Sumoylation is an essential post-translational modification that is catalysed by a small
number of modifying enzymes but regulates thousands of target proteins in a dynamic …

The native chemical ligation reaction (NCL) involves reacting a C-terminal peptide thioester
with an N-terminal cysteinyl peptide to produce a native peptide bond between the two …

Protein semisynthesis—defined herein as the assembly of a protein from a combination of
synthetic and recombinant fragments—is a burgeoning field of chemical biology that has …

Both ubiquitination and SUMOylation are dynamic post-translational modifications that
regulate thousands of target proteins to control virtually every cellular process …

Nature has developed a plethora of protein machinery to operate and maintain nearly every
task of cellular life. These processes are tightly regulated via post‐expression modifications …

Organic chemistry allows for the modification and chemical preparation of protein analogues
for various studies. The thiolate side chain of the Cys residue has been a key functionality in …

A mild, organophotocatalytic N–O bond cleavage of Weinreb amides is disclosed, thereby
expanding the chemistry of this venerable motif beyond acylation. This redox neutral …

Histone ubiquitination affects the structure and function of nucleosomes through tightly
regulated dynamic reversible processes. The efficient preparation of ubiquitinated histones …

Posttranslational modification of proteins by ubiquitin (Ub), ie, ubiquitination, mediates a
variety of cellular processes, including protein homeostasis, cell cycle, DNA repair, and viral …

S-to-N acyl transfer is a high-yielding chemoselective process for amide bond formation. It is
widely utilized by chemists for synthetic applications, including peptide and protein …