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- W3047845065 endingPage "85" @default.
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- W3047845065 abstract "The decoration of proteins with post-translational modifications (PTMs) serves as a mechanism to expand the functional repertoire of the proteome. Tyrosine sulfation is a PTM that has been shown to be a key regulator of extracellular protein-protein interactions in a select number of examples. However, the challenges associated with identifying and characterising the functional consequences of tyrosine sulfation have hindered our ability to understand the full scope of its role in the wider proteome when compared with that of other PTMs, for example, phosphorylation and glycosylation. In this account, we highlight recent advances in the prediction and detection of tyrosine sulfation and outline the need for continued innovation in this area. We also discuss the utility of emerging solid-phase synthesis and peptide ligation strategies for accessing libraries of homogeneously sulfated peptides and proteins to help reveal functional aspects of the sulfoproteome." @default.
- W3047845065 created "2020-08-13" @default.
- W3047845065 creator A5050211442 @default.
- W3047845065 creator A5053176470 @default.
- W3047845065 date "2020-10-01" @default.
- W3047845065 modified "2023-10-02" @default.
- W3047845065 title "Revealing the functional roles of tyrosine sulfation using synthetic sulfopeptides and sulfoproteins" @default.
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- W3047845065 doi "https://doi.org/10.1016/j.cbpa.2020.05.007" @default.
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- W3047845065 hasPublicationYear "2020" @default.
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