{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhao J"],"funding":["National Institute of Neurological Disorders and Stroke","NIA NIH HHS","NCRR NIH HHS","NINDS NIH HHS","National Institutes of Health","National Institute of General Medical Sciences","NIH HHS","NIGMS NIH HHS","National Science Foundation"],"pagination":["20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8991655"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["<h4>Background</h4>Alpha-synuclein (α-syn) exhibits pathological misfolding in many human neurodegenerative disorders. We previously showed that α-syn is arginylated in the mouse brain and that lack of arginylation leads to neurodegeneration in mice.<h4>Methods</h4>Here, we tested α-syn arginylation in human brain pathology using newly derived antibodies in combination with Western blotting, biochemical assays, and experiments in live neurons.<h4>Results</h4>We found that α-syn was arginylated in the human brain on E46 and E83, two sites previously implicated in α-syn pathology and familial cases of Parkinson's disease. The levels of arginylation in different brain samples ranged between ~ 3% and ~ 50% of the total α-syn pool, and this arginylation nearly exclusively concentrated in the su"],"journal":["Translational neurodegeneration"],"pubmed_title":["α-Synuclein arginylation in the human brain."],"pmcid":["PMC8991655"],"funding_grant_id":["R01NS102435","U19 AG062418","S10 RR023444","RR-023444","R35GM122505","R01 NS120625","R01NS120625","CHE-1827457","R35 GM122505","R01 NS102435","MRI-0820996","P30 AG072979"],"pubmed_authors":["Dong DW","Huang Y","Luk KC","Shimogawa M","Petersson EJ","Pan B","Kashina A","Zhao J","Fina M","Rhoades E"],"additional_accession":[]},"is_claimable":false,"name":"α-Synuclein arginylation in the human brain.","description":"<h4>Background</h4>Alpha-synuclein (α-syn) exhibits pathological misfolding in many human neurodegenerative disorders. We previously showed that α-syn is arginylated in the mouse brain and that lack of arginylation leads to neurodegeneration in mice.<h4>Methods</h4>Here, we tested α-syn arginylation in human brain pathology using newly derived antibodies in combination with Western blotting, biochemical assays, and experiments in live neurons.<h4>Results</h4>We found that α-syn was arginylated in the human brain on E46 and E83, two sites previously implicated in α-syn pathology and familial cases of Parkinson's disease. The levels of arginylation in different brain samples ranged between ~ 3% and ~ 50% of the total α-syn pool, and this arginylation nearly exclusively concentrated in the su","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-22T03:57:47.183Z","creation":"2025-04-05T20:49:22.923Z"},"accession":"S-EPMC8991655","cross_references":{"pubmed":["35395956"],"doi":["10.1186/s40035-022-00295-0"]}}