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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2005-7-18
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pubmed:abstractText |
Parkinson's disease (PD) is a progressive neurodegenerative movement disorder that results primarily from the death of dopaminergic neurons in the substantia nigra. Although the etiology of PD is incompletely understood, the recent discovery of genes associated with rare monogenic forms of the disease, together with earlier studies and new experimental animal models, has provided important and novel insight into the molecular pathways involved in disease pathogenesis. Increasing evidence indicates that deficits in mitochondrial function, oxidative and nitrosative stress, the accumulation of aberrant or misfolded proteins, and ubiquitin-proteasome system dysfunction may represent the principal molecular pathways or events that commonly underlie the pathogenesis of sporadic and familial forms of PD .
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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/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PARK7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN-induced putative kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Synucleins,
http://linkedlifedata.com/resource/pubmed/chemical/UCHL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin Thiolesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/parkin protein
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pubmed:status |
MEDLINE
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pubmed:issn |
0147-006X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
57-87
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16022590-Animals,
pubmed-meshheading:16022590-Humans,
pubmed-meshheading:16022590-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:16022590-Models, Biological,
pubmed-meshheading:16022590-Mutation,
pubmed-meshheading:16022590-Nerve Tissue Proteins,
pubmed-meshheading:16022590-Oncogene Proteins,
pubmed-meshheading:16022590-Parkinson Disease,
pubmed-meshheading:16022590-Proteasome Endopeptidase Complex,
pubmed-meshheading:16022590-Protein Kinases,
pubmed-meshheading:16022590-Signal Transduction,
pubmed-meshheading:16022590-Synucleins,
pubmed-meshheading:16022590-Ubiquitin,
pubmed-meshheading:16022590-Ubiquitin Thiolesterase,
pubmed-meshheading:16022590-Ubiquitin-Protein Ligases
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pubmed:year |
2005
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pubmed:articleTitle |
Molecular pathophysiology of Parkinson's disease.
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pubmed:affiliation |
Institute for Cell Engineering, Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. dmoore20@jhmi.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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