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

Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation

1 Oct 1995

Abstract excerpt

The core of human immunodeficiency virus type 1 is derived from two precursor polyproteins, Pr55gag and Pr160gag-pol. The Gag precursor can assemble into immature virus-like particles when expressed by itself, while the Gag-Pol precursor lacks particle-forming ability. We have shown previously that the Gag precursor is able to "rescue" the Gag-Pol precursor into virus-like particles when the two polyproteins are...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophages and microbial interactions
Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment

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

Source

Identifiers

PMID: 7666514
DOI: 10.1128/jvi.69.10.6106-6114.1995

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

Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporationPMID 7666514Read ↗

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

Analysis of minimal human immunodeficiency virus type 1 gag coding sequences capable of virus-like particle assembly and release.Semantic proximity Read ↗

Efficient Particle Production by Minimal Gag Constructs Which Retain the Carboxy-Terminal Domain of Human Immunodeficiency Virus Type 1 Capsid-p2 and a Late Assembly DomainSemantic proximity Read ↗

The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity.Semantic proximity Read ↗

The nonmyristylated Pr160gag-pol polyprotein of human immunodeficiency virus type 1 interacts with Pr55gag and is incorporated into viruslike particlesSemantic proximity Read ↗

Determinants in the HTLV-1 capsid major homology region that are critical for virus particle assemblySemantic proximity Read ↗

Mutation of dileucine-like motifs in the human immunodeficiency virus type 1 capsid disrupts virus assembly, gag-gag interactions, gag-membrane binding, and virion maturation.Semantic proximity Read ↗

The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycleSemantic proximity Read ↗

Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutantsSemantic proximity Read ↗

Functional domains of the capsid protein of human immunodeficiency virus type 1Semantic proximity Read ↗

Mutations of Conserved Residues in the Major Homology Region Arrest Assembling HIV-1 Gag as a Membrane-Targeted Intermediate Containing Genomic RNA and Cellular ProteinsSemantic proximity Read ↗

Extensive regions of pol are required for efficient human immunodeficiency virus polyprotein processing and particle maturation.Semantic proximity Read ↗

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