The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Oxidative Protein Folding Is Driven by the Electron Transport System
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Citations
Cites
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
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
Chemistry and Enzymology of Disulfide Cross-Linking in Proteins
Fass, D., & Thorpe, C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00123 · Cited by 321
(2000) · PubMed · Cited by 242
Allen, S., Balabanidou, V., Sideris, D. P., Lisowsky, T., & Tokatlidis, K. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.049 · Cited by 235
Pathways of disulfide bond formation in Escherichia coli
Messens, J., & Collet, J.-F. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.12.011 · Cited by 174
A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1
Dabir, D. V., Leverich, E. P., Kim, S., Tsai, F. D., Hirasawa, M., Knaff, D. B., & Koehler, C. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601909 · Cited by 162
Ando, K., Hirao, S., Kabe, Y., Ogura, Y., Sato, I., Yamaguchi, Y., Wada, T., & Handa, H. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn416 · Cited by 155
Two phases of disulfide bond formation have differing requirements for oxygen
Koritzinsky, M., Levitin, F., van den Beucken, T., Rumantir, R. A., Harding, N. J., Chu, K. C., Boutros, P. C., Braakman, I., & Wouters, B. G. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201307185 · Cited by 136
Regulation of the protein disulfide proteome by mitochondria in mammalian cells
Yang, Y., Song, Y., & Loscalzo, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702027104 · Cited by 129
DsbG, a protein disulfide isomerase with chaperone activity
Shao, F., Bader, M. W., Jakob, U., & Bardwell, J. C. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13349 · Cited by 116
Self-citationSingh, A. K., Bhattacharyya-Pakrasi, M., & Pakrasi, H. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800982200 · Cited by 73
Chavez, D., Amarquaye, G. N., Mejia-Santana, A., Dyotima, Ryan, K., Zeng, L., & Landeta, C. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107383 · Cited by 4
Metadata
- Authors
- Bader, M., Muse, W., Ballou, D. P., Gassner, C., & Bardwell, J. C. A.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1999-07
- Volume
- 98
- Issue
- 2
- Pages
- 217-227
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2126079531
- Cited by
- 385
- References
- 1
- FWCI
- 9.13
- Type
- journal article
- Language
- en
- Open access
- bronze
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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Data sources
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.
