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

Effect of mutations in the V3 loop of HIV-1 gp120 on infectivity and susceptibility to proteolytic cleavage.

AIDS research and human retroviruses - 1 Feb 1993

Schulz T F, Reeves J D, Hoad J G, Tailor C, Stephens P, Clements G, Ortlepp S, Page K A, Moore J P, Weiss R A

Abstract excerpt

It has been suggested that the V3 domain of human immunodeficiency virus type 1 (HIV-1) isolates has to interact with a cell-surface-associated or endosomal proteinase during virus entry into susceptible cells. To investigate this hypothesis, we examined the effect of several mutations in the V3 loop on its susceptibility to proteolytic cleavage by thrombin and cathepsin E and compared it with the effect of these...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites

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

Share to Cell Line

Share to HIV Envelope Protein gp120

Share to Molecular Sequence Data

Share to Mutation

Share to Thrombin

Source

Identifiers

PMID: 8457383
DOI: 10.1089/aid.1993.9.159

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.

Research trail→

Click a neighbor to travelStep 1 · 9 closest

Effect of mutations in the V3 loop of HIV-1 gp120 on infectivity and susceptibility to proteolytic cleavage.PMID 8457383Read ↗

[Structural and functional relationships demonstrated by the study of V3 loop heterogeneity].Semantic proximity Read ↗

Identification of the principal neutralizing determinant of human immunodeficiency virus type 1 as a fusion domainSemantic proximity Read ↗

Structural analysis of the envelope gp120 V3 loop for some HIV-1 variants circulating in the countries of Eastern Europe.Semantic proximity Read ↗

Small amino acid changes in the V3 hypervariable region of gp120 can affect the T-cell-line and macrophage tropism of human immunodeficiency virus type 1.Semantic proximity Read ↗

Molecular determinants of the V3 loop of human immunodeficiency virus type 1 glycoprotein gp120 responsible for controlling cell tropism.Semantic proximity Read ↗

Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site.Semantic proximity Read ↗

Mutational analysis of the putative substrate-binding site of 3C proteinase of coxsackievirus B3.Semantic proximity Read ↗

In vitro inhibition of R5 HIV-1 infectivity by X4 V3-derived synthetic peptides.Semantic proximity Read ↗

Loss of a neutralizing epitope by a spontaneous point mutation in the V3 loop of HIV-1 isolated from an infected laboratory worker.Semantic proximity Read ↗

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