S-Nitrosylation of IRP 2 Regulates Its Stability via the Ubiquitin-Proteasome Pathway

@inproceedings{Kim2003SNitrosylationOI,
  title={S-Nitrosylation of IRP 2 Regulates Its Stability via the Ubiquitin-Proteasome Pathway},
  author={Sangwon Kim and Simon S Wing and Prem Ponka},
  year={2003}
}
O5, 2001). We deemed it important to define the mechanism of IRP2 degradation by NO. In this study we demonstrated that IRP2 is S-nitrosylated by SNP and that this nitrosylation leads to its degradation via the ubiquitin-proteasome pathway. * Corresponding author. Mailing address: Lady Davis Institute for Medical Research, Jewish General Hospital, 3755 Cote Ste-Catherine Rd., Montreal, QC H3T 1E2, Canada. Phone: (514) 340-8260. Fax: (514) 340-7502. E-mail: prem.ponka@mcgill.ca. 330 on S etem er… CONTINUE READING