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Amyloid, tau, pathogen infection and antimicrobial protection in Alzheimer’s disease –conformist, nonconformist, and realistic prospects for AD pathogenesis
Open accessAbstract
BACKGROUND: Alzheimer's disease (AD) is a fatal disease that threatens the quality of life of an aging population at a global scale. Various hypotheses on the etiology of AD have been developed over the years to guide efforts in search of therapeutic strategies. MAIN BODY: In this review, we focus on four AD hypotheses currently relevant to AD onset: the prevailing amyloid cascade hypothesis, the well-recognized tau hypothesis, the increasingly popular pathogen (viral infection) hypothesis, and the infection-related antimicrobial protection hypothesis. In briefly reviewing the main evidence supporting each hypothesis and discussing the questions that need to be addressed, we hope to gain a better understanding of the complicated multi-layered interactions in potential causal and/or risk factors in AD pathogenesis. As a defining feature of AD, the existence of amyloid deposits is likely fundamental to AD onset but is insufficient to wholly reproduce many complexities of the disorder. A similar belief is currently also applied to hyperphosphorylated tau aggregates within neurons, where tau has been postulated to drive neurodegeneration in the presence of pre-existing Aβ plaques in the brain. Although infection of the central nerve system by pathogens such as viruses may increase AD risk, it is yet to be determined whether this phenomenon is applicable to all cases of sporadic AD and whether it is a primary trigger for AD onset. Lastly, the antimicrobial protection hypothesis provides insight into a potential physiological role for Aβ peptides, but how Aβ/microbial interactions affect AD pathogenesis during aging awaits further validation. Nevertheless, this hypothesis cautions potential adverse effects in Aβ-targeting therapies by hindering potential roles for Aβ in anti-viral protection. CONCLUSION: AD is a multi-factor complex disorder, which likely requires a combinatorial therapeutic approach to successfully slow or reduce symptomatic memory decline. A better understanding of how various causal and/or risk factors affecting disease onset and progression will enhance the likelihood of conceiving effective treatment paradigms, which may involve personalized treatment strategies for individual patients at varying stages of disease progression.
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“Related pathogens include Helicobacter pylori, various bacteria of the liver, gut, lungs (pneumonia) and mouth, as well as viruses to include Epstein Barr virus, CMV, HIV, oral herpes HSV-1, genital herpes HSV-2, human herpesvirus (HHV)-6A/HHV-7 (recently reviewed in [530]). These pathogens can infiltrate the CNS and dysregulate AD-associated neurological function.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [530]
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“Many studies have linked AD to a diverse variety of bacterial and viral pathogens [529–531].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [530]
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“Significant overlap exists between the expression of AD-associated genes and genomic viral load in the CNS; for example, viral abundance may determine AD progression through the regulation of genes associated with APP processing [529–531].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [530]
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“A recent multi-omic study identified an enrichment of HHV-6A and HHV-7 in AD patients compared to controls [529–531].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [530]
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Items 201–320 of 320
An Overview on the Clinical Development of Tau-Based Therapeutics
Medina, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041160 · Cited by 156
The oxidative stress hypothesis in Alzheimer's disease.
Pădurariu, M., Ciobica, A. S., Lefter, R. M., Șerban, I. L., Ștefănescu, C., & Chiriță, R. (2013) · PubMed · Cited by 155
Molecular Mechanisms for Herpes Simplex Virus Type 1 Pathogenesis in Alzheimer’s Disease
Harris, S. A., & Harris, E. A. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00048 · Cited by 154
The Past and the Future of Alzheimer’s Disease Fluid Biomarkers
Blennow, K., & Zetterberg, H. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170773 · Cited by 154
RNA binding proteins co-localize with small tau inclusions in tauopathy
Maziuk, B. F., Apicco, D. J., Cruz, A. L., Jiang, L., Ash, P. E. A., da Rocha, E. L., Zhang, C., Yu, W. H., Leszyk, J., Abisambra, J. F., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0574-5 · Cited by 151
Self-citationRodriguez‐Vieitez, E., Ni, R., Gulyás, B. Z., Tóth, M., Häggkvist, J., Halldin, C., Voytenko, L. P., Marutle, A., & Nordberg, A. K. (2015) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-015-3047-0 · Cited by 149
Braak, H., & Del Tredici, K. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhy152 · Cited by 148
Wang, Y., Garg, S., Mandelkow, E., & Mandelkow�, E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380955 · Cited by 145
Oskar Fischer and the study of dementia
Goedert, M. (2008) · Brain · doi:10.1093/brain/awn256 · Cited by 144
Reynolds, M. R., Reyes, J. F., Fu, Y., Bigio, E. H., Guillozet-Bongaarts, A. L., Berry, R. W., & Binder, L. I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2143-06.2006 · Cited by 143
Herpesviruses in brains in Alzheimer's and Parkinson's diseases
Hemling, N., Röyttä, M., Rinne, J. O., Pöllänen, P., Broberg, E., Tapio, V., Vahlberg, T. J., & Hukkanen, V. (2003) · Annals of Neurology · doi:10.1002/ana.10662 · Cited by 142
Acetylation: a new key to unlock tau’s role in neurodegeneration
Cook, C. N., Stankowski, J. N., Carlomagno, Y., Stetler, C. T., & Petrucelli, L. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt259 · Cited by 140
APOE ε2 is associated with increased tau pathology in primary tauopathy
Zhao, N., Liu, C.-C., Van Ingelgom, A. J., Linares, C., Kurti, A., Knight, J. A., Heckman, M. G., Diehl, N. N., Shinohara, M., Martens, Y. A., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06783-0 · Cited by 139
Self-citationTau: From research to clinical development
Holtzman, D. M., Carrillo, M. C., Hendrix, J. A., Bain, L. J., Catafau, A. M., Gault, L. M., Goedert, M., Mandelkow, E., Mandelkow, E., Miller, D. S., et al. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.018 · Cited by 139
Hyperphosphorylation determines both the spread and the morphology of tau pathology
Hu, W. H., Zhang, X., Tung, Y. C., Xie, S.-T., Liu, F., & Iqbal, K. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.01.014 · Cited by 137
Injury markers predict time to dementia in subjects with MCI and amyloid pathology
van Rossum, I. A., Vos, S. J. B., Burns, L., Knol, D. L., Scheltens, P., Soininen, H., Wahlund, L.-O., Hampel, H., Tsolaki, M., Minthon, L., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e3182704056 · Cited by 136
Liedtke, W., Opalka, B., Zimmermann, C. W., & Lignitz, E. (1993) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(93)90082-a · Cited by 136
Review: Impact of Helicobacter pylori on Alzheimer's disease: What do we know so far?
Doulberis, M., Kotronis, G., Thomann, R., Pοlyzos, S. A., Boziki, M. K., Gialamprinou, D., Deretzi, G., Katsinelos, P., & Kountouras, J. (2017) · Helicobacter · doi:10.1111/hel.12454 · Cited by 134
3D culture models of Alzheimer’s disease: a road map to a “cure-in-a-dish”
Choi, S. H., Kim, Y. H., Quinti, L., Tanzi, R. E., & Kim, D. Y. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0139-7 · Cited by 132
West, T., Hu, Y., Verghese, P. B., Bateman, R. J., Braunstein, J. B., Fogelman, I., Budur, K., Florian, H., Mendonca, N., & Holtzman, D. M. (2017) · PubMed · doi:10.14283/jpad.2017.36 · Cited by 132
Relevance of Phosphorylation and Truncation of Tau to the Etiopathogenesis of Alzheimer’s Disease
Zhou, Y., Shi, J., Chu, D., Hu, W. H., Guan, Z., Gong, C., Iqbal, K., & Liu, F. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00027 · Cited by 130
Golgi fragmentation in Alzheimer's disease
Joshi, G. S., Bekier, M. E., & Wang, Y. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00340 · Cited by 129
Aberrant subcellular neuronal calcium regulation in aging and Alzheimer's disease
Camandola, S., & Mattson, M. P. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.005 · Cited by 128
Metformin promotes tau aggregation and exacerbates abnormal behavior in a mouse model of tauopathy
Barini, E., Antico, O., Zhao, Y., Asta, F., Tucci, V., Catelani, T., Marotta, R., Xu, H., & Gasparini, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0082-7 · Cited by 126
Fülöp, T., Itzhaki, R. F., Balin, B. J., Miklossy, J., & Barron, A. E. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00362 · Cited by 123
Herpes simplex virus type 1 and Alzheimer's disease: possible mechanisms and signposts
Itzhaki, R. F. (2017) · The FASEB Journal · doi:10.1096/fj.201700360 · Cited by 120
Mechanisms of restriction of viral neuroinvasion at the blood–brain barrier
Miner, J. J., & Diamond, M. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.10.008 · Cited by 118
O‐GlcNAcylation: A regulator of tau pathology and neurodegeneration
Gong, C., Liu, F., & Iqbal, K. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.02.011 · Cited by 117
The therapeutics of Alzheimer's disease: Where we stand and where we are heading
Selkoe, D. J. (2013) · Annals of Neurology · doi:10.1002/ana.24001 · Cited by 116
Hiruma, H., Katakura, T., Takahashi, S., Ichikawa, T., & Kawakami, T. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08967.2003 · Cited by 114
Multisite assessment of NIA‐AA guidelines for the neuropathologic evaluation of Alzheimer's disease
Montine, T. J., Monsell, S. E., Beach, T. G., Bigio, E. H., Bu, Y., Cairns, N. J., Frosch, M., Henriksen, J., Kofler, J., Kukull, W. A., et al. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2015.07.492 · Cited by 113
Human amyloid β‐induced neuroinflammation is an early event in neurodegeneration
Craft, J. M., Watterson, D. M., & Eldik, L. J. V. (2005) · Glia · doi:10.1002/glia.20306 · Cited by 111
Harding, A., Gonder, U., Robinson, S. J., Crean, S., & Singhrao, S. K. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00398 · Cited by 110
Serrano‐Pozo, A., Qian, J., Muzikansky, A., Monsell, S. E., Montine, T. J., Frosch, M. P., Betensky, R. A., & Hyman, B. T. (2016) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlw026 · Cited by 110
Lacovich, V., Espíndola, S. L., Alloatti, M., Devoto, V. M. P., Cromberg, L. E., Čarná, M. E., Forte, G., Gallo, J., Bruno, L., Stokin, G. B., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2305-16.2016 · Cited by 108
Tau reduction in the presence of amyloid-β prevents tau pathology and neuronal death in vivo
DeVos, S. L., Corjuc, B. T., Commins, C., Dujardin, S., Bannon, R. N., Corjuc, D., Moore, B. D., Bennett, R. E., Jorfi, M., Gonzales, J. A., et al. (2018) · Brain · doi:10.1093/brain/awy117 · Cited by 106
Pathological Changes of Tau Related to Alzheimer’s Disease
Chu, D., & Liu, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00457 · Cited by 106
Miyamoto, T., Stein, L. R., Thomas, R., Djukic, B., Taneja, P., Knox, J. A., Vossel, K. A., & Mucke, L. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0176-x · Cited by 106
Periodontitis, Microbiomes and their Role in Alzheimer’s Disease
Pritchard, A. B., Crean, S., Olsen, I., & Singhrao, S. K. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00336 · Cited by 104
Jiang, S., Nandy, P., Wang, W., Ma, X., Hsia, J., Wang, C., Wang, Z., Niu, M., Siedlak, S. L., Torres, S. L., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0238-8 · Cited by 104
Benedict, C., & Grillo, C. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00215 · Cited by 101
Pallas‐Bazarra, N., Jurado‐Arjona, J., Navarrete, M., Esteban, J. A., Hernández, F., Ávila, J., & Llorens‐Martín, M. (2016) · The EMBO Journal · doi:10.15252/embj.201593518 · Cited by 101
APP physiological and pathophysiological functions: insights from animal models
Guo, Q., Wang, Z., Li, H., Wiese, M., & Zheng, H. (2011) · Cell Research · doi:10.1038/cr.2011.116 · Cited by 101
Self-citationAnti-tau antibody administration increases plasma tau in transgenic mice and patients with tauopathy
Yanamandra, K., Patel, T. K., Jiang, H., Schindler, S., Ulrich, J. D., Boxer, A. L., Miller, B. L., Kerwin, D. R., Gallardo, G., Stewart, F., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal2029 · Cited by 100
Oral Inflammation, Tooth Loss, Risk Factors, and Association with Progression of Alzheimer's Disease
Singhrao, S. K., Harding, A., Simmons, T. L., Robinson, S. J., Kesavalu, L. N., & Crean, S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140387 · Cited by 100
Tau hyperphosphorylation induces oligomeric insulin accumulation and insulin resistance in neurons
Rodriguez‐Rodriguez, P., Matton, A., Merino‐Serrais, P., Parrado‐Fernández, C., Rábano, A., Winblad, B. G., Ávila, J., Ferrer, I., & Cedazo-Mínguez, Á. (2017) · Brain · doi:10.1093/brain/awx256 · Cited by 99
Alzheimer's disease: The amyloid hypothesis on trial
Harrison, J. R., & Owen, M. J. (2016) · The British Journal of Psychiatry · doi:10.1192/bjp.bp.115.167569 · Cited by 98
Park, J., Choi, H., Min, J., Kim, B., Lee, S., Yun, J. W., Choi, M., Chang, K., & Lee, D. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12984 · Cited by 93
Internalized Tau sensitizes cells to stress by promoting formation and stability of stress granules
Brunello, C. A., Yan, X., & Huttunen, H. J. (2016) · Scientific Reports · doi:10.1038/srep30498 · Cited by 89
Ball, M. J., Lukiw, W. J., Kammerman, E. M., & Hill, J. M. (2013) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2012.07.005 · Cited by 89
Aβ accumulation causes MVB enlargement and is modelled by dominant negative VPS4A
Willén, K., Edgar, J. R., Hasegawa, T., Tanaka, N., Futter, C. E., & Gouras, G. K. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0203-y · Cited by 86
Wren, M. C., Zhao, J., Liu, C., Murray, M. E., Atagi, Y., Davis, M. D., Fu, Y., Okano, H. J., Ogaki, K., Strongosky, A. J., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0042-7 · Cited by 86
Self-citationYang, J., Li, S., He, X., Cheng, C., & Le, W. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0106-3 · Cited by 86
Granulovacuolar degeneration: a neurodegenerative change that accompanies tau pathology
Köhler, C. N. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1562-0 · Cited by 85
van Rossum, I. A., Visser, P. J., Knol, D. L., van der Flier, W. M., Teunissen, C. E., Barkhof, F., Blankenstein, M. A., & Scheltens, P. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111694 · Cited by 84
Wu, X., Piña-Crespo, J., Zhang, Y., Chen, X., & Xu, H. (2017) · Chinese Medical Journal · doi:10.4103/0366-6999.220313 · Cited by 82
HSV-1 in brain and risk of Alzheimer's disease.
Beffert, U., Bertrand, P., Champagne, D. L., Gauthier, S., & Poirier, J. (1998) · The Lancet · doi:10.1016/s0140-6736(05)79057-7 · Cited by 80
Violet, M., Chauderlier, A., Delattre, L., Tardivel, M., Chouala, M. S., Sultan, A., Marciniak, E., Humez, S., Binder, L. I., Kayed, R., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.09.003 · Cited by 80
In vivo PET imaging of neuroinflammation in Alzheimer’s disease
Lagarde, J., Sarazin, M., & Bottlaender, M. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1731-x · Cited by 79
Herpes and Alzheimer’s Disease: Subversion in the Central Nervous System and How It Might Be Halted
Itzhaki, R. F. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160607 · Cited by 76
Neuritic and Diffuse Plaque Associations with Memory in Non-Cognitively Impaired Elderly
Malek-Ahmadi, M., Perez, S. E., Chen, K., & Mufson, E. J. (2016) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160365 · Cited by 73
Degradation or aggregation: the ramifications of post-translational modifications on tau
Park, S., Lee, J. H., Jeon, J. H., & Lee, M. J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.6.077 · Cited by 73
Selective vulnerability in neurodegeneration: insights from clinical variants of Alzheimer's disease
Mattsson, N., Schott, J. M., Hardy, J., Turner, M. R., & Zetterberg, H. (2016) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2015-311321 · Cited by 72
Acetylated tau in Alzheimer's disease: An instigator of synaptic dysfunction underlying memory loss
Tracy, T. E., & Gan, L. (2017) · BioEssays · doi:10.1002/bies.201600224 · Cited by 72
Choi, H., Kim, H. J., Kim, J., Kim, S., Yang, J., Lee, W., Park, Y., Hyeon, S. J., Lee, D.-S., Ryu, H., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0164-1 · Cited by 71
Völgyi, K., Juhász, G. D., Kovács, Z., & Penke, B. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150710095035 · Cited by 71
Hill, J. M., Ball, M. J., Neumann, D. M., Azcuy, A. M., Bhattacharjee, P. S., Bouhanik, S., Clément, C., Lukiw, W. J., Foster, T. P., Kumar, M., et al. (2008) · Journal of Virology · doi:10.1128/jvi.00686-08 · Cited by 69
Pir, G. J., Choudhary, B. C., Mandelkow�, E., & Mandelkow, E. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0096-1 · Cited by 65
Congdon, E. E., Lin, Y., Rajamohamedsait, H. B., Shamir, D. B., Krishnaswamy, S., Rajamohamedsait, W. J., Rasool, S., González‐Calle, V., Levenga, J., Gu, J., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0126-z · Cited by 64
Evidence for altered insulin receptor signaling in Alzheimer's disease
Griffith, C. M., Eid, T., Rose, G. M., & Patrylo, P. R. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.01.008 · Cited by 64
Human tau expression reduces adult neurogenesis in a mouse model of tauopathy
Komuro, Y., Xu, G., Bhaskar, K., & Lamb, B. T. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.002 · Cited by 64
Membrane Localization of β-Amyloid 1–42 in Lysosomes
Liu, R., Zhou, Q., Ji, S., Zhou, Q., Feng, D., Wu, Y., & Sui, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.036798 · Cited by 64
Cox, K. K., Combs, B., Abdelmesih, B., Morfini, G. A., Brady, S. T., & Kanaan, N. M. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.07.015 · Cited by 62
Woodling, N. S., & Andreasson, K. I. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00016 · Cited by 62
Aguayo, S. D., Schuh, C. M. A. P., Vicente, B., & Aguayo, L. G. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180319 · Cited by 62
Alzheimer's disease and periodontitis - an elusive link
Gurav, A. N. (2014) · Revista da Associação Médica Brasileira · doi:10.1590/1806-9282.60.02.015 · Cited by 62
Tyrosine Nitration within the Proline-Rich Region of Tau in Alzheimer's Disease
Reyes, J. F., Fu, Y., Vana, L., Kanaan, N. M., & Binder, L. I. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.01.030 · Cited by 61
Targeting psychologic stress signaling pathways in Alzheimer’s disease
Futch, H. S., Croft, C. L., Truong, V., Krause, E. G., & Golde, T. E. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0190-z · Cited by 61
Tau-dependent suppression of adult neurogenesis in the stressed hippocampus
Dioli, C., Patrício, P., Trindade, R., Pinto, L., Silva, J. M., Morais, M., Ferreiro, E. B., Borges, S., Mateus‐Pinheiro, A., Rodrigues, A. J., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.103 · Cited by 59
AAV-mediated expression of anti-tau scFvs decreases tau accumulation in a mouse model of tauopathy
Ising, C., Gallardo, G., Leyns, C. E. G., Wong, C. H., Jiang, H., Stewart, F., Koscal, L. J., Roh, J., Robinson, G. O., Remolina Serrano, J., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20162125 · Cited by 57
Agadjanyan, M. G., Zagorski, K., Petrushina, I., Davtyan, H., Kazarian, K., Antonenko, M., Davis, J. L., Bon, C., Blurton-Jones, M. M., Cribbs, D. H., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0172-1 · Cited by 56
Bai, Y., Li, M., Zhou, Y., Ma, L., Qiao, Q., Hu, W., Li, W., Wills, Z. P., & Gan, W. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0228-2 · Cited by 56
A subset of senile dementia with high incidence of the apolipoprotein E ϵ2 allele
Ikeda, K., Akiyama, H., Arai, T., Sahara, N., Mori, H., Usami, M., Sakata, M., Mizutani, T., Wakabayashi, K., & Takahashi, H. (1997) · Annals of Neurology · doi:10.1002/ana.410410522 · Cited by 55
Neuroimaging biomarkers in Alzheimer’s disease and other dementias
Villemagne, V. L., & Chételat, G. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.01.004 · Cited by 55
Deng, M., He, W., Tan, Y., Han, H., Hu, X., Xia, K., Zhang, Z., & Yan, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.480079 · Cited by 53
Tau acts as a mediator forAlzheimer's disease‐related synaptic deficits
Liao, D., Miller, E. C., & Teravskis, P. J. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12504 · Cited by 53
Strang, K. H., Goodwin, M. S., Riffe, C. J., Moore, B. D., Chakrabarty, P., Levites, Y., Golde, T. E., & Giasson, B. I. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0458-0 · Cited by 53
Mutual Relationship between Tau and Central Insulin Signalling: Consequences for AD and Tauopathies?
Gratuze, M., Joly‐Amado, A., Vieau, D., Buée, L., & Blum, D. L. (2018) · Neuroendocrinology · doi:10.1159/000487641 · Cited by 51
Argyrophilic grain disease is associated with apolipoprotein E ε2 allele
Ghebremedhin, E., Schultz, C., Botez, G., Rüb, U., Sassin, I., Braak, E., & Braak, H. (1998) · Acta Neuropathologica · doi:10.1007/s004010050886 · Cited by 50
Selective tau tyrosine nitration in non-AD tauopathies
Reyes, J. F., Geula, C., Vana, L., & Binder, L. I. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0898-8 · Cited by 46
Reduced brain insulin signaling: A seminal process in Alzheimer's disease pathogenesis
Bloom, G. S., Lazo, J. S., & Norambuena, A. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.09.016 · Cited by 44
Audrain, M., Fol, R. R., Dutar, P., Potier, B., Billard, J., Flament, J., Alves, S., Burlot, M., Dufayet‐Chaffaud, G., Bemelmans, A., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0070-y · Cited by 44
Arnerić, S. P., Batrla‐Utermann, R., Beckett, L. A., Bittner, T., Blennow, K., Carter, L., Dean, R. A., Engelborghs, S., Genius, J., Gordon, M. F., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160573 · Cited by 44
Distribution of herpes simplex virus DNA in the brains of human long-term survivors of encephalitis
Nicoll, J. A. R., Love, S., & Kinrade, E. (1993) · Neuroscience Letters · doi:10.1016/0304-3940(93)90740-c · Cited by 42
Jamieson, G. A., Maitland, N. J., Craske, J., Wilcock, G. K., & Itzhaki, R. F. (1991) · Biochemical Society Transactions · doi:10.1042/bst019122s · Cited by 41
Boehm, J. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12251 · Cited by 41
Murray, M., & Dickson, D. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt254 · Cited by 39
Lack of Evidence for a Role of HHV-6 in the Pathogenesis of Alzheimer’s Disease
Agostini, S., Mancuso, R., Baglio, F., Cabinio, M., Hernis, A., Guerini, F. R., Calabrese, E., Nemni, R., & Clerici, M. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150464 · Cited by 39
Progression of Alzheimer histopathological changes.
Duyckaerts, C. J., Colle, M.-A., Dessi, F., Piette, F., & Hauw, J. (1998) · PubMed · Cited by 38
Mechanisms of CNS invasion and damage by parasites
Kristensson, K., Masocha, W., & Bentivoglio, M. (2013) · Handbook of clinical neurology · doi:10.1016/b978-0-444-53490-3.00002-9 · Cited by 37
Network-driven plasma proteomics expose molecular changes in the Alzheimer’s brain
Jaeger, P. A., Lucin, K. M., Britschgi, M., Vardarajan, B. N., Huang, R.-P., Kirby, E. D., Abbey, R. J., Boeve, B. F., Boxer, A. L., Farrer, L. A., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0095-2 · Cited by 35
Blood-based near-infrared spectroscopy for the rapid low-cost detection of Alzheimer's disease
Paraskevaidi, M., Morais, C. L. M., Freitas, D. L. D., Lima, K. M. G., Mann, D. M. A., Allsop, D., Martin‐Hirsch, P. L., & Martin, F. L. (2018) · The Analyst · doi:10.1039/c8an01205a · Cited by 34
How do soluble oligomers of amyloid β-protein impair hippocampal synaptic plasticity?
Li, L. (2010) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2010.00005 · Cited by 33
Sanders, V. J. (1997) · Archives of Neurology · doi:10.1001/archneur.1997.00550200020005 · Cited by 32
Itzhaki, R. F., & Lin, W.-T. (1998) · Biochemical Society Transactions · doi:10.1042/bst0260273 · Cited by 31
Anti-aggregant tau mutant promotes neurogenesis
Joseph, M., Anglada‐Huguet, M., Paesler, K., Mandelkow�, E., & Mandelkow, E. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0230-8 · Cited by 30
A seeding based cellular assay of tauopathy
Xu, Y., Martini‐Stoica, H., & Zheng, H. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0100-9 · Cited by 26
Self-citationSolomos, A. C., & Rall, G. F. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00336 · Cited by 25
Zheng, B.-W., Li, Y., Dai, X., Jiang, Z.-F., & Huang, H. (2016) · Neurological Research · doi:10.1080/01616412.2015.1133485 · Cited by 24
Distinct tau PET imaging patterns in typical and atypical Alzheimer’s disease
Sarazin, M., Lagarde, J., & Bottlaender, M. (2016) · Brain · doi:10.1093/brain/aww041 · Cited by 20
Vesicular Axonal Transport is Modified In Vivo by Tau Deletion or Overexpression in Drosophila
Talmat-Amar, Y., Arribat, Y., & Parmentier, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030744 · Cited by 20
Modification of Tau by 8-Nitroguanosine 3′,5′-Cyclic Monophosphate (8-Nitro-cGMP)
Yoshitake, J., Soeda, Y., Ida, T., Sumioka, A., Yoshikawa, M., Matsushita, K., Akaike, T., & Takashima, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.734350 · Cited by 20
Jamieson, C. A., Maitland, N. J., & Itzhaki, R. F. (1992) · Archives of Gerontology and Geriatrics · doi:10.1016/s0167-4943(05)80019-6 · Cited by 16
Alzheimer's Disease: It's More Than Aβ
Buxbaum, J. N. (2016) · The FASEB Journal · doi:10.1096/fj.201601179 · Cited by 13
Doulberis, M., Kountouras, J., Pοlyzos, S. A., Tzivras, D., Vardaka, E., Kountouras, C., Tzilves, D., Kotronis, G., Boutsikou, E., Gialamprinou, D., et al. (2018) · Helicobacter · doi:10.1111/hel.12534 · Cited by 13
Monitoring the progression of Alzheimer’s disease with τ-PET: Table 1
Thal, D. R., & Vandenberghe, R. R. (2016) · Brain · doi:10.1093/brain/aww057 · Cited by 6
Sequential CT scanning in radiation myelopathy
Tugendhaft, P., Balériaux, D., Gérard, J.-M., & Hildebrand, J. G. (1984) · Journal of Neuro-Oncology · doi:10.1007/bf00253277 · Cited by 6
New connections: Amyloid-β, calcium, and the synapse
Ferrarelli, L. K. (2017) · Science Signaling · doi:10.1126/scisignal.aao3024 · Cited by 4
Harnessing innate immunity to fight neurodegeneration
Mushegian, A. A. (2017) · Science Signaling · doi:10.1126/scisignal.aam8102 · Cited by 2
New connections: Understanding the tumor through the stroma
Ferrarelli, L. K. (2017) · Science Signaling · doi:10.1126/scisignal.aao5803 · Cited by 1
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Metadata
- Authors
- Li, H., Liu, C.-C., Zheng, H., & Huang, T. Y.
- Affiliations
- Mayo Clinic in Florida (US)
- Baylor College of Medicine (US)
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Corresponding author
- Li, Hongmei
- Huang, Timothy Y.
- Venue
- Translational Neurodegeneration
- Published
- 2018-12
- Volume
- 7
- Issue
- 1
- Pages
- 34-34
- ISSN
- 2047-9158 (ISSN-L)
- PMC
- PMC6306008
- OpenAlex
- W2906630689
- Cited by
- 103
- References
- 321
- Citations by year
- 2026: 8 · 2025: 5 · 2024: 12 · 2023: 16 · 2022: 13 · 2021: 16 · 2020: 25 · 2019: 8
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Translational Neurodegeneration (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (AG059217, AG061875, AG062257, AG057509, AG054111, AG020670, AG057981)
- BrightFocus Foundation (A2016346F)
- Alzheimer Association (AARG-17-500335)
- Florida Department of Health (8AZ07)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid hypothesis, tau hypothesis, viral infection hypothesis, amyloid-beta, tau hyperphosphorylation, neurodegeneration, AD pathogenesis, risk factors, personalized treatment
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