Protein Oxidation in Aging, Disease, and Oxidative Stress

Mechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite

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Mitochondria, Oxidants, and Aging

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Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases

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Protein degradation and protection against misfolded or damaged proteins.

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Vitamin C as an Antioxidant: Evaluation of Its Role in Disease Prevention

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Molecular biomarkers of oxidative stress in aquatic organisms in relation to toxic environmental pollutants

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The Immunomodulatory and Anti-Inflammatory Role of Polyphenols

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The IKK NF-κB system: a treasure trove for drug development

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The antioxidant properties of serum albumin

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Chronic inflammation and oxidative stress in human carcinogenesis

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Oxidation events and skin aging

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Protein carbonylation in human diseases

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Toward a new recommended dietary allowance for vitamin C based on antioxidant and health effects in humans

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An integrated view of oxidative stress in aging: basic mechanisms, functional effects, and pathological considerations

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Mitochondrial damage induced by conditions of oxidative stress

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Reactive oxygen species, aging and antioxidative nutraceuticals

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Oxidative Stress: Relationship with Exercise and Training

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Drug-induced oxidative stress and toxicity

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Functions of ROS in Macrophages and Antimicrobial Immunity

Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633

p62 Is a Common Component of Cytoplasmic Inclusions in Protein Aggregation Diseases

Zatloukal, K., Stumptner, C., Fuchsbichler, A., Heid, H., Schnoelzer, M., Kenner, L., Kleinert, R., Prinz, M., Aguzzi, A., & Denk, H. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64369-6 · Cited by 624

Physiology of the prion protein

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Photoaging: mechanisms and repair

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Proteomic identification of oxidatively modified proteins in Alzheimer’s disease brain. Part I: Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1

Castegna, A., Aksenov, M., Aksenova, M., Thongboonkerd, V., Klein, J. B., Pierce, W. M., Booze, R., Markesbery, W. R., & Butterfield, D. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00914-0 · Cited by 581

Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging

Salminen, A., Huuskonen, J., Ojala, J., Kauppinen, A., Kaarniranta, K., & Suuronen, T. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2007.09.002 · Cited by 581

Ageing, age-related diseases and oxidative stress: What to do next?

Luo, J., Mills, K., le Cessie, S., Noordam, R., & van Heemst, D. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100982 · Cited by 581

Roles of amyloid β-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment

Butterfield, D. A., Reed, T., Newman, S. F., & Sultana, R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.037 · Cited by 564

Aging as an event of proteostasis collapse

Taylor, R. C., & Dillin, A. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004440 · Cited by 538

Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism

Bota, D. A., & Davies, K. J. A. (2002) · Nature Cell Biology · doi:10.1038/ncb836 · Cited by 557

Stable markers of oxidant damage to proteins and their application in the study of human disease

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Oxidative stress in Alzheimer disease

Gella, A., & Durany, N. (2009) · Cell Adhesion & Migration · doi:10.4161/cam.3.1.7402 · Cited by 459

Adiposopathy

Bays, H. E. (2011) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2011.02.038 · Cited by 431

Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins

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Mitochondrial adenine nucleotide translocase is modified oxidatively during aging

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Regulation of cell function by methionine oxidation and reduction

Hoshi, T., & Heinemann, S. H. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.0001j.x · Cited by 384

On the biodegradability of polyethylene glycol, polypeptoids and poly(2-oxazoline)s

Ulbricht, J., Jordan, R., & Luxenhofer, R. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.02.029 · Cited by 348

Pathophysiology of oxidative stress in diabetes mellitus

Lipinski, B. (2001) · Journal of Diabetes and its Complications · doi:10.1016/s1056-8727(01)00143-x · Cited by 324

Mechanisms that Regulate Stem Cell Aging and Life Span

Signer, R. A. J., & Morrison, S. J. (2013) · Cell Stem Cell · doi:10.1016/j.stem.2013.01.001 · Cited by 320

Natural and synthetic antioxidants: An updated overview

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Redox regulation of protein kinases

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Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: Implications for degradation of oxidized proteins

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Exercise training decreases DNA damage and increases DNA repair and resistance against oxidative stress of proteins in aged rat skeletal muscle

Radák, Z., Naito, H., Kaneko, T., Tahara, S., Nakamoto, H., Takahashi, R., Cardozo-Pelaez, F., & Goto, S. (2002) · Pfl�gers Archiv European Journal of Physiology · doi:10.1007/s00424-002-0918-6 · Cited by 269

Evidence of Oxidative Stress in the Neocortex in Incidental Lewy Body Disease

Dalfó, E., Portero-Otín, M., Ayala, V., Martínez, A., Pamplona, R., & Ferrer, I. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000179050.54522.5a · Cited by 261

Aging Hallmarks and Progression and Age-Related Diseases: A Landscape View of Research Advancement

Tenchov, R., Sasso, J. M., Wang, X., & Zhou, Q. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00531 · Cited by 276

The Triplet Code From First Principles

Trifonov, E. N. (2004) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2004.10506975 · Cited by 246

Mitochondrial dysfunction leads to telomere attrition and genomic instability

Liu, L., Trimarchi, J. R., Smith, P. J. S., & Keefe, D. L. (2002) · Aging Cell · doi:10.1046/j.1474-9728.2002.00004.x · Cited by 237

Mechanisms of Resistance to Oxidative and Nitrosative Stress: Implications for Fungal Survival in Mammalian Hosts

Missall, T. A., Lodge, J. K., & McEwen, J. E. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.4.835-846.2004 · Cited by 223

The Importance of Proteins in Defense Against Oxidation

Bourdon, E., & Blache, D. (2001) · Antioxidants & Redox Signaling · doi:10.1089/152308601300185241 · Cited by 220

Oxidative Damage to Specific Proteins in Replicative and Chronological-aged Saccharomyces cerevisiae

Reverter-Branchat, G., Cabiscol, E., Tamarit, J., & Ros, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404849200 · Cited by 218

Endogenous oxidative stress: relationship to aging, longevity and caloric restriction

Barja, G. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00008-9 · Cited by 215

Oxidatively damaged proteins of heart mitochondrial electron transport complexes

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Sources and implications of NADH/NAD+ redox imbalance in diabetes and its complications

Yan, L.-J., Wu, J., Jin, Z., & Zheng, H. (2016) · Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy · doi:10.2147/dmso.s106087 · Cited by 198

Glutathione Peroxidase-1 Regulates Mitochondrial Function to Modulate Redox-dependent Cellular Responses

Handy, D. E., Lubos, E., Yang, Y., Galbraith, J. D., Kelly, N., Zhang, Y.-Y., Leopold, J. A., & Loscalzo, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900392200 · Cited by 187

Reactive oxygen species: the unavoidable environmental insult?

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Oxidative damage and phospholipid fatty acyl composition in skeletal muscle mitochondria from mice underexpressing or overexpressing uncoupling protein 3

BRAND, M. D., PAMPLONA, R., PORTERO-OTÍN, M., REQUENA, J. R., ROEBUCK, S. J., BUCKINGHAM, J. A., CLAPHAM, J. C., & CADENAS, S. (2002) · Biochemical Journal · doi:10.1042/bj20021077 · Cited by 184

Apoptosis or Senescence-like Growth Arrest: Influence of Cell-Cycle Position, P53, P21 and Bax in H2O2 Response of Normal Human FIbroblasts

CHEN, Q. M., LIU, J., & MERRETT, J. B. (2000) · Biochemical Journal · doi:10.1042/bj3470543 · Cited by 280

Untitled work

Menzies (2007) · doi:10.1093/brain/awm223 · Cited by 177

Protein oxidative damage in the stratum corneum: evidence for a link between environmental oxidants and the changing prevalence and nature of atopic dermatitis in Japan.

Niwa, Y., Sumi, H., Kawahira, K., Terashima, T., Nakamura, T., & Akamatsu, H. (2003) · British Journal of Dermatology · doi:10.1046/j.1365-2133.2003.05417.x · Cited by 152

Interplay of Guanine Oxidation and G-Quadruplex Folding in Gene Promoters

Fleming, A. M., & Burrows, C. J. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b11050 · Cited by 152

Comparison of Anti-Oxidant and Anti-Inflammatory Effects between Fresh and Aged Black Garlic Extracts

Jeong, Y., Ryu, J., Shin, J.-H., Kang, M., Kang, J., Han, J., & Kang, D. (2016) · Molecules · doi:10.3390/molecules21040430 · Cited by 148

Transcriptional Signatures of Aging

Stegeman, R., & Weake, V. M. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.06.019 · Cited by 146

4-Hydroxynonenal-modified amyloid-β peptide inhibits the proteasome: possible importance in Alzheimer’s disease*

Shringarpure, R., Grune, T., Sitte, N., & Davies*, K. J. A. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000660 · Cited by 140

Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid

Salsbury, F. R., Knutson, S. T., Poole, L. B., & Fetrow, J. S. (2008) · Protein Science · doi:10.1110/ps.073096508 · Cited by 125

In vivo protective effects of ferulic acid ethyl ester against amyloid-beta peptide 1–42-induced oxidative stress

Perluigi, M., Joshi, G., Sultana, R., Calabrese, V., De Marco, C., Coccia, R., Cini, C., & Butterfield, D. A. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20879 · Cited by 125

Activation of the Nrf2 Cell Defense Pathway by Ancient Foods: Disease Prevention by Important Molecules and Microbes Lost from the Modern Western Diet

Senger, D. R., Li, D., Jaminet, S.-C., & Cao, S. (2016) · PLOS ONE · doi:10.1371/journal.pone.0148042 · Cited by 124

Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats

Moon, K.-H., Hood, B. L., Kim, B.-J., Hardwick, J. P., Conrads, T. P., Veenstra, T. D., & Song, B. J. (2006) · Hepatology · doi:10.1002/hep.21372 · Cited by 120

The Triangle of Death in Alzheimer's Disease Brain: The Aberrant Cross-Talk Among Energy Metabolism, Mammalian Target of Rapamycin Signaling, and Protein Homeostasis Revealed by Redox Proteomics

Di Domenico, F., Barone, E., Perluigi, M., & Butterfield, D. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6759 · Cited by 114

Increased Protein and Lipid Oxidative Damage in Mitochondria Isolated from Lymphocytes from Patients with Alzheimer's Disease: Insights into the Role of Oxidative Stress in Alzheimer's Disease and Initial Investigations into a Potential Biomarker for this Dementing Disorder

Sultana, R., Mecocci, P., Mangialasche, F., Cecchetti, R., Baglioni, M., & Butterfield, D. A. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-101425 · Cited by 111

Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria

Yarian, C. S., Rebrin, I., & Sohal, R. S. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.135 · Cited by 111

Identification of α-dicarbonyl scavengers for cellular protection against carbonyl stress

Wondrak, G. T., Cervantes-Laurean, D., Roberts, M. J., Qasem, J. G., Kim, M., Jacobson, E. L., & Jacobson, M. K. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00915-7 · Cited by 108

Protein Carbonylation in Skeletal Muscles: Impact on Function

Barreiro, E., & Hussain, S. N. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2808 · Cited by 108

IRS2 increases mitochondrial dysfunction and oxidative stress in a mouse model of Huntington disease

Sadagurski, M., Cheng, Z., Rozzo, A., Palazzolo, I., Kelley, G. R., Dong, X., Krainc, D., & White, M. F. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46305 · Cited by 107

Inside the β Cell: Molecular Stress Response Pathways in Diabetes Pathogenesis

Kulkarni, A., Muralidharan, C., May, S. C., Tersey, S. A., & Mirmira, R. G. (2022) · Endocrinology · doi:10.1210/endocr/bqac184 · Cited by 95

Maternal serum metabolome and traffic-related air pollution exposure in pregnancy

Yan, Q., Liew, Z., Uppal, K., Cui, X., Ling, C., Heck, J. E., von Ehrenstein, O. S., Wu, J., Walker, D. I., Jones, D. P., et al. (2019) · Environment International · doi:10.1016/j.envint.2019.05.066 · Cited by 91

Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1–10, 1–16 fragments of human and mouse β-amyloid peptide

Kowalik-Jankowska, T., Ruta, M., Wiśniewska, K., Łankiewicz, L., & Dyba, M. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.03.001 · Cited by 92

The oxidative damage theory of aging

Lin, M. T., & Flint Beal, M. (2003) · Clinical Neuroscience Research · doi:10.1016/s1566-2772(03)00007-0 · Cited by 89

Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells

Kim, B., Hood, B. L., Aragon, R. A., Hardwick, J. P., Conrads, T. P., Veenstra, T. D., & Song, B. J. (2006) · PROTEOMICS · doi:10.1002/pmic.200500447 · Cited by 83

Induction of Covalently Crosslinked p62 Oligomers with Reduced Binding to Polyubiquitinated Proteins by the Autophagy Inhibitor Verteporfin

Donohue, E., Balgi, A. D., Komatsu, M., & Roberge, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114964 · Cited by 79

Impact of fluoxetine on liver damage in rats

Inkielewicz-Stępniak, I. (2011) · Pharmacological Reports · doi:10.1016/s1734-1140(11)70510-2 · Cited by 75

Dose-Dependent Increase of Oxidative Damage in the Testes of Rats Subjected to Acute Iron Overload

Lucesoli, F., Caligiuri, M., Roberti, M. F., Perazzo, J. C., & Fraga, C. G. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1476 · Cited by 75

Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications

Song, B.-J., Abdelmegeed, M. A., Yoo, S.-H., Kim, B.-J., Jo, S. A., Jo, I., & Moon, K.-H. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.05.013 · Cited by 73

Redox proteomics identification of specifically carbonylated proteins in the hippocampi of triple transgenic Alzheimer’s disease mice at its earliest pathological stage

Shen, L., Chen, C., Yang, A., Chen, Y., Liu, Q., & Ni, J. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.04.005 · Cited by 73

C-Phycocyanin protects against acute tributyltin chloride neurotoxicity by modulating glial cell activity along with its anti-oxidant and anti-inflammatory property: A comparative efficacy evaluation with N-acetyl cysteine in adult rat brain

Mitra, S., Siddiqui, W. A., & Khandelwal, S. (2015) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2015.06.016 · Cited by 67

Increased nitroxidative stress promotes mitochondrial dysfunction in alcoholic and nonalcoholic fatty liver disease

Song, B.-J., Abdelmegeed, M. A., Henderson, L. E., Yoo, S.-H., Wan, J., Purohit, V., Hardwick, J. P., & Moon, K.-H. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/781050 · Cited by 67

Analysis of protein carbonylation — pitfalls and promise in commonly used methods

Rogowska-Wrzesinska, A., Wojdyla, K., Nedić, O., Baron, C. P., & Griffiths, H. R. (2014) · Free Radical Research · doi:10.3109/10715762.2014.944868 · Cited by 65

Urinary oxidative stress markers in children with autism

Damodaran, L. P. M., & Arumugam, G. (2011) · Redox Report · doi:10.1179/1351000211y.0000000012 · Cited by 64

Mechanism of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy)-mediated mitochondrial dysfunction in rat liver

Moon, K., Upreti, V. V., Yu, L., Lee, I. J., Ye, X., Eddington, N. D., Veenstra, T. D., & Song, B. (2008) · PROTEOMICS · doi:10.1002/pmic.200800215 · Cited by 62

Role of Protein Carbonylation in Skeletal Muscle Mass Loss Associated with Chronic Conditions

Barreiro, E. (2016) · Proteomes · doi:10.3390/proteomes4020018 · Cited by 56

Oxidative Stress and Proteostasis Network: Culprit and Casualty of Alzheimer’s-Like Neurodegeneration

Di Domenico, F., Head, E., Butterfield, D. A., & Perluigi, M. (2014) · Advances in Geriatrics · doi:10.1155/2014/527518 · Cited by 50

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

A mutant light-chain ferritin that causes neurodegeneration has enhanced propensity toward oxidative damage

Baraibar, M. A., Barbeito, A. G., Muhoberac, B. B., & Vidal, R. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.015 · Cited by 45

Protective effect of ferulic acid ethyl ester against oxidative stress mediated by UVB irradiation in human epidermal melanocytes

Di Domenico, F., Di Domenico, F., Perluigi, M., Foppoli, C., Blarzino, C., Coccia, R., De Marco, F., Butterfield, D. A., & Cini, C. (2009) · Free Radical Research · doi:10.1080/10715760902777329 · Cited by 41

Proteomic identification of specifically carbonylated brain proteins in APPNLh/APPNLh×PS-1P264L/PS-1P264L human double mutant knock-in mice model of Alzheimer disease as a function of age

Sultana, R., Robinson, R. A. S., Di Domenico, F., Abdul, H. M., Clair, D. K. S., Markesbery, W. R., Cai, J., Pierce, W. M., & Butterfield, D. A. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.015 · Cited by 41

Improvement of enzymatic stability and intestinal permeability of deuterohemin-peptide conjugates by specific multi-site N-methylation

Dong, Q.-G., Zhang, Y., Wang, M.-S., Feng, J., Zhang, H.-H., Wu, Y.-G., Gu, T.-J., Yu, X.-H., Jiang, C.-L., Chen, Y., et al. (2012) · Amino Acids · doi:10.1007/s00726-012-1322-y · Cited by 36

Protein folding stabilities are a major determinant of oxidation rates for buried methionine residues

Walker, E. J., Bettinger, J. Q., Welle, K. A., Hryhorenko, J. R., Molina Vargas, A. M., O’Connell, M. R., & Ghaemmaghami, S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101872 · Cited by 35

Age-related variations of protein carbonyls in human saliva and plasma: is saliva protein carbonyls an alternative biomarker of aging?

Wang, Z., Wang, Y., Liu, H., Che, Y., Xu, Y., & E, L. (2015) · AGE · doi:10.1007/s11357-015-9781-1 · Cited by 35

Investigation of therapeutic effect of curcumin α and β glucoside anomers against Alzheimer’s disease by the nose to brain drug delivery

Ahmadi, N., Hosseini, M.-J., Rostamizadeh, K., & Anoush, M. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147517 · Cited by 28

Selectivity in ROS-Induced Peptide Backbone Bond Cleavage

Stringfellow, H. M., Jones, M. R., Green, M. C., Wilson, A. K., & Francisco, J. S. (2014) · The Journal of Physical Chemistry A · doi:10.1021/jp508877m · Cited by 28

The Effects of Amyloid and Tau on Functional Network Connectivity in Older Populations

Wales, R. M., & Leung, H.-C. (2021) · Brain Connectivity · doi:10.1089/brain.2020.0902 · Cited by 26

Proteotoxic Stress Desensitizes TGF-beta Signaling Through Receptor Downregulation in Retinal Pigment Epithelial Cells

Tan, X., Chen, C., Zhu, Y., Deng, J., Qiu, X., Huang, S., Shang, F., Cheng, B., & Liu, Y. (2017) · Current Molecular Medicine · doi:10.2174/1566524017666170619113435 · Cited by 20

Role of TGF-β1-independent changes in protein neosynthesis, p38αMAPK, and cdc42 in hydrogen peroxide-induced senescence-like morphogenesis

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A simple method to systematically study oxidatively modified proteins in biological samples and its applications

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