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Alzheimer’s Disease: The Challenge of the Second Century
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In the first of our State of the Art Review series, David M. Holtzman, John C. Morris, and Alison M. Goate explore the rapid pace of Alzheimer’s disease research and the challenges to translating research breakthroughs into clinical treatments.
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“Growing evidence suggests that AD pathology, such as cerebral Aβ accumulation, probably begins one to two decades before onset of clinical symptoms (Holtzman et al. 2011, Perrin et al. 2009).”
From miR‐186 is decreased in aged brain and suppresses BACE 1 expression (2016) · cites this paper as Holtzman et al. 2011
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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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
RetractedRETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009) · Nature · doi:10.1038/nature07767 · Cited by 992
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
A default mode of brain function
Raichle, M. E., MacLeod, A. M., Snyder, A. Z., Powers, W. J., Gusnard, D. A., & Shulman, G. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.676 · Cited by 12,190
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
The Clinical Dementia Rating (CDR): Current version and scoring rules
Morris, J. C. (1993) · Neurology · doi:10.1212/wnl.43.11.2412-a · Cited by 9,882
Self-citationCorder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
Finding the missing heritability of complex diseases
Manolio, T. A., Collins, F. S., Cox, N. J., Goldstein, D. B., Hindorff, L. A., Hunter, D. J., McCarthy, M. I., Ramos, E. M., Cardon, L. R., Chakravarti, A., et al. (2009) · Nature · doi:10.1038/nature08494 · Cited by 8,336
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade
Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70299-6 · Cited by 4,806
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Keren-Shaul, H., Spinrad, A., Weiner, A., Matcovitch-Natan, O., Dvir-Szternfeld, R., Ulland, T. K., David, E., Baruch, K., Lara-Astaiso, D., Toth, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.018 · Cited by 5,493
Knopman, D. S., Amieva, H., Petersen, R. C., Chételat, G., Holtzman, D. M., Hyman, B. T., Nixon, R. A., & Jones, D. T. (2021) · Nature Reviews Disease Primers · doi:10.1038/s41572-021-00269-y · Cited by 2,606
Self-citationSingle-cell transcriptomic analysis of Alzheimer’s disease
Mathys, H., Davila-Velderrain, J., Peng, Z., Gao, F., Mohammadi, S., Young, J. Z., Menon, M., He, L., Abdurrob, F., Jiang, X., et al. (2019) · Nature · doi:10.1038/s41586-019-1195-2 · Cited by 2,568
Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188
Oxidative stress and the amyloid beta peptide in Alzheimer’s disease
Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185
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
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis
Karch, C. M., & Goate, A. M. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.05.006 · Cited by 1,357
Self-citationTREM2 Maintains Microglial Metabolic Fitness in Alzheimer’s Disease
Ulland, T. K., Song, W. M., Huang, S. C.-C., Ulrich, J. D., Sergushichev, A., Beatty, W. L., Loboda, A. A., Zhou, Y., Cairns, N. J., Kambal, A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.023 · Cited by 1,263
Self-citationBiomarker Modeling of Alzheimer’s Disease
Jack, C. R., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.12.003 · Cited by 1,002
Self-citationDistinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986
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
Dementia in China: epidemiology, clinical management, and research advances
Jia, L., Quan, M., Fu, Y., Zhao, T., Li, Y., Wei, C., Tang, Y., Qin, Q., Wang, F., Qiao, Y., et al. (2020) · The Lancet Neurology · doi:10.1016/s1474-4422(19)30290-x · Cited by 875
An epigenetic blockade of cognitive functions in the neurodegenerating brain
Gräff, J., Rei, D., Guan, J.-S., Wang, W.-Y., Seo, J., Hennig, K. M., Nieland, T. J. F., Fass, D. M., Kao, P. F., Kahn, M., et al. (2012) · Nature · doi:10.1038/nature10849 · Cited by 853
TREM2-mediated early microglial response limits diffusion and toxicity of amyloid plaques
Wang, Y., Ulland, T. K., Ulrich, J. D., Song, W., Tzaferis, J. A., Hole, J. T., Yuan, P., Mahan, T. E., Shi, Y., Gilfillan, S., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151948 · Cited by 840
Self-citationREST and stress resistance in ageing and Alzheimer’s disease
Lu, T., Aron, L., Zullo, J., Pan, Y., Kim, H., Chen, Y., Yang, T.-H., Kim, H., Drake, D., Liu, X., et al. (2014) · Nature · doi:10.1038/nature13163 · Cited by 784
TREM2 — a key player in microglial biology and Alzheimer disease
Ulland, T. K., & Colonna, M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0072-1 · Cited by 735
Overcoming the Blood–Brain Barrier: The Role of Nanomaterials in Treating Neurological Diseases
Furtado, D., Björnmalm, M., Ayton, S., Bush, A. I., Kempe, K., & Caruso, F. (2018) · Advanced Materials · doi:10.1002/adma.201801362 · Cited by 708
Histone acetylation: molecular mnemonics on the chromatin
Gräff, J., & Tsai, L.-H. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3427 · Cited by 680
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Lee, E. B., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3121 · Cited by 659
Memory loss in Alzheimer's disease
Jahn, H. (2013) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2013.15.4/hjahn · Cited by 653
Targeting the β secretase BACE1 for Alzheimer's disease therapy
Yan, R., & Vassar, R. J. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70276-x · Cited by 645
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622
“Early intervention will require an early and informative biomarker.(4,95) In vitro, the formation of corruptive seeds is a relatively slow, stochastic process,(96) although once a seed is present, aggregation proceeds quite rapidly.”
BackgroundWang, C., & Holtzman, D. M. (2020) · Neuropsychopharmacology · doi:10.1038/s41386-019-0478-5 · Cited by 615
Self-citationInterplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight
Shi, Y., & Holtzman, D. M. (2018) · Nature Reviews Immunology · doi:10.1038/s41577-018-0051-1 · Cited by 595
Self-citationBrier, M. R., Thomas, J. B., Snyder, A. Z., Benzinger, T. L., Zhang, D., Raichle, M. E., Holtzman, D. M., Morris, J. C., & Ances, B. M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5698-11.2012 · Cited by 595
Self-citationAt the interface of sensory and motor dysfunctions and Alzheimer’s disease.
Albers, M. W., Gilmore, G. C., Kaye, J., Murphy, C., Wingfield, A., Bennett, D. A., Boxer, A. L., Buchman, A. S., Cruickshanks, K. J., Devanand, D. P., et al. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.04.514 · Cited by 589
Self-citationAutophagy: machinery and regulation
Yin, Z., Pascual, C., & Klionsky, D. J. (2016) · Microbial Cell · doi:10.15698/mic2016.12.546 · Cited by 582
Animal models of neurodegenerative diseases
Dawson, T. M., Golde, T. E., & Lagier-Tourenne, C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0236-8 · Cited by 576
Suppression of eIF2α kinases alleviates Alzheimer's disease–related plasticity and memory deficits
Ma, T., Trinh, M. A., Wexler, A. J., Bourbon, C., Gatti, E., Pierre, P., Cavener, D. R., & Klann, E. (2013) · Nature Neuroscience · doi:10.1038/nn.3486 · Cited by 575
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
Roh, J. H., Huang, Y., Bero, A. W., Kasten, T., Stewart, F. R., Bateman, R. J., & Holtzman, D. M. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004291 · Cited by 563
Self-citationVerghese, P. B., Castellano, J. M., Garai, K., Wang, Y., Jiang, H., Shah, A., Bu, G., Frieden, C., & Holtzman, D. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220484110 · Cited by 556
Self-citationLeyns, C. E. G., Ulrich, J. D., Finn, M. B., Stewart, F. R., Koscal, L. J., Remolina Serrano, J., Robinson, G. O., Anderson, E., Colonna, M., & Holtzman, D. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710311114 · Cited by 517
“Amyloid-β (Aβ) aggregates form extracellular plaques, while hyperphosphorylated tau (p-tau) is present in intracellular neurofibrillary tangles (1).”
BackgroundSelf-citationThe vascular basement membrane in the healthy and pathological brain
Thomsen, M. S., Routhe, L. G., & Moos, T. (2017) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x17722436 · Cited by 512
Resolving controversies on the path to Alzheimer's therapeutics
Selkoe, D. J. (2011) · Nature Medicine · doi:10.1038/nm.2460 · Cited by 494
New insights into the role of TREM2 in Alzheimer’s disease
Gratuze, M., Leyns, C. E. G., & Holtzman, D. M. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0298-9 · Cited by 489
Self-citationThe expanding amyloid family: Structure, stability, function, and pathogenesis
Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R., & Eisenberg, D. S. (2021) · Cell · doi:10.1016/j.cell.2021.08.013 · Cited by 475
Alzheimer’s Disease Genetics: From the Bench to the Clinic
Karch, C. M., Cruchaga, C., & Goate, A. M. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.041 · Cited by 473
Self-citationThe amyloid cascade-inflammatory hypothesis of Alzheimer disease: implications for therapy
McGeer, P. L., & McGeer, E. G. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1177-7 · Cited by 467
Therapeutic 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
Yin, F. (2023) · The FEBS Journal · doi:10.1111/febs.16344 · Cited by 441
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
Trushina, E., Dutta, T., Persson, X.-M. T., Mielke, M. M., & Petersen, R. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063644 · Cited by 438
Synaptic Impairment in Alzheimer’s Disease: A Dysregulated Symphony
Forner, S., Baglietto-Vargas, D., Martini, A. C., Trujillo-Estrada, L., & LaFerla, F. M. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.04.002 · Cited by 430
Targeting protein aggregation for the treatment of degenerative diseases
Eisele, Y. S., Monteiro, C., Fearns, C., Encalada, S. E., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4593 · Cited by 426
Eimer, W. A., & Vassar, R. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-2 · Cited by 425
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BackgroundBACE1 inhibitor drugs in clinical trials for Alzheimer’s disease
Vassar, R. J. (2014) · Alzheimer s Research & Therapy · doi:10.1186/s13195-014-0089-7 · Cited by 421
TREM2 variants: new keys to decipher Alzheimer disease pathogenesis
Colonna, M., & Wang, Y. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.7 · Cited by 418
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Liu, C., Xu, X., Li, B., Situ, B., Pan, W., Hu, Y., An, T., Yao, S., & Zheng, L. (2018) · Nano Letters · doi:10.1021/acs.nanolett.8b01184 · Cited by 411
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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Brier, M. R., Thomas, J., Fagan, A. M., Hassenstab, J. J., Holtzman, D. M., Benzinger, T. L. S., Morris, J. C., & Ances, B. M. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.10.081 · Cited by 394
Self-citationPreventing Alzheimer’s Disease
Selkoe, D. J. (2012) · Science · doi:10.1126/science.1228541 · Cited by 391
Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
Lee, J., Culyba, E. K., Powers, E. T., & Kelly, J. W. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.624 · Cited by 387
Zhao, J. J., O’Connor, T., & Vassar, R. J. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-150 · Cited by 379
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
Spectral-Domain OCT Measurements in Alzheimer’s Disease
Chan, V. T. T., Sun, Z., Tang, S., Chen, L. J., Wong, A., Tham, C. C. Y., Wong, T. Y., Chen, C., Ikram, M. K., Whitson, H. E., et al. (2018) · Ophthalmology · doi:10.1016/j.ophtha.2018.08.009 · Cited by 368
Bisht, K., Sharma, K. P., & Tremblay, M. (2018) · Neurobiology of Stress · doi:10.1016/j.ynstr.2018.05.003 · Cited by 366
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Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361
Tramutola, A., Triplett, J. C., Di Domenico, F., Niedowicz, D. M., Murphy, M. P., Coccia, R., Perluigi, M., & Butterfield, D. A. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13037 · Cited by 347
Perluigi, M., Di Domenico, F., & Butterfield, D. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.014 · Cited by 339
γ-Secretase in Alzheimer’s disease
Hur, J. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00754-8 · Cited by 339
Cook, C. N., Carlomagno, Y., Gendron, T. F., Dunmore, J. H., Scheffel, K., Stetler, C. T., Davis, M., Dickson, D. W., Jarpe, M. B., Deture, M. A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt402 · Cited by 325
Wright, A. L., Zinn, R., Hohensinn, B., Konen, L. M., Beynon, S. B., Tan, R. P., Clark, I. A., Abdipranoto, A., & Vissel, B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059586 · Cited by 322
Glucagon-like peptide-1: a multi-faceted anti-inflammatory agent
Mehdi, S. F., Pusapati, S., Anwar, M. S., Lohana, D., Kumar, P., Nandula, S. A., Nawaz, F. K., Tracey, K., Yang, H., LeRoith, D., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1148209 · Cited by 317
Alzheimer's disease: synapses gone cold
Koffie, R. M., Hyman, B. T., & Spires‐Jones, T. L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-63 · Cited by 316
Fyn inhibition rescues established memory and synapse loss in Alzheimer mice
Kaufman, A. C., Salazar, S. V., Haas, L. T., Yang, J., Kostylev, M. A., Jeng, A. T., Robinson, S. A., Gunther, E. C., van Dyck, C. H., Nygaard, H. B., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24394 · Cited by 314
Rodriguez‐Vieitez, E., Saint‐Aubert, L., Carter, S. F., Almkvist, O., Farid, K., Schöll, M., Chiotis, K., Þórðardóttir, S., Graff, C., Wall, A. E., et al. (2016) · Brain · doi:10.1093/brain/awv404 · Cited by 307
Neill, C. O. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.02.025 · Cited by 300
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
Self-citationApolipoprotein E, Especially Apolipoprotein E4, Increases the Oligomerization of Amyloid β Peptide
Hashimoto, T., Serrano-Pozo, A., Hori, Y., Adams, K. W., Takeda, S., Banerji, A. O., Mitani, A., Joyner, D., Thyssen, D. H., Bacskai, B. J., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1542-12.2012 · Cited by 294
Self-citationSynaptic 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
Lim, A. S. P., Yu, L., Kowgier, M. E., Schneider, J. A., Buchman, A. S., & Bennett, D. A. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.4215 · Cited by 269
Dendritic spines: Revisiting the physiological role
Chidambaram, S. B., Rathipriya, A. G., Bolla, S. R., Bhat, A., Ray, B., Mahalakshmi, A. M., Manivasagam, T., Thenmozhi, A. J., Essa, M. M., Guillemin, G. J., et al. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.01.005 · Cited by 266
Neuronal hyperactivity--A key defect in Alzheimer’s disease?
Busche, M. A., & Konnerth, A. (2015) · BioEssays · doi:10.1002/bies.201500004 · Cited by 266
Urolithin A attenuates memory impairment and neuroinflammation in APP/PS1 mice
Gong, Z., Huang, J., Xu, B., Ou, Z., Zhang, L., Lin, X., Ye, X., Kong, X., Long, D., Sun, X., et al. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1450-3 · Cited by 265
β-Hydroxybutyrate inhibits inflammasome activation to attenuate Alzheimer’s disease pathology
Shippy, D. C., Wilhelm, C. R., Viharkumar, P. A., Raife, T. J., & Ulland, T. K. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01948-5 · Cited by 266
Microglial translational profiling reveals a convergent APOE pathway from aging, amyloid, and tau
Kang, S. S., Ebbert, M. T. W., Baker, K. E., Cook, C., Wang, X., Sens, J. P., Kocher, J.-P., Petrucelli, L., & Fryer, J. D. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20180653 · Cited by 260
“Alzheimer’s disease (AD) is the leading form of dementia, marked by key pathological features of extracellular amyloid plaque deposition and intracellular neurofibrillary tangles composed of hyperphosphorylated tau (Holtzman et al., 2011).”
BackgroundProgress in gene therapy for neurological disorders
Simonato, M., Bennett, J., Boulis, N. M., Castro, M. G., Fink, D. J., Goins, W. F., Gray, S. J., Lowenstein, P. R., Vandenberghe, L. H., Wilson, T. J., et al. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.56 · Cited by 257
Impact of TREM2R47H variant on tau pathology–induced gliosis and neurodegeneration
Gratuze, M., Leyns, C. E. G., Sauerbeck, A. D., St-Pierre, M.-K., Xiong, M., Kim, N., Serrano, J. R., Tremblay, M.-È., Kummer, T. T., Colonna, M., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138179 · Cited by 252
Self-citationStructural and Functional Dysbiosis of Fecal Microbiota in Chinese Patients With Alzheimer's Disease
Ling, Z., Zhu, M., Yan, X., Cheng, Y., Shao, L., Liu, X., Jiang, R., & Wu, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.634069 · Cited by 252
Partial volume correction in quantitative amyloid imaging
Su, Y., Blazey, T. M., Snyder, A. Z., Raichle, M. E., Marcus, D. S., Ances, B. M., Bateman, R. J., Cairns, N. J., Aldea, P., Cash, L., et al. (2015) · NeuroImage · doi:10.1016/j.neuroimage.2014.11.058 · Cited by 247
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Self-citation
Metadata
- Authors
- Holtzman, D. M., Morris, J. C., & Goate, A. M.
- Affiliations
- Washington University in St. Louis (US)
- Venue
- Science Translational Medicine
- Published
- 2011-04-06
- Volume
- 3
- Issue
- 77
- Pages
- 77sr1-77sr1
- ISSN
- 1946-6234 (ISSN-L)
- 1946-6242
- PMC
- PMC3130546
- OpenAlex
- W2005483591
- Cited by
- 1,424
- References
- 225
- Citations by year
- 2026: 53 · 2025: 81 · 2024: 99 · 2023: 102 · 2022: 93 · 2021: 93 · 2020: 100 · 2019: 124 · 2018: 116 · 2017: 101 · 2016: 92 · 2015: 95 · 2014: 95 · 2013: 86 · 2012: 69
- FWCI
- 9.56
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Translational Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R01AG035083, RC1AG035654, P50AG005681, P01AG003991, R37AG013956, U19AG032438, U01AG032438, R01AG016208, P01AG026276)
- 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, dementia, disease prevalence, pathogenesis, translational research, early detection
- MeSH terms
- Alzheimer Disease, Humans, Amyloid beta-Peptides, tau Proteins, Disease Progression, Presenilins
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