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

Targeting an evolutionarily conserved “E-L-L” motif in spike protein to identify a small molecule fusion inhibitor against SARS-CoV-2

22 Oct 2022

Abstract excerpt

L" ("E-L-L") motif present within the HR2 domain of all human and nonhuman coronavirus spike (S) proteins that play a crucial role in stabilizing its postfusion six-helix bundle (6-HB) structure and thus, fusion-mediated viral entry. Mutations within this motif reduce the fusogenicity of the S protein without affecting its stability or membrane localization. We found that posaconazole, an FDA-approved drug, binds...

Read the complete abstract on PubMed

Topics

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

Share to Influenza Virus Research Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to vaccines and immunoinformatics approaches

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36712339
DOI: 10.1093/pnasnexus/pgac198

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeting an evolutionarily conserved “E-L-L” motif in spike protein to identify a small molecule fusion inhibitor against SARS-CoV-2PMID 36712339Read ↗

Targeting an evolutionarily conserved “E-L-L” motif in the spike protein to develop a small molecule fusion inhibitor against SARS-CoV-2Semantic proximity Read ↗

Research Progress on Spike-Dependent SARS-CoV-2 Fusion Inhibitors and Small Molecules Targeting the S2 Subunit of SpikeSemantic proximity Read ↗

Spike Glycoprotein Is Central to Coronavirus Pathogenesis-Parallel Between m-CoV and SARS-CoV-2Semantic 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 ↗

The "LLQY" Motif on SARS-CoV-2 Spike Protein Affects S Incorporation into Virus Particles.Semantic proximity Read ↗

Nanomolar inhibition of SARS-CoV-2 infection by an unmodified peptide targeting the pre-hairpin intermediate of the spike proteinSemantic proximity Read ↗

Spike glycoprotein and host cell determinants of SARS-CoV-2 entry and cytopathic effectsSemantic proximity Read ↗

SARS-CoV-2 spike N-terminal domain modulates TMPRSS2-dependent viral entry and fusogenicitySemantic proximity Read ↗

Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitorsSemantic proximity Read ↗

Domains and Functions of Spike Protein in Sars-Cov-2 in the Context of Vaccine Design.Semantic proximity Read ↗

SARS-CoV-2 Omicron Variant Spike Glycoprotein Mutation Q954H Enhances Fusion Core Stability.Semantic proximity Read ↗

Stabilization of the Metastable Prefusion Conformation of SARS-CoV-2 Spike Glycoprotein through N-linked Glycosylation on S2 SubunitSemantic proximity Read ↗

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