The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Reactive Oxygen-Mediated Protein Oxidation in Aging and Disease
Abstract
Highly reactive oxygen species that are formed during normal metabolism and under conditions of oxidative stress are able to oxidize proteins or convert lipid and carbohydrate derivatives to compounds that react with functional groups on proteins. Among other changes, these ROS-mediated reactions lead to the formation of protein carbonyl derivatives, which serves as a marker of ROS-mediated protein damage. On the basis of this marker, it is established that oxidatively damaged protein is associated with aging and some diseases. The accumulation of oxidatively damaged protein reflects the balance among a myriad of factors that govern the rates of ROS generation and the rate at which damaged protein is degraded. Peroxynitrite, which is formed under normal physiological conditions, is able to oxidize methionine residues in proteins and to nitrate tyrosine residues; however, its ability to do so is dependent on the availability of CO2, which stimulates the nitration of tyrosine residues but inhibits the oxidation of methionine residues. Nitration of tyrosine residues may contribute to peroxynitrite toxicity, as nitration precludes the phosphorylation or nucleotidylation of tyrosine residues and thereby seriously compromises one of the most important mechanisms of cellular regulation and signal transduction.
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Cites
The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
Pryor, W. A., & Squadrito, G. L. (1995) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1995.268.5.l699 · Cited by 1,511
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-citationMetal-catalyzed oxidation of proteins. Physiological consequences
Stadtman, E. R., & Oliver, C. N. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52199-2 · Cited by 862
Self-citationMechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite
Lymar, S. V., Jiang, Q., & Hurst, J. K. (1996) · Biochemistry · doi:10.1021/bi960331h · Cited by 299
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2‐Oxo‐histidine as a novel biological marker for oxidatively modified proteins
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Vitamin C as an Antioxidant: Evaluation of Its Role in Disease Prevention
Padayatty, S. J., Katz, A., Wang, Y., Eck, P., Kwon, O., Lee, J.-H., Chen, S., Corpe, C., Dutta, A., Dutta, S. K., et al. (2003) · Journal of the American College of Nutrition · doi:10.1080/07315724.2003.10719272 · Cited by 1,949
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
Changes in Proinflammatory Cytokine Activity after Menopause
Pfeilschifter, J., Köditz, R., Pfohl, M., & Schatz, H. (2002) · Endocrine Reviews · doi:10.1210/edrv.23.1.0456 · Cited by 914
Regulation of protein function by S‐glutathiolation in response to oxidative and nitrosative stress
Klatt, P., & Lamas, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01601.x · Cited by 745
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Rhee, S. G. (1999) · Experimental & Molecular Medicine · doi:10.1038/emm.1999.9 · Cited by 701
Metadata
- Authors
- Stadtman, E. R., & Berlett, B. S.
- Venue
- Drug Metabolism Reviews
- Publisher
- Informa UK Limited
- Published
- 1998-01
- Volume
- 30
- Issue
- 2
- Pages
- 225-243
- ISSN
- 0360-2532 (ISSN-L)
- 1097-9883
- OpenAlex
- W2164066515
- Cited by
- 891
- References
- 7
- FWCI
- 10.58
- Type
- journal article
- Language
- en
- Open access
- closed
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- Stadtman, E. R., & Berlett, B. S. (1998). Reactive Oxygen-Mediated Protein Oxidation in Aging and Disease. Drug Metabolism Reviews. https://doi.org/10.3109/03602539808996310
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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.
