The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
From Selenium to Selenoproteins: Synthesis, Identity, and Their Role in Human Health
Abstract
The requirement of the trace element selenium for life and its beneficial role in human health has been known for several decades. This is attributed to low molecular weight selenium compounds, as well as to its presence within at least 25 proteins, named selenoproteins, in the form of the amino acid selenocysteine (Sec). Incorporation of Sec into selenoproteins employs a unique mechanism that involves decoding of the UGA codon. This process requires multiple features such as the selenocysteine insertion sequence (SECIS) element and several protein factors including a specific elongation factor EFSec and the SECIS binding protein 2, SBP2. The function of most selenoproteins is currently unknown; however, thioredoxin reductases (TrxR), glutathione peroxidases (GPx) and thyroid hormone deiodinases (DIO) are well characterised selenoproteins involved in redox regulation of intracellular signalling, redox homeostasis and thyroid hormone metabolism. Recent evidence points to a role for selenium compounds as well as selenoproteins in the prevention of some forms of cancer. A number of clinical trials are either underway or being planned to examine the effects of selenium on cancer incidence. In this review we describe some of the recent progress in our understanding of the mechanism of selenoprotein synthesis, the role of selenoproteins in human health and disease and the therapeutic potential of some of these proteins.
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Cites
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Selenium in global food systems
Combs, G. F. (2001) · British Journal of Nutrition · doi:10.1079/bjn2000280 · Cited by 1,129
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114
Deiodinases: implications of the local control of thyroid hormone action
Bianco, A. C., & Kim, B. W. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29812 · Cited by 845
Yant, L. J., Ran, Q., Rao, L., Van Remmen, H., Shibatani, T., Belter, J. G., Motta, L., Richardson, A., & Prolla, T. A. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01360-6 · Cited by 797
Early Embryonic Lethality Caused by Targeted Disruption of the Mouse Thioredoxin Gene
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“The central role played by the Trx system in development was highlighted by the embryonic lethal phenotype of the Trx gene (Txn) knockout mouse model (224).”
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
Self-citationConrad, 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
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Mutations in SECISBP2 result in abnormal thyroid hormone metabolism
Dumitrescu, A. M., Liao, X.-H., Abdullah, M. S. Y., Lado-Abeal, J., Majed, F. A., Moeller, L. C., Boran, G., Schomburg, L., Weiss, R. E., & Refetoff, S. (2005) · Nature Genetics · doi:10.1038/ng1654 · Cited by 412
Cited by
Epidemiology of Pancreatic Cancer: Global Trends, Etiology and Risk Factors
Rawla, P., Sunkara, T., & Gaduputi, V. (2019) · World Journal of Oncology · doi:10.14740/wjon1166 · Cited by 2,269
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
Self-citationSelenium in human health and disease
Fairweather-Tait, S. J., Bao, Y., Broadley, M. R., Collings, R., Ford, D., Hesketh, J. E., & Hurst, R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3275 · Cited by 1,330
Selenium biochemistry and its role for human health
Roman, M., Jitaru, P., & Barbante, C. (2014) · Metallomics · doi:10.1039/c3mt00185g · Cited by 823
Halliwell, B. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.01.028 · Cited by 759
Metadata
- Authors
- Papp, L. V., Lu, J., Holmgren, A., & Khanna, K. K.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2007-07
- Volume
- 9
- Issue
- 7
- Pages
- 775-806
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2094305716
- Cited by
- 1,338
- References
- 14
- FWCI
- 58.36
- Type
- journal article
- Language
- en
- Open access
- closed
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