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

Journal of virology - 1 Nov 2002

Liang Chen, Hu Jing, Russell Rodney S, Roldan Ariel, Kleiman Lawrence, Wainberg Mark A

Abstract excerpt

A 14-amino-acid spacer peptide termed SP1 that separates the capsid (CA) and nucleocapsid (NC) sequences plays an active role in the assembly of human immunodeficiency virus type 1. This activity of SP1 involves its amino-terminal residues that, together with adjacent CA residues, constitute a putative alpha-helical structure spanning Gag residues from positions 359 to 371. In this study, we have determined that...

Read the complete abstract on PubMed

Topics

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

Share to Capsid
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Gene Expression Regulation, Viral

Share to Gene Products, gag

Share to Jurkat Cells

Share to Virion

Share to Virus Assembly

Source

Open in PubMed Open full text

Identifiers

PMID: 12388733
DOI: 10.1128/jvi.76.22.11729-11737.2002
PMCID: PMC136778

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag.PMID 12388733Read ↗

Mutation of the SP1 sequence impairs both multimerization and membrane-binding activities of human immunodeficiency virus type 1 Gag.Semantic proximity Read ↗

Critical Role of the Human T-Cell Leukemia Virus Type 1 Capsid N-Terminal Domain for Gag-Gag Interactions and Virus Particle Assembly.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 spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity.Semantic 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 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 ↗

Important role for the CA-NC spacer region in the assembly of bovine immunodeficiency virus Gag protein.Semantic proximity Read ↗

Second-Site Compensatory Mutations of HIV-1 Capsid MutationsSemantic proximity Read ↗

Higher-Order Structure of the Rous Sarcoma Virus SP Assembly DomainSemantic proximity Read ↗

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

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

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