[HTML][HTML] Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I …
A Colige, F Ruggiero, I Vandenberghe, J Dubail… - Journal of Biological …, 2005 - ASBMB
Processing of fibrillar collagens is required to generate collagen monomers able to self-
assemble into elongated and cylindrical collagen fibrils. ADAMTS-2 belongs to the" A
disintegrin and metalloproteinase with thrombospondin type 1 motifs"(ADAMTS) family. It is
responsible for most of the processing of the aminopropeptide of type I procollagen in the
skin, and it also cleaves type II and type III procollagens. ADAMTS are complex secreted
enzymes that are implicated in various physiological and pathological processes. Despite …
assemble into elongated and cylindrical collagen fibrils. ADAMTS-2 belongs to the" A
disintegrin and metalloproteinase with thrombospondin type 1 motifs"(ADAMTS) family. It is
responsible for most of the processing of the aminopropeptide of type I procollagen in the
skin, and it also cleaves type II and type III procollagens. ADAMTS are complex secreted
enzymes that are implicated in various physiological and pathological processes. Despite …