Shutting down parts of the glycome
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Rillahan, C.D., _et al_. _Nat. Chem. Biol._ 8, 661–668 (2012). The transfer of a fucose or sialic acid sugar to a growing polysaccharide represents one step in a complex process that is
poorly understood. Twenty sialyltransferases and 14 fucosyltransferases encoding variable acceptor specificities, activities and expression patterns are encoded in the human genome. To date,
fluorinated analogs that block the transition state of these enzymes have not been membrane permeable, prompting Rillahan _et al_. to modify them by peracetylation. These protected analogs
are neutrally charged and can slip into the cell, where sialic acid and fucose salvage pathway enzymes revert them to their unprotected form. The resulting membrane-permeable,
family-specific inhibitors also shut down new biosynthesis through metabolic feedback, making them promising tools for dissecting the roles of fucosylated and sialylated glycans in cell
communication and immunity. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Shutting down parts of the glycome. _Nat Methods_ 9, 782 (2012).
https://doi.org/10.1038/nmeth.2128 Download citation * Published: 30 July 2012 * Issue Date: August 2012 * DOI: https://doi.org/10.1038/nmeth.2128 SHARE THIS ARTICLE Anyone you share the
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