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LIFE SCIENCE TECHNOLOGIES: Glycoproteomics: The Sweet Smell Of We're-Getting-There

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Science  07 Jan 2011:
Vol. 331, Issue 6013, pp. 95
DOI: 10.1126/science.331.6013.95

Summary

Quick: What's the most abundant posttranslational modification on eukaryotic proteins? It's not phosphorylation. Some 50 percent of eukaryotic proteins, and not just those on the cell surface, are dusted with sugars like some molecular pastry. Those glycan modifications mediate inter-molecular and intercellular binding events from fertility to immunity. Yet for years, researchers in the sugar and protein communities have operated independently of one another, cataloging sugars free of protein, or proteins free of sugar, and ne'er the twain shall meet. Today, though, the two communities are bridging their technical divide. "We are in a transition now," says James Paulson, principal investigator of the Consortium for Functional Glycomics. Glycoproteomics, he says, "is becoming mainstream."