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High-throughput identification of substrate specificity for protein kinase by using an improved one-bead-one-compound library approach

Authors
Kim, YG (Kim, Yun-Gon)Shin, DS (Shin, Dong-Sik)Kim, EM (Kim, Eun-Mi)Park, HY (Park, Hyung-Yeon)Lee, CS (Lee, Chang-Soo)Kim, JH (Kim, June-Hyung)Lee, BS (Lee, Bon-Su)Lee, YS (Lee, Yoon-Sik)Kim, BG (Kim, Byung-Gee)
Issue Date
Jul-2007
Publisher
WILEY-V C H VERLAG GMBH
Keywords
enzymes; high-throughput screening; mass spectrometry; peptides; substrate specificity
Citation
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, v.46, no.28, pp.5408 - 5411
Journal Title
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume
46
Number
28
Start Page
5408
End Page
5411
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/148494
DOI
10.1002/anie.200700195
ISSN
1433-7851
Abstract
(Graph Presented) 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.
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