@article {35384,
	title = {A genetically encoded multifunctional unnatural amino acid for versatile protein manipulations in living cells},
	journal = {Chemical ScienceChemical Science},
	volume = {7},
	number = {12},
	year = {2016},
	pages = {7055-7060},
	publisher = {The Royal Society of Chemistry},
	type = {10.1039/C6SC02615J},
	abstract = {The genetic code expansion strategy allowed incorporation of unnatural amino acids (UAAs) bearing diverse functional groups into proteins, providing a powerful toolkit for protein manipulation in living cells. We report a multifunctional UAA, Nε-p-azidobenzyloxycarbonyl lysine (PABK), that possesses a panel of unique properties capable of fulfilling various protein manipulation purposes. In addition to being used as a bioorthogonal ligation handle, an infrared probe and a photo-affinity reagent, PABK was shown to be chemically decaged by trans-cyclooctenols via a strain-promoted 1,3-dipolar cycloaddition, which provides a new bioorthogonal cleavage strategy for intracellular protein activation. The biocompatibility and efficiency of this method were demonstrated by decaging of a PABK-caged firefly luciferase under living conditions. We further extended this method to chemically rescue a bacterial toxin OspF inside mammalian host cells.},
	isbn = {2041-6520},
	author = {Ge, Yun and Xinyuan Fan and Peng R. Chen}
}
