@misc{10481/67274,
year = {2020},
month = {9},
url = {http://hdl.handle.net/10481/67274},
abstract = {This Communication reports the first general method for rapid, chemoselective, and modular functionalization of serine residues in native polypeptides, which uses a reagent platform based on the P(V) oxidation state. This redox-economical approach can be used to append nearly any kind of cargo onto serine, generating a stable, benign, and hydrophilic phosphorothioate linkage. The method tolerates all other known nucleophilic functional groups of naturally occurring proteinogenic amino acids. A variety of applications can be envisaged by this expansion of the toolbox of site-selective bioconjugation methods.},
organization = {Financial support for this work was provided by the Marie Skłodow-ska-Curie Global Fellowships (749359-EnanSET, N.M.P) within the European Union research and inno-vation framework programme (2014-2020)},
publisher = {American Chemical Society},
title = {Serine-Selective Bioconjugation},
doi = {https://pubs.acs.org/doi/10.1021/jacs.0c05595},
author = {Vantourout, Julien C and Rao Adusumalli, Srinivasa and Knouse, Kyle W. and Flood, Dillon and Ramirez, Antonio and Muñoz Padial, Natalia and Israte, Alena and Maziarz, Katarzyna and deGruyter, Justine N. and Merchant, Rohan R. and Qiao, Jennifer X. and Schmidt, Michael A. and Deery, Michael J. and Eastgate, Martin D. and Dawson, Philip E. and Bernardes, Gonçalo J. L. and Baran, Phil S.},
}