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

Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62.

Journal of virology - 1 Mar 1990

Lobigs M, Garoff H

Abstract excerpt

The precursor protein p62 of the prototype alphavirus Semliki Forest virus (SFV) undergoes during transport to the cell surface a proteolytic cleavage to form the mature envelope glycoprotein E2. To investigate the biological significance of this cleavage event, single amino acid substitutions were introduced at the cleavages site through mutagenesis of cDNA corresponding to the structural region of the SFV...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Line
Share to Kinetics

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

Share to Molecular Sequence Data

Share to Mutation

Share to Oligonucleotide Probes

Share to Plasmids

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 2304141
DOI: 10.1128/JVI.64.3.1233-1240.1990
PMCID: PMC249238

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62.PMID 2304141Read ↗

Processing of the p62 envelope precursor protein of Semliki Forest virus.Semantic proximity Read ↗

Spike protein oligomerization control of Semliki Forest virus fusion.Semantic proximity Read ↗

An interaction site of the envelope proteins of Semliki Forest virus that is preserved after proteolytic activation.Semantic proximity Read ↗

The dynamic envelope of a fusion class II virus. E3 domain of glycoprotein E2 precursor in Semliki Forest virus provides a unique contact with the fusion protein E1.Semantic proximity Read ↗

Mutations that promote furin-independent growth of Semliki Forest virus affect p62-E1 interactions and membrane fusion.Semantic proximity Read ↗

The nucleocapsid-binding spike subunit E2 of Semliki Forest virus requires complex formation with the E1 subunit for activity.Semantic proximity Read ↗

Cholesterol is required in the exit pathway of Semliki Forest virus.Semantic proximity Read ↗

Effect of mutations in the SARS-CoV-2 spike protein on protein stability, cleavage, and cell-cell fusion functionSemantic proximity Read ↗

Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein.Semantic proximity Read ↗

Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.Semantic proximity Read ↗

fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunit.Semantic proximity Read ↗

Differential roles of two conserved glycine residues in the fusion peptide of Semliki Forest virus.Semantic proximity Read ↗

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