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Identifying Selective Protein Tyrosine Phosphatase Substrates and Inhibitors from a Fluorogenic, Combinatorial Peptide Library
Author(s) -
Mitra Sayantan,
Barrios Amy M.
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800046
Subject(s) - protein tyrosine phosphatase , phosphatase , tyrosine , peptide , substrate (aquarium) , peptide library , biochemistry , enzyme , computational biology , selectivity , biology , chemistry , gene , peptide sequence , ecology , catalysis
Protein tyrosine phosphatases are increasingly recognized as enzymes that exhibit exquisite substrate selectivity with important roles in cellular signaling, and have been identified as attractive therapeutic targets in human diseases including autoimmunity, obesity, diabetes, and cancer. A new approach was developed to rapidly and efficiently profile the substrate selectivity of protein tyrosine phosphatase and is described herein.