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Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD
Abstract
Early Alzheimer's disease (EAD) is the intermediary stage between mild cognitive impairment (MCI) and late-stage Alzheimer's disease (AD). The symptoms of EAD mirror the disease advancement between the two phases. Dementia, memory deficits, and cognitive decline are more pronounced as the disease progresses. Oxidative stress in brain is reported in MCI and AD, including lipid peroxidation indexed by protein-bound 4-hydroxy-2-nonenal (HNE). There are limited data regarding the proteomics analysis of brain from subjects with EAD and even less concerning the possible relationship of EAD HNE-modified brain proteins with HNE-modified proteins in MCI and AD. Proteomics was utilized to investigate excessively HNE-bound brain proteins in EAD compared to those in control. These new results provide potentially valuable insight into connecting HNE-bound brain proteins in EAD to those previously identified in MCI and AD, since EAD is a transitional stage between MCI and late-stage AD. In total, six proteins were found to be excessively covalently bound by HNE in EAD inferior parietal lobule (IPL) compared to age-related control brain. These proteins play roles in antioxidant defense (manganese superoxide dismutase), neuronal communication and neurite outgrowth (dihydropyriminidase-related protein 2), and energy metabolism (alpha-enolase, malate dehydrogenase, triosephosphate isomerase, and F1 ATPase, alpha subunit). This study shows that there is an overlap of brain proteins in EAD with previously identified oxidatively modified proteins in MCI and late-stage AD. The results are consistent with the hypothesis that oxidative stress, in particular lipid peroxidation, is an early event in the progression of AD, and is the first to identify in EAD identical brain proteins previously identified as HNE-modified in MCI and late-state AD.
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“MDH is oxidatively modified by HNE in early AD inferior parietal lobule (IPL) [55] and its carbonylation is induced by Aβ in vitro and in vivo [63,65,66].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
In the citing paper
“The activities of LDH, aconitase, and ATP synthase are significantly decreased as a result of oxidation [54,55,56,61]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
In the citing paper
“The carbonylation of ATP synthase is induced in vivo by Aβ [73], and it is significantly modified by HNE in MCI hippocampus and IPL [56], early AD IPL [55], and late AD IPL [54] in addition to being significantly nitrated in late AD hippocampus [57].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
In the citing paper
“however, the activity of MDH is significantly increased [55].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
In the citing paper
“MnSOD is oxidatively modified by HNE in early AD IPL, resulting in a significant decrease in enzyme activity [55]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [55]
Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Alzheimer's Disease: A Disorder of Cortical Cholinergic Innervation
Coyle, J. T., Price, D. L., & DeLong, M. R. (1983) · Science · doi:10.1126/science.6338589 · Cited by 3,052
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383
Reaume, A. G., Elliott, J. L., Hoffman, E. K., Kowall, N. W., Ferrante, R. J., Siwek, D. F., Wilcox, H. M., Flood, D. G., Beal, M. F., Brown, R. H., et al. (1996) · Nature Genetics · doi:10.1038/ng0596-43 · Cited by 1,285
Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide
Butterfield, D. A., Drake, J., Pocernich, C., & Castegna, A. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02173-6 · Cited by 1,114
Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment
Scheff, S. W., Price, D. A., Schmitt, F. A., & Mufson, E. J. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.012 · Cited by 1,017
Butterfield, D. A., & Lauderback, C. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00794-3 · Cited by 1,013
Keller, J. N., Kindy, M. S., Holtsberg, F. W., St. Clair, D. K., Yen, H.-C., Germeyer, A., Steiner, S. M., Bruce-Keller, A. J., Hutchins, J. B., & Mattson, M. P. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-02-00687.1998 · Cited by 863
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 1×
“…(indexed by free or protein-bound 4-hydroxy-2- nonenal (HNE)), and DNA and RNA oxidation (indexed by 8- hydroxy-2-deoxyguanosine and 8-hydroxyguanosine, respectively) have been reported from subjects with AD and MCI (Butterfield et al., 2006b,c, 2007; Hensley et al., 1995; Lauderback et al., 2001).”
Neuron numbers and dendritic extent in normal aging and Alzheimer’s disease
Coleman, P. D., & Flood, D. G. (1987) · Neurobiology of Aging · doi:10.1016/0197-4580(87)90127-8 · Cited by 772
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Kudryavtseva, A. V., Krasnov, G. S., Dmitriev, A. A., Alekseev, B. Y., Kardymon, O. L., Садритдинова, А. Ф., Fedorova, M., Pokrovsky, A. V., Melnikova, N. V., Каприн, А. Д., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9821 · Cited by 564
Butterfield, D. A., Swomley, A. M., & Sultana, R. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5027 · Cited by 526
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Masaldan, S., Bush, A. I., Devos, D., Rolland, A., & Moreau, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.033 · Cited by 494
Pathological aspects of lipid peroxidation
Nègre‐Salvayre, A., Augè, N., Ayala, V., Başağa, H., Boada, J., Brenke, R., Chapple, S. J., Cohen, G., Fehér, J., Grune, T., et al. (2010) · Free Radical Research · doi:10.3109/10715762.2010.498478 · Cited by 465
Interaction of aldehydes derived from lipid peroxidation and membrane proteins
Pizzimenti, S., Ciamporcero, E. S., Daga, M., Pettazzoni, P., Arcaro, A., Cetrangolo, G., Minelli, R., Dianzani, C., Lepore, A., Gentile, F., et al. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00242 · Cited by 382
Lipid peroxidation and neurodegenerative disease
Reed, T. T. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.027 · Cited by 385
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 336
Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 322
The role of lipid peroxidation in neurological disorders
Shichiri, M. (2014) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.14-10 · Cited by 282
The lipid peroxidation product 4-hydroxy-2-nonenal: Advances in chemistry and analysis
Spickett, C. M. (2013) · Redox Biology · doi:10.1016/j.redox.2013.01.007 · Cited by 269
4-Hydroxy-2-nonenal: a critical target in oxidative stress?
Breitzig, M., Bhimineni, C., Lockey, R. F., & Kolliputi, N. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00101.2016 · Cited by 284
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
Self-citationRedox Proteomics: Chemical Principles, Methodological Approaches and Biological/Biomedical Promises
Bachi, A., Dalle‐Donne, I., & Scaloni, A. (2012) · Chemical Reviews · doi:10.1021/cr300073p · Cited by 265
Venkateshappa, C., Harish, G., Mahadevan, A., Srinivas Bharath, M. M., & Shankar, S. K. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0755-8 · Cited by 232
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
Perluigi, M., Coccia, R., & Butterfield, D. A. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4406 · Cited by 229
Lushchak, O. V., Piroddi, M., Galli, F., & Lushchak, V. I. (2013) · Redox Report · doi:10.1179/1351000213y.0000000073 · Cited by 195
Alzheimer's Disease: Redox Dysregulation As a Common Denominator for Diverse Pathogenic Mechanisms
Rommy von Bernhardi, M., & Eugenín, J. L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4082 · Cited by 193
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Bradley‐Whitman, M. A., & Lovell, M. A. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1517-6 · Cited by 192
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 194
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Salvadores, N., Sanhueza, M., Manque, P., & Court, F. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00451 · Cited by 182
Trans-4-hydroxy-2-hexenal, a product of n-3 fatty acid peroxidation: Make some room HNE…
Long, E. K., & Picklo, M. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.015 · Cited by 178
Antioxidant enzymes as redox-based biomarkers: a brief review
Yang, H., & Lee, T. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.4.274 · Cited by 181
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Sousa, B. C., Pitt, A. R., & Spickett, C. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.003 · Cited by 172
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
Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications
Butterfield, D. A., Marzia Perluigi, A., Reed, T. T., Muharib, T., Hughes, C. P., Robinson, R. A. S., & Rukhsana Sultana, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4109 · Cited by 171
Role of By-Products of Lipid Oxidation in Alzheimer's Disease Brain: A Focus on Acrolein
Singh, M., Nam, D. T., Arseneault, M., & Ramassamy, C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100405 · Cited by 162
Gururaj Joshi, A., Aluise, C. D., Cole, M. P., Rukhsana Sultana, A., Pierce, W. M. J., Vore, M. E., Clair, D. K. S., & Butterfield, D. A. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.01.021 · Cited by 159
Oxidative stress and lipid peroxidation are upstream of amyloid pathology
Arimon, M., Takeda, S., Post, K. E., Svirsky, S. E., Hyman, B. T., & Berezovska, O. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.06.013 · Cited by 157
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Spickett, C. M., Wiswedel, I., Siems, W., Žarković, K., & Žarković, N. (2010) · Free Radical Research · doi:10.3109/10715762.2010.498476 · Cited by 156
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Curtis, J. M., Hahn, W. S., Long, E. K., Burrill, J. S., Arriaga, E. A., & Bernlohr, D. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.05.008 · Cited by 164
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Orosz, F., Oláh, J., & Ovádi, J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.012 · Cited by 152
Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 152
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Foret, M. K., Lincoln, R., Carmo, S. D., Cuello, A. C., & Cosa, G. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00761 · Cited by 150
CuII(atsm) inhibits ferroptosis: Implications for treatment of neurodegenerative disease
Southon, A. G., Szostak, K., Acevedo, K. M., Dent, K. A., Volitakis, I., Belaidi, A. A., Barnham, K. J., Crouch, P. J., Ayton, S., Donnelly, P. S., et al. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14881 · Cited by 143
DNA polymerase β deficiency leads to neurodegeneration and exacerbates Alzheimer disease phenotypes
Sýkora, P., Misiak, M., Wang, Y., Ghosh, S., Leandro, G. D. S., Liu, D., Tian, J. Y., Baptiste, B. A., Cong, W., Brenerman, B. M., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1356 · Cited by 140
Ates, G., Goldberg, J., Currais, A. J. M., & Maher, P. A. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101648 · Cited by 131
Barone, E., Di Domenico, F., Mancuso, C., & Butterfield, D. A. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.09.018 · Cited by 127
Self-citationExploring the Biology of Lipid Peroxidation-Derived Protein Carbonylation
Fritz, K. S., & Petersen, D. R. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200169n · Cited by 129
Butterfield, D. A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.06.006 · Cited by 126
Yoval‐Sánchez, B., & Rodríguez‐Zavala, J. S. (2012) · Chemical Research in Toxicology · doi:10.1021/tx2005184 · Cited by 125
Early dysregulation of the mitochondrial proteome in a mouse model of Alzheimer's disease
Chou, J. L., Shenoy, D. V., Thomas, N., Choudhary, P. K., LaFerla, F. M., Goodman, S. R., & Breen, G. A. M. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2010.12.012 · Cited by 123
Ghosh, D., LeVault, K. R., Barnett, A., & Brewer, G. J. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6192-11.2012 · Cited by 124
Butterfield, D. A., Reed, T. T., & Rukhsana Sultana, A. (2010) · Free Radical Research · doi:10.3109/10715762.2010.520014 · Cited by 125
Moya‐Alvarado, G., Gershoni‐Emek, N., Perlson, E., & Bronfman, F. C. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r115.053330 · Cited by 124
Di Domenico, F., Barone, E., Perluigi, M., & Butterfield, D. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6759 · Cited by 114
Mass spectrometry and redox proteomics: Applications in disease
Butterfield, D. A., Gu, L., Domenico, F. D., & Robinson, R. A. S. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21374 · Cited by 113
Butterfield, D. A., Domenico, F. D., Swomley, A. M., Head, E., & Marzia Perluigi, A. (2014) · Biochemical Journal · doi:10.1042/bj20140772 · Cited by 112
Mechanisms of neurodegeneration shared between multiple sclerosis and Alzheimer’s disease
Lassmann, H. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0607-8 · Cited by 112
Redox proteomics and amyloid β-peptide: Insights into Alzheimer disease
Butterfield, D. A., & Boyd‐Kimball, D. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14589 · Cited by 105
Self-citationSalminen, A., Haapasalo, A., Kauppinen, A., Kaarniranta, K., Soininen, H. S., & Hiltunen, M. O. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.001 · Cited by 107
Vascular and metabolic dysfunction in Alzheimer’s disease: a review
Murray, I. V. J., Proza, J. F., Sohrabji, F., & Lawler, J. M. (2011) · Experimental Biology and Medicine · doi:10.1258/ebm.2011.010355 · Cited by 104
Strategy to reduce free radical species in Alzheimer’s disease: an update of selected antioxidants
Domenico, F. D., Barone, E., Marzia Perluigi, A., & Butterfield, D. A. (2014) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.955853 · Cited by 103
Redox active metals in neurodegenerative diseases
Acevedo, K. M., Masaldan, S., Opazo, C., & Bush, A. I. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01731-9 · Cited by 102
Interactions of glutathione transferases with 4-hydroxynonenal
Balogh, L. M., & Atkins, W. M. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.558092 · Cited by 105
Domenico, F. D., Pupo, G., Tramutola, A., Giorgi, A., Schininà, M. E., Coccia, R., Head, E., Butterfield, D. A., & Marzia Perluigi, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.027 · Cited by 98
Barrera, G., Gentile, F., Pizzimenti, S., Canuto, R. A., Daga, M., Arcaro, A., Cetrangolo, G. P., Lepore, A., Ferretti, C., Dianzani, C., et al. (2016) · Antioxidants · doi:10.3390/antiox5010007 · Cited by 98
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
Self-citationButterfield, D. A. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101049 · Cited by 98
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 93
Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease
Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85
“MnSOD is oxidatively modified by HNE in early AD IPL, resulting in a significant decrease in enzyme activity [55] and is also oxidatively modified by HNE in late AD IPL [54].”
BackgroundInfluentialD’Souza, Y., Elharram, A., Soon-Shiong, R., Andrew, R. D., & Bennett, B. M. (2015) · Molecular Brain · doi:10.1186/s13041-015-0117-y · Cited by 87
An update on clinical proteomics in Alzheimer’s research
Korolainen, M. A., Nyman, T. A., Aittokallio, T. A., & Pirttilä, T. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06558.x · Cited by 88
The calcium–iron connection in ferroptosis-mediated neuronal death
Gleitze, S., Paula-Lima, A. C., Núñez, M. T., & Hidalgo, C. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.08.231 · Cited by 84
Uchida, Y., Kan, H., Sakurai, K., Oishi, K., & Matsukawa, N. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.938092 · Cited by 88
Mitochondrial lipids in neurodegeneration
Aufschnaiter, A., Kohler, V., Diessl, J., Peselj, C., Carmona‐Gutiérrez, D., Keller, W., & Büttner, S. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2463-1 · Cited by 91
Jové, M., Pradas, I., Domínguez-González, M., Ferrer, I., & Pamplona, R. (2018) · Redox Biology · doi:10.1016/j.redox.2018.101082 · Cited by 84
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
Hensley, K., Christov, A., Kamat, S., Zhang, X. C., Jackson, K. W., Snow, S., & Post, J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5247-09.2010 · Cited by 78
Hensley, K., & Kursula, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160076 · Cited by 72
Hill, R. L., Kulbe, J. R., Singh, I. N., Wang, J. A., & Hall, E. D. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.06.028 · Cited by 75
Functionalized nanosystems for targeted mitochondrial delivery
Durazo, S. A., & Kompella, U. B. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.11.001 · Cited by 73
Elharram, A., Czegledy, N. M., Golod, M., Milne, G. L., Pollock, E. D., Bennett, B. M., & Shchepinov, M. S. (2017) · FEBS Journal · doi:10.1111/febs.14291 · Cited by 74
Targeting Mitochondria in Alzheimer Disease: Rationale and Perspectives
Lanzillotta, C., Domenico, F. D., Marzia Perluigi, A., & Butterfield, D. A. (2019) · CNS Drugs · doi:10.1007/s40263-019-00658-8 · Cited by 75
Zhang, Y., Yang, X., Wang, S., & Song, S. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b03793 · Cited by 70
Haddad, M., Hervé, V., Ben Khedher, M. R., Rabanel, J.-M., & Ramassamy, C. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8129 · Cited by 68
Kanninen, K. M., White, A. R., Koıstınaho, J., & Malm, T. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/985085 · Cited by 70
Inflammatory Markers in Mild Cognitive Impairment: A Meta-Analysis
Saleem, M., Herrmann, N., Swardfager, W., Eisen, R. B., & Lanctôt, K. L. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150042 · Cited by 64
Rahmadi, A., Steiner, N., & Münch, G. W. (2011) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2011.079 · Cited by 63
Lim, D., Jeong, J., & Song, J. (2021) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13653 · Cited by 64
Lee, H. P., Pancholi, N., Esposito, L., Previll, L. A., Wang, X., Zhu, X., Smith, M. A., & Lee, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028033 · Cited by 61
Metabolic control of signalling pathways and metabolic auto‐regulation
Lorendeau, D., Christen, S., Rinaldi, G., & Fendt, S. (2015) · Biology of the Cell · doi:10.1111/boc.201500015 · Cited by 60
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
The Role of Mitochondrial Aldehyde Dehydrogenase 2 (ALDH2) in Neuropathology and Neurodegeneration.
Chen, C., Joshi, A. U., & Mochly‐Rosen, D. (2016) · PubMed · Cited by 58
Lu, J., Wang, X., Wu, A., Cao, Y. L., Dai, X., Liang, Y., & Li, X. (2022) · Phytotherapy Research · doi:10.1002/ptr.7395 · Cited by 59
Keeney, J. T. R., Swomley, A. M., Harris, J. L., Fiorini, A., Mitov, M. I., Marzia Perluigi, A., Rukhsana Sultana, A., & Butterfield, D. A. (2011) · Neurotoxicity Research · doi:10.1007/s12640-011-9287-2 · Cited by 56
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
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Metadata
- Authors
- Reed, T. T., Pierce, W. M., Markesbery, W. R., & Butterfield, D. A.
- Affiliations
- University of Kentucky (US)
- University of Louisville (US)
- Corresponding author
- Butterfield, D. Allan
- Venue
- Brain Research
- Publisher
- Elsevier BV
- Published
- 2009-06
- Volume
- 1274
- Pages
- 66-76
- ISSN
- 0006-8993 (ISSN-L)
- OpenAlex
- W2076534507
- Cited by
- 190
- References
- 79
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 8 · 2022: 7 · 2021: 13 · 2020: 12 · 2019: 9 · 2018: 11 · 2017: 8 · 2016: 14 · 2015: 13 · 2014: 14 · 2013: 16 · 2012: 16
- FWCI
- 13.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG-0288383, P01AG010836, P01AG005119, AG 10836, AG0 5119)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- early Alzheimer's disease, 4-hydroxynonenal, lipid peroxidation, oxidative stress, protein oxidation, brain proteomics, inferior parietal lobule, manganese superoxide dismutase, alpha-enolase, malate dehydrogenase, triosephosphate isomerase, F1-ATPase, antioxidant defense, energy metabolism, neural communication, disease progression
- MeSH terms
- Aged, Aged, 80 and over, Aldehydes, Alzheimer Disease, Brain, Female, Humans, Male, Proteins, Blotting, Western, Lipid Peroxidation, Oxidative Stress, Disease Progression, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Proteomics
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