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Tyrosine (Tyr) sulfation is a common posttranslational modification of secreted proteins or membrane-bound proteins that is implicated in numerous physiological and pathological processes. The Tyr sulfation modifies proteinprotein interactions involved in leukocyte adhesion, homeostasis, and receptor-mediated signaling. To data, 80 Tyrsulfated proteins have been identified. As new methodologies and bioinformatics for the detection of Tyr sulfation become available, the number of Tyr-sulfated acceptor proteins discovered is bound to increase. Further, recent advances in microscopy and fluorescence technology will provide information on the true spatial and temporal nature of Tyr-sulfated proteins within the intact cell. This review summarizes the methods for the detection of Tyr O-sulfation as well as the biological functions of sulfated Tyr. Further, illustrative examples of the impact of Tyr sulfation on the pharmacological properties are presented.

Citation

Nobuya Sasaki. Current status and future prospects for research on tyrosine sulfation. Current pharmaceutical biotechnology. 2012 Nov;13(14):2632-41

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PMID: 22039814

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