Proteomic identification of nitrated brain proteins in early Alzheimer’s disease inferior parietal lobule
Open accessAbstract
Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by progressive decline in multiple cognitive domains. Its pathological hallmarks include senile plaques and neurofibrillary tangles. Mild cognitive impairment (MCI) is the earliest detectable stage of AD with limited symptomology and no dementia. The yearly conversion rate of patients from MCI to AD is 10–15%, although conversion back to normal is possible in a small percentage. Early diagnosis of AD is important in an attempt to intervene or slow the advancement of the disease. Early AD (EAD) is a stage following MCI and characterized by full‐blown dementia; however, information involving EAD is limited. Oxidative stress is well‐established in MCI and AD, including protein oxidation. Protein nitration also is an important oxidative modification observed in MCI and AD, and proteomic analysis from our laboratory identified nitrated proteins in both MCI and AD. Therefore, in the current study, a proteomics approach was used to identify nitrated brain proteins in the inferior parietal lobule from four subjects with EAD. Eight proteins were found to be significantly nitrated in EAD: peroxiredoxin 2, triose phosphate isomerase, glutamate dehydrogenase, neuropolypeptide h3, phosphoglycerate mutase1, H+– transporting ATPase, α‐enolase and fructose‐1,6‐bisphosphate aldolase. Many of these proteins are also nitrated in MCI and late‐stage AD, making this study the first to our knowledge to link nitrated proteins in all stages of AD. These results are discussed in terms of potential involvement in the progression of this dementing disorder.
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Redox proteomics has identified specifically oxidized or nitrosated proteins in brain from late-stage Alzheimer disease, amnestic mild cognitive impairment, and preclinical Alzheimer disease.
“The techniques of redox proteomics34 allowed specific oxidatively or nitrosatively modified proteins (that is, PC-, protein bound HNE-, and/or 3-NT-modified proteins) to be identified in brain from subjects with late-stage AD, aMCI and PCAD20,24,34,35.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [24]
The Introduction reports protein nitration in MCI and late-stage AD, and the Discussion compares identified nitrated proteins across MCI, early AD, and late AD. This paper does not report identifications in preclinical AD (PCAD); its own proteomic study examined early AD. The cited passages also do not establish the claimed range of protein-carbonyl and HNE modifications. (LLM, conf=0.87)
Experimental — accuracy not yet measuredIn Down syndrome, loss of mitochondrial anterograde transport down axons leads to loss of ion gradients in presynaptic membranes and damaging calcium-related changes.
“Consequent loss of ion gradients in presynaptic membranes that is secondary to loss of mitochondrial anterograde transport down axons, with consequent damaging Ca2+-related changes (discussed earlier), occurs12,24,34,42.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [24]
The Discussion’s “Metabolic enzymes” section says impaired glycolysis in Alzheimer’s disease can affect ion pumps and potential gradients; “ATP production” describes damaging effects of disrupted Ca2+ homeostasis. Neither passage links these effects to loss of mitochondrial anterograde transport down axons or establishes the proposed sequence in Down syndrome. (LLM, conf=0.83)
Experimental — accuracy not yet measured3-nitrotyrosine levels, indicating peroxynitrite damage, are elevated in Alzheimer disease and amnestic mild cognitive impairment.
“Elevated levels of 3-nitrotyrosine (3-NT), suggestive of damage by peroxynitrite (Table 1) are also observed in AD18,24 and aMCI25.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [24]
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1 retracted
Retracted: Elevated expression of CaMKIIγ during osteoclastogenesis and its functional implications
Yao, C., Stern, P. H., & Zhang, L. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21155 · Cited by 47 · see citing works
RetractedNeuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
HYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542 · see citing works
Consensus Recommendations for the Postmortem Diagnosis of Alzheimer’s Disease
(1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00057-2 · Cited by 981 · see citing works
Grundman, M. (2004) · Archives of Neurology · doi:10.1001/archneur.61.1.59 · Cited by 972 · see citing works
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× · see citing works
“ATP synthase also is lower in brains from subjects with MCI, and these results are consistent with the notion of loss of enzymatic activity of oxidatively modified proteins [30, 32].”
ResultSelf-citationEvidence of neuronal oxidative damage in Alzheimer's disease.
Good, P. F., Werner, P., Hsu, A., Olanow, C. W., & Perl, D. P. (1996) · Europe PMC (PubMed Central) · Cited by 600 · see citing works
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
Self-citationProtein Nitration in Parkinsonʼs Disease
Good, P. F., Hsu, A., Werner, P., Perl, D. P., & Olanow, C. W. (1998) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199804000-00006 · Cited by 540 · see citing works
Proteomic identification of nitrated proteins in Alzheimer's disease brain
Castegna, A., Thongboonkerd, V., Klein, J. B., Lynn, B. C., Markesbery, W. R., & Butterfield, D. A. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01786.x · Cited by 535 · see citing works
Self-citationNeuropathologic 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
Self-citationMild cognitive impairment: transition between aging and Alzheimer's disease.
Petersen, R. C. (2000) · PubMed · Cited by 383 · see citing works
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
Self-citationRhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376 · see citing works
Zhang, P., Liu, B., Kang, S. W., Seo, M. S., Rhee, S. G., & Obeid, L. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30615 · Cited by 368 · see citing works
Bioenergetic and oxidative stress in neurodegenerative diseases
Bowling, A. C., & Beal, M. F. (1995) · Life Sciences · doi:10.1016/0024-3205(95)00055-b · Cited by 364 · see citing works
Identification of nitrated proteins in Alzheimer’s disease brain using a redox proteomics approach
Sultana, R., Poon, H. F., Cai, J., Pierce, W. M., Merchant, M., Klein, J. B., Markesbery, W. R., & Butterfield, D. A. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.10.004 · Cited by 364 · see citing works
Self-citationOxidative stress in Alzheimer's disease brain: New insights from redox proteomics
Butterfield, D. A., Perluigi, M., & Sultana, R. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.06.026 · Cited by 363 · see citing works
Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders
Krapfenbauer, K., Engidawork, E., Cairns, N. J., Fountoulakis, M., & Lübec, G. (2003) · Brain Research · doi:10.1016/s0006-8993(02)04243-9 · Cited by 288 · see citing works
Proteome analysis of human substantia nigra in Parkinson's disease
Basso, M., Giraudo, S., Corpillo, D., Bergamasco, B., Lopiano, L., & Fasano, M. (2004) · PROTEOMICS · doi:10.1002/pmic.200400848 · Cited by 271 · see citing works
Rukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2021 · Cited by 259 · see citing works
Calabrese, V., Guagliano, E., Sapienza, M. A., Panebianco, M., Calafato, S., Puleo, E., Pennisi, G., Mancuso, C., Butterfield, D. A., & Stella, A. G. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9203-y · Cited by 241 · see citing works
Butterfield, D. A., Reed, T. T., Marzia Perluigi, A., Marco, C. M. D., Coccia, R., Keller, J. N., Markesbery, W. R., & Rukhsana Sultana, A. (2007) · Brain Research · doi:10.1016/j.brainres.2007.02.084 · Cited by 238 · see citing works
Self-citationProteomics Analysis of the Alzheimer's Disease Hippocampal Proteome
Rukhsana Sultana, A., Debra Boyd-kimball, A., Cai, J., Pierce, W. M. J., Klein, J. B., Merchant, M. L., & Butterfield, D. A. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11203 · Cited by 231 · see citing works
MacMillan-Crow, L. A., & Thompson, J. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1202 · Cited by 227 · see citing works
Calabrese, V., Rukhsana Sultana, A., Scapagnini, G., Guagliano, E., Sapienza, M. A., Bella, R., Kański, J., Pennisi, G., Mancuso, C., Stella, A. M. G., et al. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1975 · Cited by 227 · see citing works
Kanski, J., Behring, A., Pelling, J., & Schöneich, C. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01030.2003 · Cited by 217 · see citing works
Mitochondrial dysfunction, oxidative stress and neurodegeneration
Mancuso, M., Coppedè, F., Migliore, L., Siciliano, G., & Murri, L. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-10110 · Cited by 209 · see citing works
Oxidative stress and mitochondrial dysfunction in neurodegeneration
Schapira, A. H. V. (1996) · Current Opinion in Neurology · doi:10.1097/00019052-199608000-00003 · Cited by 200 · see citing works
Tangpong, J., Cole, M. P., Rukhsana Sultana, A., Estus, S., Vore, M. E., Clair, W. H. S., Ratanachaiyavong, S., Clair, D. K. S., & Butterfield, D. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04179.x · Cited by 184 · 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
Protein Nitration in a Mouse Model of Familial Amyotrophic Lateral Sclerosis
Casoni, F., Basso, M., Massignan, T., Gianazza, E., Cheroni, C., Salmona, M., Bendotti, C., & Bonetto, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413111200 · Cited by 180 · see citing works
Tohgi, H., Abe, T., Yamazaki, K., Murata, T., Ishizaki, E., & Isobe, C. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00406-1 · Cited by 173 · see citing works
Berlett, B. S., Friguet, B., Yim, M. B., Chock, P. B., & Stadtman, E. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.1776 · Cited by 171 · see citing works
Newman, S. F., Rukhsana Sultana, A., Marzia Perluigi, A., Coccia, R., Cai, J., Pierce, W. M. J., Klein, J. B., Turner, D. M., & Butterfield, D. A. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21275 · Cited by 166 · see citing works
Self-citationPoon, H. F., Frasier, M. A., Shreve, N., Calabrese, V., Wolozin, B. L., & Butterfield, D. A. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.12.009 · Cited by 165 · see citing works
Sultana, R., & Butterfield, D. A. (2004) · Neurochemical Research · doi:10.1007/s11064-004-7028-0 · Cited by 153 · 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
Self-citationKim, S. H., Fountoulakis, M., Cairns, N. J., & Lübec, G. (2001) · Springer eBooks · doi:10.1007/978-3-7091-6262-0_18 · Cited by 142 · see citing works
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
Reynolds, M. R., Reyes, J. F., Fu, Y., Bigio, E. H., Guillozet-Bongaarts, A. L., Berry, R. W., & Binder, L. I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2143-06.2006 · Cited by 140 · see citing works
Mitochondria and Neurodegeneration
Petrozzi, L., Ricci, G., Giglioli, N. J., Siciliano, G., & Mancuso, M. (2007) · Bioscience Reports · doi:10.1007/s10540-007-9038-z · Cited by 139 · see citing works
Mitochondrial dysfunction in sporadic and genetic Alzheimer's disease
Hauptmann, S., Keil, U., Scherping, I., Bonert, A., Eckert, A., & Müller, W. E. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.03.012 · Cited by 134 · see citing works
Poon, H. F., Vaishnav, R., Getchell, T. V., Getchell, M. L., & Butterfield, D. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.006 · Cited by 131 · see citing works
Kim, S. H., Vlkolinský, R., Cairns, N. J., & Lübec, G. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000661 · Cited by 124 · see citing works
Glycolytic enzymes from human autoptic brain cortex: Normal aged and demented cases
Iwangoff, P., Armbruster, R., Enz, A., & Meier‐Ruge, W. (1980) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(80)90120-7 · Cited by 118 · see citing works
Reversible inhibition of mammalian glutamine synthetase by tyrosine nitration
Görg, B., Qvartskhava, N., Voß, P., Grune, T., Häussinger, D., & Schliess, F. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.081 · Cited by 115 · see citing works
Nitration in Neurodegeneration: Deciphering the “Hows” “nYs”
Reynolds, M. R., Berry, R. W., & Binder, L. I. (2007) · Biochemistry · doi:10.1021/bi700430y · Cited by 114 · see citing works
Role of excitotoxicity in human neurological disease
Beal, M. F. (1992) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(92)90035-j · Cited by 114 · see citing works
Proteomic identification of age-dependent protein nitration in rat skeletal muscle
Kański, J., Alterman, M. A., & Schöneich, C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00500-8 · Cited by 108 · see citing works
Association of atp synthase α-chain with neurofibrillary degeneration in alzheimer’s disease
Sergeant, N., Wattez, A., Galvn-valencia, M., Ghestem, A., David, J., Lemoine, J., Sautire, P.-E., Dachary, J., Mazat, J., Michalski, J., et al. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00747-9 · Cited by 103 · see citing works
Fluoride Exposure Attenuates Expression of Streptococcus pyogenes Virulence Factors
Thongboonkerd, V., Luengpailin, J., Cao, J., Pierce, W. M. J., Cai, J., Klein, J. B., & Doyle, R. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200746200 · Cited by 102 · see citing works
Zheng, J., & Ramirez, V. D. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1063 · Cited by 100 · see citing works
Ichimiya, S., Davis, J. G., O’Rourke, D. M., et al. (1997) · DNA and Cell Biology · doi:10.1089/dna.1997.16.311 · Cited by 98 · see citing works
Olfactory dysfunction in three neurodegenerative diseases.
Rl, D., Dp, P., Jc, S., Km, C., Jd, P., Reyes, P. F., & Kurland, L. T. (1991) · PubMed · Cited by 89 · see citing works
Castegna, A., Thongboonkerd, V., Klein, J. B., Lynn, B. C., Wang, Y., Osaka, H., Wada, K., & Butterfield, D. A. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02288.x · Cited by 89 · see citing works
Sultana, R., Reed, T., Perluigi, M., Coccia, R., Pierce, W. M., & Butterfield, D. A. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00065.x · Cited by 87 · see citing works
Self-citationRukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2005) · Journal of Chromatography B · doi:10.1016/j.jchromb.2005.09.024 · Cited by 72 · see citing works
Mitochondrial Dysfunction and Alzheimers Disease
Chen, X., Stern, D. M., & Yan, S. D. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025215 · Cited by 71 · see citing works
Oxidative stress and mitochondrial dysfunction in neurodegeneration.
Hj, T., Packer, L., & Medori, R. (1994) · PubMed · Cited by 71 · see citing works
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
Kishi, H., Mukai, T., Hirono, A., Fujii, H., Miwa, S., & Hori, K. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8623 · Cited by 68 · see citing works
Royall, D. R., Chiodo, L. K., Polk, M. J., et al. (2002) · Neuroepidemiology · doi:10.1159/000048619 · Cited by 67 · see citing works
Kowaltowski, A. J., Vercesi, A. E., Rhee, S. G., & Netto, L. E. S. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01526-x · Cited by 65 · see citing works
Facheris, M., Beretta, S., & Ferrarese, C. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6210 · Cited by 61 · see citing works
Jung, O., Marklund, S. L., Xia, N., Busse, R., & Brandes, R. P. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000254823.15843.1f · Cited by 51 · see citing works
Eber, S., Pekrun, A., Bardosi, A., et al. (1991) · European Journal of Pediatrics · doi:10.1007/bf02026706 · Cited by 50 · see citing works
Oxidative damage and mitochondrial dysfunction in neurodegenerative diseases
Browne, S. E., & Beal, M. F. (1994) · Biochemical Society Transactions · doi:10.1042/bst0221002 · Cited by 50 · see citing works
Toward High-Throughput Drug Screening Using Mass Spectrometry
Maurer, H. H., & Peters, F. T. (2005) · Therapeutic Drug Monitoring · doi:10.1097/01.ftd.0000180224.19384.f0 · Cited by 47 · see citing works
Peroxiredoxin I and II inhibit H2O2‐induced cell death in MCF‐7 cell lines
Bae, J., Ahn, S., Han, W., & Noh, D. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21241 · Cited by 47 · see citing works
Human Olfactory Receptor Neurons Express Heat Shock Protein 70: Age-Related Trends
Getchell, T. V., Krishna, N. S. R., Sparks, D. L., et al. (1995) · Annals of Otology Rhinology & Laryngology · doi:10.1177/000348949510400108 · Cited by 44 · see citing works
The role of nitric oxide in amyotrophic lateral sclerosis
Urushitani, M. (2001) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/146608201316949415 · Cited by 43 · see citing works
Oxidative stress in the aging murine olfactory bulb: Redox proteomics and cellular localization
Vaishnav, R., Getchell, M. L., Poon, H. F., Barnett, K. R., Hunter, S. A., Pierce, W. M. J., Klein, J. B., Butterfield, D. A., & Getchell, T. V. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21130 · Cited by 42 · see citing works
Reix, S., Mechawar, N., Susín, S. A., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.01.003 · Cited by 35 · see citing works
Focused Proteomics in Post-Mortem Human Spinal Cord
Ekegren, T., Hanrieder, J., Aquilonius, S., & Bergquist, J. (2006) · Journal of Proteome Research · doi:10.1021/pr060237f · Cited by 32 · see citing works
Lymphocyte Glutamate Dehydrogenase Activity in Normal Aging and Neurological Diseases
Iwatsuji, K., Nakamura, S., & Kameyama, M. (2009) · Gerontology · doi:10.1159/000213026 · Cited by 29 · see citing works
Triosephosphate isomerase deficiency: 2 new cases
Zanella, A., Mariani, M., Colombo, M. B., et al. (1985) · Scandinavian Journal of Haematology · doi:10.1111/j.1600-0609.1985.tb00771.x · Cited by 19 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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Butterfield, D. A., & Halliwell, B. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0132-6 · Cited by 1,954 · see citing works
Self-citationOxidative stress and mitochondrial dysfunction in Alzheimer’s disease
Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357 · see citing works
Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease
Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654 · see citing works
Butterfield, D. A., Swomley, A. M., & Sultana, R. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5027 · Cited by 526 · see citing works
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
Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases
Nixon, R. A., & Rubinsztein, D. C. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00757-5 · Cited by 435 · see citing works
Butterfield, D. A., & Boyd-Kimball, D. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170543 · Cited by 403 · see citing works
Di Domenico, F., Barone, E., Perluigi, M., & Butterfield, D. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6759 · Cited by 114 · see citing works
Asiatic acid protects primary neurons against C2-ceramide-induced apoptosis
Zhang, X., Wu, J., Dou, Y., Xia, B., Rong, W., Rimbach, G., & Lou, Y. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.01.006 · Cited by 99 · see citing works
CNS Peroxiredoxins and Their Regulation in Health and Disease
Bell, K. F. S., & Hardingham, G. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3567 · Cited by 71 · see citing works
Amyloid-β Peptide Nitrotyrosination Stabilizes Oligomers and Enhances NMDAR-Mediated Toxicity
Guivernau, B., Bonet, J., Valls-Comamala, V., Bosch-Morató, M., Godoy, J. A., Inestrosa, N. C., Perálvarez-Marín, A., Fernández-Busquets, X., Andreu, D., Oliva, B., et al. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.1081-16.2016 · Cited by 69 · see citing works
Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases
Yeo, W., Kim, Y. J., Kabir, M. H., Kang, J. W., & Kim, K. P. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21429 · Cited by 61 · see citing works
Sutinen, E. M., Korolainen, M. A., Häyrinen, J., Alafuzoff, I., Petratos, S., Salminen, A., Soininen, H., Pirttilä, T., & Ojala, J. O. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00214 · Cited by 34 · see citing works
- Authors
- Reed, T. T., Pierce Jr., W. M., Turner, D. M., Markesbery, W. R., & Allan Butterfield, D.
- Affiliations
- University of Kentucky (US)
- University of Louisville (US)
- ORCID
- Reed, Tanea T.
- Venue
- Journal of Cellular and Molecular Medicine
- Publisher
- Wiley
- Published
- 2008-08-22
- Volume
- 13
- Issue
- 8b
- Pages
- 2019-2029
- ISSN
- 1582-1838 (ISSN-L)
- 1582-4934
- PMC
- PMC2819643
- OpenAlex
- W2029887257
- Cited by
- 135
- References
- 78
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 7 · 2023: 5 · 2022: 6 · 2021: 8 · 2020: 8 · 2019: 6 · 2018: 8 · 2017: 7 · 2016: 7 · 2015: 9 · 2014: 7 · 2013: 10 · 2012: 9
- FWCI
- 6.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Cellular and Molecular Medicine (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (P30AG028383, P01AG010836, P01AG005119, 3P30 AG-028383, AG 10836, AG0 5119)
- Topics
- Health Sciences › Medicine › Physiology › 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
- Alzheimer's disease, early Alzheimer's disease, protein nitration, inferior parietal lobule, oxidative stress, mild cognitive impairment, peroxiredoxin 2, triosephosphate isomerase, glutamate dehydrogenase, phosphoglycerate mutase 1, alpha-enolase, fructose-1,6-bisphosphate aldolase, disease progression
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Female, Humans, Male, Nerve Tissue Proteins, Nitrates, Parietal Lobe, Proteomics
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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