Amyloid β -Peptide (1–42)-Induced Oxidative Stress in Alzheimer Disease: Importance in Disease Pathogenesis and Progression

“Mini-mental state”

Folstein, M. F., Folstein, S. E., & McHugh, P. R. (1975) · Journal of Psychiatric Research · doi:10.1016/0022-3956(75)90026-6 · Cited by 88,282 · see citing works

[Japanese version of the Neuropsychiatric Inventory--a scoring system for neuropsychiatric disturbance in dementia patients].

Hirono, N., Mori, E., Ikejiri, Y., Imamura, T., Shimomura, T., Hashimoto, M., Yamashita, H., & Ikeda, M. (1997) · PubMed · Cited by 21,010 · see citing works

Special Care Units and Traditional Care in Dementia: Relationship with Behavior, Cognition, Functional Status and Quality of Life - A Review

Kok, J. S., Berg, I. J., & Scherder, E. J. A. (2013) · Dementia and Geriatric Cognitive Disorders Extra · doi:10.1159/000353441 · Cited by 20,589 · see citing works

Older Adults' Reasons for Using Technology while Aging in Place

Peek, S. T. M., Luijkx, K. G., Rijnaard, M. D., Nieboer, M. E., van der Voort, C. S., Aarts, S., van Hoof, J., Vrijhoef, H. J., & Wouters, E. (2015) · Gerontology · doi:10.1159/000430949 · Cited by 19,803 · see citing works

Sensitivity and False Alarm Rate of a Fall Sensor in Long-Term Fall Detection in the Elderly

Kangas, M., Korpelainen, R., Vikman, I., Nyberg, L., & Jämsä, T. J. (2014) · Gerontology · doi:10.1159/000362720 · Cited by 19,003 · see citing works

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works

Mild cognitive impairment as a diagnostic entity

Petersen, R. C. (2004) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2004.01388.x · Cited by 7,864 · see citing works

Toward defining the preclinical stages of Alzheimer’s disease: Recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease

Sperling, R. A., Aisen, P. S., Beckett, L. A., Bennett, D. A., Craft, S., Fagan, A. M., Iwatsubo, T., Jack, C. R., Kaye, J., Montine, T. J., et al. (2011) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.03.003 · Cited by 7,155 · see citing works

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 · see citing works

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431 · see citing works

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · see citing works

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599 · see citing works

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 · see citing works

Alzheimer Disease in the US Population: Prevalence Estimates Using the 2000 Census

Hebert, L. E., Scherr, P. A., Bienias, J. L., Bennett, D. A., & Evans, D. A. (2003) · Archives of Neurology · doi:10.1001/archneur.60.8.1119 · Cited by 2,168 · see citing works

Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature

Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · cited 1× · see citing works

The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022 · 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

Prediction of AD with MRI-based hippocampal volume in mild cognitive impairment

Jack, C. R., Petersen, R. C., Xu, Y. C., O’Brien, P. C., Smith, G. E., Ivnik, R. J., Boeve, B. F., Waring, S. C., Tangalos, E. G., & Kokmen, E. (1999) · Neurology · doi:10.1212/wnl.52.7.1397 · Cited by 1,404 · see citing works

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 · see citing works

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 · see citing works

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 1,107 · see citing works

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 1,053 · see citing works

Oxidative damage to mitochondrial DNA is increased in Alzheimer’s disease

Mecocci, P., MacGarvey, U., & Beal, M. F. (1994) · Annals of Neurology · doi:10.1002/ana.410360510 · Cited by 1,037 · see citing works

Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives

Mattson, M. P. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.4.1081 · Cited by 1,006 · see citing works

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 999 · see citing works

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 · see citing works

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 · see citing works

Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration

Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., & Selkoe, D. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017033108 · Cited by 876 · see citing works

Discrimination between Alzheimer dementia and controls by automated analysis of multicenter FDG PET

Herholz, K., Salmon, E., Perani, D., Baron, J.-C., Holthoff, V., Frölich, L., Schönknecht, P., Ito, K., Mielke, R., & Kalbe, E. (2002) · NeuroImage · doi:10.1006/nimg.2002.1208 · Cited by 832 · see citing works

Oxidative Alterations in Alzheimer's Disease

Markesbery, W. R., & Carney, J. M. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00215.x · Cited by 789 · see citing works

Involvement of Caspases in Proteolytic Cleavage of Alzheimer’s Amyloid-β Precursor Protein and Amyloidogenic Aβ Peptide Formation

Gervais, F. G., Xu, D., Robertson, G. S., Vaillancourt, J. P., Zhu, Y., Huang, J., LeBlanc, A. C., Smith, D., Rigby, M., Shearman, M. S., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80748-5 · Cited by 784 · see citing works

A Role for 4‐Hydroxynonenal, an Aldehydic Product of Lipid Peroxidation, in Disruption of Ion Homeostasis and Neuronal Death Induced by Amyloid β‐Peptide

Mark, R. J., Lovell, M. A., Markesbery, W. R., Uchida, K., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68010255.x · Cited by 781 · 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 1× · see citing works

RNA Oxidation Is a Prominent Feature of Vulnerable Neurons in Alzheimer’s Disease

Nunomura, A., Perry, G., Pappolla, M., Wade, R., Hirai, K., Chiba, S., & Smith, M. A. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-06-01959.1999 · Cited by 768 · see citing works

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 · see citing works

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721 · see citing works

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 · see citing works

Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent

Ranganathan, R., Lu, K. P., Hunter, T. R., & Noel, J. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80273-1 · Cited by 703 · see citing works

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 · 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

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 653 · see citing works

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 · see citing works

Mild cognitive impairment

Chételat, G., Desgranges, B., Sayette, V. D. L., Viader, F., Eustache, F., & Baron, J. (2003) · Neurology · doi:10.1212/01.wnl.0000055847.17752.e6 · Cited by 604 · 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

Cell death and diseases related to oxidative stress: 4-hydroxynonenal (HNE) in the balance

Dalleau, S., Baradat, M., Guéraud, F., & Huc, L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.138 · Cited by 580 · see citing works

Neurofibrillary Tangles, Amyloid, and Memory in Aging and Mild Cognitive Impairment

Guillozet-Bongaarts, A. L., Weıntraub, S., Mash, D. C., & Mesulam, M. M. (2003) · Archives of Neurology · doi:10.1001/archneur.60.5.729 · Cited by 572 · 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

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

Oxidative Stress and Neurodegenerative Disorders

Li, J., Wuliji, O., Li, W., Jiang, Z.-G., & Ghanbari, H. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141224438 · Cited by 511 · see citing works

Peptide Compositions of the Cerebrovascular and Senile Plaque Core Amyloid Deposits of Alzheimer′s Disease

Miller, D. L., Papayannopoulos, I. A., Styles, J., Bobin, S. A., Lin, Y. Y., Biemann, K., & Iqbal, K. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1112 · Cited by 510 · see citing works

Electrochemical Analysis of Protein Nitrotyrosine and Dityrosine in the Alzheimer Brain Indicates Region-Specific Accumulation

Hensley, K., Maidt, M. L., Yu, Z., Sang, H., Markesbery, W. R., & Floyd, R. A. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-20-08126.1998 · Cited by 508 · see citing works

Amyloid-β oligomers: their production, toxicity and therapeutic inhibition

Walsh, D. M., Klyubin, I. V., Fadeeva, J. V., Rowan, M. J., & Selkoe, D. J. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300552 · Cited by 507 · see citing works

Increased Nuclear DNA Oxidation in the Brain in Alzheimer's Disease

Gabbita, S. P., Lovell, M. A., & Markesbery, W. R. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71052034.x · Cited by 479 · see citing works

Analysis of Heterogeneous βA4 Peptides in Human Cerebrospinal Fluid and Blood by a Newly Developed Sensitive Western Blot Assay

Ida, N., Hartmann, T., Pantel, J., Schrüder, J., Zerfaß, R., Fürstl, H., Sandbrink, R., Masters, C. L., & Beyreuther, K. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22908 · Cited by 476 · see citing works

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 · 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

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 · 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 amyloid precursor protein: beyond amyloid.

Zheng, H., & Koo, E. H. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-5 · Cited by 403 · see citing works

Rapid Communication: Characterization of β‐Amyloid Peptide from Human Cerebrospinal Fluid

Vigo‐Pelfrey, C., Lee, D., Keim, P., Lieberburg, I., & Schenk, D. B. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09841.x · Cited by 385 · see citing works

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

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

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 · see citing works

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 · see citing works

β-Amyloid-Associated Free Radical Oxidative Stress and Neurotoxicity: Implications for Alzheimer’s Disease

Butterfield, D. A. (1997) · Chemical Research in Toxicology · doi:10.1021/tx960130e · 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

Advances in Alzheimer's disease

Katzman, R., & Saitoh, T. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.3.2001787 · Cited by 357 · see citing works

Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress

Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., et al. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1080 · Cited by 352 · see citing works

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 · see citing works

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 · 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

Discussion

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

Alzheimer's disease – synergistic effects of glucose deficit, oxidative stress and advanced glycation endproducts

Münch, G. W., Schinzel, R., Loske, C., Wong, A. O., Durany, N., Li, J. J., Vlassara, H., Smith, M. A., Perry, G. L., & Riederer, P. F. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050069 · Cited by 302 · see citing works

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 · see citing works

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 272 · see citing works

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 · see citing works

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 267 · see citing works

Structural Analysis of α-Enolase

Subramanian, A. K., & Miller, D. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5958 · Cited by 265 · see citing works

Oxidative DNA damage in peripheral leukocytes of mild cognitive impairment and AD patients

Migliore, L., Fontana, I., Trippi, F., Colognato, R., Coppedè, F., Tognoni, G., Nucciarone, B., & Siciliano, G. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.07.016 · Cited by 263 · see citing works

Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures

Schmidt, M., Sachse, C., Richter, W., Chen, X., Fändrich, M., & Grigorieff, N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905007106 · Cited by 261 · see citing works

Increased oxidative damage in nuclear and mitochondrial DNA in mild cognitive impairment

Wang, J., Markesbery, W. R., & Lovell, M. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03615.x · Cited by 260 · 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

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 · see citing works

Intraneuronal Aβ42 accumulation in Down syndrome brain: Original Articles

Mori, C., Spooner, E. T., Wisniewski, K. E., Wisniewski, T. M., Yamaguchi, H., Saido, T. C., Tolan, D. R., Selkoe, D. J., & Lemere, C. A. (2002) · Amyloid · doi:10.3109/13506120208995241 · Cited by 255 · 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

Increased oxidative stress in Alzheimer's disease as assessed with 4-hydroxynonenal but not malondialdehyde

McGrath, L. T. (2001) · QJM · doi:10.1093/qjmed/94.9.485 · Cited by 253 · see citing works

Intraneuronal Aβ-Amyloid Precedes Development of Amyloid Plaques in Down Syndrome

Gyure, K. A., Durham, R., Stewart, W. F., Smialek, J. E., & Troncoso, J. C. (2001) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2001-125-0489-iaapdo · Cited by 248 · see citing works

Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds

Stefani, M., & Rigacci, S. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140612411 · Cited by 239 · see citing works

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 239 · see citing works

Oxidative imbalance in patients with mild cognitive impairment and Alzheimer’s disease

GUIDI, I., GALIMBERTI, D., LONATI, S., NOVEMBRINO, C., BAMONTI, F., TIRITICCO, M., FENOGLIO, C., VENTURELLI, E., BARON, P., & BRESOLIN, N. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.01.001 · Cited by 203 · see citing works

Oxidative Stress in Alzheimer’s Disease: Are We Connecting the Dots?

Rosini, M., Simoni, E., Milelli, A., Minarini, A., & Melchiorre, C. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400970m · Cited by 202 · see citing works

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 · 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

Nitric Oxide in Cell Survival: A Janus Molecule

Calabrese, V., Cornelius, C., Rizzarelli, E., Owen, J. B., Dinkova‐Kostova, A. T., & Butterfield, D. A. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2721 · Cited by 195 · see citing works

Age-dependent Accumulation of Soluble Amyloid β (Aβ) Oligomers Reverses the Neuroprotective Effect of Soluble Amyloid Precursor Protein-α (sAPPα) by Modulating Phosphatidylinositol 3-Kinase (PI3K)/Akt-GSK-3β Pathway in Alzheimer Mouse Model

Jiménez, S., Torres, M., Vizuete, M., Sanchez-Varo, R. M., Sánchez‐Mejías, E., Trujillo‐Estrada, L., Carmona‐Cuenca, I., Caballero, C., Ruano, D., Gutiérrez, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209718 · Cited by 190 · 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

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

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 187 · see citing works

The Identification and Characterization of Oxidized RNAs in Alzheimer's Disease

Shan, X., Tashiro, H., & Lin, C. G. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-12-04913.2003 · Cited by 185 · 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

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

Oxidative Stress and Down Syndrome: A Route toward Alzheimer-Like Dementia

Marzia Perluigi, A., & Butterfield, D. A. (2011) · Current Gerontology and Geriatrics Research · doi:10.1155/2012/724904 · Cited by 180 · see citing works

REVIEW: Pin1 in Alzheimer's disease

Butterfield, D. A., Abdul, H. M., Opii, W. O., Newman, S. F., Gururaj Joshi, A., Ansari, M. A., & Rukhsana Sultana, A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03995.x · Cited by 179 · see citing works

Access to diagnostic evaluation and treatment for dementia in Europe

Waldemar, G., Phung, T. K. T., Burns, A. S., Georges, J., Hansen, F. R., Iliffe, S., Marking, C., Rikkert, M. G. M. O., Selmès, J., Stoppe, G., et al. (2006) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.1652 · Cited by 177 · 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

PET amyloid-beta imaging in preclinical Alzheimer's disease

Vlassenko, A. G., Benzinger, T. L. S., & Morris, J. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.005 · Cited by 173 · see citing works

Methionine residue 35 is important in amyloid β-peptide-associated free radical oxidative stress

Varadarajan, S., Yatin, S. M., Kański, J., Jahanshahi, F., & Butterfield, D. A. (1999) · Brain Research Bulletin · doi:10.1016/s0361-9230(99)00093-3 · Cited by 169 · see citing works

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 167 · see citing works

Peroxynitrite‐Induced Alterations in Synaptosomal Membrane Proteins

Koppal, T., Drake, J., Yatin, S. M., Jordan, B., Varadarajan, S., Bettenhausen, L., & Butterfield, D. A. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720310.x · Cited by 166 · see citing works

FDG-PET measurement is more accurate than neuropsychological assessments to predict global cognitive deterioration in patients with mild cognitive impairment

Chételat, G., Eustache, F., Viader, F., Sayette, V. D. L., Pèlerin, A., Mézenge, F., Hannequin, D., Dupuy, B., Baron, J., & Desgranges, B. (2005) · Neurocase · doi:10.1080/13554790490896938 · Cited by 164 · see citing works

Non-neuronal Enolase Is an Endothelial Hypoxic Stress Protein

Aaronson, R. M., Graven, K. K., Tucci, M., McDonald, R. J., & Farber, H. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27752 · Cited by 155 · see citing works

Neuropathological role of PI3K/Akt/mTOR axis in Down syndrome brain

Perluigi, M., Pupo, G., Tramutola, A., Cini, C., Coccia, R., Barone, E., Head, E., Butterfield, D. A., & Di Domenico, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.04.007 · Cited by 155 · see citing works

Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer’s amyloid β-peptide 1–42

Butterfield, D. A., & Kański, J. (2002) · Peptides · doi:10.1016/s0196-9781(02)00066-9 · Cited by 151 · see citing works

Elevated oxidative stress in models of normal brain aging and Alzheimer's disease

Butterfield, D. A., Howard, B. J., Yatin, S. M., Koppal, T., Drake, J., Hensley, K., Aksenov, M. Y., Aksenova, M. V., Subramaniam, R., Varadarajan, S., et al. (1999) · Life Sciences · doi:10.1016/s0024-3205(99)00442-7 · Cited by 148 · see citing works

Redox Homeostasis and Cellular Stress Response in Aging and Neurodegeneration

Calabrese, V., Cornelius, C., Mancuso, C., Lentile, R., Stella, A. M. G., & Butterfield, D. A. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-029-8_17 · Cited by 146 · see citing works

Coxsackievirus and adenovirus receptor (CAR) mediates atrioventricular-node function and connexin 45 localization in the murine heart

Lim, B.-K., Xiong, D., Dörner, A., Youn, T., Yung, A., Liu, T., Gu, Y., Dalton, N. D., Wright, A. T., Evans, S. Μ., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34777 · Cited by 146 · 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

Twenty years of Alzheimer’s disease‐causing mutations

Goate, A., & Hardy, J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07575.x · Cited by 137 · see citing works

Proteomic identification of nitrated brain proteins in early Alzheimer’s disease inferior parietal lobule

Reed, T. T., Pierce Jr., W. M., Turner, D. M., Markesbery, W. R., & Allan Butterfield, D. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00478.x · Cited by 135 · see citing works

Cognitive-enhancing and antioxidant activities of inhaled coriander volatile oil in amyloid β(1–42) rat model of Alzheimer's disease

Cioancă, O., Hriţcu, L., Mihăşan, M., & Hăncianu, M. (2013) · Physiology & Behavior · doi:10.1016/j.physbeh.2013.08.006 · Cited by 129 · see citing works

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 · see citing works

The Janus face of the heme oxygenase/biliverdin reductase system in Alzheimer disease: It's time for reconciliation

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 · see citing works

Redox Proteomics Identification of Oxidatively Modified Brain Proteins in Alzheimer's Disease and Mild Cognitive Impairment: Insights into the Progression of this Dementing Disorder

Butterfield, D. A., & Rukhsana Sultana, A. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12107 · Cited by 126 · see citing works

Elevation of 12/15 lipoxygenase products in AD and mild cognitive impairment

Yao, Y., Clark, C. M., Trojanowski, J. Q., Lee, V. M. ‐., & Praticò, D. (2005) · Annals of Neurology · doi:10.1002/ana.20558 · Cited by 126 · see citing works

Quantification of oxidized RNAs in Alzheimer's disease

Shan, X., & Lin, C.-L. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.03.022 · Cited by 125 · see citing works

Heme oxygenase-1 posttranslational modifications in the brain of subjects with Alzheimer disease and mild cognitive impairment

Barone, E., Domenico, F. D., Rukhsana Sultana, A., Coccia, R., Mancuso, C., Marzia Perluigi, A., & Butterfield, D. A. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.03.020 · Cited by 124 · see citing works

Remarkable increase in the concentration of 8-hydroxyguanosine in cerebrospinal fluid from patients with Alzheimer’s disease

Abe, T., Tohgi, H., Isobe, C., Murata, T., & Sato, C. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10349 · Cited by 124 · see citing works

Association between frontal cortex oxidative damage and beta-amyloid as a function of age in Down syndrome

Cenini, G., Dowling, A. L. S., Beckett, T. L., Barone, E., Mancuso, C., Murphy, M. P., LeVine, H., Lott, I. T., Schmitt, F. A., Butterfield, D. A., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.001 · Cited by 122 · see citing works

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 · see citing works

Alzheimer's Disease and the Amyloid β-Protein

Walsh, D. M., & Teplow, D. B. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00012-6 · Cited by 120 · see citing works

Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: An initial assessment

Butterfield, D. A., Gnjec, A., Poon, H. F., Castegna, A., Pierce, W. M. J., Klein, J. B., & Martins, R. N. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-10407 · Cited by 120 · see citing works

Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy

Lim, J., Balaštík, M., Lee, T. H., Nakamura, K., Liou, Y., Sun, A., Finn, G., Pastorino, L., Lee, V. M. ‐., & Lu, K. P. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34308 · Cited by 116 · see citing works

Protein Levels and Activity of Some Antioxidant Enzymes in Hippocampus of Subjects with Amnestic Mild Cognitive Impairment

Rukhsana Sultana, A., Piroddi, M., Galli, F., & Butterfield, D. A. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9593-0 · Cited by 115 · see citing works

Mutations in amyloid precursor protein and presenilin‐1 genes increase the basal oxidative stress in murine neuronal cells and lead to increased sensitivity to oxidative stress mediated by amyloid β‐peptide (1–42), H2O2 and kainic acid: implications for Alzheimer's disease

Abdul, H. M., Rukhsana Sultana, A., Keller, J. N., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03647.x · Cited by 114 · see citing works

The expression of key oxidative stress-handling genes in different brain regions in alzheimer’s disease

Aksenov, M., Tucker, H., Nair, P., Aksenova, M. V., Butterfield, D., Estus, S., & Markesbery, W. (1998) · Journal of Molecular Neuroscience · doi:10.1385/jmn:11:2:151 · Cited by 113 · see citing works

The 1999 SWISS-2DPAGE database update

Hoogland, C. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.286 · Cited by 111 · see citing works

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

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

Design, synthesis and biological evaluation of imine resveratrol derivatives as multi-targeted agents against Alzheimer's disease

Li, S., Wang, X., & Kong, L. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.10.068 · Cited by 110 · see citing works

B- Amyloid increases neuronal susceptibility to injufy by glucose deprivation

Copani, A., Koh, J., & Cotman, C. W. (1991) · Neuroreport · doi:10.1097/00001756-199112000-00008 · Cited by 109 · see citing works

SWISS‐2DPAGE, ten years later

Hoogland, C., Mostaguir, K., Sanchez, J., Hochstrasser, D. F., & Appel, R. D. (2004) · PROTEOMICS · doi:10.1002/pmic.200300830 · Cited by 105 · see citing works

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 · see citing works

Relationship between plaques, tangles, and loss of cortical cholinergic fibers in alzheimer disease

Geula, C., Mesulam, M. M., Saroff, D. M., & Wu, C.-K. (1998) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199801000-00008 · Cited by 102 · cited 1× · see citing works

Preclinical Evidence of Alzheimer Changes

Petrie, E. C., Cross, D. J., Galasko, D. R., Schellenberg, G. D., Raskind, M. A., Peskind, E. R., & Minoshima, S. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.59 · Cited by 101 · see citing works

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 · see citing works

ACE Inhibition with Captopril Retards the Development of Signs of Neurodegeneration in an Animal Model of Alzheimer’s Disease

AbdAlla, S., Langer, A., Fu, X., & Quitterer, U. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140816917 · Cited by 100 · see citing works

Oxidative and Nitrosative Modifications of Biliverdin Reductase-A in the Brain of Subjects with Alzheimer's Disease and Amnestic Mild Cognitive Impairment

Barone, E., Domenico, F. D., Cenini, G., Rukhsana Sultana, A., Coccia, R., Preziosi, P., Marzia Perluigi, A., Mancuso, C., & Butterfield, D. A. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110092 · Cited by 98 · see citing works

Segregation of a missense mutation in the amyloid β-protein precursor gene with familial Alzheimer's disease

Goate, A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s338 · Cited by 98 · see citing works

Neuronal Survival Factor from Bovine Brain Is Identical to Neuron‐Specific Enolase

Takei, N., Kondo, J., Nagaike, K., Ohsawa, K., Kato, K., & Kohsaka, S. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb08277.x · Cited by 98 · see citing works

Redox proteomics analysis of HNE-modified proteins in Down syndrome brain: clues for understanding the development of Alzheimer disease

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 · see citing works

Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Aβ(1-42): Implications for Alzheimer’s Disease

Boyd-Kimball, D., Poon, H. F., Lynn, B. C., Cai, J., Pierce Jr., W. M., Klein, J. B., Ferguson, J., Link, C. D., & Butterfield, D. A. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.07.001 · Cited by 98 · see citing works

Why Alzheimer's is a disease of memory: The attack on synapses by Aß oligomers (ADDLs)

Viola, K. L., Velasco, P. T., & Klein, W. L. (2008) · The journal of nutrition health & aging · doi:10.1007/bf02982587 · Cited by 96 · see citing works

Biliverdin reductase-A protein levels and activity in the brains of subjects with Alzheimer disease and mild cognitive impairment

Barone, E., Domenico, F. D., Cenini, G., Rukhsana Sultana, A., Cini, C., Preziosi, P., Marzia Perluigi, A., Mancuso, C., & Butterfield, D. A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.01.005 · Cited by 96 · 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

Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat brain

Hattori, T., Takei, N., Mizuno, Y., Kato, K., & Kohsaka, S. (1995) · Neuroscience Research · doi:10.1016/0168-0102(94)00849-b · Cited by 94 · see citing works

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 · see citing works

Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer’s amyloid β-peptide (1–42)

Kański, J., Aksenova, M. V., Schöneich, C., & Butterfield, D. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00821-3 · Cited by 93 · see citing works

Vitamin E in aging, dementia, and Alzheimer's disease

Joshi, Y. B., & Praticò, D. (2012) · BioFactors · doi:10.1002/biof.195 · Cited by 92 · see citing works

Pin1: A New Genetic Link between Alzheimers Disease, Cancer and Aging

Driver, J. A., & Lu, K. P. (2010) · Current Aging Science · doi:10.2174/1874609811003030158 · Cited by 92 · see citing works

Pin1 in Alzheimer's disease: Multiple substrates, one regulatory mechanism?

Balaštík, M., Lim, J., Pastorino, L., & Lu, K. P. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.01.006 · Cited by 90 · see citing works

A Disease State Fingerprint for Evaluation of Alzheimer's Disease

Mattila, J., Initiative, A. F. T. A. D. N., Koikkalainen, J. R., Virkki, A., Simonsen, A. H., van Gils, M., Waldemar, G., Soininen, H. S., & Lötjönen, J. M. P. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110365 · Cited by 89 · see citing works

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 · see citing works

Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: a regional study

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

Prolyl Isomerase Pin1 Promotes Amyloid Precursor Protein (APP) Turnover by Inhibiting Glycogen Synthase Kinase-3β (GSK3β) Activity

Ma, S. L., Pastorino, L., Zhou, X. Z., & Lu, K. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.298596 · Cited by 85 · see citing works

Biochemical Characterization of Aβ and Tau Pathologies in Mild Cognitive Impairment and Alzheimer's Disease

Tremblay, C., Pilote, M., Phivilay, A., Émond, V., Bennett, D. A., & Calon, F. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12411 · Cited by 78 · see citing works

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 · see citing works

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 · see citing works

Evaluation of Selenium, Redox Status and Their Association with Plasma Amyloid/Tau in Alzheimer’s Disease

Krishnan, S., & Rani, P. U. (2014) · Biological Trace Element Research · doi:10.1007/s12011-014-9930-x · 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

Molecular Implication of PP2A and Pin1 in the Alzheimer's Disease Specific Hyperphosphorylation of Tau

Landrieu, I., Smet‐Nocca, C., Amniai, L., Louis, J. V., Wieruszeski, J., Goris, J., Janssens, V., & Lippens, G. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021521 · Cited by 68 · see citing works

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 · see citing works

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 · see citing works

Differential expression and redox proteomics analyses of an Alzheimer disease transgenic mouse model: effects of the amyloid-β peptide of amyloid precursor proteinΞ

Robinson, R. A. S., Lange, M. L. B., Rukhsana Sultana, A., Galván, V., Fombonne, J., Gorostiza, O. F., Zhang, J., Warrier, G., Cai, J., Pierce, W. M. J., et al. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.01.005 · Cited by 61 · see citing works

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 · see citing works

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 · see citing works

Regional correlation of PET and CT in senile dementia of the Alzheimer type.

de Leon, M. J., GEORGE, A. E., Ferris, S. H., Rosenbloom, S., Christman, D. R., Gentes, C., Reisberg, ‌., Kricheff, I. I., & Wolf, A. P. (1983) · PubMed Central · Cited by 58 · see citing works

Cell Cycle Proteins in Brain in Mild Cognitive Impairment: Insights into Progression to Alzheimer Disease

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 · see citing works

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 54 · see citing works

Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein

Park, S. A., Shaked, G. M., Bredesen, D. E., & Koo, E. H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.042 · Cited by 53 · see citing works

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 · see citing works

Early‐onset Alzheimer's disease: An analysis of CT findings

Drayer, B. P., Heyman, A., Wilkinson, W. E., et al. (1985) · Annals of Neurology · doi:10.1002/ana.410170420 · Cited by 41 · see citing works

The N‐terminal copper‐binding domain of the amyloid precursor protein protects against Cu 2+ neurotoxicity in vivo

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 · see citing works

Fronto-temporal-lobe atrophy in early-stage Alzheimer's disease identified using an improved detection methodology

Farrow, T. F. D., Thiyagesh, S. N., Wilkinson, I. D., Parks, R. W., Ingram, L., & Woodruff, P. W. R. (2007) · Psychiatry Research Neuroimaging · doi:10.1016/j.pscychresns.2006.12.013 · Cited by 38 · see citing works

Plasma antioxidants and brain glucose metabolism in elderly subjects with cognitive complaints

Picco, A., Polidori, M. C., Ferrara, M., Cecchetti, R., Arnaldi, D., Baglioni, M., Morbelli, S. D., Bastiani, P., Bossert, I., Fiorucci, G., et al. (2013) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-013-2638-x · Cited by 33 · see citing works

Rat hippocampal responses up to 90 days after a single nanoceria dose extends a hierarchical oxidative stress model for nanoparticle toxicity

Hardas, S. S., Rukhsana Sultana, A., Warrier, G., Dan, M., Wu, P., Grulke, E. A., Tseng, M. T., Unrine, J. M., Graham, U. M., Yokel, R. A., et al. (2013) · Nanotoxicology · doi:10.3109/17435390.2013.868059 · Cited by 32 · see citing works

The identification of protein biomarkers for oxidative stress in Down syndrome

Marzia Perluigi, A., & Butterfield, D. A. (2011) · Expert Review of Proteomics · doi:10.1586/epr.11.36 · Cited by 29 · see citing works

Fluorinated benzophenone derivatives: Balanced multipotent agents for Alzheimer's disease

Belluti, F., Simone, A. D., Tarozzi, A., Bartolini, M., Djemil, A., Bisi, A., Gobbi, S., Montanari, S., Cavalli, A., Andrisano, V., et al. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.03.042 · Cited by 27 · see citing works

Canaries in a Coal Mine

Small, B. J., Fratiglioni, L., & Bäckman, L. (2001) · Archives of General Psychiatry · doi:10.1001/archpsyc.58.9.859 · Cited by 23 · see citing works

Do Proteomics Analyses Provide Insights into Reduced Oxidative Stress in the Brain of an Alzheimer Disease Transgenic Mouse Model with an M631L Amyloid Precursor Protein Substitution and Thereby the Importance of Amyloid-Beta-Resident Methionine 35 in Alzheimer Disease Pathogenesis?

Rukhsana Sultana, A., Robinson, R. A. S., Lange, M. L. B., Fiorini, A., Galván, V., Fombonne, J., Baker, A. S., Gorostiza, O. F., Zhang, J., Cai, J., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4470 · Cited by 22 · see citing works

Attenuated cytotoxicity but enhanced βfibril of a mutant amyloid β‐peptide with a methionine to cysteine substitution

Dai, X., Sun, Y., & Jiang, Z.-F. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.02.038 · Cited by 13 · see citing works

Targeting amyloid precursor protein secretases: Alzheimer's disease and beyond

Ganjei, J. K. (2010) · Drug News & Perspectives · doi:10.1358/dnp.2010.23.9.1507297 · Cited by 12 · see citing works

Untitled work

Kordower (1999) · doi:10.1002/1531-8249(199909)46:3

Inflammation as a central mechanism in Alzheimer's disease

Kinney, J. W., Bemiller, S. M., Murtishaw, A. S., Leisgang, A. M., Salazar, A. M., & Lamb, B. T. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.014 · Cited by 2,253 · see citing works

Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies.

Zhang, J., Zhang, Y., Wang, J., Xia, Y., Zhang, J., & Chen, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01911-3 · Cited by 1,138 · see citing works

Oxidative stress, protein modification and Alzheimer disease

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

Ceramides in Alzheimer’s Disease: Key Mediators of Neuronal Apoptosis Induced by Oxidative Stress and A <b> <i>β</i> </b> Accumulation

Jazvinšćak Jembrek, M., Hof, P. R., & Šimić, G. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/346783 · Cited by 244 · see citing works

Axonal Degeneration during Aging and Its Functional Role in Neurodegenerative Disorders

Salvadores, N., Sanhueza, M., Manque, P., & Court, F. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00451 · Cited by 182 · see citing works

Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery

Buccellato, F. R., D’Anca, M., Fenoglio, C., Scarpini, E., & Galimberti, D. (2021) · Antioxidants · doi:10.3390/antiox10091353 · Cited by 179 · see citing works

Neuropathological role of PI3K/Akt/mTOR axis in Down syndrome brain

Perluigi, M., Pupo, G., Tramutola, A., Cini, C., Coccia, R., Barone, E., Head, E., Butterfield, D. A., & Di Domenico, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.04.007 · Cited by 155 · see citing works

The Janus face of the heme oxygenase/biliverdin reductase system in Alzheimer disease: It's time for reconciliation

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 · 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

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

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

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 · see citing works

Minocycline reduces inflammatory parameters in the brain structures and serum and reverses memory impairment caused by the administration of amyloid β (1-42) in mice

Garcez, M. L., Mina, F., Bellettini-Santos, T., Carneiro, F. G., Luz, A. P., Schiavo, G. L., Andrighetti, M. S., Scheid, M. G., Bolfe, R. P., & Budni, J. (2017) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.03.010 · Cited by 102 · see citing works

The PERK-Dependent Molecular Mechanisms as a Novel Therapeutic Target for Neurodegenerative Diseases

Rozpędek-Kamińska, W., Siwecka, N., Wawrzynkiewicz, A., Wojtczak, R., Pytel, D., Diehl, J. A., & Majsterek, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062108 · Cited by 84 · see citing works

Redox changes and cellular senescence in Alzheimer's disease

Yu, N., Pasha, M., & Chua, J. J. E. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103048 · Cited by 80 · see citing works

BACE1 molecular docking and anti-Alzheimer’s disease activities of ginsenosides

Choi, R. J., Roy, A., Jung, H. J., Ali, M. Y., Min, B.-S., Park, C. H., Yokozawa, T., Fan, T.-P., Choi, J. S., & Jung, H. A. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.06.013 · 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

Oxidative challenge in Alzheimer's disease: state of knowledge and future needs

Cervellati, C., Wood, P. L., Romani, A., Valacchi, G., Squerzanti, M., Sanz, J. M., Ortolani, B., & Zuliani, G. (2016) · Journal of Investigative Medicine · doi:10.1136/jim-2015-000017 · Cited by 75 · see citing works

The Protective Effect of Exercise in Neurodegenerative Diseases: The Potential Role of Extracellular Vesicles

Fuller, O. K., Whitham, M., Mathivanan, S., & Febbraio, M. A. (2020) · Cells · doi:10.3390/cells9102182 · Cited by 60 · see citing works

Morroniside prevents H2O2 or Aβ1–42-induced apoptosis via attenuating JNK and p38 MAPK phosphorylation

Chen, K., Lu, Y., Liu, C., Zhang, L., Fang, Z., & Yu, G. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.07.047 · Cited by 57 · see citing works

Intranasal administration of dauricine loaded on graphene oxide: Multi-target therapy for Alzheimer’s disease

Wang, K., Wang, L., Chen, L., Peng, C., Luo, B., Mo, J., & Chen, W. (2021) · Drug Delivery · doi:10.1080/10717544.2021.1895909 · Cited by 55 · 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

Characterisation of premature cell senescence in Alzheimer's disease using single nuclear transcriptomics

Fancy, N. N., Smith, A. M., Caramello, A., Tsartsalis, S., Davey, K., Muirhead, R. C. J., McGarry, A., Jenkyns, M. H., Schneegans, E., Chau, V., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02727-9 · Cited by 48 · see citing works

Spirulina maxima extract prevents cell death through BDNF activation against amyloid beta 1-42 (Aβ 1-42 ) induced neurotoxicity in PC12 cells

Koh, E.-J., Kim, K.-J., Choi, J., Kang, D.-H., & Lee, B.-Y. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.02.057 · Cited by 43 · see citing works

Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4

Argyri, L., Dafnis, I., Theodossiou, T. A., Gantz, D., Stratikos, E., & Chroni, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.538124 · Cited by 30 · see citing works

“Boomerang Neuropathology” of Late-Onset Alzheimer’s Disease is Shrouded in Harmful “BDDS”: Breathing, Diet, Drinking, and Sleep During Aging

Daulatzai, M. A. (2015) · Neurotoxicity Research · doi:10.1007/s12640-015-9528-x · Cited by 12 · see citing works

Inflammatory Pathways

Griffin, W. S. T., Sheng, J. G., & Mrak, R. E. (1997) · Humana Press eBooks · doi:10.1007/978-1-59259-471-9_10 · Cited by 4 · see citing works

Alzheimer's disease: Mismatch between amyloid plaques and neuritic plaques

Braak, H., Braak, E., Ohm, T. G., & Böhl, J. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90479-5 · Cited by 90 · see citing works

The role of APP and BACE1 trafficking in APP processing and amyloid-β generation

Zhang, X., & Song, W. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt211 · Cited by 216 · see citing works

[Alzheimer's disease: cellular and molecular aspects].

Octave, J., & Pierrot, N. (2008) · PubMed · Cited by 8 · see citing works

Laboratory diagnostic tests for Alzheimer's disease.

Iqbal, K., Wang, G. P., Grundke, I., et al. (1989) · PubMed · Cited by 5 · see citing works