P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders

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 · see citing works

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · 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

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

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

Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo

Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G. P., Davies, S. W., Lehrach, H., & Wanker, E. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80514-0 · Cited by 1,291 · see citing works

Chaperone Suppression of α-Synuclein Toxicity in a <i>Drosophila</i> Model for Parkinson's Disease

Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227 · see citing works

Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models

Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works

Amyloid β-Protein Fibrillogenesis

Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046 · see citing works

Sequence of Deposition of Heterogeneous Amyloid β-Peptides and APO E in Down Syndrome: Implications for Initial Events in Amyloid Plaque Formation

Lemere, C. A., Blusztajn, J. K., Yamaguchi, H., Wisniewski, T., Saido, T. C., & Selkoe, D. J. (1996) · Neurobiology of Disease · doi:10.1006/nbdi.1996.0003 · Cited by 584 · see citing works

β-Synuclein Inhibits α-Synuclein Aggregation

Hashimoto, M., Rockenstein, E., Mante, M., Mallory, M., & Masliah, E. (2001) · Neuron · doi:10.1016/s0896-6273(01)00462-7 · Cited by 398 · see citing works

Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies

Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349 · see citing works

Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats

Perutz, M. F., & Windle, A. H. (2001) · Nature · doi:10.1038/35084141 · Cited by 199 · see citing works

Protein folding and misfolding

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

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 · see citing works

The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687 · see citing works

Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases

Soto, C., & Pritzkow, S. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0235-9 · Cited by 1,180 · see citing works

Multi-target-Directed Ligands To Combat Neurodegenerative Diseases

Cavalli, A., Bolognesi, M. L., Minarini, A., Rosini, M., Tumiatti, V., Recanatini, M., & Melchiorre, C. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm7009364 · Cited by 1,152 · 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

TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021 · 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

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

Opposing activities protect against age-onset proteotoxicity

Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W., & Dillin, A. (2006) · Science · doi:10.1126/science.1124646 · Cited by 843 · see citing works

HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin.

Iwata, A., Riley, B. E., Johnston, J. A., & Kopito, R. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508786200 · Cited by 719 · see citing works

Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs

Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y. (2004) · Nature Medicine · doi:10.1038/nm1113 · Cited by 715 · see citing works

Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641 · see citing works

Globular amyloid β‐peptide ₁₋₄₂ oligomer − a homogenous and stable neuropathological protein in Alzheimer's disease

Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559 · see citing works

Reduced IGF-1 signaling delays age-associated proteotoxicity in mice

Cohen, E., Paulsson, J. F., Blinder, P., Burstyn-Cohen, T., Du, D., Estepa, G., Adame, A., Pham, H. M., Holzenberger, M., Kelly, J. W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.11.014 · Cited by 488 · see citing works

Amyloid toxicity in Alzheimer’s disease

Reiss, A. B., Arain, H. A., Stecker, M. M., Siegart, N. M., & Kasselman, L. J. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0063 · Cited by 447 · see citing works

Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples

Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works

Aβ40 Inhibits Amyloid Deposition<i>In Vivo</i>

Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D. W., Golde, T., & McGowan, E. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4849-06.2007 · Cited by 359 · see citing works

Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering

Sandberg, A., Luheshi, L. M., Söllvander, S., Pereira de Barros, T., Macao, B., Knowles, T. P. J., Biverstål, H., Lendel, C., Ekholm-Petterson, F., Dubnovitsky, A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001740107 · Cited by 358 · see citing works

Sensitive ELISA detection of amyloid‐β protofibrils in biological samples

Englund, H., Sehlin, D., Johansson, A., Nilsson, L. N. G., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04759.x · Cited by 292 · see citing works

The role of G protein-coupled receptors in the pathology of Alzheimer's disease

Thathiah, A., & De Strooper, B. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2977 · Cited by 288 · see citing works

The Ratio of Monomeric to Aggregated Forms of Aβ40 and Aβ42 Is an Important Determinant of Amyloid-β Aggregation, Fibrillogenesis, and Toxicity

Jan, A., Gokce, O., Luthi-Carter, R., & Lashuel, H. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803159200 · Cited by 291 · see citing works

Prions and their partners in crime

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

Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission

Moreno-Gonzalez, I., & Soto, C. (2011) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2011.04.002 · Cited by 252 · see citing works

Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease

Overk, C. R., & Masliah, E. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.015 · Cited by 242 · see citing works

Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers

Luibl, V. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25843 · Cited by 203 · 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

Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer’s disease immunotherapeutics

Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research &amp; Therapy · doi:10.1186/alzrt272 · Cited by 190 · see citing works

Neuronal Cell Death in Alzheimers Disease and a Neuroprotective Factor, Humanin

Niikura, T., Tajima, H., & Kita, Y. (2006) · Current Neuropharmacology · doi:10.2174/157015906776359577 · Cited by 184 · see citing works

The Complex Molecular Biology of Amyotrophic Lateral Sclerosis (ALS)

Redler, R. L., & Dokholyan, N. V. (2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00002-3 · Cited by 172 · see citing works

A Genomewide RNA Interference Screen for Modifiers of Aggregates Formation by Mutant Huntingtin in Drosophila

Zhang, S., Binari, R., Zhou, R., & Perrimon, N. (2010) · Genetics · doi:10.1534/genetics.109.112516 · Cited by 160 · see citing works

Metabolic Activity Determines Efficacy of Macroautophagic Clearance of Pathological Oligomeric α-Synuclein

Yu, W. H., Dorado, B., Figueroa, H. Y., Wang, L., Planel, E., Cookson, M. R., Clark, L. N., & Duff, K. E. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080928 · Cited by 155 · see citing works

Seeding selectivity and ultrasensitive detection of tau aggregate conformers of Alzheimer disease

Kraus, A., Saijo, E., Metrick, M. A., Newell, K., Sigurdson, C. J., Zanusso, G., Ghetti, B., & Caughey, B. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1947-3 · Cited by 143 · see citing works

Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models

Levites, Y., Smithson, L. A., Price, R. W., Dakin, R. S., Yuan, B., Sierks, M. R., Kim, J., McGowan, E., Kim Reed, D., Rosenberry, T. L., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-6463fje · Cited by 113 · see citing works

Protein aggregation mediates stoichiometry of protein complexes in aneuploid cells

Brennan, C. M., Vaites, L. P., Wells, J. N., Santaguida, S., Paulo, J. A., Storchova, Z., Harper, J. W., Marsh, J. A., & Amon, A. (2019) · Genes &amp; Development · doi:10.1101/gad.327494.119 · Cited by 109 · see citing works

Ablation of TNF-RI/RII Expression in Alzheimer's Disease Mice Leads to an Unexpected Enhancement of Pathology

Montgomery, S. L., Mastrangelo, M. A., Habib, D., Narrow, W. C., Knowlden, S. A., Wright, T. W., & Bowers, W. J. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.07.001 · Cited by 96 · see citing works

Proteinopathy-induced neuronal senescence: a hypothesis for brain failure in Alzheimer’s and other neurodegenerative diseases

Golde, T. E., & Miller, V. M. (2009) · Alzheimer's Research &amp; Therapy · doi:10.1186/alzrt5 · Cited by 98 · see citing works

Prion Strain Differences in Accumulation of PrPSc on Neurons and Glia Are Associated with Similar Expression Profiles of Neuroinflammatory Genes: Comparison of Three Prion Strains

Carroll, J. A., Striebel, J. F., Rangel, A., Woods, T., Phillips, K., Peterson, K. E., Race, B., & Chesebro, B. (2016) · PLOS Pathogens · doi:10.1371/journal.ppat.1005551 · Cited by 92 · see citing works

17-AAG Induces Cytoplasmic α-Synuclein Aggregate Clearance by Induction of Autophagy

Riedel, M., Goldbaum, O., Schwarz, L., Schmitt, S., & Richter-Landsberg, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008753 · Cited by 87 · see citing works

RNA-seq and network analysis reveal unique glial gene expression signatures during prion infection

Carroll, J. A., Race, B., Williams, K., Striebel, J., & Chesebro, B. (2020) · Molecular Brain · doi:10.1186/s13041-020-00610-8 · Cited by 66 · see citing works

The novel vaccine peptide GV1001 effectively blocks β-amyloid toxicity by mimicking the extra-telomeric functions of human telomerase reverse transcriptase

Park, H.-H., Lee, K.-Y., Kim, S., Lee, J. W., Choi, N.-Y., Lee, E.-H., Lee, Y. J., Lee, S.-H., & Koh, S.-H. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.12.015 · Cited by 72 · see citing works

Cross Currents in Protein Misfolding Disorders: Interactions and Therapy

Morales, R., Green, K., & Soto, C. (2009) · CNS &amp; Neurological Disorders - Drug Targets · doi:10.2174/187152709789541998 · Cited by 72 · 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

Genetic Variation in N-Methyl-D-Aspartate Receptor Subunit NR3A but Not NR3B Influences Susceptibility to Alzheimer’s Disease

Liu, H.-P., Lin, W.-Y., Liu, S.-H., Wang, W.-F., Tsai, C.-H., Wu, B.-T., Wang, C.-K., & Tsai, F.-J. (2009) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000254757 · Cited by 29 · see citing works

A chemical screening approach reveals that indole fluorescence is quenched by pre-fibrillar but not fibrillar amyloid-β

Reinke, A. A., Seh, H. Y., & Gestwicki, J. E. (2009) · Bioorganic &amp; Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.07.082 · Cited by 26 · see citing works

Cellular maintenance of nuclear protein homeostasis.

Gallagher, P. S., Oeser, M. L., Abraham, A.-C., Kaganovich, D., & Gardner, R. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1530-y · Cited by 22 · see citing works

In vitro anti-cholinesterase and cognitive enhancing properties of essential oils from Piper nigrum L. and Monodora myristica (Gaertn) dunal

I J, O., S A, N., E E, E., F S, B., & E M, O. (2018) · International Journal of Pharmacology and Toxicology · doi:10.14419/ijpt.v6i2.13578 · Cited by 2 · see citing works