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

Disulfide bond formation in the human immunodeficiency virus type 1 Nef protein.

Journal of virology - 1 Mar 1993

Zazopoulos E, Haseltine W A

Abstract excerpt

Substitution of alanine for cysteine residues of the human immunodeficiency virus type 1 LAI (BRU) and ELI Nef proteins was used to determine pairing of the cysteine residues present in each protein. The results show that under nonreducing conditions, alternative pairing of the cysteines occurs. The preferred pairing of cysteine residues of the LAI and ELI proteins differs. In the experimental system used,...

Read the complete abstract on PubMed

Topics

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

Share to Acquired Immunodeficiency Syndrome
Share to Alleles
Share to Cell Line

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

Share to Cysteine

Share to Mutagenesis, Site-Directed

Share to T-Lymphocytes

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 8437238
DOI: 10.1128/JVI.67.3.1676-1680.1993
PMCID: PMC237542

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 · 8 closest

Disulfide bond formation in the human immunodeficiency virus type 1 Nef protein.PMID 8437238Read ↗

Functional contribution of cysteine residues to the human immunodeficiency virus type 1 envelope.Semantic proximity Read ↗

Contribution of disulfide bonds in the carboxyl terminus of the human immunodeficiency virus type I gp120 glycoprotein to CD4 binding.Semantic proximity Read ↗

Cysteine residues in the Vif protein of human immunodeficiency virus type 1 are essential for viral infectivity.Semantic proximity Read ↗

Stabilizing exposure of conserved epitopes by structure guided insertion of disulfide bond in HIV-1 envelope glycoprotein.Semantic proximity Read ↗

High incidence of unusual cysteine variants in gp120 envelope proteins from early HIV type 1 infections from a Phase 3 vaccine efficacy trial.Semantic proximity Read ↗

Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation.Semantic proximity Read ↗

A Recombinant Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex Stabilized by an Intermolecular Disulfide Bond between the gp120 and gp41 Subunits Is an Antigenic Mimic of the Trimeric Virion-Associated StructureSemantic proximity Read ↗

A Conserved Acidic-Cluster Motif in SERINC5 Confers Partial Resistance to Antagonism by HIV-1 Nef.Semantic proximity Read ↗

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