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A multiplexed NMR-reporter approach to measure cellular kinase and phosphatase activities in real-time

Official URL:https://doi.org/10.1021/jacs.5b02987
PubMed:View item in PubMed
Creators Name:Thongwichian, R. and Kosten, J. and Benary, U. and Rose, H.M. and Stuiver, M. and Theillet, F.X. and Dose, A. and Koch, B. and Yokoyama, H. and Schwarzer, D. and Wolf, J. and Selenko, P.
Journal Title:Journal of the American Chemical Society
Journal Abbreviation:J Am Chem Soc
Volume:137
Number:20
Page Range:6468-6471
Date:27 May 2015
Keywords:Biomolecular Nuclear Magnetic Resonance, Enzyme Activation, K562 Cells, Phosphoric Monoester Hydrolases, Phosphotransferases, Protein Kinase Inhibitors, Structure-Activity Relationship, Time Factors
Abstract:Cell signaling is governed by dynamic changes in kinase and phosphatase activities, which are difficult to assess with discontinuous readout methods. Here, we introduce an NMR-based reporter approach to directly identify active kinases and phosphatases in complex physiological environments such as cell lysates and to measure their individual activities in a semicontinuous fashion. Multiplexed NMR profiling of reporter phosphorylation states provides unique advantages for kinase inhibitor studies and reveals reversible modulations of cellular enzyme activities under different metabolic conditions.
ISSN:0002-7863
Publisher:American Chemical Society (U.S.A.)
Item Type:Article

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