Ontology highlight
ABSTRACT:
SUBMITTER: Rogerson DT
PROVIDER: S-EPMC4830402 | biostudies-literature | 2015 Jul
REPOSITORIES: biostudies-literature
Rogerson Daniel T DT Sachdeva Amit A Wang Kaihang K Haq Tamanna T Kazlauskaite Agne A Hancock Susan M SM Huguenin-Dezot Nicolas N Muqit Miratul M K MM Fry Andrew M AM Bayliss Richard R Chin Jason W JW
Nature chemical biology 20150601 7
Serine phosphorylation is a key post-translational modification that regulates diverse biological processes. Powerful analytical methods have identified thousands of phosphorylation sites, but many of their functions remain to be deciphered. A key to understanding the function of protein phosphorylation is access to phosphorylated proteins, but this is often challenging or impossible. Here we evolve an orthogonal aminoacyl-tRNA synthetase/tRNACUA pair that directs the efficient incorporation of ...[more]