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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2003-6-4
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pubmed:abstractText |
The identification of pathogenic mutations in the three genes alpha-synuclein, parkin, and ubiquitin carboxy-terminal hydrolase L1 (UCHL1) has elucidated the ubiquitin proteasome system (UPS) and its potential role as a causal pathway in Parkinson's disease (PD). In addition, polymorphisms of these three genes have been shown to be independently associated with PD. In a sample of 298 unrelated PD cases and 185 controls, we applied a two-phased approach of recursive partitioning and logistic regression analyses to explore complex interactions. For women only, we observed an epistatic interaction of UCHL1 and alpha-synuclein genotypes with significant effects on PD risk (odds ratio = 2.42; P = 0.003). Our findings are consistent with the hypothesis that PD is a multigenic disorder of the UPS.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Restriction Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNCA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Synucleins,
http://linkedlifedata.com/resource/pubmed/chemical/Thiolester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin Thiolesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Synuclein,
http://linkedlifedata.com/resource/pubmed/chemical/parkin protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0885-3185
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2003 Movement Disorder Society
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pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
631-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12784265-Case-Control Studies,
pubmed-meshheading:12784265-DNA Restriction Enzymes,
pubmed-meshheading:12784265-Female,
pubmed-meshheading:12784265-Genetic Predisposition to Disease,
pubmed-meshheading:12784265-Genotype,
pubmed-meshheading:12784265-Humans,
pubmed-meshheading:12784265-Ligases,
pubmed-meshheading:12784265-Logistic Models,
pubmed-meshheading:12784265-Male,
pubmed-meshheading:12784265-Movement Disorders,
pubmed-meshheading:12784265-Mutation,
pubmed-meshheading:12784265-Nerve Tissue Proteins,
pubmed-meshheading:12784265-Parkinson Disease,
pubmed-meshheading:12784265-Polymerase Chain Reaction,
pubmed-meshheading:12784265-Synucleins,
pubmed-meshheading:12784265-Thiolester Hydrolases,
pubmed-meshheading:12784265-Ubiquitin Thiolesterase,
pubmed-meshheading:12784265-Ubiquitin-Protein Ligases,
pubmed-meshheading:12784265-alpha-Synuclein
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pubmed:year |
2003
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pubmed:articleTitle |
Complex interactions in Parkinson's disease: a two-phased approach.
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pubmed:affiliation |
Department of Neurology, Mayo Clinic and Mayo Foundation, Rochester, Minnesota 55905, USA. dmaraganore@mayo.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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