Protein-specific chaperones: The role of hsp47 begins to gel
- 1 December 2000
- journal article
- review article
- Published by Elsevier in Current Biology
- Vol. 10 (24) , R912-R915
- https://doi.org/10.1016/s0960-9822(00)00850-2
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Embryonic Lethality of Molecular Chaperone Hsp47 Knockout Mice Is Associated with Defects in Collagen BiosynthesisThe Journal of cell biology, 2000
- Procollagen folding and assembly: The role of endoplasmic reticulum enzymes and molecular chaperonesSeminars in Cell & Developmental Biology, 1999
- 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
- Quality control in the secretory pathwayCurrent Opinion in Cell Biology, 1995
- BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulumCellular and Molecular Life Sciences, 1994
- Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiPCell, 1993
- Collagens and their Abnormalities in a Wide Spectrum of DiseasesAnnals of Medicine, 1993
- Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulumThe Journal of cell biology, 1992
- Prolyl 4-hydroxylase and its role in collagen synthesisJournal of Hepatology, 1991