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

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

Journal of medical virology - 1 Aug 2000

Wang C T, Yang A H, Chiang C C

Abstract excerpt

A human immunodeficiency virus (HIV) matrix (MA) protein mutant was constructed by duplication of 107 codons of the HIV-1 MA domain. This MA protein duplication mutant (MAII) still could assemble and process particles, had a wild-type (wt) HIV particle density, and possessed reverse transcriptase activity of about 80% of the wild type virus level. The incorporation of HIV Env and viral RNA genome was not greatly...

Read the complete abstract on PubMed

Topics

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

Share to DNA Transposable Elements
Share to Genes, gag
Share to HeLa Cells

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

Share to Microscopy, Electron

Share to RNA-Directed DNA Polymerase

Share to Viral Envelope Proteins

Share to Viral Matrix Proteins

Share to Virus Assembly

Source

Identifiers

PMID: 10897059
DOI: 10.1002/1096-9071(200008)61:4<423::aid-jmv3>3.0.co;2-9

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

Analysis of a human immunodeficiency virus type 1 gag mutant with an engineered 110-amino-acid insertion in the matrix protein domain.PMID 10897059Read ↗

Conditional infectivity of a human immunodeficiency virus matrix domain deletion mutant.Semantic proximity Read ↗

The matrix protein of human immunodeficiency virus type 1 is required for incorporation of viral envelope protein into mature virionsSemantic proximity Read ↗

Characterization of human immunodeficiency virus type 1 matrix revertants: effects on virus assembly, Gag processing, and Env incorporation into virionsSemantic proximity Read ↗

Assembly and processing of human immunodeficiency virus Gag mutants containing a partial replacement of the matrix domain by the viral protease domain.Semantic proximity Read ↗

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

Identification of domains in the simian immunodeficiency virus matrix protein essential for assembly and envelope glycoprotein incorporationSemantic proximity Read ↗

Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection.Semantic proximity Read ↗

Characterization of replication defects induced by mutations in the basic domain and C-terminus of HIV-1 matrix.Semantic proximity Read ↗

Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoproteinSemantic proximity Read ↗

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

Rescue of human immunodeficiency virus type 1 matrix protein mutants by envelope glycoproteins with short cytoplasmic domains.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 ↗

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