<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Imomnazarov K</submitter><funding>Alzheimer’s Association</funding><funding>Center for Translational Research in Neurodegenerative Disease</funding><funding>NIH NINDS</funding><funding>Aligning Science Across Parkinson’s</funding><funding>Parkinson’s Foundation</funding><funding>Alzheimer's Association</funding><funding>NIH HHS</funding><pagination>3643</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11011978</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>25(7)</volume><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 &lt;i>Drosophila melanogaster&lt;/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</pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>Biochemical Fractionation of Human α-Synuclein in a &lt;i>Drosophila&lt;/i> Model of Synucleinopathies.</pubmed_title><pmcid>PMC11011978</pmcid><funding_grant_id>AARG-D-22-972117</funding_grant_id><funding_grant_id>AARG-D-22–972117</funding_grant_id><funding_grant_id>P40 OD018537</funding_grant_id><funding_grant_id>1RF1NS28800</funding_grant_id><funding_grant_id>ASAP-020527</funding_grant_id><pubmed_authors>Lopez-Scarim J</pubmed_authors><pubmed_authors>Bagheri I</pubmed_authors><pubmed_authors>Martin-Pena A</pubmed_authors><pubmed_authors>Tansey MG</pubmed_authors><pubmed_authors>Imomnazarov K</pubmed_authors><pubmed_authors>Joers V</pubmed_authors></additional><is_claimable>false</is_claimable><name>Biochemical Fractionation of Human α-Synuclein in a &lt;i>Drosophila&lt;/i> Model of Synucleinopathies.</name><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 &lt;i>Drosophila melanogaster&lt;/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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Mar</publication><modification>2026-04-21T03:29:07.096Z</modification><creation>2025-04-06T16:20:54.563Z</creation></dates><accession>S-EPMC11011978</accession><cross_references><pubmed>38612454</pubmed><doi>10.3390/ijms25073643</doi></cross_references></HashMap>