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

Role of the conserved dipeptide Gly75 and Cys76 on HIV-1 Vpr function.

Virology - 10 Jul 1995

Mahalingam S, Collman R G, Patel M, Monken C E, Srinivasan A

Abstract excerpt

Vpr is one of the accessory proteins encoded by the HIV-1 genome. Several interesting features associated with Vpr include incorporation into virus particles, ability to oligomerize, localization in the nucleus, and positive effect on virus production and replication. In order to understand the structure-function relationship of Vpr, we have analyzed the role of the Gly75 and Cys76 (GC) residues which are highly...

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 Cell Nucleus
Share to Conserved Sequence

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

Share to Genetic Vectors

Share to HeLa Cells

Share to Mutation

Share to Viral Proteins

Source

Identifiers

PMID: 7618286
DOI: 10.1006/viro.1995.1368

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

Role of the conserved dipeptide Gly75 and Cys76 on HIV-1 Vpr function.PMID 7618286Read ↗

HIV-1 Vpr: A Closer Look at the Multifunctional Protein from the Structural PerspectiveSemantic proximity Read ↗

Identification of residues in the N-terminal acidic domain of HIV-1 Vpr essential for virion incorporation.Semantic proximity Read ↗

HIV1-viral protein R (Vpr) mutations: associated phenotypes and relevance for clinical pathologies.Semantic proximity Read ↗

Incorporation of Vpr into human immunodeficiency virus type 1 requires a direct interaction with the p6 domain of the p55 gag precursor.Semantic proximity Read ↗

Structure-functional analysis of human immunodeficiency virus type 1 (HIV-1) Vpr: role of leucine residues on Vpr-mediated transactivation and virus replication.Semantic proximity Read ↗

Human immunodeficiency virus type 1 Vpr: functions and molecular interactionsSemantic proximity Read ↗

Transdominant activity of human immunodeficiency virus type 1 Vpr with a mutation at residue R73.Semantic proximity Read ↗

The p6gag domain of human immunodeficiency virus type 1 is sufficient for the incorporation of Vpr into heterologous viral particlesSemantic proximity Read ↗

Nuclear import, virion incorporation, and cell cycle arrest/differentiation are mediated by distinct functional domains of human immunodeficiency virus type 1 VprSemantic proximity Read ↗

Functional Analysis of the Simian Immunodeficiency Virus Vpx Protein: Identification of Packaging Determinants and a Novel Nuclear Targeting DomainSemantic proximity Read ↗

Mutation of dileucine-like motifs in the human immunodeficiency virus type 1 capsid disrupts virus assembly, gag-gag interactions, gag-membrane binding, and virion maturation.Semantic proximity Read ↗

Functional analysis of HIV-1 Vpr: identification of determinants essential for subcellular localization.Semantic proximity Read ↗

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