Methionine-35 of A β (1–42): Importance for Oxidative Stress in Alzheimer Disease

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063

Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease

Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326

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

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447

Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease

Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239

The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction

Huang, X., Atwood, C., Hartshorn, M. A., Multhaup, G., Goldstein, L. E., Scarpa, R. C., Cuajungco, M. P., Gray, D. N., Lim, J. T., Moir, R. D., et al. (1999) · Biochemistry · doi:10.1021/bi990438f · Cited by 1,117

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

Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression

Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104

Metals, oxidative stress and neurodegenerative disorders

Jomová, K., Vondráková, D., Lawson, M. K., & Valko, M. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0563-x · Cited by 1,074

Lipid peroxidation and protein oxidation in Alzheimer’s disease brain: potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress

Butterfield, D. A., & Lauderback, C. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00794-3 · Cited by 1,013

Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial

Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988

Biologically relevant metal ion‐dependent hydroxyl radical generation An update

Halliwell, B. B., & Gutteridge, J. M. C. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80911-y · Cited by 884

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 1×

Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease

Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738

Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity

Varadarajan, S., Yatin, S., Aksenova, M., & Butterfield, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4274 · Cited by 735

Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer’s disease brain contribute to neuronal death1

Allanbutterfield, D., Castegna, A., Lauderback, C. M., & Drake, J. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00340-2 · Cited by 715

Structure‐Activity Analyses of β‐Amyloid Peptides: Contributions of the β25–35 Region to Aggregation and Neurotoxicity

Pike, C. J., Walencewicz‐Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., & Cotman, C. W. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010253.x · Cited by 699

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 658

The redox chemistry of the Alzheimer's disease amyloid β peptide

Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608

Oxidative Modifications and Down-regulation of Ubiquitin Carboxyl-terminal Hydrolase L1 Associated with Idiopathic Parkinson's and Alzheimer's Diseases

Choi, J., Levey, A. I., Weintraub, S. T., Rees, H. D., Gearing, M., Chin, L.-S., & Li, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314124200 · Cited by 568

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

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

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

Protein oxidation in the brain in Alzheimer's disease

Aksenov, M. Y., Aksenova, M. V., Butterfield, D. A., Geddes, J. W., & Markesbery, W. R. (2001) · Neuroscience · doi:10.1016/s0306-4522(00)00580-7 · Cited by 505

Relative Abundance of Alzheimer A Beta Amyloid Peptide Variants in Alzheimer Disease and normal Aging

Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L., Roses, A. D., Tjernberg, L. O., Silberring, J., Gandy, S. E., Winblad, B., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8378 · Cited by 468

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

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

Methionine in proteins defends against oxidative stress

Luo, S., & Levine, R. L. (2008) · The FASEB Journal · doi:10.1096/fj.08-118414 · Cited by 462

β-Amyloid Peptide Free Radical Fragments Initiate Synaptosomal Lipoperoxidation in a Sequence-Specific Fashion: Implications to Alzheimer′s Disease

Butterfield, D. A., Hensley, K., Harris‐White, M. E., Mattson, M. P., & Carney, J. M. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1508 · Cited by 404

A second cytotoxic proteolytic peptide derived from amyloid β-protein precursor

Lu, D. C.-T., Rabizadeh, S., Chandra, S. S., Shayya, R. F., Ellerby, L., Ye, X., Salvesen, G. S., Koo, E. H., & Bredesen, D. E. (2000) · Nature Medicine · doi:10.1038/74656 · Cited by 403

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

Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease

Schöneich, C. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.009 · Cited by 372

Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid β-peptide (1–42) in a transgenic Caenorhabditis elegans model

Drake, J. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00225-7 · Cited by 371

Different Mechanisms of Oxidative Stress and Neurotoxicity for Alzheimer‘s Aβ(1−42) and Aβ(25−35)

Varadarajan, S., Kanski, J., Aksenova, M., Lauderback, C., & Butterfield, D. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010452r · Cited by 346

Oxidation of Methionine Residues of Proteins: Biological Consequences

Stadtman, E. R., Moskovitz, J., & Levine, R. L. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770310239 · Cited by 344

Discussion

(1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00056-1 · Cited by 330

Degradation of the Alzheimer Disease Amyloid β-Peptide by Metal-dependent Up-regulation of Metalloprotease Activity

White, A. R., Du, T., Laughton, K. M., Volitakis, I., Sharples, R. A., Xilinas, M. E., Hoke, D. E., Holsinger, R. M. D., Evin, G., Cherny, R. A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602487200 · Cited by 284

Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment

Markesbery, W. R., Kryscio, R. J., Lovell, M. A., & Morrow, J. D. (2005) · Annals of Neurology · doi:10.1002/ana.20629 · Cited by 277

The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1–42)-induced oxidative stress and neurotoxicity

Butterfield, D. A., & Debra Boyd-kimball, A. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.10.014 · Cited by 270

The Lipid Peroxidation Product, 4‐Hydroxy‐2‐trans‐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

Drug Development Based on the Metals Hypothesis of Alzheimer's Disease

Bush, A. I. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-15208 · Cited by 267

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

Genome-wide association studies in Alzheimer’s disease

Bertram, L., & Tanzi, R. E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp406 · Cited by 257

Decrease in Peptide Methionine Sulfoxide Reductase in Alzheimer's Disease Brain

Gabbita, S. P., Aksenov, M. Y., Lovell, M. A., & Markesbery, W. R. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0731660.x · Cited by 256

Effects of injected Alzheimer beta-amyloid cores in rat brain.

Frautschy, S. A., Baird, A., & Cole, G. M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8362 · Cited by 254

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

Vitamin E Prevents Alzheimer's Amyloid ß-Peptide (1-42)-Induced Neuronal Protein Oxidation and Reactive Oxygen Species Production

Yatin, S. M., Varadarajan, S., & Butterfield, D. A. (2000) · Journal of Alzheimer s Disease · doi:10.3233/jad-2000-2212 · Cited by 241

Reversal of Alzheimer’s-like pathology and behavior in human APP transgenic mice by mutation of Asp664

Galvan, V., Gorostiza, O. F., Banwait, S., Ataie, M., Logvinova, A. V., Sitaraman, S., Carlson, E., Sagi, S. A., Chevallier, N., Jin, K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509695103 · Cited by 239

Oxidatively modified proteins in Alzheimer’s disease (AD), mild cognitive impairment and animal models of AD: role of Abeta in pathogenesis

Sultana, R., Perluigi, M., & Butterfield, D. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0517-0 · Cited by 215

Oxidative Nerve Cell Death in Alzheimers Disease and Stroke: Antioxidants as Neuroprotective Compounds

Behl, C., & Moosmann, B. (2002) · Biological Chemistry · doi:10.1515/bc.2002.053 · Cited by 203

Free Radical Reactions of Methionine in Peptides: Mechanisms Relevant to β-Amyloid Oxidation and Alzheimer's Disease

Schöneich, C., Pogocki, D., Hug, G. L., & Bobrowski, K. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036733b · Cited by 199

Amyloid Accumulation and Pathogensis of Alzheimer’s Disease: Significance of Monomeric, Oligomeric and Fibrillar Aβ

Glabe, C. C. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_8 · Cited by 193

Neurotoxic, Redox-competent Alzheimer's β-Amyloid Is Released from Lipid Membrane by Methionine Oxidation

Barnham, K. J., Ciccotosto, G. D., Tickler, A. K., Ali, F. E. A., Smith, D. G., Williamson, N. A., Lam, Y.-H., Carrington, D., Tew, D. J., Kocak, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305494200 · Cited by 191

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

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

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 181

The biochemistry of methionine sulfoxide residues in proteins

Brot, N., & Weissbach, H. (1982) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(82)90204-3 · Cited by 171

Neuronal Death and Survival Under Oxidative Stress in Alzheimer and Parkinson Diseases

Nunomura, A., Moreira, P. I., Lee, H., Zhu, X., Castellani, R. J., Smith, M. A., & Perry, G. L. (2007) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152707783399201 · Cited by 140

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 132

Oxidation of Methionine 35 Attenuates Formation of Amyloid β-Peptide 1–40 Oligomers

Palmblad, M., Westlind‐Danielsson, A., & Bergquist, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112218200 · Cited by 130

Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization

Murray, M. M., Bernstein, S. L., Nyugen, V., Condron, M. M., Teplow, D. B., & Bowers, M. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8092604 · Cited by 128

Examination of the current top candidate genes for AD in a genome-wide association study

Feulner, T. M., Laws, S. M., Friedrich, P., Wagenpfeil, S., Wurst, S. H. R., Riehle, C., Kuhn, K. A., Krawczak, M., Schreiber, S., Nikolaus, S., et al. (2010) · Molecular Psychiatry · doi:10.1038/mp.2008.141 · Cited by 128

Oxidative Damage to Proteins, Lipids, and DNA in Cortical Brain Regions from Patients with Dementia with Lewy Bodies

Lyras, L., Perry, R. H., Perry, E. K., Ince, P. G., Jenner, A. M., Jenner, P. G., & Halliwell, B. B. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71010302.x · Cited by 121

β-Amyloid peptide increases levels of iron content and oxidative stress in human cell and Caenorhabditis elegans models of Alzheimer disease

Wan, L., Nie, G., Zhang, J., Luo, Y., Zhang, P., Zhang, Z., & Zhao, B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.10.707 · Cited by 121

Trolox and 17β-Estradiol Protect against Amyloid β-Peptide Neurotoxicity by a Mechanism That Involves Modulation of the Wnt Signaling Pathway

Quintanilla, R. A., Muñoz, F. J., Metcalfe, M., Hitschfeld, M., Olivares, G. H., Godoy, J. A., & Inestrosa, N. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411936200 · Cited by 114

Depletion of Vitamin E Increases Amyloid β Accumulation by Decreasing Its Clearances from Brain and Blood in a Mouse Model of Alzheimer Disease

Nishida, Y., Ito, S., Ohtsuki, S., Yamamoto, N., Takahashi, T., Iwata, N., Jishage, K.-I., Yamada, H., Sasaguri, H., Yokota, S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054056 · Cited by 106

Amyloid β‐Peptides Increase Annular and Bulk Fluidity and Induce Lipid Peroxidation in Brain Synaptic Plasma Membranes

Avdulov, N. A., Chochina, S. V., Igbavboa, U., O‘Hare, E., Schroeder, F., Cleary, J. P., & Wood, W. G. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68052086.x · Cited by 106

Alzheimer’s amyloid β-peptide (1–42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: An intriguing role for methionine 35

Clementi, M. E., Pezzotti, M., Orsini, F., Sampaolese, B., Mezzogori, D., Grassi, C., Giardina, B., & Misiti, F. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.137 · Cited by 105

Melatonin protects SHSY5Y neuroblastoma cells from cobalt‐induced oxidative stress, neurotoxicity and increased β‐amyloid secretion

Olivieri, G., Hess, C. W., Savaskan, E., Ly, C. V., Meier, F., Baysang, G., Brockhaus, M., & Müller-Spahn, F. (2001) · Journal of Pineal Research · doi:10.1034/j.1600-079x.2001.310406.x · Cited by 105

SET protein (TAF1β, I2PP2A) is involved in neuronal apoptosis induced by an amyloid precursor protein cytoplasmic subdomain

Madeira, A., Pommet, J., Prochiantz, A., & Allinquant, B. (2005) · The FASEB Journal · doi:10.1096/fj.05-3839fje · Cited by 102

Enhanced Toxicity and Cellular Binding of a Modified Amyloid β Peptide with a Methionine to Valine Substitution

Ciccotosto, G. D., Tew, D. J., Curtain, C. C., Smith, D., Carrington, D., Masters, C. L., Bush, A. I., Cherny, R. A., Cappai, R., & Barnham, K. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406465200 · Cited by 101

Oxidatively modified RNA in mild cognitive impairment

Lovell, M. A., & Markesbery, W. R. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.07.030 · Cited by 93

Alzheimer β protein mediated oxidative damage of mitochondrial DNA: Prevention by melatonin

Pappolla, M. A., Chyan, Y., Pöeggeler, B., Bozner, P., Ghiso, J. A., LeDoux, S. P., & Wilson, G. L. (1999) · Journal of Pineal Research · doi:10.1111/j.1600-079x.1999.tb00619.x · Cited by 89

Enzymatic reactions involved in the repair of oxidized proteins

Mary, J., Vougier, S., Picot, C. R., Perichon, M., Petropoulos, I., & Friguet, B. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.06.008 · Cited by 87

Enhanced brain levels of 8,12- iso -iPF 2α -VI differentiate AD from frontotemporal dementia

Yao, Y., Zhukareva, V., Sung, S., Clark, C. M., Rokach, J., Lee, V. M.-Y., Trojanowski, J. Q., & Praticò, D. (2003) · Neurology · doi:10.1212/01.wnl.0000070185.02546.5d · Cited by 86

Role of glycine-33 and methionine-35 in Alzheimer’s amyloid β-peptide 1–42-associated oxidative stress and neurotoxicity

Kański, J., Varadarajan, S., Aksenova, M. V., & Butterfield, D. A. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00097-7 · Cited by 83

Development of a Method for Quantification of Acrolein−Deoxyguanosine Adducts in DNA Using Isotope Dilution-Capillary LC/MS/MS and Its Application to Human Brain Tissue

Liu, X., Lovell, M. A., & Lynn, B. C. (2005) · Analytical Chemistry · doi:10.1021/ac050624t · Cited by 79

Radioiodinated clioquinol as a biomarker for β‐amyloid: Zn2+ complexes in Alzheimer's disease

Opazo, C., Luza, S., Villemagne, V. L., Volitakis, I., Rowe, C. C., Barnham, K. J., Altschul, D., Masters, C. L., Cherny, R. A., & Bush, A. I. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00196.x · Cited by 76

Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Aβ(1–42)☆

Rukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2005) · Journal of Chromatography B · doi:10.1016/j.jchromb.2005.09.024 · Cited by 72

Role of phenylalanine 20 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity.

Boyd-Kimball, D., Abdul, H. M., Reed, T. T., Sultana, R., & Butterfield, D. (2004) · Chemical Research in Toxicology · doi:10.1021/tx049796w · Cited by 67

Redox Properties of Met35in Neurotoxic β-Amyloid Peptide. A Molecular Modeling Study

Pogocki, D., & Schöneich, C. (2002) · Chemical Research in Toxicology · doi:10.1021/tx0101550 · Cited by 66

Chapter 9 Alzheimer's Disease Genetics

Bertram, L. (2009) · International review of neurobiology · doi:10.1016/s0074-7742(09)00409-7 · Cited by 63

Cyclic oxidation and reduction of methionine residues of proteins in antioxidant defense and cellular regulation

Stadtman, E. R. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.10.001 · Cited by 61

The hydrophobic environment of Met35 of Alzheimer's Aβ(1–42) is important for the neurotoxic and oxidative properties of the peptide

Kański, J., Aksenova, M. V., & Butterfield, D. A. (2002) · Neurotoxicity Research · doi:10.1080/10298420290023945 · Cited by 58

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Johansson, A., Bergquist, J., Volbracht, C., Päiviö, A., Leist, M., Lannfelt, L., & Westlind‐Danielsson, A. (2007) · Neuroreport · doi:10.1097/wnr.0b013e3280b07c21 · Cited by 53

Despite its role in assembly, methionine 35 is not necessary for amyloid β‐protein toxicity

Maiti, P., Lomakin, A., Benedek, G. B., & Bitan, G. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06692.x · Cited by 46

Oxidation of methionine 35 reduces toxicity of the amyloid beta-peptide(1–42) in neuroblastoma cells (IMR-32) via enzyme methionine sulfoxide reductase A expression and function

Misiti, F., Clementi, M. E., & Giardina, B. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.01.002 · Cited by 44

Long-term prevention of Alzheimer's disease-like behavioral deficits in PDAPP mice carrying a mutation in Asp664

Galván, V., Zhang, J., Gorostiza, O. F., Banwait, S., Huang, W., Ataie, M., Tang, H., & Bredesen, D. E. (2008) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.03.035 · Cited by 43

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Cerpa, W. F., Barría, M. I., Chacón, M. A., Suazo, M., González, M., Opazo, C., Bush, A. I., & Inestrosa, N. C. (2004) · The FASEB Journal · doi:10.1096/fj.03-1349fje · Cited by 41

Possible involvement of copper(II) in Alzheimer disease.

Kowalik‐Jankowska, T., Ruta-Dolejsz, M., Wiśniewska, K., Łankiewicz, L., & Kozłowski, H. (2002) · Environmental Health Perspectives · doi:10.1289/ehp.02110s5869 · Cited by 38

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Clementi, M. E., Martorana, G. E., Pezzotti, M., Giardina, B., & Misiti, F. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.03.006 · Cited by 33

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LaBrenz, S. R., Calmann, M. A., Heavner, G. A., & Tolman, G. (2008) · PubMed · Cited by 13

Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185

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Jiang, T., Sun, Q., & Chen, S. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.07.005 · Cited by 605

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Ke, P. C., Sani, M., Ding, F., Käkinen, A., Javed, I., Separovic, F., Davis, T. P., & Mezzenga, R. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00372b · Cited by 340

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Tramutola, A., Lanzillotta, C., Perluigi, M., & Butterfield, D. A. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.06.005 · Cited by 303

doi:10.4061/2011/198430 Review Article Methionine-35 of Aβ(1–42): Importance for Oxidative Stress in Alzheimer Disease

Butterfield, D. A., & Rukhsana Sultana, A. (2011)

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