title: Sensitive label-free monitoring of protein kinase activity and inhibition using ferric ions coordinated to phosphorylated sites as electrocatalysts.
abstract: Ferric ions show high affinity to the kinase-generated phosphorylated sites of peptides. Thus, the high electrocatalytic activity of the coordinated ferric ions toward the reduction of hydrogen peroxide can be used for sensitive label-free monitoring of protein kinase activity and inhibition.
authors: State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210093, China. xhxia@nju.edu.cn.
authors: Min
authors: M
authors: Wang
authors: Gui-Xia
authors: GX
authors: Wang
authors: Fang-Nan
authors: FN
authors: Xiao
authors: Yun
authors: Y
authors: Zhao
authors: Kang
authors: K
authors: Wang
authors: Xing-Hua
authors: XH
authors: Xia
mesh_terms: D000595:Amino Acid Sequence; D017868:Cyclic AMP-Dependent Protein Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D055664:Electrochemical Techniques / Q000379:methods; D057075:Enzyme Assays / Q000379:methods; D005290:Ferric Compounds / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D007477:Ions / Q000378:metabolism; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation
chemical_list: D005290:Ferric Compounds; D007477:Ions; D010455:Peptides; D006861:Hydrogen Peroxide; D017868:Cyclic AMP-Dependent Protein Kinases