Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s disease

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

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

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

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

Memantine in Moderate-to-Severe Alzheimer's Disease

Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043

Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)

Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774

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

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

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

Intraneuronal Aβ42 Accumulation in Human Brain

Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991

Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology

GERAD consortium, Chapuis, J., Hansmannel, F., Gistelinck, M., Mounier, A., Van Cauwenberghe, C., Kolen, K. V., Geller, F., Sottejeau, Y., Harold, D., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.1 · Cited by 407

Review on Alzheimer’s Disease: Inhibition of Amyloid Beta and Tau Tangle Formation

Ashrafian, H., Zadeh, E. H., & Khan, R. H. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.192 · Cited by 368

Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity

Friedrich, R. P., Tepper, K., Rönicke, R., Soom, M., Westermann, M., Reymann, K., Kaether, C., & Fändrich, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904532106 · Cited by 303

Drosophila melanogaster as a model organism for Alzheimer’s disease

Prüßing, K., Voigt, A., & Schulz, J. B. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-35 · Cited by 235

Inhibition of GSK-3 Ameliorates Aβ Pathology in an Adult-Onset Drosophila Model of Alzheimer's Disease

Sofola, O., Kerr, F., Rogers, I., Killick, R., Augustin, H., Gandy, C., Allen, M. J., Hardy, J., Lovestone, S., & Partridge, L. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001087 · Cited by 174

Sleep Interacts with Aβ to Modulate Intrinsic Neuronal Excitability

Tabuchi, M., Lone, S. R., Liu, S., Liu, Q., Zhang, J., Spira, A. P., & Wu, M. N. (2015) · Current Biology · doi:10.1016/j.cub.2015.01.016 · Cited by 165

Expression of β-Amyloid Induced Age-Dependent Presynaptic and Axonal Changes in Drosophila

Zhao, X.-L., Wang, W.-A., Tan, J.-X., Huang, J.-K., Zhang, X., Zhang, B.-Z., Wang, Y.-H., YangCheng, H.-Y., Zhu, H.-L., Sun, X.-J., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3699-09.2010 · Cited by 130

Traumatic injury induces stress granule formation and enhances motor dysfunctions in ALS/FTD models

Anderson, E. N., Gochenaur, L., Singh, A., Grant, R., Patel, K., Watkins, S., Wu, J. Y., & Pandey, U. B. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy047 · Cited by 96

Mechanism of Neuronal versus Endothelial Cell Uptake of Alzheimer's Disease Amyloid β Protein

Kandimalla, K. K., Scott, O. G., Fulzele, S., Davidson, M. W., & Poduslo, J. F. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004627 · Cited by 88

Aβ exacerbates the neuronal dysfunction caused by human tau expression in a Drosophila model of Alzheimer's disease

Folwell, J., Cowan, C. M., Ubhi, K. K., Shiabh, H., Newman, T. A., Shepherd, D., & Mudher, A. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.09.014 · Cited by 83

Modeling the complex pathology of Alzheimer's disease in Drosophila

Fernandez-Funez, P., de Mena, L., & Rincon-Limas, D. E. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.013 · Cited by 69

Central and peripheral circadian clocks and their role in Alzheimer's disease

Chauhan, R., Chen, K.-F., Kent, B. A., & Crowther, D. C. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.030627 · Cited by 58

p62 Plays a Protective Role in the Autophagic Degradation of Polyglutamine Protein Oligomers in Polyglutamine Disease Model Flies

Saitoh, Y., Fujikake, N., Okamoto, Y., Popiel, H. A., Hatanaka, Y., Ueyama, M., Suzuki, M., Gaumer, S., Murata, M., Wada, K., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.590281 · Cited by 55

A Drosophila Model of Alzheimer's Disease

Crowther, D. C., Page, R., Chandraratna, D., & Lomas, D. A. (2006) · Methods in Enzymology · doi:10.1016/s0076-6879(06)12015-7 · Cited by 55

Parp mutations protect from mitochondrial toxicity in Alzheimer’s disease

Yu, Y., Fedele, G., Celardo, I., Loh, S. H. Y., & Martins, L. M. (2021) · Cell Death & Disease · doi:10.1038/s41419-021-03926-y · Cited by 46

Neuroprotective Effects of PARP Inhibitors in Drosophila Models of Alzheimer’s Disease

Maggiore, A., Casale, A. M., Toscanelli, W., Cappucci, U., Rotili, D., Grieco, M., Gagné, J.-P., Poirier, G. G., d’Erme, M., & Piacentini, L. (2022) · Cells · doi:10.3390/cells11081284 · Cited by 40

Integrated biology approach reveals molecular and pathological interactions among Alzheimer’s Aβ42, Tau, TREM2, and TYROBP in Drosophila models

Sekiya, M., Wang, M., Fujisaki, N., Sakakibara, Y., Quan, X., Ehrlich, M. E., De Jager, P. L., Bennett, D. A., Schadt, E. E., Gandy, S., et al. (2018) · Genome Medicine · doi:10.1186/s13073-018-0530-9 · Cited by 38

Detoxification of amyloid β fibrils by curcumin derivatives and their verification in a Drosophila Alzheimer's model

Utomo, R. Y., Sugie, A., Okada, S., Miura, K., & Nakamura, H. (2022) · Chemical Communications · doi:10.1039/d1cc07000b · Cited by 18

TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models

Roy, B., Contu, V. R., Jeziorek, M., Friedman, W. J., & Wong, C.-O. (2026) · doi:10.64898/2026.10.21.760809