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Among the hundreds of posttranslational modifications, limited proteolysis, also known as processing, is special: It is irreversible, near ubiquitous, and by trimming peptide chains from their ends or cutting proteins into two, proteolysis forms shorter chains displaying new termini. The unique chemistry and location of α-amino-termini and carboxyl-termini in a protein engender special chemical and physical properties to a protein. Hence, modification of protein termini is often associated with new biological activities of a protein. We highlight recent proteomic developments enabling high throughput identification of protein termini. This has revolutionized degradomics and protein characterization by mapping the specificity of terminal modifications and of proteases, and has been used to directly identify new protease substrates and molecular pathways altered by proteolysis. [ABSTRACT FROM AUTHOR]

: Network modeling of interactions between proteases and their inhibitors reveals a network of new protein connections and cascades in the protease web. [ABSTRACT FROM AUTHOR]