Abstract
We studied the intrinsic tyrosine kinase activity and substrate specificity of c-Abl and Bcr-Abl protein tyrosine kinases (PTKs) using the peptide substrates discovered from a synthetic combinatorial peptide library. Our data indicate that the phosphorylation of these peptides by Bcr-Abl was consistently stronger than that by c-Abl. Bcr-Abl also showed substrate preference towards those peptides with one or more positive charges.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2279-2284 |
| Number of pages | 6 |
| Journal | Bioorganic and Medicinal Chemistry Letters |
| Volume | 8 |
| Issue number | 17 |
| DOIs | |
| State | Published - Sep 8 1998 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Organic Chemistry
- Drug Discovery
- Pharmaceutical Science
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Cite this
Wu, J. J., Phan, H., & Lam, K. (1998). Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl. Bioorganic and Medicinal Chemistry Letters, 8(17), 2279-2284. https://doi.org/10.1016/S0960-894X(98)00413-2