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High‐Throughput Identification of Substrate Specificity for Protein Kinase by Using an Improved One‐Bead‐One‐Compound Library Approach
Author(s) -
Kim YunGon,
Shin DongSik,
Kim EunMi,
Park HyungYeon,
Lee ChangSoo,
Kim JuneHyung,
Lee BonSu,
Lee YoonSik,
Kim ByungGee
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200700195
Subject(s) - substrate (aquarium) , identification (biology) , throughput , bead , peptide library , function (biology) , computational biology , computer science , chemistry , information retrieval , biology , biochemistry , microbiology and biotechnology , gene , materials science , peptide sequence , telecommunications , botany , ecology , composite material , wireless
Pick and choose : The identification of the substrate specificity of a protein kinase is critical in understanding its role and function in a cellular signal transduction network. A high‐throughput platform was developed for the identification of tyrosine kinase substrate specificity by using an improved one‐bead‐one‐compound ladder peptide library and MALDI‐TOF MS.