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

Access to Document

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

Cite this

@article{fa9b7a3a112b43efb098bc71b89bb690,

title = "Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl",

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.",

author = "Wu, {Jinzi J.} and Hoang Phan and Kit Lam",

year = "1998",

month = sep,

day = "8",

doi = "10.1016/S0960-894X(98)00413-2",

language = "English (US)",

volume = "8",

pages = "2279--2284",

journal = "Bioorganic and Medicinal Chemistry Letters",

issn = "0960-894X",

publisher = "Elsevier Limited",

number = "17",

}

TY - JOUR

T1 - Comparison of the intrinsic kinase activity and substrate specificity of c-Abl and Bcr-Abl

AU - Wu, Jinzi J.

AU - Phan, Hoang

AU - Lam, Kit

PY - 1998/9/8

Y1 - 1998/9/8

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0032497398&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032497398&partnerID=8YFLogxK

U2 - 10.1016/S0960-894X(98)00413-2

DO - 10.1016/S0960-894X(98)00413-2

M3 - Article

C2 - 9873528

AN - SCOPUS:0032497398

VL - 8

SP - 2279

EP - 2284

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

SN - 0960-894X

IS - 17

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this