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http://purl.uniprot.org/citations/17015834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17015834http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17015834http://www.w3.org/2000/01/rdf-schema#comment"DJ-1/PARK7, a cancer- and Parkinson's disease (PD)-associated protein, protects cells from toxic stresses. However, the functional basis of this protection has remained elusive. We found that loss of DJ-1 leads to deficits in NQO1 [NAD(P)H quinone oxidoreductase 1], a detoxification enzyme. This deficit is attributed to a loss of Nrf2 (nuclear factor erythroid 2-related factor), a master regulator of antioxidant transcriptional responses. DJ-1 stabilizes Nrf2 by preventing association with its inhibitor protein, Keap1, and Nrf2's subsequent ubiquitination. Without intact DJ-1, Nrf2 protein is unstable, and transcriptional responses are thereby decreased both basally and after induction. This effect of DJ-1 on Nrf2 is present in both transformed lines and primary cells across human and mouse species. DJ-1's effect on Nrf2 and subsequent effects on antioxidant responses may explain how DJ-1 affects the etiology of both cancer and PD, which are seemingly disparate disorders. Furthermore, this DJ-1/Nrf2 functional axis presents a therapeutic target in cancer treatment and justifies DJ-1 as a tumor biomarker."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0607260103"xsd:string
http://purl.uniprot.org/citations/17015834http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0607260103"xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Ting J.P."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Ting J.P."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Mak T.W."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Mak T.W."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Conti B.J."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Conti B.J."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Clements C.M."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"Clements C.M."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"McNally R.S."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/author"McNally R.S."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/pages"15091-15096"xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/pages"15091-15096"xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/title"DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/title"DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/volume"103"xsd:string
http://purl.uniprot.org/citations/17015834http://purl.uniprot.org/core/volume"103"xsd:string