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α-Synuclein-Induced Membrane Remodeling Is Driven by Binding Affinity, Partition Depth, and Interleaflet Order Asymmetry
[Image: see text] We have investigated the membrane remodeling capacity of the N-terminal membrane-binding domain of α-synuclein (α-Syn(100)). Using fluorescence correlation spectroscopy and vesicle clearance assays, we show that α-Syn(100) fully tubulates POPG vesicles, the first demonstration that...
Tallennettuna:
| Päätekijät: | , , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Chemical
Society
2014
|
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4105054/ https://ncbi.nlm.nih.gov/pubmed/24960410 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja5016958 |
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