FLEXIQinase, a mass spectrometry-based assay, to unveil multi-kinase mechanisms

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FLEXIQinase, a mass spectrometry-based assay, to unveil multi-kinase mechanisms

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Title: FLEXIQinase, a mass spectrometry-based assay, to unveil multi-kinase mechanisms
Author: Singh, Sasha Anna; Winter, Dominic; Bilimoria, Parizad Maheyar; Bonni, Azad; Steen, Hanno; Steen, Judith A.

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Citation: Singh, Sasha, Dominic Winter, Parizad M. Bilimoria, Azad Bonni, Hanno Steen, and Judith A. Steen. 2013. FLEXIQinase, a mass spectrometry-based assay, to unveil multi-kinase mechanisms. Nature Methods 9(5): 504-508.
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Abstract: We introduce a mass spectrometry-based method that provides residue-resolved quantitative information about protein phosphorylation. In this FLEXIQinase assay we combined our Full-Length Expressed Stable Isotope-labeled Protein for Quantification strategy (FLEXIQuant) with a traditional kinase assay to determine the mechanisms of multi-kinase substrate phosphorylation such as priming-dependent kinase activities. The assay monitors the decrease in signal intensity of the substrate peptides and the concomitant increase in the (n×80 Da)-shifted phosphorylated peptide. We analyzed the c-Jun N-terminal Kinase (JNK)-dependent glycogen synthase kinase 3β (GSK3β) activity on doublecortin (DCX) revealing mechanistic details about the role of phosphorylation cross-talk in GSK3β activity and permitting an advanced model for GSK3β-mediated signaling.
Published Version: doi:10.1038/nmeth.1970
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3595540/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:10605430
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