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, reliable, and reproducible cell fusion assay to quantify SARS-Cov-2 spike interaction with hACE2

24 Jun 2021

Abstract excerpt

COVID-19 is a global crisis of unimagined dimensions. Currently, Remedesivir is only fully licensed FDA therapeutic. A major target of the vaccine effort is the SARS-CoV-2 spike-hACE2 interaction, and assessment of efficacy relies on time consuming neutralization assay. Here, we developed a cell fusion assay based upon spike-hACE2 interaction. The system was tested by transient co-transfection of 293T cells,...

Read the complete abstract on PubMed

Topics

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

Share to COVID-19 Clinical Research Studies
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: 34166473
DOI: 10.1371/journal.ppat.1009683

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

Rapid, reliable, and reproducible cell fusion assay to quantify SARS-Cov-2 spike interaction with hACE2PMID 34166473Read ↗

A pseudovirus-based method to dynamically mimic SARS-CoV-2-associated cell-to-cell fusion and transmissionSemantic proximity Read ↗

SARS-CoV-2 Alpha, Beta, and Delta variants display enhanced Spike-mediated syncytia formation.Semantic proximity Read ↗

Deletion of ER-retention Motif on SARS-CoV-2 Spike Protein Reduces Cell Hybrid During Cell-cell FusionSemantic proximity Read ↗

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

SARS-CoV-2 Requires Cholesterol for Viral Entry and Pathological Syncytia FormationSemantic proximity Read ↗

Human Immunodeficiency Viruses Pseudotyped with SARS-CoV-2 Spike Proteins Infect a Broad Spectrum of Human Cell Lines through Multiple Entry MechanismsSemantic proximity Read ↗

Optimized pseudotyping conditions for the SARS-COV2 Spike glycoproteinSemantic proximity Read ↗

Pseudotyped virus infection of multiplexed ACE2 libraries reveals SARS-CoV-2 variant shifts in receptor usage.Semantic proximity Read ↗

SARS CoV-2 nucleoprotein enhances the infectivity of lentiviral spike particlesSemantic proximity Read ↗

Spike protein mediated membrane fusion during SARS‐CoV‐2 infectionSemantic proximity Read ↗

Pseudotyped virus infection of multiplexed ACE2 libraries reveals SARS-CoV-2 variant shifts in receptor usageSemantic proximity Read ↗

Inhibition of SARS-CoV-2 infection (previously 2019-nCoV) by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusionSemantic proximity Read ↗

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