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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5675
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pubmed:dateCreated |
2004-5-28
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pubmed:abstractText |
Parkin is an E3 ubiquitin ligase involved in the ubiquitination of proteins that are important in the survival of dopamine neurons in Parkinson's disease (PD). We show that parkin is S-nitrosylated in vitro, as well as in vivo in a mouse model of PD and in brains of patients with PD and diffuse Lewy body disease. Moreover, S-nitrosylation inhibits parkin's ubiquitin E3 ligase activity and its protective function. The inhibition of parkin's ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in these disorders by impairing the ubiquitination of parkin substrates.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Donors,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNCAIP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sncaip protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Synucleins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
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:month |
May
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
28
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pubmed:volume |
304
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1328-31
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15105460-Alzheimer Disease,
pubmed-meshheading:15105460-Animals,
pubmed-meshheading:15105460-Brain,
pubmed-meshheading:15105460-Carrier Proteins,
pubmed-meshheading:15105460-Catalytic Domain,
pubmed-meshheading:15105460-Cell Death,
pubmed-meshheading:15105460-Cell Line,
pubmed-meshheading:15105460-Cysteine Proteinase Inhibitors,
pubmed-meshheading:15105460-Humans,
pubmed-meshheading:15105460-Lewy Body Disease,
pubmed-meshheading:15105460-MPTP Poisoning,
pubmed-meshheading:15105460-Mice,
pubmed-meshheading:15105460-Mice, Knockout,
pubmed-meshheading:15105460-Nerve Tissue Proteins,
pubmed-meshheading:15105460-Nitric Oxide,
pubmed-meshheading:15105460-Nitric Oxide Donors,
pubmed-meshheading:15105460-Nitric Oxide Synthase,
pubmed-meshheading:15105460-Parkinson Disease,
pubmed-meshheading:15105460-Recombinant Proteins,
pubmed-meshheading:15105460-Synucleins,
pubmed-meshheading:15105460-Transfection,
pubmed-meshheading:15105460-Ubiquitin,
pubmed-meshheading:15105460-Ubiquitin-Protein Ligases
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pubmed:year |
2004
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pubmed:articleTitle |
S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function.
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pubmed:affiliation |
Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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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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