The Globular Domain of the Proα1(I) N-Propeptide Is Not Required for Secretion, Processing by Procollagen N-Proteinase, or Fibrillogenesis of Type I Collagen in Mice
Open Access
- 1 January 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (4) , 2605-2613
- https://doi.org/10.1074/jbc.m106181200
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Conformational Requirements of Collagenous Peptides for Recognition by the Chaperone Protein HSP47Journal of Biological Chemistry, 2000
- Substrate Recognition of Collagen-specific Molecular Chaperone HSP47Journal of Biological Chemistry, 1999
- Molecular recognition in procollagen chain assemblyMatrix Biology, 1998
- Expression and function of heat shock protein 47: A collagen-specific molecular chaperone in the endoplasmic reticulumMatrix Biology, 1998
- Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signalingMatrix Biology, 1998
- cDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix componentsProceedings of the National Academy of Sciences, 1997
- Identification of the molecular recognition sequence which determines the type-specific assembly of procollagenThe EMBO Journal, 1997
- Hsp47: a collagen-specific molecular chaperoneTrends in Biochemical Sciences, 1996
- Endoplasmic reticulum protein HSP47 binds specifically to the N‐Terminal globular domain of the amino‐propeptide of the procollagen I α1(I)‐chainJournal of Cellular Biochemistry, 1995
- COLLAGENS: Molecular Biology, Diseases, and Potentials for TherapyAnnual Review of Biochemistry, 1995