Transferability of N-terminal mutations of pyrrolysyl-tRNA synthetase in one species to that in another species on unnatural amino acid incorporation efficiency. [PDF]
Williams TL +5 more
europepmc +1 more source
Engineering a promiscuous pyrrolysyl-tRNA synthetase by a high throughput FACS screen
The Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNAPyl are used to facilitate the incorporation of non-canonical amino acids (ncAAs) into the genetic code of bacterial and eukaryotic cells by orthogonally reassigning the amber codon.
Michael Groll +9 more
core +1 more source
Engineered triply orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs enable the genetic encoding of three distinct non-canonical amino acids. [PDF]
Dunkelmann DL +3 more
europepmc +1 more source
Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion. [PDF]
Koch NG, Budisa N.
europepmc +1 more source
Engineering a Polyspecific Pyrrolysyl-tRNA Synthetase by a High Throughput FACS Screen. [PDF]
Hohl A +8 more
europepmc +1 more source
Mutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs. [PDF]
Willis JCW, Chin JW.
europepmc +1 more source
Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase. [PDF]
Suzuki T +7 more
europepmc +1 more source
An Evolved Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase/tRNA Pair Is Highly Active and Orthogonal in Mammalian Cells. [PDF]
Beránek V, Willis JCW, Chin JW.
europepmc +1 more source
Evolving the N-Terminal Domain of Pyrrolysyl-tRNA Synthetase for Improved Incorporation of Noncanonical Amino Acids. [PDF]
Sharma V +5 more
europepmc +1 more source
An efficient pyrrolysyl-tRNA synthetase for economical production of MeHis-containing enzymes.
Hutton AE +7 more
europepmc +1 more source

