Abstract
Parkinson's disease (PD) is the most common neurodegenerative movement disorder. The major motor disabilities of PD are associated with the extensive loss of dopaminergic neurons in the substantia nigra pars compacta. The physiological changes and biochemical pathways involved in the selective demise of these neurons are still unclear. Recent studies have demonstrated that alterations or reductions in ubiquitin-mediated proteasome function can be causal of at least some forms of parkinsonism, and multiple lines of evidence suggest that this mechanism of protein degradation may play an important role in the etiology of PD.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Cysteine Endopeptidases / genetics
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Cysteine Endopeptidases / metabolism*
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Drosophila Proteins / metabolism
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Humans
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Ligases / deficiency
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Ligases / genetics
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Multienzyme Complexes / genetics
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Multienzyme Complexes / metabolism*
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Nerve Tissue Proteins / metabolism
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Neurons / metabolism*
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Neurons / pathology
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Parkinson Disease / genetics
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Parkinson Disease / metabolism*
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Proteasome Endopeptidase Complex
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Receptors, Endothelin
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Substantia Nigra / metabolism*
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Substantia Nigra / pathology
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Substantia Nigra / physiopathology
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Synucleins
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Thiolester Hydrolases / metabolism
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Ubiquitin / genetics
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Ubiquitin / metabolism*
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Ubiquitin Thiolesterase
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Ubiquitin-Protein Ligases*
Substances
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Drosophila Proteins
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Multienzyme Complexes
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Nerve Tissue Proteins
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Pael-R protein, Drosophila
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Receptors, Endothelin
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Synucleins
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Ubiquitin
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Ubiquitin-Protein Ligases
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parkin protein
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Thiolester Hydrolases
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Ubiquitin Thiolesterase
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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Ligases