Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog.

@article{Rogerson2015EfficientGE,
  title={Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog.},
  author={Daniel T. Rogerson and A. Sachdeva and K. Wang and T. Haq and Agne Kazlauskaite and Susan M. Hancock and N. Huguenin-Dezot and M. M. Muqit and A. Fry and R. Bayliss and J. Chin},
  journal={Nature chemical biology},
  year={2015},
  volume={11 7},
  pages={
          496-503
        }
}
  • Daniel T. Rogerson, A. Sachdeva, +8 authors J. Chin
  • Published 2015
  • Biology, Medicine
  • Nature chemical biology
  • 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… CONTINUE READING
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