Quantitative affinity-based chemical proteomics of TrkA inhibitorsElectronic supplementary information (ESI) available: Preparation of affinity resin; recombinant protein pull-downs and competition with drug; TrkA enrichment from PC12 cells and competitive proteomics; MRM-based protein quantitation. See DOI: 10.1039/c2md00271j

Quantitative affinity-based chemical proteomics of TrkA inhibitorsElectronic supplementary information (ESI) available: Preparation of affinity resin; recombinant protein pull-downs and competition with drug; TrkA enrichment from PC12 cells and competitive proteomics; MRM-based protein quantitation. See DOI: 10.1039/c2md00271j

Quantitative chemical proteomics enabled affinity-isolation and enrichment of the tyrosine receptor kinase TrkA and protein isolation was competed by the inhibitors purvalanol B and staurosporine in a dose-related manner. These methods will advance occupancy biomarker development and our understandi...

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Hauptverfasser: Albrow, Victoria E, Fernandes, Carla, Beal, David M, Selby, Matthew D, Fernandez-Ocaa, Mireia, Rumpel, Klaus C, Jones, Lyn H
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Sprache:eng
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Zusammenfassung:Quantitative chemical proteomics enabled affinity-isolation and enrichment of the tyrosine receptor kinase TrkA and protein isolation was competed by the inhibitors purvalanol B and staurosporine in a dose-related manner. These methods will advance occupancy biomarker development and our understanding of TrkA biochemistry in disease. Quantitative chemical proteomics enabled the creation of an occupancy biomarker for the tyrosine receptor kinase TrkA
ISSN:2040-2503
2040-2511
DOI:10.1039/c2md00271j