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

NMR Model of the Entire Membrane-Interacting Region of the HIV-1 Fusion Protein and Its Perturbation of Membrane Morphology

22 Apr 2021

Abstract excerpt

HIV-1 envelope glycoprotein (Env) is a transmembrane protein that mediates membrane fusion and viral entry. The membrane-interacting regions of the Env, including the membrane-proximal external region (MPER), the transmembrane domain (TMD), and the cytoplasmic tail (CT), not only are essential for fusion and Env incorporation but also can strongly influence the antigenicity of the Env. Previous studies have...

Read the complete abstract on PubMed

Topics

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

Share to HIV Research and Treatment
Share to Lipid Membrane Structure and Behavior
Share to Mosquito-borne diseases and control

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33882664
DOI: 10.1021/jacs.1c01762

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

NMR Model of the Entire Membrane-Interacting Region of the HIV-1 Fusion Protein and Its Perturbation of Membrane MorphologyPMID 33882664Read ↗

Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41.Semantic 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 ↗

Structural basis for membrane anchoring of HIV-1 envelope spike.Semantic proximity Read ↗

HIV-1 Envelope Conformation, Allostery, and DynamicsSemantic 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 ↗

Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements.Semantic proximity Read ↗

Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.Semantic proximity Read ↗

HIV-1 Env trimers asymmetrically engage CD4 receptors in membranesSemantic 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 ↗

Functional and Structural Characterization of HIV-1 gp41 Ectodomain Regions in Phospholipid Membranes Suggests that the Fusion-active Conformation Is ExtendedSemantic proximity Read ↗

N-Glycans Modulate HIV-1 Env Conformational PlasticitySemantic proximity Read ↗

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

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