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

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

Journal of virology - 1 Jun 1995

Kräusslich H G, Fäcke M, Heuser A M, Konvalinka J, Zentgraf H

Abstract excerpt

Morphogenesis of retroviruses involves ordered assembly of the structural Gag- and Gag-Pol polyproteins, with subsequent budding from the plasma membrane and proteolytic cleavage by the viral proteinase (PR). Two cleavage sites exist between the capsid (CA) and nucleocapsid (NC) domains of the human immunodeficiency virus (HIV) type 1 Gag polyprotein which are separated by a 14-amino-acid spacer peptide of...

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

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

Share to Microscopy, Electron

Share to Molecular Sequence Data

Share to Mutation

Share to Peptide Fragments

Share to Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 7745687
DOI: 10.1128/JVI.69.6.3407-3419.1995
PMCID: PMC189053

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

The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity.PMID 7745687Read ↗

The conserved carboxy terminus of the capsid domain of human immunodeficiency virus type 1 gag protein is important for virion assembly and release.Semantic proximity Read ↗

Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity.Semantic proximity Read ↗

Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag.Semantic proximity Read ↗

Mutations in the spacer peptide and adjoining sequences in Rous sarcoma virus Gag lead to tubular budding.Semantic proximity Read ↗

Role of the C terminus Gag protein in human immunodeficiency virus type 1 virion assembly and maturation.Semantic proximity Read ↗

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

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

HIV Gag polyprotein: processing and early viral particle assemblySemantic proximity Read ↗

The choreography of HIV-1 proteolytic processing and virion assembly.Semantic proximity Read ↗

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

Phenotypic characterization of insertion mutants of the human immunodeficiency virus type 1 Gag precursor expressed in recombinant baculovirus-infected cells.Semantic 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 ↗

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