{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361699994610440960.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1126/science.1101738"}},{"identifier":{"@type":"URI","@value":"https://www.science.org/doi/pdf/10.1126/science.1101738"}}],"dc:title":[{"@value":"Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>Aberrant α-synuclein degradation is implicated in Parkinson's disease pathogenesis because the protein accumulates in the Lewy inclusion bodies associated with the disease. Little is known, however, about the pathways by which wild-type α-synuclein is normally degraded. We found that wild-type α-synuclein was selectively translocated into lysosomes for degradation by the chaperone-mediated autophagy pathway. The pathogenic A53T and A30P α-synuclein mutants bound to the receptor for this pathway on the lysosomal membrane, but appeared to act as uptake blockers, inhibiting both their own degradation and that of other substrates. These findings may underlie the toxic gain-of-function by the mutants.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381699994610440961","@type":"Researcher","foaf:name":[{"@value":"Ana Maria Cuervo"}],"jpcoar:affiliationName":[{"@value":"Department of Anatomy and Structural Biology, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA."},{"@value":"Neurobiology Laboratory, Foundation of Biomedical Research of the Academy of Athens, Athens 11527, Greece and Department of Neurology and Pathology, Columbia University, New York, NY 10032, USA."},{"@value":"Center for Neurologic Diseases, Brigham and Women's Hospital, Department of Neurology, Harvard MedicalSchool, Cambridge, MA 02139, USA."},{"@value":"Departments of Psychiatry and Neurology, Columbia University, Department of Neuroscience, New York State Psychiatric Institute, New York, NY 10032, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994610440960","@type":"Researcher","foaf:name":[{"@value":"Leonidas Stefanis"}],"jpcoar:affiliationName":[{"@value":"Department of Anatomy and Structural Biology, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA."},{"@value":"Neurobiology Laboratory, Foundation of Biomedical Research of the Academy of Athens, Athens 11527, Greece and Department of Neurology and Pathology, Columbia University, New York, NY 10032, USA."},{"@value":"Center for Neurologic Diseases, Brigham and Women's Hospital, Department of Neurology, Harvard MedicalSchool, Cambridge, MA 02139, USA."},{"@value":"Departments of Psychiatry and Neurology, Columbia University, Department of Neuroscience, New York State Psychiatric Institute, New York, NY 10032, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994610440964","@type":"Researcher","foaf:name":[{"@value":"Ross Fredenburg"}],"jpcoar:affiliationName":[{"@value":"Department of Anatomy and Structural Biology, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA."},{"@value":"Neurobiology Laboratory, Foundation of Biomedical Research of the Academy of Athens, Athens 11527, Greece and Department of Neurology and Pathology, Columbia University, New York, NY 10032, USA."},{"@value":"Center for Neurologic Diseases, Brigham and Women's Hospital, Department of Neurology, Harvard MedicalSchool, Cambridge, MA 02139, USA."},{"@value":"Departments of Psychiatry and Neurology, Columbia University, Department of Neuroscience, New York State Psychiatric Institute, New York, NY 10032, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994610440963","@type":"Researcher","foaf:name":[{"@value":"Peter T. Lansbury"}],"jpcoar:affiliationName":[{"@value":"Department of Anatomy and Structural Biology, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA."},{"@value":"Neurobiology Laboratory, Foundation of Biomedical Research of the Academy of Athens, Athens 11527, Greece and Department of Neurology and Pathology, Columbia University, New York, NY 10032, USA."},{"@value":"Center for Neurologic Diseases, Brigham and Women's Hospital, Department of Neurology, Harvard MedicalSchool, Cambridge, MA 02139, USA."},{"@value":"Departments of Psychiatry and Neurology, Columbia University, Department of Neuroscience, New York State Psychiatric Institute, New York, NY 10032, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994610440962","@type":"Researcher","foaf:name":[{"@value":"David Sulzer"}],"jpcoar:affiliationName":[{"@value":"Department of Anatomy and Structural Biology, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA."},{"@value":"Neurobiology Laboratory, Foundation of Biomedical Research of the Academy of Athens, Athens 11527, Greece and Department of Neurology and Pathology, Columbia University, New York, NY 10032, USA."},{"@value":"Center for Neurologic Diseases, Brigham and Women's Hospital, Department of Neurology, Harvard MedicalSchool, Cambridge, MA 02139, USA."},{"@value":"Departments of Psychiatry and Neurology, Columbia University, Department of Neuroscience, New York State Psychiatric Institute, New York, NY 10032, USA."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00368075"},{"@type":"EISSN","@value":"10959203"}],"prism:publicationName":[{"@value":"Science"}],"dc:publisher":[{"@value":"American Association for the Advancement of Science (AAAS)"}],"prism:publicationDate":"2004-08-27","prism:volume":"305","prism:number":"5688","prism:startingPage":"1292","prism:endingPage":"1295"},"reviewed":"false","url":[{"@id":"https://www.science.org/doi/pdf/10.1126/science.1101738"}],"createdAt":"2004-08-26","modifiedAt":"2024-01-09","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050851175691394432","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"PROTACs and Other Chemical Protein Degradation Technologies for the Treatment of Neurodegenerative Disorders"}]},{"@id":"https://cir.nii.ac.jp/crid/1360002215789866240","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Dynein Dysfunction Disrupts Intracellular Vesicle Trafficking Bidirectionally and Perturbs Synaptic Vesicle Docking via Endocytic 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