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- W2006265169 endingPage "342" @default.
- W2006265169 startingPage "327" @default.
- W2006265169 abstract "Posttranslational modifications (PTM) including glycosylation, phosphorylation, acetylation, methylation and ubiquitination dynamically alter the proteome. The evolutionarily conserved enzymes O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) and O-GlcNAcase are responsible for the addition and removal, respectively, of the nutrient-sensitive PTM of protein serine and threonine residues with O-GlcNAc. Indeed, the O-GlcNAc modification acts at every step in the “central dogma” of molecular biology and alters signaling pathways leading to amplified or blunted biological responses. The cellular roles of OGT and the dynamic PTM O-GlcNAc have been clarified with recently developed chemical tools including high-throughput assays, structural and mechanistic studies and potent enzyme inhibitors. These evolving chemical tools complement genetic and biochemical approaches for exposing the underlying biological information conferred by O-GlcNAc cycling." @default.
- W2006265169 created "2016-06-24" @default.
- W2006265169 creator A5017683745 @default.
- W2006265169 creator A5019509986 @default.
- W2006265169 creator A5057106217 @default.
- W2006265169 creator A5081114129 @default.
- W2006265169 date "2014-07-01" @default.
- W2006265169 modified "2023-10-17" @default.
- W2006265169 title "Chemical tools to explore nutrient-driven O-GlcNAc cycling" @default.
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