Design of Cell-Penetrating Domain Antibodies via a Genetically Encoded β-Lactam Amino Acid. [PDF]
Rabb JD, Kruse LE, Lin Q.
europepmc +1 more source
Hydrophobic tuning with non-canonical amino acids in a copper metalloenzyme. [PDF]
Fischer S +3 more
europepmc +1 more source
Cellular Site-Specific Incorporation of Noncanonical Amino Acids in Synthetic Biology. [PDF]
Niu W, Guo J.
europepmc +1 more source
Adding α,α-disubstituted and β-linked monomers to the genetic code of an organism. [PDF]
Dunkelmann DL +9 more
europepmc +1 more source
Genetic Code Expansion: Recent Developments and Emerging Applications. [PDF]
Huang Y +5 more
europepmc +1 more source
Directed evolution of aminoacyl-tRNA synthetases through in vivo hypermutation. [PDF]
Furuhata Y +3 more
europepmc +1 more source
Incorporation of Multiple β<sup>2</sup>-Hydroxy Acids into a Protein <i>In Vivo</i> Using an Orthogonal Aminoacyl-tRNA Synthetase. [PDF]
Hamlish NX +4 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
Engineering mutually orthogonal PylRS/tRNA pairs for dual encoding of functional histidine analogues
The availability of an expanded genetic code opens exciting new opportunities in enzyme design and engineering. In this regard histidine analogues have proven particularly versatile, serving as ligands to augment metalloenzyme function and as catalytic ...
Sarah Lovelock +2 more
exaly +2 more sources
Ancestral archaea expanded the genetic code with pyrrolysine [PDF]
The pyrrolysyl-tRNA synthetase (PylRS) facilitates the cotranslational installation of the 22nd amino acid pyrrolysine. Owing to its tolerance for diverse amino acid substrates, and its orthogonality in multiple organisms, PylRS has emerged as a major ...
Han-Kai Jiang, Takahito Mukai, Xian Fu
exaly +2 more sources

