@article{lee_kurra_yang_torres-kolbus_deiters_liu_2014, title={Genetically encoded unstrained olefins for live cell labeling with tetrazine dyes}, volume={50}, ISSN={["1364-548X"]}, DOI={10.1039/c4cc06435f}, abstractNote={A number of non-canonical amino acids (NCAAs) with unstrained olefins are genetically encoded using mutant pyrrolysyl-tRNA synthetase-tRNA(Pyl)(CUA) pairs. These NCAAs readily undergo inverse electron-demand Diels-Alder cycloadditions with tetrazine dyes, leading to selective labeling of proteins bearing these NCAAs in live cells.}, number={86}, journal={CHEMICAL COMMUNICATIONS}, author={Lee, Yan-Jiun and Kurra, Yadagiri and Yang, Yanyan and Torres-Kolbus, Jessica and Deiters, Alexander and Liu, Wenshe R.}, year={2014}, pages={13085–13088} }
 @article{lee_kurra_yang_torres-kolbus_deiters_liu_2014, title={Genetically encoded unstrained olefins for live cell labeling with tetrazine dyes (vol 50, pg 13085, 2014)}, volume={50}, ISSN={["1364-548X"]}, DOI={10.1039/c4cc90401j}, abstractNote={Correction for ‘Genetically encoded unstrained olefins for live cell labeling with tetrazine dyes’ by Yan-Jiun Lee et al., Chem. Commun., 2014, DOI: 10.1039/c4cc06435f.}, number={87}, journal={CHEMICAL COMMUNICATIONS}, author={Lee, Yan-Jiun and Kurra, Yadagiri and Yang, Yanyan and Torres-Kolbus, Jessica and Deiters, Alexander and Liu, Wenshe R.}, year={2014}, month={Nov}, pages={13396–13396} }
 @article{torres-kolbus_chou_liu_deiters_2014, title={Synthesis of Non-linear Protein Dimers through a Genetically Encoded Thiol-ene Reaction}, volume={9}, ISSN={["1932-6203"]}, DOI={10.1371/journal.pone.0105467}, abstractNote={Site-specific incorporation of bioorthogonal unnatural amino acids into proteins provides a useful tool for the installation of specific functionalities that will allow for the labeling of proteins with virtually any probe. We demonstrate the genetic encoding of a set of alkene lysines using the orthogonal PylRS/PylTCUA pair in Escherichia coli. The installed double bond functionality was then applied in a photoinitiated thiol-ene reaction of the protein with a fluorescent thiol-bearing probe, as well as a cysteine residue of a second protein, showing the applicability of this approach in the formation of heterogeneous non-linear fused proteins.}, number={9}, journal={PLOS ONE}, author={Torres-Kolbus, Jessica and Chou, Chungjung and Liu, Jihe and Deiters, Alexander}, year={2014}, month={Sep} }
 @article{kurra_odoi_lee_yang_lu_wheeler_torres-kolbus_deiters_liu_2014, title={Two Rapid Catalyst-Free Click Reactions for In Vivo Protein Labeling of Genetically Encoded Strained Alkene/Alkyne Functionalities}, volume={25}, ISSN={["1043-1802"]}, DOI={10.1021/bc500361d}, abstractNote={Detailed kinetic analyses of inverse electron-demand Diels–Alder cycloaddition and nitrilimine-alkene/alkyne 1,3-diploar cycloaddition reactions were conducted and the reactions were applied for rapid protein bioconjugation. When reacted with a tetrazine or a diaryl nitrilimine, strained alkene/alkyne entities including norbornene, trans-cyclooctene, and cyclooctyne displayed rapid kinetics. To apply these “click” reactions for site-specific protein labeling, five tyrosine derivatives that contain a norbornene, trans-cyclooctene, or cyclooctyne entity were genetically encoded into proteins in Escherichia coli using an engineered pyrrolysyl-tRNA synthetase-tRNACUAPyl pair. Proteins bearing these noncanonical amino acids were successively labeled with a fluorescein tetrazine dye and a diaryl nitrilimine both in vitro and in living cells.}, number={9}, journal={BIOCONJUGATE CHEMISTRY}, author={Kurra, Yadagiri and Odoi, Keturah A. and Lee, Yan-Jiun and Yang, Yanyan and Lu, Tongxiang and Wheeler, Steven E. and Torres-Kolbus, Jessica and Deiters, Alexander and Liu, Wenshe R.}, year={2014}, month={Sep}, pages={1730–1738} }
 @article{lang_davis_torres-kolbus_chou_deiters_chin_2012, title={Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction}, volume={4}, ISSN={["1755-4330"]}, DOI={10.1038/nchem.1250}, abstractNote={The site-specific incorporation of bioorthogonal groups via genetic code expansion provides a powerful general strategy for site-specifically labelling proteins with any probe. However, the slow reactivity of the bioorthogonal functional groups that can be encoded genetically limits the utility of this strategy. We demonstrate the genetic encoding of a norbornene amino acid using the pyrrolysyl tRNA synthetase/tRNACUA pair in Escherichia coli and mammalian cells. We developed a series of tetrazine-based probes that exhibit ‘turn-on’ fluorescence on their rapid reaction with norbornenes. We demonstrate that the labelling of an encoded norbornene is specific with respect to the entire soluble E. coli proteome and thousands of times faster than established encodable bioorthogonal reactions. We show explicitly the advantages of this approach over state-of-the-art bioorthogonal reactions for protein labelling in vitro and on mammalian cells, and demonstrate the rapid bioorthogonal site-specific labelling of a protein on the mammalian cell surface. The site-specific incorporation of a norbornene amino acid into proteins via genetic code expansion, together with the synthesis of a series of tetrazine-based probes that exhibit turn-on fluorescence on their fast cycloaddition with norbornene, enables rapid protein labelling on mammalian cells.}, number={4}, journal={NATURE CHEMISTRY}, author={Lang, Kathrin and Davis, Lloyd and Torres-Kolbus, Jessica and Chou, Chungjung and Deiters, Alexander and Chin, Jason W.}, year={2012}, month={Apr}, pages={298–304} }
 @article{arbely_torres-kolbus_deiters_chin_2012, title={Photocontrol of Tyrosine Phosphorylation in Mammalian Cells via Genetic Encoding of Photocaged Tyrosine}, volume={134}, ISSN={["0002-7863"]}, DOI={10.1021/ja3046958}, abstractNote={We report the first site-specific genetic encoding of photocaged tyrosine into proteins in mammalian cells. By photocaging Tyr701 of STAT1 we demonstrate that it is possible to photocontrol tyrosine phosphorylation and signal transduction in mammalian cells.}, number={29}, journal={JOURNAL OF THE AMERICAN CHEMICAL SOCIETY}, author={Arbely, Eyal and Torres-Kolbus, Jessica and Deiters, Alexander and Chin, Jason W.}, year={2012}, month={Jul}, pages={11912–11915} }