ArticleJournal of the American Chemical Society2017
Stability and Water Accessibility of the Trimeric Membrane Anchors of the HIV-1 Envelope Spikes.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
9 citing papers in PubMed, 29 citations in OpenAlex.
- Rab11-FIP1C Is Dispensable for HIV-1 Replication in Primary CD4Journal of virology · 2022Article
- Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes fromBiochimica et biophysica acta. Biomembranes · 2021Article
- Structure, membrane topology and influence of cholesterol of the membrane proximal region: transmembrane helical anchor sequence of gp41 from HIV.Scientific reports · 2020Article
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein.Nature communications · 2020Article
- Targeting trimeric transmembrane domain 5 of oncogenic latent membrane protein 1 using a computationally designed peptide.Chemical science · 2019Article
- Article
- RAACBook: a web server of reduced amino acid alphabet for sequence-dependent inference by using Chou's five-step rule.Database : the journal of biological databases and curation · 2019Article
- HIV-1 Env gp41 Transmembrane Domain Dynamics Are Modulated by Lipid, Water, and Ion Interactions.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
HIV-1 envelope spike (Env) is a type I membrane protein that mediates viral entry. Recent studies showed that its transmembrane domain (TMD) forms a trimer in lipid bilayer whose structure has several peculiar features that remain difficult to explain. One is the presence of an arginine R696 in the middle of the TM helix. Additionally, the N- and C-terminal halves of the TM helix form trimeric cores of opposite nature (hydrophobic and hydrophilic, respectively). Here we determined the membrane partition and solvent accessibility of the TMD in bicelles that mimic a lipid bilayer. Solvent paramagnetic relaxation enhancement analysis showed that the R696 is indeed positioned close to the center of the bilayer, but, surprisingly, can exchange rapidly with water as indicated by hydrogen-deuterium exchange measurements. The solvent accessibility of R696 is likely mediated by the hydrophilic core, which also showed fast water exchange. In contrast, the N-terminal hydrophobic core showed extremely slow solvent exchange, suggesting the trimer formed by this region is extraordinarily stable. Our data explain how R696 is accommodated in the middle of the membrane while reporting the overall stability of the Env TMD trimer in lipid bilayer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.