<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Schechter M</submitter><funding>National Institute of Neurological Disorders and Stroke</funding><funding>NIA NIH HHS</funding><funding>Israel Science Foundation</funding><funding>NINDS NIH HHS</funding><funding>National Institute on Aging</funding><pagination>24</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7104492</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>α-Synuclein (α-Syn) is a protein implicated in the pathogenesis of Parkinson's disease (PD). α-Syn has been shown to associate with membranes and bind acidic phospholipids. However, the physiological importance of these associations to the integrity of axons is not fully clear.&lt;h4>Methods&lt;/h4>Biochemical, immunohistochemical and ultrastructural analyses in cultured neurons, transgenic mouse brains, PD and control human brains.&lt;h4>Results&lt;/h4>We analyzed the ultrastructure of cross-sectioned axons localized to white matter tracts (WMTs), within the dorsal striatum of old and symptomatic α-Syn transgenic mouse brains. The analysis indicated a higher density of axons of thinner diameter. Our findings in cultured cortical neurons indicate a role for α-Syn in elongation of th</pubmed_abstract><journal>Molecular neurodegeneration</journal><pubmed_title>A role for α-Synuclein in axon growth and its implications in corticostriatal glutamatergic plasticity in Parkinson's disease.</pubmed_title><pmcid>PMC7104492</pmcid><funding_grant_id>U24 NS072026</funding_grant_id><funding_grant_id>P30 AG019610</funding_grant_id><funding_grant_id>P30 AG19610</funding_grant_id><funding_grant_id>182/12</funding_grant_id><pubmed_authors>Grigoletto J</pubmed_authors><pubmed_authors>Glickstein H</pubmed_authors><pubmed_authors>Beach TG</pubmed_authors><pubmed_authors>Serrano GE</pubmed_authors><pubmed_authors>Abd-Elhadi S</pubmed_authors><pubmed_authors>Sharon R</pubmed_authors><pubmed_authors>Friedman A</pubmed_authors><pubmed_authors>Schechter M</pubmed_authors></additional><is_claimable>false</is_claimable><name>A role for α-Synuclein in axon growth and its implications in corticostriatal glutamatergic plasticity in Parkinson's disease.</name><description>&lt;h4>Background&lt;/h4>α-Synuclein (α-Syn) is a protein implicated in the pathogenesis of Parkinson's disease (PD). α-Syn has been shown to associate with membranes and bind acidic phospholipids. However, the physiological importance of these associations to the integrity of axons is not fully clear.&lt;h4>Methods&lt;/h4>Biochemical, immunohistochemical and ultrastructural analyses in cultured neurons, transgenic mouse brains, PD and control human brains.&lt;h4>Results&lt;/h4>We analyzed the ultrastructure of cross-sectioned axons localized to white matter tracts (WMTs), within the dorsal striatum of old and symptomatic α-Syn transgenic mouse brains. The analysis indicated a higher density of axons of thinner diameter. Our findings in cultured cortical neurons indicate a role for α-Syn in elongation of th</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Mar</publication><modification>2025-04-18T11:48:55.576Z</modification><creation>2020-05-22T15:35:54Z</creation></dates><accession>S-EPMC7104492</accession><cross_references><pubmed>32228705</pubmed><doi>10.1186/s13024-020-00370-y</doi></cross_references></HashMap>