The ubiquitin pathway in Parkinson's disease

Elisabeth Leroy, Rebecca Boyer, Georg Auburger, Barbara Leube, Gudrun Ulm, Eva Mezey, Gyongyi Harta, Michael J. Brownstein, Sobhanadditya Jonnalagada, Tanya Chernova, Anindya Dehejia, Christian Lavedan, Thomas Gasser, Peter J. Steinbach, Keith D. Wilkinson and Mihael H. Polymeropoulos
Additional contact information
Elisabeth Leroy: Genetic Disease Research Branch, NHGRI, NIH
Rebecca Boyer: Genetic Disease Research Branch, NHGRI, NIH
Georg Auburger: Genetic Disease Research Branch, NHGRI, NIH
Barbara Leube: University Hospital
Gudrun Ulm: Paracelcus-Elena-Klinik
Eva Mezey: Basic Neuroscience Program, NINDS, NIH
Gyongyi Harta: Basic Neuroscience Program, NINDS, NIH
Michael J. Brownstein: Section on Genetics, NIMH, NIH
Sobhanadditya Jonnalagada: Emory University School of Medicine
Tanya Chernova: Emory University School of Medicine
Anindya Dehejia: Genetic Disease Research Branch, NHGRI, NIH
Christian Lavedan: Genetic Disease Research Branch, NHGRI, NIH
Thomas Gasser: Neurologische Klinik, Klinikum Grosshadern, Ludwig-Maximilians-Universitat
Peter J. Steinbach: Center for Molecular Modeling, CIT, NIH
Keith D. Wilkinson: Emory University School of Medicine
Mihael H. Polymeropoulos: Genetic Disease Research Branch, NHGRI, NIH

Nature, 1998, vol. 395, issue 6701, 451-452

Abstract: Abstract Mutations of the α-synuclein gene1,2 have been identified in some familial forms of Parkinson's disease, and α-synuclein protein has been shown to accumulate in the brains of patients with the disease3. These findings suggest that Parkinson's disease may be caused by the abnormal aggregation of α-synuclein protein. Here we have identified in a German family with Parkinson's disease a missense mutation in the ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) gene. We show that this mutation, Ile93Met, causes a partial loss of the catalytic activity of this thiol protease, which could lead to aberrations in the proteolytic pathway and aggregation of proteins.

Date: 1998
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/26652 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:395:y:1998:i:6701:d:10.1038_26652

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/26652

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().