{"database":"bioimages","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":[null],"species":["hiPSC derived neurons"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-BIAD465"],"repository":["bioimages"],"figure_sub":["Protocols","Study Component","organisation","Study Protocols"],"pubmed_authors":["Noemi Esteras ","Sonia Ghandi","Bhanu P. Singh","Mathew H. Horrocks","Gurvier S. Viridi","Zeniba Shadman","James R. Evans ","David J. Clarke ","Laura Tosatto","Minee L. Choi ","Lucy Collinson ","Andrey Y. Abramov","Catherine Maclachlan","Katie Morris ","Anna Wernick","Maragarida Rodrigues","Plamena R. Angelova","Alexey V. Berezhnov","Evgenia Fedotova","Kiani Jeacock","Alexandre Chappard","Dilan Athauda ","David Klenerman","Chris Peddie","Daniel Little ","Tilo Kunath","Suman De","Paul Gissen ","Andrey Y. Vinikurov","Weilia Zhang"],"additional_accession":[]},"is_claimable":false,"name":"Structural conversion of α-synuclein at the mitochondria induces neuronal toxicity\t\t\t\t\t\t","description":"Aggregation of alpha-synuclein (α-Syn) drives Parkinson’s disease, although the initial stages of\nself-assembly and structural conversion have not been captured inside neurons. We track the\nintracellular conformational states of α-Syn utilizing a single-molecule Förster resonance energy\ntransfer (smFRET) biosensor and show that α-Syn converts from its monomeric state to form two\ndistinct oligomeric states in neurons in a concentration-dependent and sequence-specific\nmanner. 3D FRET-Correlative light and electron microscopy (FRET- CLEM) reveals the structural\norganization and location of aggregation hotspots inside the neuron. Notably, multiple\nintracellular seeding events occur preferentially on membrane surfaces, especially at the\nmitochondrial membranes. The mitochondrial lipid, cardioli","dates":{"release":"2022-05-11T00:00:00Z","modification":"2022-05-27T11:11:06.681Z","creation":"2022-05-27T11:11:06.681Z"},"accession":"S-BIAD465","cross_references":{}}