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Updated: May 3, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
[Novel deglycosylation-independent roles for peptide N-glycanase]
Isabelle Chantret1, Alain Couvineau1, Stuart Moore1
1Inserm U773, centre de recherche Bichat Beaujon CRB3, Faculté de médecine Xavier Bichat, 75018 Paris, France - Université Paris 7 Denis Diderot, site Bichat, 16, rue Henri Huchard, 75018, Paris, France.
Abstract:
The primary function of peptide N-glycanase (PNGase) is thought to be the deglycosylation of endoplasmic reticulum associated degradation (ERAD) substrates. However, inhibition of PNGase appears to have little effect upon the destruction rate of many ERAD substrates, and recent data demonstrate deglycosylation-independent functions for PNGase. Whatever the roles of PNGase turn out to be, the identification of a patient presenting with PNGase deficiency will advance our understanding of the importance of this multifunctional protein in human physiology.
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