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

Biochemical evidence of a role for matrix trimerization in HIV-1 envelope glycoprotein incorporation.

Proceedings of the National Academy of Sciences of the United States of America - 12 Jan 2016

Tedbury Philip R, Novikova Mariia, Ablan Sherimay D, Freed Eric O

Abstract excerpt

The matrix (MA) domain of HIV Gag has important functions in directing the trafficking of Gag to sites of assembly and mediating the incorporation of the envelope glycoprotein (Env) into assembling particles. HIV-1 MA has been shown to form trimers in vitro; however, neither the presence nor the role of MA trimers has been documented in HIV-1 virions. We developed a cross-linking strategy to reveal MA trimers in...

Read the complete abstract on PubMed

Topics

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

Share to Cross-Linking Reagents
Share to Disulfides

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

Share to env Gene Products, Human Immunodeficiency Virus

Share to gag Gene Products, Human Immunodeficiency Virus

Share to Protein Multimerization

Share to Threonine

Share to Viral Matrix Proteins

Share to Virion

Source

Open in PubMed Open full text

Identifiers

PMID: 26711999
DOI: 10.1073/pnas.1516618113
PMCID: PMC4720328

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

Biochemical evidence of a role for matrix trimerization in HIV-1 envelope glycoprotein incorporation.PMID 26711999Read ↗

HIV-1 Matrix Trimerization-Impaired Mutants Are Rescued by Matrix Substitutions That Enhance Envelope Glycoprotein Incorporation.Semantic proximity Read ↗

Global rescue of defects in HIV-1 envelope glycoprotein incorporation: implications for matrix structure.Semantic proximity Read ↗

Structural characterization of HIV-1 matrix mutants implicated in envelope incorporation.Semantic proximity Read ↗

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

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

Trimer Enhancement Mutation Effects on HIV-1 Matrix Protein Binding Activities.Semantic proximity Read ↗

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

The role of matrix in HIV-1 envelope glycoprotein incorporationSemantic proximity Read ↗

Mutations in the matrix protein of human immunodeficiency virus type 1 inhibit surface expression and virion incorporation of viral envelope glycoproteins in CD4+ T lymphocytes.Semantic proximity Read ↗

Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of gag membrane targeting.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 ↗

Second site reversion of HIV-1 envelope protein baseplate mutations maps to the matrix protein.Semantic proximity Read ↗

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