Mechanism of the antichaperone activity of protein disulfide isomerase: facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDI.

Abstract

Protein disulfide isomerase (PDI), a folding catalyst and chaperone can, under certain conditions, facilitate the misfolding and aggregation of its substrates. This behavior, termed antichaperone activity [Puig, A., and Gilbert, H. F., (1994) J. Biol. Chem. 269, 25889] may provide a common mechanism for aggregate formation in the cell, both as a normal… (More)

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@article{Sideraki2000MechanismOT, title={Mechanism of the antichaperone activity of protein disulfide isomerase: facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDI.}, author={V Sideraki and Hiram F. Gilbert}, journal={Biochemistry}, year={2000}, volume={39 5}, pages={1180-8} }