ArticleNature communications2022
Membrane-mediated protein interactions drive membrane protein organization.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- High-speed atomic force microscopy of membrane proteins: From dynamic imaging to integrative structural biology.Current opinion in structural biology · 2026Review
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- Label-Free Single Protein Dynamics Revealed by Metasurface-Enhanced Raman Spectroscopy.ACS nano · 2026Article
- Decoding protein-phospholipid interaction networks in cancer: the role of acyl-chain remodeling.RSC chemical biology · 2026Review
- Fabrication of focused electron beam induced deposition tips for high-speed atomic force microscopy using benchtop scanning electron microscopy.Nature protocols · 2026Review
- The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026Review
- Clustering of SARS-CoV-2 membrane proteins in lipid bilayer membranes.PLoS computational biology · 2026Article
- HS-AFM Applications to Study Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Lipidomic Comparison of Detergent-Soluble and Detergent-Resistant Lipid Domains Isolated From Rat Cerebellum and the Effect of Hypoxia-Ischemia Using UPLC-HDMSJournal of mass spectrometry : JMS · 2026Article
- High-Speed Atomic Force Microscopy Reveals the Dynamic Interplay of Membrane Proteins is Lipid-Modulated.Small science · 2025Article
- Plasma membrane recycling drives reservoir formation during Toxoplasma gondii intracellular replication.PLoS biology · 2025Article
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
- Cholesterol-dependent dimerization and conformational dynamics of EphA2 receptors from coarse-grained and all-atom simulations.Structure (London, England : 1993) · 2025Article
- Molecular contacts in self-assembling clusters of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Creating Coarse-Grained Systems with COBY: Toward Higher Accuracy of Complex Biological Systems.Journal of chemical information and modeling · 2025Article
- Article
- A structural biology compatible file format for atomic force microscopy.Nature communications · 2025Article
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
- Quaternary arrangements of membrane proteins: an aquaporin case.Biochemical Society transactions · 2024Review
- Utilizing Molecular Dynamics Simulations, Machine Learning, Cryo-EM, and NMR Spectroscopy to Predict and Validate Protein Dynamics.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The plasma membrane's main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the biophysical determinants of membrane-mediated protein interactions must be considered to understand membrane protein organization. Here, we used high-speed atomic force microscopy and kinetic and membrane elastic theory to investigate the behavior of a model membrane protein in oligomerization and assembly in controlled lipid environments. We find that membrane hydrophobic mismatch modulates oligomerization and assembly energetics, and 2D organization. Our experimental and theoretical frameworks reveal how membrane organization can emerge from Brownian diffusion and a minimal set of physical properties of the membrane constituents.
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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.