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      Rethinking Cysteine Protective Groups:S-Alkylsulfonyl-l-Cysteines for Chemoselective Disulfide Formation

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          Cellular incorporation of unnatural amino acids and bioorthogonal labeling of proteins.

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            Formation and transfer of disulphide bonds in living cells.

            Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of protein disulphide bonds in prokaryotes and eukaryotes are remarkably similar, and they share several mechanistic features. The recent identification of new redox-active proteins in humans and yeast that mechanistically parallel the more established redox-active enzymes indicates that there might be further uncharacterized redox pathways throughout the cell.
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              Protective Groups in Organic Synthesis

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                Author and article information

                Journal
                Chemistry - A European Journal
                Chem. Eur. J.
                Wiley
                09476539
                December 12 2016
                December 12 2016
                October 31 2016
                : 22
                : 50
                : 18085-18091
                Affiliations
                [1 ]Institute of Organic Chemistry; Johannes Gutenberg University Mainz; 55099 Mainz Germany
                Article
                10.1002/chem.201604391
                27797427
                6ae4f35f-b363-43d6-a89c-857161d895a6
                © 2016

                http://doi.wiley.com/10.1002/tdm_license_1.1

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