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

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

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

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

Hansen, M., Nielsen, S. E., & Berg, K. (1989) · Journal of Immunological Methods · doi:10.1016/0022-1759(89)90397-9 · Cited by 3,488

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

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

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

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

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 1,156

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

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

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

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

Selkoe, D. J. (1997) · Science · doi:10.1126/science.275.5300.630 · Cited by 879

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

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 841

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 832

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

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

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 699

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 644

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

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 618

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

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006123022403 · Cited by 515

Alpha-2 macroglobulin is genetically associated with Alzheimer disease

Blacker, D., Wilcox, M. A., Laird, N. M., Rodes, L., Horvath, S. M., Go, R. C. P., Perry, R., Watson, B., Bassett, S. S., McInnis, M. G., et al. (1998) · Nature Genetics · doi:10.1038/1243 · Cited by 486

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 452

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 452

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 430

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 428

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 414

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

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

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

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

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

Structural and kinetic features of amyloid β-protein fibrillogenesis

Teplow, D. B. (1998) · Amyloid · doi:10.3109/13506129808995290 · Cited by 284

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

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

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

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

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

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

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

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

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 190

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

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

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 128

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 117

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

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

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

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

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 81

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

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

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

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

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

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 39

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

Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates

Walsh, D., Hartley, D., Kusumoto, Y., Fezoui, Y., Condron, M., Lomakin, A. A., Benedek, G., Selkoe, D., & Teplow, D. (1999) · eScholarship (California Digital Library)

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 452

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 699

Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease.

Kirkitadze, M. D., & Kowalska, A. (2005) · Acta Biochimica Polonica · doi:10.18388/abp.2005_3454 · Cited by 77

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