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http://purl.uniprot.org/citations/24658080http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24658080http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24658080http://www.w3.org/2000/01/rdf-schema#comment"Moyamoya disease is an idiopathic human cerebrovascular disorder that is characterized by progressive stenosis and abnormal collateral vessels. We recently identified mysterin/RNF213 as its first susceptibility gene, which encodes a 591-kDa protein containing enzymatically active P-loop ATPase and ubiquitin ligase domains and is involved in proper vascular development in zebrafish. Here we demonstrate that mysterin further contains two tandem AAA+ ATPase modules and forms huge ring-shaped oligomeric complex. AAA+ ATPases are known to generally mediate various biophysical and mechanical processes with the characteristic ring-shaped structure. Fluorescence correlation spectroscopy and biochemical evaluation suggested that mysterin dynamically changes its oligomeric forms through ATP/ADP binding and hydrolysis cycles. Thus, the moyamoya disease-associated gene product is a unique protein that functions as ubiquitin ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.org/dc/terms/identifier"doi:10.1038/srep04442"xsd:string
http://purl.uniprot.org/citations/24658080http://purl.org/dc/terms/identifier"doi:10.1038/srep04442"xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Nagata K."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Nagata K."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Fujiyoshi Y."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Fujiyoshi Y."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Nishikawa K."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Nishikawa K."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Hoseki J."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Hoseki J."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kotani Y."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kotani Y."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kitamura A."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kitamura A."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kinjo M."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kinjo M."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Morito D."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Morito D."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kiso K."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/author"Kiso K."xsd:string
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24658080http://purl.uniprot.org/core/date"2014"xsd:gYear