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

Discrete domains within the rotavirus VP5* direct peripheral membrane association and membrane permeability.

Journal of virology - 1 Feb 2004

Golantsova Nina E, Gorbunova Elena E, Mackow Erich R

Abstract excerpt

Cleavage of the rotavirus spike protein, VP4, is required for rotavirus-induced membrane permeability and viral entry into cells. The VP5* cleavage product selectively permeabilizes membranes and liposomes and contains an internal hydrophobic domain that is required for membrane permeability. Here we investigate VP5* domains (residues 248 to 474) that direct membrane binding. We determined that expressed VP5...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane Permeability
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COS Cells

Share to Gene Expression Regulation, Viral

Share to Hydrophobic and Hydrophilic Interactions

Share to Membrane Fusion

Share to Rotavirus

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 14747568
DOI: 10.1128/jvi.78.4.2037-2044.2004
PMCID: PMC369428

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Discrete domains within the rotavirus VP5* direct peripheral membrane association and membrane permeability.PMID 14747568Read ↗

Effect of mutations in VP5 hydrophobic loops on rotavirus cell entry.Semantic proximity Read ↗

Mutations in the rotavirus spike protein VP4 reduce trypsin sensitivity but not viral spread.Semantic proximity Read ↗

Genome delivery and ion channel properties are altered in VP4 mutants of poliovirus.Semantic proximity Read ↗

Structural and functional properties of an unusual internal fusion peptide in a nonenveloped virus membrane fusion protein.Semantic proximity Read ↗

Infectious Bursal Disease Virus VP5 Polypeptide: A Phosphoinositide-Binding Protein Required for Efficient Cell-to-Cell Virus DisseminationSemantic proximity Read ↗

The viroporin activity of the minor structural proteins VP2 and VP3 is required for SV40 propagation.Semantic proximity Read ↗

Functional Genetic and Biophysical Analyses of Membrane Disruption by Human AdenovirusSemantic proximity Read ↗

A single polar residue and distinct membrane topologies impact the function of the infectious bronchitis coronavirus E protein.Semantic proximity Read ↗

Functional refolding of the penetration protein on a non-enveloped virus.Semantic proximity Read ↗

Charged residues are involved in membrane fusion mediated by a hydrophilic peptide located in vesicular stomatitis virus G protein.Semantic proximity Read ↗

Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation.Semantic proximity Read ↗

In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein.Semantic proximity Read ↗

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