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- W1965482690 abstract "The discovery of pyrrolysine not only expanded the set of the known proteinogenic amino acids but also revealed unusual features of its encoding mechanism. The engagement of a canonical stop codon and a unique aminoacyl-tRNA synthetase–tRNA pair that can be used to accommodate a broad range of unnatural amino acids while maintaining strict orthogonality in a variety of prokaryotic and eukaryotic expression systems has proven an invaluable combination. Within a few years since its properties were elucidated, the pyrrolysine translational machinery has become a popular choice for the synthesis of recombinant proteins bearing a wide variety of otherwise hard-to-introduce functional groups. It is also central to the development of new synthetic strategies that rely on stop-codon suppression." @default.
- W1965482690 created "2016-06-24" @default.
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- W1965482690 date "2011-06-01" @default.
- W1965482690 modified "2023-09-26" @default.
- W1965482690 title "The pyrrolysine translational machinery as a genetic-code expansion tool" @default.
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- W1965482690 doi "https://doi.org/10.1016/j.cbpa.2011.03.007" @default.
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