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

Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions.

Journal of virology - 1 Aug 1993

Wyatt R, Sullivan N, Thali M, Repke H, Ho D, Robinson J, Posner M, Sodroski J

Abstract excerpt

Deletions of the major variable regions (V1/V2, V3, and V4) of the human immunodeficiency virus type 1 (HIV-1) gp120 exterior envelope glycoprotein were created to study the role of these regions in function and antigenicity. Deletion of the V4 region disrupted processing of the envelope glycopro...

Topics

Animals
CD4 Antigens
Cell Line
Cloning, Molecular
Genes, env
Genetic Variation
HIV Envelope Protein gp120
HIV Envelope Protein gp41
HIV-1
Kinetics
Mutagenesis, Site-Directed
Neutralization Tests

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Sequence Deletion

Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 8331723
DOI: 10.1128/JVI.67.8.4557-4565.1993
PMCID: PMC237840

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8331723-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions.PMID 8331723Read ↗

Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response.Semantic proximity Read ↗

HIV-1 Envelope Glycoprotein Variable Loops Are Indispensable for Envelope Structural Integrity and Virus EntrySemantic proximity Read ↗

Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoproteinSemantic proximity Read ↗

Inhibition of human immunodeficiency virus (HIV-1) infectivity by expression of poorly or broadly neutralizing antibodies against Env in virus-producing cellsSemantic proximity Read ↗

Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding.Semantic proximity Read ↗

Removal of N-linked glycosylation sites in the V1 region of simian immunodeficiency virus gp120 results in redirection of B-cell responses to V3.Semantic proximity Read ↗

Optimization of human immunodeficiency virus type 1 envelope glycoproteins with V1/V2 deleted, using virus evolution.Semantic proximity Read ↗

Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion eventsSemantic proximity Read ↗

The HIV-1 Envelope Glycoproteins: Fusogens, Antigens, and ImmunogensSemantic proximity Read ↗

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

Effect of Major Deletions in the V1 and V2 Loops of a Macrophage-Tropic HIV Type 1 Isolate on Viral Envelope Structure, Cell Entry, and ReplicationSemantic proximity Read ↗

The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodiesSemantic proximity Read ↗

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