Identification of an amino‐terminal substrate‐binding domain in theYersiniatyrosine phosphatase that is required for efficient recognition of focal adhesion targets
Author:
Affiliation:
1. Department of Molecular Genetics and Microbiology, School of Medicine, State University of New York at Stony Brook, Stony Brook, NY 11794‐5222, USA.
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-2958.1998.01014.x
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2. Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts.
3. Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
4. How pathogens expolit interactions mediated by SH3 domains
5. Inhibition of the Fc receptor‐mediated oxidative burst in macrophages by the Yersinia pseudotuberculosis tyrosine phosphatase;Bliska J.B.;Infect Immun,1995
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