Cellular Receptors of Amyloid β Oligomers (AβOs) in Alzheimer’s Disease
Open accessAbstract
It is estimated that Alzheimer’s disease (AD) affects tens of millions of people, comprising not only suffering patients, but also their relatives and caregivers. AD is one of age-related neurodegenerative diseases (NDs) characterized by progressive synaptic damage and neuronal loss, which result in gradual cognitive impairment leading to dementia. The cause of AD remains still unresolved, despite being studied for more than a century. The hallmark pathological features of this disease are senile plaques within patients’ brain composed of amyloid beta (Aβ) and neurofibrillary tangles (NFTs) of Tau protein. However, the roles of Aβ and Tau in AD pathology are being questioned and other causes of AD are postulated. One of the most interesting theories proposed is the causative role of amyloid β oligomers (AβOs) aggregation in the pathogenesis of AD. Moreover, binding of AβOs to cell membranes is probably mediated by certain proteins on the neuronal cell surface acting as AβO receptors. The aim of our paper is to describe alternative hypotheses of AD etiology, including genetic alterations and the role of misfolded proteins, especially Aβ oligomers, in Alzheimer’s disease. Furthermore, in this review we present various putative cellular AβO receptors related to toxic activity of oligomers.
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Misfolded Aβ and tau proteins accumulate in the AD brain in a neurodegenerative cascade leading to cognitive decline and dementia.
“Misfolded Aβ and tau proteins accumulate in the AD brain in a neurodegenerative cascade leading to cognitive decline and dementia [4,5,6,7,8,9].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [8]
Cognitive deficits in mild cognitive impairment patients and decreased executive and reasoning abilities in Alzheimer's disease are caused by oxidative damage of small Aβ oligomers to synaptic membranes.
“Cognitive deficits in MCI patients and decreased executive and reasoning abilities in AD are caused by the oxidative damage of small Aβ oligomers to the synaptic membranes [83,84,85].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [83]
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Cites
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
The nuclear receptor superfamily: the second decade
Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90199-x · Cited by 6,964 · see citing works
G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALS
Gilman, A. G. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.003151 · Cited by 6,405 · see citing works
The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works
Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268 · 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
Hearing loss and cognitive decline in older adults
Lin, F. R., Yaffe, K., Xia, J., Xue, Q.-L., Harris, T. B., Purchase-Helzner, E., Satterfield, S., Ayonayon, H. N., Ferrucci, L., Simonsick, E. M., et al. (2013) · JAMA Internal Medicine · doi:10.1001/jamainternmed.2013.1868 · Cited by 4,017 · see citing works
Clinical and biomarker changes in dominantly inherited Alzheimer's disease
Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814 · see citing works
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
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
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · see citing works
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492 · see citing works
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012 · see citing works
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works
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
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592 · see citing works
Translating cell biology into therapeutic advances in Alzheimer's disease
Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,588 · see citing works
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · 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
Neeper, M. P., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y., Elliston, K. O., Stern, D., & SHAW, A. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42138-2 · Cited by 1,542 · see citing works
Uber eine eigenartige Erkrankung der Hirnrinde
Alzheimer, A. (1907) · Medical Entomology and Zoology · Cited by 1,503 · see citing works
Borchelt, D. R., Thinakaran, G., Eckman, C. B., Lee, M. K., Davenport, F., Ratovitsky, T., Prada, C.-M., Kim, G., Seekins, S., Yager, D., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80230-5 · Cited by 1,478 · see citing works
Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance
Castellano, J. M., Kim, J., Stewart, F. R., Jiang, H., DeMattos, R. B., Patterson, B. W., Fagan, A. M., Morris, J. C., Mawuenyega, K. G., Cruchaga, C., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002156 · Cited by 1,227 · cited 1× · see citing works
“Additionally, a quantitative evaluation in transgenic mice bearing human APP and APOE genes has shown decreased Aβ clearance in APOE4 carriers in comparison with E3 and E2 mice, which was paralleled by the degree of Aβ deposition [21].”
BackgroundLacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188 · see citing works
Alzheimer disease: Epidemiology, diagnostic criteria, risk factors and biomarkers
Reitz, C., & Mayeux, R. P. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.024 · Cited by 1,180 · see citing works
Alzheimer’s disease is type 3 diabetes—Evidence reviewed
de la Monte, S. M., & Wands, J. R. (2008) · Journal of Diabetes Science and Technology · doi:10.1177/193229680800200619 · Cited by 1,158 · see citing works
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works
Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions
William Rebeck, G., Reiter, J. S., Strickland, D. K., & Hyman, B. T. (1993) · Neuron · doi:10.1016/0896-6273(93)90070-8 · Cited by 1,107 · see citing works
Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
Ehehalt, R., Keller, P., Haass, C., Thiele, C., & Simons, K. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207113 · Cited by 1,107 · see citing works
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
AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042 · see citing works
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
Tau pathology in Alzheimer disease and other tauopathies
Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037 · see citing works
Mahley, R. W., Weisgraber, K. H., & Huang, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600549103 · Cited by 912 · see citing works
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882 · see citing works
Ma, J., Yee, A., Brewer, H. B., Das, S., & Potter, H. (1994) · Nature · doi:10.1038/372092a0 · Cited by 871 · see citing works
Koffie, R. M., Meyer-Luehmann, M., Hashimoto, T., Adams, K. W., Mielke, M. L., Garcia-Alloza, M., Micheva, K. D., Smith, S. J., Kim, M. L., Lee, V. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811698106 · Cited by 850 · see citing works
Megalin and cubilin: multifunctional endocytic receptors
Christensen, E., & Birn, H. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm778 · Cited by 829 · see citing works
Diabetes-Associated Sustained Activation of the Transcription Factor Nuclear Factor-κB
Bierhaus, A., Schiekofer, S., Schwaninger, M., Andrassy, M., Humpert, P. M., Chen, J., Hong, M., Luther, T., Henle, T., Klöting, I., et al. (2001) · Diabetes · doi:10.2337/diabetes.50.12.2792 · Cited by 826 · see citing works
Synaptic alterations in CA1 in mild Alzheimer disease and mild cognitive impairment
Scheff, S. W., Price, D. A., Schmitt, F. A., DeKosky, S. T., & Mufson, E. J. (2007) · Neurology · doi:10.1212/01.wnl.0000260698.46517.8f · Cited by 824 · see citing works
β-Amyloid1–42 Binds to α7 Nicotinic Acetylcholine Receptor with High Affinity
Wang, H.-Y., Lee, D. H. S., D’Andrea, M. R., Peterson, P. A., Shank, R. P., & Reitz, A. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5626 · Cited by 818 · see citing works
Apolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease
Holtzman, D. M., Herz, J., & Bu, G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006312 · Cited by 782 · see citing works
TREM2 Is a Receptor for β-Amyloid that Mediates Microglial Function
Zhao, Y., Wu, X., Li, X., Jiang, L.-L., Gui, X., Liu, Y., Sun, Y., Zhu, B., Piña-Crespo, J. C., Zhang, M., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.031 · Cited by 763 · see citing works
Maruyama, M., Shimada, H., Suhara, T., Shinotoh, H., Ji, B., Maeda, J., Zhang, M.-R., Trojanowski, J. Q., Lee, V. M.-Y., Ono, M., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.037 · Cited by 760 · see citing works
Turner, P. R., O’Connor, K., Tate, W. P., & Abraham, W. C. (2003) · Progress in Neurobiology · doi:10.1016/s0301-0082(03)00089-3 · Cited by 751 · see citing works
The role of inflammation in Alzheimer’s disease
Tuppo, E. E., & Arias, H. R. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.07.009 · Cited by 734 · see citing works
Evolution of the neuropathology of Alzheimer's disease
Braak, H., & Braak, E. (1996) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1996.tb05866.x · Cited by 710 · see citing works
Duce, J. A., Tsatsanis, A., Cater, M. A., James, S., Robb, E. L., Wikhe, K., Leong, S. L., Perez, K. A., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 682 · see citing works
De Felice, F. G., Vieira, M. N. N., Bomfim, T. R., Decker, H., Velasco, P. T., Lambert, M. P., Viola, K. L., Zhao, W.-Q., Ferreira, S. T., & Klein, W. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809158106 · Cited by 657 · see citing works
Control of GluR1 AMPA receptor function by cAMP-dependent protein kinase
Banke, T. G., Bowie, D., Lee, H.-K., Huganir, R. L., Schousboe, A., & Traynelis, S. F. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00089.2000 · Cited by 652 · see citing works
Proteolytic processing and cell biological functions of the amyloid precursor protein
Strooper, B. D., & Annaert, W. G. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.11.1857 · Cited by 628 · see citing works
Dechant, G., & Barde, Y. (2002) · Nature Neuroscience · doi:10.1038/nn1102-1131 · Cited by 606 · see citing works
Lemere, C. A., Blusztajn, J. K., Yamaguchi, H., Wisniewski, T., Saido, T. C., & Selkoe, D. J. (1996) · Neurobiology of Disease · doi:10.1006/nbdi.1996.0003 · Cited by 584 · see citing works
Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572 · see citing works
Late onset Alzheimer’s disease genetics implicates microglial pathways in disease risk
Efthymiou, A. G., & Goate, A. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0184-x · Cited by 562 · see citing works
Saito, A., Pietromonaco, S. F., Loo, A. K., & Farquhar, M. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.21.9725 · Cited by 561 · see citing works
Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
Lansbury, P. T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3342 · Cited by 553 · see citing works
Deane, R., Bell, R. D., Sagare, A. P., & Zloković, B. V. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601867 · Cited by 549 · see citing works
Synapse Formation and Function Is Modulated by the Amyloid Precursor Protein
Priller, C., Bauer, T., Mitteregger, G., Krebs, B., Kretzschmar, H. A., & Herms, J. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1450-06.2006 · Cited by 548 · see citing works
Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527 · see citing works
Self-Assembly of Aβ <sub>1</sub> <sub>-</sub> <sub>42</sub> into Globular Neurotoxins
Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., Jones, B. W., Fernandez, S. J., Lacor, P. N., Horowitz, P., et al. (2003) · Biochemistry · doi:10.1021/bi030029q · Cited by 522 · see citing works
Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling
Murai, K. K., Nguyen, L. N., Irie, F., Yamaguchi, Y., & Pasquale, E. B. (2003) · Nature Neuroscience · doi:10.1038/nn994 · Cited by 516 · see citing works
Alzheimer's disease – do tauists and baptists finally shake hands?
Mudher, A. K., & Lovestone, S. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)02031-2 · Cited by 512 · see citing works
PirB is a Functional Receptor for Myelin Inhibitors of Axonal Regeneration
Atwal, J. K., Pinkston-Gosse, J., Syken, J., Stawicki, S. S., Wu, Y., Shatz, C. J., & Tessier‐Lavigne, M. (2008) · Science · doi:10.1126/science.1161151 · Cited by 503 · see citing works
Modulation of NMDA Receptor- Dependent Calcium Influx and Gene Expression Through EphB Receptors
Takasu, M. A., Dalva, M. B., Zigmond, R. E., & Greenberg, M. E. (2002) · Science · doi:10.1126/science.1065983 · Cited by 497 · see citing works
SIRT1 in Neurodevelopment and Brain Senescence
Herskovits, A. Z., & Guarente, L. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.028 · Cited by 493 · see citing works
Apolipoprotein E, Dementia, and Cortical Deposition of β-Amyloid Protein
Polvikoski, T., Sulkava, R., Haltia, M., Kainulainen, K., Vuorio, A., Verkkoniemi, A., Niinistö, L., Halonen, P., & Kontula, K. (1995) · New England Journal of Medicine · doi:10.1056/nejm199511093331902 · Cited by 493 · see citing works
Lemere, C. A., Lopera, F., Kosik, K. S., Lendon, C. L., Ossa, J., Saido, T. C., Yamaguchi, H., Ruiz, A., Martinez, A., Madrigal, L., et al. (1996) · Nature Medicine · doi:10.1038/nm1096-1146 · Cited by 487 · see citing works
Sirtuin 1 Reduction Parallels the Accumulation of Tau in Alzheimer Disease
Julien, C., Tremblay, C., Émond, V., Lebbadi, M., Salem, N., Bennett, D. A., & Calon, F. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181922348 · Cited by 467 · see citing works
Glycans in the immune system and The Altered Glycan Theory of Autoimmunity: A critical review
Maverakis, E. M., Kim, K., Shimoda, M., Gershwin, M. E., Patel, F., Wilken, R., Raychaudhuri, S. P., Ruhaak, L. R., & Lebrilla, C. B. (2015) · Journal of Autoimmunity · doi:10.1016/j.jaut.2014.12.002 · Cited by 456 · see citing works
Nagele, R. G., D’Andrea, M. R., Anderson, W. J., & Wang, H.-Y. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00460-2 · Cited by 456 · see citing works
Johnson, L. V., Leitner, W. P., Rivest, A. J., Staples, M. K., Radeke, M. J., & Anderson, D. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192203399 · Cited by 447 · see citing works
Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro.
(1994) · PubMed Central · Cited by 441 · see citing works
TREM2, microglia, and neurodegenerative diseases
Yeh, F. L., Hansen, D. V., & Sheng, M. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.008 · Cited by 440 · cited 10× · see citing works
“Normal proteolytic maturation of full-length TREM2 at the plasma membrane is disturbed in mutations of TREM2 gene, resulting in impaired phagocytosis, which may contribute to the pathogenesis of AD [179].”
BackgroundInfluentialReversing EphB2 depletion rescues cognitive functions in Alzheimer model
Cissé, M., Halabisky, B., Harris, J., Devidze, N., Dubal, D. B., Sun, B., Orr, A., Lotz, G., Kim, D. H., Hamto, P., et al. (2011) · Nature · doi:10.1038/nature09635 · Cited by 433 · see citing works
Zlokovic, B. V., Martel, C. L., Matsubara, E., McComb, J. G., Zheng, G., McCluskey, R. T., Frangione, B., & Ghiso, J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4229 · Cited by 430 · see citing works
Bidirectional modulation of synaptic functions by Eph/ephrin signaling
Klein, R. (2008) · Nature Neuroscience · doi:10.1038/nn.2231 · 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
Association of γ-Secretase with Lipid Rafts in Post-Golgi and Endosome Membranes
Vetrivel, K. S., Cheng, H., Lin, W., Sakurai, T., Li, T., Nukina, N., Wong, P. C., Xu, H., & Thinakaran, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407986200 · Cited by 413 · see citing works
Noradrenergic mechanisms in neurodegenerative diseases: a theory
Marien, M. R., Colpaert, F. C., & Rosenquist, A. C. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.02.002 · Cited by 411 · see citing works
Kim, T., Vidal, G. S., Djurisic, M., William, C. M., Birnbaum, M. E., Garcia, K. C., Hyman, B. T., & Shatz, C. J. (2013) · Science · doi:10.1126/science.1242077 · Cited by 410 · see citing works
The amyloid precursor protein: beyond amyloid.
Zheng, H., & Koo, E. H. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-5 · Cited by 403 · see citing works
Deane, R., Wu, Z., & Zlokovic, B. V. (2004) · Stroke · doi:10.1161/01.str.0000143452.85382.d1 · Cited by 392 · see citing works
Boehm, J., Kang, M.-G., Johnson, R. C., Esteban, J., Huganir, R. L., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.06.013 · Cited by 382 · see citing works
Alberdi, E. M., Sánchez‐Gómez, M. V., Cavaliere, F., Pérez‐Samartín, A., Zugaza, J. L., Trullás, R., Domercq, M., & Matute, C. (2010) · Cell Calcium · doi:10.1016/j.ceca.2009.12.010 · Cited by 364 · see citing works
Li, F. R., & Tsien, J. Z. (2009) · New England Journal of Medicine · doi:10.1056/nejmcibr0902052 · Cited by 363 · see citing works
APOE genotype-specific differences in the innate immune response
Vitek, M. P., Brown, C. M., & Colton, C. A. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.11.014 · Cited by 362 · see citing works
Aβ40 Inhibits Amyloid Deposition<i>In Vivo</i>
Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D. W., Golde, T., & McGowan, E. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4849-06.2007 · Cited by 359 · see citing works
Amyloid beta from axons and dendrites reduces local spine number and plasticity
Wei, W., Nguyen, L. N., Kessels, H. W., Hagiwara, H., Sisodia, S., & Malinow, R. (2010) · Nature Neuroscience · doi:10.1038/nn.2476 · Cited by 357 · see citing works
Liang, F.-X., Kume, S., & Koya, D. (2009) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2009.101 · Cited by 356 · 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
Yang, T., Li, S., Xu, H., Walsh, D. M., & Selkoe, D. J. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1698-16.2016 · Cited by 347 · see citing works
Oxidative Stress Signaling in Alzheimers Disease
Su, B., Wang, X., Nunomura, A., Moreira, P., Lee, H.-G., Perry, G., Smith, M., & Zhu, X. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898451 · Cited by 344 · see citing works
Genetic Classification of Primary Neurodegenerative Disease
Hardy, J., & Gwinn, K. A. (1998) · Science · doi:10.1126/science.282.5391.1075 · Cited by 341 · see citing works
PirB restricts ocular-dominance plasticity in visual cortex
Syken, J., GrandPre, T., Kanold, P. O., & Shatz, C. J. (2006) · Science · doi:10.1126/science.1128232 · Cited by 340 · see citing works
How does brain insulin resistance develop in Alzheimer's disease?
De Felice, F. G., Lourenco, M. V., & Ferreira, S. T. (2014) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2013.12.004 · Cited by 337 · see citing works
Immune signalling in neural development, synaptic plasticity and disease
Boulanger, L. M., & Shatz, C. J. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1428 · Cited by 334 · see citing works
Evans, K. C., Berger, E. P., Cho, C. G., Weisgraber, K. H., & Lansbury, P. T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.763 · Cited by 333 · see citing works
The radiologic prediction of Alzheimer disease: the atrophic hippocampal formation.
de Leon, M. J., Golomb, J. B., GEORGE, A. E., Convit, A. J., Tarshish, C. Y., McRae, T., Santi, S. D., Smith, G. S., Ferris, S. H., & Noz, M. E. (1993) · PubMed Central · Cited by 322 · see citing works
A novel pair of immunoglobulin-like receptors expressed by B cells and myeloid cells
Kubagawa, H., Burrows, P. D., & Cooper, M. D. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5261 · Cited by 319 · see citing works
Soluble Aβ Inhibits Specific Signal Transduction Cascades Common to the Insulin Receptor Pathway
Townsend, M., Mehta, T., & Selkoe, D. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610390200 · Cited by 318 · see citing works
Coding variants in TREM2 increase risk for Alzheimer's disease
Jin, S. C., Benitez, B. A., Karch, C. M., Cooper, B., Skorupa, T., Carrell, D., Norton, J. B., Hsu, S., Harari, O., Cai, Y., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu277 · Cited by 314 · see citing works
Type 3 diabetes is sporadic Alzheimer׳s disease: Mini-review
de la Monte, S. M. (2014) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2014.06.008 · Cited by 312 · see citing works
EPHA4 is a disease modifier of amyotrophic lateral sclerosis in animal models and in humans
Hoecke, A. V., Schoonaert, L., Lemmens, R., Timmers, M., Staats, K. A., Laird, A. S., Peeters, E., Philips, T., Goris, A., Dubois, B., et al. (2012) · Nature Medicine · doi:10.1038/nm.2901 · Cited by 304 · see citing works
Compartmentalization of β-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
Riddell, D. R., Christie, G., Hussain, I., & Dingwall, C. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00394-3 · Cited by 303 · see citing works
Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus
Henkemeyer, M. J., Itkis, O. S., Ngo, M., Hickmott, P. W., & Ethell, I. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200306033 · Cited by 302 · see citing works
TMP21 is a presenilin complex component that modulates γ-secretase but not ɛ-secretase activity
Chen, F., Hasegawa, H., Schmitt‐Ulms, G., Kawarai, T., Böhm, C., Katayama, T., Gu, Y., Sanjo, N., Glista, M. J., Rogaeva, E. A., et al. (2006) · Nature · doi:10.1038/nature04667 · Cited by 301 · see citing works
Song, W., Hooli, B., Mullin, K., Jin, S. C., Cella, M., Ulland, T. K., Wang, Y., Tanzi, R. E., & Colonna, M. (2017) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.07.004 · Cited by 297 · see citing works
Changes in Brain Function Occur Years before the Onset of Cognitive Impairment
Beason‐Held, L. L., Goh, J. O. S., An, Y., Kraut, M. A., O’Brien, R., Ferrucci, L., & Resnick, S. M. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1402-13.2013 · Cited by 289 · see citing works
Interaction between Human Prion Protein and Amyloid-β (Aβ) Oligomers
Chen, S., Yadav, S. P., & Surewicz, W. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145516 · Cited by 288 · see citing works
Thomas, M. J., Moody, T. D., Makhinson, M., & O’Dell, T. J. (1996) · Neuron · doi:10.1016/s0896-6273(00)80179-8 · Cited by 283 · see citing works
Cellular prion protein regulates β-secretase cleavage of the Alzheimer's amyloid precursor protein
Parkin, E. T., Watt, N. T., Hussain, I., Eckman, E. A., Eckman, C. B., Manson, J. C., Baybutt, H. N., Turner, A. J., & Hooper, N. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609621104 · Cited by 274 · 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
Szot, P., White, S. S., Greenup, J. L., Leverenz, J. B., Peskind, E. R., & Raskind, M. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4265-05.2006 · Cited by 249 · see citing works
Spreading of Neurodegenerative Pathology via Neuron-to-Neuron Transmission of -Amyloid
Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J., & Hallbeck, M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0615-12.2012 · Cited by 244 · see citing works
You, H., Tsutsui, S., Hameed, S., Kannanayakal, T. J., Chen, L., Xia, P., Engbers, J. D. T., Lipton, S. A., Stys, P. K., & Zamponi, G. W. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110789109 · Cited by 243 · see citing works
Genome-Wide Association Studies in Alzheimer Disease
Waring, S. C., & Rosenberg, R. N. (2008) · Archives of Neurology · doi:10.1001/archneur.65.3.329 · Cited by 238 · see citing works
Ni, Y., Zhao, X., Bao, G., Zou, L., Teng, L., Wang, Z., Song, M., Xiong, J., Bai, Y., & Pei, G. (2006) · Nature Medicine · doi:10.1038/nm1485 · Cited by 237 · see citing works
Interacting Brain Systems Modulate Memory Consolidation
McIntyre, C. K., McGaugh, J. D., & Williams, C. (2011) · Neuroscience and Biobehavioral Reviews · doi:10.1016/j.neubiorev.2011.11.001 · Cited by 233 · see citing works
Lanz, T. A., Carter, D. B., & Merchant, K. M. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00079-2 · Cited by 227 · see citing works
Identification of Glycoprotein 330 as an Endocytic Receptor for Apolipoprotein J/Clusterin
Kounnas, M. Z., Loukinova, E. B., Stefansson, S., Harmony, J. A. K., Brewer, B., Strickland, D. K., & Argraves, W. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13070 · Cited by 225 · see citing works
Dysregulation of neuronal calcium homeostasis in Alzheimer's disease – A therapeutic opportunity?
Александровна, П. Е., Pchitskaya, E. I., & Борисович, Б. И. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.053 · Cited by 213 · see citing works
Alzheimer disease and Down syndrome: factors in pathogenesis
Lott, I. T., & Head, E. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.08.005 · Cited by 212 · see citing works
Oddo, S., Caccamo, A., Green, K. N., Liang, K., Tran, L., Chen, Y., Leslie, F. M., & LaFerla, F. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408500102 · Cited by 211 · see citing works
Selective neuronal degeneration induced by soluble oligomeric amyloid beta‐protein
Kim, H., Chae, S., Lee, D., Chromy, B. A., Lee, S. C., Park, Y., Klein, W. L., Krafft, G. A., & Hong, S. (2002) · The FASEB Journal · doi:10.1096/fj.01-0987fje · Cited by 210 · see citing works
Neuronal amyloid-β accumulation within cholinergic basal forebrain in ageing and Alzheimer’s disease
Baker‐Nigh, A., Vahedi, S., Davis, E., Weıntraub, S., Bigio, E. H., Klein, W. L., & Geula, C. (2015) · Brain · doi:10.1093/brain/awv024 · Cited by 205 · see citing works
Gelinas, J. N., & Nguyen, P. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4175-04.2005 · Cited by 205 · see citing works
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
Fu, A. K. Y., Hung, K.-W., Huang, H., Gu, S., Shen, Y., Cheng, E. Y. L., Ip, F. C. F., Huang, X., Fu, W.-Y., & Ip, N. Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405803111 · Cited by 201 · see citing works
Weksler, M. E., Relkin, N. R., Turkenich, R., LaRusse, S., Zhou, L., & Szabo, P. (2002) · Experimental Gerontology · doi:10.1016/s0531-5565(02)00029-3 · Cited by 200 · see citing works
Hammad, S. M., Ranganathan, S., Loukinova, E. B., Twal, W. O., & Argraves, W. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18644 · Cited by 197 · see citing works
New Insights into the Roles of Megalin/LRP2 and the Regulation of its Functional Expression
Marzolo, M., & Farfán, P. (2011) · Biological Research · doi:10.4067/s0716-97602011000100012 · Cited by 195 · see citing works
Zhao, W.-Q., Santini, F., Breese, R., Ross, D., Zhang, X. D., Stone, D. J., Ferrer, M., Townsend, M., Wolfe, A. L., Seager, M. A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057182 · Cited by 188 · see citing works
Aβ-independent processes—rethinking preclinical AD
Chételat, G. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.21 · Cited by 184 · see citing works
APCCdh1 mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity
Fu, A. K. Y., Hung, K.-W., Fu, W., Shen, C., Chen, Y., Xia, J., Lai, K., & Ip, N. Y. (2010) · Nature Neuroscience · doi:10.1038/nn.2715 · Cited by 181 · see citing works
Tau Proteins and Neurofibrillary Degeneration
Goedert, M., Spillantini, M. G., & Crowther, R. A. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00671.x · Cited by 178 · see citing works
Li, S., Jin, M., Zhang, D., Yang, T., Koeglsperger, T., Fu, H., & Selkoe, D. J. (2013) · Neuron · doi:10.1016/j.neuron.2012.12.040 · Cited by 177 · see citing works
Role of adrenoceptor subtypes in memory consolidation
Gibbs, M. E., & Summers, R. J. (2002) · Progress in Neurobiology · doi:10.1016/s0301-0082(02)00023-0 · Cited by 175 · see citing works
Ephrin regulation of synapse formation, function and plasticity
Hruska, M., & Dalva, M. B. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.03.004 · Cited by 162 · see citing works
Chin, J., Palop, J. J., Yu, G.-Q., Kojima, N., Masliah, E., & Mucke, L. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0277-04.2004 · Cited by 161 · see citing works
The role of APOE on lipid homeostasis and inflammation in normal brains
Rebeck, G. W. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075408 · Cited by 160 · see citing works
Synaptotoxicity of Alzheimer Beta Amyloid Can Be Explained by Its Membrane Perforating Property
Sepúlveda, F. J., Parodí, J., Peoples, R. W., Opazo, C., & Aguayo, L. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011820 · Cited by 155 · see citing works
Eph receptors in the adult brain
Yamaguchi, Y., & Pasquale, E. B. (2004) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2004.04.003 · Cited by 154 · see citing works
Perini, G., Bianca, V. D., Politi, V., Valle, G. D., Prà, I. D., Rossi, F., & Armato, U. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20011797 · Cited by 152 · see citing works
Zhao, D., Watson, J. B., & Xie, C.-W. (2004) · Journal of Neurophysiology · doi:10.1152/jn.00485.2004 · Cited by 151 · see citing works
Domert, J., Rao, S. B., Agholme, L., Brorsson, A., Marcusson, J. O., Hallbeck, M., & Nath, S. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.12.019 · Cited by 151 · see citing works
The role of tau phosphorylation and cleavage in neuronal cell death
Chun, W. (2006) · Frontiers in bioscience · doi:10.2741/2097 · Cited by 142 · see citing works
Haas, L. T., Salazar, S. V., Kostylev, M. A., Um, J. W., Kaufman, A. C., & Strittmatter, S. M. (2015) · Brain · doi:10.1093/brain/awv356 · Cited by 140 · see citing works
Brain Insulin Resistance in Alzheimer's Disease and its Potential Treatment with GLP-1 Analogs
Talbot, K. (2014) · Neurodegenerative Disease Management · doi:10.2217/nmt.13.73 · Cited by 139 · see citing works
Yamin, G. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.21998 · Cited by 136 · see citing works
Site-Specific Blockade of RAGE-V<sub>d</sub>Prevents Amyloid-β Oligomer Neurotoxicity
Sturchler, E., Galichet, A., Weibel, M., Leclerc, E., & Heizmann, C. W. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4878-07.2008 · Cited by 136 · see citing works
Nistor, M., Don, M., Parekh, M., Sarsoza, F. M., Goodus, M. T., López, G., Kawas, C. H., Leverenz, J. B., Doran, E. W., Lott, I. T., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.023 · Cited by 135 · see citing works
Maren, S., Tocco, G., Standley, S., Baudry, M., & Thompson, R. F. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9654 · Cited by 134 · see citing works
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
Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131 · see citing works
FcγRIIb mediates amyloid-β neurotoxicity and memory impairment in Alzheimer’s disease
Kam, T.-I., Song, S., Gwon, Y., Park, H., Yan, J.-J., Im, I., Choi, J.-W., Choi, T.-Y., Kim, J., Song, D.-K., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66827 · Cited by 128 · see citing works
Amyloid-β effects on synapses and memory require AMPA receptor subunit GluA3
Reinders, N. R., Pao, Y., Renner, M., Matos, C. D. S., Lodder, T. R., Malinow, R., & Kessels, H. W. H. G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614249113 · Cited by 126 · see citing works
Heraldo, F. H., Arantes, C., Santos, T. G., Machado, C. F., Roffé, M., Haji, G. N., Lee, K. S., Magalhães, A. C., Caetano, F. A., Mancini, G. L., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-161653 · Cited by 123 · see citing works
Targeting Orphan Nuclear Receptors for Treatment of Metabolic Diseases and Autoimmunity
Burris, T. P., Busby, S. A., & Griffin, P. R. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.12.011 · Cited by 119 · see citing works
Walling, S. G., & Harley, C. W. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4426-03.2004 · Cited by 117 · see citing works
Williams, C., Mehrian Shai, R., Wu, Y., Hsu, Y.-H., Sitzer, T., Spann, B., McCleary, C., Mo, Y., & Miller, C. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004936 · Cited by 116 · see citing works
Lin, Y., Min, M., Chiu, T., & Yang, H. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-10-04173.2003 · Cited by 116 · see citing works
Gutierrez-Castellanos, N., Da Silva-Matos, C. M., Zhou, K., Canto, C. B., Renner, M. C., Koene, L. M. C., Ozyildirim, O., Sprengel, R., Kessels, H. W., & De Zeeuw, C. I. (2017) · Neuron · doi:10.1016/j.neuron.2016.11.046 · Cited by 111 · see citing works
Simón, A. M., de Maturana, R. L., Ricobaraza, A., Escribano, L., Schiapparelli, L., Cuadrado‐Tejedor, M., Pérez‐Mediavilla, A., Ávila, J., Rı́o, J. D., & Frechilla, D. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1096 · Cited by 110 · see citing works
Lee, H. R., Shin, H. K., Park, S. Y., Kim, H. Y., Lee, W. S., Rhim, B. Y., Hong, K. W., & Kim, C. D. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23421 · Cited by 110 · see citing works
Beraldo, F. H., Arantes, C., Santos, T. G., Queiroz‐Hazarbassanov, N., Young, K. F., Rylett, R. J., Markus, R. P., Prado, M. A. M., & Martins, V. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157263 · Cited by 106 · see citing works
Miñano-Molina, A. J., España, J., Martín, E., Barneda‐Zahonero, B., Fadó, R., Solé, M., Trullás, R., Saura, C. A., & Rodrı́guez-Álvarez, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.227504 · Cited by 103 · see citing works
Assembly of a β2‐adrenergic receptor—GluR1 signalling complex for localized cAMP signalling
Joiner, M.-L. A., Lisé, M.-F., Yuen, E. Y., Kam, A. Y. F., Zhang, M., Hall, D. D., Malik, Z. A., Qian, H., Chen, Y., Ulrich, J. D., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.344 · Cited by 101 · see citing works
Younan, N. D., Sarell, C. J., Davies, P., Brown, D. R., & Viles, J. H. (2013) · The FASEB Journal · doi:10.1096/fj.12-222588 · Cited by 100 · see citing works
Why Vitamin D in Alzheimer's Disease? The Hypothesis
Gezen‐Ak, D., Yılmazer, S., & Dursun, E. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131970 · Cited by 98 · see citing works
Alzheimer's disease: The forgetting gene
Spinney, L. (2014) · Nature · doi:10.1038/510026a · Cited by 98 · see citing works
Ito, S., Ohtsuki, S., Nezu, Y., Koitabashi, Y., Murata, S., & Terasaki, T. (2011) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-8-20 · Cited by 97 · see citing works
Wang, D., Govindaiah, G., Liu, R., Arcangelis, V. D., Cox, C. L., & Xiang, Y. K. (2010) · The FASEB Journal · doi:10.1096/fj.10-156661 · Cited by 95 · see citing works
Zhang, Y., Hong, Y., Bounhar, Y., Blacker, M., Roucou, X., Tounekti, O., Vereker, E., Bowers, W. J., Federoff, H. J., Goodyer, C. G., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-19-07385.2003 · Cited by 92 · see citing works
A Ganglioside-induced Toxic Soluble Aβ Assembly
Yamamoto, N., Matsubara, E., Maeda, S., Minagawa, H., Takashima, A., Maruyama, W., Michikawa, M., & Yanagisawa, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606202200 · Cited by 91 · see citing works
Aβ propagation and strains: Implications for the phenotypic diversity in Alzheimer's disease
Condello, C., & Stöhr, J. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.03.014 · Cited by 87 · see citing works
EphA4 Activation of c-Abl Mediates Synaptic Loss and LTP Blockade Caused by Amyloid-β Oligomers
Vargas, L. M., Leal, N. R., Estrada, L. D., González, A., Serrano, F. G., Araya, K. A., Gysling, K., Inestrosa, N. C., Pasquale, E. B., & Alvarez, A. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092309 · Cited by 85 · see citing works
Daly, C. J., & McGrath, J. C. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.02.008 · Cited by 84 · see citing works
Pathogenesis of Abeta Oligomers in Synaptic Failure
Sivanesan, S., Tan, A., & Rajadas, J. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310030011 · Cited by 84 · see citing works
β2-Adrenergic receptor supports prolonged theta tetanus-induced LTP
Qian, H., Matt, L., Zhang, M., Nguyen, M., Patriarchi, T., Koval, O. M., Anderson, M. E., He, K., Lee, H., & Hell, J. W. (2012) · Journal of Neurophysiology · doi:10.1152/jn.00374.2011 · Cited by 82 · see citing works
Wang, D., Yuen, E. Y., Zhou, Y., Yan, Z., & Xiang, Y. K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.244335 · Cited by 80 · see citing works
Shioi, J., Georgakopoulos, A., Mehta, P. D., Kouchi, Z., Litterst, C. M., Baki, L., & Robakis, N. K. R. K. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04391.x · Cited by 78 · see citing works
Synaptic plasticity through activation of GluA3-containing AMPA-receptors
Renner, M. C., Albers, E. H., Gutierrez-Castellanos, N., Reinders, N. R., van Huijstee, A. N., Xiong, H., Lodder, T. R., & Kessels, H. W. (2017) · eLife · doi:10.7554/elife.25462 · Cited by 75 · see citing works
Costantini, C., Rossi, F., Formaggio, E., Bernardoni, R., Cecconi, D., & Bianca, V. D. (2005) · Journal of Molecular Neuroscience · doi:10.1385/jmn:25:2:141 · Cited by 74 · see citing works
NMDA-Receptor Activation but Not Ion Flux Is Required for Amyloid-Beta Induced Synaptic Depression
Tamburri, A., Dudilot, A., Licea, S., Bourgeois, C., & Boehm, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065350 · Cited by 73 · see citing works
Minakami, R., Katsuki, F., Yamamoto, T. S., Nakamura, K. D., & Sugiyama, H. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1349 · Cited by 71 · see citing works
Guntupalli, S., Jang, S. E., Zhu, T., Huganir, R. L., Widagdo, J., & Anggono, V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.774554 · Cited by 70 · see citing works
Vargas, L. M., Cerpa, W. F., Muñoz, F. J., Zanlungo, S., & Alvarez, A. R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.01.023 · Cited by 69 · see citing works
da Silva, G. S. S., Melo, H. M., Lourenco, M. V., Silva, N. M. L. E., de Carvalho, M. B., Alves‐Leon, S. V., de Souza, J. M., Klein, W. L., da‐Silva, W. S., Ferreira, S. T., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.753525 · Cited by 67 · see citing works
Starkey, H. D. V., Kirk, C. A. V., Bixler, G. V., Imperio, C. G., Kale, V. P., Serfass, J. M., Farley, J. A., Han, Y., Warrington, J. P., Han, S. I., et al. (2012) · Journal of Molecular Neuroscience · doi:10.1007/s12031-012-9783-8 · Cited by 66 · see citing works
Beraldo, F. H., Ostapchenko, V. G., Caetano, F. A., Guimarães, A. L. S., Ferretti, G. D. S., Daude, N., Bertram, L. N., Nogueira, K. D. O. P. C., Silva, J. L., Westaway, D. A., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.738286 · Cited by 65 · see citing works
Lue, L.-F., Schmitz, C., & Walker, D. G. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2014.09.050 · Cited by 63 · see citing works
Branca, C., Wisely, E. V., Hartman, L. K., Caccamo, A., & Oddo, S. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.06.011 · Cited by 61 · see citing works
Rui, Y., Gu, J., Yu, K., Hartzell, H. C., & Zheng, J. Q. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-10 · Cited by 61 · see citing works
Genomic Profiling in Nuclear Receptor-Mediated Toxicity
Woods, C. G., Heuvel, J. P. V., & Rusyn, I. (2007) · Toxicologic Pathology · doi:10.1080/01926230701311351 · Cited by 60 · see citing works
Shi, X., Sun, K., Hu, R., Liu, X.-Y., Hu, Q., Sun, X., Yao, B., Sun, N., Hao, J., Wei, P., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1327-16.2016 · Cited by 59 · see citing works
Persistence of Aβ seeds in APP null mouse brain
Ye, L., Fritschi, S. K., Schelle, J., Obermüller, U., Degenhardt, K., Kaeser, S. A., Eisele, Y. S., Walker, L. C., Baumann, F., Staufenbiel, M., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4117 · Cited by 58 · see citing works
p53-Dependent Transcriptional Control of Cellular Prion by Presenilins
Vincent, B., Sunyach, C., Orzechowski, H., George‐Hyslop, P. S., & Checler, F. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0789-09.2009 · Cited by 56 · see citing works
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2 of the 230 references couldn’t be matched to a known paper.
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Chen, X., & Mobley, W. C. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00659 · Cited by 291 · see citing works
Li, S., & Selkoe, D. J. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15007 · Cited by 264 · see citing works
Tolar, M., Hey, J., Power, A., & Abushakra, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126355 · Cited by 246 · see citing works
Buccellato, F. R., D’Anca, M., Fenoglio, C., Scarpini, E., & Galimberti, D. (2021) · Antioxidants · doi:10.3390/antiox10091353 · Cited by 179 · see citing works
The Toxicity and Polymorphism of β-Amyloid Oligomers
Huang, Y., & Liu, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124477 · Cited by 168 · see citing works
Liver Dysfunction as a Novel Player in Alzheimer’s Progression: Looking Outside the Brain
Estrada, L. D., Ahumada, P., Cabrera, D., & Arab, J. P. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00174 · Cited by 144 · see citing works
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
Cano, A., Turowski, P., Ettcheto, M., Duskey, J. T., Tosi, G., Sánchez-López, E., García, M. L., Camins, A., Souto, E. B., Ruiz, A., et al. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-021-00864-x · Cited by 122 · see citing works
Microglial large extracellular vesicles propagate early synaptic dysfunction in Alzheimer’s disease
Gabrielli, M., Prada, I., Joshi, P., Falcicchia, C., D’Arrigo, G., Rutigliano, G., Battocchio, E., Zenatelli, R., Tozzi, F., Radeghieri, A., et al. (2022) · Brain · doi:10.1093/brain/awac083 · Cited by 106 · see citing works
The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer′s Disease (AD)
Mroczko, B., Groblewska, M., & Litman‐Zawadzka, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194661 · Cited by 106 · see citing works
Self-citationGarbuz, D. G., Zatsepina, O. G., & Evgen’ev, M. B. (2021) · Molecular Biology · doi:10.1134/s002689332104004x · Cited by 95 · see citing works
Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies
Buccellato, F. R., D’Anca, M., Tartaglia, G. M., Del Fabbro, M., Scarpini, E., & Galimberti, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813900 · Cited by 94 · see citing works
Cell models for Alzheimer’s and Parkinson’s disease: At the interface of biology and drug discovery
Cetin, S., Knez, D., Gobec, S., Kos, J., & Pišlar, A. H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112924 · Cited by 87 · see citing works
Amyloid-β and Phosphorylated Tau are the Key Biomarkers and Predictors of Alzheimer’s Disease
Pradeepkiran, J. A., Baig, J., Islam, M. A., Kshirsagar, S., & Reddy, P. H. (2024) · Aging and Disease · doi:10.14336/ad.2024.0286 · Cited by 81 · see citing works
Amyloid beta acts synergistically as a pro-inflammatory cytokine
LaRocca, T. J., Cavalier, A. N., Roberts, C. M., Lemieux, M. R., Ramesh, P., Garcia, M. A., & Link, C. D. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105493 · Cited by 76 · see citing works
microRNAs as early biomarkers of Alzheimer’s disease: a synaptic perspective
Siedlecki-Wullich, D., Miñano-Molina, A. J., & Rodríguez-Álvarez, J. (2021) · Cells · doi:10.3390/cells10010113 · Cited by 76 · see citing works
Viles, J. H. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202215785 · Cited by 72 · see citing works
Tubulin tyrosination regulates synaptic function and is disrupted in Alzheimer’s disease
Peris, L., Parato, J., Qu, X., Soleilhac, J.-M., Lanté, F., Kumar, A., Pero, M. E., Hernández, J. M., Corrao, C., Falivelli, G., et al. (2021) · Brain · doi:10.1093/brain/awab436 · Cited by 65 · see citing works
Chen, Y., Wang, S., Ren, J., Zhao, H., Cui, M., Li, N., Li, M. C., & Zhang, C. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c01602 · Cited by 65 · see citing works
Ortiz-Sanz, C., Balantzategi, U., Quintela‐López, T., Ruiz, A., Luchena, C., Zuazo-Ibarra, J., Capetillo‐Zarate, E., Matute, C., Zugaza, J. L., & Alberdi, E. M. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04687-y · Cited by 55 · see citing works
Alzheimer’s disease: a mini-review for the clinician
Madnani, R. S. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1178588 · Cited by 52 · see citing works
β-amyloid and Oxidative Stress: Perspectives in Drug Development
Caruso, G., Spampinato, S. F., Cardaci, V., Caraci, F., Sortino, M. A., & Merlo, S. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666191209115431 · Cited by 45 · see citing works
Rishton, G. M., Look, G. C., Ni, Z., Zhang, J. Y., Wang, Y., Huang, Y., Wu, X., Izzo, N. J., Mozzoni, K., Limegrover, C. S., et al. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.1c00048 · Cited by 45 · see citing works
Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease
Colom‐Cadena, M., Toombs, J., Simzer, E. M., Holt, K., McGeachan, R. I., Tulloch, J., Jackson, R. J., Catterson, J. H., Spires-Jones, M. P., Rose, J. L., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02679-6 · Cited by 41 · see citing works
Platelet-generated amyloid beta peptides in Alzheimer's disease and glaucoma.
Inyushin, M. Y., Zayas‐Santiago, A., Rojas, L. V., Kucheryavykh, Y. V., & Kucheryavykh, L. Y. (2019) · PubMed · doi:10.14670/hh-18-111 · Cited by 40 · see citing works
Signaling via the p75 neurotrophin receptor facilitates amyloid-β-induced dendritic spine pathology
Patnaik, A., Zagrebelsky, M., Korte, M., & Holz, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-70153-4 · Cited by 40 · see citing works
Ailioaie, L. M., Ailioaie, C., & Litscher, G. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030916 · Cited by 37 · see citing works
Prions and Neurodegenerative Diseases: A Focus on Alzheimer’s Disease
Crestini, A., Santilli, F., Martellucci, S., Carbone, E., Sorice, M., Piscopo, P., & Mattei, V. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215171 · Cited by 35 · see citing works
Liu, S., Li, S., Lin, J., Li, J., & Yang, H. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c00287 · Cited by 35 · see citing works
The Role of α-Synuclein in Etiology of Neurodegenerative Diseases
Krawczuk, D., Groblewska, M., Mroczko, J., Winkel, I., & Mroczko, B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179197 · Cited by 33 · see citing works
Self-citationde Rijke, T. J., Doting, M. H. E., van Hemert, S., Deyn, P. P. D., Munster, B. C. V., Harmsen, H. J. M., & Sommer, I. E. (2022) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2022.879491 · Cited by 32 · see citing works
Tobeh, N. S., & Bruce, K. D. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1259012 · Cited by 31 · see citing works
Song, C., Zhang, T., & Zhang, Y. (2022) · Molecules · doi:10.3390/molecules27196751 · Cited by 31 · see citing works
Sultana, O. F., Hia, R. A., & Reddy, P. H. (2024) · Antioxidants · doi:10.3390/antiox13020202 · Cited by 31 · see citing works
Post-Translational Modifications of BACE1 in Alzheimer's Disease
Wen, W., Li, P., Liu, P., Xu, S., Wang, F., & Huang, J. H. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210121163224 · Cited by 30 · see citing works
New Insights into Microglial Mechanisms of Memory Impairment in Alzheimer’s Disease
Li, N., Deng, M., Hu, G., Li, N., Yuan, H., & Zhou, Y. (2022) · Biomolecules · doi:10.3390/biom12111722 · Cited by 30 · see citing works
Manipulated Mesenchymal Stem Cells Applications in Neurodegenerative Diseases
Sadatpoor, S. O., Salehi, Z., Rahban, D., & Salimi, A. (2020) · International Journal of Stem Cells · doi:10.15283/ijsc19031 · Cited by 28 · see citing works
Mini-review: Amyloid degradation toxicity hypothesis of Alzheimer’s disease
Zaretsky, D. V., & Zaretskaia, M. V. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135959 · Cited by 27 · see citing works
Trojan, E., Tylek, K., Schröder, N., Kahl, I., Brandenburg, L.-O., Mastromarino, M., Leopoldo, M., Basta-Kaim, A., & Lacivita, E. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02543-2 · Cited by 26 · see citing works
Ren, Z., Guo, W., Sun, S., Liu, X., Fan, Z., Wang, F., Ibrahim, A. A., Umar, A., Alkhanjaf, A. A. M., & Baskoutas, S. (2023) · Microchimica Acta · doi:10.1007/s00604-023-06014-4 · Cited by 23 · see citing works
Patients with Alzheimer’s disease have an increased removal rate of soluble beta-amyloid-42
Zaretsky, D. V., Zaretskaia, M. V., Molkov, Y. I., & Initiative, A. D. N. (2022) · PLoS ONE · doi:10.1371/journal.pone.0276933 · Cited by 22 · see citing works
O’Day, D. H. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45080393 · Cited by 22 · see citing works
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 21 · see citing works
Switching On/Off Amyloid Plaque Formation in Transgenic Animal Models of Alzheimer’s Disease
Kozin, S. A., Kechko, O. I., Adzhubei, A. A., Makarov, A. А., & Mitkevich, V. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010072 · Cited by 21 · see citing works
O’Day, D. H. (2024) · Biomolecules · doi:10.3390/biom14020173 · Cited by 21 · see citing works
Manna, P. R., Reddy, A. P., Pradeepkiran, J. A., Kshirsagar, S., & Reddy, P. H. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166596 · Cited by 20 · see citing works
The N-formyl peptide receptors: contemporary roles in neuronal function and dysfunction
Cussell, P. J. G., Escalada, M. G., Milton, N. G. N., & Paterson, A. W. J. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.272566 · Cited by 20 · see citing works
Rasool, D., & Jahani‐Asl, A. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03168-4 · Cited by 19 · see citing works
Pramanik, R., Dey, A., Chakrabarty, A. K., Banerjee, D., Narwaria, A., Sharma, S. K., Rai, R. K., Katiyar, C. K., & Dubey, S. K. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118402 · Cited by 18 · see citing works
β-Amyloid activates reactive astrocytes by enhancing glycolysis of astrocytes
Zhang, Y., Yang, X., Zhuang, J., Zhang, H., & Gao, C. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-07319-y · Cited by 18 · see citing works
Mukem, S., Thongbuakaew, T., & Khornchatri, K. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e07310 · Cited by 17 · see citing works
Loss of slc39a14 causes simultaneous manganese hypersensitivity and deficiency in zebrafish
Tuschl, K., White, R. J., Trivedi, C. A., Valdivia, L. E., Niklaus, S., Bianco, I. H., Dadswell, C., González‐Méndez, R., Sealy, I. M., Neuhauss, S. C. F., et al. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.044594 · Cited by 17 · see citing works
O’Day, D. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021393 · Cited by 17 · see citing works
Durell, S. R., Kayed, R., & Guy, H. R. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26301 · Cited by 16 · see citing works
Zhang, X., Huai, Y., Cai, J., Song, C., & Zhang, Y. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.12.014 · Cited by 16 · see citing works
Ho, A., Ngala, B., Yamada, C., Garcia, C., Duarte, C. L., Akkaoui, J., Ciolac, D., Nusbaum, A., Kochen, W. R., Efremova, D., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115435 · Cited by 15 · see citing works
Jafni, S., Sathya, S., Arunkumar, M., Kiruthiga, C., Jeyakumar, M., Murugesh, E., & Devi, K. P. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117536 · Cited by 14 · see citing works
Natarajan, B., Zhou, Q., Maduraiveeran, G., & Kannan, P. (2026) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2026.217682 · Cited by 12 · see citing works
Zhang, T., Song, C., Zheng, C., Chen, X., & Zhang, Y. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01219-2 · Cited by 12 · see citing works
Demuth, H., Hosseini, S., Düsedau, H. P., Dunay, I. R., Körte, M., & Zagrebelsky, M. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1163087 · Cited by 11 · see citing works
Carbone, M. G., Pagni, G., Tagliarini, C., Marazziti, D., & Pomara, N. (2021) · Life · doi:10.3390/life11080750 · Cited by 11 · see citing works
Varshavskaya, K. B., Petrushanko, I. Y., Mitkevich, V. A., Barykin, E. P., & Makarov, A. А. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1362581 · Cited by 10 · see citing works
Preparation and Characterization of Zn(II)-Stabilized Aβ42 Oligomers
Díaz, A. G., Cataldi, R., Mannini, B., & Vendruscolo, M. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00084 · Cited by 10 · see citing works
β-Amyloids and Immune Responses Associated with Alzheimer’s Disease
Kolobova, E. A., Petrushanko, I. Y., Mitkevich, V. A., Makarov, A. А., & Grigorova, I. (2024) · Cells · doi:10.3390/cells13191624 · Cited by 10 · see citing works
Natarajan, C., Cook, C., Ramaswamy, K., & Krishnan, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043372 · Cited by 10 · see citing works
A New Insight on Feasibility of Pre-, Pro-, and Synbiotics-based Therapies in Alzheimer’s Disease
Talebi, M., Ebrahimi, V., Rasouli, A., Farjami, A., Soofiyani, S. R., Soleimanian, A., Forouhandeh, H., & Tarhriz, V. (2022) · Journal of Reports in Pharmaceutical Sciences · doi:10.4103/jrptps.jrptps_170_21 · Cited by 8 · see citing works
Recombinant Integrin β1 Signal Peptide Blocks Gliosis Induced by Aβ Oligomers
Ortiz-Sanz, C., Llavero, F., Zuazo-Ibarra, J., Balantzategi, U., Quintela‐López, T., Wyssenbach, A., Capetillo‐Zarate, E., Matute, C., Alberdi, E. M., & Zugaza, J. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105747 · Cited by 7 · see citing works
Viles, J. H. (2023) · Angewandte Chemie · doi:10.1002/ange.202215785 · Cited by 7 · see citing works
Schreiner, T. G., Ciobanu, R. C., & Schreiner, O. D. (2026) · Biomedicines · doi:10.3390/biomedicines14030522 · Cited by 6 · see citing works
Eyvani, K., Letafatkar, N., & Babaei, P. (2024) · Experimental Aging Research · doi:10.1080/0361073x.2024.2377440 · Cited by 5 · see citing works
A New Bistable Switch Model of Alzheimer’s Disease Pathogenesis
Burlando, B., Losacco, S., Villa, V., Fedele, E., & Ricciarelli, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137061 · Cited by 4 · see citing works
Jia, T., Wang, H., Chi, W., Zhou, W., Guo, L., Dai, Y., Bian, K., Sun, Z., Ding, X., & Yu, Y. (2023) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2023.123727 · Cited by 4 · see citing works
Gopalakrishna, R., Lin, C. Y. H., Oh, A., Le, C., Yang, S., Hicks, A., Kindy, M. S., Mack, W. J., & Bhat, N. R. (2022) · FEBS Letters · doi:10.1002/1873-3468.14467 · Cited by 4 · see citing works
Jia, M., Wang, C., Mei, J., Ahmad, S., Nouman, M. F., & Ai, H. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00862 · Cited by 3 · see citing works
Li, H., Zheng, C., Zheng, Y., Wen, K., & Zhang, Y. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2024.110141 · Cited by 3 · see citing works
Amyloid beta binding partners in the brain tissue of older adults
Oveisgharan, S., Yu, L., Wang, Y., Yang, J., Vialle, R. A., Lopes, K. D. P., Tasaki, S., Young‐Pearse, T. L., Jager, P. L. D., Petyuk, V., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70882 · Cited by 2 · see citing works
Aβ40 Fibril Assembly on Human Cerebral Smooth Muscle Cells Impairs Cell Viability
Irizarry, B. A., Davis, J., Rajpoot, J., Zhu, X. A., Xu, F., Smith, S. O., & Nostrand, W. E. V. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00478 · Cited by 2 · see citing works
All-trans retinoic acid in Alzheimer's disease
Beheshti, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815854-8.00035-5 · Cited by 2 · see citing works
Pu, Z., Luo, D., Shuai, B., Xu, Y., Liu, M., & Zhao, J. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04347-5 · Cited by 2 · see citing works
Li, H., Zheng, C., Wen, K., Zhang, T., & Zhang, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104501 · Cited by 1 · see citing works
Treatment options for Alzheimer’s Disease: An overview of the amyloid, tau, and alternate hypotheses
Eroltu, K. (2023) · Journal of High School Science · doi:10.64336/001c.89250 · Cited by 1 · see citing works
Sharma, R., Shkirkova, K., Mack, W. J., & Gopalakrishna, R. (2026) · Journal of dementia and Alzheimer's disease · doi:10.3390/jdad3020027 · Cited by 1 · see citing works
Patients with Alzheimer’s disease have increased cellular amyloid uptakePreprint
Zaretsky, D. V., Zaretskaia, M. V., Molkov, Y. I., & Initiative, A. D. N. (2022) · medRxiv · doi:10.1101/2022.01.12.22269196 · Cited by 1 · see citing works
Endocytosis in β-amyloid biology and Alzheimer’s disease
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Santos, D. G. (2024) · theses.fr (ABES) · doi:10.70675/b3ed4de5zcd9ez4421za129z0a05130d86b9
Deng, L., Li, H., Yang, S., Chen, F., Qiao, J., 包慧中, Wang, X., Fang, S., Xu, B., & Tang, Z. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04654-1
Fagla, B. M., Zhao, G., Valencia‐Olvera, A. C., Weng, J. M., Rosa, C. D., Ticiani, E., Tai, L. M., Veiga-Lopez, A., & Buhimschi, I. A. (2026) · Placenta · doi:10.1016/j.placenta.2026.06.015
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Khursheed, A., Shang, Q., Zhang, H., Tian, Y., Szwedziak, P., Volkov, V. A., & Viles, J. H. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2610068123
Jia, M., Mei, J., Guan, Y., Wang, Z., & Ai, H. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6c00207
Zheng, C., Wen, K., Li, H., Zhang, T., & Zhang, Y. (2026) · Cells · doi:10.3390/cells15151379
- Authors
- Mroczko, B., Groblewska, M., Litman-Zawadzka, A., Kornhuber, J., & Lewczuk, P.
- Affiliations
- Medical University of Białystok (PL)
- University Clinical Hospital In Bialystok (PL)
- Department of Neurodegeneration Diagnostics, Medical University of Białystok, 15-089 Białystok, Poland
- Friedrich-Alexander-Universität Erlangen-Nürnberg (DE)
- Corresponding author
- Mroczko, Barbara
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2018-06-27
- Volume
- 19
- Issue
- 7
- Pages
- 1884
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6073792
- OpenAlex
- W2810634108
- Cited by
- 97
- References
- 230
- Citations by year
- 2026: 9 · 2025: 6 · 2024: 15 · 2023: 16 · 2022: 22 · 2021: 15 · 2020: 8 · 2019: 5 · 2018: 1
- FWCI
- 0.95
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- OPUS Repository (Kooperativer Bibliotheksverbund Berlin-Brandenburg) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Uniwersytet Medyczny w Bialymstoku (N/ST/ZB/18/002/1198)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta oligomers, amyloid-beta aggregation, neurofibrillary tangles, tau protein, amyloid plaques, misfolded proteins, protein misfolding, genetic alterations
- MeSH terms
- Alzheimer Disease, Animals, Humans, Amyloid beta-Peptides, Neurofibrillary Tangles, Protein Aggregation, Pathological
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