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ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
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Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106585200 · Cited by 393
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Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409
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Lushchak, V. I. (2012) · Journal of Amino Acids · doi:10.1155/2012/736837 · Cited by 1,266
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Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213
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Muller, F. L., Lustgarten, M. S., Jang, Y., Richardson, A., & Van Remmen, H. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.034 · Cited by 1,053
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Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031
Reich, H. J., & Hondal, R. J. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00031 · Cited by 923
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Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631
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Jacob, C. (2006) · Natural Product Reports · doi:10.1039/b609523m · Cited by 373
Gerashchenko, M. V., Lobanov, A. V., & Gladyshev, V. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120799109 · Cited by 302
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Metadata
- Authors
- Biteau, B., Labarre, J., & Toledano, M. B.
- Venue
- Nature
- Published
- 2003-10
- Volume
- 425
- Issue
- 6961
- Pages
- 980-984
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2049713754
- Cited by
- 970
- References
- 1
- FWCI
- 13.62
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
