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- W2106983325 abstract "Abstract The study of protein kinases has become a matter of great importance in the development of new drugs for the treatment of diseases, including cancer and inflammation. Substrate screening is the first step in the fundamental investigation of protein kinases and the development of inhibitors for use in drug discovery. Towards this goal, various studies have been reported regarding the development of phospho‐peptide detection methods and the screening of phosphorylated peptide sites by protein kinases. This review introduces the detection methods for phosphorylation events using the reagents with (γ 32 P)ATP, ligand‐linked ATP, phospho‐peptide‐specific antibodies and metal chelating compounds. Chemical modification methods using β‐elimination for the detection of phospho‐Ser/Thr peptides are introduced as well. In addition, the implementations of combinatorial peptide libraries for screening peptide substrates of protein kinases are discussed. The phage display approach has been suggested as an alternative method of using synthetic peptides for screening the substrate specificities of protein kinase. However, a solid phase assay using a peptide library‐bound polymer resin or a peptide‐arrayed glass chip is preferred for high throughput screening (HTS). © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 753–762, 2010. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com" @default.
- W2106983325 created "2016-06-24" @default.
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- W2106983325 date "2010-01-01" @default.
- W2106983325 modified "2023-09-23" @default.
- W2106983325 title "Substrate screening of protein kinases: Detection methods and combinatorial peptide libraries" @default.
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