The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum
Open accessAbstract
The endoplasmic reticulum (ER) supports disulfide bond formation by a poorly understood mechanism requiring protein disulfide isomerase (PDI) and ERO1. In yeast, Ero1p-mediated oxidative folding was shown to depend on cellular flavin adenine dinucleotide (FAD) levels but not on ubiquinone or heme, and Ero1p was shown to be a FAD-binding protein. We reconstituted efficient oxidative folding in vitro using FAD, PDI, and Ero1p. Disulfide formation proceeded by direct delivery of oxidizing equivalents from Ero1p to folding substrates via PDI. This kinetic shuttling of oxidizing equivalents could allow the ER to support rapid disulfide formation while maintaining the ability to reduce and rearrange incorrect disulfide bonds.
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Cites
[70] Determination of glutathione and glutathione disulfide in biological samples
Anderson, M. E. (1985) · Methods in Enzymology · doi:10.1016/s0076-6879(85)13073-9 · Cited by 2,748
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
The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
Kispal, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 700
Stevens, T., Esmon, B., & Schekman, R. (1982) · Cell · doi:10.1016/0092-8674(82)90241-0 · Cited by 572
The ERO1 Gene of Yeast Is Required for Oxidation of Protein Dithiols in the Endoplasmic Reticulum
Frand, A. R., & Kaiser, C. A. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80017-9 · Cited by 494
Pollard, M. G., Travers, K. J., & Weissman, J. S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80018-0 · Cited by 440
Self-citationLyles, M. M., & Gilbert, H. F. (1991) · Biochemistry · doi:10.1021/bi00217a004 · Cited by 419
A pathway for disulfide bond formation in vivo.
Bardwell, J. C., Lee, J. O., Jander, G., Martin, N., Belin, D., & Beckwith, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.1038 · Cited by 408
Frand, A. R., & Kaiser, C. A. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80198-7 · Cited by 387
Oxidative Protein Folding Is Driven by the Electron Transport System
Bader, M., Muse, W., Ballou, D. P., Gassner, C., & Bardwell, J. C. A. (1999) · Cell · doi:10.1016/s0092-8674(00)81016-8 · Cited by 385
Cited by
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M., Sadri, N., Yun, C., Popko, B., Paules, R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,323
ER stress and the unfolded protein response
Schröder, M., & Kaufman, R. J. (2005) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2004.06.056 · Cited by 1,747
Oxidative protein folding in eukaryotes
Tu, B. P., & Weissman, J. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311055 · Cited by 1,041
Self-citationThe Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
Görlach, A., Klappa, P., & Kietzmann, D. T. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 615
Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2625 · Cited by 572
Metadata
- Authors
- Tu, B. P., Ho-Schleyer, S. C., Travers, K. J., & Weissman, J. S.
- Venue
- Science
- Published
- 2000-11-24
- Volume
- 290
- Issue
- 5496
- Pages
- 1571-1574
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2029112137
- Cited by
- 447
- References
- 23
- FWCI
- 7.75
- Type
- journal article
- Language
- en
- Open access
- green
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- Tu, B. P., Ho-Schleyer, S. C., Travers, K. J., & Weissman, J. S. (2000). Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum. Science. https://doi.org/10.1126/science.290.5496.1571
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
