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| pubmed-article:15105460 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:15105460 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:15105460 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15105460 | pubmed:issue | 5675 | lld:pubmed |
| pubmed-article:15105460 | pubmed:dateCreated | 2004-5-28 | lld:pubmed |
| pubmed-article:15105460 | 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. | lld:pubmed |
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| pubmed-article:15105460 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15105460 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15105460 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15105460 | pubmed:month | May | lld:pubmed |
| pubmed-article:15105460 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:15105460 | pubmed:author | pubmed-author:DawsonTed MTM | lld:pubmed |
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| pubmed-article:15105460 | pubmed:author | pubmed-author:MarshLauraL | lld:pubmed |
| pubmed-article:15105460 | pubmed:author | pubmed-author:ThomasBobbyB | lld:pubmed |
| pubmed-article:15105460 | pubmed:author | pubmed-author:LiXiaojieX | lld:pubmed |
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| pubmed-article:15105460 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15105460 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:15105460 | pubmed:volume | 304 | lld:pubmed |
| pubmed-article:15105460 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15105460 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15105460 | pubmed:pagination | 1328-31 | lld:pubmed |
| pubmed-article:15105460 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15105460 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15105460 | pubmed:articleTitle | S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. | lld:pubmed |
| pubmed-article:15105460 | pubmed:affiliation | Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. | lld:pubmed |
| pubmed-article:15105460 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15105460 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15105460 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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