Abstract
The abnormal aggregation of α-synuclein (αSyn) is considered as connection with the development of synucleinopathies such as Parkinson’s disease, and lipid could be one of crucial inducers. Familial Parkinson’s disease (FPD) mutation of αSyn can change its properties and may impact its interactions with lipid. In this study, using multiple fluorescence techniques, we found that H50Q mutation can increase αSyn binding to synaptic-like vesicle, which could be helpful to uncover the H50Q mutation-related pathology of αSyn.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
