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

Probing Affinity, Avidity, Anticooperativity, and Competition in Antibody and Receptor Binding to the SARS-CoV-2 Spike by Single Particle Mass Analyses

4 Nov 2021

Abstract excerpt

Determining how antibodies interact with the spike (S) protein of the SARS-CoV-2 virus is critical for combating COVID-19. Structural studies typically employ simplified, truncated constructs that may not fully recapitulate the behavior of the original complexes. Here, we combine two single particle mass analysis techniques (mass photometry and charge-detection mass spectrometry) to enable the measurement of full...

Read the complete abstract on PubMed

Topics

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

Share to Monoclonal and Polyclonal Antibodies Research
Share to SARS-CoV-2 and COVID-19 Research
Share to SARS-CoV-2 detection and testing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34845440
DOI: 10.1021/acscentsci.1c00804

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Probing Affinity, Avidity, Anticooperativity, and Competition in Antibody and Receptor Binding to the SARS-CoV-2 Spike by Single Particle Mass AnalysesPMID 34845440Read ↗

Cooperativity and induced oligomerisation control the interaction of SARS-CoV-2 with its cellular receptor and patient-derived antibodiesSemantic proximity Read ↗

A cell-based, spike protein binding assay highlights differences in antibody neutralising capacity for SARS-CoV-2 variantsSemantic proximity Read ↗

Distinct Binding Modes of Inter-Spike Cross-Linking Suggest a Supplementary Mechanism for SARS-CoV-2 Antibody NeutralizationSemantic proximity Read ↗

Mass Photometry Reveals Distinct ACE2 Binding Stoichiometries across SARS-CoV-2 Omicron Subvariants.Semantic proximity Read ↗

Steric hindrance of antibody binding in an Omicron spike fusion intermediate.Semantic proximity Read ↗

Structural basis of SARS-Cov-2 spike recognition by engineered synthetic multivalent VHH antibodiesSemantic proximity Read ↗

Characterization of Nanobody Binding to Distinct Regions of the SARS-CoV-2 Spike Protein by Flow VirometrySemantic proximity Read ↗

Mapping the allosteric effects that define functional activity of SARS-CoV-2 specific antibodiesSemantic proximity Read ↗

Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery coreSemantic proximity Read ↗

The Answer Lies in the Energy: How Simple Atomistic Molecular Dynamics Simulations May Hold the Key to Epitope Prediction on the Fully Glycosylated SARS-CoV‑2 Spike ProteinSemantic proximity Read ↗

Single-Particle Characterization of SARS-CoV-2 Isoelectric Point and Comparison to Variants of InterestSemantic proximity Read ↗

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