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Review
. 2006 Nov;44(2):63-72.
doi: 10.1016/j.jdermsci.2006.07.004. Epub 2006 Sep 14.

Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis

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Review

Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis

Stéphane Chavanas et al. J Dermatol Sci. 2006 Nov.

Abstract

Deimination corresponds to the transformation of arginine residues within a peptide sequence into citrulline residues. Catalyzed by peptidylarginine deiminases, it decreases the net positive charge of proteins, alters intra and intermolecular ionic interactions and probably the folding of target proteins. Deimination has recently been implicated in several physiological and pathological processes. Here, we describe the enzymes involved in this post-translational modification, focusing on their expression, location and roles in skin, as well as their known protein substrates in the epidermis and hair follicles. We discuss also the potential involvement of deimination in human diseases including cutaneous disorders.

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