Post-translational modifications (PTMs) amplify diverse cellular functions by covalently adding functional groups such as phosphate, acetate, amide, or methyl groups to proteins. The PTM enzymes and resulting modifications are too numerous to list here. Phosphorylation, a common mechanism in regulating downstream cellular signaling (i.e., via kinases), is one of the most common PTMs. Many eukaryotic proteins can also be modified by glycosylation. Attaching carbohydrates to proteins is implicated in protein folding, improved stability and other regulatory functions such as signaling. Environmental or pathological conditions can lead to dysregulation of PTM activities resulting in the perturbation of the intracellular networks governed by each. As a result, PTM enzymes such as kinases and glycosyltransferases are targets or are starting to be targeted for drug development.
Traditional assay technologies such as mass spectrometry, or antibody-based techniques such as ELISA or western blotting are cumbersome and not easily amenable to high throughput drug discovery. We have developed a detection technology platform highly suitable to screening of PTM enzymatic activities when nucleotides are substrates or products. In this webinar we will demonstrate how cellular mechanisms driven by PTM can be addressed by analyzing the biochemical activities of the involved enzymes using a simple suite of bioluminescent nucleotide detection assays.
Hicham Zegzouti, PhD
Senior Research Scientist
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