{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Imomnazarov K"],"funding":["Alzheimer’s Association","Center for Translational Research in Neurodegenerative Disease","NIH NINDS","Aligning Science Across Parkinson’s","Parkinson’s Foundation","Alzheimer's Association","NIH HHS"],"pagination":["3643"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11011978"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(7)"],"pubmed_abstract":["Synucleinopathies are a group of central nervous system pathologies that are characterized by the intracellular accumulation of misfolded and aggregated α-synuclein in proteinaceous depositions known as Lewy Bodies (LBs). The transition of α-synuclein from its physiological to pathological form has been associated with several post-translational modifications such as phosphorylation and an increasing degree of insolubility, which also correlate with disease progression in post-mortem specimens from human patients. Neuronal expression of α-synuclein in model organisms, including <i>Drosophila melanogaster</i>, has been a typical approach employed to study its physiological effects. Biochemical analysis of α-synuclein solubility via high-speed ultracentrifugation with buffers of increasing d"],"journal":["International journal of molecular sciences"],"pubmed_title":["Biochemical Fractionation of Human α-Synuclein in a <i>Drosophila</i> Model of Synucleinopathies."],"pmcid":["PMC11011978"],"funding_grant_id":["AARG-D-22-972117","AARG-D-22–972117","P40 OD018537","1RF1NS28800","ASAP-020527"],"pubmed_authors":["Lopez-Scarim J","Bagheri I","Martin-Pena A","Tansey MG","Imomnazarov K","Joers V"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical Fractionation of Human α-Synuclein in a <i>Drosophila</i> Model of Synucleinopathies.","description":"Synucleinopathies are a group of central nervous system pathologies that are characterized by the intracellular accumulation of misfolded and aggregated α-synuclein in proteinaceous depositions known as Lewy Bodies (LBs). The transition of α-synuclein from its physiological to pathological form has been associated with several post-translational modifications such as phosphorylation and an increasing degree of insolubility, which also correlate with disease progression in post-mortem specimens from human patients. Neuronal expression of α-synuclein in model organisms, including <i>Drosophila melanogaster</i>, has been a typical approach employed to study its physiological effects. Biochemical analysis of α-synuclein solubility via high-speed ultracentrifugation with buffers of increasing d","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-04-21T03:29:07.096Z","creation":"2025-04-06T16:20:54.563Z"},"accession":"S-EPMC11011978","cross_references":{"pubmed":["38612454"],"doi":["10.3390/ijms25073643"]}}