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 · see citing works

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 · see citing works

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

Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051 · see citing works

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

Hansen, M., Nielsen, S. E., & Berg, K. (1989) · Journal of Immunological Methods · doi:10.1016/0022-1759(89)90397-9 · Cited by 3,526 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 · see citing works

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,794 · see citing works

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 · see citing works

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 · see citing works

Amyloid, the presenilins and Alzheimer’s disease

Hardy, J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01030-2 · Cited by 1,370 · see citing works

Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene

Chartier-Harlin, M.-C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L., Goate, A., Rossor, M., Roques, P., Hardy, J., et al. (1991) · Nature · doi:10.1038/353844a0 · Cited by 1,214 · see citing works

Amyloid β-Protein Fibrillogenesis

Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,139 · 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

The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways

Kelly, J. W. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80016-x · Cited by 998 · see citing works

Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand

Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R., Thyberg, J., Terenius, L., & Nordstedt, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8545 · Cited by 963 · see citing works

β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy

Soto, C. A., Sigurdsson, E. M., Morelli, L., Kumar, R., Castaño, E. M., & Frangione, B. (1998) · Nature Medicine · doi:10.1038/nm0798-822 · Cited by 874 · see citing works

Alzheimer's Disease--Genotypes, Phenotype, and Treatments

Selkoe, D. J. (1997) · Science · doi:10.1126/science.275.5300.630 · Cited by 871 · see citing works

In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity

Pike, C. J., Walencewicz, A. J., Glabe, C. G., & Cotman, C. W. (1991) · Brain Research · doi:10.1016/0006-8993(91)91553-d · Cited by 829 · see citing works

A Familial Alzheimer's Disease Locus on Chromosome 1

Levy‐Lahad, E., Wijsman, E. M., Nemens, E. J., Anderson, L., Goddard, K. A. B., Weber, J. L., Bird, T. D., & Schellenberg, G. D. (1995) · Science · doi:10.1126/science.7638621 · Cited by 811 · see citing works

Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism

Brahms, S., & Brahms, J. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90282-x · Cited by 792 · see citing works

On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants.

Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A., & Teplow, D. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1125 · Cited by 784 · see citing works

Observation of metastable Aβ amyloid protofibrils by atomic force microscopy

Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90255-6 · Cited by 691 · see citing works

Alpha-2 macroglobulin is genetically associated with Alzheimer disease

Blacker, D., Wilcox, M., Laird, N. M., Rodes, L., Horvath, S. M., Go, R. C. P., Perry, R. T., Watson, B., Bassett, S. S., McInnis, M. G., et al. (1998) · Nature Genetics · doi:10.1038/1243 · Cited by 642 · see citing works

Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease

Barrow, C. J., Yasuda, A., Kenny, P. T. M., & Zagorski, M. G. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90106-t · Cited by 636 · see citing works

Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation.

Klunk, W. E., Pettegrew, J. W., & Abraham, D. J. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.8.2666510 · Cited by 625 · see citing works

Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains

Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618 · see citing works

Aging renders the brain vulnerable to amyloid β-protein neurotoxicity

Guela, C., Wu, C.-K., Saroff, D., Lorenzo, A., Yuan, M., & Yankner, B. A. (1998) · Nature Medicine · doi:10.1038/nm0798-827 · Cited by 520 · see citing works

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006123022403 · Cited by 518 · see citing works

Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein

Harper, J. D., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90303-3 · Cited by 453 · see citing works

Isolation of Low‐Molecular‐Weight Proteins from Amyloid Plaque Fibers in Alzheimer's Disease

Selkoe, D. J., Abraham, C. R., Podlisny, M. B., & Duffy, L. K. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb08501.x · Cited by 450 · see citing works

Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide

Perczel, A., Park, K., & Fasman, G. D. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90046-a · Cited by 436 · see citing works

The toxicity in vitro of β-amyloid protein

Iversen, L. L., Mortishire‐Smith, R. J., Pollack, S. J., & Shearman, M. S. (1995) · Biochemical Journal · doi:10.1042/bj3110001 · Cited by 425 · see citing works

Inhibition of PC12 cell redox activity is a specific,early indicator of the mechanism of beta-amyloid-mediated celldeath.

Shearman, M. S., RAGAN, C. I., & Iversen, L. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1470 · Cited by 411 · see citing works

Glutamate receptor-induced 45Ca2+ accumulation in cortical cell culture correlates with subsequent neuronal degeneration

Hartley, D. M., Kurth, M., Bjerkness, L., Weiss, J. H., & Choi, D. W. (1993) · Journal of Neuroscience · doi:10.1523/jneurosci.13-05-01993.1993 · Cited by 381 · see citing works

Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths

Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Krafft, G. A., & Holzman, T. F. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80591-0 · Cited by 381 · see citing works

Physical, morphological and functional differences between ph 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta.

Wood, S. J., Maleeff, B., Hart, T., & Wetzel, R. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0133 · Cited by 337 · see citing works

The α-Helical to β-Strand Transition in the Amino-terminal Fragment of the Amyloid β-Peptide Modulates Amyloid Formation

Soto, C. A., Castaño, E. M., Frangione, B., & Inestrosa, N. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3063 · Cited by 321 · see citing works

Quantifying Amyloid β-Peptide (Aβ) Aggregation Using the Congo Red-Aβ (CR–Aβ) Spectrophotometric Assay

Klunk, W. E., Jacob, R. F., & Mason, R. P. (1999) · Analytical Biochemistry · doi:10.1006/abio.1998.2933 · Cited by 310 · see citing works

Structural and kinetic features of amyloid β-protein fibrillogenesis

Teplow, D. B. (1998) · Amyloid · doi:10.3109/13506129808995290 · Cited by 280 · see citing works

First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro.

Naiki, H., & Nakakuki, K. (1996) · PubMed · Cited by 244 · see citing works

Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

Inouye, H., Fraser, P., & Kirschner, D. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81393-6 · Cited by 239 · see citing works

A New Pathogenic Mutation in the APP Gene (I716V) Increases the Relative Proportion of A 42(43)

Eckman, C. B., Mehta, N. D., Crook, R., Perez-tur, J., Prihar, G., Pfeiffer, E., Graff-Radford, N., Hinder, P., Yager, D., Zenk, B., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.12.2087 · Cited by 236 · see citing works

A Strategy for Designing Inhibitors of β-Amyloid Toxicity

Ghanta, J., Shen, C.-L., Kiessling, L. L., & Murphy, R. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.29525 · Cited by 224 · see citing works

The Toxicity of the Alzheimer's β-Amyloid Peptide Correlates with a Distinct Fiber Morphology

Seilheimer, B., Bohrmann, B., Bondolfi, L., Müller, F., Stüber, D., & Döbeli, H. (1997) · Journal of Structural Biology · doi:10.1006/jsbi.1997.3859 · Cited by 207 · see citing works

Aggregation State and Neurotoxic Properties of Alzheimer Beta-Amyloid Peptide

Howlett, D. R., JENNINGS, K. H., Lee, D. C., Clark, M. S. G., Brown, F., Wetzel, R. B., Wood, S. J., Camilleri, P., & Roberts, G. W. (1995) · Neurodegeneration · doi:10.1006/neur.1995.0003 · Cited by 204 · see citing works

The Intracellular Component of Cellular 3‐(4,5‐Dimethylthiazol‐2‐yl)‐2,5‐Diphenyltetrazolium Bromide (MTT) Reduction Is Specifically Inhibited by β‐Amyloid Peptides

Shearman, M. S., Hawtin, S. R., & Tailor, V. J. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65010218.x · Cited by 204 · see citing works

Cytotoxic Amyloid Peptides Inhibit Cellular 3‐(4,5‐Dimethylthiazol‐2‐yl)‐2,5‐Diphenyltetrazolium Bromide (MTT) Reduction by Enhancing MTT Formazan Exocytosis

Liu, Y., & Schubert, D. A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69062285.x · Cited by 195 · see citing works

Kinetics of aggregation of synthetic β-amyloid peptide

Tomski, S. J., & Murphy, R. M. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90735-f · Cited by 149 · see citing works

Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein.

Roher, A. E., WOLFE, D. E., Palutke, M., & Kukuruga, D. L. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.8.2662 · Cited by 136 · see citing works

Amyloid β peptide alters intracellular vesicle trafficking and cholesterol homeostasis

Liu, Y., Peterson, D. A., & Schubert, D. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13266 · Cited by 127 · see citing works

The conformation of Alzheimer's β peptide determines the rate of amyloid formation and its resistance to proteolysis

Soto, C. A., & Castaño, E. M. (1996) · Biochemical Journal · doi:10.1042/bj3140701 · Cited by 116 · see citing works

β-amyloid peptide in vitro toxicity: Lot-to-lot variability

May, P. C., Gitter, B. D., Waters, D. C., Simmons, L. K., Becker, G. W., Small, J. S., & Robison, P. M. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90064-5 · Cited by 116 · see citing works

Aggregation and Metal‐Binding Properties of Mutant Forms of the Amyloid Aβ Peptide of Alzheimer's Disease

Clements, A., Allsop, D., Walsh, D. M., & Williams, C. H. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66020740.x · Cited by 116 · see citing works

Mapping the heparin-binding sites on type I collagen monomers and fibrils.

Antonio, J. D. S., Lander, A. D., Karnovsky, M. J., & Slayter, H. S. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.125.5.1179 · Cited by 107 · see citing works

Therapeutic Approaches Related to Amyloid-.beta. Peptide and Alzheimer's Disease

Schenk, D. B., Rydel, R. E., May, P. C., Little, S. P., Panetta, J., Lieberburg, I. M., & Sinha, S. (1995) · Journal of Medicinal Chemistry · doi:10.1021/jm00021a001 · Cited by 82 · see citing works

Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes

Abe, K., & Saitō, H. (1998) · Neuroscience Research · doi:10.1016/s0168-0102(98)00055-8 · Cited by 80 · see citing works

De novo design and structural characterization of an alpha-helical hairpin peptide: a model system for the study of protein folding intermediates.

Fezoui, Y., Weaver, D. L., & Osterhout, J. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.9.3675 · Cited by 72 · see citing works

The neurotoxicity of amyloid beta protein in aged primates

McKee, A. C., Kawall, N. W., Schumacher, J. S., & Beal, M. F. (1998) · Amyloid · doi:10.3109/13506129809007283 · Cited by 64 · see citing works

An Ultrastructural Study of Amyloid Intermediates in Aβ1–42 Fibrillogenesis

Nybo, M., Svehag, & Nielsen, H. (1999) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.1999.00526.x · Cited by 55 · see citing works

Solution structure of αtα, a helical hairpin peptide of de novo design

Fezoui, Y., Connolly, P. J., & Osterhout, J. J. (1997) · Protein Science · doi:10.1002/pro.5560060907 · Cited by 48 · see citing works

Spectroscopic characterization of conformational differences between PrPC and PrPSc: an α-helix to β-sheet transition

Baldwin, M. A., Pan, K.-M., Nguyen, J. T., Huang, Z., Groth, D., Serban, A. V., Gasset, M., Mehlhorn, I., Fletterick, R. J., Cohen, F. E., et al. (1994) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1994.0041 · Cited by 43 · see citing works

HISTOCHEMICAL OBSERVATIONS ON AMYLOID WITH REFERENCE TO POLARIZATION MICROSCOPY

DeLellis, R. A., Glenner, G. G., & Ram, J. S. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.10.663-a · Cited by 40 · see citing works

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 6,435 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 1,643 · see citing works

P <scp>ROTOFIBRILS</scp> , P <scp>ORES</scp> , F <scp>IBRILS, AND</scp> N <scp>EURODEGENERATION</scp> : 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 · see citing works

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 · see citing works

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 1,543 · see citing works

Unfolding the role of protein misfolding in neurodegenerative diseases

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

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 · see citing works

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. (2008) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,424 · see citing works

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 · see citing works

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 1,280 · see citing works

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 · see citing works

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 · see citing works

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 1,087 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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

Hartley, D. M., Walsh, D. M., Ye, C., Diehl, T. S., Vasquez, S., Vassilev, P., Teplow, D. B., & Selkoe, D. J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 965 · see citing works

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 · see citing works

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 · see citing works

Structure–neurotoxicity relationships of amyloid β-protein oligomers

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Protein aggregation diseases: pathogenicity and therapeutic perspectives

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