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

Functional importance of the D614G mutation in the SARS-CoV-2 spike protein.

Biochemical and biophysical research communications - 29 Jan 2021

Jackson Cody B, Zhang Lizhou, Farzan Michael, Choe Hyeryun

Abstract excerpt

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped virus which binds its cellular receptor angiotensin-converting enzyme 2 (ACE2) and enters hosts cells through the action of its spike (S) glycoprotein displayed on the surface of the virion. Compared to the reference strain of SARS-CoV-2, the majority of currently circulating isolates possess an S protein variant characterized by an...

Read the complete abstract on PubMed

Topics

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

Share to Glycine
Share to Protein Domains
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Aspartic Acid

Share to Binding Sites

Share to COVID-19

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 33220921
DOI: 10.1016/j.bbrc.2020.11.026
PMCID: PMC7664360

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional importance of the D614G mutation in the SARS-CoV-2 spike protein.PMID 33220921Read ↗

D614G mutation of SARS-CoV-2 spike protein enhances viral infectivitySemantic proximity Read ↗

Naturally mutated spike proteins of SARS-CoV-2 variants show differential levels of cell entrySemantic proximity Read ↗

Making sense of spike D614G in SARS-CoV-2 transmission.Semantic proximity Read ↗

Structure-function relations of the SARS-CoV-2 spike protein and impact of mutations in the variants of concern.Semantic proximity Read ↗

Mutation informatics: SARS-CoV-2 receptor-binding domain of the spike protein.Semantic proximity Read ↗

SARS-CoV-2 spike D614G change enhances replication and transmission.Semantic proximity Read ↗

SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity.Semantic proximity Read ↗

SARS-CoV-2: phylogenetic status, mutations and therapeutic research based on spike protein.Semantic proximity Read ↗

Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions with ACE2Semantic proximity Read ↗

The Spike D614G mutation increases SARS-CoV-2 infection of multiple human cell typesSemantic proximity Read ↗

SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity.Semantic proximity Read ↗

Sequence variation of SARS-CoV-2 spike protein may facilitate stronger interaction with ACE2 promoting high infectivitySemantic proximity Read ↗

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