ArticleJournal of the American Chemical Society2018
Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 Membrane-Proximal External Region and Transmembrane Domain in Phospholipid Bilayers.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 68 citations in OpenAlex.
- Structure and Dynamics of the HIV-1 Envelope Protein on the Virion Envelope.Journal of the American Chemical Society · 2026Article
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- Structure and Dynamics of the HIV-1 Envelope Protein on the Virion Envelope.bioRxiv : the preprint server for biology · 2026Article
- Lipid Acyl Chain-Driven α-Synuclein Fibril Polymorphisms and Neuronal Pathologies.ACS chemical neuroscience · 2026Article
- Carbon-13 Centerband-Only Detection of EXchange with Dynamic Nuclear Polarization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structural Heterogeneity of the Membrane-Interacting Region of the HIV-1 Envelope Glycoprotein.Journal of the American Chemical Society · 2025Article
- Conformational Variability of HIV-1 Env Trimer and Viral Vulnerability.bioRxiv : the preprint server for biology · 2025Article
- Structural Heterogeneity of the Membrane-Interacting Region of the HIV-1 Envelope Glycoprotein.bioRxiv : the preprint server for biology · 2025Article
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- The membrane-proximal external region of human immunodeficiency virus (HIV-1) envelope glycoprotein trimers in A18-lipid nanodiscs.Communications biology · 2025Article
- Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infection.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Viral Membrane Fusion: A Dance Between Proteins and Lipids.Annual review of virology · 2023Review
- Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing.International journal of molecular sciences · 2023Review
- Article
- Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope.Communications biology · 2022Article
- SARS-CoV-2 Envelope Protein Forms Clustered Pentamers in Lipid Bilayers.Biochemistry · 2022Article
- Dynamic HIV-1 spike motion creates vulnerability for its membrane-bound tripod to antibody attack.Nature communications · 2022Article
- Functional Delineation of a Protein-Membrane Interaction Hotspot Site on the HIV-1 Neutralizing Antibody 10E8.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The HIV-1 glycoprotein, gp41, mediates fusion of the virus lipid envelope with the target cell membrane during virus entry into cells. Despite extensive studies of this protein, inconsistent and contradictory structural information abounds in the literature about the C-terminal membrane-interacting region of gp41. This C-terminal region contains the membrane-proximal external region (MPER), which harbors the epitopes for four broadly neutralizing antibodies, and the transmembrane domain (TMD), which anchors the protein to the virus lipid envelope. Due to the difficulty of crystallizing and solubilizing the MPER-TMD, most structural studies of this functionally important domain were carried out using truncated peptides either in the absence of membrane-mimetic solvents or bound to detergents and lipid bicelles. To determine the structural architecture of the MPER-TMD in the native environment of lipid membranes, we have now carried out a solid-state NMR study of the full MPER-TMD segment bound to cholesterol-containing phospholipid bilayers.
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