Enzymatic Characterization of Recombinant Enzymes of O-GlcNAc Cycling
The dynamic addition of O -GlcNAc to target proteins is now recognized as a majo
The dynamic addition of O -GlcNAc to target proteins is now recognized as a major signaling paradigm impacting phosphorylation, protein turnover, gene expression, and other posttranslational modifications influencing epigenetics. Here we describe the production of and methods for assay of the recombinant enzymes of O -GlcNAc cycling: O -linked GlcNAc Transferase (OGT) and O -GlcNAcase (OGA).
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Determining Allosteric Modulator Mechanism of Action: Integration of Radioligand Binding and Functio
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Synthesis, Mass Spectrometric Characterization, and Analysis of the PPAR Agonist GW1516 and Its Majo
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