The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Two Enzymes in One
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Cites
Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
Neumann, C. A., Krause, D. S., Carman, C. V., Das, S., Dubey, D. P., Abraham, J. L., Bronson, R. T., Fujiwara, Y., Orkin, S. H., & Van Etten, R. A. (2003) · Nature · doi:10.1038/nature01819 · Cited by 801
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Redox Redux: Revisiting PTPs and the Control of Cell Signaling
Tonks, N. K. (2005) · Cell · doi:10.1016/j.cell.2005.05.016 · Cited by 702
Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603
Self-citationRhee, S. G., & Woo, H. A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3393 · Cited by 463
Self-citationThe mammalian ribo-interactome reveals ribosome functional diversity and heterogeneity
Simsek, D., Tiu, G. C., Flynn, R. A., Byeon, G. W., Leppek, K., Xu, A. F., Chang, H. Y., & Barna, M. (2017) · Cell · doi:10.1016/j.cell.2017.05.022 · Cited by 439
Thiol-based redox switches in eukaryotic proteins
Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373
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Niforou, K., Cheimonidou, C., & Trougakos, I. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.01.017 · Cited by 250
Peroxiredoxin 1 – an antioxidant enzyme in cancer
Ding, C., Fan, X., & Wu, G. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12955 · Cited by 232
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ER stress causes widespread protein aggregation and prion formation
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The Lifespan-regulator p66Shc in mitochondria: redox enzyme or redox sensor?
Gertz, M., & Steegborn, C. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3147 · Cited by 75
Latimer, H. R., & Veal, E. A. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2327 · Cited by 68
Lechardeur, D., Fernandez, A., Robert, B., Gaudu, P., Trieu-Cuot, P., Lamberet, G., & Gruss, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.024505 · Cited by 47
Kritsiligkou, P., Rand, J. D., Weids, A. J., Wang, X., Kershaw, C. J., & Grant, C. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001824 · Cited by 36
Metadata
- Authors
- Jang, H. H., Lee, K. O., Chi, Y. H., Jung, B. G., Park, S. K., Park, J. H., Lee, J. R., Lee, S. S., Moon, J. C., Yun, J. W., Choi, Y. O., Kim, W. Y., Kang, J. S., Cheong, G.-W., Yun, D.-J., Rhee, S. G., Cho, M. J., & Lee, S. Y.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2004-05
- Volume
- 117
- Issue
- 5
- Pages
- 625-635
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2062901635
- Cited by
- 767
- References
- 1
- FWCI
- 9.40
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
