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rdf:type |
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lifeskim:mentions |
umls-concept:C0026336,
umls-concept:C0030567,
umls-concept:C0178539,
umls-concept:C0242606,
umls-concept:C0243043,
umls-concept:C0285890,
umls-concept:C0332621,
umls-concept:C1314939,
umls-concept:C1424222,
umls-concept:C1442792,
umls-concept:C2347946
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pubmed:issue |
4
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pubmed:dateCreated |
2008-4-2
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pubmed:abstractText |
Parkinson's disease (PD) is a neurodegenerative pathology whose molecular etiopathogenesis is not known. Novel contributions have come from familial forms of PD caused by alterations in genes with apparently unrelated physiological functions. The gene coding for alpha-synuclein (alpha-syn) (PARK1) has been investigated as alpha-syn is located in Lewy bodies (LB), intraneuronal inclusions in the substantia nigra (SN) of PD patients. A-syn has neuroprotective chaperone-like and antioxidant functions and is involved in dopamine storage and release. DJ-1 (PARK7), another family-PD-linked gene causing an autosomal recessive form of the pathology, shows antioxidant and chaperone-like activities too.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18382667-12428807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18382667-12834338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18382667-12846969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18382667-12846986,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18382667-9462735
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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 |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e1884
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18382667-Cell Line, Tumor,
pubmed-meshheading:18382667-DNA, Complementary,
pubmed-meshheading:18382667-Gene Library,
pubmed-meshheading:18382667-Gene Silencing,
pubmed-meshheading:18382667-Genes, Recessive,
pubmed-meshheading:18382667-HSP70 Heat-Shock Proteins,
pubmed-meshheading:18382667-Humans,
pubmed-meshheading:18382667-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:18382667-Lewy Bodies,
pubmed-meshheading:18382667-Models, Biological,
pubmed-meshheading:18382667-Oncogene Proteins,
pubmed-meshheading:18382667-Oxidative Stress,
pubmed-meshheading:18382667-Parkinson Disease,
pubmed-meshheading:18382667-RNA, Messenger,
pubmed-meshheading:18382667-Substantia Nigra,
pubmed-meshheading:18382667-alpha-Synuclein
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pubmed:year |
2008
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pubmed:articleTitle |
DJ-1 modulates alpha-synuclein aggregation state in a cellular model of oxidative stress: relevance for Parkinson's disease and involvement of HSP70.
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pubmed:affiliation |
Department of Neuroscience, Mario Negri Institute for Pharmacological Research, Milan, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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