The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals
Open accessAbstract
Oxidation of proteins by reactive oxygen species is associated with aging, oxidative stress, and many diseases. Although free and protein-bound methionine residues are particularly sensitive to oxidation to methionine sulfoxide derivatives, these oxidations are readily repaired by the action of methionine sulfoxide reductase (MsrA). To gain a better understanding of the biological roles of MsrA in metabolism, we have created a strain of mouse that lacks the MsrA gene. Compared with the wild type, this mutant: ( i ) exhibits enhanced sensitivity to oxidative stress (exposure to 100% oxygen); ( ii ) has a shorter lifespan under both normal and hyperoxic conditions; ( iii ) develops an atypical (tip-toe) walking pattern after 6 months of age; ( iv ) accumulates higher tissue levels of oxidized protein (carbonyl derivatives) under oxidative stress; and ( v ) is less able to up-regulate expression of thioredoxin reductase under oxidative stress. It thus seems that MsrA may play an important role in aging and neurological disorders.
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Cites
The p66shc adaptor protein controls oxidative stress response and life span in mammals
Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712
A mutation in succinate dehydrogenase cytochrome b causes oxidative stress and ageing in nematodes.
Ishii, N., Fujii, M., Hartman, P. S., Tsuda, M., Yasuda, K., Senoo-Matsuda, N., Yanase, S., Ayusawa, D., & Suzuki, K. (1998) · Nature · doi:10.1038/29331 · Cited by 687
Moskovitz, J., Rahman, M. A., Strassman, J., Yancey, S. O., Kushner, S. R., Brot, N., & Weissbach, H. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.3.502-507.1995 · Cited by 294
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Cited by
Chemistry and biology of reactive oxygen species in signaling or stress responses
Dickinson, B. C., & Chang, C. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.607 · Cited by 1,821
The oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392
Radical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122
Trends in oxidative aging theories
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
Metadata
- Authors
- Moskovitz, J., Bar-Noy, S., Williams, W. M., Requena, J., Berlett, B. S., & Stadtman, E. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-10-23
- Volume
- 98
- Issue
- 23
- Pages
- 12920-12925
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2011667964
- Cited by
- 677
- References
- 3
- FWCI
- 9.23
- Type
- journal article
- Language
- en
- Open access
- green
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