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Corrections to: "Inactive and Highly Active, Proteolytically Processed Transglutaminase-5 in Epithelial Cells"

        Correction to:J Invest Dermatol (2008) 128, 2760–6. doi:10.1038/jid.2008.146
        In the article by Pietroni et al., an acknowledgment was inadvertently omitted. The work was supported by a grant from Ricerca Finalizzata RF73 2006 (to EC).
        The authors regret the error.

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        • Inactive and Highly Active, Proteolytically Processed Transglutaminase-5 in Epithelial Cells
          Journal of Investigative DermatologyVol. 128Issue 12
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            Transglutaminases (TGs) are Ca2+-dependent enzymes capable of catalyzing transamidation of glutamine residues to form intermolecular isopeptide bonds. These enzymes are involved in various biological phenomena, including blood coagulation, wound healing, cell death, tissue repair, and terminal differentiation of keratinocytes. Among the TG-family members, TG5 is one of the latest identified enzymes and therefore the less characterized at the functional level. In this work, we reported that TG5 is proteolytically processed in the baculovirus expression system and in mammal epithelial cells.
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