| http://purl.uniprot.org/citations/20861018 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20861018 | http://www.w3.org/2000/01/rdf-schema#comment | "Early onset dystonia is commonly associated with the deletion of one of a pair of glutamate residues (ΔE302/303) near the C terminus of torsinA, a member of the AAA+ protein family (ATPases associated with a variety of cellular activities) located in the endoplasmic reticulum lumen. The functional consequences of the disease-causing mutation, ΔE, are not currently understood. By contrast to other AAA+ proteins, torsin proteins contain two conserved cysteine residues in the C-terminal domain, one of which is located in the nucleotide sensor II motif. Depending on redox status, an ATP hydrolysis mutant of torsinA interacts with lamina-associated polypeptide 1 (LAP1) and lumenal domain like LAP1 (LULL1). Substitution of the cysteine in sensor II diminishes the redox-regulated interaction of torsinA with these substrates. Significantly, the dystonia-causing mutation, ΔE, alters the ability of torsinA to mediate the redox-regulated interactions with LAP1 and LULL1. Limited proteolysis experiments reveal redox- and mutation-dependent changes in the local conformation of torsinA as a function of nucleotide binding. These results indicate that the cysteine-containing sensor II plays a critical role in redox sensing and the nucleotide and partner binding functions of torsinA and suggest that loss of this function of torsinA contributes to the development of DYT1 dystonia."xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.123471"xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/author | "Zhu L."xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/author | "Millen L."xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/author | "Thomas P.J."xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/author | "Mendoza J.L."xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/pages | "37271-37280"xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/title | "A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding."xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://purl.uniprot.org/core/volume | "285"xsd:string |
| http://purl.uniprot.org/citations/20861018 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20861018 |
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| http://purl.uniprot.org/uniprot/O14656 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20861018 |
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