@article{open1217,
          volume = {13},
          number = {12},
           month = {November},
          author = {Akhilesh Kumar and Shweta Tikoo and Shuvadeep Maity and Shantanu Sengupta and Sagar Sengupta and Amandeep Kaur and Anand Kumar Bachhawat},
            note = {Copyright of this article belongs to NPG.},
           title = {Mammalian proapoptotic factor ChaC1 and its homologues function as {\ensuremath{\gamma}}-glutamyl cyclotransferases acting specifically on glutathione.},
       publisher = {Nature publishing group},
            year = {2012},
         journal = {EMBO reports},
           pages = {1095--101},
        keywords = {apoptosis; ChaC1; {\ensuremath{\gamma}}-glutamyl cyclotransferases       },
             url = {http://crdd.osdd.net/open/1217/},
        abstract = {ChaC1 is a mammalian proapoptic protein of unknown function induced during endoplasmic reticulum stress. We show using in vivo studies and novel in vitro assays that the ChaC family of proteins function as {\ensuremath{\gamma}}-glutamyl cyclotransferases acting specifically to degrade glutathione but not other {\ensuremath{\gamma}}-glutamyl peptides. The overexpression of these proteins (but not the catalytically dead E{\ensuremath{>}}Q mutants) led to glutathione depletion and enhanced apoptosis in yeast. The ChaC family is conversed across all phyla and represents a new pathway for glutathione degradation in living cells, and the first cytosolic pathway for glutathione degradation in mammalian cells.}
}