Identification of Protein-tyrosine Phosphatase 1B as the Major Tyrosine Phosphatase Activity Capable of Dephosphorylating and Activating c-Src in Several Human Breast Cancer Cell Lines-Reference-Cited by-同舟云学术

Identification of Protein-tyrosine Phosphatase 1B as the Major Tyrosine Phosphatase Activity Capable of Dephosphorylating and Activating c-Src in Several Human Breast Cancer Cell Lines

Published:2000-12 Issue:52 Volume:275 Page:41439-41446
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bjorge Jeffrey D.,Pang Andrew,Fujita Donald J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference67 articles.

1. CELLULAR FUNCTIONS REGULATED BY SRC FAMILY KINASES

2. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src

3. The Csk-like proteins Lsk, Hyl, and Matk represent the same Csk homologous kinase (Chk) and are regulated by stem cell factor in the megakaryoblastic cell line MO7e

4. Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src.

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