ArticleSmall science2025
High-Speed Atomic Force Microscopy Reveals the Dynamic Interplay of Membrane Proteins is Lipid-Modulated.
Article in Small science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
- High-speed atomic force microscopy of membrane proteins: From dynamic imaging to integrative structural biology.Current opinion in structural biology · 2026Review
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5 authors.
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Abstract
The solvent of membrane proteins is the membrane lipids in which they are embedded. Therefore, the nature of the lipids that surround membrane proteins impacts their dynamics and interactions. Unfortunately, how membrane proteins dynamically interact is difficult to study, and little is experimentally known how membrane proteins interplay in a membrane at the molecular scale. Herein, high-speed atomic force microscopy (HS-AFM) is used to dynamically image a well-controlled bottom-up system consisting of two aquaporin-fold membrane proteins, pentameric FocA and tetrameric GlpF, that interact in membranes composed of varying amounts of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and
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