Soluble protein oligomers as emerging toxins in Alzheimer’s and other amyloid diseases

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works

Global prevalence of dementia: a Delphi consensus study

Ferri, C. P., Prince, M. J., Brayne, C., Brodaty, H., Fratiglioni, L., Ganguli, M., Hall, K. S., Hasegawa, K., Hendrie, H. C., Huang, Y., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)67889-0 · Cited by 5,336 · see citing works

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · see citing works

Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment

Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397 · 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

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · see citing works

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works

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

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

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

Pathways towards and Away from Alzheimer’s Disease

Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052 · 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

Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity

Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., & Selkoe, D. J. (1999) · Nature · doi:10.1038/19077 · Cited by 1,913 · 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

Purification and cloning of amyloid precursor protein β-secretase from human brain

Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612 · see citing works

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611 · see citing works

Regulation of NMDA receptor trafficking by amyloid-β

Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · see citing works

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works

Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.

Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324 · see citing works

Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline

Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268 · see citing works

Clinical, pathological, and neurochemical changes in dementia: a subgroup with preserved mental status and numerous neocortical plaques

Katzman, R., Terry, R., DeTeresa, R., Brown, T., Davies, P., Fuld, P., Renbing, X., & Peck, A. (1988) · Annals of Neurology · doi:10.1002/ana.410230206 · Cited by 1,225 · see citing works

Aβ Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease

Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188 · see citing works

Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer’s disease

Giannakopoulos, P., Herrmann, F. R., Bussière, T., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Gold, G., & Hof, P. R. (2003) · Neurology · doi:10.1212/01.wnl.0000063311.58879.01 · Cited by 1,118 · see citing works

Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss

Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061 · see citing works

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E., Hawkins, P. N., Dobson, C. M., Radford, S. E., Blake, C., et al. (1997) · Nature · doi:10.1038/385787a0 · Cited by 1,049 · see citing works

AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss

Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042 · see citing works

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 1,038 · 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

Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease

Oddo, S. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.08.012 · Cited by 980 · see citing works

Calcium dyshomeostasis and intracellular signalling in alzheimer's disease

LaFerla, F. M. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn960 · Cited by 970 · see citing works

Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers

Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954 · see citing works

Neurotoxicity of a prion protein fragment

Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., & Tagliavini, F. (1993) · Nature · doi:10.1038/362543a0 · Cited by 950 · see citing works

The most infectious prion protein particles

Silveira, J. R., Raymond, G. J., Hughson, A. G., Race, R. E., Sim, V. L., Hayes, S. F., & Caughey, B. (2005) · Nature · doi:10.1038/nature03989 · Cited by 899 · see citing works

Aβ Oligomers Induce Neuronal Oxidative Stress through an N-Methyl-D-aspartate Receptor-dependent Mechanism That Is Blocked by the Alzheimer Drug Memantine

De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882 · see citing works

Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model

Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858 · see citing works

ALZHEIMER'S DISEASE INTERNATIONAL

Graham, N., & Brodaty, H. (1997) · International Journal of Geriatric Psychiatry · doi:10.1002/(sici)1099-1166(199707)12:7 · Cited by 852 · see citing works

Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer’s disease

Georganopoulou, D. G., Chang, L., Nam, J.-M., Thaxton, C. S., Mufson, E. J., Klein, W. L., & Mirkin, C. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409336102 · Cited by 835 · see citing works

β-Amyloid1–42 Binds to α7 Nicotinic Acetylcholine Receptor with High Affinity

Wang, H.-Y., Lee, D. H. S., D’Andrea, M. R., Peterson, P. A., Shank, R. P., & Reitz, A. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5626 · Cited by 818 · see citing works

Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.

Westermark, P., Engström, U., Johnson, K. H., Westermark, G. T., & Betsholtz, C. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5036 · Cited by 807 · see citing works

Tau is essential to β-amyloid-induced neurotoxicity

Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807 · see citing works

α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils

Lashuel, H. A., Petre, B. M., Wall, J. S., Simon, M. N., Nowak, R. J., Walz, T., & Lansbury, P. T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00735-0 · Cited by 802 · 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

Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H., & LaFerla, F. M. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.003 · Cited by 780 · see citing works

Sp1 and TAFII130 Transcriptional Activity Disrupted in Early Huntington's Disease

Dunah, A. W., Jeong, H., Griffin, A. M., Kim, Y., Standaert, D. G., Hersch, S. M., Mouradian, M. M., Young, A. B., Tanese, N., & Krainc, D. (2002) · Science · doi:10.1126/science.1072613 · Cited by 708 · see citing works

Intraneuronal Alzheimer Aβ42 Accumulates in Multivesicular Bodies and Is Associated with Synaptic Pathology

Takahashi, R. H., Milner, T. A., Li, F., Nam, E. E., Edgar, M. A., Yamaguchi, H., Beal, M. F., Xu, H., Greengard, P., & Gouras, G. K. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64463-x · Cited by 706 · see citing works

Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques

Scott, M., FOSTER, D. B., Mirenda, C. A., Serban, D., Coufal, F. J., Wälchli, M., Torchia, M., Groth, D., Carlson, G. A., DeArmond, S. J., et al. (1989) · Cell · doi:10.1016/0092-8674(89)90608-9 · Cited by 695 · see citing works

Human lysozyme gene mutations cause hereditary systemic amyloidosis

Pepys, M. B., Hawkins, P. N., Booth, D. R., Vigushin, D. M., Tennent, G. A., Soutar, A. K., Totty, N. F., Nguyen, O., Blake, C. C. F., Terry, C. J., et al. (1993) · Nature · doi:10.1038/362553a0 · Cited by 654 · see citing works

ULTRASTRUCTURAL STUDIES IN ALZHEIMER'S PRESENILE DEMENTIA.

Terry, R. D., Gonatas, N. K., & WEISS, M. (1964) · PubMed · Cited by 650 · see citing works

Effects of secreted oligomers of amyloid β‐protein on hippocampal synaptic plasticity: a potent role for trimers

Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., & Selkoe, D. J. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.103754 · Cited by 619 · 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

The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles.

Janson, J., Ashley, R. H., Harrison, D. J., McIntyre, S., & Butler, P. C. (1999) · Diabetes · doi:10.2337/diabetes.48.3.491 · Cited by 614 · see citing works

Prion (PrPSc)-specific epitope defined by a monoclonal antibody

Korth, C., Stierli, B., Streit, P., et al. (1997) · Nature · doi:10.1038/36337 · Cited by 567 · see citing works

The Formation of Highly Soluble Oligomers of α-Synuclein Is Regulated by Fatty Acids and Enhanced in Parkinson's Disease

Sharon, R., Bar-Joseph, I., Frosch, M. P., Walsh, D. M., Hamilton, J. A., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00024-2 · Cited by 562 · see citing works

Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus

Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527 · 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

Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β

Hoshi, M. M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., & Sato, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1237107100 · Cited by 494 · see citing works

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 490 · see citing works

New Frontiers in Alzheimer's Disease Genetics

Tanzi, R. E., & Bertram, L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00476-7 · Cited by 464 · see citing works

Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease?

Goldberg, M. S., & Lansbury, P. T. (2000) · Nature Cell Biology · doi:10.1038/35017124 · Cited by 456 · see citing works

Neuronal and glial calcium signaling in Alzheimer’s disease

Mattson, M. P., & Chan, S. L. (2003) · Cell Calcium · doi:10.1016/s0143-4160(03)00128-3 · Cited by 454 · see citing works

Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain

Takahashi, R. H., Almeida, C. G., Kearney, P. F., Yu, F., Lin, M. T., Milner, T. A., & Gouras, G. K. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5167-03.2004 · Cited by 445 · see citing works

Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers

De Felice, F. G., Wu, D., Lambert, M. P., Fernandez, S. J., Velasco, P. T., Lacor, P. N., Bigio, E. H., Jerecic, J., Acton, P. J., Shughrue, P. J., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.029 · Cited by 432 · see citing works

Reactive oxygen species and synaptic plasticity in the aging hippocampus

Serrano, F., & Klann, E. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.05.002 · Cited by 421 · see citing works

Reversible memory loss in a mouse transgenic model of Alzheimer’s disease

Kotilinek, L. A., Bacskai, B., Westerman, M., Kawarabayashi, T., Younkin, L., Hyman, B. T., Younkin, S., & Ashe, K. H. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06331.2002 · Cited by 420 · see citing works

Formation of β-amyloid protein deposits in brains of transgenic mice

Quon, D. H., Wang, Y., Catalano, R., Scardina, J. M., Murakami, K., & Cordell, B. (1991) · Nature · doi:10.1038/352239a0 · Cited by 397 · see citing works

Amyloid β-Protein Oligomerization

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

Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease

Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507892200 · Cited by 379 · see citing works

Oxidative injury in diseases of the central nervous system: focus on alzheimer’s disease

Praticò, D., & Delanty, N. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00547-7 · Cited by 378 · see citing works

Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity

Bucciantini, M., Calloni, G., Chiti, F., Formigli, L., Nosi, D., Dobson, C. M., & Stefani, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400348200 · Cited by 369 · see citing works

Aggregation of Secreted Amyloid β-Protein into Sodium Dodecyl Sulfate-stable Oligomers in Cell Culture

Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydel, R. E., Teplow, D. B., & Selkoe, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9564 · Cited by 364 · see citing works

Deposition of Transthyretin in Early Stages of Familial Amyloidotic Polyneuropathy

Sousa, M. M., Cardoso, I., Fernandes, R., Guimarães, A., & Saraiva, M. J. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63050-7 · Cited by 343 · see citing works

Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease

Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338 · see citing works

Temporal memory deficits in Alzheimer’s mouse models: Rescue by genetic deletion of BACE1

Ohno, M., Chang, L., Tseng, W., Oakley, H., Citron, M., Klein, W. L., Vassar, R., & Disterhoft, J. F. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04551.x · Cited by 298 · see citing works

β-Amyloid 1–42 Peptide Directly Modulates Nicotinic Receptors in the Rat Hippocampal Slice

Pettit, D. L., Shao, Z., & Yakel, J. L. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-01-j0003.2001 · Cited by 291 · see citing works

Desmin-related cardiomyopathy in transgenic mice: A cardiac amyloidosis

Sanbe, A., Osińska, H. E., Saffitz, J. E., Glabe, C. G., Kayed, R., Maloyan, A., & Robbins, J. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401900101 · Cited by 291 · see citing works

Enhanced Production and Oligomerization of the 42-residue Amyloid β-Protein by Chinese Hamster Ovary Cells Stably Expressing Mutant Presenilins

Xia, W., Zhang, J., Kholodenko, D., Citron, M., Podlisny, M. B., Teplow, D. B., Haass, C., Seubert, P. A., Koo, E. H., & Selkoe, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7977 · Cited by 282 · see citing works

Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide.

Verchere, C. B., D'Alessio, D. A., Palmiter, R. D., Weir, G. C., Bonner-Weir, S., Baskin, D. G., & Kahn, S. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3492 · Cited by 278 · see citing works

Soluble β-Amyloid1-40Induces NMDA-Dependent Degradation of Postsynaptic Density-95 at Glutamatergic Synapses

Roselli, F., Tirard, M., Lu, J., Hutzler, P., Lamberti, P., Livrea, P., Morabito, M. A., & Almeida, O. F. X. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3034-05.2005 · Cited by 276 · see citing works

Diabetes Due to a Progressive Defect in β-Cell Mass in Rats Transgenic for Human Islet Amyloid Polypeptide (HIP Rat)

Butler, A. E., Jang, J., Gurlo, T., Carty, M. D., Soeller, W. C., & Butler, P. C. (2004) · Diabetes · doi:10.2337/diabetes.53.6.1509 · Cited by 267 · see citing works

Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons

Novitskaya, V., Bocharova, O. V., Bronstein, I. B., & Baskakov, I. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511174200 · Cited by 247 · see citing works

The Role of APP Processing and Trafficking Pathways in the Formation of Amyloid β‐Proteina

Selkoe, D. J., Yamazaki, T., Citron, M., Podlisny, M. B., Koo, E. H., Teplow, D. B., & Haass, C. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34401.x · Cited by 246 · see citing works

Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis

Yan, L., Tatarek‐Nossol, M., Velkova, A., Kazantzis, A., & Kapurniotu, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507471103 · Cited by 243 · see citing works

β-Amyloid-induced Dynamin 1 Degradation Is Mediated by N-Methyl-D-Aspartate Receptors in Hippocampal Neurons

Kelly, B. L., & Ferreira, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605081200 · Cited by 240 · see citing works

Calcium, mitochondria and oxidative stress in neuronal pathology

Chinopoulos, C., & Ádám‐Vizi, V. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05103.x · Cited by 239 · see citing works

Taurine prevents the neurotoxicity of β‐amyloid and glutamate receptor agonists: activation of GABA receptors and possible implications for Alzheimer's disease and other neurological disorders

Louzada, P., Lima, A. C. P., Mendonça-Silva, D., Noël, F., de Mello, F. G., & Ferreira, S. (2004) · The FASEB Journal · doi:10.1096/fj.03-0739com · Cited by 239 · see citing works

Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington’s disease brain nuclei

Karpuj, M. V., Garren, H., Slunt, H. H., Price, D. L., Gusella, J. F., Bêcher, M. W., & Steinman, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7388 · Cited by 225 · see citing works

In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to alzheimer's disease β-protein

Castaño, E. M., Ghiso, J. A., Prelli, F. C., Gorevic, P. D., Migheli, A., & Frangione, B. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80241-8 · Cited by 225 · see citing works

The aggregation potential of human amylin determines its cytotoxicity towards islet β‐cells

Konarkowska, B., Aitken, J. F., Kistler, J., Zhang, S., & Cooper, G. J. S. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05367.x · Cited by 219 · see citing works

Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid

King, M. E., Kan, H.-M., Baas, P. W., Erişir, A., Glabe, C. G., & Bloom, G. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605187 · Cited by 215 · see citing works

Structural studies of soluble oligomers of the alzheimer β-amyloid peptide

Huang, T. H. J., Dun-Sheng, Y., Plaskos, N. P., Go, S., Yip, C. M., Fraser, P. E., & Chakrabartty, A. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3559 · Cited by 213 · see citing works

Familial Amyloid Polyneuropathy: Receptor for Advanced Glycation End Products-Dependent Triggering of Neuronal Inflammatory and Apoptotic Pathways

Sousa, M. M., Du Yan, S., Fernandes, R., Guimarães, A., Stern, D., & Saraiva, M. J. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07576.2001 · Cited by 212 · see citing works

Adult-derived neural precursors transplanted into multiple regions in the adult brain

Herrera, D. G., García‐Verdugo, J. M., & Álvarez-Buylla, A. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199912)46:6 · Cited by 204 · see citing works

Mitochondrial abnormalities and oxidative imbalance in Alzheimer disease

Zhu, X., Perry, G. L., Moreira, P. I., Aliev, G. M., Cash, A., Hirai, K., & Smith, M. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9207 · Cited by 196 · see citing works

Neuropathology of prion diseases

Budka, H. (2003) · British Medical Bulletin · doi:10.1093/bmb/66.1.121 · Cited by 196 · see citing works

Altered Fatty Acid Composition of Dopaminergic Neurons Expressing α-Synuclein and Human Brains with α-Synucleinopathies

Sharon, R., Bar-Joseph, I., Mirick, G. E., Serhan, C. N., & Selkoe, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309127200 · Cited by 187 · see citing works

A strategy for designing inhibitors of α ‐synuclein aggregation and toxicity as a novel treatment for Parkinson's disease and related disorders

El‐Agnaf, O. M. A., Paleologou, K. E., Greer, B., Abogrein, A. M., King, J. E., Salem, S. A., Fullwood, N. J., Benson, F. E., Hewitt, R., Ford, K. J., et al. (2004) · The FASEB Journal · doi:10.1096/fj.03-1346fje · Cited by 187 · see citing works

Oligomerization of Endogenous and Synthetic Amyloid β-Protein at Nanomolar Levels in Cell Culture and Stabilization of Monomer by Congo Red

Podlisny, M. B., Walsh, D. M., Amarante, P., Ostaszewski, B. L., Stimson, E. R., Maggio, J. E., Teplow, D. B., & Selkoe, D. J. (1998) · Biochemistry · doi:10.1021/bi972029u · Cited by 186 · see citing works

Contribution of somal Lewy bodies to neuronal death

Tompkins, M. M., & Hill, W. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00874-3 · Cited by 182 · see citing works

NONAMYLOIDOTIC MONOCLONAL IMMUNOGLOBULIN DEPOSITION DISEASE

Buxbaum, J. N., & Gallo, G. (1999) · Hematology/Oncology Clinics of North America · doi:10.1016/s0889-8588(05)70123-4 · Cited by 175 · see citing works

Prion Diseases: What Is the Neurotoxic Molecule?

Chiesa, R., & Harris, D. A. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0433 · Cited by 160 · see citing works

Fractionation and characterization of oligomeric, protofibrillar and fibrillar forms of β-amyloid peptide

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 · see citing works

Cytosolic Catechols Inhibit α-Synuclein Aggregation and Facilitate the Formation of Intracellular Soluble Oligomeric Intermediates

Mazzulli, J. R., Mishizen-Eberz, A. J., Giasson, B. I., Lynch, D. R., THOMAS, S. A., Nakashima, A., Nagatsu, T., Ota, A., & Ischiropoulos, H. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0896-06.2006 · Cited by 152 · see citing works

Oxidative Imbalance in Alzheimer's Disease

Zhu, X., Lee, H., Casadesús, G., Ávila, J., Drew, K. L., Perry, G. L., & Smith, M. A. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:205 · Cited by 146 · see citing works

Deposits of Amyloid β Protein in the Central Nervous System of Transgenic Mice

Wirak, D. O., Bayney, R. M., Ramabhadran, T. V., Fracasso, R. P., Hart, J., Hauer, P., Hsiau, P., Pekar, S. K., Scangos, G. A., Trapp, B. D., et al. (1991) · Science · doi:10.1126/science.1857970 · Cited by 141 · see citing works

Structural Stability and Dynamics of an Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35

Zheng, J., Ma, B., Tsai, C., & Nussinov, R. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.083246 · Cited by 135 · see citing works

Docosahexaenoic acid prevents neuronal apoptosis induced by soluble amyloid‐β oligomers

Florent‐Béchard, S., Malaplate, C., Youssef, I., Kriem, B., Koziel, V., Escanyé, M., Fifre, A., Sponne, I., Leininger‐Muller, B., Olivier, J. L., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03541.x · Cited by 131 · see citing works

The relation of islet amyloid to the clinical type of diabetes

Maloy, A. L., Longnecker, D. S., & Greenberg, E. R. (1981) · Human Pathology · doi:10.1016/s0046-8177(81)80197-9 · Cited by 129 · see citing works

Non-Fibrillar β-Amyloid Protein is Associated with Smooth Muscle Cells of Vessel Walls in Alzheimer Disease

Frackowiak, J., Żółtowska, A., & Wı́sniewski, H. M. (1994) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199411000-00011 · Cited by 128 · see citing works

Soluble Amyloid β-Protein Is a Marker of Alzheimer Amyloid in Brain But Not in Cerebrospinal Fluid

Tabaton, M., Nunzi, M. G., Xue, R., Usiak, M., AUTILIO‐GAMBETTI, L., & Gambetti, P. L. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1634 · Cited by 126 · see citing works

Antibodies against β‐amyloid reduce aβ oligomers, glycogen synthase kinase‐3β activation and τ phosphorylation in vivo and in vitro

Ma, Q., Lim, G. P., Harris‐White, M. E., Yang, F., Ambegaokar, S. S., Ubeda, O. J., Glabe, C. G., Teter, B., Frautschy, S. A., & Cole, G. M. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20734 · Cited by 126 · see citing works

Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice

Yu, Z.-X. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.8.905 · Cited by 121 · see citing works

Oligomeric Assembly of Native-like Precursors Precedes Amyloid Formation by β-2 Microglobulin

Eakin, C. M., Attenello, F. J., Morgan, C. J., & Miranker, A. D. (2004) · Biochemistry · doi:10.1021/bi049792q · Cited by 117 · see citing works

Elucidation of the Molecular Mechanism during the Early Events in Immunoglobulin Light Chain Amyloid Fibrillation

Souillac, P. O., Uversky, V. N., Millett, I. S., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109229200 · Cited by 115 · see citing works

β-Amyloid Directly Inhibits Human α4β2-Nicotinic Acetylcholine Receptors Heterologously Expressed in Human SH-EP1 Cells

Wu, J., Kuo, Y., George, A. A., Xu, L., Hu, J., & Lukas, R. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400335200 · Cited by 111 · see citing works

Normal transthyretin and synthetic transthyretin fragments from amyloid-like fibrils in vitro

Gustavsson, Å., Engström, U., & Westermark, P. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91687-8 · Cited by 109 · see citing works

Apoptotic Neuronal Cell Death Induced by the Non-fibrillar Amyloid-β Peptide Proceeds through an Early Reactive Oxygen Species-dependent Cytoskeleton Perturbation

Sponne, I., Fifre, A., Drouet, B., Klein, C., Koziel, V., Pinçon‐Raymond, M., Olivier, J. L., Chambaz, J., & Pillot, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206745200 · Cited by 108 · see citing works

Reversal of amyloid-induced heart disease in desmin-related cardiomyopathy

Sanbe, A., Osińska, H. E., Villa, C. R., Gulick, J. M., Klevitsky, R., Glabe, C. G., Kayed, R., & Robbins, J. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503324102 · Cited by 108 · see citing works

Forcing Nonamyloidogenic β-Synuclein To Fibrillate

Yamin, G., Munishkina, L. A., Karymov, M. A., Lyubchenko, Y. L., Uversky, V. N., & Fink, A. L. (2005) · Biochemistry · doi:10.1021/bi048778a · Cited by 103 · see citing works

Tau phosphorylation increases in symptomatic mice overexpressing A30P α-synuclein

Frasier, M. A., Walzer, M., McCarthy, L., Magnuson, D. J., Lee, J. M., Haas, C. A., Kahle, P. J., & Wolozin, B. L. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.07.016 · Cited by 103 · see citing works

Amyloid and Nonfibrillar Deposits in Mice Transgenic for Wild-Type Human Transthyretin: A Possible Model for Senile Systemic Amyloidosis

Teng, M.-H., Yin, J.-Y., Vidal, R., Ghiso, J. A., Kumar, A. R., Rabenou, R. A., Shah, A., Jacobson, D. R., Tagoe, C. E., Gallo, G., et al. (2001) · Laboratory Investigation · doi:10.1038/labinvest.3780246 · Cited by 96 · see citing works

A New Hypothesis for the Mechanism of Amyloid Toxicity, Based on the Calcium Channel Activity of Amyloid β Protein (AβP) in Phospholipid Bilayer Membranes

Pollard, H. B., Rojas, E., & Arispe, N. J. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23046.x · Cited by 95 · see citing works

Neuronal Apoptosis in Fatal Familial Insomnia

Dorandeu, A., Wingertsmann, L., Chrétien, F. C., Delisle, M., Vital, C., Parchi, P., Montagna, P., Lugaresi, E., Ironside, J. W., Budka, H., et al. (1998) · Brain Pathology · doi:10.1111/j.1750-3639.1998.tb00175.x · Cited by 91 · see citing works

Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N‐terminal fragments of expanded huntingtin and insoluble polymers

Hoffner, G., Island, M., & Djian, P. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03348.x · Cited by 88 · see citing works

Ion channel hypothesis for Alzheimer amyloid peptide neurotoxicity

Pollard, H. B., Arispe, N. J., & Rojas, E. (1995) · Cellular and Molecular Neurobiology · doi:10.1007/bf02071314 · Cited by 88 · see citing works

Formation of amyloid aggregates from human lysozyme and its disease‐associated variants using hydrostatic pressure

Felice, F. G. D., Vieira, M. N. N., Meirelles, M. N. L., Morozova‐Roche, L. A., Dobson, C. M., & Ferreira, S. T. (2004) · The FASEB Journal · doi:10.1096/fj.03-1072fje · Cited by 88 · see citing works

Activation of GABA(A) receptors by taurine and muscimol blocks the neurotoxicity of beta-amyloid in rat hippocampal and cortical neurons.

Paula-Lima, A., Felice, F. D. D., Brito‐Moreira, J., & Ferreira, S. (2005) · Neuropharmacology · doi:10.1016/j.neuropharm.2005.06.015 · Cited by 87 · see citing works

Detection of novel intracellular O‐synuclein oligomeric species by fluorescence lifetime imaging

Klucken, J., Outeiro, T. F., Nguyen, P. T., McLean, P. J., & Hyman, B. T. (2006) · The FASEB Journal · doi:10.1096/fj.05-5422com · Cited by 83 · see citing works

Modulation of Aβ42low-n oligomerization using a novel yeast reporter system

Bagriantsev, S. N., & Liebman, S. W. (2006) · BMC Biology · doi:10.1186/1741-7007-4-32 · Cited by 80 · see citing works

Polymorphism at Residue 129 Modulates the Conformational Conversion of the D178N Variant of Human Prion Protein 90−231

Apetri, A. C., Vanik, D. L., & Surewicz, W. K. (2005) · Biochemistry · doi:10.1021/bi051455+ · Cited by 80 · see citing works

Structural Transformations of Oligomeric Intermediates in the Fibrillation of the Immunoglobulin Light Chain LEN

Souillac, P. O., Uversky, V. N., & Fink, A. L. (2003) · Biochemistry · doi:10.1021/bi034652m · Cited by 79 · see citing works

Transthyretin oligomers induce calcium influx via voltage‐gated calcium channels

Hou, X., Parkington, H. C., Coleman, H. A., Mechler, Á., Martin, L. L., Aguilar, M., & Small, D. H. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04210.x · Cited by 74 · see citing works

Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells

Mukai, H., Isagawa, T., Goyama, E., Tanaka, S., Bence, N., Tamura, A., Ono, Y., & Kopito, R. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409283102 · Cited by 74 · see citing works

Disease-associated F198S Mutation Increases the Propensity of the Recombinant Prion Protein for Conformational Conversion to Scrapie-like Form

Vanik, D. L., & Surewicz, W. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207511200 · Cited by 73 · see citing works

Role of the single disulphide bond of β2‐microglobulin in amyloidosis in vitro

Smith, D. P., & Radford, S. E. (2001) · Protein Science · doi:10.1110/ps.4901 · Cited by 73 · see citing works

Interaction of human stefin B in the prefibrillar oligomeric form with membranes

Anderluh, G., Gutiérrez‐Aguirre, I., Rabzelj, S., Čeru, S., Kopitar‐Jerala, N., Maček, P., Türk, V., & Žerovnik, E. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04717.x · Cited by 57 · see citing works

Structural characterization of β-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro

Redecke, L., von Bergen�, M., Clos, J., Konarev, P. V., Svergun, D. I., Fittschen, U. E. A., Broekaert, J. A. C., Bruns†, O. T., Georgieva, D. N., Mandelkow�, E., et al. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.06.013 · Cited by 54 · see citing works

Neuroprotection against Aβ and glutamate toxicity by melatonin: Are GABA receptors involved?

Paula-Lima, A. C., Louzada, P. R., Mello, F. G. D., & Ferreira, S. T. (2003) · Neurotoxicity Research · doi:10.1007/bf03033152 · Cited by 53 · see citing works

Formation of islet amyloid fibrils in beta-secretory granules of transgenic mice expressing human islet amyloid polypeptide/amylin

Yagui, K., Yamaguchi, T., Kanatsuka, A., Shimada, F., Huang, C. I., Tokuyama, Y., Ohsawa, H., Yamamura, K., Miyazaki, J., Mikata, A., et al. (1995) · European Journal of Endocrinology · doi:10.1530/eje.0.1320487 · Cited by 53 · see citing works

Dynamics of yeast prion aggregates in single living cells

Kawai‐Noma, S., Ayano, S., Pack, C., Kinjo, M., Yoshida, M., Yasuda, K., & Taguchi, H. (2006) · Genes to Cells · doi:10.1111/j.1365-2443.2006.01004.x · Cited by 51 · see citing works

Amyloid β-peptide preconditioning reduces glutamate-induced neurotoxicity by promoting endocytosis of NMDA receptor

Goto, Y., Niidome, T., Akaike, A., Kihara, T., & Sugimoto, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.030 · Cited by 49 · see citing works

Amyloid-β impairs development of neuronal progenitor cells by oxidative mechanisms

Mazur‐Kolecka, B., Golabek, A. A., Nowicki, K., Flory, M. J., & Frackowiak, J. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.07.006 · Cited by 48 · see citing works

Incubation of nerve endings with a physiological concentration of Aβ1-42 activates CaV2.2(N-Type)-voltage operated calcium channels and acutely increases glutamate and noradrenaline release

Bobich, J. A., Zheng, Q., & Campbell, A. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6305 · Cited by 46 · see citing works

Amyloidogenicity and Cytotoxicity of Recombinant Mature Human Islet Amyloid Polypeptide (rhIAPP)

Lopes, D. H. J., Colin, C., Degaki, T. L., de Sousa, A. C. V., Vieira, M. N. N., Sebollela, A., Martinez, A. M. B., Bloch, C., Ferreira, S. T., & Sogayar, M. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406108200 · Cited by 46 · see citing works

Peptide Blockers of the Inhibition of Neuronal Nicotinic Acetylcholine Receptors by Amyloid β

Magdesian, M. H., Nery, A. A., Martins, A. H. B., Juliano, M. A., Juliano, L., Ulrich, H., & Ferreira, S. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502406200 · Cited by 44 · see citing works

Transgenic mouse model of familial amyloidotic polyneuropathy.

Shimada, K., Maeda, S., Murakami, T., et al. (1989) · PubMed · Cited by 40 · see citing works

Gerstmann-Sträussler-Scheinker Disease Amyloid Protein Polymerizes According to the “Dock-and-Lock” Model

Gobbi, M., Colombo, L., Morbin, M., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506164200 · Cited by 35 · see citing works

Sporadic fatal insomnia with spongiform degeneration in the thalamus and widespread PrPSc deposits in the brain

Piao, Y., Kakita, A., Watanabe, H., et al. (2005) · Neuropathology · doi:10.1111/j.1440-1789.2005.00608.x · Cited by 32 · see citing works

Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers

Vendrely, C., Valadié, H., Bednářová, L., et al. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.05.017 · Cited by 32 · see citing works

Formation of Soluble Oligomers and Amyloid Fibrils with Physical Properties of the Scrapie Isoform of the Prion Protein from the C-terminal Domain of Recombinant Murine Prion Protein mPrP-(121–231)

Martins, S. M., Frosoni, D. J., de Martinez, A. M. B., Felice, F. G. D., & Ferreira, S. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605367200 · Cited by 31 · see citing works

Metastable, Partially Folded States in the Productive Folding and in the Misfolding and Amyloid Aggregation of Proteins

Ferreira, S. T., Felice, F. G. D., & Chapeaurouge, A. D. (2006) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:44:3:539 · Cited by 29 · see citing works

Dual role of glutamatergic neurotransmission on amyloid β1–42 aggregation and neurotoxicity in embryonic avian retina

Louzada, P. R., Paula-Lima, A. C., Mello, F. G. D., & Ferreira, S. T. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01585-3 · Cited by 28 · see citing works

BSE infection in bovine PrP transgenic mice leads to hyperphosphorylation of tau-protein

Bautista, M. J., GUTIERREZ, J., Salguero, F. J., FERNANDEZDEMARCO, M., Romero-Trevejo, J. L., & Gomez-Villamandos, J. C. (2006) · Veterinary Microbiology · doi:10.1016/j.vetmic.2006.02.017 · Cited by 26 · see citing works

Molecular Heterosis of Prion Protein β-Oligomers

Tahiri‐Alaoui, A., Sim, V. L., Caughey, B. W., & James, W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606606200 · Cited by 25 · see citing works

Molecules that Disrupt Memory Circuits in Alzheimer’s Disease: The Attack on Synapses by Aβ Oligomers (ADDLs)

Klein, W. L., Lacor, P. N., Felice, F. G. D., & Ferreira, S. T. (2007) · Research and perspectives in neurosciences · doi:10.1007/978-3-540-45702-2_11 · Cited by 23 · see citing works

Tau protein, the main component of paired helical filaments

Ávila, J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s320 · Cited by 22 · see citing works

Spatial correlations between the vacuolation, prion protein deposition and surviving neurons in variant Creutzfeldt-Jakob Disease (vCJD)

Armstrong, R. A., Lantos, P. L., Ironside, J. W., et al. (2003) · Journal of Neural Transmission · doi:10.1007/s00702-003-0039-1 · Cited by 22 · see citing works

Dequalinium-induced Protofibril Formation of α-Synuclein*

Lee, C., Kim, H. J., Lee, J.-H., Cho, H.-J., Kim, J., Chung, K., Jung, S., & Paik, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m505307200 · Cited by 21 · see citing works

Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: an atomic force microscopy study.

Relini, A., Rolandi, R., Bolognesi, M., Aboudan, M., Merlini, G., Bellotti, V., & Gliozzi, A. (2004) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2004.04.007 · Cited by 19 · see citing works

Interaction of Prion Protein with Small Highly Structured RNAs: Detection and Characterization of PrP-Oligomers

Vasan, S., Mong, P. Y., & Grossman, A. I. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9063-5 · Cited by 14 · see citing works

Oligomeric forms of peptide fragment PrP(214–226) in solution are preferentially recognized by PrPSc-specific antibody

Ulrih, N. P., Skrt, M., Veranič, P., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.04.046 · Cited by 12 · see citing works

Prion (PrPSc)-Specific epitope defined by a monoclonal antibody

(1998) · Transfusion Medicine Reviews · doi:10.1016/s0887-7963(98)80077-1 · Cited by 11 · see citing works

Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques

(1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90094-m · Cited by 7 · see citing works

Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Aβ oligomers

De Felice, F. G., Vieira, M. N. N., Bomfim, T. R., Decker, H., Velasco, P. T., Lambert, M. P., Viola, K. L., Zhao, W.-Q., Ferreira, S. T., & Klein, W. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809158106 · Cited by 657 · see citing works

Alzheimer's disease, β‐amyloid, glutamate, NMDA receptors and memantine – searching for the connections

Danysz, W., & Parsons, C. G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02057.x · Cited by 500 · see citing works

The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease

Ferreira, S. T., & Klein, W. L. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.08.003 · Cited by 442 · see citing works

Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer’s disease

Ferreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373 · see citing works

Mesenchymal stem cells and cell-derived extracellular vesicles protect hippocampal neurons from oxidative stress and synapse damage induced by amyloid-β oligomers

de Godoy, M. A., Saraiva, L. M., de Carvalho, L. R. P., Vasconcelos-dos-Santos, A., Beiral, H. J. V., Ramos, A. B., Silva, L. R. D. P., Leal, R. B., Monteiro, V. H. S., Braga, C. V., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.807180 · Cited by 214 · see citing works

Neuroprotective Effects of Resveratrol Against Aβ Administration in Rats are Improved by Lipid-Core Nanocapsules

Frozza, R. L., Bernardi, A., Hoppe, J. B., Meneghetti, A. B., Matté, A., Battastini, A. M. O., Pohlmann, A. R., Guterres, S. S., & Salbego, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8401-2 · Cited by 165 · see citing works

The Role of Tau Oligomers in the Onset of Alzheimer's Disease Neuropathology

Cárdenas-Aguayo, M. D. C., Gómez-Virgilio, L., DeRosa, S., & Meraz-Ríos, M. A. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500148z · Cited by 120 · see citing works

The pathophysiology of defective proteostasis in the hypothalamus — from obesity to ageing

Cavadas, C., Aveleira, C. A., Souza, G. F. P., & Velloso, L. A. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.107 · Cited by 105 · see citing works

Val8-glucagon-like peptide-1 protects against Aβ1–40-induced impairment of hippocampal late-phase long-term potentiation and spatial learning in rats

Wang, X. H., Li, L., Hölscher, C., Pan, Y. F., Chen, X. R., & Qi, J. S. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.08.028 · Cited by 99 · see citing works

Activation of D1/D5 Dopamine Receptors Protects Neurons from Synapse Dysfunction Induced by Amyloid-β Oligomers

Jürgensen, S., Antonio, L. L., Mussi, G. E. A., Brito-Moreira, J., Bomfim, T. R., De Felice, F. G., Garrido-Sanabria, E. R., Cavalheiro, É. A., & Ferreira, S. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177790 · Cited by 88 · see citing works

Amyloid-beta oligomers increase the localization of prion protein at the cell surface: PrPC trafficking and Alzheimer’s disease

Caetano, F. A., Beraldo, F. H., Hajj, G. N. M., Guimaraes, A. L., Jürgensen, S., Wasilewska-Sampaio, A. P., Hirata, P. H. F., Souza, I., Machado, C. F., Wong, D. Y.-L., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07225.x · Cited by 74 · see citing works

An Unbalanced Synaptic Transmission: Cause or Consequence of the Amyloid Oligomers Neurotoxicity?

Sciaccaluga, M., Megaro, A., Bellomo, G., Ruffolo, G., Romoli, M., Palma, E., & Costa, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115991 · Cited by 70 · see citing works

Brain insulin, insulin‐like growth factor 1 and glucagon‐like peptide 1 signalling in Alzheimer’s disease

Ferreira, S. T. (2021) · Journal of Neuroendocrinology · doi:10.1111/jne.12959 · Cited by 59 · see citing works

Delineation of Neuroprotective Effects and Possible Benefits of AntioxidantsTherapy for the Treatment of Alzheimer's Diseases by Targeting Mitochondrial-Derived Reactive Oxygen Species: Bench to Bedside

Walia, V., Kaushik, D., Mittal, V., Kumar, K., Verma, R., Parashar, J., Akter, R., Rahman, M. H., Bhatia, S., Al-Harrasi, A., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02617-1 · Cited by 47 · see citing works

Dendritic and axonal mechanisms of Ca²⁺ elevation impair BDNF transport in Aβ oligomer–treated hippocampal neurons

Gan, K. J., & Silverman, M. A. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-12-1612 · Cited by 41 · see citing works

Amyloid β protein toxicity mediated by the formation of amyloid‐β protein precursor complexes

Lu, D. C.-T., Shaked, G. M., Masliah, E., Bredesen, D. E., & Koo, E. H. (2003) · Annals of Neurology · doi:10.1002/ana.10761 · Cited by 91 · see citing works

Gene knockout of amyloid precursor protein and amyloid precursor‐like protein‐2 increases cellular copper levels in primary mouse cortical neurons and embryonic fibroblasts

Bellingham, S. A., Ciccotosto, G. D., Needham, B. E., Fodero, L. R., White, A. R., Masters, C. L., Cappai, R., & Camakaris, J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02731.x · Cited by 100 · see citing works

The Amyloid β Precursor Protein and Cognitive Function in Alzheimer’s Disease

Marr, R. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802851-3.00004-8 · Cited by 2 · see citing works

The processing and biological function of the human amyloid precursor protein (APP): lessons from different cellular models

Kienlen‐Campard, P., Tasiaux, B., & Octave, J. N. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00170-4 · Cited by 10 · see citing works

Secretory processing of the Alzheimer amyloid βA4 protein precursor is increased by protein phosphorylation

Gillespie, S. L., Golde, T. E., & Younkin, S. G. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90442-n · Cited by 107 · see citing works