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

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

Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions

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

Inducible nitric oxide synthase stimulates dopaminergic neurodegeneration in the MPTP model of Parkinson disease

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

Oxidative damage and metabolic dysfunction in Huntington's disease: Selective vulnerability of the basal ganglia

Browne, 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

Evidence 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

Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse

Sohal, 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

The mitochondrial permeability transition pore: A molecular target for amyotrophic lateral sclerosis therapy

Martin, L. J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.009 · Cited by 80

Health Risks of Food Oxidation

Estévez, M., Li, Z., Soladoye, O. P., & Van-Hecke, T. (2017) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2016.12.005 · Cited by 75

Cellular mechanisms of peroxynitrite-induced neuronal death

Ramdial, K., Franco, M. C., & Estévez, Á. G. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.05.008 · Cited by 77

Synthesis, Modification and Turnover of Proteins during Aging

Rattan, S. I. S. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_1 · Cited by 75

Lifelong running reduces oxidative stress and degenerative changes in the testes of mice

Chigurupati, S., Son, T. G., Hyun, D. H., Lathia, J. D., Mughal, M. R., Savell, J. G., Li, S. C., Nagaraju, G. P., Chan, S. L., Arumugam, T. V., et al. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0306 · Cited by 75

Single bouts of exercise affect albumin redox state and carbonyl groups on plasma protein of trained men in a workload-dependent manner

Lamprecht, M., Greilberger, J., Schwaberger, G., Hofmann, P., & Oettl, K. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01325.2007 · Cited by 75

Insulin resistance, neuroinflammation, and Alzheimer’s disease

Najem, D., Bamji‐Mirza, M., Chang, N., Liu, Q. Y., & Zhang, W. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2013-0050 · Cited by 76

Blood Antioxidant Parameters in Sickle Cell Anemia Patients in Steady State

Lazzaretti, L. L., Griebeler, I. H., Manfredini, V. A., Brandão, V. D. M., Benfato, M. S., Santin, A. P., Wagner, S. C., de Castro, S. M., & Peralba, M. D. C. R. (2008) · Journal of the National Medical Association · doi:10.1016/s0027-9684(15)31402-4 · Cited by 73

Protective Effects of Decursin and Decursinol Angelate against Amyloid β-Protein-Induced Oxidative Stress in the PC12 Cell Line: The Role of Nrf2 and Antioxidant Enzymes

Li, L., Wei, L. I., Jung, S., Lee, Y., & Kim, Y.-H. (2011) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.100606 · Cited by 73

Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes

Choksi, K. B., & Papaconstantinou, J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.032 · Cited by 70

Hepatoprotective effect of the aqueous extract of the roots of Decalepis hamiltonii against ethanol-induced oxidative stress in rats

Srivastava, A., & Shivanandappa, T. (2006) · Hepatology Research · doi:10.1016/j.hepres.2006.04.011 · Cited by 73

Prevention of brain protein and lipid oxidation elicited by a water-soluble oryzanol enzymatic extract derived from rice bran

Parrado, J., Miramontes, E., Jover, M., M�rquez, J. C., Mejias, M. A., de Terán, L. C., Absi, E., & Bautista, J. (2003) · European Journal of Nutrition · doi:10.1007/s00394-003-0424-4 · Cited by 73

Blockade of neuronal nitric oxide synthase reduces cone cell death in a model of retinitis pigmentosa

Komeima, K., Usui, S., Shen, J., Rogers, B. S., & Campochiaro, P. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.06.020 · Cited by 74

Cell Culture Models of Oxidative Stress and Injury in the Central Nervous System

Aksenova, M. V., Aksenov, M. Y., Mactutus, C. F., & Booze, R. M. (2005) · Current Neurovascular Research · doi:10.2174/1567202052773463 · Cited by 73

Insight of brain degenerative protein modifications in the pathology of neurodegeneration and dementia by proteomic profiling

Adav, S. S., & Sze, S. K. (2016) · Molecular Brain · doi:10.1186/s13041-016-0272-9 · Cited by 75

Efficient repair of protein radicals by ascorbate

Domazou, A. S., Koppenol, W. H., & Gebicki, J. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.001 · Cited by 72

Age-related alterations in oxidatively damaged proteins of mouse skeletal muscle mitochondrial electron transport chain complexes

Choksi, K. B., Nuss, J. E., DeFord, J. H., & Papaconstantinou, J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.06.006 · Cited by 73

Suppression of caspase-3-dependent proteolytic activation of protein kinase Cδ by small interfering RNA prevents MPP+-induced dopaminergic degeneration

Yang, Y., Kaul, S., Zhang, D., Anantharam, V., & Kanthasamy, A. G. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2003.11.011 · Cited by 72

Is Cardiac Hypertrophy in Spontaneously Hypertensive Rats the Cause or the Consequence of Oxidative Stress?

Álvarez, M. C., Caldiz, C. I., Fantinelli, J. C., Garciarena, C. D., Cónsole, G. M., de Cingolani, G. E. C., & Mosca, S. M. (2008) · Hypertension Research · doi:10.1291/hypres.31.1465 · Cited by 71

Cardiac Mitochondrial Damage And Inflammation Responses in Sepsis

Zang, Q. S., Maass, D. L., Tsai, S. J., & Horton, J. W. (2007) · Surgical Infections · doi:10.1089/sur.2006.033 · Cited by 71

Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin

Khan, M. W. A., Rasheed, Z., Khan, W. A., & Ali, R. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907020034 · Cited by 72

Adaptation of the Dichlorofluorescein Assay for Detection of Radiation-Induced Oxidative Stress in Cultured Cells

Wan, X. S., Zhou, Z., & Kennedy, A. R. (2003) · Radiation Research · doi:10.1667/3099 · Cited by 71

Vascular endothelial function and oxidative stress are related to dietary niacin intake among healthy middle-aged and older adults

Kaplon, R. E., Gano, L. B., & Seals, D. R. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00969.2013 · Cited by 70

Role of Gasotransmitters in Oxidative Stresses, Neuroinflammation, and Neuronal Repair

Shefa, U., Yeo, S. G., Kim, M., Song, I. O., Jung, J., Jeong, N. Y., & Huh, Y. (2017) · BioMed Research International · doi:10.1155/2017/1689341 · Cited by 73

Minimizing Laboratory-Induced Decay in Bone Proteomics

Procopio, N., & Buckley, M. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00564 · Cited by 61

Decreased susceptibility to oxidative stress underlies the resistance of specific dopaminergic cell populations to paraquat-induced degeneration

McCormack, A. L., Atienza, J. G., Langston, J. W., & Monte, D. A. D. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.03.069 · Cited by 69

Modifications of apoptosis-related protein levels in lymphocytes of patients with Parkinson?s disease. The effect of dopaminergic treatment

Blandini, F., Cosentino, M., Mangiagalli, A., Marino, F., Samuele, A., Rasini, E., Fancellu, R., Tassorelli, C., Pacchetti, C., Martignoni, E., et al. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0123-1 · Cited by 69

Reactive oxygen species damaged human serum albumin in patients with type 1 diabetes mellitus: Biochemical and immunological studies

Rasheed, Z., & Ali, R. (2006) · Life Sciences · doi:10.1016/j.lfs.2006.07.041 · Cited by 68

Metabolism of 3-Nitrotyrosine Induces Apoptotic Death in Dopaminergic Cells

Blanchard-Fillion, B., Prou, D., Polydoro, M., Spielberg, D., Tsika, E., Wang, Z., Hazen, S. L., Koval, M. H., Przedborski, S., & Ischiropoulos, H. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1038-06.2006 · Cited by 69

Reactive Oxygen Species: Angels and Demons in the Life of a Neuron

Biswas, K., Alexander, K. D., & Francis, M. M. (2022) · NeuroSci · doi:10.3390/neurosci3010011 · Cited by 74

Circadian dysfunction and Alzheimer's disease – An updated review

Ahmad, F., Sachdeva, P., Sarkar, J., & Izhaar, R. (2022) · Aging Medicine · doi:10.1002/agm2.12221 · Cited by 70

Anti-carcinogenic action of curcumin by activation of antioxidant defence system and inhibition of NF-κB signalling in lymphoma-bearing mice

Das, L., & Vinayak, M. (2011) · Bioscience Reports · doi:10.1042/bsr20110043 · Cited by 67

Cytoprotective Effect of Valeriana officinalis Extract on an In Vitro Experimental Model of Parkinson Disease

de Oliveria, D. M., Barreto, G. E., Andrade, D. V. G. D., Saraceno, G. E., Bertolino, L.-A., Capani, F., El-Bachá, R. D. S., & Giráldez, L. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9749-y · Cited by 67

Stilbazulenyl nitrone, a novel antioxidant, is highly neuroprotective in focal ischemia

Ginsberg, M. D., Becker, D. A., Busto, R., Belayev, A., Zhang, Y., Khoutorova, L., Ley, J. J., Zhao, W., & Belayev, L. (2003) · Annals of Neurology · doi:10.1002/ana.10659 · Cited by 67

Plasma protein carbonyl levels and breast cancer risk

Rössner, P., Terry, M. B., Gammon, M. D., Agrawal, M., Zhang, F. F., Ferris, J. S., Teitelbaum, S. L., Eng, S. M., Gaudet, M. M., Neugut, A. I., et al. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00097.x · Cited by 66

Lifelong Calorie Restriction Alleviates Age-Related Oxidative Damage in Peripheral Nerves

Opalach, K., Rangaraju, S., Madorsky, I., Leeuwenburgh, C., & Notterpek, L. M. (2010) · Rejuvenation Research · doi:10.1089/rej.2009.0892 · Cited by 66

Oxidation of bovine serum albumin: identification of oxidation products and structural modifications

Guedes, S. D. M., Vitorino, R. M. P., Domingues, R., Amado, F. M. L., & Domingues, P. M. (2009) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.4149 · Cited by 66

Protein Carbonylation and Heat Shock Proteins in Human Skeletal Muscle: Relationships to Age and Sarcopenia

Beltran‐Valls, M. R., Wilkinson, D. J., Narici, M. V., Smith, K., Phillips, B. E., Caporossi, D., & Atherton, P. J. (2014) · The Journals of Gerontology Series A · doi:10.1093/gerona/glu007 · Cited by 69

Understanding Risk Factors for Alzheimer's Disease: Interplay of Neuroinflammation, Connexin-based Communication and Oxidative Stress

Quintanilla, R. A., Orellana, J. A., & Rommy von Bernhardi, M. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.016 · Cited by 67

Age‐associated mitochondrial dysfunction in skeletal muscle: Contributing factors and suggestions for long‐term interventions

Huang, J. H., & Hood, D. A. (2009) · IUBMB Life · doi:10.1002/iub.164 · Cited by 71

Protective effect of lavender oil on scopolamine induced cognitive deficits in mice and H2O2 induced cytotoxicity in PC12 cells

Xu, P., Wang, K., Lu, C., Dong, L., Gao, L., Yan, M., Aibai, S., & Liu, X. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.08.030 · Cited by 64

Pathophysiology of Lipid Droplets in Neuroglia

Smolič, T., Zorec, R., & Vardjan, N. (2021) · Antioxidants · doi:10.3390/antiox11010022 · Cited by 71

Oxidative stress in response to xenobiotics in the blue mussel Mytilus edulis L.: Evidence for variation along a natural salinity gradient of the Baltic Sea

Prevodnik, A., Gardeström, J., Lilja, K., Elfwing, T., McDonagh, B., Petrovič, N., Tedengren, M., Sheehan, D., & Bollner, T. (2007) · Aquatic Toxicology · doi:10.1016/j.aquatox.2007.01.006 · Cited by 64

Impairment of the mitochondrial electron transport chain due to sleep deprivation in mice

Andreazza, A. C., Andersen, M. L., Alvarenga, T. A., de Oliveira, M. R., Armani, F., Ruiz, F. S., Giglio, L. M. F., Moreira, J. C. F., Kapczinski, F. P., & Tufik, S. B. (2010) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2010.01.015 · Cited by 64

Super‐marathon race increases serum and urinary nitrotyrosine and carbonyl levels

Radak, Z. O., Ogonovszky, H., Dubecz, J., Pavlik, G., Sasvári, M., Pucsok, J. M., Berkes, I., Csont, T., & Ferdinandy, P. (2003) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2003.01202.x · Cited by 64

Mitochondrial pathobiology in ALS

Martin, L. J. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9395-y · Cited by 65

Targeting mitochondrial dysfunction in neurodegenerative disease: Part I

Burchell, V., Gandhi, S., Deas, E., Wood, N. W., Abramov, A. Y., & Plun‐Favreau, H. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728221003652489 · Cited by 64

Proinflammatory cytokines provoke oxidative damage to actin in neuronal cells mediated by Rac1 and NADPH oxidase

Barth, B. M., Smeets, S. S., & Kuhn, T. B. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.03.007 · Cited by 64

Preventive effects of North American ginseng (Panax quinquefolium) on diabetic nephropathy

Sen, S., Chen, S., Feng, B., Wu, Y., Lui, E. M. K., & Chakrabarti, S. (2012) · Phytomedicine · doi:10.1016/j.phymed.2012.01.001 · Cited by 62

Apelin/APJ system: A novel promising target for neurodegenerative diseases

Luo, H., Han, L., & Xu, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29001 · Cited by 61

Vascular calcium signalling and ageing

Harraz, O. F., & Jensen, L. J. (2021) · The Journal of Physiology · doi:10.1113/jp280950 · Cited by 62

Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases

Yeo, W., Kim, Y. J., Kabir, M. H., Kang, J. W., & Kim, K. P. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21429 · Cited by 61

Mechanistic inhibition of non-enzymatic glycation and aldose reductase activity by naringenin: Binding, enzyme kinetics and molecular docking analysis

Khan, M. S., Qais, F. A., Rehman, M. T., Ismail, M. H., Alokail, M. S., Altwaijry, N. A., Alafaleq, N. O., Alajmi, M. F., Salem, N., & Alqhatani, R. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.04.226 · Cited by 61

Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging

Gokulrangan, G., Zaidi, A., Michaelis, M. L., & Schöneich, C. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04334.x · Cited by 61

Glyburide inhibits non-enzymatic glycation of HSA: An approach for the management of AGEs associated diabetic complications

Qais, F. A., Sarwar, T., Ahmad, I., Khan, R. A., Shahzad, S. A., & Husain, F. M. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.096 · Cited by 60

Male rats exhibit higher oxidative protein damage than females of the same chronological age

Kayalı, R., Çakatay, U., & Tekeli, F. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.03.003 · Cited by 60

Cardiac mitochondrial damage and loss of ROS defense after burn injury: the beneficial effects of antioxidant therapy

Zang, Q. S., Maass, D. L., White, J., & Horton, J. W. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00359.2006 · Cited by 60

Environmental agents, oxidative stress and autoimmunity

Khan, M. F., & Wang, G. (2017) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.10.012 · Cited by 58

Effect of high-glucose levels on protein oxidation in cultured lens cells, and in crystalline and albumin solution and its inhibition by vitamin B6 and N-acetylcysteine: its possible relevance to cataract formation in diabetes

Jain, A. K., Lim, G., Langford, M. P., & Jain, S. K. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01109-7 · Cited by 60

Enhanced reactivity to malondialdehyde-modified proteins by systemic lupus erythematosus autoantibodies

Mansour, R. B., Lassoued, S., Elgaied, A. B. A., Haddouk, S., Marzouk, S., Bahloul, Z., Masmoudi, H., Attia, H., Aifa, S., & Fakhfakh, F. (2010) · Scandinavian Journal of Rheumatology · doi:10.3109/03009740903362511 · Cited by 59

Neuroprotective Effects of Açaí (Euterpe oleracea Mart.) against Rotenone In Vitro Exposure

Machado, A. K., Andreazza, A. C., da Silva, T. M., Boligon, A. A., do Nascimento, V., Scola, G., Duong, A., Cadoná, F. C., Ribeiro, E. E., & da Cruz, I. B. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8940850 · Cited by 60

Inhibition of cathepsins and related proteases by amino acid, peptide, and protein hydroperoxides

Headlam, H. A., Gracanin, M., Rodgers, K. J., & Davies, M. J. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.12.036 · Cited by 59

Uncoupling-mediated generation of reactive oxygen by halogenated aromatic hydrocarbons in mouse liver microsomes

Shertzer, H. G., Clay, C. D., Genter, M. B., Chames, M. C., Schneider, S. N., Oakley, G. G., Nebert, D. W., & Dalton, T. P. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.11.014 · Cited by 59

Parkinson's disease genetic mutations increase cell susceptibility to stress: Mutant α-synuclein enhances H2O2- and Sin-1-induced cell death

Jiang, H., Wu, Y.-C., Nakamura, M., Liang, Y., Tanaka, Y., Holmes, S., Dawson, V. L., Dawson, T. M., Ross, C. A., & Smith, W. W. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.07.017 · Cited by 62

Increased oxidative stress in the mitochondria isolated from lymphocytes of bipolar disorder patients during depressive episodes

Valvassori, S. S., Bavaresco, D. V., Feier, G., Recco, K. C. C., Steckert, A. V., Varela, R. B., Borges, C. P., Carvalho‐Silva, M., Gomes, L. M., STRECK, E. L., et al. (2018) · Psychiatry Research · doi:10.1016/j.psychres.2018.03.089 · Cited by 58

Prevention of Peroxynitrite-induced Apoptosis of Motor Neurons and PC12 Cells by Tyrosine-containing Peptides

Ye, Y., Quijano, C., Robinson, K. M., Ricart, K. C., Strayer, A. L., Garner, M. A., Shacka, J. J., KIRK, M. C., Barnes, S., Accavitti-Loper, M. A., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610800200 · Cited by 58

Chitosan Oligosaccharides Attenuates Oxidative-Stress Related Retinal Degeneration in Rats

Fang, I., Yang, C., Yang, C., & Chen, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077323 · Cited by 57

Toll-like Receptor 2 Is Essential for the Sensing of Oxidants during Inflammation

Paul‐Clark, M. J., McMaster, S. K., Sorrentino, R., Sriskandan, S., Bailey, L. K., Moreno, L., Ryffel, B., Quesniaux, V. F. J., & Mitchell, J. A. (2008) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200707-1019oc · Cited by 57

The Effects of Apigenin-Biosynthesized Ultra-Small Platinum Nanoparticles on the Human Monocytic THP-1 Cell Line

Gurunathan, S., Jeyaraj, M., Kang, M.-H., & Kim, J. (2019) · Cells · doi:10.3390/cells8050444 · Cited by 57

Age-dependent modulation of DNA repair enzymes by covalent modification and subcellular distribution

Szczęsny, B., Bhakat, K. K., MITRA, S. P., & Boldogh, I. R. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.07.005 · Cited by 56

The role of metallothionein II in neuronal differentiation and survival

Køhler, L. B., Berezin, V., Bock, E., & Penkowa, M. (2003) · Brain Research · doi:10.1016/j.brainres.2003.08.049 · Cited by 57

A systematic review of molecular approaches that link mitochondrial dysfunction and neuroinflammation in Parkinson’s disease

Mani, S., Sevanan, M., Krishnamoorthy, A., & Sekar, S. (2021) · Neurological Sciences · doi:10.1007/s10072-021-05551-1 · Cited by 59

Antioxidant Function of Isoflavone and 3,3′-Diindolylmethane: Are They Important for Cancer Prevention and Therapy?

Li, Y., Kong, D., Ahmad, A., Bao, B., & Sarkar, F. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5233 · Cited by 56

Pulse Radiolysis Studies for Mechanism in Biochemical Redox Reactions

Kobayashi, K. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00405 · Cited by 57

Induction of motor neuron apoptosis by free 3‐nitro‐ l ‐tyrosine

Peluffo, H., Shacka, J. J., Ricart, K. C., Bisig, C. G., Palma, L. M., Pritsch, O., Kamaid, A., Eiserich, J. P., Crow, J. P., Barbeito, L., et al. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2004.02363.x · Cited by 56

Protective action of fenugreek (Trigonella foenum graecum) seed polyphenols against alcohol-induced protein and lipid damage in rat liver

Kaviarasan, S., Sundarapandiyan, R., & Anuradha, C. V. (2008) · Cell Biology and Toxicology · doi:10.1007/s10565-007-9050-x · Cited by 54

Oxidative Stress and Protein Oxidation in Pseudoexfoliation Syndrome

Yağcı, R., Gürel, A., Ersöz, İ., Keskin, U. C., Hepşen, İ. F., Duman, S., & Yiğitoğlu, R. (2006) · Current Eye Research · doi:10.1080/02713680601001319 · Cited by 55

Selective vulnerability of motoneuron and perturbed mitochondrial calcium homeostasis in amyotrophic lateral sclerosis: implications for motoneurons specific calcium dysregulation

Jaiswal, M. K. (2014) · Molecular and Cellular Therapies · doi:10.1186/2052-8426-2-26 · Cited by 56

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RNA Granules and Diseases: A Case Study of Stress Granules in ALS and FTLD

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Estrogen-provided cardiac protection following burn trauma is mediated through a reduction in mitochondria-derived DAMPs

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Behavior of Oxidative Stress Markers in Alcoholic Liver Cirrhosis Patients

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Luteolin Suppresses Cisplatin-Induced Apoptosis in Auditory Cells: Possible Mediation Through Induction of Heme Oxygenase-1 Expression

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Methylene blue prevents methylmalonate-induced seizures and oxidative damage in rat striatum

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15-Deoxy-Δ12,14-Prostaglandin J2 Protects against Nitrosative PC12 Cell Death through Up-regulation of Intracellular Glutathione Synthesis

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Oxidative Stress and Atherosclerosis

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Targeting NADPH Oxidase and Phospholipases A2 in Alzheimer’s Disease

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Potential cytoprotection: antioxidant defence by caffeic acid phenethyl ester against free radical-induced damage of lipids, DNA, and proteins

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Free radical processes in aging, neurodegenerative diseases and other pathological states

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Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease

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Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

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