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Kim, Eun J.,Abramowitz, Lara K.,Bond, Michelle R.,Love, Dona C.,Kang, Dong W.,Leucke, Hans F.,Kang, Dae W.,Ahn, Jong-Seog,Hanover, John A. American Chemical Society 2014 Bioconjugate chemistry Vol.25 No.6
<P/><P>The dynamic glycosylation of serine/threonine residues on nucleocytoplasmic proteins with a single <I>N</I>-acetylglucosamine (<I>O</I>-GlcNAcylation) is critical for many important cellular processes. Cellular <I>O</I>-GlcNAc levels are highly regulated by two enzymes: <I>O</I>-GlcNAc transferase (OGT) is responsible for GlcNAc addition and <I>O</I>-GlcNAcase (OGA) is responsible for removal of the sugar. The lack of a rapid and simple method for monitoring OGT activity has impeded the efficient discovery of potent OGT inhibitors. In this study we describe a novel, single-well OGT enzyme assay that utilizes 6 × His-tagged substrates, a chemoselective chemical reaction, and unpurified OGT. The high-throughput Ni-NTA Plate OGT Assay will facilitate discovery of potent OGT-specific inhibitors on versatile substrates and the characterization of new enzyme variants.</P>