In recent years, powerful genetic code reprogramming methods have emerged that allow
new functional components to be embedded into proteins as noncanonical amino acid …

Various post-translational modifications can naturally occur on proteins, regulating the
activity, subcellular localization, interaction, or stability of the proteins. However, it can be …

Post‐translational modifications (PTMs) of proteins not only exponentially increase the
diversity of proteoforms, but also contribute to dynamically modulating the localization …

Post-translational modifications (PTMs) endow proteins with new properties to respond to
environmental changes or growth needs. With the development of advanced proteomics …

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 …

Over the past 16 years, genetic code expansion and reprogramming in living organisms has
been transformed by advances that leverage the unique properties of pyrrolysyl-tRNA …

Archaeal pyrrolysyl-tRNA synthetases (PylRSs) have been used to genetically encode over
200 distinct noncanonical amino acids (ncAAs) in proteins in Escherichia coli and …

Over 500 natural and synthetic amino acids have been genetically encoded in the last two
decades. Incorporating these noncanonical amino acids into proteins enables many …

Site-specific incorporation of distinct non-canonical amino acids into proteins via genetic
code expansion requires mutually orthogonal aminoacyl-tRNA synthetase/tRNA pairs …

Lysine acylation is a ubiquitous protein modification that controls various aspects of protein
function, such as the activity, localization, and stability of enzymes. Mass spectrometric …