Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction

“Mini-mental state”

Folstein, M. F., Folstein, S. E., & McHugh, P. R. (1975) · Journal of Psychiatric Research · doi:10.1016/0022-3956(75)90026-6 · Cited by 88,282 · see citing works

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · 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

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

Blessed, G., Tomlinson, B. E., & Roth, M. (1968) · British Journal of Psychiatry · doi:10.1192/bjp.114.512.797 · Cited by 4,117 · 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

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · 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

Phases of Aβ-deposition in the human brain and its relevance for the development of AD

Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490 · see citing works

Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective

Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849 · see citing works

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530 · 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

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

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

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

Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

Hartley, D. M., Walsh, D. M., Ye, C., Diehl, T. S., Vasquez, S., Vassilev, P., Teplow, D. B., & Selkoe, D. J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 965 · 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

Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers

Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., et al. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-18 · Cited by 773 · see citing works

Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease

Masliah, E., Mallory, M., Alford, M., DeTeresa, R., Hansen, L. A., McKeel, D. W., & Morris, J. C. (2001) · Neurology · doi:10.1212/wnl.56.1.127 · Cited by 720 · see citing works

Identification of normal and pathological aging in prospectively studied nondemented elderly humans

Dickson, D. W., Crystal, H. A., Mattiace, L. A., Masur, D. M., Blau, A. D., Davies, P., Yen, S.-H., & Aronson, M. K. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90027-u · Cited by 643 · see citing works

Taste and smell losses in normal aging and disease.

Schiffman, S. (1997) · Journal of the American Medical Association (JAMA) · doi:10.1001/jama.1997.03550160077042 · Cited by 592 · see citing works

The Levels of Soluble versus Insoluble Brain Aβ Distinguish Alzheimer's Disease from Normal and Pathologic Aging

Wang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567 · 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

Neuritic pathology and dementia in alzheimer's disease

McKee, A. C., Kosik, K. S., & Kowall, N. W. (1991) · Annals of Neurology · doi:10.1002/ana.410300206 · Cited by 358 · 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

Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer

Kayed, R., Pensalfini, A., Margol, L., Sokolov, Y., Sarsoza, F. M., Head, E., Hall, J. E., & Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808591200 · Cited by 348 · see citing works

Neuropathological staging of Alzheimer lesions and intellectual status in Alzheimer's and Parkinson's disease patients.

Bancher, C., Braak, H., Fischer, P., & Jellinger, K. (1993) · Neuroscience Letters · doi:10.1016/0304-3940(93)90590-h · Cited by 314 · see citing works

Olfactory Identification and Incidence of Mild Cognitive Impairment in Older Age

Wilson, R. S., Schneider, J. A., Arnold, S. E., Tang, Y., Boyle, P. A., & Bennett, D. A. (2007) · Archives of General Psychiatry · doi:10.1001/archpsyc.64.7.802 · Cited by 289 · see citing works

Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity

Cummings, B. J., & Cotman, C. W. (1995) · The Lancet · doi:10.1016/s0140-6736(95)92053-6 · Cited by 260 · see citing works

Has the amyloid cascade hypothesis for Alzheimer's disease been proved?

Hardy, J. (2006) · Current Alzheimer Research · doi:10.2174/156720506775697098 · Cited by 242 · 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

Angiotensin type 1 receptor antagonist losartan, reduces MPTP-induced degeneration of dopaminergic neurons in substantia nigra

Grammatopoulos, T. N., Jones, S. M., Ahmadi, F. A., Hoover, B. R., Snell, L. D., Skoch, J. M., Jhaveri, V. V., Poczobutt, A. M., Weyhenmeyer, J. A., & Zawada, W. M. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-1 · Cited by 165 · see citing works

Alzheimer's disease: amyloid plaques in the cerebellum

Braak, H., Braak, E., Böhl, J., & Lang, W. (1989) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(89)90197-4 · Cited by 157 · see citing works

Amyloid β protein-induced neuronal cell death: neurotoxic properties of aggregated amyloid β protein

Ueda, K., Fukui, Y., & Kageyama, H. (1994) · Brain Research · doi:10.1016/0006-8993(94)91736-1 · Cited by 104 · see citing works

Genetically augmenting tau levels does not modulate the onset or progression of Aβ pathology in transgenic mice

Oddo, S., Caccamo, A., Cheng, D., Jouleh, B., Torp, R., & LaFerla, F. M. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04607.x · Cited by 78 · see citing works

Olfactory bulb lesions in alzheimer's disease

Struble, R. G., & Clark, H. B. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90074-8 · Cited by 70 · see citing works

Pathological changes in frontal cortex from biopsy to autopsy in Alzheimer's disease

Bennett, D. A., Cochran, E. J., Saper, C. B., Leverenz, J. B., Gilley, D. W., & Wilson, R. S. (1993) · Neurobiology of Aging · doi:10.1016/0197-4580(93)90043-b · Cited by 67 · see citing works

Differences between recognition memory and remote memory for olfactory and visual stimuli in nondemented elderly individuals genetically at risk for Alzheimer's disease

Gilbert, P. E., & Murphy, C. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.01.001 · Cited by 37 · 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

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Lu, J., Qiang, W., Yau, W., Schwieters, C. D., Meredith, S. C., & Tycko, R. (2013) · Cell · doi:10.1016/j.cell.2013.08.035 · Cited by 1,087 · see citing works

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 · 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

Basic mechanisms of neurodegeneration: a critical update

Jellinger, K. A. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01010.x · Cited by 608 · see citing works

Atomic View of a Toxic Amyloid Small Oligomer

Laganowsky, A. D., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., et al. (2012) · Science · doi:10.1126/science.1213151 · Cited by 564 · see citing works

Solid-State NMR Studies of Amyloid Fibril Structure

Tycko, R. (2011) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-032210-103539 · Cited by 548 · see citing works

Mitochondrial dysfunction and oxidative stress in aging and cancer

Kudryavtseva, A. V., Krasnov, G. S., Dmitriev, A. A., Alekseev, B. Y., Kardymon, O. L., Садритдинова, А. Ф., Fedorova, M., Pokrovsky, A. V., Melnikova, N. V., Каприн, А. Д., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9821 · Cited by 551 · see citing works

Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer DiseasePreprint

Masters, C. L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006262 · Cited by 543 · see citing works

Amyloid Polymorphism: Structural Basis and Neurobiological Relevance

Tycko, R. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.017 · Cited by 441 · see citing works

Animal Models of Alzheimer Disease

LaFerla, F. M., & Green, K. N. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006320 · Cited by 419 · 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

Dissecting phenotypic traits linked to human resilience to Alzheimer’s pathology

Perez-Nievas, B. G., Stein, T. D., Tai, H.-C., Dols-Icardo, O., Scotton, T. C., Barroeta-Espar, I., Fernandez-Carballo, L., de Munain, E. L., Perez, J., Marquie, M., et al. (2013) · Brain · doi:10.1093/brain/awt171 · Cited by 387 · see citing works

The cerebellum in Alzheimer’s disease: evaluating its role in cognitive decline

Jacobs, H. I. L., Hopkins, D. A., Mayrhofer, H. C., Bruner, E., van Leeuwen, F. W., Raaijmakers, W., & Schmahmann, J. D. (2017) · Brain · doi:10.1093/brain/awx194 · Cited by 339 · see citing works

Apolipoprotein E4 effects in Alzheimer’s disease are mediated by synaptotoxic oligomeric amyloid-β

Koffie, R. M., Hashimoto, T., Tai, H.-C., Kay, K. R., Serrano-Pozo, A., Joyner, D., Hou, S., Kopeikina, K. J., Frosch, M. P., Lee, V. M., et al. (2012) · Brain · doi:10.1093/brain/aws127 · Cited by 327 · see citing works

Amyloid‐beta oligomerization in Alzheimer dementia versus high‐pathology controls

Esparza, T. J., Zhao, H., Cirrito, J. R., Cairns, N. J., Bateman, R. J., Holtzman, D. M., & Brody, D. L. (2012) · Annals of Neurology · doi:10.1002/ana.23748 · Cited by 304 · see citing works

Alzheimer's Therapeutics Targeting Amyloid Beta 1–42 Oligomers II: Sigma-2/PGRMC1 Receptors Mediate Abeta 42 Oligomer Binding and Synaptotoxicity

Izzo, N. J., Xu, J., Zeng, C., Kirk, M. J., Mozzoni, K., Silky, C., Rehak, C., Yurko, R., Look, G. C., Rishton, G. M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111899 · Cited by 294 · see citing works

TLR4 mutation reduces microglial activation, increases Aβ deposits and exacerbates cognitive deficits in a mouse model of Alzheimer’s disease

Song, M., Jin, J., Lim, J.-E., Kou, J., Pattanayak, A., Rehman, J. A., Kim, H.-D., Tahara, K., Lalonde, R., & Fukuchi, K.-I. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-92 · Cited by 273 · 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

APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease

Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 259 · see citing works

Amyloid-β Receptors: The Good, the Bad, and the Prion Protein

Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256 · 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

Conformational Differences between Two Amyloid β Oligomers of Similar Size and Dissimilar Toxicity

Ladiwala, A. R. A., Litt, J., Kane, R. S., Aucoin, D., Smith, S. O., Ranjan, S., Davis, J., Nostrand, W. E. V., & Tessier, P. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329763 · Cited by 223 · see citing works

Lipid Rafts: Linking Alzheimer′s Amyloid‐βProduction, Aggregation, and Toxicity at Neuronal Membranes

Rushworth, J. V., & Hooper, N. M. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/603052 · Cited by 218 · see citing works

Trem2 Deletion Reduces Late-Stage Amyloid Plaque Accumulation, Elevates the Aβ42:Aβ40 Ratio, and Exacerbates Axonal Dystrophy and Dendritic Spine Loss in the PS2APP Alzheimer's Mouse Model

Meilandt, W. J., Ngu, H., Gogineni, A., Lalehzadeh, G., Lee, S.-H., Srinivasan, K., Imperio, J., Wu, T., Weber, M., Kruse, A. J., et al. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.1871-19.2019 · Cited by 210 · see citing works

Loss of α7 Nicotinic Receptors Enhances β-Amyloid Oligomer Accumulation, Exacerbating Early-Stage Cognitive Decline and Septohippocampal Pathology in a Mouse Model of Alzheimer's Disease

Hernandez, C. M., Kayed, R., Zheng, H., Sweatt, J. D., & Dineley, K. T. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5038-09.2010 · Cited by 204 · see citing works

A label-free electrical impedimetric biosensor for the specific detection of Alzheimer's amyloid-beta oligomers

Rushworth, J. V., Ahmed, A., Jarosz-Griffiths, H., Pollock, N. M., Hooper, N. M., & Millner, P. A. (2013) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.12.036 · Cited by 196 · see citing works

Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates

Klingstedt, T., Åslund, A., Simon, R., Johansson, L. B. G., Mason, J., Nyström, S., Hammarström, P., & Nilsson, K. P. (2011) · Organic and biomolecular chemistry · doi:10.1039/c1ob05637a · Cited by 183 · see citing works

Direct three-dimensional visualization of membrane disruption by amyloid fibrils

Milanesi, L., Sheynis, T., Xue, W., Orlova, E. V., Hellewell, A. L., Jelinek, R., Hewitt, E. W., Radford, S. E., & Saibil, H. R. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206325109 · Cited by 194 · see citing works

Abeta, oxidative stress in Alzheimer disease: Evidence based on proteomics studies

Swomley, A. M., Förster, S., Keeney, J. T. R., Triplett, J. C., Zhang, Z., Rukhsana Sultana, A., & Butterfield, D. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.015 · Cited by 190 · see citing works

A Sensitive Aβ Oligomer Assay Discriminates Alzheimer's and Aged Control Cerebrospinal Fluid

Savage, M. J., Kalinina, J., Wolfe, A. L., Tugusheva, K., Korn, R., Cash-Mason, T., Maxwell, J. W., Hatcher, N. G., Haugabook, S. J., Wu, G., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1675-13.2014 · Cited by 183 · see citing works

Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?

Zraika, S., Hull, R. L., Verchere, C. B., Clark, A., Potter, K. J., Fraser, P. E., Raleigh, D. P., & Kahn, S. E. (2010) · Diabetologia · doi:10.1007/s00125-010-1671-6 · Cited by 181 · see citing works

Alzheimer's Therapeutics Targeting Amyloid Beta 1–42 Oligomers I: Abeta 42 Oligomer Binding to Specific Neuronal Receptors Is Displaced by Drug Candidates That Improve Cognitive Deficits

Izzo, N. J., Staniszewski, A., To, L., Fa, M., Teich, A. F., Saeed, F., Wostein, H., Walko, T., Vaswani, A., Wardius, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111898 · Cited by 180 · see citing works

Diversity of Amyloid-beta Proteoforms in the Alzheimer’s Disease Brain

Wildburger, N. C., Esparza, T. J., LeDuc, R. D., Fellers, R. T., Thomas, P. M., Cairns, N. J., Kelleher, N. L., Bateman, R. J., & Brody, D. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-10422-x · Cited by 164 · see citing works

The Amyloid Phenomenon and Its Significance in Biology and MedicinePreprint

Dobson, C. M., Knowles, T. P. J., & Vendruscolo, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033878 · Cited by 166 · see citing works

The Emerging Relationship Between Interstitial Fluid–Cerebrospinal Fluid Exchange, Amyloid-β, and Sleep

Boespflug, E. L., & Iliff, J. J. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.11.031 · Cited by 171 · see citing works

Role of Vitamin E in the Treatment of Alzheimer’s Disease: Evidence from Animal Models

Gugliandolo, A., Bramanti, P., & Mazzon, E. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122504 · Cited by 167 · see citing works

<i><scp>APOE</scp></i>‐modulated Aβ‐induced neuroinflammation in Alzheimer's disease: current landscape, novel data, and future perspective

Tai, L. M., Ghura, S., Koster, K. P., Liakaite, V., Maienschein‐Cline, M., Kanabar, P., Collins, N., Ben‐Aissa, M., Lei, A. Z., Bahroos, N., et al. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13072 · Cited by 165 · see citing works

Levels of Soluble Apolipoprotein E/Amyloid-β (Aβ) Complex Are Reduced and Oligomeric Aβ Increased with APOE4 and Alzheimer Disease in a Transgenic Mouse Model and Human Samples*

Tai, L. M., Bilousova, T., Jungbauer, L., Roeske, S. K., Youmans, K. L., Yu, C., Poon, W. W., Cornwell, L. B., Miller, C. A., Vinters, H. V., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442103 · Cited by 165 · see citing works

Intraneuronal Aβ detection in 5xFAD mice by a new Aβ-specific antibody

Youmans, K. L., Tai, L. M., Kanekiyo, T., Stine Jr, W. B., Michon, S.-C., Nwabuisi-Heath, E., Manelli, A. M., Fu, Y., Riordan, S., Eimer, W. A., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-8 · Cited by 164 · see citing works

Aluminum, copper, iron and zinc differentially alter amyloid-Aβ1–42 aggregation and toxicity

Bolognin, S., Luigi Messori, A., Drago, D., Gabbiani, C., Cendron, L., & Zatta, P. F. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.02.009 · Cited by 162 · see citing works

Ceftriaxone ameliorates tau pathology and cognitive decline via restoration of glial glutamate transporter in a mouse model of Alzheimer's disease

Zumkehr, J., Rodríguez‐Ortiz, C. J., Cheng, D., Kieu, Z., Wai, T., Hawkins, C., Kilian, J., Lim, S., Medeiros, R., & Kitazawa, M. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.04.005 · Cited by 152 · see citing works

Prion Protein-mediated Toxicity of Amyloid-β Oligomers Requires Lipid Rafts and the Transmembrane LRP1

Rushworth, J. V., Jarosz-Griffiths, H., Watt, N. T., & Hooper, N. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400358 · Cited by 151 · see citing works

Activated iron-containing microglia in the human hippocampus identified by magnetic resonance imaging in Alzheimer disease

Zeineh, M. M., Chen, Y., Kitzler, H. H., Hammond, R., Vogel, H., & Rutt, B. K. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.05.022 · Cited by 151 · see citing works

Sorting out the trash: the spatial nature of eukaryotic protein quality control

Sontag, E. M., Vonk, W. I. M., & Frydman, J. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.12.006 · Cited by 146 · see citing works

Cerebral amyloid angiopathy in the aetiology and immunotherapy of Alzheimer disease

Weller, R. O., Preston, S., Subash, M., & Carare, R. O. (2009) · Alzheimer s Research & Therapy · doi:10.1186/alzrt6 · Cited by 145 · see citing works

Protein Microgels from Amyloid Fibril Networks

Shimanovich, U., Efimov, I., Mason, T. G., Flagmeier, P., Buell, A. K., Gedanken, A., Linse, S. S., Åkerfeldt, K. S., Dobson, C. M., Weitz, D. A., et al. (2014) · ACS Nano · doi:10.1021/nn504869d · Cited by 142 · see citing works

Affinity of copper and zinc ions to proteins and peptides related to neurodegenerative conditions (Aβ, APP, α-synuclein, PrP)

Zawisza, I. A., Rózga, M., & Bal, W. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.012 · Cited by 138 · see citing works

Neuropathology after active Aβ42 immunotherapy: implications for Alzheimer’s disease pathogenesis

Boche, D., Denham, N., Holmes, C., & Nicoll, J. A. R. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0719-5 · Cited by 135 · see citing works

Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models

Kostylev, M. A., Kaufman, A. C., Nygaard, H. B., Patel, P., Haas, L. T., Gunther, E. C., Vortmeyer, A., & Strittmatter, S. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.643577 · Cited by 133 · see citing works

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Rinauro, D. J., Chiti, F., Vendruscolo, M., & Limbocker, R. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00651-2 · Cited by 132 · see citing works

The pleiotropic effects of omega-3 docosahexaenoic acid on the hallmarks of Alzheimer's disease

Belkouch, M., Hachem, M., Elgot, A., Van, A. L., Picq, M., Guichardant, M., Lagarde, M., & Bernoud‐Hubac, N. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.03.002 · Cited by 128 · see citing works

Deficiency of TYROBP, an adapter protein for TREM2 and CR3 receptors, is neuroprotective in a mouse model of early Alzheimer’s pathology

Haure-Mirande, J.-V., Audrain, M., Fanutza, T., Kim, S. H., Klein, W. L., Glabe, C., Readhead, B., Dudley, J. T., Blitzer, R. D., Wang, M., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1737-3 · Cited by 127 · see citing works

Soluble Amyloid-beta Aggregates from Human Alzheimer’s Disease Brains

Esparza, T. J., Wildburger, N. C., Jiang, H., Gangolli, M., Cairns, N. J., Bateman, R. J., & Brody, D. L. (2016) · Scientific Reports · doi:10.1038/srep38187 · Cited by 124 · see citing works

Neuroinflammatory Signals in Alzheimer Disease and APP/PS1 Transgenic Mice

López‐González, I., Schlüter, A., Aso, E., Garcia‐Esparcia, P., Ansoleaga, B., Llorens, F., Carmona, M., Moreno, J. R., Fuso, A., Portero‐Otín, M., et al. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000176 · Cited by 125 · see citing works

Biomarkers in Alzheimer's disease drug development

Cummings, J. L. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.06.004 · Cited by 121 · see citing works

Naturally Occurring Autoantibodies against β-Amyloid: Investigating Their Role in Transgenic Animal andIn VitroModels of Alzheimer's Disease

Dodel, R. C., Balakrishnan, K., Keyvani, K., Deuster, O., Neff, F., Andrei‐Selmer, L., Röskam, S., Stüer, C., Al‐Abed, Y., Noelker, C., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4401-10.2011 · Cited by 127 · see citing works

Intracellular amyloid and the neuronal origin of Alzheimer neuritic plaques

Pensalfini, A., Albay, R., Rasool, S., Wu, J. W., Hatami, A., Arai, H., Margol, L., Milton, S., Poon, W. W., Corrada, M. M., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.011 · Cited by 120 · see citing works

Role of Cholesterol in APP Metabolism and Its Significance in Alzheimer’s Disease Pathogenesis

Maulik, M., Westaway, D. A., Jhamandas, J. H., & Kar, S. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8337-y · Cited by 117 · see citing works

Soluble apoE/Aβ complex: mechanism and therapeutic target for APOE4-induced AD risk

Tai, L. M., Mehra, S., Shete, V., Estus, S., Rebeck, G. W., Bu, G., & LaDu, M. J. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-2 · Cited by 116 · see citing works

The Cysteine Protease Inhibitor, E64d, Reduces Brain Amyloid-β and Improves Memory Deficits in Alzheimer's Disease Animal Models by Inhibiting Cathepsin B, but not BACE1, β-Secretase Activity

Hook, G., HOOK, V. Y. H., & Kindy, M. S. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110101 · Cited by 111 · see citing works

β-Amyloid Fibrils in Alzheimer Disease Are Not Inert When Bound to Copper Ions but Can Degrade Hydrogen Peroxide and Generate Reactive Oxygen Species

Mayes, J., Tinker, C. L., Kolosov, O., Zhang, H., Tabner, B. J., & Allsop, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525212 · Cited by 109 · see citing works

Metal binding sites in amyloid oligomers: Complexes and mechanisms

Miller, Y., Ma, B., & Nussinov, R. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.12.022 · Cited by 103 · see citing works

Strategy to reduce free radical species in Alzheimer’s disease: an update of selected antioxidants

Domenico, F. D., Barone, E., Marzia Perluigi, A., & Butterfield, D. A. (2014) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.955853 · Cited by 102 · 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

Biflavonoids Are Superior to Monoflavonoids in Inhibiting Amyloid-β Toxicity and Fibrillogenesis via Accumulation of Nontoxic Oligomer-like Structures

Thapa, A., Woo, E., Chi, E. Y., Sharoar, M. G., Jin, H.-G., Shin, S. Y., & Park, I. (2011) · Biochemistry · doi:10.1021/bi101731d · Cited by 102 · see citing works

APOE4 enhances age-dependent decline in cognitive function by down-regulating an NMDA receptor pathway in EFAD-Tg mice

Liu, D.-S., Pan, X.-D., Zhang, J., Shen, H., Collins, N. C., Cole, A. M., Koster, K. P., Ben Aissa, M., Dai, X.-M., Zhou, M., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0002-2 · Cited by 99 · see citing works

Lesions without symptoms: understanding resilience to Alzheimer disease neuropathological changes

Gómez-Isla, T., & Frosch, M. P. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-022-00642-9 · Cited by 96 · see citing works

Ferulic acid ethyl ester as a potential therapy in neurodegenerative disorders

Rukhsana Sultana, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.015 · Cited by 94 · see citing works

EFAD transgenic mice as a human APOE relevant preclinical model of Alzheimerʼns disease

Tai, L. M., Balu, D., Avila-Munoz, E., Abdullah, L., Thomas, R., Collins, N., Valencia-Olvera, A. C., & LaDu, M. J. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r076315 · Cited by 93 · see citing works

Amyloid-β Pathology and APOE Genotype Modulate Retinoid X Receptor Agonist Activity in Vivo

Tai, L. M., Koster, K. P., Luo, J., Lee, S., Wang, Y., Collins, N. C., Aissa, M. B., Thatcher, G. R. J., & LaDu, M. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.600833 · Cited by 93 · see citing works

Synthesis and biological evaluation of deferiprone-resveratrol hybrids as antioxidants, Aβ 1–42 aggregation inhibitors and metal-chelating agents for Alzheimer's disease

Xu, P., Zhang, M., Sheng, R., & Ma, Y. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.12.045 · Cited by 92 · see citing works

Aging in the Canine and Feline Brain

Vite, C. H., & Head, E. (2014) · Veterinary Clinics of North America Small Animal Practice · doi:10.1016/j.cvsm.2014.07.008 · Cited by 91 · see citing works

Non-canonical soluble amyloid-beta aggregates and plaque buffering: controversies and future directions for target discovery in Alzheimer’s disease

Brody, D. L., Jiang, H., Wildburger, N. C., & Esparza, T. J. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0293-3 · Cited by 84 · see citing works

The missing link in the amyloid cascade of Alzheimer’s disease – Metal ions

Tiiman, A., Palumaa, P., & Tõugu, V. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.023 · Cited by 88 · see citing works

Characterization of Aldh2 -/- mice as an age-related model of cognitive impairment and Alzheimer’s disease

D’Souza, Y., Elharram, A., Soon-Shiong, R., Andrew, R. D., & Bennett, B. M. (2015) · Molecular Brain · doi:10.1186/s13041-015-0117-y · Cited by 86 · see citing works

Non-Fibrillar Oligomeric Amyloid-β within Synapses

Pickett, E. K., Koffie, R. M., Wegmann, S., Henstridge, C. M., Herrmann, A. G., Colom‐Cadena, M., Lleó, A., Kay, K. R., Vaught, M., Soberman, R. J., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160007 · Cited by 87 · see citing works

An update on clinical proteomics in Alzheimer’s research

Korolainen, M. A., Nyman, T. A., Aittokallio, T. A., & Pirttilä, T. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06558.x · Cited by 86 · see citing works

Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic ResonancePreprint

Tycko, R. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024083 · Cited by 86 · see citing works

Designed α-sheet peptides inhibit amyloid formation by targeting toxic oligomers

Hopping, G., Kellock, J., Barnwal, R. P., Law, P. B., Bryers, J. D., Varani, G., Caughey, B. W., & Daggett, V. (2014) · eLife · doi:10.7554/elife.01681 · Cited by 85 · see citing works

Integrative approach to sporadic Alzheimer’s disease: deficiency of TYROBP in cerebral Aβ amyloidosis mouse normalizes clinical phenotype and complement subnetwork molecular pathology without reducing Aβ burden

Haure-Mirande, J.-V., Wang, M., Audrain, M., Fanutza, T., Kim, S. H., Heja, S., Readhead, B., Dudley, J. T., Blitzer, R. D., Schadt, E. E., et al. (2019) · Molecular Psychiatry · doi:10.1038/s41380-018-0255-6 · Cited by 84 · see citing works

Recent Progress in Alzheimer’s Disease Research, Part 1: Pathology

Hane, F. T., Lee, B. Y., & Leonenko, Z. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160882 · Cited by 84 · see citing works

Structural investigation of the C-terminal catalytic fragment of presenilin 1

Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Młynarczyk, K., Puławski, W., Ghoshdastider, U., Koliński, M., Filipek, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000778107 · Cited by 83 · see citing works

Recent insights on astrocyte mechanisms in CNS homeostasis, pathology, and repair

Hart, C. G., & Karimi‐Abdolrezaee, S. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24922 · Cited by 85 · see citing works

Olfactory Dysfunction as a Global Biomarker for Sniffing out Alzheimer’s Disease: A Meta-Analysis

Kotecha, A., Corrêa, A., Fisher, K., & Rushworth, J. V. (2018) · Biosensors · doi:10.3390/bios8020041 · Cited by 82 · see citing works

Activating AhR alleviates cognitive deficits of Alzheimer's disease model mice by upregulating endogenous Aβ catabolic enzyme Neprilysin

Cheng, Q., Yang, C., Lu, M., Bao, J., Shen, H., Deng, B., Li, S., Li, W., Zhang, M., & Cao, C. (2021) · Theranostics · doi:10.7150/thno.61601 · Cited by 82 · see citing works

Amyloid-β Peptide and Oligomers in the Brain and Cerebrospinal Fluid of Aged Canines

Head, E., Pop, V., Sarsoza, F. M., Kayed, R., Beckett, T. L., Studzinski, C. M., Tomic, J. L., Glabe, C. G., & Murphy, M. P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1397 · Cited by 80 · see citing works

Alzheimer's Disease and Amyloid: Culprit or Coincidence?

Skaper, S. D. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00011-9 · Cited by 80 · see citing works

Nanoscale structure of amyloid-β plaques in Alzheimer’s disease

Querol‐Vilaseca, M., Colom‐Cadena, M., Pegueroles, J., Núñez‐Llaves, R., Luque-Cabecerans, J., Muñoz, L., Andilla, J., Belbin, O., Spires‐Jones, T. L., Gelpí, E., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-41443-3 · Cited by 77 · see citing works

Immunization with Bacillus Calmette-Guérin (BCG) alleviates neuroinflammation and cognitive deficits in APP/PS1 mice via the recruitment of inflammation-resolving monocytes to the brain

Zuo, Z., Qi, F., Yang, J., Wang, X., Wu, Y., Wen, Y., Yuan, Q., Zou, J., Guo, K., & Yao, Z. B. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.02.001 · Cited by 79 · see citing works

Affinity of Cu+ for the Copper-Binding Domain of the Amyloid-β Peptide of Alzheimer’s Disease

Feaga, H. A., Maduka, R. C., Foster, M. N., & Szalai, V. A. (2011) · Inorganic Chemistry · doi:10.1021/ic100967s · Cited by 78 · see citing works

Amyloid-β and Tau Pathology of Alzheimer's Disease Induced by Diabetes in a Rabbit Animal Model

Bitel, C. L., Kasinathan, C., Kaswala, R. H., Klein, W. L., & Frederikse, P. H. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120571 · Cited by 77 · see citing works

Highly potent soluble amyloid-β seeds in human Alzheimer brain but not cerebrospinal fluid

Fritschi, S. K., Langer, F., Kaeser, S. A., Maia, L. F., Portelius, E., Pinotsi, D., Kaminski, C. F., Winkler, D. T., Maetzler, W., Keyvani, K., et al. (2014) · Brain · doi:10.1093/brain/awu255 · Cited by 78 · see citing works

In Vivo Assessment of Retinal Biomarkers by Hyperspectral Imaging: Early Detection of Alzheimer’s Disease

More, S. S., Beach, J. M., McClelland, C. M., Mokhtarzadeh, A., & Vince, R. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00331 · Cited by 74 · see citing works

Neuroendocrine hormone amylin in diabetes

Zhang, X., Pan, Y.-H., Huang, Y., & Zhao, H. (2016) · World Journal of Diabetes · doi:10.4239/wjd.v7.i9.189 · Cited by 75 · see citing works

Keampferol-3-O-rhamnoside abrogates amyloid beta toxicity by modulating monomers and remodeling oligomers and fibrils to non-toxic aggregates

Sharoar, M. G., Thapa, A., Shahnawaz, M., Ramasamy, V. S., Woo, E., Shin, S. S., & Park, I. (2012) · Journal of Biomedical Science · doi:10.1186/1423-0127-19-104 · Cited by 72 · see citing works

Prion-like seeding and nucleation of intracellular amyloid-β

Olsson, T. T., Klementieva, O. L., & Gouras, G. K. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.01.015 · Cited by 72 · see citing works

Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer’s disease

Sideris, D. I., Danial, J. S. H., Emin, D., Ruggeri, F. S., Xia, Z., Zhang, Y. P., Lobanova, E., Dakin, H., De, S., Miller, A., et al. (2021) · Brain Communications · doi:10.1093/braincomms/fcab147 · Cited by 71 · see citing works

CSF Biomarkers in the Early Diagnosis of Mild Cognitive Impairment and Alzheimer’s Disease

Papaliagkas, V. T., Kalinderi, K., Vareltzis, P. K., Μoraitou, D., Papamitsou, T., & Chatzidimitriou, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108976 · Cited by 73 · see citing works

General Principles Underpinning Amyloid Structure

Taylor, A. I. P., & Staniforth, R. A. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.878869 · Cited by 68 · see citing works

A fibril-specific, conformation-dependent antibody recognizes a subset of Aβ plaques in Alzheimer disease, Down syndrome and Tg2576 transgenic mouse brain

Sarsoza, F. M., Saing, T., Kayed, R., Dahlin, R., Dick, M. B., Broadwater-Hollifield, C., Mobley, S., Lott, I. T., Doran, E. W., Gillen, D. L., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0530-3 · Cited by 44 · see citing works

Amyloid-β Oligomers Relate to Cognitive Decline in Alzheimer's Disease

Jongbloed, W., Bruggink, K. A., Kester, M. I., Visser, P.-J., Scheltens, P., Blankenstein, M. A., Verbeek, M. M., Teunissen, C. E., & Veerhuis, R. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-142136 · Cited by 68 · see citing works

Oligomeric Aβ in Alzheimer's Disease: Relationship to Plaque and Tangle Pathology, APOE Genotype and Cerebral Amyloid Angiopathy

Helmond, Z. V., Miners, J. S., Kehoe, P. G., & Love, S. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00321.x · Cited by 43 · see citing works

Discrete Pools of Oligomeric Amyloid-β Track with Spatial Learning Deficits in a Mouse Model of Alzheimer Amyloidosis

Chiang, A. C. A., Fowler, S., Reddy, R., Pletniková, O., Troncoso, J. C., Sherman, M. A., Lesné, S., & Jankowsky, J. L. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.11.011 · Cited by 15 · see citing works

P2‐256: Histological localization of amyloid‐β oligomers in the human brain during the course of Alzheimer's disease

Panchal, M., Lacor, P. N., Klein, W. L., & Duyckaerts, C. J. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.1137