The absence of orthogonal aminoacyl-transfer RNA (tRNA) synthetases that accept non-l-α-
amino acids is a primary bottleneck hindering the in vivo translation of sequence-defined …

Site-specific incorporation of unnatural amino acids (Uaas) in living cells relies on
engineered aminoacyl-transfer RNA synthetase–tRNA pairs borrowed from a distant domain …

Reversible phosphorylation is a fundamental mechanism for controlling protein function.
Despite the critical roles phosphorylated proteins play in physiology and disease, our ability …

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

Site‐specific incorporation of multiple distinct noncanonical amino acids (ncAAs) into
proteins in mammalian cells is a promising technology, where each ncAA must be assigned …

Incorporation of more than one noncanonical amino acid (ncAA) within a single protein
endows the resulting construct with multiple useful features such as augmented molecular …

Understanding the post‐translational modifications of targeted proteins is of great
significance for manipulating the physiological processes of eukaryotes. Chemical biology …

Protein posttranslational modifications (PTMs) play critical roles in regulating cellular
activities. Here we provide a survey of genetic code expansion (GCE) methods that were …

Suppressor transfer RNAs (sup-tRNAs) are receiving renewed attention for their promising
therapeutic properties in treating genetic diseases caused by nonsense mutations …

Stop codon suppression using dedicated tRNA/aminoacyl-tRNA synthetase (aaRS) pairs
allows for genetically encoded, site-specific incorporation of non-canonical amino acids …