ArticleNature communications2020
Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
39 citing papers in PubMed.
- Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026Review
- Structure and Dynamics of the HIV-1 Envelope Protein on the Virion Envelope.Journal of the American Chemical Society · 2026Article
- HIV-1 Env Heterogeneity: Cleavage, Trafficking, and Antigenic Consequences for Virions and Infected Cells.Viruses · 2026Review
- Article
- Structure and Dynamics of the HIV-1 Envelope Protein on the Virion Envelope.bioRxiv : the preprint server for biology · 2026Article
- N-Glycans modulate tilting of HIV-1 envelope glycoprotein.Nature communications · 2026Article
- Reconstructing a Missing Link of HIV-1 Assembly: HIV-1 Envelope-Matrix Interactions in a Native Viral Context.bioRxiv : the preprint server for biology · 2026Article
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Characterization of full-length and cytoplasmic tail-truncated envelope glycoproteins incorporated into human immunodeficiency virus (HIV-1) virions and virus-like particles.Journal of virology · 2025Article
- Structural Heterogeneity of the Membrane-Interacting Region of the HIV-1 Envelope Glycoprotein.Journal of the American Chemical Society · 2025Article
- The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodies.Nature reviews. Microbiology · 2025Review
- Conformational Variability of HIV-1 Env Trimer and Viral Vulnerability.bioRxiv : the preprint server for biology · 2025Article
- Impaired migration and lung invasion of human melanoma by a novel small molecule targeting the transmembrane domain of death receptor p75EMBO molecular medicine · 2025Article
- Mechanistic insight into the dynamics of Mur ligase through a comprehensive timescale-specific approach.Communications chemistry · 2025Article
- Structural Heterogeneity of the Membrane-Interacting Region of the HIV-1 Envelope Glycoprotein.bioRxiv : the preprint server for biology · 2025Article
- Plant Lectin, MoMo30, Pressures HIV-1 to Select for Variants with Deleted N-Linked Glycosylation Sites.Viruses · 2025Article
- Article
- Article
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- SIV monoclonal antibody administration spanning treatment interruption in macaques delays viral rebound and selects escape variants.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
The prefusion conformation of HIV-1 envelope protein (Env) is recognized by most broadly neutralizing antibodies (bnAbs). Studies showed that alterations of its membrane-related components, including the transmembrane domain (TMD) and cytoplasmic tail (CT), can reshape the antigenic structure of the Env ectodomain. Using nuclear magnetic resonance (NMR) spectroscopy, we determine the structure of an Env segment encompassing the TMD and a large portion of the CT in bicelles. The structure reveals that the CT folds into amphipathic helices that wrap around the C-terminal end of the TMD, thereby forming a support baseplate for the rest of Env. NMR dynamics measurements provide evidences of dynamic coupling across the TMD between the ectodomain and CT. Pseudovirus-based neutralization assays suggest that CT-TMD interaction preferentially affects antigenic structure near the apex of the Env trimer. These results explain why the CT can modulate the Env antigenic properties and may facilitate HIV-1 Env-based vaccine design.
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