The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions
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Citations
Cites
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro
Abate, C., Patel, L., Rauscher, F. J., & Curran, T. (1990) · Science · doi:10.1126/science.2118682 · Cited by 1,573
Trachootham, D., Zhou, Y., Zhang, H., Demizu, Y., Chen, Z., Pelicano, H., Chiao, P. J., Achanta, G., Arlinghaus, R. B., Liu, J., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.009 · Cited by 1,080
Thioredoxin and Related Molecules–From Biology to Health and Disease
Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724
Early Embryonic Lethality Caused by Targeted Disruption of the Mouse Thioredoxin Gene
Matsui, M., Oshima, M., Oshima, H., Takaku, K., Maruyama, T., Yodoi, J., & Taketo, M. M. (1996) · Developmental Biology · doi:10.1006/dbio.1996.0208 · Cited by 546
Thioredoxin Reductase Is Irreversibly Modified by Curcumin
Fang, J., Lu, J., & Holmgren, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414645200 · Cited by 521
Conrad, M., Jakupoglu, C., Moreno, S. G., Lippl, S., Banjac, A., Schneider, M., Beck, H., Hatzopoulos, A. K., Just, U., Sinowatz, F., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9414-9423.2004 · Cited by 485
Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
Tong, K. I., Kobayashi, A., Katsuoka, F., & Yamamoto, M. (2006) · Biological Chemistry · doi:10.1515/bc.2006.164 · Cited by 473
Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438
Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
Lee, T.-H. (2003) · Blood · doi:10.1182/blood-2002-08-2548 · Cited by 420
Cited by
The thioredoxin antioxidant system
Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055
Reich, H. J., & Hondal, R. J. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00031 · Cited by 923
Selenium biochemistry and its role for human health
Roman, M., Jitaru, P., & Barbante, C. (2014) · Metallomics · doi:10.1039/c3mt00185g · Cited by 823
Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 677
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
Metadata
- Authors
- Arnér, E. S. J.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2009-06
- Volume
- 1790
- Issue
- 6
- Pages
- 495-526
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W1984568177
- Cited by
- 673
- References
- 17
- FWCI
- 17.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions. https://app.cochat.ai/papers/10.1016/j.bbagen.2009.01.014
- The paper
- Arnér, E. S. J. (2009). Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions. Biochimica et Biophysica Acta (BBA) - General Subjects. https://doi.org/10.1016/j.bbagen.2009.01.014
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.