Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen.

@article{Wilson1998ProteinDI,
  title={Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen.},
  author={Rebecca R Wilson and Joanne Lees and Neil J Bulleid},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 16},
  pages={9637-43}
}
Protein-disulfide isomerase (PDI) has been shown to be a multifunctional enzyme catalyzing the formation of disulfide bonds, as well as being a component of the enzymes prolyl 4-hydroxylase (P4-H) and microsomal triglyceride transfer protein. It has also been proposed to function as a molecular chaperone during the refolding of denatured proteins in vitro. To investigate the role of this multifunctional protein within a cellular context, we have established a semi-permeabilized cell system that… CONTINUE READING
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