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• W2116095417 abstract "The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases. Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins is still challenging. In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin. On-resin proteolysis using trypsin followed by LC–MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line. Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins. To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins. About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response." @default.
• W2116095417 created "2016-06-24" @default.
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• W2116095417 date "2013-01-18" @default.
• W2116095417 modified "2023-09-29" @default.
• W2116095417 title "Proteome Wide Purification and Identification of <i>O</i>-GlcNAc-Modified Proteins Using Click Chemistry and Mass Spectrometry" @default.
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• W2116095417 doi "https://doi.org/10.1021/pr300967y" @default.
• W2116095417 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4946622" @default.
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• W2116095417 hasPublicationYear "2013" @default.
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