Lipid packing defects are necessary and sufficient for membrane binding of α-synuclein
Abstract α-Synuclein (αSyn), an intrinsically disordered protein implicated in Parkinson’s disease, is thought to initiate aggregation by binding to cellular membranes. Previous studies suggest that anionic lipids are necessary for this binding. However, these studies largely focused on unmodified α...
Saved in:
| Main Authors: | David H. Johnson, Orianna H. Kou, John M. White, Stephanie Y. Ramirez, Antonis Margaritakis, Peter J. Chung, Vance W. Jaeger, Wade F. Zeno |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-08-01
|
| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-025-08622-7 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Intracellular α-synuclein assemblies are sufficient to alter nanoscale diffusion in the striatal extracellular space
by: J. Estaun-Panzano, et al.
Published: (2024-12-01) -
Necessary and sufficient conditions in theorems
by: Edmundas Mazėtis, et al.
Published: (2024-12-01) -
Identification of synaptosomal proteins binding to monomeric and oligomeric α-synuclein.
by: Cristine Betzer, et al.
Published: (2015-01-01) -
Anion Binding and Aggregation of N‑Terminal α‑Synuclein Peptides
by: Ruiqing Wang, et al.
Published: (2025-05-01) -
More with less: only the necessary and sufficient
by: Elena Mussinelli
Published: (2025-07-01)