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- W2022087931 startingPage "154" @default.
- W2022087931 abstract "Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. While their functions in the ER have been thoroughly studied, much less is known about their roles in non-ER locations, where, however, they have been shown to be involved in important biological processes. At least three proteins of this family from higher vertebrates have been found in unusual locations (i.e., the cell surface, the extracellular space, the cytosol, and the nucleus), reached through an export mechanism which has not yet been understood. In some cases their function in the non-ER location is clearly related to their redox properties, but in most cases their mechanism of action has still to be disclosed, although their propensity to associate with other proteins or even with DNA might be the main factor responsible for their activities." @default.
- W2022087931 created "2016-06-24" @default.
- W2022087931 creator A5000910044 @default.
- W2022087931 creator A5025499313 @default.
- W2022087931 creator A5063258448 @default.
- W2022087931 creator A5084496226 @default.
- W2022087931 date "2002-10-16" @default.
- W2022087931 modified "2023-10-02" @default.
- W2022087931 title "Proteins of the PDI family: Unpredicted non-ER locations and functions" @default.
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