The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy

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

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works

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

Toward defining the preclinical stages of Alzheimer’s disease: Recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease

Sperling, R. A., Aisen, P. S., Beckett, L. A., Bennett, D. A., Craft, S., Fagan, A. M., Iwatsubo, T., Jack, C. R., Kaye, J., Montine, T. J., et al. (2011) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.03.003 · Cited by 7,155 · see citing works

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 6,435 · see citing works

2016 Alzheimer's disease facts and figures

Alzheimer's Association (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.001 · Cited by 5,069 · see citing works

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice

Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210 · 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

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

A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline

Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738 · see citing works

Phase 3 Trials of Solanezumab for Mild-to-Moderate Alzheimer's Disease

Doody, R. S., Thomas, R. G., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., Raman, R., Sun, X., Aisen, P. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1312889 · Cited by 1,668 · see citing works

2015 Alzheimer's disease facts and figures

Alzheimer's Association (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.02.003 · Cited by 1,641 · see citing works

Depletion of microglia and inhibition of exosome synthesis halt tau propagation

Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560 · see citing works

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

Cohen, S. I. A., Linse, S. S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,410 · see citing works

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 · 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

The Genetics of Alzheimer Disease: Back to the Future

Bertram, L., Lill, C. M., & Tanzi, R. E. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.013 · Cited by 834 · see citing works

Three dimensions of the amyloid hypothesis: time, space and 'wingmen'

Musiek, E. S., & Holtzman, D. M. (2015) · Nature Neuroscience · doi:10.1038/nn.4018 · Cited by 697 · see citing works

An overview of APP processing enzymes and products.

Chow, V. W., Mattson, M. P., Wong, P. C., & Gleichmann, M. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8104-z · Cited by 684 · see citing works

Soluble Aβ Oligomers Inhibit Long-Term Potentiation through a Mechanism Involving Excessive Activation of Extrasynaptic NR2B-Containing NMDA Receptors

Li, S., Jin, M., Koeglsperger, T., Shepardson, N. E., Shankar, G. M., & Selkoe, D. J. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0203-11.2011 · Cited by 664 · see citing works

DT‐01‐04: The efficacy of RVT‐101, a 5‐ht6 receptor antagonist, as an adjunct to donepezil in adults with mild‐to‐moderate Alzheimer's disease: Completer analysis of a phase 2b study

Lombardo, I., Ramaswamy, G., Piscitelli, S. C., & Friedhoff, L. T. (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.08.154 · Cited by 656 · see citing works

Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons

Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A. O., Wısnıewskı, T., Gunther, E. C., & Strittmatter, S. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3178 · Cited by 654 · see citing works

Common mechanisms of amyloid oligomer pathogenesis in degenerative disease

Glabe, C. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.04.017 · Cited by 569 · see citing works

A causative link between the structure of aberrant protein oligomers and their toxicity

Campioni, S., Mannini, B., Zampagni, M., Pensalfini, A., Parrini, C., Evangelisti, E., Relini, A., Stefani, M., Dobson, C. M., Cecchi, C., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.283 · Cited by 552 · see citing works

The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain

Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 502 · see citing works

Presenilins and -Secretase: Structure, Function, and Role in Alzheimer DiseasePreprint

Strooper, B. D., Iwatsubo, T., & Wolfe, M. S. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006304 · Cited by 465 · see citing works

A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: the pattern of spread is determined by connectivity, not proximity

Ahmed, Z., Cooper, J., Murray, T. K., Garn, K., McNaughton, E., Clarke, H., Parhizkar, S., Ward, M. A., Cavallini, A., Jackson, S., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1254-6 · Cited by 460 · see citing works

Alzheimer's disease

Mucke, L. (2009) · Nature · doi:10.1038/461895a · Cited by 456 · see citing works

The contribution of neuroinflammation to amyloid toxicity in Alzheimer's disease

Minter, M. R., Taylor, J. M., & Crack, P. J. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13411 · Cited by 451 · see citing works

Molecular Mechanisms of Amyloid Oligomers Toxicity

Kayed, R., & Lasagna‐Reeves, C. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129001 · Cited by 417 · see citing works

Brain amyloid-β oligomers in ageing and Alzheimer’s disease

Lesné, S., Sherman, M. A., Grant, M. K. O., Kuskowski, M. A., Schneider, J. A., Bennett, D. A., & Ashe, K. H. (2013) · Brain · doi:10.1093/brain/awt062 · Cited by 407 · see citing works

Neurodegenerative Diseases: Expanding the Prion Concept

Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361 · see citing works

α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration

Tran, H., Chung, C. H.-Y., Iba, M., Zhang, B., Trojanowski, J. Q., Luk, K. C., & Lee, V. M. ‐. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.033 · Cited by 324 · see citing works

Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites

Freir, D. B., Nicoll, A. J., Klyubin, I. V., Panico, S., Donald, J. M. M., Risse, E., Asante, E. A., Farrow, M. A., Sessions, R. B., Saibil, H. R., et al. (2011) · Nature Communications · doi:10.1038/ncomms1341 · Cited by 290 · see citing works

Mild cognitive impairment due to Alzheimer disease in the community

Petersen, R. C., Aisen, P., Boeve, B. F., Geda, Y. E., Ivnik, R. J., Knopman, D. S., Mielke, M., Pankratz, V. S., Roberts, R., Rocca, W. A., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23931 · Cited by 265 · see citing works

Amyloid β-Protein Dimers Rapidly Form Stable Synaptotoxic Protofibrils

O'Nuallain, B., Freir, D. B., Nicoll, A. J., Risse, E., Ferguson, N., Herron, C. E., Collinge, J., & Walsh, D. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3537-10.2010 · Cited by 259 · see citing works

Differential induction and spread of tau pathology in young PS19 tau transgenic mice following intracerebral injections of pathological tau from Alzheimer’s disease or corticobasal degeneration brains

Boluda, S., Iba, M., Zhang, B., Raible, K. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1373-0 · Cited by 259 · see citing works

Soluble Aβ Seeds Are Potent Inducers of Cerebral β-Amyloid Deposition

Langer, F., Eisele, Y. S., Fritschi, S. K., Staufenbiel, M., Walker, L. C., & Jucker, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3088-11.2011 · Cited by 237 · see citing works

Tau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation

Mirbaha, H., Holmes, B. B., Sanders, D. W., Bieschke, J., & Diamond, M. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.652693 · Cited by 215 · see citing works

Distinct Early Folding and Aggregation Properties of Alzheimer Amyloid-β Peptides Aβ40 and Aβ42

Chen, Y., & Glabe, C. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602363200 · Cited by 214 · see citing works

Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients

Fang, Y.-S., Tsai, K., Chang, Y.-J., Kao, P. F., Woods, R., Kuo, P. H., Wu, C., Liao, J., Chou, S.-C., Lin, V., et al. (2014) · Nature Communications · doi:10.1038/ncomms5824 · Cited by 211 · see citing works

Mechanisms of Amyloid-β Peptide Clearance: Potential Therapeutic Targets for Alzheimer's Disease

Yoon, S.-S., & AhnJo, S.-M. (2012) · Biomolecules and Therapeutics · doi:10.4062/biomolther.2012.20.3.245 · Cited by 205 · cited 1× · see citing works

Targeting the neurotoxic species in Alzheimer's disease: inhibitors of Aβ oligomerization

Felice, F. G. D., Vieira, M. N. N., Saraiva, L. M., Figueroa‐Villar, J. D., Garcia-Abreu, J., Liu, R., Chang, L., Klein, W. L., & Ferreira, S. T. (2004) · The FASEB Journal · doi:10.1096/fj.04-1764com · Cited by 193 · 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 & Therapy · doi:10.1186/alzrt272 · Cited by 190 · see citing works

Solution State Characterization of Amyloid β-Derived Diffusible Ligands

Hepler, R. W., Grimm, K. M., Nahas, D. D., Breese, R., Chen-Dodson, E., Acton, P. J., Keller, P. M., Yeager, M. D., Wang, H., Shughrue, P. J., et al. (2006) · Biochemistry · doi:10.1021/bi061850f · Cited by 181 · see citing works

Pathological Interface Between Oligomeric Alpha-Synuclein and Tau in Synucleinopathies

Sengupta, U., Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Lasagna‐Reeves, C. A., Gerson, J. E., Paulucci-Holthauzen, A. A., Krishnamurthy, S., Farhed, M., Jackson, G. R., & Kayed, R. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.12.019 · Cited by 181 · see citing works

Conformation‐Dependent Anti‐Amyloid Oligomer Antibodies

Kayed, R., & Glabe, C. G. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)13017-7 · Cited by 165 · see citing works

Plaque-bearing mice with reduced levels of oligomeric amyloid-β assemblies have intact memory function

Lesné, S., Kotilinek, L., & Ashe, K. H. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.054 · Cited by 159 · see citing works

Invited review: Prion‐like transmission and spreading of tau pathology

Clavaguera, F., Hench, J., Goedert, M., & Tolnay, M. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12197 · Cited by 156 · see citing works

Factors associated with resistance to dementia despite high Alzheimer disease pathology

Erten‐Lyons, D., Woltjer, R. L., Dodge, H. H., Nixon, R. A., Vorobik, R., Calvert, J. F., Leahy, M., Montine, T. J., & Kaye, J. A. (2009) · Neurology · doi:10.1212/01.wnl.0000341273.18141.64 · Cited by 148 · see citing works

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration

Liu, P., Reed, M. N., Kotilinek, L., Grant, M. K. O., Forster, C. L., Qiang, W., Shapiro, S. L., Reichl, J. H., Chiang, A. C. A., Jankowsky, J. L., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.05.021 · Cited by 143 · see citing works

Passive Immunization with Phospho-Tau Antibodies Reduces Tau Pathology and Functional Deficits in Two Distinct Mouse Tauopathy Models

Sankaranarayanan, S., Barten, D. M., Vana, L., Devidze, N., Yang, L., Cadelina, G. W., Hoque, N., DeCarr, L. B., Keenan, S., Lin, A., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125614 · Cited by 143 · see citing works

Synaptotoxic Amyloid-β Oligomers: A Molecular Basis for the Cause, Diagnosis, and Treatment of Alzheimer's Disease?

Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 141 · see citing works

Days to criterion as an indicator of toxicity associated with human Alzheimer amyloid‐β oligomers

Gandy, S., Simon, A. J., Steele, J., Lublin, A. L., Lah, J. J., Walker, L. C., Levey, A. I., Krafft, G. A., Levy, E., Checler, F., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22052 · Cited by 137 · see citing works

Formation and Propagation of Tau Oligomeric Seeds

Gerson, J. E., & Kayed, R. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00093 · Cited by 137 · see citing works

Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain

Lasagna‐Reeves, C. A., Glabe, C. G., & Kayed, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.236257 · Cited by 136 · see citing works

Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane

Jang, H., Connelly, L. S., Arce, F. T., Ramachandran, S., Kagan, B. L., Lal, R., & Nussinov, R. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300916f · Cited by 133 · see citing works

Immunotherapeutic Approaches Targeting Amyloid-β, α-Synuclein, and Tau for the Treatment of Neurodegenerative Disorders

Valera, E., Spencer, B. J., & Masliah, E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0397-z · Cited by 129 · see citing works

Dynamic Analysis of Amyloid β-Protein in Behaving Mice Reveals Opposing Changes in ISF versus Parenchymal Aβ during Age-Related Plaque Formation

Hong, S., Quintero-Monzon, O., Ostaszewski, B. L., Podlisny, D. R., Cavanaugh, W. T., Yang, T., Holtzman, D. M., Cirrito, J. R., & Selkoe, D. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3272-11.2011 · Cited by 111 · see citing works

TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo

Choksi, D. K., Roy, B., Chatterjee, S., Yusuff, T., Bakhoum, M. F., Sengupta, U., Ambegaokar, S. S., Kayed, R., & Jackson, G. R. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt498 · Cited by 107 · see citing works

Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., & Kayed, R. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.023 · Cited by 103 · see citing works

Lack of correlation between plaque burden and cognition in the aged monkey

Sloane, J. A., Pietropaolo, M., Rosene, D. L., Moss, M. B., Peters, A., Kemper, T. L., & Abraham, C. R. (1997) · Acta Neuropathologica · doi:10.1007/s004010050735 · Cited by 101 · see citing works

Postsynaptic Receptors for Amyloid-β Oligomers as Mediators of Neuronal Damage in Alzheimer’s Disease

Dinamarca, M. C., Ríos, J. A., & Inestrosa, N. C. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00464 · Cited by 98 · see citing works

Absence of amyloid β oligomers at the postsynapse and regulated synaptic Zn2+ in cognitively intact aged individuals with Alzheimer’s disease neuropathology

Bjorklund, N. L., Reese, L. C., Sadagoparamanujam, V.-M., Ghirardi, V., Woltjer, R. L., & Taglialatela, G. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-23 · Cited by 98 · see citing works

Soluble oligomers and fibrillar species of amyloid β-peptide differentially affect cognitive functions and hippocampal inflammatory response

He, Y., Zheng, M., Ma, Y., Han, X., Ma, X.-Q., Qu, C., & Du, Y. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.10.129 · Cited by 86 · see citing works

Receptor for advanced glycation endproduct modulators: a new therapeutic target in Alzheimer’s disease

Walker, D. G., Lue, L. F., Paul, G., Patel, A., & Sabbagh, M. N. (2015) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2015.1001490 · Cited by 77 · see citing works

Isolated Amyloid-β(1–42) Protofibrils, But Not Isolated Fibrils, Are Robust Stimulators of Microglia

Paranjape, G. S., Gouwens, L. K., Osborn, D. C., & Nichols, M. R. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn2001238 · Cited by 76 · see citing works

Systemic vaccination with anti‐oligomeric monoclonal antibodies improves cognitive function by reducing Aβ deposition and tau pathology in 3xTg‐AD mice

Rasool, S., Martínez‐Coria, H., Wu, J., LaFerla, F. M., & Glabe, C. G. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12305 · Cited by 74 · see citing works

The aqueous phase of Alzheimer's disease brain contains assemblies built from ∼4 and ∼7 kDa Aβ species

Donald, J. M. M., O’Malley, T. T., Liu, W., Mably, A. J., Brinkmalm, G., Portelius, E., Wittbold, W. M., Frosch, M. P., & Walsh, D. M. (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.01.005 · Cited by 71 · see citing works

The coexistence of an equal amount of Alzheimer's amyloid‐β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway

Chang, Y., & Chen, Y. (2014) · FEBS Journal · doi:10.1111/febs.12813 · Cited by 68 · see citing works

Amyloid-β oligomers as a template for secondary amyloidosis in Alzheimer's disease

Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Krishnamurthy, S., Paulucci-Holthauzen, A. A., Sengupta, U., Lasagna‐Reeves, C. A., Ahmad, Y., Jackson, G. R., & Kayed, R. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.008 · Cited by 67 · see citing works

Combination therapies: The next logical Step for the treatment of synucleinopathies?

Valera, E., & Masliah, E. (2015) · Movement Disorders · doi:10.1002/mds.26428 · Cited by 62 · see citing works

Possible modification of Alzheimer’s disease by statins in midlife: interactions with genetic and non-genetic risk factors

Shinohara, M., Sato, N., Shimamura, M., Kurinami, H., Hamasaki, T., Chatterjee, A., Rakugi, H., & Morishita, R. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00071 · Cited by 59 · see citing works

β-Amyloid oligomers in aging and Alzheimer’s disease

Zahs, K. R., & Ashe, K. H. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00028 · Cited by 53 · see citing works

Critical analysis of Alzheimer rsquo s amyloid-beta nbsp toxicity to mitochondria

Kaminsky, Y. G. (2015) · Frontiers in bioscience · doi:10.2741/4304 · Cited by 53 · see citing works

Anti-Aβ antibodies incapable of reducing cerebral Aβ oligomers fail to attenuate spatial reference memory deficits in J20 mice

Mably, A. J., Liu, W., Donald, J. M. M., Dodart, J., Bard, F., Lemere, C. A., O’Nuallain, B., & Walsh, D. M. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.07.008 · Cited by 52 · see citing works

Intracranial administration of deglycosylated C-terminal-specific anti-Aβ antibody efficiently clears amyloid plaques without activating microglia in amyloid-depositing transgenic mice

Carty, N., Wilcock, D. M., Rosenthal, A., Grimm, J., Pons, J., Ronan, V., Gottschall, P. E., Gordon, M. N., & Morgan, D. (2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-11 · Cited by 49 · see citing works

An N-terminal antibody promotes the transformation of amyloid fibrils into oligomers and enhances the neurotoxicity of amyloid-beta: the dust-raising effect

Liu, Y.-H., Bu, X., Liang, C., Wang, Y., Zhang, T., Jiao, S., Zeng, F., Yao, X., Zhou, H., Deng, J., et al. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0379-4 · Cited by 47 · see citing works

Inflammatory risk factors and pathologies promoting Alzheimer's disease progression: is RAGE the key?

Matrone, C., Djelloul, M., Taglialatela, G., & Perrone, L. (2015) · PubMed · doi:10.14670/hh-30.125 · Cited by 46 · see citing works

A Conformation Change in the Carboxyl Terminus of Alzheimer's Aβ(1–40) Accompanies the Transition from Dimer to Fibril as Revealed by Fluorescence Quenching Analysis

Garzon-Rodriguez, W., Vega, A., Sepulveda-Becerra, M., Milton, S. C. F., Johnson, D. A., Yatsimirsky, A. K., & Glabe, C. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000756200 · Cited by 45 · see citing works

Small Aβ1–42 oligomer‐induced membrane depolarization of neuronal and microglial cells: Role of N‐methyl‐D‐aspartate receptors

Morkūnienė, R., Čižas, P., Jankevičiūtė, S., Petrolis, R., Arandarčikaitė, O., Kriščiukaitis, A., & Borutaitė, V. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23510 · Cited by 41 · see citing works

Astrocytes contain amyloid-β annular protofibrils in Alzheimer's disease brains

Lasagna‐Reeves, C. A., & Kayed, R. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.08.027 · Cited by 40 · see citing works

Vaccination with a non-human random sequence amyloid oligomer mimic results in improved cognitive function and reduced plaque deposition and micro hemorrhage in Tg2576 mice

Rasool, S., Albay, R., Martínez‐Coria, H., Breydo, L., Wu, J., Milton, S. C. F., Misra, S., Tran, A. T., Pensalfini, A., LaFerla, F. M., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-37 · Cited by 38 · see citing works

Immunotherapy alleviates amyloid-associated synaptic pathology in an Alzheimer’s disease mouse model

Dorostkar, M. M., Burgold, S., Filser, S., Barghorn, S., Schmidt, B., Anumala, U. R., Hillen, H., Klein, C., & Herms, J. W. (2014) · Brain · doi:10.1093/brain/awu280 · Cited by 38 · see citing works

Resting microglia react to Aβ42 fibrils but do not detect oligomers or oligomer-induced neuronal damage

Ferrera, D., Mazzaro, N., Canale, C., & Gasparini, L. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.05.023 · Cited by 33 · see citing works

Single-Molecule Imaging Reveals Aβ42:Aβ40 Ratio-Dependent Oligomer Growth on Neuronal Processes

Johnson, R. D., Schauerte, J. A., Chang, C.-C., Wisser, K. C., Althaus, J. C., Carruthers, C. J. L., Sutton, M. A., Steel, D. G., & Gafni, A. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.12.051 · Cited by 33 · see citing works

Elucidating Molecular Mass and Shape of a Neurotoxic Aβ Oligomer

Sebollela, A. S., Mustata, G.-M., Luo, K., Velasco, P. T., Viola, K. L., Cline, E. N., Shekhawat, G. S., Wilcox, K. C., Dravid, V. P., & Klein, W. L. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500156r · Cited by 25 · see citing works

Antibodies bound to Aβ oligomers potentiate the neurotoxicity of Aβ by activating microglia

Morkūnienė, R., Žvirblienė, A., Dalgėdienė, I., Čižas, P., Jankevičiūtė, S., Baliūtytė, G., Jokubka, R., Jankunec, M., Valinčius, G., & Borutaitė, V. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12332 · Cited by 21 · see citing works

Antibody against Small Aggregated Peptide Specifically Recognizes Toxic Aβ-42 Oligomers in Alzheimer’s Disease

Bodani, R. U., Sengupta, U., Castillo‐Carranza, D. L., Guerrero‐Munoz, M. J., Gerson, J. E., Rudra, J. S., & Kayed, R. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00231 · Cited by 21 · see citing works

Design of Metastable β-Sheet Oligomers from Natively Unstructured Peptide

Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Sengupta, U., White, M. A., & Kayed, R. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn4001395 · Cited by 18 · see citing works

Fibrillar seeds alleviate amyloid-β cytotoxicity by omitting formation of higher-molecular-weight oligomers

Wu, W., Liu, Q. R., Sun, X., Yu, J.-S., Zhao, D.-S., Yu, Y., Luo, J., Hu, J., Yu, Z., Zhao, Y., et al. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.08.088 · Cited by 15 · see citing works

Oligomeric amyloid-β(1–42) induces THP-1 human monocyte adhesion and maturation

Crouse, N. R., Ajit, D., Udan, M. L. D., & Nichols, M. R. (2008) · Brain Research · doi:10.1016/j.brainres.2008.11.093 · Cited by 15 · see citing works

The proteostasis network and its decline in ageing

Hipp, M. S., Kasturi, P., & Hartl, F. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0101-y · Cited by 1,642 · see citing works

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works

The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade

Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870 · see citing works

Alzheimer's Disease: Treatment Strategies and Their Limitations.

Passeri, E., Elkhoury, K., Morsink, M., Broersen, K., Linder, M., Tamayol, A., Malaplate, C., Yen, F. T., & Arab-Tehrany, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213954 · Cited by 592 · see citing works

Current state of Alzheimer’s fluid biomarkers

Molinuevo, J. L., Ayton, S., Batrla, R., Bednar, M. M., Bittner, T., Cummings, J., Fagan, A. M., Hampel, H., Mielke, M. M., Mikulskis, A., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1932-x · Cited by 518 · see citing works

Aducanumab, gantenerumab, BAN2401, and ALZ-801—The first wave of amyloid-targeting drugs for Alzheimer’s disease with potential for near term approval

Tolar, M., Abushakra, S., Hey, J. A., Porsteinsson, A., & Sabbagh, M. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00663-w · Cited by 354 · see citing works

Past, present and future of therapeutic strategies against amyloid-β peptides in Alzheimer’s disease: a systematic review

Jeremic, D., Jiménez-Díaz, L., & Navarro-López, J. D. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101496 · Cited by 306 · see citing works

The path forward in Alzheimer's disease therapeutics: Reevaluating the amyloid cascade hypothesis

Tolar, M., Abushakra, S., & Sabbagh, M. (2020) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2019.09.075 · Cited by 275 · see citing works

Natural Compounds for Alzheimer’s Disease Therapy: A Systematic Review of Preclinical and Clinical Studies

Andrade, S., Ramalho, M. J., Loureiro, J. A., & Pereira, M. D. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092313 · Cited by 240 · see citing works

Molecular Mechanisms and Genetics of Oxidative Stress in Alzheimer’s Disease

Cioffi, F., Adam, R. H. I., & Broersen, K. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190863 · Cited by 204 · see citing works

Amyloid-β42/40 ratio drives tau pathology in 3D human neural cell culture models of Alzheimer’s disease

Kwak, S. S., Washicosky, K. J., Brand, E., von Maydell, D., Aronson, J., Kim, S., Capen, D. E., Cetinbas, M., Sadreyev, R., Ning, S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15120-3 · Cited by 151 · see citing works

Glycogen Synthase Kinase 3β: A New Gold Rush in Anti-Alzheimer’s Disease Multitarget Drug Discovery?: Miniperspective

De Simone, A., Tumiatti, V., Andrisano, V., & Milelli, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00931 · Cited by 110 · see citing works

Oxidative Damage and Antioxidant Response in Frontal Cortex of Demented and Nondemented Individuals with Alzheimer’s Neuropathology

Fracassi, A., Marcatti, M., Zolochevska, O., Tabor, N., Woltjer, R., Moreno, S., & Taglialatela, G. (2021) · The Journal of Neuroscience · doi:10.1523/jneurosci.0295-20.2020 · Cited by 81 · see citing works

Aducanumab—Hope or Disappointment for Alzheimer’s Disease

Wojtunik-Kulesza, K., Rudkowska, M., & Orzeł-Sajdłowska, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054367 · Cited by 73 · see citing works

Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes

Piccialli, I., Tedeschi, V., Caputo, L., D’Errico, S., Ciccone, R., De Feo, V., Secondo, A., & Pannaccione, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.876614 · Cited by 73 · see citing works

LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions

Zhao, P., Xu, Y., Jiang, L.-L., Fan, X., Ku, Z., Li, L., Liu, X., Deng, M., Arase, H., Zhu, J.-J., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00550-y · Cited by 54 · see citing works

Focal-type, but not Diffuse-type, Amyloid Beta Plaques are Correlated with Alzheimer’s Neuropathology, Cognitive Dysfunction, and Neuroinflammation in the Human Hippocampus

Liu, F., Sun, J., Wang, X., Jin, S., Sun, F., Wang, T., Yuan, B., Qiu, W., & Ma, C. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00927-5 · Cited by 48 · see citing works

Amyloid β induces interneuron-specific changes in the hippocampus of APPNL-F mice

Sos, K. E., Mayer, M. I., Takács, V. T., Major, A., Bardóczi, Z., Beres, B. M., Szeles, T., Saito, T., Saido, T. C., Mody, I., et al. (2020) · PLOS ONE · doi:10.1371/journal.pone.0233700 · Cited by 37 · see citing works

VGF in Cerebrospinal Fluid Combined With Conventional Biomarkers Enhances Prediction of Conversion From MCI to AD

Llano, D. A., Devanarayan, P., & Devanarayan, V. (2019) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0000000000000328 · Cited by 35 · see citing works

Mitochondrial ubiquitin ligase alleviates Alzheimer’s disease pathology via blocking the toxic amyloid-β oligomer generation

Takeda, K., Uda, A., Mitsubori, M., Nagashima, S., Iwasaki, H., Ito, N., Shiiba, I., Ishido, S., Matsuoka, M., Inatome, R., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01720-2 · Cited by 32 · see citing works

Tunneling nanotubes: A novel pharmacological target for neurodegenerative diseases?

Wang, X.-T., Sun, H., Chen, N.-H., & Yuan, Y.-H. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105541 · Cited by 22 · see citing works

Restoring microglial and astroglial homeostasis using DNA immunization in a down Syndrome mouse model.

Illouz, T., Madar, R., Biragyn, A., & Okun, E. (2019) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2018.10.004 · Cited by 22 · see citing works

Membrane interaction to intercellular spread of pathology in Alzheimer’s disease

Valappil, D. K., Mini, N. J., Dilna, A., & Nath, S. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.936897 · Cited by 19 · see citing works

Multiomics blood-based biomarkers predict Alzheimer's predementia with high specificity in a multicentric cohort study

Souchet, B., Michaïl, A., Heuillet, M., Dupuy-Gayral, A., Haudebourg, E., Pech, C., Berthemy, A., Autelitano, F., Billoir, B., Domoto-Reilly, K., et al. (2024) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2024.34 · Cited by 15 · see citing works

Covalent organic framework-based ratiometric electrochemical sensing platform for ultrasensitive determination of amyloid-β 42 oligomer

Liu, J., Zhao, H., Hu, S., Li, N., Cui, M., Han, B., Li, M., & Zhang, C. (2024) · Talanta · doi:10.1016/j.talanta.2024.126699 · Cited by 15 · see citing works

Factors determining the cytotoxic nature of pathogenic amyloid proteins

Vadukul, D. M. (2018) · Figshare

Oligomer Formation of Amyloid-β(29–42) from Its Monomers Using the Hamiltonian Replica-Permutation Molecular Dynamics Simulation

Itoh, S., & Okumura, H. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b03828 · Cited by 50 · see citing works

基礎の部 ● 演題 2デスミン心筋症マウスに対するニコランジルの心筋保護効果

三部篤 (2011) · Therapeutic research

Therapy of Amyloid Diseases

LINKE, R. P. (1993) · Renal Failure · doi:10.3109/08860229309054951 · Cited by 8 · see citing works