Substrate Recognition of Collagen-specific Molecular Chaperone HSP47

This publication has 28 references indexed in Scilit:

• Effect of HSP47 on Prolyl 4-Hydroxylation of Collagen Model Peptides.
  Cell Structure and Function, 1999
• Protein disulfide Isomerase Acts as a Molecular Chaperone during the Assembly of Procollagen
  Journal of Biological Chemistry, 1998
• Molecular chaperones in cellular protein folding
  Nature, 1996
• Hsp47: a collagen-specific molecular chaperone
  Trends in Biochemical Sciences, 1996
• Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
  Cell, 1995
• 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
• Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
  The Journal of cell biology, 1992
• The Biosynthesis of Collagen and Its Disorders
  New England Journal of Medicine, 1979
• An Affinity‐Column Procedure Using Poly(l‐proline) for the Purification of Prolyl Hydroxylase
  European Journal of Biochemistry, 1975
• Synthesis of Poly-(l-prolyl-l-prolylglycyl) of Defined Molecular Weights
  Bulletin of the Chemical Society of Japan, 1968