Implications of peptide assemblies in amyloid diseases

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

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α-Synuclein in Lewy bodies

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Protein folding and misfolding

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

The Association Between Quantitative Measures of Dementia and of Senile Change in the Cerebral Grey Matter of Elderly Subjects

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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

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

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The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease

Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

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

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The amyloid state and its association with protein misfolding diseases.

Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382

Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo

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

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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

Alzheimer’s disease drug-development pipeline: Few candidates, frequent failures

Cummings, J. L., Morstorf, T., & Zhong, K. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt269 · Cited by 1,744

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

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

Rapid induction of Alzheimer A beta amyloid formation by zinc

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-Synuclein in Parkinson's Disease

Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

Bartels, T., Choi, J. G., & Selkoe, D. J. (2011) · Nature · doi:10.1038/nature10324 · Cited by 1,263

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

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111

Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation

Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096

Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044

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

Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins

Wang, X., Su, B., Siedlak, S. L., Moreira, P. I., Fujioka, H., Wang, Y., Casadesus, G., & Zhu, X. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804871105 · Cited by 835

Structural Classification of Toxic Amyloid Oligomers

Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783

Metals and neuroscience

Bush, A. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00073-3 · Cited by 731

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652

Physiology of the prion protein

Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617

The redox chemistry of the Alzheimer's disease amyloid β peptide

Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608

Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer's disease

D'Amelio, M., Cavallucci, V., Middei, S., Marchetti, C., Pacioni, S., Ferri, A., Diamantini, A., De Zio, D., Carrara, P., Battistini, L., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2709 · Cited by 572

Loss-of-function mutations in SLC30A8 protect against type 2 diabetes

Go-T2D Consortium, Flannick, J., T2D-GENES Consortium, Thorleifsson, G., Beer, N. L., Jacobs, S. B. R., Grarup, N., Burtt, N. P., Mahajan, A., Fuchsberger, C., et al. (2014) · Nature Genetics · doi:10.1038/ng.2915 · Cited by 492

Kuru in the 21st century—an acquired human prion disease with very long incubation periods

Collinge, J., Whitfield, J., McKintosh, E., Beck, J., Mead, S., Thomas, D. J., & Alpers, M. P. (2006) · The Lancet · doi:10.1016/s0140-6736(06)68930-7 · Cited by 427

Increased β-Cell Apoptosis Prevents Adaptive Increase in β-Cell Mass in Mouse Model of Type 2 Diabetes

Butler, A. E., Janson, J., Soeller, W. C., & Butler, P. C. (2003) · Diabetes · doi:10.2337/diabetes.52.9.2304 · Cited by 411

The Secreted β-Amyloid Precursor Protein Ectodomain APPsα Is Sufficient to Rescue the Anatomical, Behavioral, and Electrophysiological Abnormalities of APP-Deficient Mice

Ring, S., Weyer, S. W., Kilian, S. B., Waldron, E., Pietrzik, C. U., Filippov, M. A., Herms, J., Buchholz, C., Eckman, C. B., Korte, M., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.1026-07.2007 · Cited by 390

Prions and their partners in crime

Caughey, B., & Baron, G. S. (2006) · Nature · doi:10.1038/nature05294 · Cited by 295

Prion protein attenuates excitotoxicity by inhibiting NMDA receptors

Khosravani, H., Zhang, Y., Tsutsui, S., Hameed, S., Altier, C., Hamid, J., Chen, L., Villemaire, M., Ali, Z., Jirik, F. R., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200711002 · Cited by 275

Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease

Mandelkow, E., Von Bergen, M., Biernat, J., & Mandelkow, E. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00053.x · Cited by 243

The Amyloid Formation Mechanism in Human IAPP: Dimers Have β-Strand Monomer−Monomer Interfaces

Dupuis, N. F., Wu, C., Shea, J.-E., & Bowers, M. T. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1081537 · Cited by 216

Pathogenesis of prion diseases: current status and future outlook

Aguzzi, A., & Heikenwalder, M. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1492 · Cited by 207

The role of peptides and receptors of the calcitonin family in the regulation of bone metabolism

Naot, D., & Cornish, J. (2008) · Bone · doi:10.1016/j.bone.2008.07.003 · Cited by 182

Islet amyloid polypeptide toxicity and membrane interactions

Cao, P., Abedini, A., Wang, H., Tu, L.-H., Zhang, X., Schmidt, A. M., & Raleigh, D. P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305517110 · Cited by 146

A Physiological Role for Amyloid-β Protein: Enhancement of Learning and Memory

Morley, J. E., Farr, S. A., Banks, W. A., Johnson, S. N., Yamada, K. A., & Xu, L. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-1230 · Cited by 141

Immunotherapy for neurodegenerative diseases: Focus on α-synucleinopathies

Valera, E., & Masliah, E. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.013 · Cited by 132

Methionine-35 of A β (1–42): Importance for Oxidative Stress in Alzheimer Disease

Butterfield, D. A., & Sultana, R. (2011) · Journal of Amino Acids · doi:10.4061/2011/198430 · Cited by 124

Quantification of Modified Amyloid β Peptides in Alzheimer Disease and Down Syndrome Brains

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Ultrastructural Localization of Intraneuronal Aβ-Peptide in Alzheimer Disease Brains

Gómez-Ramos, P., & Asunción Morán, M. (2007) · Journal of Alzheimer's Disease · doi:10.3233/jad-2007-11109 · Cited by 76

A Decade of the Protein Corona

Ke, P. C., Lin, S., Parak, W. J., Davis, T. P., & Caruso, F. (2017) · ACS Nano · doi:10.1021/acsnano.7b08008 · Cited by 672

Multicomponent peptide assemblies

Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 346

Detection of amyloid fibrils in Parkinson’s disease using plasmonic chirality

Kumar, J., Eraña, H., López-Martínez, E., Claes, N., Martín, V. F., Solís, D. M., Bals, S., Cortajarena, A. L., Castilla, J., & Liz-Marzán, L. M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721690115 · Cited by 312