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

Uncovering Neurodegenerative Protein Modifications via Proteomic Profiling

Gallart‐Palau, X., Serra, A., & Sze, S. K. (2015) · International review of neurobiology · doi:10.1016/bs.irn.2015.06.002 · Cited by 29

Drosophila Ubiquitin C-Terminal Hydrolase Knockdown Model of Parkinson’s Disease

Tran, H., Dang, S., Nguyễn, T. T., Huynh, M. A., Đào, L. M., Kamei, K., Yamaguchi, M., & Thảo, Đ. T. P. (2018) · Scientific Reports · doi:10.1038/s41598-018-22804-w · Cited by 31

LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess H 2 O 2

Kathiresan, M., & English, A. M. (2016) · Chemical Science · doi:10.1039/c6sc03125k · Cited by 30

Ubiquitin carboxyl-terminal hydrolase L-1 in brain: Focus on its oxidative/nitrosative modification and role in brains of subjects with Alzheimer disease and mild cognitive impairment

Butterfield, D. A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.10.036 · Cited by 31

Antioxidant and hepatoprotective activity of the methanol extract of Careya arborea bark in Ehrlich ascites carcinoma-bearing mice

Natesan, S., Badami, S., Dongre, S. H., & Bhojraj, S. (2008) · Journal of Natural Medicines · doi:10.1007/s11418-008-0237-0 · Cited by 30

Peroxynitrite Induces an Alternative NF-κB Activation Pathway in L8 Rat Myoblasts

Bar‐Shai, M., & Reznick, A. Z. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.639 · Cited by 31

Ethyl-EPA in Huntington disease—Potentially relevant mechanism of action

Murck, H., & Manku, M. (2007) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2006.10.020 · Cited by 30

Endomorphins, endogenous opioid peptides, provide antioxidant defense in the brain against free radical-induced damage

Lin, X., Yang, D.-J., Cai, W.-Q., Zhao, Q., Gao, Y., Chen, Q., & Wang, R. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2003.09.007 · Cited by 30

Carbonylation of platelet proteins occurs as consequence of oxidative stress and thrombin activation, and is stimulated by ageing and type 2 diabetes

Alexandru, N., Constantin, A. L., & Popov, D. (2008) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2008.104 · Cited by 29

Effects of the extract of Anemopaegma mirandum (Catuaba) on Rotenone-induced apoptosis in human neuroblastomas SH-SY5Y cells

Andrade, D. V. G. D., de Oliveria, D. M., Barreto, G. E., Bertolino, L.-A., Saraceno, G. E., Capani, F., & Giráldez, L. (2008) · Brain Research · doi:10.1016/j.brainres.2008.01.006 · Cited by 29

Mitochondrial oxidative stress in female and male rat brain after ex vivo carbon monoxide treatment

Taşkıran, D., Nesil, T., & Alkan, K. (2007) · Human & Experimental Toxicology · doi:10.1177/0960327107076882 · Cited by 28

Upstream Pathways Controlling Mitochondrial Function in Major Psychosis

Machado, A. K., Pan, A. Y., da Silva, T. M., Duong, A., & Andreazza, A. C. (2016) · The Canadian Journal of Psychiatry · doi:10.1177/0706743716648297 · Cited by 30

New insights into non-enzymatic glycation of human serum albumin biopolymer: A study to unveil its impaired structure and function

Raghav, A., Ahmad, J., Alam, K., & Khan, A. U. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.03.086 · Cited by 28

Molecular mechanisms of action of styrene toxicity in blood plasma and liver

Niaz, K., Mabqool, F., Khan, F., Hassan, F. I., Baeeri, M., Nigjeh, M. N., Hassani, S., Gholami, M., & Abdollahi, M. R. (2017) · Environmental Toxicology · doi:10.1002/tox.22441 · Cited by 29

Mitochondria-Targeting Antioxidant Provides Cardioprotection through Regulation of Cytosolic and Mitochondrial Zn2+ Levels with Re-Distribution of Zn2+-Transporters in Aged Rat Cardiomyocytes

Olğar, Y., Tuncay, E., & Turan, B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153783 · Cited by 29

Burn serum causes a CD14-dependent mitochondrial damage in primary cardiomyocytes

Zang, Q. S., Maass, D. L., Wigginton, J. G., Barber, R. C., Martinez, B., Idris, A. H., Horton, J. W., & Nwariaku, F. E. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00927.2009 · Cited by 29

A new technique for the quantitative assessment of 8-oxoguanine in nuclear DNA as a marker of oxidative stress. Application to dystrophin-deficient DMD skeletal muscles

Nakae, Y., Stoward, P. J., Bespalov, I. A., Melamede, R. J., & Wallace, S. S. (2005) · Histochemistry and Cell Biology · doi:10.1007/s00418-005-0037-5 · Cited by 28

Sepsis-induced Cardiac Mitochondrial Damage and Potential Therapeutic Interventions in the Elderly

Zang, Q. S. (2014) · Aging and Disease · doi:10.14336/ad.2014.0500137 · Cited by 28

Bioflavonoid (Hesperidin) Restrains Protein Oxidation and Advanced Glycation End Product Formation by Targeting AGEs and Glycolytic Enzymes

Khan, M. S., Rehman, M. T., Alajmi, M. F., Alajmi, M. F., Alruwaished, G. I., Alokail, M. S., & Khan, M. R. (2021) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-021-00997-8 · Cited by 28

The potential role of Keap1-Nrf2 pathway in the pathogenesis of Alzheimer’s disease, type 2 diabetes, and type 2 diabetes-related Alzheimer’s disease

He, L., & Sun, Y. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00762-z · Cited by 30

Studies on peroxynitrite-modified H1 histone: Implications in systemic lupus erythematosus

Khan, M. A., Dixit, K., Moinuddin, M., Arif, Z., & Alam, K. (2013) · Biochimie · doi:10.1016/j.biochi.2013.09.026 · Cited by 28

Oxidative damage of aromatic dipeptides by the environmental oxidants NO 2 ˙ and O 3

Gamon, L. F., White, J. M., & Wille, U. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob01577k · Cited by 28

Combinatorial Determination of Ischemia Modified Albumin and Protein Carbonyl in the Diagnosis of NonST-Elevation Myocardial Infarction

Maneewong, K., Mekrungruangwong, T., Luangaram, S., Thongsri, T., & Kumphune, S. (2011) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-011-0118-2 · Cited by 28

Effects of glutathione, Trolox and desferrioxamine on hemoglobin-induced protein oxidative damage: Anti-oxidant or pro-oxidant?

Lu, N., Chen, W., & Peng, Y. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.03.009 · Cited by 28

In Vivo and In Vitro Effects of Metals in Reactive Oxygen Species Production, Protein Carbonylation, and DNA Damage in Land Snails Eobania vermiculata

Itziou, A., Kaloyianni, M. G., & Dimitriadis, V. K. (2010) · Archives of Environmental Contamination and Toxicology · doi:10.1007/s00244-010-9583-5 · Cited by 28

Oral integrity and salivary profile in myeloma patients undergoing high-dose therapy followed by autologous SCT

Avivi, I. M., Avraham, S., Koren‐Michowitz, M., Zuckerman, T., Aviv, A., Ofran, Y., Benyamini, N., Nagler, A., Rowe, J. M., & Nagler, R. M. (2008) · Bone Marrow Transplantation · doi:10.1038/bmt.2008.387 · Cited by 29

The polyphenol quercetin protects themev‐1mutant ofCaenorhabditis elegansfrom glucose‐induced reduction of survival under heat‐stress depending on SIR‐2.1, DAF‐12, and proteasomal activity

Fitzenberger, E., Deusing, D. J., Marx, C., Boll, M., Lüersen, K., & Wenzel, U. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201300718 · Cited by 27

The molecular mechanism of aging and the role in neurodegenerative diseases

Zhao, J., Han, Z.-J., Ding, L., Wang, P., He, X., & Li, L. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e24751 · Cited by 35

Role of peroxynitrite induced structural changes on H2B histone by physicochemical method

Khan, M. A., Alam, K., Dixit, K., & Rizvi, M. M. A. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.10.085 · Cited by 27

Lophirones B and C Extenuate AFB1‐Mediated Oxidative Onslaught on Cellular Proteins, Lipids, and DNA through Nrf‐2 Expression

Ajiboye, T. O., Yakubu, M. T., & Oladiji, A. T. (2014) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.21598 · Cited by 27

Toxicity of four pharmaceuticals from different classes to isolated plankton species

El-Bassat, R., Touliabah, H. E.-S., & Harisa, G. I. (2012) · African Journal of Aquatic Science · doi:10.2989/16085914.2012.666376 · Cited by 27

The protective effect of ascorbic acid derivative on PC12 cells: Involvement of its ROS scavenging ability

Du, C., Liu, J., Su, W., Ren, Y., & Wei, D. (2003) · Life Sciences · doi:10.1016/j.lfs.2003.07.014 · Cited by 27

Physicochemical and immunological studies on 4-hydroxynonenal modified HSA: Implications of protein damage by lipid peroxidation products in the etiopathogenesis of SLE

Khatoon, F., Moinuddin, M., Alam, K., & Ali, A. (2012) · Human Immunology · doi:10.1016/j.humimm.2012.08.011 · Cited by 27

The cyclooxygenase site, but not the peroxidase site of cyclooxygenase‐2 is required for neurotoxicity in hypoxic and ischemic injury

Li, W., Wu, S., Ahmad, M., Jiang, J., Liu, H., Nagayama, T., Rose, M. E., Tyurin, V. A., Tyurina, Y. Y., Borisenko, G. G., et al. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06674.x · Cited by 27

Oxidatively modified proteins and DNA in digestive gland cells of the fresh-water mussel Unio tumidus in the presence of tannic acid and its derivatives

Łabieniec, M., & Gabryelak, T. (2006) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2005.10.013 · Cited by 27

Antioxidant network expression abrogates oxidative posttranslational modifications in mice

Mital, R., Zhang, W., Cai, M., Huttinger, Z. M., Goodman, L. A., Wheeler, D. G., Ziolo, M. T., Dwyer, K. M., D'Apice, A. J. F., Zweier, J. L., et al. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01285.2010 · Cited by 27

Implications for oxidative stress and astrocytes following 26S proteasomal depletion in mouse forebrain neurones

Elkharaz, J., Ugun‐Klusek, A., Constantin‐Teodosiu, D., Lawler, K., Mayer, R. J., Billett, E. E., Lowe, J. S., & Bedford, L. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.07.002 · Cited by 28

Effects of Plant Extracts on the Reversal of Glucose-Induced Impairment of Stress-Resistance in Caenorhabditis elegans

Fitzenberger, E., Deusing, D. J., Wittkop, A., Kler, A., Kriesl, E., Bonnländer, B., & Wenzel, U. (2014) · Plant Foods for Human Nutrition · doi:10.1007/s11130-013-0399-0 · Cited by 26

Cerebrovascular expression of proteins related to inflammation, oxidative stress and neurotoxicity is altered with aging

Tripathy, D., Yin, X., Sanchez, A. C., Luo, J., Martinez, J. M., & Grammas, P. (2010) · Journal of Neuroinflammation · doi:10.1186/1742-2094-7-63 · Cited by 26

Protective effect of apocynin on antimycin A‐induced cell damage in osteoblastic MC3T3 ‐E1 cells

Choi, E. M., & Lee, Y. (2011) · Journal of Applied Toxicology · doi:10.1002/jat.1689 · Cited by 26

Malondialdehyde Suppresses Cerebral Function by Breaking Homeostasis between Excitation and Inhibition in Turtle Trachemys scripta

Li, F., Yang, Z., Yang, L., Wei, Y., Wang, J., Yin, D., & He, R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015325 · Cited by 26

A comparative ‘bottom up’ proteomics strategy for the site-specific identification and quantification of protein modifications by electrophilic lipids

Han, B., Hare, M. C., Wickramasekara, S. I., Fang, Y., & Maier, C. S. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.07.029 · Cited by 26

Cumulative 3-nitrotyrosine in specific muscle proteins is associated with muscle loss during aging

Murakami, H., Guillet, C., Tardif, N., Salles, J., Migné, C., Boirie‌, Y., & Walrand, S. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.11.007 · Cited by 29

Mitochondrial dysfunction and lipid peroxidation in rat frontal cortex by chronic NMDA administration can be partially prevented by lithium treatment

Kim, H. K., Isaacs-Trepanier, C., Elmi, N., Rapoport, S. I., & Andreazza, A. C. (2016) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2016.02.001 · Cited by 26

Identification of Temporal Characteristic Networks of Peripheral Blood Changes in Alzheimer’s Disease Based on Weighted Gene Co-expression Network Analysis

Tang, R.-H., & Liu, H. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00083 · Cited by 27

Proteomics and Redox-Proteomics of the Effects of Herbicides on a Wild-Type WineSaccharomyces cerevisiaeStrain

Braconi, D., Bernardini, G., Possenti, S., Laschi, M., Arena, S., Scaloni, A., Geminiani, M., Sotgiu, M., & Santucci, A. (2008) · Journal of Proteome Research · doi:10.1021/pr800372q · Cited by 26

Quantification of 3‐Nitrotyrosine Levels Using a Benchtop Ion Trap Mass Spectrometry Method

Nicholls, S. J., Shen, Z., Fu, X., Levison, B. S., & Hazen, S. L. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96022-9 · Cited by 25

Astrocyte plasticity revealed by adaptations to severe proteotoxic stress

Titler, A. M., Posimo, J. M., & Leak, R. K. (2013) · Cell and Tissue Research · doi:10.1007/s00441-013-1571-4 · Cited by 25

Neutrophil-mediated oxidation of enkephalins via myeloperoxidase-dependent addition of superoxide

Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.033 · Cited by 24

A synthetic chalcone derivative, 2-hydroxy-3′,5,5′-trimethoxychalcone (DK-139), triggers reactive oxygen species-induced apoptosis independently of p53 in A549 lung cancer cells

Gil, H.-N., Jung, E., Koh, D., Lim, Y., Lee, Y. H., & Shin, S. Y. (2018) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2018.11.003 · Cited by 24

Involvement of NO in the convulsive behavior and oxidative damage induced by the intrastriatal injection of methylmalonate

Royes, L. F. F., Fighera, M. R., Furian, A. F., Oliveira, M. S., Fiorenza, N. G., Myskiw, J. D. C., Frussa‐Filho, R., & Mello, C. F. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.11.038 · Cited by 24

Nitrite and nitrotyrosine concentrations in articular cartilage, subchondral bone, and trabecular bone of normal juvenile, normal adult, and osteoarthritic adult equine metacarpophalangeal joints.

van der Harst, M. R., Bull, S., Brama, P. A. J., Barneveld, A., van Weeren, P. R., & van de Lest, C. H. A. (2006) · PubMed · Cited by 24

Protective Effects of Propolis and Chitosan Nanoparticles against Ibuprofen-Induced Hepatotoxicity in Albino Rats

AlKandari, F. M., Mohamed, H. S., Ahmed, S. A., Mahmoud, B., & Mahmoud, A. M. (2024) · Diseases · doi:10.3390/diseases12030049 · Cited by 23

Brain iron metabolism and its perturbation in neurological diseases

Crichton, R. R., Dexter, D. T., & Ward, R. J. (2011) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-011-0472-z · Cited by 23

Oxidative modifications in glycated insulin

Guedes, S. D. M., Vitorino, R. M. P., Domingues, M. R., Amado, F. M. L., & Domingues, P. M. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-3757-x · Cited by 23

Shotgun Redox Proteomics: Identification and Quantitation of Carbonylated Proteins in the UVB-Resistant Marine Bacterium, Photobacterium angustum S14

Matallana‐Surget, S., Cavicchioli, R., Fauconnier, C., Wattiez, R., Leroy, B., Joux, F., Raftery, M. J., & Lebaron, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068112 · Cited by 23

·OH Oxidation Toward S- and OH-Containing Amino Acids

Uranga, J., Mujika, J. I., & Matxain, J. M. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b09825 · Cited by 23

Unsaturated aldehyde, 4-hydroxynonenal (HNE) alters the structural integrity of HSA with consequences in the immuno-pathology of rheumatoid arthritis

Khan, F., Moinuddin, M., Mir, A. R., Islam, S., Abidi, M., Husain, M. A., & Khan, R. H. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.01.188 · Cited by 23

High throughput assay for evaluation of reactive carbonyl scavenging capacity

Vidal, N., Cavaille, J. P., Graziani, F., Robin, M., Ouari, O., Pietri, S., & Stocker, P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.01.016 · Cited by 23

Trichloroethylene metabolism in the rat ovary reduces oocyte fertilizability

Wu, K. L., & Berger, T. (2007) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2007.06.038 · Cited by 23

Improved Anti‐Inflammatory and Pharmacokinetic Properties for Superoxide Dismutase by Chemical Glycosidation with Carboxymethylchitin

Valdivia, A., Pérez, Y., Domínguez, A., Caballero, J., Gómez, L., Schacht, E. H., & Villalonga, R. (2005) · Macromolecular Bioscience · doi:10.1002/mabi.200400114 · Cited by 23

Brain iron metabolism and its perturbation in neurological diseases

Crichton, R. R., Dexter, D. T., & Ward, R. J. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_1 · Cited by 22

P2X7 Receptor: an Emerging Target in Alzheimer’s Disease

Huang, Q., Ying, J., Yu, W., Dong, Y., Xiong, H., Zhang, Y., Liu, J., Wang, X., & Hua, F. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03699-9 · Cited by 26

Mutation in G6PD gene leads to loss of cellular control of protein glutathionylation: Mechanism and implication

Ayene, I. S., Biaglow, J. E., Kachur, A. V., Stamato, T. D., & Koch, C. J. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21394 · Cited by 22

Optimization and application of microwave-assisted acid hydrolysis for rapid quantification of protein oxidation markers using LC–MS

Afiuni‐Zadeh, S., Guo, X., Azimi, G., & Lankmayr, E. P. (2011) · Talanta · doi:10.1016/j.talanta.2011.07.050 · Cited by 22

Study of interactions between phenolic compounds and H2O2 or Cu(II) ions in B14 Chinese hamster cells

Łabieniec, M., & Gabryelak, T. (2006) · Cell Biology International · doi:10.1016/j.cellbi.2006.05.013 · Cited by 22

A top-down LC-FTICR MS-based strategy for characterizing oxidized calmodulin in activated macrophages

Lourette, N. M., Smallwood, H. S., Wu, S., Robinson, E. W., Squier, T. C., Smith, R. D., & Paša‐Tolić, L. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2010.02.027 · Cited by 22

Oxidative Damage Mediated by Herbicides on Yeast Cells

Braconi, D., Possenti, S., Laschi, M., Geminiani, M., Lusini, P., Bernardini, G., & Santucci, A. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf800074p · Cited by 22

Protective effects of endomorphins, endogenous opioid peptides in the brain, on human low density lipoprotein oxidation

Lin, X., Xue, L.-Y., Wang, R., Zhao, Q., & Chen, Q. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05150.x · Cited by 22

Weight increase and overweight are associated with DNA oxidative damage in skeletal muscle

de la Maza, M. P., Olivares, D., Hirsch, S., Sierralta, W. D., Vivien Gattas, Z., Barrera, G., Bunout, D. C., Leiva, L., & Fernández, M. (2006) · Clinical Nutrition · doi:10.1016/j.clnu.2006.02.008 · Cited by 22

Oxidative Protein Damage Is Associated With Elevated Serum Interleukin-6 Levels Among Older Moderately to Severely Disabled Women Living in the Community

Dayhoff-Brannigan, M., Ferrucci, L., Sun, K., Fried, L. P., Walston, J. D., Varadhan, R., Guralnik, J. M., & Semba, R. D. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.2.179 · Cited by 22

Prevalence of auto-antibodies against D-ribose-glycated-hemoglobin in diabetes mellitus

Siddiqui, Z., Faisal, M., Alatar, A. R., & Ahmad, S. (2019) · Glycobiology · doi:10.1093/glycob/cwz012 · Cited by 21

Modulation of Cell Death in Age-Related Diseases

Tezil, T., & Başağa, H. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660702 · Cited by 21

The Clinical Application of Ozonetherapy

Bocci, V. A. (2010) · Springer eBooks · doi:10.1007/978-90-481-9234-2_9 · Cited by 24

Influence of selenium on the emergence of neuro tubule defects in a neuron-like cell line and its implications for amyotrophic lateral sclerosis

Maraldi, T., Beretti, F., Anselmi, L., Franchin, C., Arrigoni, G., Braglia, L., Mandrioli, J., Vinceti, M., & Marmiroli, S. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.09.015 · Cited by 21

Influence of feeding thermally peroxidized soybean oil on growth performance, digestibility, gut integrity, and oxidative stress in nursery pigs

Kerr, B. J., Lindblom, S. C., & Overholt, M. F. (2020) · Journal of Animal Science · doi:10.1093/jas/skaa016 · Cited by 21

Effects of Rhus tripartitum fruit extract on CCl 4 -induced hepatotoxicity and cisplatin-induced nephrotoxicity in rats

Tlili, N., Feriani, A., Allagui, M. S., Saadoui, E., Khaldi, A., & Nasri, N. (2016) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2016-0029 · Cited by 21

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Binding and Repressive Activities of Apolipoprotein E3 and E4 Isoforms on the Human ApoD Promoter

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Repair of Protein Radicals by Antioxidants

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Multiple measures of functionality exhibit progressive decline in a parallel, stochastic fashion in Drosophila Sod2 null mutants

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Salivary Gland Dysfunction in Patients with Chronic Heart Failure Is Aggravated by Nitrosative Stress, as Well as Oxidation and Glycation of Proteins

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Human Ran Cysteine 112 Oxidation by Pervanadate Regulates Its Binding to Keratins

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