Sequence-specific Recognition of Collagen Triple Helices by the Collagen-specific Molecular Chaperone HSP47
Open Access
- 1 September 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (38) , 35007-35012
- https://doi.org/10.1074/jbc.m202782200
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternaeThe Journal of cell biology, 2001
- Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed StructureJournal of Biological Chemistry, 2001
- HSP47 Binds Cooperatively to Triple Helical Type I Collagen but Has Little Effect on the Thermal Stability or Rate of RefoldingPublished by Elsevier ,2001
- Conformational Requirements of Collagenous Peptides for Recognition by the Chaperone Protein HSP47Journal of Biological Chemistry, 2000
- Procollagen Traverses the Golgi Stack without Leaving the Lumen of Cisternae: Evidence for Cisternal MaturationPublished by Elsevier ,1998
- Protein disulfide Isomerase Acts as a Molecular Chaperone during the Assembly of ProcollagenJournal of Biological Chemistry, 1998
- Hsp47: a collagen-specific molecular chaperoneTrends in Biochemical Sciences, 1996
- Coexpression of the collagen-binding stress protein HSP47 gene and the alpha 1(I) and alpha 1(III) collagen genes in carbon tetrachloride-induced rat liver fibrosis.Journal of Clinical Investigation, 1994
- Procollagen is more stable in cellulo than in vitroEuropean Journal of Biochemistry, 1984
- Folding Mechanism of the Triple Helix in Type‐III Collagen and Type‐III pN–CollagenEuropean Journal of Biochemistry, 1980