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

Residues in the membrane-spanning domain core modulate conformation and fusogenicity of the HIV-1 envelope glycoprotein.

Virology - 1 Sept 2010

Shang Liang, Hunter Eric

Abstract excerpt

The membrane-spanning domain (MSD) of human immunodeficiency virus type I (HIV-1) envelope glycoprotein (Env) is critical for its biological activity. Initial studies have defined an almost invariant "core" structure in the MSD and demonstrated that it is crucial for anchoring Env in the membrane and virus entry. We show here that amino acid substitutions in the MSD "core" do not influence specific virus-cell...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to env Gene Products, Human Immunodeficiency Virus
Share to HIV-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Proteins

Share to Protein Conformation

Share to Protein Structure, Tertiary

Share to Saccharomyces cerevisiae Proteins

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 20605619
DOI: 10.1016/j.virol.2010.03.016
PMCID: PMC2902644

Genes

CXCR4

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

Residues in the membrane-spanning domain core modulate conformation and fusogenicity of the HIV-1 envelope glycoprotein.PMID 20605619Read ↗

Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection.Semantic proximity Read ↗

Truncation of the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Defines Elements Required for Fusion, Incorporation, and InfectivitySemantic proximity Read ↗

Subdomain Folding and Biological Activity of the Core Structure from Human Immunodeficiency Virus Type 1 gp41: Implications for Viral Membrane FusionSemantic proximity Read ↗

HIV-1 Entry and Membrane Fusion InhibitorsSemantic proximity Read ↗

Cholesterol-Dependent Membrane Fusion Induced by the gp41 Membrane-Proximal External Region–Transmembrane Domain Connection Suggests a Mechanism for Broad HIV-1 NeutralizationSemantic proximity Read ↗

C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmaticSemantic proximity Read ↗

HIV-1 Envelope Conformation, Allostery, and DynamicsSemantic proximity Read ↗

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

The Conformational States of the HIV-1 Envelope GlycoproteinsSemantic proximity Read ↗

Inhibition of Human Immunodeficiency Virus Type 1 Infectivity by the gp41 Core: Role of a Conserved Hydrophobic Cavity in Membrane FusionSemantic proximity Read ↗

Global Increases in Human Immunodeficiency Virus Neutralization Sensitivity Due to Alterations in the Membrane-Proximal External Region of the Envelope Glycoprotein Can be Minimized by Distant State 1-Stabilizing ChangesSemantic proximity Read ↗

A V3 Loop-Dependent gp120 Element Disrupted by CD4 Binding Stabilizes the Human Immunodeficiency Virus Envelope Glycoprotein TrimerSemantic proximity Read ↗

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