Internalized Antibodies to the Aβ Domain of APP Reduce Neuronal Aβ and Protect against Synaptic Alterations

Alzheimer's Disease Is a Synaptic Failure

Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420

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

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126

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

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876

Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation

Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530

Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160

Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease

Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012

High-Level Neuronal Expression of Aβ1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation

Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856

Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease

Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,506

Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease

Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431

Immunotherapy Targeting Pathological Tau Conformers in a Tangle Mouse Model Reduces Brain Pathology with Associated Functional Improvements

Asuni, A. A., Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2361-07.2007 · Cited by 506

Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease

Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372

Can Alzheimer disease be prevented by amyloid-β immunotherapy?

Lemere, C. A., & Masliah, E. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2009.219 · Cited by 351

β-amyloid Peptides and Amyloid Plaques in Alzheimer's Disease

Gouras, G. K., Olsson, T. T., & Hansson, O. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0313-y · Cited by 346

Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306

Immunotherapy Targeting Pathological Tau Prevents Cognitive Decline in a New Tangle Mouse Model

Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4363-10.2010 · Cited by 272

Phenylbutyrate rescues dendritic spine loss associated with memory deficits in a mouse model of Alzheimer disease

Ricobaraza, A., Cuadrado‐Tejedor, M., Marco, S., Pérez‐Otaño, I., & García‐Osta, A. (2012) · Hippocampus · doi:10.1002/hipo.20883 · Cited by 239

Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils

Habicht, G., Haupt, C., Friedrich, R. P., Hortschansky, P., Sachse, C., Meinhardt, J., Wieligmann, K., Gellermann, G. P., Brodhun, M., Götz, J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703793104 · Cited by 221

Antibody Uptake into Neurons Occurs Primarily via Clathrin-dependent Fcγ Receptor Endocytosis and Is a Prerequisite for Acute Tau Protein Clearance

Congdon, E. E., Gu, J., Sait, H. B. R., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491001 · Cited by 195

Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice

Boimel, M., Grigoriadis, N., Lourbopoulos, A., Haber, E., Abramsky, O., & Rosenmann, H. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.05.010 · Cited by 174

Two Novel Tau Antibodies Targeting the 396/404 Region Are Primarily Taken Up by Neurons and Reduce Tau Protein Pathology

Gu, J., Congdon, E. E., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494922 · Cited by 169

Soluble amyloid precursor proteins in the cerebrospinal fluid as novel potential biomarkers of Alzheimer's disease: a multicenter study

Lewczuk, P., Kamrowski‐Kruck, H., Peters, O., Heuser, I., Jessen, F., Popp, J., Bürger, K., Hampel, H. J., Frölich, L., Wolf, S., et al. (2008) · Molecular Psychiatry · doi:10.1038/mp.2008.84 · Cited by 160

An amyloid-β protofibril-selective antibody prevents amyloid formation in a mouse model of Alzheimer's disease

Lord, A., Gumucio, A., Englund, H., Sehlin, D., Sundquist, V. S., Söderberg, L., Möller, C., Gellerfors, P., Lannfelt, L., Pettersson, F. E., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.08.007 · Cited by 158

Amyloid‐ß‐directed immunotherapy for Alzheimer's disease

Lannfelt, L., Relkin, N. R., & Siemers, E. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12168 · Cited by 161

HSV-1 and Alzheimer’s disease: more than a hypothesis

Piacentini, R., De Chiara, G., Li Puma, D. D., Ripoli, C., Marcocci, M. E., Garaci, E., Palamara, A. T., & Grassi, C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00097 · Cited by 130

A framework to understand the variations of PSD-95 expression in brain aging and in Alzheimer's disease

Savioz, A., Leuba, G., & Vallet, P. G. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.09.004 · Cited by 127

Synaptic Activity Reduces Intraneuronal Aβ, Promotes APP Transport to Synapses, and Protects against Aβ-Related Synaptic Alterations

Tampellini, D., Rahman, N., Gallo, E. F., Huang, Z., Dumont, M., Capetillo-Zarate, E., Ma, T., Zheng, R., Lu, B., Nanus, D. M., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2292-09.2009 · Cited by 127

Immunotherapy for Alzheimer‘s Disease: From Anti-β-Amyloid to Tau-Based Immunization Strategies

Panza, F., Frisardi, V., Solfrizzi, V., Imbimbo, B. P., Logroscino, G., Santamato, A., Greco, A., Seripa, D., & Pilotto, A. (2012) · Immunotherapy · doi:10.2217/imt.11.170 · Cited by 130

Intracerebroventricular amyloid-β antibodies reduce cerebral amyloid angiopathy and associated micro-hemorrhages in aged Tg2576 mice

Thakker, D. R., Weatherspoon, M. R., Harrison, J., Keene, T. E., Lane, D. S., Kaemmerer, W. F., Stewart, G. R., & Shafer, L. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813404106 · Cited by 124

Assembly, Maturation, and Trafficking of the γ-Secretase Complex in Alzheimers Disease

Dries, D. R., & Yu, G. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954695 · Cited by 126

Intracellular Accumulation of Amyloid- (A ) Protein Plays a Major Role in A -Induced Alterations of Glutamatergic Synaptic Transmission and Plasticity

Ripoli, C., Cocco, S., Puma, D. D. L., Piacentini, R., Mastrodonato, A., Scala, F., Puzzo, D., D’Ascenzo, M., & Grassi, C. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1201-14.2014 · Cited by 131

Aβ Immunotherapy: Intracerebral Sequestration of Aβ by an Anti-Aβ Monoclonal Antibody 266 with High Affinity to Soluble Aβ

Yamada, K., Yabuki, C., Seubert, P., Schenk, D., Hori, Y., Ohtsuki, S., Terasaki, T., Hashimoto, T., & Iwatsubo, T. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2021-09.2009 · Cited by 117

Immunotherapy Targeting Pathological Tau Protein in Alzheimer's Disease and Related Tauopathies

Sigurdsson, E. M. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-15202 · Cited by 116

β-Amyloid Modulation of Synaptic Transmission and Plasticity

Venkitaramani, D. V., Chin, J., Netzer, W. J., Gouras, G. K., Lesné, S., Malinow, R., & Lombroso, P. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3478-07.2007 · Cited by 118

Early-onset network hyperexcitability in presymptomatic Alzheimer’s disease transgenic mice is suppressed by passive immunization with anti-human APP/Aβ antibody and by mGluR5 blockade

Kazim, S. F., Chuang, S.-C., Zhao, W., Wong, R. K. S., Bianchi, R., & Iqbal, K. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00071 · Cited by 109

Intravenous Immunoglobulins as a Treatment for Alzheimerʼs Disease

Dodel, R. C., Neff, F., Noelker, C., Pul, R., Du, Y., Bacher, M., & Oertel, W. H. (2010) · Drugs · doi:10.2165/11533070-000000000-00000 · Cited by 113

Synaptic activity and Alzheimer's disease: a critical update

Tampellini, D. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00423 · Cited by 110

Tau-Based Therapeutics for Alzheimer’s Disease: Active and Passive Immunotherapy

Panza, F., Solfrizzi, V., Seripa, D., Imbimbo, B. P., Lozupone, M., Santamato, A., Tortelli, R., Galizia, I., Prete, C., Daniele, A., et al. (2016) · Immunotherapy · doi:10.2217/imt-2016-0019 · Cited by 113

Long-term electromagnetic field treatment enhances brain mitochondrial function of both Alzheimer's transgenic mice and normal mice: a mechanism for electromagnetic field-induced cognitive benefit?

Dragicevic, N., Bradshaw, P. C., Mamcarz, M. B., Lin, X., Wang, L., Cao, C., & Arendash, G. W. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.04.012 · Cited by 104

Tau as a Therapeutic Target for Alzheimers Disease

Boutajangout, A., Sigurdsson, E. M., & Krishnamurthy, P. K. (2011) · Current Alzheimer Research · doi:10.2174/156720511796717195 · Cited by 102

Herpes Simplex Virus type-1 infection induces synaptic dysfunction in cultured cortical neurons via GSK-3 activation and intraneuronal amyloid-β protein accumulation

Piacentini, R., Puma, D. D. L., Ripoli, C., Marcocci, M. E., Chiara, G. D., Garaci, E., Palamara, A. T., & Grassi, C. (2015) · Scientific Reports · doi:10.1038/srep15444 · Cited by 98

RAGE–TXNIP axis is required for S100B-promoted Schwann cell migration, fibronectin expression and cytokine secretion

Sbai, O., Devi, T. S., Melone, M. A. B., Feron, F. P., Khrestchatisky, M., Singh, L. P., & Perrone, L. (2010) · Journal of Cell Science · doi:10.1242/jcs.074674 · Cited by 96

Intraneuronal Aβ accumulation induces hippocampal neuron hyperexcitability through A-type K+ current inhibition mediated by activation of caspases and GSK-3

Scala, F., Fusco, S., Ripoli, C., Piacentini, R., Puma, D. D. L., Spinelli, M., Laezza, F., Grassi, C., & D’Ascenzo, M. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.10.034 · Cited by 98

Dendritic Spine Instability Leads to Progressive Neocortical Spine Loss in a Mouse Model of Huntington's Disease

Murmu, R. P., Li, W., Holtmaat, A., & Li, J.-Y. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5284-12.2013 · Cited by 95

MicroRNA-Related Cofilin Abnormality in Alzheimer's Disease

Yao, J., Hennessey, T., Flynt, A. S., Lai, E. C., Beal, M. F., & Lin, M. T. S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015546 · Cited by 93

Aβ Internalization by Neurons and Glia

Mohamed, A., & Chaves, E. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/127984 · Cited by 94

Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration

Kuszczyk, M. A., Sanchez, S., Pankiewicz, J., Kim, J., Duszczyk, M., Guridi, M., Asuni, A. A., Sullivan, P. M., Holtzman, D. M., & Sadowski, M. J. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.01.034 · Cited by 89

Antibody-Mediated Clearance of Brain Amyloid-β: Mechanisms of Action, Effects of Natural and Monoclonal Anti-Aβ Antibodies, and Downstream Effects

Loeffler, D. A. (2023) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-230025 · Cited by 90

Murine models of Alzheimer's disease and their use in developing immunotherapies

Wısnıewskı, T., & Sigurdsson, E. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.05.004 · Cited by 84

Dopamine Transporter Endocytic Trafficking in Striatal Dopaminergic Neurons: Differential Dependence on Dynamin and the Actin Cytoskeleton

Gabriel, L. R., Wu, S., Kearney, P. J., Bellve, K. D., Standley, C., Fogarty, K. E., & Melikian, H. E. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3284-13.2013 · Cited by 78

Monoacylglycerol lipase inhibitor JZL184 reduces neuroinflammatory response in APdE9 mice and in adult mouse glial cells

Pihlaja, R., Helin, J. S., Eskola, O., Vasara, J., Lopez‐Picon, F. R., Haaparanta‐Solin, M., & Rinne, J. O. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0305-9 · Cited by 85

Herpes Simplex Virus Type-1 Infection Impairs Adult Hippocampal Neurogenesis via Amyloid-β Protein Accumulation

Puma, D. D. L., Piacentini, R., Leone, L., Gironi, K., Marcocci, M. E., Chiara, G. D., Palamara, A. T., & Grassi, C. (2019) · Stem Cells · doi:10.1002/stem.3072 · Cited by 75

Potential of the Antibody Against cis–Phosphorylated Tau in the Early Diagnosis, Treatment, and Prevention of Alzheimer Disease and Brain Injury

Lu, K. P., Kondo, A., Albayram, Ö., Herbert, M. K., Liu, H., & Zhou, X. Z. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.2027 · Cited by 74

Endogenous Aβ causes cell death via early tau hyperphosphorylation

Amadoro, G., Corsetti, V., Ciotti, M. T., Florenzano, F., Capsoni, S., Amato, G., & Calissano, P. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.06.005 · Cited by 74

Mechanistic Studies of Antibody-Mediated Clearance of Tau Aggregates Using an ex vivo Brain Slice Model

Krishnamurthy, P., Deng, Y., & Sigurdsson, E. M. (2011) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2011.00059 · Cited by 73

Antibodies against Alpha-Synuclein Reduce Oligomerization in Living Cells

Näsström, T., Gonçalves, S. A., Sahlin, C., Nordström, E. K. L., Sundquist, V. S., Lannfelt, L., Bergström, J. J. E., Outeiro, T. F., & Ingelsson, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027230 · Cited by 70

RAGE recycles at the plasma membrane in S100B secretory vesicles and promotes Schwann cells morphological changes

Perrone, L., Peluso, G., & Melone, M. A. B. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21474 · Cited by 66

Synaptic activity protects against AD and FTD-like pathology via autophagic-lysosomal degradation

Akwa, Y., Gondard, E., Mann, A., Capetillo‐Zarate, E., Alberdi, E. M., Matute, C., Marty, S., Vaccari, T., Lozano, A. M., Baulieu, E. E., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.142 · Cited by 62

Mutant Presenilin 1 Increases the Expression and Activity of BACE1

Giliberto, L., Borghi, R., Piccini, A., Mangerini, R., Sorbi, S., Cirmena, G., Garuti, A., Ghetti, B. F., Tagliavini, F., Mughal, M. R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805685200 · Cited by 56

Synapses, synaptic activity and intraneuronal Aβ in Alzheimer’s disease

Tampellini, D. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00013 · Cited by 58

Aβ1–42 reduces synapse number and inhibits neurite outgrowth in primary cortical and hippocampal neurons: A quantitative analysis

Evans, N. A., Facci, L., OWEN, D. E., Soden, P. E., Burbidge, S. A., Prinjha, R. K., Richardson, J. C., & Skaper, S. D. (2008) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2008.08.001 · Cited by 56

Vaccination as a Therapeutic Approach to Alzheimer's Disease

Wısnıewskı, T., & Boutajangout, A. (2010) · Mount Sinai Journal of Medicine A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20156 · Cited by 53

Soluble Beta-Amyloid Precursor Protein Is Related to Disease Progression in Amyotrophic Lateral Sclerosis

Steinacker, P., Fang, L., Kühle, J., Petzold, A., Tumani, H., Ludolph, A. C., Otto, M., & Brettschneider, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023600 · Cited by 44

Lipid rafts are primary mediators of amyloid oxidative attack on plasma membrane

Zampagni, M., Evangelisti, E., Cascella, R., Liguri, G., Becatti, M., Pensalfini, A., Uberti, D. L., Cenini, G., Memo, M., Bagnoli, S., et al. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0603-8 · Cited by 44

What is the role of amyloid precursor protein dimerization?

Khalifa, N. B., Hees, J. V., Tasiaux, B., Huysseune, S., Smith, S. O., Constantinescu, S. N., Octave, J., & Kienlen‐Campard, P. (2010) · Cell Adhesion & Migration · doi:10.4161/cam.4.2.11476 · Cited by 42

Does Impairment of Adult Neurogenesis Contribute to Pathophysiology of Alzheimer's Disease? A Still Open Question

Puma, D. D. L., Piacentini, R., & Grassi, C. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.578211 · Cited by 46

Intracellular Amyloid β-Protein As a Therapeutic Target for Treating Alzheimers Disease

Ohyagi, Y. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898514 · Cited by 42

Immunotherapeutic approaches for Alzheimer’s disease in transgenic mouse models

Wısnıewskı, T., & Boutajangout, A. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0236-2 · Cited by 39

Anti-tau oligomers passive vaccination for the treatment of Alzheimer disease

Kayed, R. (2010) · Human Vaccines · doi:10.4161/hv.6.11.12689 · Cited by 38

Antibodies to cell surface proteins redirect intracellular trafficking pathways

Pierre, C. A. S., Leonard, D. M., Corvera, S., Kurt‐Jones, E. A., & Finberg, R. W. (2011) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2011.05.011 · Cited by 38

Advances on the Understanding of the Origins of Synaptic Pathology in AD

Lacor, P. N. (2007) · Current Genomics · doi:10.2174/138920207783769530 · Cited by 40

Resistance is futile: antineuronal autoimmunity in multiple sclerosis.

Huizinga, R., Linington, C., & Amor, S. (2008) · Trends in immunology · doi:10.1016/j.it.2007.11.002 · Cited by 43

Naturally Occurring Autoantibodies Against β-Amyloid

Bach, J., & Dodel, R. C. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3461-0_7 · Cited by 36

Immunotherapy for Tauopathies

Gu, J., & Sigurdsson, E. M. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9576-5 · Cited by 36

Concentrations of beta-amyloid precursor protein processing products in cerebrospinal fluid of patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Steinacker, P., Hendrich, C., Sperfeld, A., Jesse, S., Lehnert, S., Pabst, A., Arnim, C. A. F. V., Mottaghy, F. M., Uttner, I., Tumani, H., et al. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0271-4 · Cited by 32

Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging

Wu, Q., Lin, Y., Gu, J., & Sigurdsson, E. M. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.08.041 · Cited by 31

Cognitive Enhancers (Nootropics). Part 3: Drugs Interacting with Targets other than Receptors or Enzymes. Disease-modifying Drugs

Froestl, W., Pfeifer, A., & Muhs, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121729 · Cited by 27

Tau Immunotherapies for Alzheimer’s Disease and Related Tauopathies: Status of Trials and Insights from Preclinical Studies

Sigurdsson, E. M. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231238 · Cited by 28

A relevant in vitro human model for the study of Zika virus antibody-dependent enhancement

Londono-Renteria, B. L., Troupin, A., Cardenas, J. C., Hall, A., Perez, O., Cardenas, L. D., Hartstone‐Rose, A., Halstead, S. B., & Colpitts, T. M. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000833 · Cited by 23

Lesion of the subiculum reduces the spread of amyloid beta pathology to interconnected brain regions in a mouse model of Alzheimer’s disease

George, S., Rönnbäck, A., Gouras, G. K., Petit, G. H., Grueninger, F., Winblad, B., Graff, C., & Brundin, P. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-17 · Cited by 23

Protein Conformational Pathology in Alzheimers and Other Neurodegenerative Diseases; New Targets for Therapy

Žerovnik, E. (2010) · Current Alzheimer Research · doi:10.2174/156720510790274437 · Cited by 23

Homo- and Heterodimerization of Proteins in Cell Signaling: Inhibition and Drug Design

Singh, S. S., & Jois, S. D. S. (2017) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2017.08.003 · Cited by 23

Non-invasive characterization of β-amyloid1-40 vasoactivity by functional magnetic resonance imaging in mice

Luo, F., Seifert, T. R., Edalji, R. P., Loebbert, R. W., Hradil, V. P., Harlan, J. E., Schmidt, M. U., Nimmrich, V., Cox, B. F., & Fox, G. B. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.04.021 · Cited by 23

Amyloid-β Peptide-specific DARPins as a Novel Class of Potential Therapeutics for Alzheimer Disease

Hanenberg, M., McAfoose, J., Kulic, L., Welt, T., Wirth, F., Parizek, P., Strobel, L., Cattepoel, S., Späni, C. B., Derungs, R., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564013 · Cited by 22

Harnessing the Immune System for Treatment and Detection of Tau Pathology

Congdon, E. E., Krishnaswamy, S., & Sigurdsson, E. M. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132435 · Cited by 20

Reciprocal regulation of cholesterol and beta amyloid at the subcellular level in Alzheimer’s disease

Chaves, E. (2012) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y2012-076 · Cited by 18

Neurofilament light as an immune target for pathogenic antibodies

Puentes, F., van der Star, B. J., Boomkamp, S. D., Kipp, M., Boon, L., Boscá, I., Raffel, J., Gnanapavan, S., van der Valk, P., Stephenson, J., et al. (2017) · Immunology · doi:10.1111/imm.12797 · Cited by 17

Recombinant GST-I-Aβ28-induced efficient serum antibody against Aβ42

Huang, X., Wang, J., Cui, L., Zou, X., & Zhang, Y. (2009) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2009.10.026 · Cited by 17

Immunotherapy for Alzheimer's disease: attacking amyloid-β from the inside

Arbel, M., & Solomon, B. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.09.005 · Cited by 16

Structures of Aβ-Related Peptide−Monoclonal Antibody Complexes,

Gardberg, A. S., Dice, L. T., Pridgen, K., Ko, J., Patterson, P. H., Ou, S. K.-H., Wetzel, R. B., & Dealwis, C. G. (2009) · Biochemistry · doi:10.1021/bi9001216 · Cited by 16

Prophylactic active immunization with a novel epitope vaccine improves cognitive ability by decreasing amyloid plaques and neuroinflammation in APP/PS1 transgenic mice

Ding, L., Meng, Y., Zhang, H., Yin, W., Yan, Y., & Cao, Y. (2017) · Neuroscience Research · doi:10.1016/j.neures.2017.01.003 · Cited by 15

The type of Aβ-related neuronal degeneration differs between amyloid precursor protein (APP23) and amyloid β-peptide (APP48) transgenic mice

Upadhaya, A. R., Scheibe, F., Kosterin, I., Abramowski, D., Gerth, J., Kumar, S., Liebau, S., Yamaguchi, H., Walter, J., Staufenbiel, M., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-77 · Cited by 14

Disease Modifying Therapies for Alzheimer's Disease Targeting AβOligomers: Implications for Therapeutic Mechanisms

Matsubara, E., Takamura, A., Okamoto, Y., Oono, H., Nakata, T., Wakasaya, Y., Kawarabayashi, T., & Shoji, M. (2013) · BioMed Research International · doi:10.1155/2013/984041 · Cited by 12

A light at the end of the tunnel – from mutation identification to a potential treatment for Alzheimer’s disease

Lannfelt, L. (2023) · Upsala Journal of Medical Sciences · doi:10.48101/ujms.v128.10316 · Cited by 12

An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature

Cascella, R., Banchelli, M., Ghadami, S. A., Ami, D., Gagliani, M. C., Bigi, A., Staderini, T., Tampellini, D., Cortese, K., Cecchi, C., et al. (2022) · Annals of Medicine · doi:10.1080/07853890.2022.2148734 · Cited by 10

Selective neutralization of APP-C99 with monoclonal antibodies reduces the production of Alzheimer's Aβ peptides

Houacine, J., Bolmont, T., Aeschbach, L., Oulad‐Abdelghani, M., & Fraering, P. C. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.12.033 · Cited by 10

Conformation‐specific antibodies against multiple amyloid protofibril species from a single amyloid immunogen

Bonito-Oliva, A., Schedin‐Weiss, S., Younesi, S. S., Tiiman, A., Adura, C., Paknejad, N., Brendel, M., Romin, Y., Parchem, R. J., Graff, C., et al. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14119 · Cited by 10

Anti-Aβ antibodies bound to neuritic plaques enhance microglia activity and mitigate tau pathology

Laversenne, V., Nazeeruddin, S., Källstig, E., Colin, P., Voize, C., & Schneider, B. L. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01069-3 · Cited by 11

Anti‐amyloid precursor protein immunoglobulins inhibit amyloid‐β production by steric hindrance

Thomas, R. S., Liddell, J. E., & Kidd, E. J. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07942.x · Cited by 10

Immunotherapies for Parkinson’s Disease: Progression of Clinical Development

Teng, J. S., Ooi, Y. Y., Chye, S. M., Ling, A. P. K., & Koh, R. Y. (2021) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527320666210526160926 · Cited by 10

Specific serum antibody binding to phosphorylated and non-phosphorylated tau in non-cognitively impaired, mildly cognitively impaired, and Alzheimer’s disease subjects: an exploratory study

Klaver, A. C., Coffey, M. P., Bennett, D. A., & Loeffler, D. A. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0100-x · Cited by 9

Therapeutic applications of antibodies in non-infectious neurodegenerative diseases

Krishnamurthy, P., & Sigurdsson, E. M. (2011) · New Biotechnology · doi:10.1016/j.nbt.2011.03.020 · Cited by 8

Endocytic mechanisms and drug discovery in neurodegenerative diseases

Zhang, M. (2008) · Frontiers in bioscience · doi:10.2741/3140 · Cited by 8

Multiple Antigenic Peptide System Coupled with Amyloid Beta Protein Epitopes As An Immunization Approach to Treat Alzheimer’s Disease

Sun, D., Qiao, Y., Jiang, X., Li, P., Kuai, Z., Gong, X., Liu, D., Fu, Q., Sun, L., He, L., et al. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00020 · Cited by 7

The toxicity of β-amyloid is attenuated by interaction with its specific human scFv E3 in vitro

Yue, S., Li, Y., Wang, X., Bai, H., Xia, J., Jiang, L., Ji, Y. I., Fan, L., He, Z.-G., & Chen, Q. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.04.009 · Cited by 7

Analysis of Vesicular Trafficking in Primary Neurons by Live Imaging

Tampellini, D., & Gouras, G. K. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-328-8_22 · Cited by 4

Developing injectable immunoglobulins to treat cognitive impairment in Alzheimer's disease

Steinitz, M. O. (2008) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.8.5.633 · Cited by 5

Tau Immunotherapy

Sigurdsson, E. M. (2016) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-3560-4_8 · Cited by 3

Nutrient signaling pathways regulate amyloid clearance and synaptic loss in Alzheimer’s diseasePreprint

Mondal, M., Bali, J., Tzioras, M., Paolicelli, R. C., Jawaid, A., Malnar, M., Dominko, K., Udayar, V., Halima, S. B., Vadodaria, K. C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.13.381186 · Cited by 3

Aβ antibodies target not only amyloid plaques but also distinct brain cells and vessels

Wen, G., Lindblom, N., Zhan, X., Garcia, M. G., Deierborg, T., Kobro‐Flatmoen, A., & Gouras, G. K. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71121 · Cited by 2

O4–06–08: Internalized antibodies to the Aβ domain of APP reduce intraneuronal Aβ and protect against synaptic alterations

Tampellini, D., Magrané, J., Takahashi, R. H., Li, F., Almeida, C. G., & Gouras, G. K. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.343

Amyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo

Klyubin, I., Walsh, D. M., Lemere, C. A., Cullen, W. K., Shankar, G. M., Betts, V., Spooner, E. T., Jiang, L., Anwyl, R., Selkoe, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1234 · Cited by 489

Immunotherapy for Alzheimer's disease: attacking amyloid-β from the inside

Arbel, M., & Solomon, B. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.09.005 · Cited by 16

The role of intracellular amyloid β in Alzheimer's disease

Li, M. C., Chen, L., Lee, D. H. S., Yu, L., & Zhang, Y. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.08.002 · Cited by 118

β-Amyloid Immunotherapy Prevents Synaptic Degeneration in a Mouse Model of Alzheimer's Disease

Buttini, M., Masliah, E., Barbour, R., Grajeda, H., Motter, R., Johnson-Wood, K., Khan, K., Seubert, P., Freedman, S., Schenk, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1697-05.2005 · Cited by 176