Amyloid β-Protein Fibrillogenesis

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429

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

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Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

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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

Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill

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Candidate gene for the chromosome 1 familial Alzheimer’s disease locus

Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.

Pan, K. M., Baldwin, M. A., Nguyen, J. T., Gasset, M., Serban, A. V., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10962 · Cited by 2,281

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

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

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,780

Protein Misfolding, Functional Amyloid, and Human Disease

Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

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

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434

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

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

Stefani, M., & Dobson, C. M. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0464-5 · Cited by 1,670

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

APP Processing and Synaptic Function

Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644

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

Unfolding the role of protein misfolding in neurodegenerative diseases

Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506

Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,462

Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease

Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431

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

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209

Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease

Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Lu, J., Qiang, W., Yau, W., Schwieters, C. D., Meredith, S. C., & Tycko, R. (2013) · Cell · doi:10.1016/j.cell.2013.08.035 · Cited by 1,105

Amyloid fibrillogenesis: themes and variations

Rochet, J., & Lansbury, P. T. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00049-4 · Cited by 1,095

Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior

Selkoe, D. J. (2008) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.02.016 · Cited by 1,038

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

Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?

Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989

Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., & Selkoe, D. J. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 817

Amyloid β-peptide (1-42)-induced Oxidative Stress and Neurotoxicity: Implications for Neurodegeneration in Alzheimer's Disease Brain. A Review

Allan Butterfield, D. (2002) · Free Radical Research · doi:10.1080/1071576021000049890 · Cited by 786

Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

Conway, K. A., Harper, J. D., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi991447r · Cited by 786

Structure–neurotoxicity relationships of amyloid β-protein oligomers

Ono, K., Condron, M. M., & Teplow, D. B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905127106 · Cited by 782

Protein aggregation diseases: pathogenicity and therapeutic perspectives

Aguzzi, A., & O’Connor, T. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3050 · Cited by 766

Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory

Turner, P. R., O’Connor, K., Tate, W. P., & Abraham, W. C. (2003) · Progress in Neurobiology · doi:10.1016/s0301-0082(03)00089-3 · Cited by 796

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

Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. Cohen

Kirkitadze, M. D., Condron, M. M., & Teplow, D. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4970 · Cited by 690

Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer’s disease

Lipinski, M. M., Zheng, B., Lu, T., Yan, Z., Py, B. F., Ng, A., Xavier, R. J., Li, C., Yankner, B. A., Scherzer, C. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009485107 · Cited by 680

Small Molecule Inhibitors of Aggregation Indicate That Amyloid β Oligomerization and Fibrillization Pathways Are Independent and Distinct

Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680

Amyloid β-Protein Assembly and Alzheimer Disease

Roychaudhuri, R., Yang, M., Hoshi, M. M., & Teplow, D. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800036200 · Cited by 630

What is the role of protein aggregation in neurodegeneration?

Ross, C. A., & Poirier, M. A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1742 · Cited by 623

Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies

Kirkitadze, M. D., Bitan, G., & Teplow, D. B. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10328 · Cited by 589

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

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

Protein Aggregation in the Brain: The Molecular Basis for Alzheimer’s and Parkinson’s Diseases

Irvine, G. B., El‐Agnaf, O. M. A., Shankar, G. M., & Walsh, D. M. (2008) · Molecular Medicine · doi:10.2119/2007-00100.irvine · Cited by 567

Inhibition of Amyloid β Protein Fibrillation by Polymeric Nanoparticles

Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Lindman, S., Minogue, A. M., Thulin, E., Walsh, D. M., Dawson, K. A., & Linse, S. S. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8041806 · Cited by 547

Aβ toxicity in Alzheimer’s disease: globular oligomers (ADDLs) as new vaccine and drug targets

Klein, W. L. (2002) · Neurochemistry International · doi:10.1016/s0197-0186(02)00050-5 · Cited by 551

Semen-Derived Amyloid Fibrils Drastically Enhance HIV Infection

Münch, J., Rücker, E., Ständker, L., Adermann, K., Goffinet, C., Schindler, M., Wildum, S., Chinnadurai, R., Rajan, D., Specht, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.014 · Cited by 544

The significance of the cholinergic system in the brain during aging and in Alzheimer’s disease

Schliebs, R., & Arendt, T. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0579-2 · Cited by 548

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

Raman Spectroscopic Characterization of Secondary Structure in Natively Unfolded Proteins: α-Synuclein

Maiti, N. C., Apetri, M. M., Zagorski, M. G., CAREY, P. R., & Anderson, V. E. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0356176 · Cited by 524

Amyloid fibrils

Rambaran, R. N., & Serpell, L. C. (2008) · Prion · doi:10.4161/pri.2.3.7488 · Cited by 531

Retinal amyloid pathology and proof-of-concept imaging trial in Alzheimer’s disease

Koronyo, Y., Biggs, D., Barrón, E., Boyer, D. S., Pearlman, J. A., Au, W. J., Kile, S. J., Blanco, A., Fuchs, D.-T. S., Ashfaq, A., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.93621 · Cited by 521

Protein oxidation in the brain in Alzheimer's disease

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

The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain

Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 401

Amyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo

Klyubin, I., Walsh, D. M., Lemere, C. A., Cullen, W. K., Shankar, G. M., Betts, V., Spooner, E. T., Jiang, L., Anwyl, R., Selkoe, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1234 · Cited by 489

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

Amyloid Precursor Protein, Presenilins, and α-Synuclein: Molecular Pathogenesis and Pharmacological Applications in Alzheimer’s Disease

Suh, Y.-H., & Checler, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.469 · Cited by 476

The Alzheimer’s Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR Study

Sgourakis, N. G., Yan, Y., McCallum, S. A., Wang, C., & Garcı́a, A. E. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.093 · Cited by 460

ThT 101: a primer on the use of thioflavin T to investigate amyloid formation

Malmos, K. G., Blancas‐Mejía, L. M., Weber, B., Büchner, J., Ramı́rez-Alvarado, M., Naiki, H., & Otzen, D. E. (2017) · Amyloid · doi:10.1080/13506129.2017.1304905 · Cited by 468

REVIEW: Curcumin and Alzheimer’s disease

Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450

Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

Bieschke, J., Herbst, M., Wiglenda, T., Friedrich, R. P., Boeddrich, A., Schiele, F., Kleckers, D., del Amo, J. M. L., Grüning, B. A., Wang, Q., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.719 · Cited by 452

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

Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world

Stefani, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.004 · Cited by 433

Selective cytotoxicity of intracellular amyloid β peptide1–42 through p53 and Bax in cultured primary human neurons

Zhang, Y., McLaughlin, R., Goodyer, C., & LeBlanc, A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110119 · Cited by 418

Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins

Butterfield, D. A., & Kański, J. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00249-4 · Cited by 420

Therapeutically effective antibodies against amyloid-β peptide target amyloid-β residues 4–10 and inhibit cytotoxicity and fibrillogenesis

McLaurin, J., Cecal, R., Kierstead, M. E., Tian, X., Phinney, A. L., Manea, M., French, J. E., Lambermon, M. H. L., Darabie, A. A., Brown, M. E., et al. (2002) · Nature Medicine · doi:10.1038/nm790 · Cited by 415

The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy

Gaeta, A., & Hider, R. C. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706416 · Cited by 411

Congo Red and amyloids: history and relationship

Yakupova, E. I., Bobyleva, L. G., Vikhlyantsev, I. M., & Bobylev, A. G. (2018) · Bioscience Reports · doi:10.1042/bsr20181415 · Cited by 408

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

In Vivo Assessment of Brain Interstitial Fluid with Microdialysis Reveals Plaque-Associated Changes in Amyloid-β Metabolism and Half-Life

Cirrito, J. R., May, P. C., O'Dell, M. A., Taylor, J. W., Parsadanian, M., Cramer, J. W., Audia, J. E., Nissen, J. S., Bales, K. R., Paul, S. M., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08844.2003 · Cited by 394

Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process

Hellstrand, E., Boland, B., Walsh, D. M., & Linse, S. S. (2009) · ACS Chemical Neuroscience · doi:10.1021/cn900015v · Cited by 394

Amyloid β-Protein Oligomerization

Bitan, G., Lomakin, A., & Teplow, D. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102223200 · Cited by 387

Two Types of Alzheimer's β-Amyloid (1–40) Peptide Membrane Interactions: Aggregation Preventing Transmembrane Anchoring Versus Accelerated Surface Fibril Formation

Bokvist, M., Lindström, F., Watts, A. G., & Gröbner, G. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.046 · Cited by 379

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

Dissecting the Assembly of Aβ16–22 Amyloid Peptides into Antiparallel β Sheets

Klimov, D. K., & Thirumalai, D. (2003) · Structure · doi:10.1016/s0969-2126(03)00031-5 · Cited by 359

Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies

Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349

Amyloid-β Aggregation

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

Insight Into the Kinetic of Amyloid β (1–42) Peptide Self‐Aggregation: Elucidation of Inhibitors’ Mechanism of Action

Bartolini, M., Bertucci, C., Bolognesi, M. L., Cavalli, A., Melchiorre, C., & Andrisano, V. (2007) · ChemBioChem · doi:10.1002/cbic.200700427 · Cited by 355

Competing Pathways Determine Fibril Morphology in the Self-assembly of β2-Microglobulin into Amyloid

Gosal, W. S., Morten, I. J., Hewitt, E. W., Smith, D. A., Thomson, N. H., & Radford, S. E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.06.040 · Cited by 347

Kinetic Studies of Amyloid β-Protein Fibril Assembly

Fezoui, Y., & Teplow, D. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204168200 · Cited by 342

Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity

Fändrich, M. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.006 · Cited by 346

Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42

LIU, R., Barkhordarian, H., Emadi, S., PARK, C., & Sierks, M. R. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.02.003 · Cited by 343

Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity

Chen, S., Berthelier, V., Yang, W., & Wetzel, R. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4850 · Cited by 334

On the nucleation of amyloid β‐protein monomer folding

Lazo, N. D., Grant, M. A., Condron, M. M., Rigby, A. C., & Teplow, D. B. (2005) · Protein Science · doi:10.1110/ps.041292205 · Cited by 333

Role of Oxidative Stress in the Progression of Alzheimer's Disease

Rukhsana Sultana, A., & Butterfield, D. A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1222 · Cited by 336

Characterization of β amyloid assemblies in drusen: the deposits associated with aging and age-related macular degeneration

Anderson, D. H., Talaga, K. C., Rivest, A. J., Barron, E., Hageman, G. S., & Johnson, L. V. (2004) · Experimental Eye Research · doi:10.1016/j.exer.2003.10.011 · Cited by 319

Emerging ideas on the molecular basis of protein and peptide aggregation

Thirumalai, D. (2003) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(03)00032-0 · Cited by 314

Neprilysin Degrades Both Amyloid β Peptides 1–40 and 1–42 Most Rapidly and Efficiently among Thiorphan- and Phosphoramidon-sensitive Endopeptidases

Shirotani, K., Tsubuki, S., Iwata, N., Takaki, Y., Yamao‐Harigaya, W., Maruyama, K., Kiryu‐Seo, S., Kiyama, H., Iwata, H., Tomita, T., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008511200 · Cited by 312

Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice

Martins, I. C., Kuperstein, I., Wilkinson, H. R., Maes, E., Vanbrabant, M., Jonckheere, W., Gelder, P. V., Hartmann, D., D’Hooge, R., Strooper, B. D., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601953 · Cited by 318

Alzheimer's disease: synapses gone cold

Koffie, R. M., Hyman, B. T., & Spires‐Jones, T. L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-63 · Cited by 316

Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia

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Sensitive ELISA detection of amyloid‐β protofibrils in biological samples

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