Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling
- 1 February 1998
- journal article
- review article
- Published by Elsevier in Matrix Biology
- Vol. 16 (7) , 399-408
- https://doi.org/10.1016/s0945-053x(98)90013-0
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- The family of procollagen n-proteinases: Molecular cloning, expression and localisation of a novel member, a putative metallopeptidase of 33 kDa (PRSM-1)Matrix Biology, 1996
- The role of sea urchin embryo BMP-1 in skeleton assemblyMatrix Biology, 1996
- Structure of the Type I Collagen Molecule Based on Conformational Energy Computations: The Triple-stranded Helix and the N-terminal Telopep tideJournal of Molecular Biology, 1995
- Evidence for a Triple Helix Recognition Site in the Hemopexin‐like Domains of Human Fibroblast and Neutrophil Interstitial CollagenasesaAnnals of the New York Academy of Sciences, 1994
- Surface-induced aggregation of type I procollagenJournal of Molecular Biology, 1987
- Heritable Diseases of CollagenNew England Journal of Medicine, 1984
- The Biosynthesis of Collagen and Its DisordersNew England Journal of Medicine, 1979
- The Biosynthesis of Collagen and Its DisordersNew England Journal of Medicine, 1979
- Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagenBiochemistry, 1978
- Procollagen peptidase: Its mode of action on the native substrateCell, 1975