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

SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy

15 Feb 2022

Abstract excerpt

SARS-CoV-2 surface S glycoprotein-the target of antibodies and vaccines-is responsible for binding to the cellular receptor hACE2. The interactions between S and hACE2 trigger structural rearrangements of S from closed to open conformations prerequisite for virus entry. Under the selection pressure imposed by adaptation to the human host and increasing vaccinations and convalescent patients, SARS-CoV-2 is...

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 About Contact Helena Bioinformatics

Source

Identifiers

PMID: 35164561
DOI: 10.1128/mbio.03227-21

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary StrategyPMID 35164561Read ↗

SARS-CoV-2 variants exhibit increased kinetic stability of open spike conformations as an evolutionary strategySemantic proximity Read ↗

Spike Protein Mutation-Induced Changes in the Kinetic and Thermodynamic Behavior of Its Receptor Binding Domains Explain Their Higher Propensity to Attain Open States in SARS-CoV-2 Variants of ConcernSemantic proximity Read ↗

SARS-CoV-2 Omicron variations reveal mechanisms controlling cell entry dynamics and antibody neutralizationSemantic proximity Read ↗

Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein.Semantic proximity Read ↗

Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants.Semantic proximity Read ↗

Molecular insights into the adaptive evolution of SARS-CoV-2 spike proteinSemantic proximity Read ↗

The SARS-CoV-2 Spike Variant D614G Favors an Open Conformational StateSemantic proximity Read ↗

Energetics of Spike Protein Opening of SARS-CoV-1 and SARS-CoV-2 and Its Variants of Concern: Implications in Host Receptor Scanning and Transmission.Semantic proximity Read ↗

Conformational stability of SARS-CoV-2 glycoprotein spike variantsSemantic proximity Read ↗

Population Dynamics and Structural Effects at Short and Long Range Support the Hypothesis of the Selective Advantage of the G614 SARS-CoV-2 Spike VariantSemantic proximity Read ↗

Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM.Semantic proximity Read ↗

Timeline of changes in spike conformational dynamics in emergent SARS-CoV-2 variants reveal progressive stabilization of trimer stalk with altered NTD dynamicsSemantic proximity Read ↗

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