ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structure and activity of lipid bilayer within a membrane-protein transporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
What it found
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Who cites it
90 citing papers in PubMed, 158 citations in OpenAlex.
- Connexin 26 in Hearing Health and Disease: StructuralFoundations, Mutation Mechanisms, and Therapeutic Perspectives.International journal of molecular sciences · 2026Review
- The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026Review
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- Lipids regulate epidermal growth factor receptor activation by its ligands.Biochemical Society transactions · 2026Review
- Molecular basis for multidrug efflux by an anaerobic-associated RND transporter.Nature communications · 2025Article
- Cell membrane biomimetic nanoplatforms: a new strategy for immune escape and precision targeted therapy.Materials today. Bio · 2025Review
- Active regulation of the epidermal growth factor receptor by the membrane bilayer.bioRxiv : the preprint server for biology · 2025Article
- Advances in native cell membrane nanoparticles system.Current opinion in structural biology · 2025Review
- Structural and functional analysis of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Capturing the native structure of membrane proteins using vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides.Nature communications · 2025Article
- Cholesterol-dependent enzyme activity of human TSPO1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Metallic nanoparticles: a promising novel therapeutic tool against antimicrobial resistance and spread of superbugs.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025Review
- A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs.Nature methods · 2025Article
- Functional analysis of Candida albicans Cdr1 through homologous and heterologous expression studies.FEMS yeast research · 2025Review
- Tunable Terpolymer Series for the Systematic Investigation of Membrane Proteins.Biomacromolecules · 2025Article
- Review
- Fasting the mitochondria to prevent neurodegeneration: the role of ceramides.Frontiers in neuroscience · 2025Review
- On the Properties of Styrene-Maleic Acid Copolymer-Lipid Nanoparticles: A Solution NMR Perspective.Polymers · 2024Article
- Conformations of membrane human immunodeficiency virus (HIV-1) envelope glycoproteins solubilized in Amphipol A18 lipid-nanodiscs.Journal of virology · 2024Article
30 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Membrane proteins function in native cell membranes, but extraction into isolated particles is needed for many biochemical and structural analyses. Commonly used detergent-extraction methods destroy naturally associated lipid bilayers. Here, we devised a detergent-free method for preparing cell-membrane nanoparticles to study the multidrug exporter AcrB, by cryo-EM at 3.2-Å resolution. We discovered a remarkably well-organized lipid-bilayer structure associated with transmembrane domains of the AcrB trimer. This bilayer patch comprises 24 lipid molecules; inner leaflet chains are packed in a hexagonal array, whereas the outer leaflet has highly irregular but ordered packing. Protein side chains interact with both leaflets and participate in the hexagonal pattern. We suggest that the lipid bilayer supports and harmonizes peristaltic motions through AcrB trimers. In AcrB D407A, a putative proton-relay mutant, lipid bilayer buttresses protein interactions lost in crystal structures after detergent-solubilization. Our detergent-free system preserves lipid-protein interactions for visualization and should be broadly applicable.
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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.