Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability

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

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

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975

Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions

Saudou, F., Finkbeiner, S. M., Devys, D., & Greenberg, M. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81782-1 · Cited by 1,598

Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530

A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513

Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417

Aβ Oligomers – a decade of discovery

Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938

P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders

Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,316

Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy

Bu, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2620 · Cited by 1,168

Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦

Demuro, A., Mina, E. W., Kayed, R., Milton, S. C. F., Parker, I., & Glabe, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500997200 · Cited by 1,057

In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis

Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

Hamley, I. W. (2012) · Chemical Reviews · doi:10.1021/cr3000994 · Cited by 892

LRP/Amyloid β-Peptide Interaction Mediates Differential Brain Efflux of Aβ Isoforms

Deane, R., Wu, Z., Sagare, A., Davis, J., Du Yan, S., Hamm, K., Xu, F., Parisi, M., LaRue, B., Hu, H. W., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.017 · Cited by 828

Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641

Peptide Fibrillization

Hamley, I. W. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200700861 · Cited by 624

Insulin, insulin-degrading enzyme and amyloid-β peptide in Alzheimer's disease: review and hypothesis

Qiu, W. Q., & Folstein, M. F. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.01.004 · Cited by 557

Self-Assembly of Aβ 1 - 42 into Globular Neurotoxins

Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., Jones, B. W., Fernandez, S. J., Lacor, P. N., Horowitz, P., et al. (2003) · Biochemistry · doi:10.1021/bi030029q · Cited by 522

Alzheimer's disease: synaptic dysfunction and Aβ

Shankar, G. M., & Walsh, D. M. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-48 · Cited by 486

Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide

Cerf, E., Sarroukh, R., Tamamizu‐Kato, S., Breydo, L., Derclaye, S., Dufrêne, Y. F., Narayanaswami, V., Goormaghtigh, E., Ruysschaert, J., & Raussens, V. (2009) · Biochemical Journal · doi:10.1042/bj20090379 · Cited by 511

Different Conformations of Amyloid β Induce Neurotoxicity by Distinct Mechanisms in Human Cortical Neurons

Deshpande, A. M., Mina, E. W., Glabe, C. G., & Busciglio, J. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1189-06.2006 · Cited by 508

Small assemblies of unmodified amyloid $beta;-protein are the proximate neurotoxin in Alzheimer?s disease

Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 494

Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation)

Kozłowski, H., Janicka-Kłos, A., Brasuń, J., Gaggelli, E., Valensin, D., & Valensin, G. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.05.011 · Cited by 481

Antiamyloidogenic and Neuroprotective Functions of Cathepsin B: Implications for Alzheimer's Disease

Mueller-Steiner, S., Zhou, Y., Arai, H., Roberson, E. D., Sun, B., Chen, J., Wang, X., Yu, G.-Q., Esposito, L., Mucke, L., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.027 · Cited by 482

CD22 blockade restores homeostatic microglial phagocytosis in ageing brains

Pluvinage, J. V., Haney, M. S., Smith, B. A. H., Sun, J., Iram, T., Bonanno, L., Li, L., Lee, D. P., Morgens, D. W., Yang, A. C., et al. (2019) · Nature · doi:10.1038/s41586-019-1088-4 · Cited by 459

ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins

Sarroukh, R., Goormaghtigh, E., Ruysschaert, J., & Raussens, V. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.04.012 · Cited by 449

Role of toll-like receptor signalling in A uptake and clearance

Tahara, K., Kim, H.-D., Jin, J.-J., Maxwell, J. A., Li, L., & Fukuchi, K.-I. (2006) · Brain · doi:10.1093/brain/awl249 · Cited by 493

TLR2 Is a Primary Receptor for Alzheimer’s Amyloid β Peptide To Trigger Neuroinflammatory Activation

Liu, S., Liu, Y., Hao, W., Wolf, L., Kiliaan, A. J., Penke, B., Rübe, C. E., Walter, J., Heneka, M. T., Hartmann, T., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1101121 · Cited by 439

Block of Long-Term Potentiation by Naturally Secreted and Synthetic Amyloid β-Peptide in Hippocampal Slices Is Mediated via Activation of the Kinases c-Jun N-Terminal Kinase, Cyclin-Dependent Kinase 5, and p38 Mitogen-Activated Protein Kinase as well as Metabotropic Glutamate Receptor Type 5

Wang, Q., Walsh, D. M., Rowan, M. J., Selkoe, D. J., & Anwyl, R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1633-03.2004 · Cited by 437

Accelerating Amyloid-β Fibrillization Reduces Oligomer Levels and Functional Deficits in Alzheimer Disease Mouse Models

Cheng, I. H.-J., Scearce-Levie, K. A., Legleiter, J. A., Palop, J. J., Gerstein, H., Bien‐Ly, N., Puolivaöli, J., Lesné, S., Ashe, K. H., Muchowski, P. J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701078200 · Cited by 418

Preparing Synthetic Aβ in Different Aggregation States

Stine, W. B., Jungbauer, L., Yu, C., & LaDu, M. J. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-744-0_2 · Cited by 403

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

Lashuel, H. A., & Lansbury, P. T. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004422 · Cited by 407

Heat Shock Proteins 70 and 90 Inhibit Early Stages of Amyloid β-(1–42) Aggregation in Vitro

Evans, C. G., Wisén, S., & Gestwicki, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606192200 · Cited by 396

Metals and amyloid‐β in Alzheimer's disease

Maynard, C. J., Bush, A. I., Masters, C. L., Cappai, R., & Li, Q. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00434.x · Cited by 356

Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s disease

Crowther, D. C., Kinghorn, K. J., Miranda, E., Page, R., Curry, J. A., Duthie, F., Gubb, D., & Lomas, D. A. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.12.025 · Cited by 369

LPS receptor (CD14): a receptor for phagocytosis of Alzheimer's amyloid peptide

Liu, Y., Walter, S., Stagi, M., Cherny, D., Letièmbre, M., Schulz‐Schaeffer, W., Heine, H., Penke, B., Neumann, H., & Fassbender, K. C. (2005) · Brain · doi:10.1093/brain/awh531 · Cited by 349

Elevation of glutathione as a therapeutic strategy in Alzheimer disease

Pocernich, C. B., & Butterfield, D. A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.003 · Cited by 351

Amyloid-β Aggregation

Finder, V. H., & Glockshuber, R. (2007) · Neurodegenerative Diseases · doi:10.1159/000100355 · Cited by 367

Targeting amyloid-β in glaucoma treatment

Guo, L., Salt, T. E., Luong, V., Wood, N. W., Cheung, W., Maaß, A., Ferrari, G., Russo‐Marie, F., Sillito, A. M., Cheetham, M. E., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703707104 · Cited by 346

Amyloid β-Protein: Monomer Structure and Early Aggregation States of Aβ42 and Its Pro 19 Alloform

Bernstein, S. L., Wyttenbach, T., Baumketner, A., Shea, J., Bitan, G., Teplow, D. B., & Bowers, M. T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044531p · Cited by 349

Transthyretin Aggregation under Partially Denaturing Conditions Is a Downhill Polymerization

Hurshman, A. R., White, J. T., Powers, E. T., & Kelly, J. W. (2004) · Biochemistry · doi:10.1021/bi049621l · Cited by 340

Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction

Tomic, J. L., Pensalfini, A., Head, E., & Glabe, C. G. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.024 · Cited by 336

Medicinal Inorganic Chemistry Approaches to Passivation and Removal of Aberrant Metal Ions in Disease

Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332

Copper-Dependent Inhibition of Human Cytochrome c Oxidase by a Dimeric Conformer of Amyloid-β1-42

Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327

The role of amyloid β peptide 42 in Alzheimer's disease

Findeis, M. A. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.06.006 · Cited by 338

The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures

Yerbury, J. J., Poon, S., Meehan, S., Thompson, B. C., Kumita, J. R., Dobson, C. M., & Wilson, M. R. (2007) · The FASEB Journal · doi:10.1096/fj.06-7986com · Cited by 330

Negatively Charged Gold Nanoparticles Inhibit Alzheimer's Amyloid‐β Fibrillization, Induce Fibril Dissociation, and Mitigate Neurotoxicity

Liao, Y., Chang, Y., Yoshiike, Y., Chang, Y. C., & Chen, Y. (2012) · Small · doi:10.1002/smll.201201068 · Cited by 324

Sensitive ELISA detection of amyloid‐β protofibrils in biological samples

Englund, H., Sehlin, D., Johansson, A., Nilsson, L. N. G., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04759.x · Cited by 292

Amyloid‐beta oligomerization in Alzheimer dementia versus high‐pathology controls

Esparza, T. J., Zhao, H., Cirrito, J. R., Cairns, N. J., Bateman, R. J., Holtzman, D. M., & Brody, D. L. (2012) · Annals of Neurology · doi:10.1002/ana.23748 · Cited by 319

Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia

Sondag, C. M., Dhawan, G., & Combs, C. K. (2009) · Journal of Neuroinflammation · doi:10.1186/1742-2094-6-1 · Cited by 295

The Ratio of Monomeric to Aggregated Forms of Aβ40 and Aβ42 Is an Important Determinant of Amyloid-β Aggregation, Fibrillogenesis, and Toxicity

Jan, A., Gokce, O., Luthi-Carter, R., & Lashuel, H. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803159200 · Cited by 291

Microglial phagocytosis induced by fibrillar β-amyloid is attenuated by oligomeric β-amyloid: implications for Alzheimer’s disease

Pan, X.-D., Zhu, Y.-G., Lin, N., Zhang, J., Ye, Q.-Y., Huang, H.-P., & Chen, X.-C. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-45 · Cited by 292

Nanotechnologies for Alzheimer's disease: diagnosis, therapy, and safety issues

Brambilla, D., Droumaguet, B. L., Nicolas, J., Hashemi, S. H., Wu, L., Moghimi, S. M., Couvreur, P., & Andrieux, K. (2011) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2011.03.008 · Cited by 302

Elucidation of Primary Structure Elements Controlling Early Amyloid β-Protein Oligomerization

Bitan, G., Vollers, S. S., & Teplow, D. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300825200 · Cited by 291

Overview on the Effects of N-Acetylcysteine in Neurodegenerative Diseases

Tardiolo, G., Bramanti, P., & Mazzon, E. (2018) · Molecules · doi:10.3390/molecules23123305 · Cited by 299

Amyloid beta peptide and NMDA induce ROS from NADPH oxidase and AA release from cytosolic phospholipase A 2 in cortical neurons

Shelat, P. B., Chalimoniuk, M., Wang, J., Strosznajder, J. B., Lee, J. C., Sun, A. Y., Simonyi, Á., & Sun, G. Y. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05347.x · Cited by 288

Amyloid-β Protein Oligomer at Low Nanomolar Concentrations Activates Microglia and Induces Microglial Neurotoxicity

Maezawa, I., Zimin, P. I., Wulff, H., & Jin, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135244 · Cited by 293

Amyloid-β Aggregates Cause Alterations of Astrocytic Metabolic Phenotype: Impact on Neuronal Viability

Allaman, I., Gavillet, M., Bélanger, M., Laroche, T., Viertl, D., Lashuel, H. A., & Magistretti, P. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5098-09.2010 · Cited by 291

Amyloid β-protein oligomers and Alzheimer’s disease

Hayden, E. Y., & Teplow, D. B. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt226 · Cited by 276

A 1-42-RAGE Interaction Disrupts Tight Junctions of the Blood-Brain Barrier Via Ca2+-Calcineurin Signaling

Kook, S.-H., Hong, H. S., Moon, M., Ha, C. M., Chang, S., & Mook‐Jung, I. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6102-11.2012 · Cited by 279

Aβ-degrading enzymes: potential for treatment of Alzheimer disease

Miners, J. S., Barua, N., Kehoe, P. G., Gill, S., & Love, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182345e46 · Cited by 265

High‐molecular‐weight β‐amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients

Fukumoto, H., Tokuda, T., Kasai, T., Ishigami, N., Hidaka, H., Kondo, M., Allsop, D., & Nakagawa, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-150359 · Cited by 264

Amyloid β‐peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease

Verdier, Y., Zarándi, M., & Penke, B. (2004) · Journal of Peptide Science · doi:10.1002/psc.573 · Cited by 267

Intracellular Aβ and cognitive deficits precede β-amyloid deposition in transgenic arcAβ mice

Knobloch, M., Konietzko, U., Krebs, D. C., & Nitsch, R. M. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.019 · Cited by 259

APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease

Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 268

Nuclear factor erythroid 2-related factor 2 protects against beta amyloid

Kanninen, K. M., Malm, T., Jyrkkänen, H.-K., Goldsteins, G., Keksa-Goldsteine, V., Tanila, H., Yamamoto, M. P., Ylä‐Herttuala, S., Levonen, A., & Koıstınaho, J. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.07.010 · Cited by 259

On the Seeding and Oligomerization of pGlu-Amyloid Peptides (in vitro)

Schilling, S., Lauber, T., Schaupp, M., Manhart, S., Scheel, E., Böhm, G., & Demuth, H.-U. (2006) · Biochemistry · doi:10.1021/bi0612667 · Cited by 254

Amyloid β‐protein monomer structure: A computational and experimental study

Baumketner, A., Bernstein, S. L., Wyttenbach, T., Bitan, G., Teplow, D. B., Bowers, M. T., & Shea, J. (2006) · Protein Science · doi:10.1110/ps.051762406 · Cited by 247

Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences

Yang, M., & Teplow, D. B. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.039 · Cited by 255

Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease

Crouch, P. J., Harding, S.-M. E., White, A. R., Camakaris, J., Bush, A. I., & Masters, C. L. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.07.013 · Cited by 254

Neurogenic Effect of -Amyloid Peptide in the Development of Neural Stem Cells

Lopez-Toledano, M. A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0974-04.2004 · Cited by 241

Reversal of long-term dendritic spine alterations in Alzheimer disease models

Smith, D. L., Pozueta, J., Gong, B., Arancio, O., & Shelanski, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908706106 · Cited by 229

β-Amyloid1–42Induces Neuronal Death through the p75 Neurotrophin Receptor

Sotthibundhu, A., Sykes, A. M., Fox, B., Underwood, C. K., Thangnipon, W., & Coulson, E. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0350-08.2008 · Cited by 238

Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study

Urbanc, B., Betnel, M., Cruz, L., Bitan, G., & Teplow, D. B. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9096303 · Cited by 234

The relationship between stress and Alzheimer's disease

Justice, N. J. (2018) · Neurobiology of Stress · doi:10.1016/j.ynstr.2018.04.002 · Cited by 237

Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus

Ashraf, G., Greig, N., Khan, T., Hassan, I., Tabrez, S., Shakil, S., Sheikh, I., Zaidi, S., Akram, M., Jabir, N., et al. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140917095514 · Cited by 236

Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death

Resende, R., Ferreiro, E., Pereira, C., & Resende de Oliveira, C. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.06.036 · Cited by 235

Importance of MAPK pathways for microglial pro-inflammatory cytokine IL-1β production

Kim, S. H., Smith, C. J., & Eldik, L. J. V. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00126-x · Cited by 241

Cholesterol metabolism and transport in the pathogenesis of Alzheimer’s disease

Martins, I. J., Berger, T. R., Sharman, M. J., Verdile, G., Fuller, S. J., & Martins, R. N. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06408.x · Cited by 237

Metal Ions Differentially Influence the Aggregation and Deposition of Alzheimer's β-Amyloid on a Solid Template

Ha, C., Ryu, J., & Park, C. B. (2007) · Biochemistry · doi:10.1021/bi7000032 · Cited by 231

High-resolution Atomic Force Microscopy of Soluble Aβ42 Oligomers

Mastrangelo, I. A., Ahmed, M., Sato, T., Liu, W., Wang, C., Hough, P. V. C., & Smith, S. O. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.042 · Cited by 236

Curcumin-decorated nanoliposomes with very high affinity for amyloid-β1-42 peptide

Mourtas, S., Canovi, M., Zona, C., Aurilia, D., Niarakis, A., Ferla, B. L., Salmona, M., Nicotra, F., Gobbi, M., & Antimisiaris, S. G. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.10.027 · Cited by 234

Human neprilysin is capable of degrading amyloid β peptide not only in the monomeric form but also the pathological oligomeric form

Kanemitsu, H., Tomiyama, T., & Mori, H. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00898-x · Cited by 228

Disruption of fast axonal transport is a pathogenic mechanism for intraneuronal amyloid beta

Pigino, G. F., Morfini, G. A., Atagi, Y., Deshpande, A., Yu, C., Jungbauer, L. M., LaDu, M. J., Busciglio, J. A., & Brady, S. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901229106 · Cited by 233

Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer’s disease

Ling, Y., Morgan, K., & Kalsheker, N. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00133-x · Cited by 224

Differential effects of oligomeric and fibrillar amyloid-β1–42 on astrocyte-mediated inflammation

White, J. A., Manelli, A. M., Holmberg, K. H., Eldik, L. J. V., & LaDu, M. J. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.12.013 · Cited by 223

Neurotoxic protein oligomers — what you see is not always what you get

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Wang, S., Wang, Y., Su, Y., Zhou, W., Yang, S., Zhang, R., Zhao, M., Li, Y., Zhang, Z., Zhan, D., et al. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.03.003 · Cited by 221

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Sanz‐Blasco, S., Valero, R. A., Rodríguez‐Crespo, I., Villalobos, C., & Núñez, L. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002718 · Cited by 221

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Noy, D., Solomonov, I., Sinkevich, O., Arad, T., Kjær, K., & Sagi, I. (2008) · Journal of the American Chemical Society · doi:10.1021/ja076282l · Cited by 216

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Matsuzaki, K. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.009 · Cited by 220

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Chou, I.-H., Benford, M. E., Beier, H. T., Coté, G. L., Wang, M., Jing, N., Kameoka, J., & Good, T. A. (2008) · Nano Letters · doi:10.1021/nl0808132 · Cited by 213

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Malaplate, C., Florent‐Béchard, S., Youssef, I., Koziel, V., Sponne, I., Kriem, B., Leininger‐Muller, B., Olivier, J. L., Oster, T., & Pillot, T. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.02.010 · Cited by 224

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Gobbi, M., Re, F., Canovi, M., Beeg, M., Gregori, M., Sesana, S., Sonnino, S., Brogioli, D., Musicanti, C., Gasco, P., et al. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.04.044 · Cited by 192

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Bode, D. C., Baker, M. D., & Viles, J. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762526 · Cited by 210

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Lim, C. Z. J., Zhang, Y., Chen, Y., Zhao, H., Stephenson, M. C., Ho, N. R. Y., Chen, Y., Chung, J., Reilhac, A., Loh, T. P., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09030-2 · Cited by 209

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Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202

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Salvadores, N., Shahnawaz, M., Scarpini, E. A., Tagliavini, F., & Soto, C. A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.031 · Cited by 205

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Bitan, G., & Teplow, D. B. (2004) · Accounts of Chemical Research · doi:10.1021/ar000214l · Cited by 196

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Wogulis, M., Wright, S., Cunningham, D., Chilcote, T., Powell, K., & Rydel, R. E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2381-04.2005 · Cited by 233

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Arunagiri, A., Singh, P. K., Jacob, R. S., & Maji, S. K. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/606802 · Cited by 215

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Urbanc, B., Cruz, L., Ding, F., Sammond, D. W., Khare, S. D., Buldyrev, S. V., Stanley, E., & Dokholyan, N. V. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.040980 · Cited by 194

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White, M. R., Kandel, R., Tripathi, S., Condon, D., Qi, L., Taubenberger, J., & Hartshorn, K. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101364 · Cited by 193

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Piccini, A., Russo, C., Gliozzi, A., Relini, A., Vitali, A., Borghi, R., Giliberto, L., Armirotti, A., D’Arrigo, C., Bachi, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501694200 · Cited by 192

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Habtemariam, S. (2016) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2016/2680409 · Cited by 195

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Lee, J., Friedman, J. E., Angel, I., Kozak, A., & Koh, J. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.01.005 · Cited by 190

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Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015

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Ferrera, D., Canale, C., Benfenati, F., & Gasparini, L. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.04.173

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Deshpande, A. M., Mina, E. W., Glabe, C. G., & Busciglio, J. A. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1752

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Ward, R. V., JENNINGS, K. H., Jepras, R., Neville, W. A., OWEN, D. E., HAWKINS, J., Christie, G., Davis, J. B., George, A. R., Karran, E. H., et al. (2000) · Biochemical Journal · doi:10.1042/bj3480137 · Cited by 153