A rapid method for determining protein kinase phosphorylation specificity
Top Cited Papers
- 29 September 2004
- journal article
- research article
- Published by Springer Nature in Nature Methods
- Vol. 1 (1) , 27-29
- https://doi.org/10.1038/nmeth708
Abstract
Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.Keywords
This publication has 14 references indexed in Scilit:
- An Oriented Peptide Array Library (OPAL) Strategy to Study Protein-Protein InteractionsJournal of Biological Chemistry, 2004
- Target Specificity Analysis of the Abl Kinase using Peptide Microarray DataJournal of Molecular Biology, 2004
- One‐thousand‐and‐one substrates of protein kinase CK2?The FASEB Journal, 2003
- The Protein Kinase Complement of the Human GenomeScience, 2002
- A motif-based profile scanning approach for genome-wide prediction of signaling pathwaysNature Biotechnology, 2001
- Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-AblBioorganic & Medicinal Chemistry Letters, 1998
- TGF-β SIGNAL TRANSDUCTIONAnnual Review of Biochemistry, 1998
- Determination of the Specific Substrate Sequence Motifs of Protein Kinase C IsozymesJournal of Biological Chemistry, 1997
- A Structural Basis for Substrate Specificities of Protein Ser/Thr Kinases: Primary Sequence Preference of Casein Kinases I and II, NIMA, Phosphorylase Kinase, Calmodulin-Dependent Kinase II, CDK5, and Erk1Molecular and Cellular Biology, 1996
- The specificity of the transforming growth factor beta receptor kinases determined by a spatially addressable peptide library.Proceedings of the National Academy of Sciences, 1995