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Cited by 524

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The protein disulphide-isomerase family: unravelling a string of folds

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David M. Ferrari, Hans‐Dieter Söling·1999·Biochemical Journal

Abstract

The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys- tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins, including peptide binding, cell adhesion and perhaps chaperone activities. Attention is now turning to the non-redox-active domains of the PDIs, which may play an important role in all of the known activities of these proteins. Thus the presence of both redox-active and -inactive domains within these proteins portends a complexity of functions differentially accommodated by the various family members.

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Metadata

Authors
Ferrari, D. M., & Söling, H.
Venue
Biochemical Journal
Publisher
Portland Press
Published
1999-03-25
Volume
339
Issue
1
Pages
1-1
ISSN
0264-6021 (ISSN-L)
OpenAlex
W2005145242
Cited by
524
References
2
FWCI
11.35
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The protein disulphide-isomerase family: unravelling a string of folds. https://app.cochat.ai/papers/10.1042/0264-6021:3390001
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Ferrari, D. M., & Söling, H. (1999). The protein disulphide-isomerase family: unravelling a string of folds. Biochemical Journal. https://doi.org/10.1042/0264-6021%3A3390001

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