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

Direct evidence that the N-terminal heptad repeat of Sendai virus fusion protein participates in membrane fusion.

Journal of molecular biology - 24 Sept 1999

Ghosh J K, Shai Y

Abstract excerpt

Recent studies have demonstrated the importance of heptad repeat regions within envelope proteins of viruses in mediating conformational changes at various stages of viral infection. However, it is not clear if heptad repeats have a direct role in the actual fusion event. Here we have synthesized, fluorescently labeled and functionally and structurally characterized a wild-type 70 residue peptide (SV-117)...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Endopeptidase K
Share to Erythrocytes

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

Share to Hemolysis

Share to Liposomes

Share to Membrane Fusion

Share to Spectroscopy, Fourier Transform Infrared

Share to Viral Fusion Proteins

Source

Identifiers

PMID: 10497019
DOI: 10.1006/jmbi.1999.3097

Genes

ATR

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

Direct evidence that the N-terminal heptad repeat of Sendai virus fusion protein participates in membrane fusion.PMID 10497019Read ↗

Structure-function study of a heptad repeat positioned near the transmembrane domain of Sendai virus fusion protein which blocks virus-cell fusion.Semantic proximity Read ↗

Mutations in the fusion peptide and adjacent heptad repeat inhibit folding or activity of the Newcastle disease virus fusion protein.Semantic proximity Read ↗

Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.Semantic proximity Read ↗

Dual Mutation Events in the Haemagglutinin-Esterase and Fusion Protein from an Infectious Salmon Anaemia Virus HPR0 Genotype Promote Viral Fusion and Activation by an Ubiquitous Host Protease.Semantic proximity Read ↗

Mutations in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusionSemantic proximity Read ↗

Two mutations in the HR2 region of Newcastle disease virus fusion protein with a cleavage motif "RRQRRL" are critical for fusogenic activity.Semantic proximity Read ↗

Mutations in the NDV fusion protein HR4 region decreased fusogenic activity due to failed protein expression.Semantic proximity Read ↗

Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement.Semantic proximity Read ↗

Mutations in the Leucine Zipper-Like Motif of the Human Parainfluenza Virus 3 Fusion Protein Impair Fusion Activity.Semantic proximity Read ↗

A discrete stage of baculovirus GP64-mediated membrane fusion.Semantic proximity Read ↗

A recombinant vesicular stomatitis virus bearing a lethal mutation in the glycoprotein gene uncovers a second site suppressor that restores fusion.Semantic proximity Read ↗

Hyperfusogenic Mutations Destabilize the Postfusion Six-Helix Bundle of the Measles Virus Fusion Glycoprotein.Semantic proximity Read ↗

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