The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Protein Oxidation
Abstract
A bstract: The oxidative modification of proteins by reactive species, especially reactive oxygen species, is implicated in the etiology or progression of a panoply of disorders and diseases. These reactive species form through a large number of physiological and non‐physiological reactions. An increase in the rate of their production or a decrease in their rate of scavenging will increase the oxidative modification of cellular molecules, including proteins. For the most part, oxidatively modified proteins are not repaired and must be removed by proteolytic degradation, and a decrease in the efficiency of proteolysis will cause an increase in the cellular content of oxidatively modified proteins. The level of these modified molecules can be quantitated by measurement of the protein carbonyl content, which has been shown to increase in a variety of diseases and processes, most notably during aging. Accumulation of modified proteins disrupts cellular function either by loss of catalytic and structural integrity or by interruption of regulatory pathways.
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Cites
Role of oxidative stress in diabetic complications: a new perspective on an old paradigm.
Baynes, J. W., & Thorpe, S. R. (1999) · Diabetes · doi:10.2337/diabetes.48.1.1 · Cited by 2,441
Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A., & Butterfield, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3270 · Cited by 1,086
Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease.
Yoritaka, A., Hattori, N., Uchida, K., Tanaka, M., Stadtman, E. R., & Mizuno, Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2696 · Cited by 981
Self-citationHensley, K., Hall, N., Subramaniam, R., Cole, P., Harris, M., Aksenov, M., Aksenova, M., Gabbita, S. P., Wu, J. F., Carney, J. M., et al. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65052146.x · Cited by 779
Markesbery, W. R., & Lovell, M. A. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00009-8 · Cited by 680
Cited by
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases
Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-014-0446-0 · Cited by 2,886
Valavanidis, A., Vlahogianni, T., Dassenakis, M., & Scoullos, M. (2006) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2005.03.013 · Cited by 1,795
Hussain, S. P., Hofseth, L. J., & Harris, C. C. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1046 · Cited by 1,690
Potential Role of Carotenoids as Antioxidants in Human Health and Disease
Fiedor, J., & Burda, K. (2014) · Nutrients · doi:10.3390/nu6020466 · Cited by 1,420
Metadata
- Authors
- STADTMAN, E. R., & LEVINE, R. L.
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 2000-01
- Volume
- 899
- Issue
- 1
- Pages
- 191-208
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- OpenAlex
- W4211019851
- Cited by
- 1,007
- References
- 5
- FWCI
- 8.22
- Type
- journal article
- Language
- en
- Open access
- closed
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- STADTMAN, E. R., & LEVINE, R. L. (2000). Protein Oxidation. Annals of the New York Academy of Sciences. https://doi.org/10.1111/j.1749-6632.2000.tb06187.x
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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.
