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

Exposing structural variations in SARS-CoV-2 evolution.

Scientific reports - 11 Nov 2021

Yang Jiaan, Zhang Peng, Cheng Wen Xiang, Lu Youyong, Gang Wu, Ren Gang

Abstract excerpt

The mutation of SARS-CoV-2 influences viral function as residue replacements affect both physiochemical properties and folding conformations. Although a large amount of data on SARS-CoV-2 is available, the investigation of how viral functions change in response to mutations is hampered by a lack of effective structural analysis. Here, we exploit the advances of protein structure fingerprint technology to study...

Read the complete abstract on PubMed

Topics

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

Share to Angiotensin-Converting Enzyme 2
Share to COVID-19
Share to Protein Folding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Interaction Maps

Share to Protein Multimerization

Share to SARS-CoV-2

Share to Severe acute respiratory syndrome-related coronavirus

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 34764391
DOI: 10.1038/s41598-021-01650-3
PMCID: PMC8586246

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exposing structural variations in SARS-CoV-2 evolution.PMID 34764391Read ↗

Exposing Structural Variations in SARS-CoV-2 EvolutionSemantic proximity Read ↗

Comparative Study of the Mutations Observed in the SARS-CoV-2 RBD Variants of Concern and Their Impact on the Interaction with the ACE2 Protein.Semantic proximity Read ↗

D614G mutation and SARS-CoV-2: impact on S-protein structure, function, infectivity, and immunity.Semantic proximity Read ↗

Structural Comparison and Drug Screening of Spike Proteins of Ten SARS-CoV-2 VariantsSemantic proximity Read ↗

Investigating the role of binding free energy, binding affinity and antibody escape in the evolution of SARS-CoV-2 spike proteinSemantic proximity Read ↗

Evolutionary Insights into the Envelope Protein of SARS-CoV-2Semantic proximity Read ↗

Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2Semantic proximity Read ↗

Mutational landscape and in silico structure models of SARS-CoV-2 spike receptor binding domain reveal key molecular determinants for virus-host interaction.Semantic proximity Read ↗

Decomposition of the SARS-CoV-2-ACE2 interface reveals a common trend among emerging viral variantsSemantic proximity Read ↗

SARS-CoV-2 journey: from alpha variant to omicron and its sub-variants.Semantic proximity Read ↗

Mutations in SARS-CoV-2; Consequences in structure, function, and pathogenicity of the virus.Semantic proximity Read ↗

Molecular Insights into the Variability in Infection and Immune Evasion Capabilities of SARS-CoV-2 Variants: A Sequence and Structural Investigation of the RBD Domain.Semantic proximity Read ↗

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