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

Topics Community

Article

Structural Consequences of Variation in SARS-CoV-2 B.1.1.7

30 Apr 2021

Abstract excerpt

New globally circulating SARS-CoV-2 strains are causing concern about evolution of virus transmissibility, fitness and immune evasion mechanisms. A variant emerging from the United Kingdom called SARS-CoV-2 VUI 202012/01, or B.1.1.7, is thought to exhibit increased transmissibility that results from replication 4-10 times faster than the original Wuhan virus (Wuhan-Hu-1). Although this property is suspected to...

Source

Identifiers

PMID: 33969357
DOI: 10.33696/immunology.3.085

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural Consequences of Variation in SARS-CoV-2 B.1.1.7PMID 33969357Read ↗

Evolution of the SARS-CoV-2 spike protein in the human hostSemantic proximity Read ↗

In Silico Investigation of the New UK (B.1.1.7) and South African (501Y.V2) SARS-CoV-2 Variants with a Focus at the ACE2–Spike RBD InterfaceSemantic proximity Read ↗

Effect of natural mutations of SARS-CoV-2 on spike structure, conformation and antigenicitySemantic proximity Read ↗

Evolution of the SARS-CoV-2 spike protein in the human hostSemantic proximity Read ↗

In silico investigation of the new UK (B.1.1.7) and South African (501Y.V2) SARS-CoV-2 variants with a focus at the ACE2-Spike RBD interfaceSemantic proximity Read ↗

Possible link between higher transmissibility of B.1.617 and B.1.1.7 variants of SARS-CoV-2 and increased structural stability of its spike protein and hACE2 affinitySemantic proximity Read ↗

Evolution, correlation, structural impact and dynamics of emerging SARS-CoV-2 variantsSemantic proximity Read ↗

Computational Investigation of Selected Spike Protein Mutations in SARS-CoV-2: Delta, Omicron, and Some Circulating SubvariantsSemantic proximity Read ↗

A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein.Semantic proximity Read ↗

A Comprehensive Analysis of Structural and Functional Changes Induced by SARS-CoV-2 Spike Protein MutationsSemantic proximity Read ↗

Impact of South African 501.V2 Variant on SARS-CoV-2 Spike Infectivity and Neutralization: A Structure-based Computational AssessmentSemantic proximity Read ↗

Mutations in the B.1.1.7 SARS-CoV-2 spike protein reduce receptor-binding affinity and induce a flexible link to the fusion peptideSemantic proximity Read ↗

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