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

Single-molecule force stability of the SARS-CoV-2-ACE2 interface in variants-of-concern.

Nature nanotechnology - 1 Mar 2024

Bauer Magnus S, Gruber Sophia, Hausch Adina, Melo Marcelo C R, Gomes Priscila S F C, Nicolaus Thomas, Milles Lukas F, Gaub Hermann E, Bernardi Rafael C, Lipfert Jan

Abstract excerpt

Mutations in SARS-CoV-2 have shown effective evasion of population immunity and increased affinity to the cellular receptor angiotensin-converting enzyme 2 (ACE2). However, in the dynamic environment of the respiratory tract, forces act on the binding partners, which raises the question of whether not only affinity but also force stability of the SARS-CoV-2-ACE2 interaction might be a selection factor for...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Angiotensin-Converting Enzyme 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COVID-19

Share to ACE2 gene

Share to Kinetics

Share to Mutation

Share to Protein Binding

Share to SARS-CoV-2

Source

Identifiers

PMID: 38012274
DOI: 10.1038/s41565-023-01536-7

Genes

ACE2

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

Single-molecule force stability of the SARS-CoV-2-ACE2 interface in variants-of-concern.PMID 38012274Read ↗

Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2Semantic proximity Read ↗

A Tethered Ligand Assay to Probe SARS-CoV-2:ACE2 InteractionsSemantic proximity Read ↗

Molecular insights into receptor binding energetics and neutralization of SARS-CoV-2 variants.Semantic proximity Read ↗

Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2.Semantic proximity Read ↗

A Tethered Ligand Assay to Probe the SARS-CoV-2 ACE2 Interaction under Constant ForceSemantic proximity Read ↗

Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule levelSemantic proximity Read ↗

Mutation-driven adaptation of ACE2-RBD binding revealed by integrative molecular dynamics analysis.Semantic proximity Read ↗

Force-Activated Slip-Catch-Slip Bonds Stabilize Virus InteractionsSemantic proximity Read ↗

Free Energy Perturbation Calculations of Mutation Effects on SARS-CoV-2 RBD::ACE2 Binding Affinity.Semantic proximity Read ↗

Free energy perturbation calculations of mutation effects on SARS-CoV-2 RBD::ACE2 binding affinitySemantic proximity Read ↗

Conformational stability of the bacterial adhesin, FimH, with an inactivating mutation.Semantic proximity Read ↗

Allosteric communication between ACE2 active site and binding interface with SARS-CoV-2.Semantic proximity Read ↗

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