Redox proteomics: from bench to bedside.

Redox proteomics: from bench to bedside.
Adv Exp Med Biol. 2014;806:301-17
Authors: Ckless K
Abstract
In general protein posttranslation modifications (PTMs) involve the covalent addition of functional groups or molecules to specific amino acid residues in proteins. These modifications include phosphorylation, glycosylation, S-nitrosylation, acetylation, lipidation, among others (Angew Chem Int Ed Engl 44(45):7342-7372, 2005). Although other amino acids can undergo different kinds of oxidative posttranslational modifications (oxPTMs) (Exp Gerontol 36(9):1495-1502, 2001), in this chapter oxPTM will be considered specifically related to Cysteine oxidation, and redox proteomics here is translated as a comprehensive investigation of oxPTMs, in biological systems, using diverse technical approaches. Protein Cysteine residues are not the only amino acid that can be target for oxidative modifications in proteins (Exp Gerontol 36(9):1495-1502, 2001; Biochim Biophys Acta 1814(12):1785-1795, 2011), but certainly it is among the most reactive amino acid (Nature 468(7325):790-795, 2010). Interestingly, it is one of the least abundant amino acid, but it often occurs in the functional sites of proteins (J Mol Biol 404(5):902-916, 2010). In addition, the majority of the Cysteine oxidations are reversible, indicating potential regulatory mechanism of proteins. The global analysis of oxPTMs has been increasingly recognized as an important area of pro...

Source: exp Mol Med - October 3, 2014 Category: Molecular Biology Authors: Ckless K Tags: Adv Exp Med Biol Source Type: research