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The protein disulphide-isomerase family: unravelling a string of folds
Open accessAbstract
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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Cites
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
Cited by
de Marco, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-26 · Cited by 367
Jones, D. P., Go, Y.-M., Anderson, C. L., Ziegler, T. R., Kinkade, J. M., & Kirlin, W. G. (2004) · The FASEB Journal · doi:10.1096/fj.03-0971fje · Cited by 301
Intramolecular chaperones: polypeptide extensions that modulate protein folding
Shinde, U., & Inouye, M. (2000) · Seminars in Cell & Developmental Biology · doi:10.1006/scdb.1999.0349 · Cited by 141
Laurindo, F. R. M., Fernandes, D. C., Amanso, A. M., Lopes, L. R., & Santos, C. X. C. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.2011 · Cited by 87
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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- 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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