targets and VirulenceSemantic proximity Read ↗

Structural Ramifications of Spike Protein D614G Mutation in SARS-CoV-2Semantic proximity Read ↗

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