VOLUME 278 (2003) PAGES 3671–3678
This article has been withdrawn by the authors upon request from the Journal. The Journal raised questions regarding Figs. 3 and 4A. The authors were able to locate original data for some panels, and for the others, the authors state that new experiments were performed. The authors assert that all of the results reported in this article are valid, some of which have been validated in the literature by different groups (e.g. Choi et al. (2011) Autophagy 7, 1052; Hemelaar et al. (2003) J. Biol. Chem. 278, 51841; Shu et al. (2010) Autophagy 6, 936; Tanida et al. (2004) Int. J. Biochem. Cell. Biol. 36, 2503).
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Published online: January 25, 2019
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- Human Autophagins, a Family of Cysteine Proteinases Potentially Implicated in Cell Degradation by AutophagyJournal of Biological ChemistryVol. 278Issue 6
- PreviewWe have cloned four human cDNAs encoding putative cysteine proteinases that have been tentatively called autophagins. These proteins are similar to Apg4/Aut2, a yeast enzyme involved in the activation of Apg8/Aut7 during the process of autophagy. The identified proteins ranging in length from 393 to 474 amino acids also contain several structural features characteristic of cysteine proteinases including a conserved cysteine residue that is essential for the catalytic properties of these enzymes.
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