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

Mutation-directed chemical cross-linking of human immunodeficiency virus type 1 gp41 oligomers.

Journal of virology - 1 Feb 1998

McInerney T L, El Ahmar W, Kemp B E, Poumbourios P

Abstract excerpt

The human immunodeficiency virus type 1 transmembrane protein gp41 oligomer anchors the attachment protein, gp120, to the viral envelope and mediates viral envelope-cell membrane fusion following gp120-CD4 receptor-chemokine coreceptor binding. We have used mutation-directed chemical cross-linking with bis(sulfosuccinimidyl)suberate (BS3) to investigate the architecture of the gp41 oligomer. Treatment of gp41...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Cross-Linking Reagents
Share to HIV-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Envelope Protein gp120

Share to HIV Envelope Protein gp41

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 9445056
DOI: 10.1128/JVI.72.2.1523-1533.1998
PMCID: PMC124634

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation-directed chemical cross-linking of human immunodeficiency virus type 1 gp41 oligomers.PMID 9445056Read ↗

Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope proteinSemantic proximity Read ↗

Functional analysis of the disulfide-bonded loop/chain reversal region of human immunodeficiency virus type 1 gp41 reveals a critical role in gp120-gp41 association.Semantic proximity Read ↗

Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein.Semantic proximity Read ↗

The Human Immunodeficiency Virus Type 1 gp120 V2 Domain Mediates gp41-Independent Intersubunit ContactsSemantic proximity Read ↗

The fusion activity of HIV-1 gp41 depends on interhelical interactions.Semantic proximity Read ↗

Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41.Semantic proximity Read ↗

Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein.Semantic proximity Read ↗

Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex.Semantic proximity Read ↗

Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state.Semantic proximity Read ↗

Interhelical Interactions in the gp41 Core: Implications for Activation of HIV-1 Membrane Fusion<sup>,</sup>Semantic proximity Read ↗

Variable-loop-deleted variants of the human immunodeficiency virus type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits.Semantic proximity Read ↗

Oligomeric and Conformational Properties of a Proteolytically Mature, Disulfide-Stabilized Human Immunodeficiency Virus Type 1 gp140 Envelope GlycoproteinSemantic proximity Read ↗

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