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

Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling.

Journal of virology - 1 May 2007

Aguilar Hector C, Matreyek Kenneth A, Choi Daniel Y, Filone Claire Marie, Young Sophia, Lee Benhur

Abstract excerpt

The cytoplasmic tails of the envelope proteins from multiple viruses are known to contain determinants that affect their fusogenic capacities. Here we report that specific residues in the cytoplasmic tail of the Nipah virus fusion protein (NiV-F) modulate its fusogenic activity. Truncation of the cytoplasmic tail of NiV-F greatly inhibited cell-cell fusion. Deletion and alanine scan analysis identified a tribasic...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Antibodies, Monoclonal

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

Share to Blotting, Western

Share to Chlorocebus aethiops

Share to Immunoprecipitation

Share to Membrane Fusion

Share to Vero Cells

Share to Viral Fusion Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 17301148
DOI: 10.1128/JVI.02205-06
PMCID: PMC1900187

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

Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling.PMID 17301148Read ↗

A Quantitative and Kinetic Fusion Protein-Triggering Assay Can Discern Distinct Steps in the Nipah Virus Membrane Fusion CascadeSemantic proximity Read ↗

Endocytosis of the Nipah virus glycoproteins.Semantic proximity Read ↗

Differential Features of Fusion Activation within the ParamyxoviridaeSemantic proximity Read ↗

Relevance of potential endocytosis motifs in Cedar virus glycoprotein G for its biological activity.Semantic proximity Read ↗

N-Glycans on the Nipah virus attachment glycoprotein modulate fusion and viral entry as they protect against antibody neutralization.Semantic proximity Read ↗

The paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Semantic proximity Read ↗

Structural Insight into Paramyxovirus and Pneumovirus Entry InhibitionSemantic proximity Read ↗

Evolution of antiviral resistance captures a transient interdomain functional interaction between chikungunya virus envelope glycoproteins.Semantic proximity Read ↗

Viral Membrane Fusion: A Dance Between Proteins and LipidsSemantic proximity Read ↗

Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanismSemantic proximity Read ↗

A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F).Semantic proximity Read ↗

Mutations in the Cytoplasmic Domain of the Newcastle Disease Virus Fusion Protein Confer Hyperfusogenic Phenotypes Modulating Viral Replication and PathogenicitySemantic proximity Read ↗

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