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

Defective assembly and intracellular transport of mutant paramyxovirus hemagglutinin-neuraminidase proteins containing altered cytoplasmic domains.

Journal of virology - 1 Aug 1990

Parks G D, Lamb R A

Abstract excerpt

The hemagglutinin-neuraminidase (HN) integral membrane protein of paramyxoviruses is expressed at the cell surface as a tetramer consisting of a pair of disulfide-linked dimers. HN has a large C-terminal ectodomain, a 19-residue uncleaved signal-anchor domain, and a 17-residue N-terminal cytoplasmic tail. Various mutant HN genes were constructed to examine the role of residues flanking the signal-anchor domain,...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cell Line
Share to Fluorescent Antibody Technique

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

Share to Genes, Viral

Share to Molecular Sequence Data

Share to Mutation

Share to Oligonucleotide Probes

Share to Plasmids

Source

Open in PubMed Open full text

Identifiers

PMID: 2164588
DOI: 10.1128/JVI.64.8.3605-3616.1990
PMCID: PMC249653

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

Defective assembly and intracellular transport of mutant paramyxovirus hemagglutinin-neuraminidase proteins containing altered cytoplasmic domains.PMID 2164588Read ↗

Intracellular processing and transport of NH2-terminally truncated forms of a hemagglutinin-neuraminidase type II glycoprotein.Semantic proximity Read ↗

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

Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5.Semantic proximity Read ↗

The role of the individual cysteine residues in the formation of the mature, antigenic HN protein of Newcastle disease virus.Semantic proximity Read ↗

Down-regulation of paramyxovirus hemagglutinin-neuraminidase glycoprotein surface expression by a mutant fusion protein containing a retention signal for the endoplasmic reticulum.Semantic proximity Read ↗

Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum.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 ↗

Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk.Semantic proximity Read ↗

Intracellular processing of the human respiratory syncytial virus fusion glycoprotein: amino acid substitutions affecting folding, transport and cleavage.Semantic proximity Read ↗

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

Nuclear localized Influenza nucleoprotein N-terminal deletion mutant is deficient in functional vRNP formation.Semantic proximity Read ↗

An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replicationSemantic proximity Read ↗

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