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Neuropathological Alterations in Alzheimer Disease
Open accessAbstract
The neuropathological hallmarks of Alzheimer disease (AD) include "positive" lesions such as amyloid plaques and cerebral amyloid angiopathy, neurofibrillary tangles, and glial responses, and "negative" lesions such as neuronal and synaptic loss. Despite their inherently cross-sectional nature, postmortem studies have enabled the staging of the progression of both amyloid and tangle pathologies, and, consequently, the development of diagnostic criteria that are now used worldwide. In addition, clinicopathological correlation studies have been crucial to generate hypotheses about the pathophysiology of the disease, by establishing that there is a continuum between "normal" aging and AD dementia, and that the amyloid plaque build-up occurs primarily before the onset of cognitive deficits, while neurofibrillary tangles, neuron loss, and particularly synaptic loss, parallel the progression of cognitive decline. Importantly, these cross-sectional neuropathological data have been largely validated by longitudinal in vivo studies using modern imaging biomarkers such as amyloid PET and volumetric MRI.
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“In particular, Lewy pathology in AD is most frequent in olfactory bulb and the amygdala [23, 123].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [23]
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“The direct connection between Aβ and MAPT pathology is poorly understood, as shown by the weak correlation between the distribution of Aβ pathology and the distribution of MAPT pathology in humans (Serrano-Pozo et al., 2011; Perez-Nievas et al., 2013; Scheltens et al., 2021).”
From β-amyloid accumulation enhances microtubule associated protein tau pathology in an APPNL-G-F/MAPTP301S mouse model of Alzheimer’s disease (2024) · cites this paper as Serrano-Pozo et al., 2011
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“Some of the dystrophic neurites associated with neuritic plaques contain tau filaments, which can have a paired helical filament morphology with electron microscopy [23].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [23]
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“Additionally eosinophilic Hirano bodies, granulovacuolar degeneration (GVD) and cerebral amyloid angiopathy (CAA) are also common [18, 23].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [23]
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“Dense cored NPs are also accompanied by synaptic loss, activated microglia and reactive astrocytes [23, 29, 36].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [23]
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“Amyloid deposits in CAA are enriched in Aβ40 (while parenchymal deposits are enriched in Aβ42 species) and can affect small arteries, arterioles and even capillaries of the gray matter of the cerebral cortices and in leptomeningeal vessels [18, 23].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [23]
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“Interestingly the parietal and occipital cortices are more vulnerable than the frontal and temporal lobes, and leptomeningeal arteries are more vulnerable than parenchymal vessels [23].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [23]
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“Alzheimer’s pathology can be found in cognitively normal patients at the time of autopsy, and this preclinical phase can also be observed in patients with mild cognitive impairment that do not meet the criteria for clinical AD [4, 23].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [23]
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“Accumulation of amyloid-beta (Αβ) is a histological hallmark of the AD brain1.”
From Amyloid-β induces lipid droplet-mediated microglial dysfunction via the enzyme DGAT2 in Alzheimer’s disease (2025) · cites this paper as [1]
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“AD is the leading cause of dementia characterized by key neuronal hallmarks: extracellular deposition of Aβ plaques, formation of intracellular neurofibrillary tangles, and neuronal loss (1, 2).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [1]
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“Neurodegeneration is a pathological hallmark of AD 20 , which is exacerbated in a mouse model of tauopathy expressing APOE4 (refs. 12,21).”
From APOE4 impairs the microglial response in Alzheimer’s disease by inducing TGFβ-mediated checkpoints (2023) · cites this paper as [20]
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“The amyloid hypothesis of AD posits that excessive accumulation of amyloid-β peptide leads to neurofibrillary tangles composed of aggregated hyperphosphorylated tau84.”
From The use of brain organoids to investigate neural development and disease (2017) · cites this paper as [84]
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2 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedTsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003135 · Cited by 281
Self-citationRetractedNeuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 9×
“The NFTs are argyrophilic and can be shown by silver impregnation methods such as the Gallyas technique (Braak and Braak 1991).”
BackgroundMethodInfluentialMild Cognitive Impairment: Clinical Characterization and Outcome
Petersen, R. C., Smith, G. E., Waring, S. C., Ivnik, R. J., Tangalos, E. G., & Kokmen, E. (1999) · Archives of Neurology · doi:10.1001/archneur.56.3.303 · Cited by 8,980
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mild cognitive impairment as a diagnostic entity
Petersen, R. C. (2004) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2004.01388.x · Cited by 7,864
Diagnosis and management of dementia with Lewy bodies: Third report of the DLB consortium
McKeith, I. G., Dickson, D. W., Lowe, J., Emre, M., O'Brien, J. T., Feldman, H., Cummings, J., Duda, J. E., Lippa, C., Perry, E. K., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000187889.17253.b1 · Cited by 5,069
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Current concepts in mild cognitive impairment
Petersen, R. C., Doody, R., Kurz, A., Mohs, R. C., Morris, J. C., Rabins, P. V., Ritchie, K., Rossor, M., Thal, L., & Winblad, B. (2001) · Archives of Neurology · doi:10.1001/archneur.58.12.1985 · Cited by 4,781
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
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- [200]200. Terry R, Hansen L, Masliah E. 1994. Structural basis of the cognitive alterations in Alzheimer disease. In Alzheimer disease (ed. R. Terry, R. Katzman), pp. 179 -196.
Cited by
Sorted by citations
The neuropathological diagnosis of Alzheimer's disease
DeTure, M. A., & Dickson, D. W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0333-5 · Cited by 3,329
“Still neurons with tangles can be long lasting, perhaps persisting as ghost tangles for decades [23].”
BackgroundInfluentialComprehensive Review on Alzheimer’s Disease: Causes and Treatment
Breijyeh, Z., & Karaman, R. (2020) · Molecules · doi:10.3390/molecules25245789 · Cited by 2,789
Lane, C. A., Hardy, J., & Schott, J. M. (2018) · European Journal of Neurology · doi:10.1111/ene.13439 · Cited by 2,616
Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750
Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies
Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425
PET Imaging of Tau Deposition in the Aging Human Brain
Schöll, M., Lockhart, S. N., Schonhaut, D. R., O’Neil, J. P., Janabi, M., Ossenkoppele, R., Baker, S. L., Vogel, J. W., Faria, J., Schwimmer, H. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.028 · Cited by 1,214
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
Self-citationEpidemiology of Alzheimer DiseasePreprint
Mayeux, R. P., & Stern, Y. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006239 · Cited by 1,127
Sala Frigerio, C., Wolfs, L., Fattorelli, N., Thrupp, N., Voytyuk, I., Schmidt, I., Mancuso, R., Chen, W.-T., Woodbury, M. E., Srivastava, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.099 · Cited by 926
Self-citationNeurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000
Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future
Zhang, Y., Chen, H., Li, R., Sterling, K., & Song, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01484-7 · Cited by 988
Maternal immune activation and abnormal brain development across CNS disorders
Knuesel, I., Chicha, L., Britschgi, M., Schobel, S. A., Bodmer, M., Hellings, J. A., Toovey, S., & Prinssen, E. P. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.187 · Cited by 880
Role of Phenolic Compounds in Human Disease: Current Knowledge and Future Prospects
Rahman, M. M., Rahaman, M. S., Islam, M. R., Rahman, F., Mithi, F. M., Alqahtani, T., Almikhlafi, M. A., Alghamdi, S. Q., Alruwaili, A. S., Hossain, M. S., et al. (2021) · Molecules · doi:10.3390/molecules27010233 · Cited by 945
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Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836
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Raulin, A.-C., Doss, S. V., Trottier, Z. A., Ikezu, T. C., Bu, G., & Liu, C.-C. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00574-4 · Cited by 756
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Porsteinsson, A. P., Isaacson, R. S., Knox, S., Sabbagh, M. N., & Rubino, I. (2021) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2021.23 · Cited by 744
Machine learning framework for early MRI-based Alzheimer's conversion prediction in MCI subjects
Moradi, E., Pepe, A., Gaser, C., Huttunen, H. J., & Tohka, J. (2014) · NeuroImage · doi:10.1016/j.neuroimage.2014.10.002 · Cited by 740
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Moujalled, D., Strasser, A., & Liddell, J. R. (2021) · Cell Death & Differentiation · doi:10.1038/s41418-021-00814-y · Cited by 749
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Musiek, E. S., & Holtzman, D. M. (2015) · Nature Neuroscience · doi:10.1038/nn.4018 · Cited by 662
Lee, J.-H., Yang, D.-S., Goulbourne, C. N., Im, E., Stavrides, P., Pensalfini, A., Chan, H., Bouchet-Marquis, C., Bleiwas, C., Berg, M. J., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01084-8 · Cited by 638
Rathore, S., Habes, M., Iftikhar, M. A., Shacklett, A., & Davatzikos, C. (2017) · NeuroImage · doi:10.1016/j.neuroimage.2017.03.057 · Cited by 622
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Abbott, N. J., Pizzo, M. E., Preston, J. E., Janigro, D., & Thorne, R. G. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1812-4 · Cited by 593
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van der Kant, R., Goldstein, L. S. B., & Ossenkoppele, R. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-019-0240-3 · Cited by 580
Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548
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Roy, E. R., Wang, B., Wan, Y.-W., Chiu, G., Cole, A., Yin, Z., Propson, N. E., Xu, Y., Jankowsky, J. L., Liu, Z., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133737 · Cited by 563
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Wiseman, F. K., Al-Janabi, T., Hardy, J., Karmiloff-Smith, A., Nizetic, D., Tybulewicz, V. L. J., Fisher, E. M. C., & Strydom, A. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3983 · Cited by 562
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Kamat, P. K., Kalani, A., Rai, S., Swarnkar, S., Tota, S., Nath, C., & Tyagi, N. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-9053-6 · Cited by 511
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Villemagne, V. L., Fodero-Tavoletti, M. T., Masters, C. L., & Rowe, C. C. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70252-2 · Cited by 501
Mathys, H., Peng, Z., Boix, C. A., Victor, M. B., Leary, N., Babu, S., Abdelhady, G., Jiang, X., Ng, A. P., Ghafari, K., et al. (2023) · Cell · doi:10.1016/j.cell.2023.08.039 · Cited by 495
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Gratuze, M., Leyns, C. E. G., & Holtzman, D. M. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0298-9 · Cited by 489
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Raz, L., Knoefel, J. E., & Bhaskar, K. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.164 · Cited by 512
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Yeh, F. L., Hansen, D. V., & Sheng, M. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.008 · Cited by 440
Stancu, I.-C., Cremers, N., Vanrusselt, H., Couturier, J., Vanoosthuyse, A., Kessels, S., Lodder, C., Brône, B., Huaux, F., Octave, J.-N., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-01957-y · Cited by 447
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Caccamo, A., Branca, C., Piras, I. S., Ferreira, E., Huentelman, M. J., Liang, W. S., Readhead, B., Dudley, J. T., Spangenberg, E. E., Green, K. N., et al. (2017) · Nature Neuroscience · doi:10.1038/nn.4608 · Cited by 482
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Krstic, D., & Knuesel, I. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.236 · Cited by 457
Tai, H.-C., Serrano-Pozo, A., Hashimoto, T., Frosch, M. P., Spires-Jones, T. L., & Hyman, B. T. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 443
Self-citationTherapeutic strategies for Alzheimer's disease in clinical trials
Godyń, J., Jończyk, J., Panek, D., & Malawska, B. (2015) · Pharmacological Reports · doi:10.1016/j.pharep.2015.07.006 · Cited by 462
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Yamazaki, Y., & Kanekiyo, T. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091965 · Cited by 451
Gowrishankar, S., Yuan, P., Wu, Y., Schrag, M., Paradise, S., Grutzendler, J., De Camilli, P., & Ferguson, S. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510329112 · Cited by 406
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Zheng, Q., & Wang, X. (2024) · Protein & Cell · doi:10.1093/procel/pwae026 · Cited by 483
Spasov, S., Passamonti, L., Duggento, A., Lió, P., & Toschi, N. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.01.031 · Cited by 445
Power, M. C., Adar, S. D., Yanosky, J. D., & Weuve, J. (2016) · NeuroToxicology · doi:10.1016/j.neuro.2016.06.004 · Cited by 422
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Ng, T. K. S., Ho, C. S. H., Tam, W., Kua, E. H., & Ho, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020257 · Cited by 432
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Chi, H., Chang, H.-Y., & Sang, T.-K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103082 · Cited by 412
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Götz, J., Bodea, L., & Goedert, M. (2018) · Nature reviews. Neuroscience · doi:10.1038/s41583-018-0054-8 · Cited by 422
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Lackie, R. E., Maciejewski, A., Ostapchenko, V. G., Marques-Lopes, J., Choy, W., Duennwald, M. L., Prado, V. F., & Prado, M. A. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00254 · Cited by 390
Zhong, L., Xu, Y., Zhuo, R., Wang, T., Wang, K., Huang, R., Wang, D., Gao, Y., Zhu, Y., Sheng, X., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09118-9 · Cited by 371
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the Synaptic Health Endpoints Working Group, Colom-Cadena, M., Spires-Jones, T., Zetterberg, H., Blennow, K., Caggiano, A., DeKosky, S. T., Fillit, H., Harrison, J. E., Schneider, L. S., et al. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00588-4 · Cited by 328
Bisht, K., Sharma, K. P., & Tremblay, M. (2018) · Neurobiology of Stress · doi:10.1016/j.ynstr.2018.05.003 · Cited by 366
Iannotti, F. A., Marzo, V. D., & Petrosino, S. (2016) · Progress in Lipid Research · doi:10.1016/j.plipres.2016.02.002 · Cited by 373
Numakawa, T., Odaka, H., & Adachi, N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113650 · Cited by 367
Bordi, M., Berg, M. J., Mohan, P. S., Peterhoff, C. M., Alldred, M. J., Che, S., Ginsberg, S. D., & Nixon, R. A. (2016) · Autophagy · doi:10.1080/15548627.2016.1239003 · Cited by 353
Beyond the neuron–cellular interactions early in Alzheimer disease pathogenesis
Henstridge, C. M., Hyman, B. T., & Spires-Jones, T. L. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0113-1 · Cited by 348
Self-citationMonoamine oxidase B inhibitor, selegiline, reduces 18F-THK5351 uptake in the human brain
Ng, K. P., Pascoal, T. A., Mathotaarachchi, S. S., Therriault, J., Kang, M. S., Shin, M., Guiot, M.-C., Guo, Q., Harada, R., Comley, R. A., et al. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0253-y · Cited by 351
Liss, J. L., Seleri Assunção, S., Cummings, J., Atri, A., Geldmacher, D. S., Candela, S. F., Devanand, D. P., Fillit, H. M., Susman, J., Mintzer, J., et al. (2021) · Journal of Internal Medicine · doi:10.1111/joim.13244 · Cited by 312
de la Monte, S. M. (2017) · Drugs · doi:10.1007/s40265-016-0674-0 · Cited by 331
de Wolf, F., Ghanbari, M., Licher, S., McRae‐McKee, K., Gras, L. A., Weverling, G. J., Wermeling, P. R., Sedaghat, S., Ikram, M. K., Waziry, R., et al. (2020) · Brain · doi:10.1093/brain/awaa054 · Cited by 325
Kim, D.-G., Krenz, A., Toussaint, L. E., Maurer, K. J., Robinson, S.-A., Yan, A., Torres, L., & Bynoe, M. S. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0467-5 · Cited by 330
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Rao, V. K., Carlson, E. A., & Yan, S. S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.003 · Cited by 330
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Inestrosa, N. C., & Varela-Nallar, L. (2014) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt051 · Cited by 324
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Rusek, M., Pluta, R., Ułamek-Kozioł, M., & Czuczwar, S. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20163892 · Cited by 319
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Ferrari, C., & Sorbi, S. (2021) · Physiological Reviews · doi:10.1152/physrev.00015.2020 · Cited by 343
Hendrickx, D. A. E., van Eden, C. G., Schuurman, K. G., Hamann, J., & Huitinga, I. (2017) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2017.04.007 · Cited by 313
Pleiotropic Effects of GLP-1 and Analogs on Cell Signaling, Metabolism, and Function
Rowlands, J., Heng, J., Newsholme, P., & Carlessi, R. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00672 · Cited by 302
Dendritic Tau in Alzheimer’s Disease
Ittner, A., & Ittner, L. M. (2018) · Neuron · doi:10.1016/j.neuron.2018.06.003 · Cited by 278
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Stanciu, G. D., Luca, A., Rusu, R.-N., Bild, V., Chiriac, S. I. B., Solcan, C., Bild, W., & Ababei, D. C. (2019) · Biomolecules · doi:10.3390/biom10010040 · Cited by 307
Xu, M., Zhang, D., Luo, R., Wu, Y., Zhou, H., Kong, L., Bi, R., & Yao, Y. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.08.012 · Cited by 296
Emerging roles of innate and adaptive immunity in Alzheimer’s disease
Chen, X., & Holtzman, D. M. (2022) · Immunity · doi:10.1016/j.immuni.2022.10.016 · Cited by 297
Μιλτιάδους, Α., Tzimourta, K. D., Afrantou, T., Ioannidis, P., Grigoriadis, N., Tsalikakis, D., Angelidis, P. A., Tsipouras, M. G., Glavas, E., Γιαννακέας, Ν., et al. (2023) · Data · doi:10.3390/data8060095 · Cited by 293
Chen, X., & Mobley, W. C. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00659 · Cited by 302
Restoring Wnt/β-catenin signaling is a promising therapeutic strategy for Alzheimer’s disease
Jia, L., Piña-Crespo, J., & Li, Y. (2019) · Molecular Brain · doi:10.1186/s13041-019-0525-5 · Cited by 288
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Bader, J. M., Geyer, P. E., Müller, J. B., Strauss, M. T., Koch, M., Leypoldt, F., Koertvelyessy, P., Bittner, D., Schipke, C. G., Incesoy, E. I., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20199356 · Cited by 286
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Perez-Nievas, B. G., & Serrano-Pozo, A. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00114 · Cited by 282
Self-citationHippocampal neurogenesis: Learning to remember
Lazarov, O., & Hollands, C. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.006 · Cited by 297
Balez, R., Steiner, N., Engel, M., Muñoz, S. S., Lum, J. S., Wu, Y., Wang, D., Vallotton, P., Sachdev, P. S., O’Connor, M. D., et al. (2016) · Scientific Reports · doi:10.1038/srep31450 · Cited by 280
Shi, M., Chu, F., Zhu, F., & Zhu, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.870517 · Cited by 275
Park, H., Oh, J., Shim, G., Cho, B., Chang, Y., Kim, S., Baek, S., Kim, H., Shin, J., Choi, H. G., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0352-0 · Cited by 277
Lost after translation: missorting of Tau protein and consequences for Alzheimer disease
Zempel, H., & Mandelkow�, E. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.08.004 · Cited by 284
WNT signaling in neuronal maturation and synaptogenesis
Rosso, S. B., & Inestrosa, N. C. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00103 · Cited by 272
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Busche, M. A., & Konnerth, A. (2015) · BioEssays · doi:10.1002/bies.201500004 · Cited by 266
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Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270
Microglial activation correlates in vivo with both tau and amyloid in Alzheimer’s disease
Dani, M., Wood, M., Mizoguchi, R., Fan, Z., Walker, Z., Morgan, R., Hinz, R., Biju, M., Kuruvilla, T., Brooks, D. J., et al. (2018) · Brain · doi:10.1093/brain/awy188 · Cited by 270
The biological pathways of Alzheimer disease: a review
Calabrò, M., Rinaldi, C., Santoro, G., & Crisafulli, C. (2020) · AIMS neuroscience · doi:10.3934/neuroscience.2021005 · Cited by 287
Shaw, L. M., Arias, J., Blennow, K., Galasko, D., Molinuevo, J. L., Salloway, S., Schindler, S., Carrillo, M. C., Hendrix, J. A., Ross, A., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.07.220 · Cited by 266
Unger, M. S., Li, E., Scharnagl, L., Poupardin, R., Altendorfer, B., Mrowetz, H., Hutter-Paier, B., Weiger, T. M., Heneka, M. T., Attems, J., et al. (2020) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.05.070 · Cited by 248
Molecular signatures underlying neurofibrillary tangle susceptibility in Alzheimer’s disease
Otero-Garcia, M., Mahajani, S. U., Wakhloo, D., Tang, W., Xue, Y.-Q., Morabito, S., Pan, J., Oberhauser, J., Madira, A. E., Shakouri, T., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.06.021 · Cited by 262
Kandimalla, R. J. L., Mańczak, M., Yin, X., Wang, R., & Reddy, P. H. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx381 · Cited by 256
RetractedSynaptic Contacts Enhance Cell-to-Cell Tau Pathology Propagation
Calafate, S., Buist, A., Miśkiewicz, K., Vijayan, V. A., Daneels, G., Strooper, B. D., de Wit, J., Verstreken, P., & Moechars, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.043 · Cited by 277
Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256
Metadata
- Authors
- Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T.
- Affiliations
- Harvard University (US)
- University of California San Diego (US)
- Venue
- Cold Spring Harbor Perspectives in Medicine
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-09-01
- Volume
- 1
- Issue
- 1
- Pages
- a006189-a006189
- ISSN
- 2157-1422 (ISSN-L)
- PMC
- PMC3234452
- OpenAlex
- W2096963202
- Semantic Scholar
- 875ea5aa27548adac085b276cf2ba404af4ae139
- Cited by
- 3,345
- References
- 247
- Citations by year
- 2026: 150 · 2025: 269 · 2024: 316 · 2023: 343 · 2022: 348 · 2021: 379 · 2020: 318 · 2019: 261 · 2018: 263 · 2017: 214 · 2016: 168 · 2015: 137 · 2014: 101 · 2013: 44 · 2012: 26
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (AG5131, AG08487, NS057096, AG10435, AG18840)
- National Institute on Aging (AG18840, AG-08487, P01AG010435, R37AG018440, P50AG005131, AG-5131, R01AG008487, P50 AG05134, P01AG022074, AG22074, P50AG005134, U19AG010483, AG10435)
- National Institute of Neurological Disorders and Stroke (P30NS057096, NS057096)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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, neuropathology, amyloid plaques, cerebral amyloid angiopathy, neurofibrillary tangles, glial response, synaptic loss, neuronal loss, clinicopathological correlation, normal aging, cognitive decline, amyloid PET, volumetric MRI, imaging biomarkers
- MeSH terms
- Aging, Alzheimer Disease, Humans, Magnetic Resonance Imaging, Cerebral Amyloid Angiopathy, Neurofibrillary Tangles, Lewy Body Disease, Positron-Emission Tomography, Plaque, Amyloid, Cognitive Dysfunction
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