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

Rapid characterization of spike variants via mammalian cell surface display

1 Dec 2021

Abstract excerpt

The SARS-CoV-2 spike protein is a critical component of vaccines and a target for neutralizing monoclonal antibodies (nAbs). Spike is also undergoing immunogenic selection with variants that increase infectivity and partially escape convalescent plasma. Here, we describe Spike Display, a high-throughput platform to rapidly characterize glycosylated spike ectodomains across multiple coronavirus-family proteins. We...

Read the complete abstract on PubMed

Topics

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

Share to CRISPR and Genetic Engineering
Share to Monoclonal and Polyclonal Antibodies Research
Share to SARS-CoV-2 and COVID-19 Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34919820
DOI: 10.1016/j.molcel.2021.11.024

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

Rapid characterization of spike variants via mammalian cell surface displayPMID 34919820Read ↗

Rapid characterization of spike variants via mammalian cell surface displaySemantic proximity Read ↗

Neutralization potency of monoclonal antibodies recognizing dominant and subdominant epitopes on SARS-CoV-2 Spike is impacted by the B.1.1.7 variant.Semantic proximity Read ↗

A High-Resolution Approach to Mapping Spike Protein Evolution for Advancing Antibody Therapy DesignSemantic proximity Read ↗

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

Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 ReceptorSemantic proximity Read ↗

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

ACE2-binding exposes the SARS-CoV-2 fusion peptide to broadly neutralizing coronavirus antibodiesSemantic proximity Read ↗

Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human Ace2 ReceptorSemantic proximity Read ↗

Insertion in the N-Terminal Domain of the SARS-CoV-2 Spike Glycoprotein Affects Antibody Recognition and Phenotypic Properties.Semantic proximity Read ↗

Spike Proteins of SARS –CoV-2: a detailed perspective on structure, receptor binding, antigenicity, vaccine development and neutralizationSemantic proximity Read ↗

Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants.Semantic proximity Read ↗

Deep mutational scanning of whole SARS-CoV-2 spike in an inverted infection systemSemantic proximity Read ↗

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