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- W3005110010 abstract "Abnormal intracellular presence of aggregates of misfolded alpha-synuclein (AS) and tau are well-known hallmarks of Parkinson's disease (PD) and Alzheimer's disease (AD), respectively. Coexistence of AS and tau in cases of AD and PD, as well as accelerated filament formation of AS in the presence of tau molecules can be considered as hints for the existence of in vivo interactions between these two proteins. Studies on the interaction between monomers of AS and tau have shown an interaction between the C-terminal domain of AS and tau. Here we report the progress of the single-particle cryo-EM structure of the fibrillar form of AS under the interaction with tau. Titan Krios electron microscope, equipped with GATAN K3 camera, was used for image acquisition. Roughly, 1,040,000 segments were extracted from 14,146 manually picked filaments from 1,799 motion corrected and dose-weighted micrographs. 2-D averages of the aligned segments showed the formation of the 2-stranded AS helical filaments, with possibly tau interacting with AS on the outer surface of the helices, despite not being resolved clearly from the class averages, despite the relatively high resolution of the map (4.4Å based on FSC) that helps for resolving the secondary structure of AS. The structure of tau cannot be resolved unambiguously in the reconstructions, but is visible in raw images, which hints to the presence of heterogeneity in the structure or conformation of tau protein when interacting with AS filaments. The structure is being refined for a better global and local resolution. Supported by NIH." @default.
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- W3005110010 date "2020-02-01" @default.
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- W3005110010 title "Single Particle Cryo-EM Structure of Alpha-Synuclein Fibrils Interacting with Tau" @default.
- W3005110010 doi "https://doi.org/10.1016/j.bpj.2019.11.406" @default.
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