In protein trans-splicing, an intein domain split into two polypeptide chains mediates linkage
of the flanking amino acid sequences, the N-and C-terminal exteins, with a native peptide …

Protein splicing is an intricate self-catalyzed protein rearrangement that converts an inactive
protein precursor to biologically active proteins. In the past decade, mechanistic studies and …

The judicious application of intein technologies to biological problems has resulted in
powerful tools for biomedical research. Inteins are intervening sequences that excise …

Protein trans-splicing by split inteins holds great potential for the chemical modification and
semisynthesis of proteins. However, the structural requirements of the extein sequences …

Intein‐based protein cleavages, if carried out in a controllable way, can be useful tools of
recombinant protein purification, ligation, and cyclization. However, existing methods using …

Protein trans-splicing using split inteins is a powerful and convenient reaction to chemically
modify recombinantly expressed proteins under mild conditions. In particular, semisynthetic …

Inteins are autocatalytic protein domains that post-translationally excise from protein
precursors and ligate their flanking regions with a peptide bond, in a process called protein …

Inteins are intervening protein domains with self-splicing ability that can be used as
molecular switches to control activity of their host protein. Successfully engineering an intein …

A split‐intein consists of two complementary fragments (N‐intein and C‐intein) that can
associate to carry out protein trans‐splicing. The Ssp GyrB S11 split‐intein is an engineered …

Protein splicing is a naturally occurring process in which a protein editor, called an intein,
performs a molecular disappearing act by cutting itself out of a host protein in a traceless …