Regulation of protein function through thiol-based redox switches plays an important role in
the response and adaptation to local and global changes in the cellular levels of reactive …

Inteins are nature's escape artists; they facilitate their excision from flanking polypeptides
(exteins) concomitant with extein ligation to produce a mature host protein. Splicing requires …

Intein-mediated protein splicing has become an essential tool in modern biotechnology.
Fundamental progress in the structure and catalytic strategies of cis-and trans-splicing …

Inteins are mobile genetic elements capable of self-splicing post-translationally. They exist
in all three domains of life including in viruses and bacteriophage, where they have a …

Self-cleaving affinity tags, based on engineered intein protein domains, have been touted as
a universal single step purification platform for tagless non-mAb proteins. These approaches …

Protein splicing is mediated by inteins that auto-catalytically join two separated protein
fragments with a peptide bond. Here we engineered a genetically encoded synthetic …

We introduce a new strategy for reduction in volumetric shrinkage of free radical
photopolymerization. Our strategy is based on the reversible reaction of disulfide bonds …

Cyclic peptides are important natural products and hold great promise for the identification of
new bioactive molecules. The split‐intein‐mediated SICLOPPS technology provides a …

Inteins are widespread self-splicing protein elements emerging as potential post-
translational environmental sensors. Here, we describe two inteins within one protein, the …

Split intein-mediated protein trans-splicing has found extensive applications in chemical
biology, protein chemistry, and biotechnology. However, an enduring limitation of all well …