High‐Throughput Identification of Substrate Specificity for Protein Kinase by Using an Improved One‐Bead‐One‐Compound Library Approach
- 2 July 2007
- journal article
- research article
- Published by Wiley in Angewandte Chemie International Edition in English
- Vol. 46 (28) , 5408-5411
- https://doi.org/10.1002/anie.200700195
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Image Subtraction Approach to Screening One-Bead-One-Compound Combinatorial Libraries with Complex Protein MixturesJournal of Combinatorial Chemistry, 2006
- Global Kinase Screening. Applications of Frontal Affinity Chromatography Coupled to Mass Spectrometry in Drug DiscoveryAnalytical Chemistry, 2005
- Novel at the libraryNature Methods, 2004
- A Novel and Rapid Encoding Method Based on Mass Spectrometry for “One-Bead-One-Compound” Small Molecule Combinatorial LibrariesJournal of the American Chemical Society, 2003
- A colorimetric enzyme‐linked on‐bead assay for identification of synthetic substrates of protein tyrosine kinasesJournal of Peptide Science, 2002
- Protein tyrosine kinases: Structure, substrate specificity, and drug discoveryBiopolymers, 1998
- A Novel Phosphotyrosine-binding Domain in the N-terminal Transforming Region of Cbl Interacts Directly and Selectively with ZAP-70 in T CellsJournal of Biological Chemistry, 1996
- Catalytic specificity of protein-tyrosine kinases is critical for selective signallingNature, 1995
- ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity.The Journal of Experimental Medicine, 1995
- A new type of synthetic peptide library for identifying ligand-binding activityNature, 1991