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- W2023174812 startingPage "739" @default.
- W2023174812 abstract "Phosphorylation acts as a molecular switch for many regulatory events in signaling pathways that drive cell division, proliferation, and apoptosis. Because of the critical nature of these protein post-translational modifications in cancer, drug development programs often focus on inhibitors for kinases and phosphatases, which control protein phosphorylation. Numerous kinase inhibitors have entered clinical use, but prediction of their efficacy and a molecular basis for patient response remain uncertain. Chemical proteomics, the combination of drug affinity chromatography with mass spectrometry, identifies potential target proteins that bind to the drugs. Phosphorylation profiling can complement chemical proteomics by cataloging modifications in the target kinases and their downstream substrates using phosphopeptide enrichment and quantitative mass spectrometry. These experiments shed light on the mechanism of disease development and illuminate candidate biomarkers to guide personalized therapeutic strategies. In this review, commonly applied technologies and workflows are discussed to illustrate the role of proteomics in examining tumor biology and therapeutic intervention using kinase inhibitors." @default.
- W2023174812 created "2016-06-24" @default.
- W2023174812 creator A5002876951 @default.
- W2023174812 creator A5010264712 @default.
- W2023174812 creator A5059758317 @default.
- W2023174812 creator A5064494204 @default.
- W2023174812 creator A5076672524 @default.
- W2023174812 date "2010-09-01" @default.
- W2023174812 modified "2023-10-11" @default.
- W2023174812 title "Methods for investigation of targeted kinase inhibitor therapy using chemical proteomics and phosphorylation profiling" @default.
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- W2023174812 doi "https://doi.org/10.1016/j.bcp.2010.03.027" @default.
- W2023174812 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2995952" @default.