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http://purl.uniprot.org/citations/21268071http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21268071http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21268071http://www.w3.org/2000/01/rdf-schema#comment"SOD2 is a key mitochondrial antioxidant enzyme and its perturbation leads to oxidative cell death, which results in various disorders. In this study, we identified a deubiquitinating enzyme USP36 that regulates the protein stability of SOD2. The regulatory effect of USP36 on SOD2 was initially identified by 2-DE and MALDI-TOF/MS analyses. In addition, endogenous USP36 and SOD2 were shown to interact in an immunoprecipitation assay, which was verified using the yeast two-hybrid system. Furthermore, we demonstrated that SOD2 binds with ubiquitin molecules to form polyubiquitination chains and undergoes degradation through the ubiquitin-proteasomal pathway. Finally, USP36 was shown to be a specific deubiquitinating enzyme that reduces the ubiquitination level of SOD2 and was involved in SOD2 protein stability by extending its half-life."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.org/dc/terms/identifier"doi:10.1002/jcb.22940"xsd:string
http://purl.uniprot.org/citations/21268071http://purl.org/dc/terms/identifier"doi:10.1002/jcb.22940"xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Baek K.H."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Baek K.H."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Kim J.H."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Kim J.H."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Kim M.S."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Kim M.S."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Ramakrishna S."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Ramakrishna S."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Lim K.H."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/author"Lim K.H."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/name"J. Cell. Biochem."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/name"J. Cell. Biochem."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/pages"498-508"xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/pages"498-508"xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/title"Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/title"Protein stability of mitochondrial superoxide dismutase SOD2 is regulated by USP36."xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/volume"112"xsd:string
http://purl.uniprot.org/citations/21268071http://purl.uniprot.org/core/volume"112"xsd:string