Ontology highlight
ABSTRACT:
SUBMITTER: Allen JJ
PROVIDER: S-EPMC2943827 | biostudies-literature | 2005 Apr
REPOSITORIES: biostudies-literature
Allen Jasmina J JJ Lazerwith Scott E SE Shokat Kevan M KM
Journal of the American Chemical Society 20050401 15
Protein phosphorylation is a major mechanism of post-translational protein modification used to control cellular signaling. A challenge in phosphoproteomics is to identify the direct substrates of each protein kinase. Herein, we describe a chemical strategy for delivery of a bio-orthogonal affinity tag to the substrates of an individual protein kinase. The kinase of interest is engineered to transfer a phosphorothioate moiety to phosphoacceptor hydroxyl groups on direct substrates. In a second n ...[more]