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

Elucidating important structural features for the binding affinity of spike ‐ SARS‐CoV ‐2 neutralizing antibody complexes

11 Nov 2021

Abstract excerpt

The coronavirus disease 2019 (COVID-19) has affected the lives of millions of people around the world. In an effort to develop therapeutic interventions and control the pandemic, scientists have isolated several neutralizing antibodies against SARS-CoV-2 from the vaccinated and convalescent individuals. These antibodies can be explored further to understand SARS-CoV-2 specific antigen-antibody interactions and...

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 Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34761442
DOI: 10.1002/prot.26277

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 · 12 closest

Elucidating important structural features for the binding affinity of spike ‐ SARS‐CoV ‐2 neutralizing antibody complexesPMID 34761442Read ↗

Fast Prediction of Binding Affinities of SARS-CoV-2 Spike Protein and Its Mutants with Antibodies through Intermolecular Interaction Modeling-Based Machine Learning.Semantic proximity Read ↗

Spike protein binding prediction with neutralizing antibodies of SARS-CoV-2Semantic proximity Read ↗

Computational Analysis of Mutations in the Receptor-Binding Domain of SARS-CoV-2 Spike and Their Effects on Antibody Binding.Semantic proximity Read ↗

Structural basis of Omicron immune evasion: A comparative computational study of Spike protein-Antibody interactionSemantic proximity Read ↗

Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating 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 ↗

A SARS-CoV-2 neutralizing antibody with extensive Spike binding coverage and modified for optimal therapeutic outcomes.Semantic proximity Read ↗

Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodiesSemantic proximity Read ↗

Antibody accessibility determines location of spike surface mutations in SARS-CoV-2 variants.Semantic proximity Read ↗

In silico Antibody Mutagenesis for Optimizing its Binding to the Spike Protein of SARS-CoV-2Semantic proximity Read ↗

Predicting spike protein NTD mutations of SARS-CoV-2 causing immune evasion by molecular dynamics simulations.Semantic proximity Read ↗

Structural Analysis of the SARS-CoV-2 Spike N-Terminal Domain Across Wild-Type and Recent Variants: A Comparative Study.Semantic proximity Read ↗

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