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Updated: May 23, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Rare and unusual glycosylation of peptides and proteins
Pierre Lafite1, Richard Daniellou
1Institut de Chimie Organique et Analytique-ICOA, Université d'Orléans, UMR CNRS 7311, Rue de Chartres, BP 6759, 45067 Orléans Cedex 2, France.
Abstract:
Glycosylation represents the most complex co- and post-translational modification of proteins. In addition to N- and O-glycans, almost all combinations, including the nature of the carbohydrate moiety and the amino-acid involved, but also the type of the chemical linkage, can be isolated from natural glycoconjugates. This diversity correlates with the importance and the variety of the biological processes (and consequently the diseases) glycosides are involved in. This review focuses on rare and unusual glycosylation of peptides and proteins.
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