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

Preassembled capsids of type D retroviruses contain a signal sufficient for targeting specifically to the plasma membrane.

Journal of virology - 1 Aug 1990

Rhee S S, Hui H X, Hunter E

Abstract excerpt

The capsids of Mason-Pfizer monkey virus (M-PMV), an immunosuppressive type D retrovirus, are preassembled in the infected cell cytoplasm and are then transported to the plasma membrane, where they are enveloped in a virus glycoprotein-containing lipid bilayer. The role of viral glycoprotein in intracellular transport of M-PMV capsids was investigated with a spontaneous mutant (5A) of M-PMV, which we show here to...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Line
Share to Cloning, Molecular

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

Share to DNA, Viral

Share to Molecular Sequence Data

Share to Mutation

Share to Plasmids

Share to Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 2370682
DOI: 10.1128/JVI.64.8.3844-3852.1990
PMCID: PMC249680

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

Preassembled capsids of type D retroviruses contain a signal sufficient for targeting specifically to the plasma membrane.PMID 2370682Read ↗

A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus.Semantic proximity Read ↗

Separate assembly and transport domains within the Gag precursor of Mason-Pfizer monkey virus.Semantic proximity Read ↗

Structural role of the matrix protein of type D retroviruses in gag polyprotein stability and capsid assembly.Semantic proximity Read ↗

A Proline-Rich Motif (PPPY) in the Gag Polyprotein of Mason-Pfizer Monkey Virus Plays a Maturation-Independent Role in Virion ReleaseSemantic proximity Read ↗

Assembly and extracellular release of chimeric HIV-1 Pr55gag retrovirus-like particles.Semantic proximity Read ↗

Role of matrix protein in the type D retrovirus replication cycle: importance of the arginine residue at position 55.Semantic proximity Read ↗

A tyrosine motif in the cytoplasmic domain of mason-pfizer monkey virus is essential for the incorporation of glycoprotein into virions.Semantic proximity Read ↗

Inhibition of Virion Maturation by Simultaneous Deletion of Glycoproteins E, I, and M of Pseudorabies VirusSemantic proximity Read ↗

Mutations in the amino terminus of foamy virus Gag disrupt morphology and infectivity but do not target assembly.Semantic proximity Read ↗

The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle AssemblySemantic proximity Read ↗

Mutations within the env gene of Mason-Pfizer monkey virus: effects on protein transport and SU-TM association.Semantic proximity Read ↗

Mutations altering the gammaretrovirus endoproteolytic motif affect glycosylation of the envelope glycoprotein and early events of the virus life cycle.Semantic proximity Read ↗

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