@article {1363141,
	title = {Detection of H2O2-mediated phosphorylation of kinase-inactive PDGFRα},
	journal = {Methods Enzymol},
	volume = {528},
	year = {2013},
	month = {2013},
	pages = {189-94},
	abstract = {Platelet-derived growth factor (PDGF) receptor α (PDGFRα) belongs to the 58-member family of receptor tyrosine kinases and contributes to a variety of physiological and pathological settings. Activation of PDGFRα proceeds by at least two mechanisms. The traditional route involves PDGF-dependent dimerization and activation of the receptor{\textquoteright}s intrinsic kinase activity. The second mechanism proceeds intracellularly and involves reactive oxygen species and Src family kinases, which activate monomeric PDGFRα. Herein we describe an assay to investigate reactive oxygen species-mediated phosphorylation of PDGFRα that is independent of the receptor{\textquoteright}s intrinsic kinase activity.},
	keywords = {Cell Line, Gene Expression Regulation, Humans, Hydrogen Peroxide, Immunoprecipitation, Mutation, Phosphorylation, Platelet-Derived Growth Factor, Reactive Oxygen Species, Receptor, Platelet-Derived Growth Factor alpha, Signal Transduction, Transfection},
	issn = {1557-7988},
	doi = {10.1016/B978-0-12-405881-1.00011-2},
	author = {Lei, Hetian and Kazlauskas, Andrius}
}
