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

Human immunodeficiency virus type 1 virion density is not determined by nucleocapsid basic residues.

Journal of virology - 1 Aug 2000

Cimarelli A, Luban J

Abstract excerpt

The human immunodeficiency virus type 1 (HIV-1) Gag polyprotein is sufficient for assembly and release of virion-like particles from the plasma membrane. To promote assembly, the Gag polyprotein must polymerize to form a shell that lines the inner membrane of nascent virions. Several techniques have been used to functionally map the domain required for Gag polymerization (the I domain). Among these methods,...

Read the complete abstract on PubMed

Topics

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

Share to Gene Products, gag
Share to HeLa Cells
Share to HIV-1

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

Share to Jurkat Cells

Share to Nucleocapsid Proteins

Share to Virion

Share to Virus Assembly

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 10888611
DOI: 10.1128/jvi.74.15.6734-6740.2000
PMCID: PMC112189

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

Human immunodeficiency virus type 1 virion density is not determined by nucleocapsid basic residues.PMID 10888611Read ↗

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 ↗

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

Analysis of a human immunodeficiency virus type 1 gag mutant with an engineered 110-amino-acid insertion in the matrix protein domain.Semantic proximity Read ↗

Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptase.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 ↗

Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA.Semantic proximity Read ↗

RNA incorporation is critical for retroviral particle integrity after cell membrane assembly of Gag complexes.Semantic proximity Read ↗

Human Immunodeficiency Virus Type 1 Gag Polyprotein Multimerization Requires the Nucleocapsid Domain and RNA and Is Promoted by the Capsid-Dimer Interface and the Basic Region of Matrix ProteinSemantic proximity Read ↗

Gag-Gag Interactions Are Insufficient to Fully Stabilize and Order the Immature HIV Gag Lattice.Semantic proximity Read ↗

Mutations in the alpha-helix directly C-terminal to the major homology region of human immunodeficiency virus type 1 capsid protein disrupt Gag multimerization and markedly impair virus particle production.Semantic proximity Read ↗

The impact of mutations affecting highly conserved amino acids in the simian immunodeficiency virus nucleocapsid protein on virion assembly, genomic RNA packaging and viral infectivity.Semantic proximity Read ↗

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