@inbook{a7a070ce8e394879923812948b801bf3,
title = "Quantification of cell signaling networks using kinase activity chemosensors",
abstract = "The ability to directly determine endogenous kinase activity in tissue homogenates provides valuable insights into signaling aberrations that underlie disease phenotypes. When activity data is collected across a panel of kinases, a unique “signaling fingerprint” is generated that allows for discrimination between diseased and normal tissue. Here we describe the use of peptide-based kinase activity sensors to fingerprint the signaling changes associated with disease states. This approach leverages the phosphorylation-sensitive sulfonamido-oxine (Sox) fluorophore to provide a direct readout of kinase enzymatic activity in unfractionated tissue homogenates from animal models or clinical samples. To demonstrate the application of this technology, we focus on a rat model of nonalcoholic fatty liver disease (NAFLD). Sox-based activity probes allow for the rapid and straightforward analysis of changes in kinase enzymatic activity associated with disease states, providing leads for further investigation using traditional biochemical approaches.",
keywords = "Cell signaling, Fluorescence-based biosensor, Kinase activity assay, Nonalcoholic fatty liver disease, Phosphorylation",
author = "Beck, {Jon R.} and Harris, {Edward N.} and Stains, {Cliff I.}",
note = "Funding Information: This work was funded by the University of Nebraska–Lincoln and the Nebraska Research Initiative. Publisher Copyright: {\textcopyright} 2017, Springer Science+Business Media LLC.",
year = "2017",
doi = "10.1007/978-1-4939-7154-1_4",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "61--70",
booktitle = "Methods in Molecular Biology",
}