Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl

Jinzi J. Wu; Hoang Phan; Kit Lam

doi:10.1016/S0960-894X(98)00413-2

Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl

Jinzi J. Wu, Hoang Phan, Kit Lam

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

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	https://doi.org/10.1016/S0960-894X(98)00413-2
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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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.",

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