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Oxidatively modified proteins in aging and disease1, 2 1Guest Editor: Earl Stadtman 2This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease” The full list of papers may be found on the homepage of the journal
Abstract
There is a large body of evidence implicating oxidative damage in the pathogenesis of both normal aging and neurodegenerative diseases. Oxidative damage to proteins has been well established. Although there are a large number of potential oxidative modifications only a few have been systematically studied. The most frequently studied marker of oxidative damage to proteins is protein carbonyl groups. 3-Nitrotyrosine is thought to be a relatively specific marker of oxidative damage mediated by peroxynitrite. Increased concentrations of both protein carbonyls and 3-nitrotyrosine have been documented in both normal aging as well as in Alzheimer's disease (AD), Parkinson's disease (PD), and amyotrophic lateral sclerosis (ALS). These findings help to provide a rationale for trials of antioxidants in neurodegenerative diseases.
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“Much evidence suggests that oxidative damage to proteins is associated with aging and is linked to protein misfolding [216,217].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [216]
Citations
Cites
A Controlled Trial of Selegiline, Alpha-Tocopherol, or Both as Treatment for Alzheimer's Disease
Sano, M., Ernesto, C., Thomas, R. G., Klauber, M. R., Schafer, K., Grundman, M., Woodbury, P., Growdon, J., Cotman, C. W., Pfeiffer, E., et al. (1997) · New England Journal of Medicine · doi:10.1056/nejm199704243361704 · Cited by 2,380
Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,567
Age-related changes in oxidized proteins.
Oliver, C. N., Ahn, B. W., Moerman, E. J., Goldstein, S., & Stadtman, E. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45598-6 · Cited by 1,306
Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296
Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease
Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239
Liberatore, G. T., Jackson-Lewis, V., Vukosavic, S., Mandir, A. S., Vila, M., McAuliffe, W. G., Dawson, V. L., Dawson, T. M., & Przedborski, S. (1999) · Nature Medicine · doi:10.1038/70978 · Cited by 1,046
Oxidative damage in Alzheimer's
Smith, M. A., Perry, G. L., Richey, P. L., Sayrec, L. M., Anderson, V. E., Beal, M. F., & Kowall, N. W. (1996) · Nature · doi:10.1038/382120b0 · Cited by 897
Self-citationBrowne, S. E., Bowling, A. C., Macgarvey, U., Baik, M. J., Berger, S. C., Muquit, M. M. K., Bird, E. D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410514 · Cited by 885
Self-citationEvidence of Increased Oxidative Damage in Both Sporadic and Familial Amyotrophic Lateral Sclerosis
Ferrante, R. J., Browne, S. E., Shinobu, L. A., Bowling, A. C., Baik, M. J., MacGarvey, U. M., Kowall, N. W., Brown, R. H., & Beal, M. F. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69052064.x · Cited by 808
Self-citationSohal, R. S., Ku, H.-H., Agarwal, S., Forster, M. J., & Lal, H. (1994) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(94)90104-x · Cited by 788
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Tyrosine nitration as mediator of cell death
Franco, M. C., & Estévez, Á. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1662-8 · Cited by 50
Oxidative stress in the brain at early preclinical stages of mouse scrapie
Yun, S., Gerlach, M., Riederer, P. F., & Klein, M. A. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.03.025 · Cited by 52
Xue, S., & Jia, J. (2006) · Brain Research · doi:10.1016/j.brainres.2006.02.121 · Cited by 49
Evidence for chronically elevated serum protein oxidation in systemic lupus erythematosus patients
Morgan, P. E., Sturgess, A. D., & Davies, M. J. (2009) · Free Radical Research · doi:10.1080/10715760802623896 · Cited by 48
Kajstura, J., Bolli, R., Sonnenblick, E. H., Anversa, P., & Leri, A. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.12.013 · Cited by 49
Kański, J., & Schöneich, C. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96016-3 · Cited by 48
Pallottini, V., Martini, C., Pascolini, A., Cavallini, G., Gori, Z., Bergamini, E., Incerpi, S., & Trentalance, A. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.02.009 · Cited by 48
Peroxynitrite transforms nerve growth factor into an apoptotic factor for motor neurons
Pehar, M., Vargas, M. R., Robinson, K. M., Cassina, P., England, P., Beckman, J. S., Alzari, P. M., & Barbeito, L. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.010 · Cited by 50
Schilling, B., Bharath, S., Row, R. H., Murray, J. M., Cusack, M. P., Capaldi, R., Freed, C. R., Prasad, K. N., Andersen, J. K., & Gibson, B. W. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400143-mcp200 · Cited by 48
Rapid and sensitive determination of protein-nitrotyrosine by ELISA: Application to human plasma
Weber, D., Kneschke, N., Grimm, S., Bergheim, I., Breusing, N., & Grune, T. (2012) · Free Radical Research · doi:10.3109/10715762.2011.652627 · Cited by 47
Abdel‐Salam, O. M. E., Khadrawy, Y. A., Salem, N. A., & Sleem, A. A. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0450-1 · Cited by 47
Shahid, A., Ali, R., Ali, N., Hasan, S. K., Rashid, S., Majed, F., & Sultana, S. (2016) · Journal of Complementary and Integrative Medicine · doi:10.1515/jcim-2015-0078 · Cited by 47
Wallace, L. M., Mehrabi, S., Bacanamwo, M., Yao, X., & Aikhionbare, F. O. (2016) · Tumor Biology · doi:10.1007/s13277-016-5101-3 · Cited by 49
Rajak, P., Khatun, S., Dutta, M., Mandi, M., & Roy, S. (2018) · Toxicology Research · doi:10.1039/c8tx00052b · Cited by 47
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Smirnova, I. V., & Pall, M. L. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/a:1024176016962 · Cited by 46
Gutiérrez-Martı́n, Y., Martı́n-Romero, F. J., Henao, F., & Gutiérrez‐Merino, C. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02964.x · Cited by 46
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Aoyama, K., Wang, F., Matsumura, N., Kiyonari, H., Shioi, G., Tanaka, K., Kinoshita, C., Kikuchi-Utsumi, K., Watabe, M., & Nakaki, T. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.016 · Cited by 45
Karki, R., & Igwe, O. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073840 · Cited by 47
Computational Study on the Attack of .OH Radicals on Aromatic Amino Acids
Mujika, J. I., Uranga, J., & Matxain, J. M. (2013) · Chemistry – A European Journal · doi:10.1002/chem.201203862 · Cited by 45
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Lindblom, S. C., Gabler, N. K., Dilger, R. N., Olson, Z. F., Loving, C. L., & Kerr, B. J. (2018) · Journal of Animal Science · doi:10.1093/jas/sky005 · Cited by 45
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Qais, F. A., & Ahmad, I. (2019) · New Journal of Chemistry · doi:10.1039/c9nj01490j · Cited by 45
Jayaraman, J., Veerappan, M., & Nalini, N. (2009) · Journal of Pharmacy and Pharmacology · doi:10.1211/jpp.61.10.0016 · Cited by 45
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Strope, T. A., Birky, C. J., & Wilkins, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169212 · Cited by 44
Sulkowski, Z. L., Chen, T., Midha, S., Zavacki, A. M., & Sajdel, E. M. (2011) · The Cerebellum · doi:10.1007/s12311-011-0319-5 · Cited by 45
Protective effects of Peroxiredoxin 6 overexpression on amyloid β-induced apoptosis in PC12 cells
Kim, I.-K., Lee, K. J., Rhee, S., Seo, S., & Pak, J. H. (2013) · Free Radical Research · doi:10.3109/10715762.2013.833330 · Cited by 44
Effect of aging on the expression of BDNF and TrkB isoforms in rat pituitary
Rage, F., Silhol, M., Binamé, F., Arancibia, S., & Tapia‐Arancibia, L. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.05.013 · Cited by 44
Differential cell death regulation between adult-unloaded and aged rat soleus muscle
Ogata, T., Machida, S., Oishi, Y., Higuchi, M., & Muraoka, I. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.02.001 · Cited by 44
Galetskiy, D., Lohscheider, J. N., Kononikhin, A. S., Popov, I. A., Николаев, Е. Н., & Adamska, I. (2011) · Plant Molecular Biology · doi:10.1007/s11103-011-9824-7 · Cited by 44
Väänänen, A. J., Kankuri, E. M., & Rauhala, P. V. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.01.007 · Cited by 44
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Jayaraman, J., Veerappan, M., & Nalini, N. (2009) · Journal of Pharmacy and Pharmacology · doi:10.1211/jpp/61.10.0016 · Cited by 43
Kim‐Han, J. S., & O’Malley, K. L. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1791 · Cited by 43
Lyu, K., Gu, L., Li, B., Lu, Y., Wu, C., Guan, H., & Yang, Z. (2016) · Harmful Algae · doi:10.1016/j.hal.2016.04.009 · Cited by 43
Tasset, I., Cruz, V. P.-D. L., Elinos, D., Carrillo-Mora, P. U., González-Herrera, I. G., Luna-López, A., Königsberg, M., Pedraza-Chaverrí, J., Maldonado, P. D., Ali, S. F., et al. (2009) · Neurosignals · doi:10.1159/000243650 · Cited by 42
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Lee, S. J., Lee, J. R., Kim, Y. H., Park, Y. S., Park, S. I., Park, H. S., & Kim, K. P. (2007) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.3145 · Cited by 42
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Maciejczyk, M., Szulimowska, J., Taranta‐Janusz, K., Wasilewska, A. M., & Zalewska, A. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9051285 · Cited by 41
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Wan, X. S., Zhou, Z., Ware, J. H., & Kennedy, A. R. (2005) · Radiation Research · doi:10.1667/rr3299 · Cited by 40
Impact of Peroxynitrite Modification on Structure and Immunogenicity of H2A Histone
Khan, M. A., Dixit, K., Jabeen, S., Moinuddin, & Alam, K. (2009) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2008.02200.x · Cited by 39
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Vishwas, D. K., Mukherjee, A., Haldar, C., Dash, D., & Nayak, M. K. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.11.012 · Cited by 39
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Kayalı, R., Çakatay, U., Uzun, H., & Genç, H. (2007) · Biogerontology · doi:10.1007/s10522-007-9107-5 · Cited by 39
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Chihara, Y., Fujimoto, K., Kondo, H., Moriwaka, Y., Sasahira, T., Hirao, Y., & Kuniyasu, H. (2007) · Pathobiology · doi:10.1159/000110029 · Cited by 39
Dkhar, P., & Sharma, R. (2010) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2010.04.005 · Cited by 39
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Watson, J. B., Arnold, M. M., Ho, Y., & O’Dell, T. J. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21040 · Cited by 39
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Deori, M., Devi, D., Kumari, S., Hazarika, A., Kalita, H., Sarma, R., & Devi, R. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00319 · Cited by 38
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McKenna, M. C., & Ferreira, G. C. (2016) · Advances in neurobiology · doi:10.1007/978-3-319-45096-4_4 · Cited by 35
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Radek, K. A., Ranzer, M. J., & DiPietro, L. A. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0209103 · Cited by 38
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Eze, F. N., & Jayeoye, T. J. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111811 · Cited by 37
Guenaou, I., Irahal, I. N., Errami, A., Lahlou, F. A., Hmimid, F., & Bourhim, N. (2021) · Molecules · doi:10.3390/molecules26195998 · Cited by 40
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Petri, S., Kollewe, K., Grothe, C., Hori, A., Dengler, R., Bufler, J., & Krampfl, K. (2006) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2006.08.005 · Cited by 37
Pinpointing oxidative modifications in proteins—recent advances in analytical methods
Törnvall, U. (2010) · Analytical Methods · doi:10.1039/c0ay00375a · Cited by 37
Morgan, P. E., Sturgess, A. D., Hennessy, A., & Davies, M. J. (2007) · Free Radical Research · doi:10.1080/10715760701684809 · Cited by 37
Kowalik‐Jankowska, T., Rajewska, A., Jankowska, E., Wiśniewska, K., & Grzonka, Z. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.05.010 · Cited by 37
Jokic, A., Sremcevic, N., Karagülle, Z., Pekmezovic, T. D., & Davidović, V. (2010) · Vojnosanitetski pregled · doi:10.2298/vsp1007573j · Cited by 36
Oloyede, H. O. B., Ajiboye, T. O., Komolafe, Y. O., & Salau, A. K. (2013) · Food Bioscience · doi:10.1016/j.fbio.2013.03.003 · Cited by 36
Fitzenberger, E., Boll, M., & Wenzel, U. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.01.012 · Cited by 36
Andreazza, A. C. (2012) · Molecular BioSystems · doi:10.1039/c2mb25118c · Cited by 36
Xanthine Oxidase/Dehydrogenase Activity as a Source of Oxidative Stress in Prostate Cancer Tissue
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López, I. A., Acuña, D., Beltrán‐Parrazal, L., Lopez, I. E., Amarnani, A., Cortes, M., & Edmond, J. (2009) · BMC Neuroscience · doi:10.1186/1471-2202-10-53 · Cited by 35
Wang, G., Wang, J., Ma, H., & Khan, M. F. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.03.010 · Cited by 37
Potential cosmetic application of essential oil extracted fromLitsea cubebafruits from China
Huang, X., Feng, Y., Huang, Y., & Li, H. (2013) · Journal of Essential Oil Research · doi:10.1080/10412905.2012.755479 · Cited by 36
Sauvaigo, S., Bonnet, M., Odin, F., Hazane‐Puch, F., Lachmann, N., Bonté, F., Kurfürst, R., & Favier, A. E. (2007) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2007.07890.x · Cited by 36
Zhang, Y., & Kiryu, H. (2023) · Scientific Reports · doi:10.1038/s41598-023-34021-1 · Cited by 37
Al-Khayri, J. M., Ravindran, M., Banadka, A., Devaiah, V. C., Priya, K., Nagella, P., & Kukkemane, K. (2024) · Pharmaceuticals · doi:10.3390/ph17101391 · Cited by 42
Neelofar, K., Arif, Z., Alam, K., & Ahmad, J. (2016) · Molecular BioSystems · doi:10.1039/c6mb00324a · Cited by 35
Lipid and protein oxidation in female patients with chronic fatigue syndrome
Tomić, S., Brkic, S. V., Marić, D., & Mikić, A. N. (2012) · Archives of Medical Science · doi:10.5114/aoms.2012.31620 · Cited by 34
Natural antioxidants in prevention and management of Alzheimer's disease
Zhao, Y. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/419 · Cited by 35
Siddiqui, Z., Ishtikhar, M., Moinuddin, M., & Ahmad, S. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.01.161 · Cited by 35
In vitro–in vivo study of CoQ10-loaded lipid nanoparticles in comparison with nanocrystals
Piao, H., Ouyang, M., Xia, D., Quan, P., Xiao, W., Song, Y., & Cui, F. (2011) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2011.07.016 · Cited by 34
Velaga, M. K., Basuri, C. K., Taylor, K. S. R., Yallapragada, P. R., Rajanna, S., & Rajanna, B. (2013) · Drug and Chemical Toxicology · doi:10.3109/01480545.2013.866137 · Cited by 34
Abdullah, K. M., Qais, F. A., Ahmad, I., & Naseem, I. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.06.009 · Cited by 34
Alagözlü, H., Görgül, A., Bi̇lgi̇han, A., Tunçer, C., & Ünal, S. (2012) · Clinics and Research in Hepatology and Gastroenterology · doi:10.1016/j.clinre.2012.03.034 · Cited by 34
Protein carbonyl levels in the aqueous humour and serum of patients with pseudoexfoliation syndrome
Yağcı, R., Ersöz, İ., Erdurmuş, M., Gürel, A., & Duman, S. (2007) · Eye · doi:10.1038/sj.eye.6702751 · Cited by 33
Monroe, R. K., & Halvorsen, S. W. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl073 · Cited by 33
Fast repair of protein radicals by urate
Domazou, A. S., Zhu, H., & Koppenol, W. H. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.045 · Cited by 33
Wu, F., Xue, Y., Tang, Q., Xu, J., Du, L., Xue, C., Takahashi, K., & Wang, Y. (2013) · Journal of Oleo Science · doi:10.5650/jos.62.717 · Cited by 33
Lee, Y. J., Chung, H.-Y., Kwak, H., & Yoon, S. O. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.07.097 · Cited by 32
Hardas, S. S., Rukhsana Sultana, A., Warrier, G., Dan, M., Wu, P., Grulke, E. A., Tseng, M. T., Unrine, J. M., Graham, U. M., Yokel, R. A., et al. (2013) · Nanotoxicology · doi:10.3109/17435390.2013.868059 · Cited by 32
AAV-Nrf2 Promotes Protection and Recovery in Animal Models of Oxidative Stress
Liang, K. J., Woodard, K., Weaver, M. A., Gaylor, J. P., Weiss, E. R., & Samulski, R. J. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2016.12.016 · Cited by 32
Silhol, M., Arancibia, S., Perrin, D., Maurice, T., Alliot, J., & Tapia‐Arancibia, L. (2008) · Rejuvenation Research · doi:10.1089/rej.2008.0791 · Cited by 36
Manikandan, P., Murugan, R. S., Abbas, H. Y., Abraham, S. K., & Nagini, S. (2007) · Journal of Medicinal Food · doi:10.1089/jmf.2006.125 · Cited by 32
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Metadata
- Authors
- Beal, M. F.
- Affiliations
- NewYork–Presbyterian Hospital (US)
- Corresponding author
- Beal, M.Flint
- ORCID
- Beal, M.Flint
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2002-05
- Volume
- 32
- Issue
- 9
- Pages
- 797-803
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W1522890520
- Cited by
- 763
- References
- 75
- Citations by year
- 2026: 3 · 2025: 10 · 2024: 17 · 2023: 15 · 2022: 18 · 2021: 29 · 2020: 24 · 2019: 28 · 2018: 25 · 2017: 23 · 2016: 28 · 2015: 23 · 2014: 43 · 2013: 44 · 2012: 45
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- oxidized proteins, oxidative damage, aging, neurodegenerative diseases, protein carbonyls, nitrotyrosine, peroxynitrite, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, antioxidants
- MeSH terms
- Aging, Humans, Nerve Tissue Proteins, Oxidation-Reduction, Reactive Oxygen Species, Oxidative Stress, Neurodegenerative Diseases, Peroxynitrous Acid
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