The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase
Open accessAbstract
Significance: Several functions in cells require reductive processes, i.e., the enzymatic catalysis of a transfer of electrons to specific cellular substrates. One major reductive system in the cytosol of human cells depends upon thioredoxin 1 (Trx1), which in turn is kept reduced by thioredoxin reductase 1 (TrxR1) using NADPH. In the present study it is shown that another protein in addition to Trx1, called thioredoxin-related protein of 14 kDa (TRP14), is highly efficient together with TrxR1 in catalyzing reduction of L-cystine or nitric oxide-derivatized cysteine residues. It is also shown that TRP14, in contrast to Trx1, is resistant to inactivation by hydrogen peroxide. These findings reveal that several TrxR1-dependent functions in cells may not be propelled solely by Trx1, but instead relate to activities of TRP14.
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Cites
Glutathione Metabolism and Its Implications for Health
Wu, G., Lupton, J. R., Turner, N. D., Fang, Y.-Z., & Yang, S. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.3.489 · Cited by 3,842
A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J., & Stamler, J. S. (2001) · Nature · doi:10.1038/35068596 · Cited by 913
Cathepsin B as a cancer target
Gondi, C. S., & Rao, J. S. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.740461 · Cited by 399
System xc− and Thioredoxin Reductase 1 Cooperatively Rescue Glutathione Deficiency
Mandal, P. K., Seiler, A., Perisic, T., Kölle, P., Banjac Canak, A., Förster, H., Weiss, N., Kremmer, E., Lieberman, M. W., Bannai, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.121327 · Cited by 269
Hashemy, S. I., & Holmgren, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801047200 · Cited by 192
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A Genetic Map of the Response to DNA Damage in Human Cells
Olivieri, M., Cho, T., Álvarez-Quilón, A., Li, K., Schellenberg, M. J., Zimmermann, M., Hustedt, N., Rossi, S. E., Adam, S., Melo, H., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.040 · Cited by 551
Cramer, S. L., Saha, A., Liu, J., Tadi, S., Tiziani, S., Yan, W., Triplett, K., Lamb, C., Alters, S. E., Rowlinson, S., et al. (2017) · Nature Medicine · doi:10.1038/nm.4232 · Cited by 538
Shields, H. J., Traa, A., & Van Raamsdonk, J. M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.628157 · Cited by 478
p53 as a hub in cellular redox regulation and therapeutic target in cancer
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Metadata
- Authors
- Pader, I., Sengupta, R., Cebula, M., Xu, J., Lundberg, J. O., Holmgren, A., Johansson, K., & Arnér, E. S. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-04-28
- Volume
- 111
- Issue
- 19
- Pages
- 6964-6969
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2066478072
- Cited by
- 166
- References
- 5
- FWCI
- 4.26
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase. https://app.cochat.ai/papers/10.1073/pnas.1317320111
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- Pader, I., Sengupta, R., Cebula, M., Xu, J., Lundberg, J. O., Holmgren, A., Johansson, K., & Arnér, E. S. J. (2014). Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1317320111
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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