4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies

Free radicals in biology and medicine

Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works

Free Radicals in Biology and Medicine

Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990 · see citing works

Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes

Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672 · see citing works

[42] Determination of aldehydic lipid peroxidation products: Malonaldehyde and 4-hydroxynonenal

Esterbauer, H., & Cheeseman, K. H. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86134-h · Cited by 3,365 · see citing works

The cholinergic hypothesis of Alzheimer’s disease: A review of progress

Francis, P. T., Palmer, A. M., Snape, M., & Wilcock, G. K. (1999) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.66.2.137 · Cited by 2,198 · cited 1× · see citing works

Oxidative Damage Is the Earliest Event in Alzheimer Disease

Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885 · see citing works

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · see citing works

From charcot to lou gehrig: deciphering selective motor neuron death in als

Cleveland, D. W., & Rothstein, J. D. (2001) · Nature reviews. Neuroscience · doi:10.1038/35097565 · Cited by 1,389 · see citing works

Ageing and neuronal vulnerability

Mattson, M. P., & Magnus, T. (2006) · Nature reviews. Neuroscience · doi:10.1038/nrn1886 · Cited by 1,075 · see citing works

Causal relation between α-synuclein locus duplication as a cause of familial Parkinson's disease

Ibáñez, P., Bonnet, A. M., Débarges, B., Lohmann, E., Tison, F., Agid, Y., Dürr, A., Brice, A., & Pollak, P. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17104-3 · Cited by 1,042 · see citing works

Classification and basic pathology of Alzheimer disease

Duyckaerts, C., Delatour, B., & Potier, M.-C. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0532-1 · Cited by 1,031 · see citing works

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 · see citing works

Impaired Proteasome Function in Alzheimer's Disease

Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848 · see citing works

Synaptic alterations in CA1 in mild Alzheimer disease and mild cognitive impairment

Scheff, S. W., Price, D. A., Schmitt, F. A., DeKosky, S. T., & Mufson, E. J. (2007) · Neurology · doi:10.1212/01.wnl.0000260698.46517.8f · Cited by 824 · see citing works

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 · see citing works

Brain Regional Correspondence Between Alzheimer's Disease Histopathology and Biomarkers of Protein Oxidation

Hensley, K., Hall, N., Subramaniam, R., Cole, P., Harris, M., Aksenov, M., Aksenova, M., Gabbita, S. P., Wu, J. F., Carney, J. M., et al. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65052146.x · Cited by 779 · cited 2× · see citing works

Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro

Busciglio, J., & Yankner, B. A. (1995) · Nature · doi:10.1038/378776a0 · Cited by 741 · see citing works

Hippocampal and entorhinal atrophy in mild cognitive impairment

Devanand, D. P., Pradhaban, G., Liu, X., Khandji, A., Santi, S. D., Segal, S., Rusinek, H., Pelton, G. H., Honig, L. S., Mayeux, R. P., et al. (2007) · Neurology · doi:10.1212/01.wnl.0000256697.20968.d7 · Cited by 739 · see citing works

Magnetic resonance imaging of the entorhinal cortex and hippocampus in mild cognitive impairment and Alzheimer's disease

Du, A. (2001) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.71.4.441 · Cited by 719 · see citing works

Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33

Goshima, Y., Nakamura, F., Strittmatter, P., & Strittmatter, S. M. (1995) · Nature · doi:10.1038/376509a0 · Cited by 707 · see citing works

Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS

Bosco, D. A., Morfini, G. A., Karabacak, M., Song, Y., Gros‐Louis, F., Pasinelli, P., Goolsby, H., Fontaine, B. A., Lemay, N., McKenna-Yasek, D. M., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2660 · Cited by 685 · see citing works

Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease

Markesbery, W. R., & Lovell, M. A. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00009-8 · Cited by 680 · see citing works

Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications

Bubber, P., Haroutunian, V., Fisch, G., Blass, J. P., & Gibson, G. E. (2005) · Annals of Neurology · doi:10.1002/ana.20474 · Cited by 622 · see citing works

Oxidative stress in ALS: Key role in motor neuron injury and therapeutic target

Barber, S. C., & Shaw, P. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.11.018 · Cited by 617 · see citing works

Increase of Brain Oxidative Stress in Mild Cognitive Impairment

Praticò, D., Clark, C. M., Liun, F., Lee, V., & Trojanowski, J. Q. (2002) · Archives of Neurology · doi:10.1001/archneur.59.6.972 · Cited by 587 · see citing works

Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase‐related protein 2, α‐enolase and heat shock cognate 71

Castegna, A., Aksenov, M. Y., Thongboonkerd, V., Klein, J. B., Pierce, W. M. J., Booze, R. M., Markesbery, W. R., & Butterfield, D. A. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01103.x · Cited by 581 · see citing works

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 · see citing works

CRMP-2 induces axons in cultured hippocampal neurons

Inagaki, N., Chihara, K., Arimura, N., Ménager, C., Kawano, Y., Matsuo, N., Nishimura, T., Amano, M., & Kaibuchi, K. (2001) · Nature Neuroscience · doi:10.1038/90476 · Cited by 544 · see citing works

The hunt for huntingtin function: interaction partners tell many different stories

Harjes, P., & Wanker, E. E. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00168-3 · Cited by 542 · see citing works

Evidence of increased oxidative damage in subjects with mild cognitive impairment

Keller, J. N., Schmitt, F. A., Scheff, S. W., Ding, Q., Chen, Q., Butterfield, D. A., & Markesbery, W. R. (2005) · Neurology · doi:10.1212/01.wnl.0000156156.13641.ba · Cited by 539 · see citing works

The Molecular Effects of Acrolein

Kehrer, J. P. (2000) · Toxicological Sciences · doi:10.1093/toxsci/57.1.6 · Cited by 532 · see citing works

Phenotypic characterization of individuals with 30-40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36-39 repeats.

Rubinsztein, D. C., Leggo, J., Coles, R., Almqvist, E., Biancalana, V., Cassiman, J. J., Chotai, K. A., Connarty, M., Crauford, D., Curtis, A., et al. (1996) · PubMed Central · Cited by 525 · see citing works

Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice

Kieran, D., Kalmár, B., Dick, J. R. T., Riddoch‐Contreras, J., Burnstock, G., & Greensmith, L. (2004) · Nature Medicine · doi:10.1038/nm1021 · Cited by 522 · see citing works

Synaptic degeneration in Alzheimer's disease

Arendt, T. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0536-x · Cited by 517 · see citing works

Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease

Lovell, M. A., & Markesbery, W. R. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm821 · Cited by 515 · see citing works

Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction.

Uchida, K., & Stadtman, E. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53264-6 · Cited by 514 · see citing works

Oxidative stress in Huntington’s disease

Browne, S. E., Ferrante, R. J., & Beal, M. F. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00216.x · Cited by 508 · see citing works

The glial glutamate transporter, GLT‐1, is oxidatively modified by 4‐hydroxy‐2‐nonenal in the Alzheimer's disease brain: the role of Aβ1–42

Lauderback, C. M., Hackett, J. M., Huang, F. F., Keller, J. N., Szweda, L. I., Markesbery, W. R., & Butterfield, D. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00451.x · Cited by 464 · see citing works

Autopsy Samples of Alzheimer's Cortex Show Increased Peroxidation In Vitro

Subbarao, K. V., Richardson, J. S., & Ang, L. C. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb08858.x · Cited by 463 · see citing works

Neuropathologic Substrate of Mild Cognitive Impairment

Markesbery, W. R., Schmitt, F. A., Kryscio, R. J., Davis, D. G., Smith, C. D., & Wekstein, D. R. (2006) · Archives of Neurology · doi:10.1001/archneur.63.1.38 · Cited by 460 · see citing works

Quantitative assessment of cortical synaptic density in Alzheimer's disease

Scheff, S. W., DeKosky, S. T., & Price, D. A. (1990) · Neurobiology of Aging · doi:10.1016/0197-4580(90)90059-9 · Cited by 446 · see citing works

Glucose metabolism and insulin receptor signal transduction in Alzheimer disease

Hoyer, S. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.02.049 · Cited by 436 · see citing works

Histological Evidence of Protein Aggregation in Mutant SOD1 Transgenic Mice and in Amyotrophic Lateral Sclerosis Neural Tissues

Watanabe, M., Dykes‐Hoberg, M., Culotta, V., Price, D. L., Wong, P. C., & Rothstein, J. D. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0443 · Cited by 432 · see citing works

Formation of Isoprostane-like Compounds (Neuroprostanes) in Vivo from Docosahexaenoic Acid*

Roberts, L., Montine, T., Markesbery, W., Tapper, A. R., Hardy, P., Chemtob, S., Dettbarn, W., & Morrow, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13605 · Cited by 430 · see citing works

Elevated 4-Hydroxynonenal in Ventricular Fluid in Alzheimer’s Disease

Lovell, M. A., Ehmann, W. D., Mattson, M. P., & Markesbery, W. R. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00108-5 · Cited by 413 · see citing works

The role of polyunsaturated fatty acids in restoring the aging neuronal membrane

Yehuda, S., Rabinovitz, S., LCARASSO, R., & Mostofsky, D. I. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00074-x · Cited by 404 · see citing works

Reactions of 4-hydroxynonenal with proteins and cellular targets

Petersen, D. R., & Doorn, J. A. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.06.012 · Cited by 393 · see citing works

Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease

Williams, T. I., Lynn, B. C., Markesbery, W. R., & Lovell, M. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.004 · Cited by 391 · see citing works

Chapter 7 Protein Oxidation Processes in Aging Brain

Butterfield, D. A., & Stadtman, E. R. (1997) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60057-7 · Cited by 390 · see citing works

Mild cognitive impairment: transition between aging and Alzheimer's disease.

Petersen, R. C. (2000) · PubMed · Cited by 383 · see citing works

Lipid peroxidation and neurodegenerative disease

Reed, T. T. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.027 · Cited by 380 · see citing works

Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease

Butterfield, D. A., Poon, H. F., St. Clair, D., Keller, J. N., Pierce, W. M., Klein, J. B., & Markesbery, W. R. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.11.002 · Cited by 377 · see citing works

Manganese superoxide dismutase in disease

MacMillan-Crow, L. A., & Cruthirds, D. L. (2001) · Free Radical Research · doi:10.1080/10715760100300281 · Cited by 371 · see citing works

Synaptic and neuritic alterations during the progression of Alzheimer's disease

Masliah, E., Mallory, M., Hansen, L., Richard, D., Alford, M., & Terry, R. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90121-x · Cited by 370 · see citing works

Free radical oxidation of polyunsaturated lipids: new mechanistic insights and the development of peroxyl radical clocks

Pratt, D. A., Tallman, K. A., & Porter, N. A. (2011) · Accounts of Chemical Research · doi:10.1021/ar200024c · Cited by 352 · see citing works

New Perspectives on Alzheimer's Disease

Price, D. L. (1986) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.09.030186.002421 · Cited by 352 · see citing works

The pathological association between down syndrome and Alzheimer disease

Mann, D. M. A. (1988) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(88)90041-3 · Cited by 346 · see citing works

Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD

Rukhsana Sultana, A., Debra Boyd-kimball, A., Poon, H. F., Cai, J., Pierce, W. M. J., Klein, J. B., Merchant, M. L., Markesbery, W. R., & Butterfield, D. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.021 · Cited by 334 · see citing works

Oxidation-induced Misfolding and Aggregation of Superoxide Dismutase and Its Implications for Amyotrophic Lateral Sclerosis

Rakhit, R., Cunningham, P., Fürtös, A., Dahan, S., Qi, X., Crow, J. P., Cashman, N. R., Kondejewski, L. H., & Chakrabartty, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207356200 · Cited by 333 · see citing works

Oxidative damage to protein in sporadic motor neuron disease spinal cord

Shaw, P. J., Ince, P. G., Falkous, G., & Mantle, D. (1995) · Annals of Neurology · doi:10.1002/ana.410380424 · Cited by 331 · see citing works

Role of Oxidative Stress in the Progression of Alzheimer's Disease

Rukhsana Sultana, A., & Butterfield, D. A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1222 · Cited by 327 · see citing works

Phosphorylation of Collapsin Response Mediator Protein-2 by Rho-kinase

Arimura, N., Inagaki, N., Chihara, K., Ménager, C., Nakamura, N., Amano, M., Iwamatsu, A., Goshima, Y., & Kaibuchi, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001032200 · Cited by 320 · see citing works

Formation of novel non-cyclooxygenase-derived prostanoids (F2-isoprostanes) in carbon tetrachloride hepatotoxicity. An animal model of lipid peroxidation.

Morrow, J. D., Awad, J. A., Kato, T., Takahashi, K., Badr, K. F., Roberts, L. J., & Burk, R. F. (1992) · Journal of Clinical Investigation · doi:10.1172/jci116143 · Cited by 319 · see citing works

Hippocampal neurons in pre-clinical Alzheimer's disease.

West, M. J., Kawas, C. H., Stewart, W. F., Rudow, G. L., & Troncoso, J. C. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.12.005 · Cited by 317 · cited 2× · see citing works

4-Hydroxynonenal and neurodegenerative diseases

Žarković, K. (2003) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(03)00024-4 · Cited by 315 · see citing works

Mitochondrial involvement in Parkinson’s disease, Huntington’s disease, hereditary spastic paraplegia and Friedreich’s ataxia

Schapira, A. H. V. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00164-9 · Cited by 310 · see citing works

Oxidative Damage in Huntington's Disease Pathogenesis

Browne, S. E., & Beal, M. F. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2061 · Cited by 309 · see citing works

Roles of the lipid peroxidation product 4-hydroxynonenal in obesity, the metabolic syndrome, and associated vascular and neurodegenerative disorders

Mattson, M. P. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.07.003 · Cited by 303 · see citing works

4‐Hydroxynonenal in the Pathomechanisms of Oxidative Stress

Poli, G., & Schaur, J. R. (2000) · IUBMB Life · doi:10.1080/713803726 · Cited by 299 · see citing works

Involvements of the lipid peroxidation product, HNE, in the pathogenesis and progression of Alzheimer's disease☆

Butterfield, D. A., Lange, M. L. B., & Rukhsana Sultana, A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.02.005 · Cited by 298 · see citing works

Protein Oxidative Damage in a Transgenic Mouse Model of Familial Amyotrophic Lateral Sclerosis

Andrus, P. K., Fleck, T. J., Gurney, M. E., & Hall, E. D. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71052041.x · Cited by 294 · see citing works

Carnosine and Carnosine-Related Antioxidants: A Review

Guiotto, A., Calderan, A., Ruzza, P., & Borin, G. (2005) · Current Medicinal Chemistry · doi:10.2174/0929867054864796 · Cited by 291 · see citing works

Alzheimer’s disease-related alterations in synaptic density: neocortex and hippocampus.

Scheff, S. W., & Price, D. A. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9s312 · Cited by 284 · see citing works

Mechanisms of mitochondrial dysfunction and energy deficiency in Alzheimer’s disease

Atamna, H., & Frey, W. H. (2007) · Mitochondrion · doi:10.1016/j.mito.2007.06.001 · Cited by 278 · see citing works

The Lipid Peroxidation Product, 4‐Hydroxy‐2‐<i>trans</i>‐Nonenal, Alters the Conformation of Cortical Synaptosomal Membrane Proteins

Subramaniam, R., Roediger, F., Jordan, B., Mattson, M. P., Keller, J. N., Waeg, G., & Butterfield, D. A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031161.x · Cited by 270 · see citing works

Induction of nitrotyrosine-like immunoreactivity in the lower motor neuron of amyotrophic lateral sclerosis

Abe, K., Pan, L.-H., Watanabe, M., Kato, T., & Itoyama, Y. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12039-7 · Cited by 263 · see citing works

Up‐Regulation of Protein Chaperones Preserves Viability of Cells Expressing Toxic Cu/Zn‐Superoxide Dismutase Mutants Associated with Amyotrophic Lateral Sclerosis

Bruening, W., Roy, J., Giasson, B. I., Figlewicz, D. A., Mushynski, W. E., & Durham, H. D. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720693.x · Cited by 263 · see citing works

Protein Oxidation and Lipid Peroxidation in Brain of Subjects with Alzheimer's Disease: Insights into Mechanism of Neurodegeneration from Redox Proteomics

Rukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2021 · Cited by 261 · see citing works

Lipid peroxidation and cell cycle signaling: 4-hydroxynonenal, a key molecule in stress mediated signaling.

Yang, Y., Sharma, R., Sharma, A., Awasthi, S., & Awasthi, S. (2003) · Acta Biochimica Polonica · doi:10.18388/abp.2003_3689 · Cited by 258 · see citing works

Redox proteomic identification of 4-Hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: Insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease

Reed, T., Perluigi, M., Sultana, R., Pierce, W. M., Klein, J. B., Turner, D. M., Coccia, R., Markesbery, W. R., & Butterfield, D. A. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.12.007 · Cited by 257 · see citing works

Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis

Rukhsana Sultana, A., Debra Boyd-kimball, A., Poon, H. F., Cai, J., Pierce, W. M. J., Klein, J. B., Markesbery, W. R., Zhou, X. Z., Lu, K. P., & Butterfield, D. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.005 · Cited by 255 · see citing works

Presence of 4‐hydroxynonenal in cerebrospinal fluid of patients with sporadic amyotrophic lateral sclerosis

Smith, R. G., Henry, Y. K., Mattson, M. P., & Appel, S. H. (1998) · Annals of Neurology · doi:10.1002/ana.410440419 · Cited by 254 · see citing works

Increased 3‐nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation

Ferrante, R. J., Shinobu, L. A., Schulz, J. B., Matthews, R. T., Thomas, C. E., Kowall, N. W., Gurney, M. E., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410420309 · Cited by 251 · see citing works

Elevated protein-bound levels of the lipid peroxidation product, 4-hydroxy-2-nonenal, in brain from persons with mild cognitive impairment

Butterfield, D. A., Reed, T., Perluigi, M., De Marco, C., Coccia, R., Cini, C., & Sultana, R. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.12.017 · Cited by 246 · see citing works

Familial amyotrophic lateral sclerosis

Hand, C. K., & Rouleau, G. A. (2002) · Muscle & Nerve · doi:10.1002/mus.10001 · Cited by 235 · see citing works

Free Radicals: Key to Brain Aging and Heme Oxygenase as a Cellular Response to Oxidative Stress

Poon, H. F., Calabrese, V., Scapagnini, G., & Butterfield, D. A. (2004) · The Journals of Gerontology Series A · doi:10.1093/gerona/59.5.m478 · Cited by 235 · see citing works

Alpha-synuclein, lipids and Parkinson’s disease

Ruipérez, V., Darios, F. D., & Davletov, B. A. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.05.004 · Cited by 233 · see citing works

Understanding the Basis for Down Syndrome Phenotypes

Roper, R. J., & Reeves, R. H. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020050 · Cited by 233 · see citing works

Suggested mechanisms for the production of 4-hydroxy-2-nonenal from the autoxidation of polyunsaturated fatty acids

Pryor, W. A., & Porter, N. A. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90153-a · Cited by 230 · see citing works

4-Hydroxynonenal in the Pathomechanisms of Oxidative Stress

Poli, G., & Schaur, J. R. (2000) · IUBMB Life · doi:10.1080/15216540051081092 · Cited by 229 · see citing works

Morphological evidence for lipid peroxidation and protein glycoxidation in spinal cords from sporadic amyotrophic lateral sclerosis patients

Shibata, N., Nagai, R., Uchida, K., Horiuchi, S., Yamada, S., Hirano, A., Kawaguchi, M., Yamamoto, T., Sasaki, S., & Kobayashi, M. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02926-2 · Cited by 224 · see citing works

Carbonyl Reductases: The Complex Relationships of Mammalian Carbonyl- and Quinone-Reducing Enzymes and Their Role in Physiology

Oppermann, U. C. T. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105316 · Cited by 222 · see citing works

Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease

Dumont, M., Wille, E., Stack, C., Calingasan, N. Y., Beal, M. F., & Lin, M. T. (2009) · The FASEB Journal · doi:10.1096/fj.09-132928 · Cited by 221 · see citing works

Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates

Martínez, A., Portero‐Otín, M., Pamplona, R., & Ferrer, I. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00326.x · Cited by 213 · see citing works

Carbonyl reductase

Forrest, G. L., & Gonzalez, B. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00196-4 · Cited by 210 · see citing works

LIPID PEROXIDATION AS CAUSE OF NIGRAL CELL DEATH IN PARKINSON'S DISEASE

Dexter, D. T., Carter, C. J., Javoy-Agid, F., Agid, Y., Lees, A. J., Jenner, P. G., & MARSDEN, C. D. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92471-2 · Cited by 207 · see citing works

Mutant Cu/Zn-Superoxide Dismutase Proteins Have Altered Solubility and Interact with Heat Shock/Stress Proteins in Models of Amyotrophic Lateral Sclerosis

Shinder, G. A., Lacourse, M.-C., Minotti, S., & Durham, H. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010759200 · Cited by 202 · see citing works

The roles of free radicals in amyotrophic lateral sclerosis: reactive oxygen species and elevated oxidation of protein, DNA, and membrane phospholipids

Liu, D., WEN, J., Liu, J., & Li, L. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.15.2318 · Cited by 199 · see citing works

4-Hydroxynonenal Induces Adaptive Response and Enhances PC12 Cell Tolerance Primarily through Induction of Thioredoxin Reductase 1 via Activation of Nrf2

Chen, Z.-H., Saito, Y., Yoshida, Y., Sekine, A., Noguchi, N., & Niki, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508556200 · Cited by 197 · see citing works

Redox proteomics identification of 4-hydroxynonenal-modified brain proteins in Alzheimer’s disease: Role of lipid peroxidation in Alzheimer’s disease pathogenesis

Perluigi, M., Sultana, R., Cenini, G., Di Domenico, F., Memo, M., Pierce, W. M., Coccia, R., & Butterfield, D. A. (2009) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200800161 · Cited by 196 · see citing works

Phospholipase A2, reactive oxygen species, and lipid peroxidation in CNS pathologies

Adibhatla, R. M., & Hatcher, J. F. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.8.560 · Cited by 196 · see citing works

Chapter 31 Reactions of nitric oxide, superoxide and peroxynitrite with superoxide dismutase in neurodegeneration

Beckman, J. S., Chen, J., Crow, J. P., & Ye, Y. Z. (1994) · Progress in brain research · doi:10.1016/s0079-6123(08)61151-6 · Cited by 195 · see citing works

Oxidatively Induced Structural Alteration of Glutamine Synthetase Assessed by Analysis of Spin Label Incorporation Kinetics: Relevance to Alzheimer's Disease

Butterfield, D. A., Hensley, K., Cole, P. S., Ramachandran, S., Aksenov, M. Y., Aksenova, M. V., Bummer, P. M., Haley, B. E., & Carney, J. M. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68062451.x · Cited by 191 · see citing works

Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD

Reed, T. T., Pierce, W. M., Markesbery, W. R., & Butterfield, D. A. (2009) · Brain Research · doi:10.1016/j.brainres.2009.04.009 · Cited by 190 · see citing works

In vivo oxidative stress in brain of Alzheimer disease transgenic mice: Requirement for methionine 35 in amyloid β-peptide of APP

Butterfield, D. A., Galván, V., Lange, M. L. B., Tang, H., Robinson, R. A. S., Spilman, P. R., Fombonne, J., Gorostiza, O. F., Zhang, J., Rukhsana Sultana, A., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.035 · Cited by 188 · see citing works

Current challenges and future applications for protein maps and post‐translational vector maps in proteome projects

Wilkins, M. R., Sanchez, J., Williams, K. L., & Hochstrasser, D. F. (1996) · Electrophoresis · doi:10.1002/elps.1150170504 · Cited by 186 · see citing works

The Oxidative Stress Metabolite 4-Hydroxynonenal Promotes Alzheimer Protofibril Formation

Siegel, S. J., Bieschke, J., Powers, E. T., & Kelly, J. W. (2007) · Biochemistry · doi:10.1021/bi061853s · Cited by 186 · see citing works

The Lipid Peroxidation Product 4‐Hydroxynonenal Inhibits Neurite Outgrowth, Disrupts Neuronal Microtubules, and Modifies Cellular Tubulin

Neely, M. D., Sidell, K. R., Graham, D. G., & Montine, T. J. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722323.x · Cited by 186 · see citing works

Proteomic Analysis of Protein Expression and Oxidative Modification in R6/2 Transgenic Mice

Marzia Perluigi, A., Poon, H. F., Maragos, W. F., Pierce, W. M. J., Klein, J. B., Calabrese, V., Cini, C., Marco, C. M. D., & Butterfield, D. A. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500090-mcp200 · Cited by 184 · see citing works

Biomarkers of oxidative stress are significantly elevated in Down syndrome

Jovanovic, S. V., Clements, D., & MacLeod, K. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00137-3 · Cited by 183 · see citing works

Alzheimer's Disease Brain: Alterations in RNA Levels and in a Ribonuclease-Inhibitor Complex

Sajdel-Sulkowska, E. M., & Marotta, C. A. (1984) · Science · doi:10.1126/science.6206567 · Cited by 181 · see citing works

Redox proteomics: from protein modifications to cellular dysfunction and disease

Butterfield, D. A., & Dalle‐Donne, I. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21404 · Cited by 180 · see citing works

α-Synuclein Selectively Binds to Anionic Phospholipids Embedded in Liquid-Disordered Domains

Stöckl, M. T., Fischer, P., Wanker, E. E., & Herrmann, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.051 · Cited by 179 · see citing works

Down syndrome: molecular mapping of the congenital heart disease and duodenal stenosis.

Korenberg, J. R., Bradley, C. M., & Distèche, C. M. (1992) · Europe PMC (PubMed Central) · Cited by 175 · see citing works

Multifunctional roles of enolase in Alzheimer’s disease brain: beyond altered glucose metabolism

Butterfield, D. A., & Lange, M. L. B. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06397.x · Cited by 175 · see citing works

Collapsin Response Mediator Protein-2 Is Associated with Neurofibrillary Tangles in Alzheimer's Disease

Yoshida, H., Watanabe, A., & Ihara, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9761 · Cited by 173 · see citing works

Studies on the mechanism of formation of 4-hydroxynonenal during microsomal lipid peroxidation

Esterbauer, H., Benedetti, A., Lång, J., Fulceri, R., Fauler, G., & Comporti, M. (1986) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(86)90329-2 · Cited by 171 · see citing works

Collapsin Response Mediator Protein-2: An Emerging Pathologic Feature and Therapeutic Target for Neurodisease Indications

Hensley, K., Venkova, K. M., Christov, A., Gunning, W. T., & Park, J. C. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8166-4 · Cited by 170 · see citing works

Modulation of lipid peroxidation and mitochondrial function improves neuropathology in Huntington’s disease mice

Lee, J.-H., Kosaras, B., Signore, S. J. D., Cormier, K., McKee, A. C., Ratan, R. R., Kowall, N. W., & Ryu, H. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0788-5 · Cited by 170 · see citing works

Activities of key glycolytic enzymes in the brains of patients with Alzheimer's disease

Bigl, M., Br�ckner, M. K., Arendt, T., Bigl, V., & Eschrich, K. (1999) · Journal of Neural Transmission · doi:10.1007/s007020050174 · Cited by 169 · see citing works

Regulation of senescence by eukaryotic translation initiation factor 5A: implications for plant growth and development

Thompson, J. E., Hopkins, M. T., Taylor, C., & Wang, T. (2004) · Trends in Plant Science · doi:10.1016/j.tplants.2004.02.008 · Cited by 167 · see citing works

Enhanced oxygen radical production in a transgenic mouse model of familial amyotrophic lateral sclerosis

Liu, R., Althaus, J. S., Ellerbrock, B. R., Becker, D. A., & Gurney, M. E. (1998) · Annals of Neurology · doi:10.1002/ana.410440510 · Cited by 165 · see citing works

Increased expression of heat shock proteins in rat brain during aging: relationship with mitochondrial function and glutathione redox state

Calabrese, V. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.01.003 · Cited by 162 · see citing works

Snaring the Function of α-Synuclein

Bonini, N. M., & Giasson, B. I. (2005) · Cell · doi:10.1016/j.cell.2005.10.017 · Cited by 162 · see citing works

Conversion of amnestic Mild Cognitive Impairment to dementia of Alzheimer type is independent to memory deterioration

Rozzini, L., Chilovi, B. V., Conti, M. Z., Bertoletti, E., Delrio, I., Trabucchi, M., & Padovani, A. (2007) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.1816 · Cited by 160 · see citing works

4-Hydroxynonenal–protein adducts: A reliable biomarker of lipid oxidation in liver diseases

Poli, G., Biasi, F., & Leonarduzzi, G. (2007) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2007.09.016 · Cited by 157 · see citing works

Alzheimer Disease and the Role of Free Radicals in the Pathogenesis of the Disease

Perry, G. L., Moreira, P. I., Santos, M. S., Oliveira, C. R., Shenk, J. C., Nunomura, A., Smith, M. A., & Zhu, X. (2008) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152708783885156 · Cited by 155 · see citing works

Oxidatively Modified GST and MRP1 in Alzheimer?s Disease Brain: Implications for Accumulation of Reactive Lipid Peroxidation Products

Sultana, R., & Butterfield, D. A. (2004) · Neurochemical Research · doi:10.1007/s11064-004-7028-0 · Cited by 153 · see citing works

Proteomic analysis of 4-hydroxy-2-nonenal-modified proteins in G93A-SOD1 transgenic mice-A model of familial amyotrophic lateral sclerosis

Marzia Perluigi, A., Poon, H. F., Hensley, K., Pierce, W. M. J., Klein, J. B., Calabrese, V., Marco, C. M. D., & Butterfield, D. A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.12.021 · Cited by 151 · see citing works

Oxidation Chemistry of Catecholamines and Neuronal Degeneration: An Update

Napolitano, A., Manini, P., & d’Ischia, M. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711795496863 · Cited by 149 · see citing works

Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice—a model of familial amyotrophic lateral sclerosis

Poon, H. F., Hensley, K., Thongboonkerd, V., Merchant, M. L., Lynn, B. C., Pierce, W. M. J., Klein, J. B., Calabrese, V., & Butterfield, D. A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.030 · Cited by 148 · see citing works

Peroxiredoxin-6 protects against mitochondrial dysfunction and liver injury during ischemia-reperfusion in mice

Eismann, T., Huber, N., Shin, T., Kuboki, S., Galloway, E., Wyder, M. A., Edwards, M. J., Greis, K. D., Shertzer, H. G., Fisher, A. B., et al. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90583.2008 · Cited by 147 · see citing works

Covalent adduction of nucleophilic amino acids by 4-hydroxynonenal and 4-oxononenal

Doorn, J. A., & Petersen, D. R. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00178-3 · Cited by 147 · see citing works

Inactivation of glutathione reductase by 4-hydroxynonenal and other endogenous aldehydes

Jagt, D. L. V., Hunsaker, L. A., Jagt, T. J. V., Gomez, M. S., Gonzales, D. M., Deck, L. M., & Royer, R. E. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00090-7 · Cited by 146 · see citing works

β-Amyloid Mediated Nitration of Manganese Superoxide Dismutase

Muthuswamy, A., Tangpong, J., Keller, J. N., Murphy, M. P., Markesbery, W. R., Kiningham, K. K., & Clair, D. K. S. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051223 · Cited by 143 · see citing works

Proteomic identification of proteins oxidized by Aβ(1–42) in synaptosomes: Implications for Alzheimer's disease

Debra Boyd-kimball, A., Castegna, A., Rukhsana Sultana, A., Poon, H. F., Petroze, R. T., Lynn, B. C., Klein, J. B., & Butterfield, D. A. (2005) · Brain Research · doi:10.1016/j.brainres.2005.02.086 · Cited by 142 · see citing works

Decreased RNA, and Increased RNA Oxidation, in Ribosomes from Early Alzheimer’s Disease

Ding, Q., Markesbery, W. R., Cecarini, V., & Keller, J. N. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9071-5 · Cited by 140 · see citing works

Cyclin-Dependent Protein Kinase 5 Primes Microtubule-Associated Protein Tau Site-Specifically for Glycogen Synthase Kinase 3β

Li, T., Hawkes, C. A., Qureshi, H. Y., Kar, S., & Paudel, H. K. (2006) · Biochemistry · doi:10.1021/bi051635j · Cited by 139 · see citing works

Neurofibrillary tangles, granulovacuolar degeneration, and neuron loss in down syndrome: Quantitative comparison with alzheimer dementia

Ball, M. J., & Nuttall, K. L. (1980) · Annals of Neurology · doi:10.1002/ana.410070512 · Cited by 138 · see citing works

Oxidative stress: A bridge between Down's syndrome and Alzheimer's disease

Zana, M., Janka, Z., & Kalman, J. L. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.03.008 · Cited by 137 · see citing works

Oxidative modification to LDL receptor-related protein 1 in hippocampus from subjects with Alzheimer disease: Implications for Aβ accumulation in AD brain

Owen, J. B., Rukhsana Sultana, A., Aluise, C. D., Erickson, M. A., Price, T. O., Bu, G., Banks, W. A., & Butterfield, D. A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.013 · Cited by 130 · see citing works

Down syndrome and beta-amyloid deposition

Head, E., & Lott, I. T. (2004) · Current Opinion in Neurology · doi:10.1097/00019052-200404000-00003 · Cited by 125 · see citing works

Synaptic Cysteine Sulfhydryl Groups as Targets of Electrophilic Neurotoxicants

LoPachin, R. M., & Barber, D. S. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl066 · Cited by 125 · see citing works

Lipid Peroxides in the Free Radical Pathophysiology of Brain Diseases

Farooqui, A. A., & Horrocks, L. A. (1998) · Cellular and Molecular Neurobiology · doi:10.1023/a:1020625717298 · Cited by 123 · see citing works

Mechanisms of Disease: DNA repair defects and neurological disease

Subba Rao, K. (2007) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0448 · Cited by 121 · see citing works

Neurochemistry and toxin models in Huntingtonʼs disease

Beal, M. F. (1994) · Current Opinion in Neurology · doi:10.1097/00019052-199412000-00012 · Cited by 120 · see citing works

Recent advances in the biochemistry and clinical relevance of the isoprostane pathway

Musiek, E. S., Yin, H., Milne, G. L., & Morrow, J. D. (2005) · Lipids · doi:10.1007/s11745-005-1460-7 · Cited by 117 · see citing works

Early Glycoxidation Damage in Brains from Down's Syndrome

Odetti, P. R., Angelini, G., Dapino, D., Zaccheo, D., Garibaldi, S., Dagna-Bricarelli, F., Piombo, G., Perry, G. L., Smith, M. A., Traverso, N., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8186 · Cited by 116 · see citing works

α-Tocopherol suppresses lipid peroxidation and behavioral and cognitive impairments in the Ts65Dn mouse model of Down syndrome

Shichiri, M., Yoshida, Y., Ishida, N., Hagihara, Y., Iwahashi, H., Tamai, H., & Niki, E. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.023 · Cited by 115 · see citing works

Albumin Is the Main Nucleophilic Target of Human Plasma: A Protective Role Against Pro-atherogenic Electrophilic Reactive Carbonyl Species?

Aldini, G., Vistoli, G., Regazzoni, L., Gamberoni, L., Facino, R. M., Yamaguchi, S., Uchida, K., & Carini, M. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700349r · Cited by 113 · see citing works

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 · see citing works

Modulation of phospholipid asymmetry in synaptosomal membranes by the lipid peroxidation products, 4-hydroxynonenal and acrolein: implications for Alzheimer's disease

Castegna, A., Lauderback, C. M., Abdul, H. M., & Butterfield, D. A. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.036 · Cited by 111 · see citing works

Loss of phospholipid asymmetry and elevated brain apoptotic protein levels in subjects with amnestic mild cognitive impairment and Alzheimer disease

Lange, M. L. B., Cenini, G., Piroddi, M., Abdul, H. M., Rukhsana Sultana, A., Galli, F., Memo, M., & Butterfield, D. A. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.11.004 · Cited by 110 · see citing works

Down Syndrome: Advances in Molecular Biology and the Neurosciences

Capone, G. T. (2001) · Journal of Developmental & Behavioral Pediatrics · doi:10.1097/00004703-200102000-00007 · Cited by 110 · see citing works

The Lipid Peroxidation Product 4-Hydroxynonenal Impairs Glutamate and Glucose Transport and Choline Acetyltransferase Activity in NSC-19 Motor Neuron Cells

Pedersen, W. A., Cashman, N. R., & Mattson, M. P. (1999) · Experimental Neurology · doi:10.1006/exnr.1998.6890 · Cited by 109 · see citing works

Copper- and Zinc-containing Superoxide Dismutase Can Act as a Superoxide Reductase and a Superoxide Oxidase

Liochev, S. I., & Fridovich, I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007891200 · Cited by 108 · see citing works

Oxidized phosphatidylcholine is a marker for neuroinflammation in multiple sclerosis brain

Qin, J., Goswami, R., Balabanov, R. D., & Dawson, G. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21206 · Cited by 108 · see citing works

Effects of 4-hydroxynonenal on isolated hepatocytes. Studies on chemiluminescence response, alkane production and glutathione status

Cadenas, E., Müller, A. F., Brigelius, R., Esterbauer, H., & Sies, H. (1983) · Biochemical Journal · doi:10.1042/bj2140479 · Cited by 106 · see citing works

Protein levels of heat shock proteins 27, 32, 60, 70, 90 and thioredoxin-1 in amnestic mild cognitive impairment: An investigation on the role of cellular stress response in the progression of Alzheimer disease

Domenico, F. D., Rukhsana Sultana, A., Hawkins, G. T., Scheff, N. N., Marzia Perluigi, A., Cini, C., & Butterfield, D. A. (2010) · Brain Research · doi:10.1016/j.brainres.2010.03.085 · Cited by 105 · see citing works

Inactivation and nitration of human superoxide dismutase (SOD) by fluxes of nitric oxide and superoxide

Demicheli, V., Quijano, C., Álvarez, B., & Radí, R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.034 · Cited by 103 · see citing works

Oxidative modification of proteins in the frontal cortex of Alzheimer's disease brain

Korolainen, M. A., Goldsteins, G., Nyman, T. A., Alafuzoff, I. I., Koıstınaho, J., & Pirttilä, T. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.11.010 · Cited by 103 · see citing works

Participation of the mitochondrial genome in the differentiation of neuroblastoma cells

Vayssière, J., Cordeau‐Lossouarn, L., Larcher, J. C., Basseville, M., Gros, F., & Croizat, B. (1992) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/bf02631065 · Cited by 103 · see citing works

Vitamin E and Other Antioxidants in Neuroprotection

Behl, C. (1999) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831.69.3.213 · Cited by 103 · see citing works

The Role of Superoxide Dismutation in Malaria Parasites

Schwartz, E., Samuni, A., Friedman, I., Hempelmann, E., & Golenser, J. (1999) · Inflammation · doi:10.1023/a:1020261600498 · Cited by 97 · see citing works

Oxidative stress occurs early in Down syndrome pregnancy: A redox proteomics analysis of amniotic fluid

Perluigi, M., di Domenico, F., Fiorini, A., Cocciolo, A., Giorgi, A., Foppoli, C., Butterfield, D. A., Giorlandino, M., Giorlandino, C., Eugenia Schininà, M., et al. (2011) · PROTEOMICS – Clinical Applications · doi:10.1002/prca.201000121 · Cited by 97 · see citing works

Redox proteomics analysis of brains from subjects with amnestic mild cognitive impairment compared to brains from subjects with preclinical Alzheimer’s disease: Insights into memory loss in MCI

Aluise, C. D., Robinson, R. A. S., Cai, J., Pierce, W. M., Markesbery, W. R., & Butterfield, D. A. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-101083 · Cited by 94 · see citing works

Changes in Brain Glucose Metabolism as a Key to the Pathogenesis of Alzheimer’s Disease

Meier‐Ruge, W., Bertoni–Freddari, C., & Iwangoff, P. (2009) · Gerontology · doi:10.1159/000213592 · Cited by 94 · see citing works

Oxidative stress and neural dysfunction in Down Syndrome

Iannello, R. C., Crack, P. J., de Haan, J. B., & Kola, I. (1999) · Springer eBooks · doi:10.1007/978-3-7091-6380-1_17 · Cited by 89 · see citing works

α-Synuclein Can Function as an Antioxidant Preventing Oxidation of Unsaturated Lipid in Vesicles

Zhu, M., Qin, Z., Hu, D., Munishkina, L. A., & Fink, A. L. (2006) · Biochemistry · doi:10.1021/bi052584t · Cited by 89 · see citing works

Increased brain protein levels of carbonyl reductase and alcohol dehydrogenase in Down Syndrome and Alzheimer’s disease

Balcz, B., Kirchner, L., Cairns, N. J., Fountoulakis, M., & Lübec, G. (2001) · Springer eBooks · doi:10.1007/978-3-7091-6262-0_15 · Cited by 88 · see citing works

Modulation of antioxidant gene expression by 4-hydroxynonenal: atheroprotective role of the Nrf2/ARE transcription pathway

Siow, R. C. M., Ishii, T., & Mann, G. E. (2007) · Redox Report · doi:10.1179/135100007x162167 · Cited by 88 · see citing works

Down Syndrome

Hayes, A., & Batshaw, M. L. (1993) · Pediatric Clinics of North America · doi:10.1016/s0031-3955(16)38548-0 · Cited by 88 · see citing works

Identification of new modulators and protein alterations in non‐apoptotic programmed cell death

Sperandio, S., Poksay, K. S., Schilling, B., Crippen, D., Gibson, B. W., & Bredesen, D. E. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22870 · Cited by 85 · see citing works

The structure and function of initiation factors in eukaryotic protein synthesis

Pestova, T. V., & Hellen, C. U. T. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000726 · Cited by 84 · see citing works

Overexpression of human phosphoglycerate kinase 1 (PGK1) induces a multidrug resistance phenotype.

Duan, Z., Lamendola, D. E., Yusuf, R., Penson, R. T., Preffer, F. I., & Seiden, M. V. (2002) · PubMed · Cited by 83 · see citing works

Preclinical Alzheimer disease: Brain oxidative stress, Aβ peptide and proteomics

Aluise, C. D., Sowell, R. A., Beckett, T. L., Murphy, M. P., Cai, J., Pierce, W. M. J., Markesbery, W. R., & Butterfield, D. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.04.011 · Cited by 83 · see citing works

Protein kinase C anchoring deficit in postmortem brains of Alzheimer's disease patients.

Battaini, F., Pascale, A., Lucchi, L., Pasinetti, G., & Govoni, S. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7151 · Cited by 82 · see citing works

Multiple evidence for an early age pro-oxidant state in Down Syndrome patients

Pallardó, F. V., Degan, P., d’Ischia, M., Kelly, F. J., Zatterale, A., Calzone, R., Castello, G., Fernández‐Delgado, R., Dunster, C., Lloret, A., et al. (2006) · Biogerontology · doi:10.1007/s10522-006-9002-5 · Cited by 79 · see citing works

Generation of α-hydroxyaldehydic compounds in the course of lipid peroxidation

Loidl‐Stahlhofen, A., Hannemann, K., & Spiteller, G. (1994) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(94)90020-5 · Cited by 79 · see citing works

Human Carbonyl Reductase Catalyzes Reduction of 4-Oxonon-2-enal

Doorn, J. A., Maser, E., Blum, A., Claffey, D. J., & Petersen, D. R. (2004) · Biochemistry · doi:10.1021/bi049136q · Cited by 79 · see citing works

Involvement of α-synuclein in Parkinson's disease and other neurodegenerative disorders

Krüger, R., Müller, T., & Riess, O. H. (2000) · Journal of Neural Transmission · doi:10.1007/s007020050002 · Cited by 70 · see citing works

In vivo PET imaging and postmortem studies suggest potentially reversible and irreversible stages of brain metabolic failure in Alzheimer’s disease

Rapoport, S. I. (1999) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/pl00014174 · Cited by 70 · see citing works

Nonepisodic Memory Deficits in Amnestic MCI

Economou, A., Papageorgiou, S. G., Karageorgiou, C. E., & Vassilopoulos, D. (2007) · Cognitive and Behavioral Neurology · doi:10.1097/wnn.0b013e31804c6fe7 · Cited by 70 · see citing works

Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases

(2006) · doi:10.1002/0471973122 · Cited by 70 · see citing works

Decreased phosphatidylethanolamine binding protein expression correlates with Aβ accumulation in the Tg2576 mouse model of Alzheimer's disease

George, A. J., Holsinger, R. M. D., McLean, C., Tan, S., Scott, H. S., Cardamone, T., Cappai, R., Masters, C. L., & Li, Q. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.03.014 · Cited by 69 · see citing works

CHOLINERGIC DEFICIT IN FRONTAL CEREBRAL CORTEX IN ALZHEIMER'S DISEASE IS AGE DEPENDENT

Rossor, M. N., Iversen, L. L., Johnson, A. L., Mountjoy, C. Q., & Roth, M. (1981) · The Lancet · doi:10.1016/s0140-6736(81)92836-1 · Cited by 69 · see citing works

Do oxidatively modified proteins cause ALS?

Valentine, J. S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01080-8 · Cited by 68 · see citing works

Increased lipid peroxidation in Down’s syndrome mouse models

Ishihara, K., Amano, K., Takaki, E., Ebrahim, A. S., Shimohata, A., Shibazaki, N., Inoue, I., Takaki, M., Ueda, Y., Sago, H., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06294.x · Cited by 67 · see citing works

Time-action Profile of the Insulin Analogue B28Asp

Heinemann, L., Kapitza, C., Starke, A. A. R., & Heise, T. (1996) · Diabetic Medicine · doi:10.1002/(sici)1096-9136(199607)13:7 · Cited by 65 · see citing works

Fructose-1,6-bisphosphate preserves intracellular glutathione and protects cortical neurons against oxidative stress

Vexler, Z. S., Wong, A. L., Francisco, C., Manabat, C., Christen, S., Täuber, M. G., Ferriero, D. M., & Gregory, G. A. (2003) · Brain Research · doi:10.1016/s0006-8993(02)03777-0 · Cited by 65 · see citing works

Mechanisms of 4-hydroxynonenal-induced neuronal microtubule dysfunction

Neely, M. D., Boutté, A. M., Milatović, D., & Montine, T. J. (2005) · Brain Research · doi:10.1016/j.brainres.2004.12.027 · Cited by 65 · see citing works

Clinical Studies of the Cholinergic Deficit in Alzheimer's Disease

Davis, B. M., Mohs, R. C., GREENWALD, B. S., Mathé, A. A., Johns, C. A., Horvath, T., & Davis, K. L. (1985) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1985.tb04184.x · Cited by 64 · see citing works

Some Cerebral Proteins and Enzyme Systems in Alzheimer's Presenile and Senile Dementia

den Velde, W. O., & STAM, F. C. (1976) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1976.tb03247.x · Cited by 64 · see citing works

Interactions between fatty acids and α-synuclein

Luäcke, C., Gantz, D., Klimtchuk, E. S., & Hamilton, J. A. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600003-jlr200 · Cited by 64 · see citing works

Antioxidant proteins in fetal brain: superoxide dismutase-1 (SOD-1) protein is not overexpressed in fetal Down syndrome

Gulesserian, T., Engidawork, E., Fountoulakis, M., & Lübec, G. (2001) · Springer eBooks · doi:10.1007/978-3-7091-6262-0_6 · Cited by 62 · see citing works

Autoxidative Transformation of Chiral ω6 Hydroxy Linoleic and Arachidonic Acids to Chiral 4-Hydroxy-2 E -nonenal

Schneider, C. G., Porter, N. A., & BRASH, A. R. (2004) · Chemical Research in Toxicology · doi:10.1021/tx049913n · Cited by 59 · see citing works

Challenging the cholinergic hypothesis in Alzheimer disease.

Davies, P. (1999) · Journal of the American Medical Association (JAMA) · doi:10.1001/jama.281.15.1433 · Cited by 56 · see citing works

Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide

Filipović, M. R., Stanić-Vučinić, D., Raicevic, S., Spasić, M. B., & Niketić, V. (2006) · Free Radical Research · doi:10.1080/10715760600944296 · Cited by 52 · see citing works

Differential expression of phosphorylated translation initiation factor 2 alpha in Alzheimer’s disease and Creutzfeldt-Jakob’s disease

Ferrer, I. (2002) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2002.t01-1-00410.x · Cited by 52 · see citing works

Increased oxidation of certain glycolysis and energy metabolism enzymes in the frontal cortex in Lewy body diseases

Gómez, A., & Ferrer, I. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21904 · Cited by 52 · see citing works

Lipid Peroxidation: Production, Metabolism, and Signaling Mechanisms of Malondialdehyde and 4-Hydroxy-2-Nonenal

Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,557 · see citing works

Assessment of lipid peroxidation by measuring malondialdehyde (MDA) and relatives in biological samples: Analytical and biological challenges

Tsikas, D. (2017) · Analytical Biochemistry · doi:10.1016/j.ab.2016.10.021 · Cited by 2,190 · see citing works

The role of iron in brain ageing and neurodegenerative disorders

Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819 · see citing works

Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans

Marrocco, I., Fabio Altieri, F., & Peluso, I. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6501046 · Cited by 874 · see citing works

Interactions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's disease

Zucca, F. A., Segura-Aguilar, J., Ferrari, E., Muñoz, P., Paris, I., Sulzer, D., Sarna, T., Casella, L., & Zecca, L. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.09.012 · Cited by 659 · see citing works

Lipid peroxidation triggers neurodegeneration: A redox proteomics view into the Alzheimer disease brain

Sultana, R., Perluigi, M., & Butterfield, D. A. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.027 · Cited by 478 · see citing works

Cadmium-Induced Oxidative Stress: Focus on the Central Nervous System

Branca, J. J. V., Fiorillo, C., Carrino, D., Paternostro, F., Taddei, N., Gulisano, M., Pacini, A., & Becatti, M. (2020) · Antioxidants · doi:10.3390/antiox9060492 · Cited by 319 · see citing works

Oxidative damage in neurodegeneration: roles in the pathogenesis and progression of Alzheimer disease

Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 306 · see citing works

Role of 4-hydroxy-2-nonenal (HNE) in the pathogenesis of alzheimer disease and other selected age-related neurodegenerative disorders

Di Domenico, F., Tramutola, A., & Butterfield, D. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.490 · Cited by 253 · see citing works

On the role of 4-hydroxynonenal in health and disease

Csala, M., Kardon, T., Legeza, B., Lizák, B., Mandl, J., Margittai, É., Puskás, F., Száraz, P., Szelényi, P., & Bánhegyi, G. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.01.015 · Cited by 244 · see citing works

Pathophysiology of mitochondrial lipid oxidation: Role of 4-hydroxynonenal (4-HNE) and other bioactive lipids in mitochondria

Xiao, M., Zhong, H., Xia, L., Tao, Y., & Yin, H. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.363 · Cited by 242 · see citing works

4-Hydroxy-nonenal—A Bioactive Lipid Peroxidation Product

Schaur, R. J., Siems, W., Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5042247 · Cited by 231 · see citing works

Brain iron deposition is linked with cognitive severity in Parkinson’s disease

Thomas, G. E. C., Leyland, L., Schrag, A. E., Lees, A. J., Acosta‐Cabronero, J., & Weil, R. S. (2020) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2019-322042 · Cited by 211 · see citing works

A step-by-step protocol for assaying protein carbonylation in biological samples

Colombo, G., Clerici, M., Garavaglia, M. E., Giustarini, D., Rossi, R., Milzani, A., & Dalle‐Donne, I. (2015) · Journal of Chromatography B · doi:10.1016/j.jchromb.2015.11.052 · Cited by 209 · see citing works

Peroxisomal metabolism and oxidative stress

Nordgren, M., & Fransen, M. (2013) · Biochimie · doi:10.1016/j.biochi.2013.07.026 · Cited by 201 · see citing works

Formation of Secondary and Tertiary Volatile Compounds Resulting from the Lipid Oxidation of Rapeseed Oil

Grebenteuch, S., Kroh, L. W., Drusch, S., & Rohn, S. (2021) · Foods · doi:10.3390/foods10102417 · Cited by 197 · see citing works

Abeta, oxidative stress in Alzheimer disease: Evidence based on proteomics studies

Swomley, A. M., Förster, S., Keeney, J. T. R., Triplett, J. C., Zhang, Z., Rukhsana Sultana, A., & Butterfield, D. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.015 · Cited by 190 · see citing works

Effects of in vivo conditions on amyloid aggregation

Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 179 · see citing works

Redox proteomics: from protein modifications to cellular dysfunction and disease

Butterfield, D. A., & Dalle‐Donne, I. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21404 · Cited by 180 · see citing works

The Interplay Among Oxidative Stress, Brain Insulin Resistance and AMPK Dysfunction Contribute to Neurodegeneration in Type 2 Diabetes and Alzheimer Disease

Barone, E., Domenico, F. D., Perluigi, M., & Butterfield, D. (2021) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2021.09.006 · Cited by 155 · see citing works

Oxidative stress in Alzheimer disease and mild cognitive impairment: evidence from human data provided by redox proteomics

Swomley, A. M., & Butterfield, D. A. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1556-z · Cited by 171 · see citing works

The Involvement of the Oxidative Stress Status in Cancer Pathology: A Double View on the Role of the Antioxidants

Kamal, F. Z., Lefter, R. M., Ali, A., Ech‐Chahad, A., Truş, C., Ciobica, A. S., & Timofte, D. V. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9965916 · Cited by 170 · see citing works

Role of oxidative stress in infectious diseases. A review

Pohanka, M. (2013) · Folia Microbiologica · doi:10.1007/s12223-013-0239-5 · Cited by 157 · see citing works

Dose-dependent functionality and toxicity of green tea polyphenols in experimental rodents

Murakami, A. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.04.018 · Cited by 152 · see citing works

Insights into the Pathogenesis of Neurodegenerative Diseases: Focus on Mitochondrial Dysfunction and Oxidative Stress

Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 150 · see citing works

Iron overload: Effects on cellular biochemistry

Nogueira, L. S., Oliveira, M. M., Pessoa, M. T., & Barbosa, L. A. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.029 · Cited by 144 · see citing works

Lipid Oxidation Derived Aldehydes and Oxysterols Between Health and Disease

Sottero, B., Leonarduzzi, G., Testa, G., Gargiulo, S., Poli, G., & Biasi, F. (2018) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.201700047 · Cited by 137 · see citing works

A mechanistic study and review of volatile products from peroxidation of unsaturated fatty acids: an aid to understanding the origins of volatile organic compounds from the human body

Ratcliffe, N. A., Wieczorek, T., Drabińska, N., Gould, O., Osborne, A., & Costello, B. D. L. (2020) · Journal of Breath Research · doi:10.1088/1752-7163/ab7f9d · Cited by 136 · see citing works

Metformin Protects against Oxidative Stress Injury Induced by Ischemia/Reperfusion via Regulation of the lncRNA-H19/miR-148a-3p/Rock2 Axis

Zeng, J., Zhu, L., Liu, J., Zhu, T., Xie, Z., Sun, X., & Zhang, H. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8768327 · Cited by 133 · see citing works

CMS121, a fatty acid synthase inhibitor, protects against excess lipid peroxidation and inflammation and alleviates cognitive loss in a transgenic mouse model of Alzheimer's disease

Ates, G., Goldberg, J., Currais, A. J. M., & Maher, P. A. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101648 · Cited by 131 · see citing works

The 2013 SFRBM Discovery Award: Selected discoveries from the Butterfield laboratory of oxidative stress and its sequela in brain in cognitive disorders exemplified by Alzheimer disease and chemotherapy induced cognitive impairment

Butterfield, D. A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.06.006 · Cited by 126 · see citing works

Lipid Peroxidation and Antioxidant Supplementation in Neurodegenerative Diseases: A Review of Human Studies

Petrović, S., Arsić, A., Ristić-Medić, D., Cvetković, Z., & Vučić, V. (2020) · Antioxidants · doi:10.3390/antiox9111128 · Cited by 119 · see citing works

4-hydroxynonenal-mediated signaling and aging

Zhang, H., & Forman, H. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.032 · Cited by 114 · see citing works

Hsp70 interactions with membrane lipids regulate cellular functions in health and disease

Balogi, Z., Multhoff, G., Jensen, T. K., Lloyd‐Evans, E., Yamashima, T., Jäättelä, M., Harwood, J. L., & Vı́gh, L. (2019) · Progress in Lipid Research · doi:10.1016/j.plipres.2019.01.004 · Cited by 112 · see citing works

The impact of oxidative stress on chaperone-mediated human sperm–egg interaction

Bromfield, E. G., Aitken, R. J., Anderson, A. L., McLaughlin, E. A., & Nixon, B. (2015) · Human Reproduction · doi:10.1093/humrep/dev214 · Cited by 111 · see citing works

Redox proteomic identification of HNE-bound mitochondrial proteins in cardiac tissues reveals a systemic effect on energy metabolism after doxorubicin treatment

Zhao, Y., Miriyala, S., Miao, L., Mitov, M. I., Schnell, D., Dhar, S. K., Cai, J., Klein, J. B., Rukhsana Sultana, A., Butterfield, D. A., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.001 · Cited by 110 · see citing works

Bestrophinopathy: An RPE-photoreceptor interface disease

Guziewicz, K. E., Sinha, D., Gómez, N. M., Zorych, K., Dutrow, E. V., Dhingra, A., Mullins, R. F., Stone, E. M., Gamm, D. M., Boesze‐Battaglia, K., et al. (2017) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2017.01.005 · Cited by 109 · see citing works

Discovery of a Potent Dual Inhibitor of Acetylcholinesterase and Butyrylcholinesterase with Antioxidant Activity that Alleviates Alzheimer-like Pathology in Old APP/PS1 Mice

Viayna, E., Coquelle, N., Cieslikiewicz-Bouet, M., Cisternas, P., Oliva, C. A., Sánchez-López, E., Ettcheto, M., Bartolini, M., De Simone, A., Ricchini, M., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01775 · Cited by 106 · see citing works

Recent advancements in the field of nanotechnology for the delivery of anti-Alzheimer drug in the brain region

Agrawal, M., Saraf, S., Saraf, S., Antimisiaris, S. G., Hamano, N., Li, S., Chougule, M. B., Shoyele, S., Gupta, U. D., Ajazuddin, M., et al. (2018) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2018.1471058 · Cited by 100 · see citing works

Pomegranate seed oil nanoemulsions for the prevention and treatment of neurodegenerative diseases: the case of genetic CJD

Mizrahi, M., Friedman‐Levi, Y., Larush, L., Frid, K., Binyamin, O., Dori, D., Fainstein, N., Ovadia, H., Ben‐Hur, T., Magdassi, S., et al. (2014) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2014.03.015 · Cited by 100 · see citing works

Regulation of autophagy, mitochondrial dynamics, and cellular bioenergetics by 4-hydroxynonenal in primary neurons

Dodson, M. B., Wani, W. Y., Redmann, M., Benavides, G. A., Johnson, M. S., Ouyang, X., Cofield, S. S., Mitra, K., Darley-Usmar, V. M., & Zhang, J. (2017) · Autophagy · doi:10.1080/15548627.2017.1356948 · Cited by 91 · see citing works

Polyunsaturated Fatty Acid Deuteration against Neurodegeneration

Shchepinov, M. S. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.01.010 · Cited by 86 · see citing works

Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease

Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85 · see citing works

Oxidative Stress in Poultry: Lessons from the Viral Infections

Rehman, Z. U., Meng, C., Sun, Y., Safdar, A., Pasha, R. H., Munir, M., & Ding, C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/5123147 · Cited by 84 · see citing works

Antioxidant Alternatives in the Treatment of Amyotrophic Lateral Sclerosis: A Comprehensive Review

Carrera‐Juliá, S., Moreno, M. L., Barrios, C., Ortí, J. E. D. L. R., & Drehmer, E. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00063 · Cited by 83 · see citing works

Protein carbonylation: Proteomics, specificity and relevance to aging

Cabiscol, E., Tamarit, J., & Ros, J. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21375 · Cited by 81 · see citing works

The Formation of Methyl Ketones during Lipid Oxidation at Elevated Temperatures

Grebenteuch, S., Kanzler, C., Klaußnitzer, S., Kroh, L. W., & Rohn, S. (2021) · Molecules · doi:10.3390/molecules26041104 · Cited by 80 · see citing works

Statins more than cholesterol lowering agents in Alzheimer disease: Their pleiotropic functions as potential therapeutic targets

Barone, E., Domenico, F. D., & Butterfield, D. A. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.10.030 · Cited by 79 · see citing works

Intake of ω-6 Polyunsaturated Fatty Acid-Rich Vegetable Oils and Risk of Lifestyle Diseases

Yamashima, T., Ota, T., Mizukoshi, E., Nakamura, H., Yamamoto, Y., Kikuchi, M., Yamashita, T., & Kaneko, S. (2020) · Advances in Nutrition · doi:10.1093/advances/nmaa072 · Cited by 78 · see citing works

Linking lipid peroxidation and neuropsychiatric disorders: focus on 4-hydroxy-2-nonenal

Romano, A., Serviddio, G., Calcagnini, S., Villani, R., Giudetti, A. M., Cassano, T., & Gaetani, S. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.046 · Cited by 77 · see citing works

Bach1 Overexpression in Down Syndrome Correlates with the Alteration of the HO-1/BVR-A System: Insights for Transition to Alzheimer's Disease

Di Domenico, F., Pupo, G., Mancuso, C., Barone, E., Paolini, F., Arena, A., Blarzino, C., Schmitt, F. A., Head, E., Butterfield, D. A., et al. (2015) · Journal of Alzheimer’s Disease · doi:10.3233/jad-141254 · Cited by 75 · see citing works

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 · see citing works

Study on Analysis of Peripheral Biomarkers for Alzheimer’s Disease Diagnosis

Rani, P., Krishnan, S., & Cathrine, C. R. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00328 · Cited by 72 · see citing works

Nrf2 knockout altered brain iron deposition and mitigated age-related motor dysfunction in aging mice

Han, K., Jin, X., Guo, X., Cao, G., Tian, S., Song, Y., Zuo, Y., Yu, P., Gao, G., & Chang, Y. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.11.019 · Cited by 72 · see citing works

Accumulation of Electrophilic Aldehydes During Postovulatory Aging of Mouse Oocytes Causes Reduced Fertility, Oxidative Stress, and Apoptosis1

Lord, T., Martin, J. H., & Aitken, R. J. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.114.122820 · Cited by 71 · see citing works

Mitochondria Alkylation and Cellular Trafficking Mapped with a Lipophilic BODIPY–Acrolein Fluorogenic Probe

Lincoln, R., Greene, L. E., Zhang, W., Louisia, S., & Cosa, G. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b08615 · Cited by 71 · see citing works

A Role for the p75 Neurotrophin Receptor in Axonal Degeneration and Apoptosis Induced by Oxidative Stress

Kraemer, B. R., Snow, J. P., Vollbrecht, P. J., Pathak, A., Valentine, W. M., Deutch, A. Y., & Carter, B. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563403 · Cited by 68 · see citing works

Heat Shock Protein A2 (HSPA2): Regulatory Roles in Germ Cell Development and Sperm Function

Nixon, B., Bromfield, E. G., Cui, J., & Iuliis, G. N. D. (2017) · Advances in anatomy, embryology and cell biology · doi:10.1007/978-3-319-51409-3_4 · Cited by 68 · see citing works

Treatment of a multiple sclerosis animal model by a novel nanodrop formulation of a natural antioxidant

Gabizon, R., Binyamin, O., Larush, L., Frid, K., Keller, G., Friedman‐Levi, Y., Ovadia, H., Abramsky, O., & Magdassi, S. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s92704 · Cited by 64 · see citing works

Carbon–Dipyrromethenes: Bright Cationic Fluorescent Dyes and Potential Application in Revealing Cellular Trafficking of Mitochondrial Glutathione Conjugates

Zhang, H., Liu, J., Sun, Y., Liu, M., & Guo, W. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c06916 · Cited by 61 · see citing works

Testosterone depletion increases the susceptibility of brain tissue to oxidative damage in a restraint stress mouse model

Son, S., Lee, J., Kim, H.-G., Kim, D. W., Ahn, Y., & Son, C. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13371 · Cited by 59 · see citing works

Redox proteomics and the dynamic molecular landscape of the aging brain

Marzia Perluigi, A., Swomley, A. M., & Butterfield, D. A. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.12.005 · Cited by 59 · see citing works

Evidence in Support of Potential Applications of Lipid Peroxidation Products in Cancer Treatment

Erejuwa, O. O., Sulaiman, S. A., & Wahab, M. S. A. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/931251 · Cited by 58 · see citing works

Inhibition of glycolysis attenuates 4-hydroxynonenal-dependent autophagy and exacerbates apoptosis in differentiated SH-SY5Y neuroblastoma cells

Dodson, M. B., Liang, Q., Johnson, M. S., Redmann, M., Fineberg, N. S., Darley-Usmar, V. M., & Zhang, J. (2013) · Autophagy · doi:10.4161/auto.26094 · Cited by 57 · see citing works

Perspectives on Oxidative Stress in Alzheimer’s Disease and Predictions of Future Research Emphases

Butterfield, D. A. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179912 · Cited by 57 · see citing works

HNE-modified proteins in Down syndrome: Involvement in development of Alzheimer disease neuropathology

Barone, E., Head, E., Butterfield, D. A., & Perluigi, M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.508 · Cited by 53 · see citing works

Iron and Alzheimer’s Disease: From Pathology to Imaging

Tran, D. Q., DiGiacomo, P., Born, D. E., Georgiadis, M., & Zeineh, M. (2022) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2022.838692 · Cited by 57 · see citing works

Comparison of simple, double and gelled double emulsions as hydroxytyrosol and n-3 fatty acid delivery systems

Flaiz, L., Freire, M., Cofrades, S., Mateos, R., Weiß, J., Jiménez-Colmenero, F., & Bou, R. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.06.005 · Cited by 54 · see citing works

Tibolone Prevents Oxidation and Ameliorates Cholinergic Deficit Induced by Ozone Exposure in the Male Rat Hippocampus

Farfán‐García, E. D., Castillo-Hernandez, M. C., Pinto‐Almazán, R., Rivas-Arancibia, S., Gallardo, J. M., & Guerra‐Araiza, C. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1385-0 · Cited by 53 · see citing works

Pathophysiology of tobacco smoke exposure: Recent insights from comparative and redox proteomics

Colombo, G., Clerici, M., Giustarini, D., Portinaro, N. M., Aldini, G., Rossi, R., Milzani, A., & Dalle‐Donne, I. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21392 · Cited by 52 · see citing works

Protective Effect of Meretrix meretrix Oligopeptides on High-Fat-Diet-Induced Non-Alcoholic Fatty Liver Disease in Mice

Huang, F., Wang, J., Yu, F., Tang, Y., Ding, G., Yang, Z., & Sun, Y. (2018) · Marine Drugs · doi:10.3390/md16020039 · Cited by 52 · see citing works

Ferroptosis: A Promising Therapeutic Target for Neonatal Hypoxic-Ischemic Brain Injury

Peeples, E. S., & Genaro‐Mattos, T. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137420 · Cited by 50 · see citing works

Protein Carbonylation: Emerging Roles in Plant Redox Biology and Future Prospects

Tola, A. J., Jaballi, A., & Missihoun, T. D. (2021) · Plants · doi:10.3390/plants10071451 · Cited by 49 · see citing works

Emulsion gels containing n-3 fatty acids and condensed tannins designed as functional fat replacers

Freire, M., Cofrades, S., Pérez‐Jiménez, J., Gómez‐Estaca, J., Jiménez-Colmenero, F., & Bou, R. (2018) · Food Research International · doi:10.1016/j.foodres.2018.07.041 · Cited by 49 · see citing works

Succination is Increased on Select Proteins in the Brainstem of the NADH dehydrogenase (ubiquinone) Fe-S protein 4 (Ndufs4) Knockout Mouse, a Model of Leigh Syndrome

Piroli, G. G., Manuel, A. M., Clapper, A. C., Walla, M. D., Baatz, J. E., Palmiter, R. D., Quintana, A., & Frizzell, N. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.051516 · Cited by 47 · see citing works

Proteolytic degradation of heat shock protein A2 occurs in response to oxidative stress in male germ cells of the mouse

Bromfield, E. G., Aitken, R. J., McLaughlin, E. A., & Nixon, B. (2016) · Molecular Human Reproduction · doi:10.1093/molehr/gaw074 · Cited by 47 · see citing works

Pomegranate as a Possible Treatment in Reducing Risk of Developing Wound Healing, Obesity, Neurodegenerative Disorders, and Diabetes Mellitus

AlMatar, M., Islam, M. R., Albarri, O., Var, İ., & Köksal, F. (2017) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557517666170419114722 · Cited by 47 · see citing works

Role of traditional Chinese medicine monomers in cerebral ischemia/reperfusion injury:a review of the mechanism

Zheng, T., Jiang, T., Huang, Z., Ma, H., & Wang, M. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1220862 · Cited by 46 · see citing works

Protein modifications by electrophilic lipoxidation products: Adduct formation, chemical strategies and tandem mass spectrometry for their detection and identification

Vasil’ev, Y. V., Tzeng, S., Huang, L., & Maier, C. S. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21389 · Cited by 44 · see citing works

Novel molecular approaches for improving enzymatic and nonenzymatic detoxification of 4-hydroxynonenal: toward the discovery of a novel class of bioactive compounds

Aldini, G., Carini, M., Yeum, K., & Vistoli, G. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.017 · Cited by 43 · see citing works

Effects of Resveratrol Supplementation on Oxidative Damage and Lipid Peroxidation Induced by Strenuous Exercise in Rats

Xiao, N. (2015) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2015.015 · Cited by 43 · see citing works

Crosstalk between Oxidative Stress and Aging in Neurodegeneration Disorders

Abdelhamid, R. F., & Nagano, S. (2023) · Cells · doi:10.3390/cells12050753 · Cited by 40 · see citing works

Probing lipid-protein adduction with alkynyl surrogates: application to Smith-Lemli-Opitz syndrome

Windsor, K., Genaro‐Mattos, T. C., Kim, H., Liu, W., Tallman, K. A., Miyamoto, S., Korade, Ž., & Porter, N. A. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m041061 · Cited by 39 · see citing works

Gsta4 Null Mouse Embryonic Fibroblasts Exhibit Enhanced Sensitivity to Oxidants: Role of 4-Hydroxynonenal in Oxidant Toxicity

McElhanon, K. E., Bose, C., Sharma, R., Wu, L., Awasthi, S., & Singh, S. P. (2013) · Open Journal of Apoptosis · doi:10.4236/ojapo.2013.21001 · Cited by 39 · see citing works

Novel insight into the therapeutical potential of flavonoids from traditional Chinese medicine against cerebral ischemia/reperfusion injury

Zhou, J., Sun, F., Zhang, W., Feng, Z., Yang, Y., & Mei, Z. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1352760 · Cited by 38 · see citing works

Early involvement of lysosome dysfunction in the degeneration of cerebral cortical neurons caused by the lipid peroxidation product 4‐hydroxynonenal

Zhang, S., Eitan, E., & Mattson, M. P. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13957 · Cited by 38 · see citing works

Biogenic aldehyde-mediated mechanisms of toxicity in neurodegenerative disease

Cagle, B. S., Crawford, R. A., & Doorn, J. A. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.12.002 · Cited by 39 · see citing works

Oxidized unsaturated fatty acids induce apoptotic cell death in cultured cells

Iuchi, K., Ema, M., Suzuki, M., Yokoyama, C., & Hisatomi, H. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.9940 · Cited by 36 · see citing works

Overview of the Neuroprotective Effects of the MAO-Inhibiting Antidepressant Phenelzine

Matveychuk, D., MacKenzie, E. M., Kumpula, D. J., Song, M.-S., Holt, A., Kar, S., Todd, K. G., Wood, P. L., & Baker, G. B. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01078-3 · Cited by 37 · see citing works

NXP031 Improves Cognitive Impairment in a Chronic Cerebral Hypoperfusion-Induced Vascular Dementia Rat Model through Nrf2 Signaling

Lee, J. M., Lee, J. H., Song, M. K., & Kim, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126285 · Cited by 35 · see citing works

Attenuation of the effects of oxidative stress by the MAO-inhibiting antidepressant and carbonyl scavenger phenelzine

Baker, G. B., Matveychuk, D., MacKenzie, E. M., Holt, A., Wang, Y., & Kar, S. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.03.003 · Cited by 33 · see citing works

Nitrooxidative Stress and Neuroinflammation Caused by Air Pollutants Are Associated with the Biological Markers of Neurodegenerative Diseases

Ramírez-Mendoza, A. A., Mendoza-Magaña, M. L., Ramírez-Herrera, M. A., Nazará, Z., & Domı́nguez-Rosales, J. A. (2024) · Antioxidants · doi:10.3390/antiox13030326 · Cited by 32 · see citing works

Electrophilic aldehyde products of lipid peroxidation selectively adduct to heat shock protein 90 and arylsulfatase A in stallion spermatozoa †

Hall, S. E., Aitken, R. J., Nixon, B., Smith, N. D., & Gibb, Z. (2017) · Biology of Reproduction · doi:10.1095/biolreprod.116.145292 · Cited by 32 · see citing works

Agmatine Mitigates Inflammation-Related Oxidative Stress in BV-2 Cells by Inducing a Pre-Adaptive Response

Milosevic, K., Stevanović, I. D., Bozic, I. D., Milosevic, A., Janjic, M. M., Laketa, D., Bjelobaba, I. M., Lavrnja, I. C., & Savić, D. Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073561 · Cited by 31 · see citing works

Mitochondrial Dysfunction and Changes in High-Energy Compounds in Different Cellular Models Associated to Hypoxia: Implication to Schizophrenia

Silva, L., Brito, M. D., Yuzawa, J. M. C., & Rosenstock, T. R. (2019) · Scientific Reports · doi:10.1038/s41598-019-53605-4 · Cited by 33 · see citing works

An Impedimetric Biosensor for Detection of Volatile Organic Compounds in Food

Calabrese, A., Battistoni, P., Ceylan, S., Zeni, L., Capo, A., Varriale, A., D’Auria, S., & Staiano, M. (2023) · Biosensors · doi:10.3390/bios13030341 · Cited by 31 · see citing works

Aldehyde Dehydrogenase 2 (ALDH2) in Rat Fatty Liver Cold Ischemia Injury

Rosello, A. P., Alva, N., Flores, M., López, A., Benítez, C. C., Folch‐Puy, E., Rolo, A. P., Palmeira, C. M., Adam, R. A., Carbonell, T., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092479 · Cited by 30 · see citing works

Oxidative stress in microbes after exposure to iron nanoparticles: analysis of aldehydes as oxidative damage products of lipids and proteins

Semerád, J., Moeder, M., Filip, J., Pivokonský, M., Filipová, A., & Cajthaml, T. (2019) · Environmental Science and Pollution Research · doi:10.1007/s11356-019-06370-w · Cited by 29 · see citing works

The Potential Mechanism and the Role of Antioxidants in Mitigating Oxidative Stress in Alzheimer’s Disease

Naik, R. A., Mir, M. N., Malik, I. A., Bhardwaj, R., Alshabrmi, F. M., Mahmoud, M. A., Alhomrani, M., Alamri, A. S., Alsanie, W. F., Hjazi, A. M., et al. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl25551 · Cited by 28 · see citing works

Oxidative Stress in Brain in Amnestic Mild Cognitive Impairment

Butterfield, D. A. (2023) · Antioxidants · doi:10.3390/antiox12020462 · Cited by 28 · see citing works

Lipid peroxidation triggers neurodegeneration: A redox proteomics view into the Alzheimer disease brain

Sultana, R., Perluigi, M., & Butterfield, D. A. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.027 · Cited by 478 · see citing works

Role of 4-hydroxy-2-nonenal (HNE) in the pathogenesis of alzheimer disease and other selected age-related neurodegenerative disorders

Di Domenico, F., Tramutola, A., & Butterfield, D. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.490 · Cited by 253 · see citing works

4-Hydroxynonenal (HNE) modified proteins in metabolic diseases

Castro, J. P., Jung, T., Grune, T., & Siems, W. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.497 · Cited by 223 · see citing works

[51] Detection of 4-hydroxy-2-nonenol adducts following lipid peroxidation from ozone exposure

Szweda, L. I., Szweda, P. A., & Holian, A. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)19053-6 · Cited by 12 · see citing works

Oxidative Stress-mediated Lipid Peroxidation-derived Lipid Aldehydes in the Pathophysiology of Neurodegenerative Diseases

Allowitz, K. V., Taylor, J., Harames, K., Yoo, J., Baloch, O. A., & Ramana, K. V. (2024) · Current Neuropharmacology · doi:10.2174/011570159x342720241014164650 · Cited by 38 · see citing works