Bi-Domain Protein Tyrosine Phosphatases Reveal an Evolutionary Adaptation to Optimize Signal Transduction
Author:
Affiliation:
1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
2. Department of Pharmacology, University of California, San Diego, La Jolla, California.
Publisher
Mary Ann Liebert Inc
Subject
Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry
Link
http://www.liebertpub.com/doi/pdf/10.1089/ars.2013.5721
Reference138 articles.
1. Structural genomics of protein phosphatases
2. Protein Tyrosine Phosphatases in the Human Genome
3. Furin-, ADAM 10-, and γ-Secretase-Mediated Cleavage of a Receptor Tyrosine Phosphatase and Regulation of β-Catenin's Transcriptional Activity
4. Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains
5. Structure of a Tyrosine Phosphatase Adhesive Interaction Reveals a Spacer-Clamp Mechanism
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