Ontology highlight
ABSTRACT:
SUBMITTER: Allen JJ
PROVIDER: S-EPMC2932705 | biostudies-literature | 2007 Jun
REPOSITORIES: biostudies-literature
Allen Jasmina J JJ Li Manqing M Brinkworth Craig S CS Paulson Jennifer L JL Wang Dan D Hübner Anette A Chou Wen-Hai WH Davis Roger J RJ Burlingame Alma L AL Messing Robert O RO Katayama Carol D CD Hedrick Stephen M SM Shokat Kevan M KM
Nature methods 20070507 6
The ubiquitous nature of protein phosphorylation makes it challenging to map kinase-substrate relationships, which is a necessary step toward defining signaling network architecture. To trace the activity of individual kinases, we developed a semisynthetic reaction scheme, which results in the affinity tagging of substrates of the kinase in question. First, a kinase, engineered to use a bio-orthogonal ATPgammaS analog, catalyzes thiophosphorylation of its direct substrates. Second, alkylation of ...[more]