Inhibitor-based affinity probes for the investigation of JAK signaling pathways

Hoefener M, Pachl F, Kuster B, Sewald N (2015)
PROTEOMICS 15(17): 3066-3074.

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Abstract
The Janus Kinase (JAK) signaling pathway plays a key role for many cellular processes and has recently been correlated with neuronal disorders. In order to understand new links of JAK family members with other signaling pathways, chemical proteomics tools with broad kinase coverage are desirable. A probe that shows outstanding kinase selectivity and allows for the enrichment of up to 133 kinases including many mitogen activated kinase (MAPK) members and JAK kinases has been developed. Furthermore, this probe was applied to establish the selectivity profile of the JAK1/2 inhibitor momelotinib that is currently evaluated in clinical phase 3 studies. These results render this probe a valuable tool for the investigation of JAK and JAK related signaling pathways and the selectivity profiling of kinase inhibitors.
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Hoefener M, Pachl F, Kuster B, Sewald N. Inhibitor-based affinity probes for the investigation of JAK signaling pathways. PROTEOMICS. 2015;15(17):3066-3074.
Hoefener, M., Pachl, F., Kuster, B., & Sewald, N. (2015). Inhibitor-based affinity probes for the investigation of JAK signaling pathways. PROTEOMICS, 15(17), 3066-3074. doi:10.1002/pmic.201400324
Hoefener, M., Pachl, F., Kuster, B., and Sewald, N. (2015). Inhibitor-based affinity probes for the investigation of JAK signaling pathways. PROTEOMICS 15, 3066-3074.
Hoefener, M., et al., 2015. Inhibitor-based affinity probes for the investigation of JAK signaling pathways. PROTEOMICS, 15(17), p 3066-3074.
M. Hoefener, et al., “Inhibitor-based affinity probes for the investigation of JAK signaling pathways”, PROTEOMICS, vol. 15, 2015, pp. 3066-3074.
Hoefener, M., Pachl, F., Kuster, B., Sewald, N.: Inhibitor-based affinity probes for the investigation of JAK signaling pathways. PROTEOMICS. 15, 3066-3074 (2015).
Hoefener, Michael, Pachl, Fiona, Kuster, Bernhard, and Sewald, Norbert. “Inhibitor-based affinity probes for the investigation of JAK signaling pathways”. PROTEOMICS 15.17 (2015): 3066-3074.
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