The mammalian proprotein convertases constitute a family of nine secretory serine
proteases that are related to bacterial subtilisin and yeast kexin. Seven of these (proprotein …

Pro-opiomelanocortin (POMC) is the archetypal polypeptide precursor of hormones and
neuropeptides. In this review, we examine the variability in the individual peptides produced …

Proteases enzymatically hydrolyze peptide bonds in substrate proteins, resulting in a
widespread, irreversible posttranslational modification of the protein's structure and …

Many viruses have membrane glycoproteins that are activated at cleavage sites containing
multiple arginine and lysine residues by cellular proteases so far not identified. The …

Previous work demonstrated that human furin is a predominantly Golgi membrane-localized
endoprotease that can efficiently process precursor proteins at paired basic residues (-Lys …

Limited endoproteolysis of inactive precursor proteins at sites marked by paired or multiple
basic amino acids is a widespread process by which biologically active peptides and …

Proproteins and prohormones are the fundamental units from which bioactive proteins and
peptides as well as neuropeptides are derived by limited proteolysis within the secretory …

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A recombinant vaccinia virus vector was used to coexpress the two candidate mouse
prohormone convertases, PC1 and PC2, together with mouse proopiomelanocortin (POMC) …

Many peptide hormones are produced from larger precursors by endoproteolysis at pairs of
basic amino acids (eg Lys-Arg and Arg-Arg) within the regulated secretory pathway in …