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

Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association.

Journal of virology - 1 Jul 2000

Barman S, Nayak D P

Abstract excerpt

Influenza virus neuraminidase (NA), a type II transmembrane protein, is directly transported to the apical plasma membrane in polarized MDCK cells. Previously, it was shown that the transmembrane domain (TMD) of NA provides a determinant(s) for apical sorting and raft association (A. Kundu, R. T. Avalos, C. M. Sanderson, and D. P. Nayak, J. Virol. 70:6508-6515, 1996). In this report, we have analyzed the...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Biological Transport
Share to Dogs

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

Share to Membrane Glycoproteins

Share to Neuraminidase

Share to Orthomyxoviridae

Share to Protein Structure, Tertiary

Share to Recombinant Fusion Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 10864667
DOI: 10.1128/jvi.74.14.6538-6545.2000
PMCID: PMC112163

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

Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association.PMID 10864667Read ↗

Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL.Semantic proximity Read ↗

Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi.Semantic proximity Read ↗

An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells.Semantic proximity Read ↗

A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin.Semantic proximity Read ↗

Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Semantic proximity Read ↗

The transmembrane domain of the respiratory syncytial virus F protein is an orientation-independent apical plasma membrane sorting sequence.Semantic proximity Read ↗

Apical budding of a recombinant influenza A virus expressing a hemagglutinin protein with a basolateral localization signal.Semantic proximity Read ↗

A cholesterol consensus motif is required for efficient intracellular transport and raft association of a group 2 HA from influenza virus.Semantic proximity Read ↗

Charged residues in the C-terminus of the P2Y1 receptor constitute a basolateral-sorting signal.Semantic proximity Read ↗

Apical targeting of syntaxin 3 is essential for epithelial cell polarity.Semantic proximity Read ↗

Aberrant membrane insertion of a cytoplasmic tail deletion mutant of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.Semantic proximity Read ↗

Differential detergent resistance of the apical and basolateral NPPases: relationship with polarized targeting.Semantic proximity Read ↗

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