| http://purl.uniprot.org/citations/25416785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25416785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25416785 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/25416785 | http://www.w3.org/2000/01/rdf-schema#comment | "Glycation is an inevitable nonenzymatic covalent reaction between proteins and endogenous reducing sugars or dicarbonyls (methylglyoxal, glyoxal) that results in protein inactivation. DJ-1 was reported to be a multifunctional oxidative stress response protein with poorly defined function. Here, we show that human DJ-1 is a protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins by acting on early glycation intermediates and releases repaired proteins and lactate or glycolate, respectively. DJ-1 deglycates cysteines, arginines, and lysines (the three major glycated amino acids) of serum albumin, glyceraldehyde-3-phosphate dehydrogenase, aldolase, and aspartate aminotransferase and thus reactivates these proteins. DJ-1 prevented protein glycation in an Escherichia coli mutant deficient in the DJ-1 homolog YajL and restored cell viability in glucose-containing media. These results suggest that DJ-1-associated Parkinsonism results from excessive protein glycation and establishes DJ-1 as a major anti-glycation and anti-aging protein."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m114.597815"xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m114.597815"xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Richarme G."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Richarme G."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Leger T."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Leger T."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Dairou J."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Dairou J."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Lamouri A."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Lamouri A."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Mihoub M."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Mihoub M."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Bui L.C."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/author | "Bui L.C."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/pages | "1885-1897"xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/pages | "1885-1897"xsd:string |
| http://purl.uniprot.org/citations/25416785 | http://purl.uniprot.org/core/title | "Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine and lysine residues."xsd:string |