Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy

The 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

Alzheimer's Disease Is a Synaptic Failure

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

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

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

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

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

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498

A simplified system for generating recombinant adenoviruses

He, T., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., & Vogelstein, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2509 · Cited by 3,209

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

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

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089

Mouse models of Alzheimer's disease

Hall, A. M., & Roberson, E. D. (2012) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.11.017 · Cited by 317

Function of microglia and macrophages in secondary damage after spinal cord injury

Ren, Y., Zhou, X., & He, X. (2014) · Neural Regeneration Research · doi:10.4103/1673-5374.143423 · Cited by 328

Recent publications from the Alzheimer's Disease Neuroimaging Initiative: Reviewing progress toward improved AD clinical trials

Weiner, M. W., Veitch, D. P., Aisen, P. S. S., Beckett, L. A., Cairns, N. J., Green, R. C., Harvey, D. J., Jack, C. R., Jagust, W. J., Morris, J. C., et al. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.11.007 · Cited by 325

Microbiota in neuroinflammation and synaptic dysfunction: a focus on Alzheimer’s disease

Bairamian, D., Sha, S., Rolhion, N., Sokol, H., Dorothée, G., Lemere, C. A., & Krantic, S. M. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00522-2 · Cited by 326

γ-Secretase in Alzheimer’s disease

Hur, J. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00754-8 · Cited by 339

Sexual dimorphism in the inflammatory response to traumatic brain injury

Villapol, S., Loane, D. J., & Burns, M. P. (2017) · Glia · doi:10.1002/glia.23171 · Cited by 320

Pathogenic tau-induced piRNA depletion promotes neuronal death through transposable element dysregulation in neurodegenerative tauopathies

Sun, W., Samimi, H., Gamez, M., Zare, H., & Frost, B. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0194-1 · Cited by 300

Tau Protein Is Required for Amyloid β-Induced Impairment of Hippocampal Long-Term Potentiation

Shipton, O. A., Leitz, J. R., Dworzak, J., Acton, C. E. J., Tunbridge, E. M., Denk, F., Dawson, H. N., Vitek, M. P., Wade-Martins, R., Paulsen, O., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2610-10.2011 · Cited by 315

PART is part of Alzheimer disease

Duyckaerts, C. J., Braak, H., Brion, J., Buée, L., Tredici, K. D., Goedert, M., Halliday, G. M., Neumann, M., Spillantini, M. G., Tolnay, M., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1390-7 · Cited by 329

Dysregulation of Ubiquitin-Proteasome System in Neurodegenerative Diseases

Zheng, Q., Huang, T. Y., Zhang, L., Zhou, Y., Luo, H., Xu, H., & Wang, X. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00303 · Cited by 327

Adult Hippocampal Neurogenesis in Aging and Alzheimer's Disease

Babcock, K. R., Page, J. S., Fallon, J. R., & Webb, A. E. (2021) · Stem Cell Reports · doi:10.1016/j.stemcr.2021.01.019 · Cited by 330

Cyclopentenone prostaglandins suppress activation of microglia: Down-regulation of inducible nitric-oxide synthase by 15-deoxy-Δ 12,14 -prostaglandin J 2

Petrova, T. V., Akama, K. T., & Eldik, L. J. V. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4668 · Cited by 311

Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage

Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314

The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease

Brothers, H. M., Gosztyla, M. L., & Robinson, S. R. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00118 · Cited by 314

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

Integrative network analysis of nineteen brain regions identifies molecular signatures and networks underlying selective regional vulnerability to Alzheimer’s disease

Wang, M., Roussos, P., McKenzie, A., Zhou, X., Kajiwara, Y., Brennand, K. J., De Luca, G. C., Crary, J. F., Casaccia, P., Buxbaum, J. D., et al. (2016) · Genome Medicine · doi:10.1186/s13073-016-0355-3 · Cited by 314

Neuroinflammation and Neuronal Loss Precede Aβ Plaque Deposition in the hAPP-J20 Mouse Model of Alzheimer’s Disease

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

GSK-3 and tau: a key duet in Alzheimer’s disease

Sayas, C. L., & Ávila, J. (2021) · Cells · doi:10.3390/cells10040721 · Cited by 314

Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade

Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313

Whole-genome sequencing reveals important role for TBK1 and OPTN mutations in frontotemporal lobar degeneration without motor neuron disease

Pottier, C., Bieniek, K. F., Finch, N., van de Vorst, M., Baker, M., Perkersen, R., Brown, P., Ravenscroft, T., van Blitterswijk, M., Nicholson, A. M., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1436-x · Cited by 312

Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer's disease

An, W.-L., Cowburn, R. F., Li, L., Braak, H., Alafuzoff, I., Iqbal, K., Iqbal, I.-G., Winblad, B., & Pei, J.-J. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63687-5 · Cited by 312

HMGB1: A Common Biomarker and Potential Target for TBI, Neuroinflammation, Epilepsy, and Cognitive Dysfunction

Paudel, Y. N., Shaikh, M. F., Chakraborti, A., Kumari, Y., Aledo-Serrano, Á., Aleksovska, K., Alvim, M. K. M., & Othman, I. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00628 · Cited by 311

Dendritic BC200 RNA in aging and in Alzheimer's disease

Mus, E., Hof, P. R., & Tiedge, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701532104 · Cited by 314

Use of Caenorhabditis elegans as a model to study Alzheimer’s disease and other neurodegenerative diseases

Alexander, A. G., Marfil, V., & Li, C. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00279 · Cited by 310

Molecular and cellular pathways of neurodegeneration in motor neurone disease

Shaw, P. J. (2005) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2004.048652 · Cited by 311

Nicotinic Acetylcholine Receptor Signalling: Roles in Alzheimer’s Disease and Amyloid Neuroprotection

Buckingham, S. D., Jones, A. K., Brown, L. A., & Sattelle, D. B. (2009) · Pharmacological Reviews · doi:10.1124/pr.108.000562 · Cited by 312

Cannabidiol in vivo blunts β‐amyloid induced neuroinflammation by suppressing IL‐1β and iNOS expression

Esposito, G., Scuderi, C., Savani, C., Steardo, L., De Filippis, D., Cottone, P., Iuvone, T., Cuomo, V, & Steardo, L. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707337 · Cited by 308

Nanotechnology-based drug delivery systems for the treatment of Alzheimer’s disease

Fonseca‐Santos, B., Chorilli, M., & Gremião, M. P. D. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s87148 · Cited by 320

Amyloid‐beta oligomerization in Alzheimer dementia versus high‐pathology controls

Esparza, T. J., Zhao, H., Cirrito, J. R., Cairns, N. J., Bateman, R. J., Holtzman, D. M., & Brody, D. L. (2012) · Annals of Neurology · doi:10.1002/ana.23748 · Cited by 319

ALS as a distal axonopathy: molecular mechanisms affecting neuromuscular junction stability in the presymptomatic stages of the disease

Moloney, E. B., de Winter, F., & Verhaagen, J. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00252 · Cited by 319

PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease

Du, F., Yu, Q., Yan, S., Hu, G., Lue, L., Walker, D., Wu, L., Yan, S. F., Tieu, K., & Yan, S. S. (2017) · Brain · doi:10.1093/brain/awx258 · Cited by 308

Microtubule-associated protein tau is essential for long-term depression in the hippocampus

Kimura, T., Whitcomb, D. J., Jo, J., Regan, P., Piers, T., Heo, S., Brown, C., Hashikawa, T., Murayama, M., Seok, H., et al. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0144 · Cited by 307

The Genetics of Parkinson Disease

Bekris, L. M., Mata, I. F., & Zabetian, C. P. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383572 · Cited by 314

The effects of microglia-associated neuroinflammation on Alzheimer’s disease

Wang, C., Zong, S., Cui, X., Wang, X., Wu, S., Wang, L., Liu, Y., & Lu, Z. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1117172 · Cited by 331

Assembly of recombinant tau into filaments identical to those of Alzheimer’s disease and chronic traumatic encephalopathy

Lövestam, S., Koh, F. A., van Knippenberg, B., Kotecha, A., Murzin, A. G., Goedert, M., & Scheres, S. H. W. (2022) · eLife · doi:10.7554/elife.76494 · Cited by 306

Tunneling nanotube (TNT)-mediated neuron-to neuron transfer of pathological Tau protein assemblies

Tardivel, M., Bégard, S., Bousset, L., Dujardin, S., Coens, A., Melki, R., Buée, L., & Colin, M. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0386-4 · Cited by 305

The Endogenous and Cell Cycle-dependent Phosphorylation of tau Protein in Living Cells: Implications for Alzheimer’s Disease

Illenberger, S., Zheng‐Fischhöfer, Q., Preuß, U., Stamer, K., Baumann, K., Trinczek, B., Biernat, J., Godemann, R., Mandelkow, E., & Mandelkow�, E. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.6.1495 · Cited by 305

Suspected non-Alzheimer disease pathophysiology — concept and controversy

Jack, C. R., Knopman, D. S., Chételat, G., Dickson, D. W., Fagan, A. M., Frisoni, G. B., Jagust, W. J., Mormino, E. C., Petersen, R. C., Sperling, R. A., et al. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.251 · Cited by 313

Adult Neurogenesis in Neurodegenerative Diseases: Figure 1.Preprint

Winner, B., & Winkler, J. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021287 · Cited by 323

Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states

Miller, Y., Ma, B., & Nussinov, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913114107 · Cited by 305

Stability properties of neuronal microtubules

Baas, P. W., Rao, A. N., Matamoros, A. J., & Leo, L. (2016) · Cytoskeleton · doi:10.1002/cm.21286 · Cited by 315

Mechanisms of secretion and spreading of pathological tau protein

Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304

The DIAN‐TU Next Generation Alzheimer's prevention trial: Adaptive design and disease progression model

Bateman, R. J., Benzinger, T. L., Berry, S., Clifford, D. B., Duggan, C., Fagan, A. M., Fanning, K., Farlow, M. R., Hassenstab, J., McDade, E. M., et al. (2017) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.07.005 · Cited by 303

Concepts and Methods for the Study of Axonal Regeneration in the CNS

Tuszynski, M. H., & Steward, O. (2012) · Neuron · doi:10.1016/j.neuron.2012.05.006 · Cited by 305

Drug repositioning for Alzheimer's disease

Corbett, A., Pickett, J., Burns, A. S., Corcoran, J. P. T., Dunnett, S. B., Edison, P., Hagan, J. J., Holmes, C., Jones, E., Katona, C., et al. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3869 · Cited by 307

Blood-brain barrier–penetrating siRNA nanomedicine for Alzheimer’s disease therapy

Zhou, Y., Zhu, F., Liu, Y., Zheng, M., Wang, Y., Zhang, D., Anraku, Y., Zou, Y., Li, J., Wu, H., et al. (2020) · Science Advances · doi:10.1126/sciadv.abc7031 · Cited by 304

Neuroprotective effects of resveratrol against β‐amyloid‐induced neurotoxicity in rat hippocampal neurons: involvement of protein kinase C

Han, Y.-S., Zheng, W., Bastianetto, S., Chabot, J., & Quirion, R. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705688 · Cited by 300

Tau induces blood vessel abnormalities and angiogenesis-related gene expression in P301L transgenic mice and human Alzheimer’s disease

Bennett, R. E., Robbins, A. B., Hu, M., Cao, X., Betensky, R. A., Clark, T., Das, S., & Hyman, B. T. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710329115 · Cited by 299

Passive Amyloid Immunotherapy Clears Amyloid and Transiently Activates Microglia in a Transgenic Mouse Model of Amyloid Deposition

Wilcock, D. M., Rojiani, A. M., Rosenthal, A., Levkowitz, G., Subbarao, S., Alamed, J., Wilson, D. H., Wilson, N., Freeman, M. J., Gordon, M. N., et al. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1090-04.2004 · Cited by 302

Hippocampal T cell infiltration promotes neuroinflammation and cognitive decline in a mouse model of tauopathy

Laurent, C., Dorothée, G., Hunot, S., Martin, E., Monnet, Y., Duchamp, M., Dong, Y., Légeron, F.-P., Leboucher, A., Burnouf, S., et al. (2017) · Brain · doi:10.1093/brain/aww270 · Cited by 303

Microglia–Neuron Communication in Epilepsy

Eyo, U. B., Murugan, M., & Wu, L. (2016) · Glia · doi:10.1002/glia.23006 · Cited by 300

Microglia in Alzheimer Disease: Well-Known Targets and New Opportunities

Hemonnot, A.-L., Hua, J., Ulmann, L., & Hirbec, H. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00233 · Cited by 298

Chronic stress and glucocorticoids: From neuronal plasticity to neurodegeneration

Vyas, S., Rodrigues, A. J., Silva, J. M., Tronche, F., Almeida, O. F. X., Sousa, N., & Sotiropoulos, I. (2016) · Neural Plasticity · doi:10.1155/2016/6391686 · Cited by 297

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

The Potential for β-Structure in the Repeat Domain of Tau Protein Determines Aggregation, Synaptic Decay, Neuronal Loss, and Coassembly with Endogenous Tau in Inducible Mouse Models of Tauopathy

Mocanu, M.-M., Nissen, A., Eckermann, K., Khlistunova, I., Biernat, J., Drexler, D., Petrova, O., Schönig, K., Bujard, H., Mandelkow, E., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2824-07.2008 · Cited by 297

TREM2 regulates microglial cell activation in response to demyelination in vivo

Cantoni, C., Bollman, B., Licastro, D., Xie, M., Mikesell, R., Schmidt, R., Yuede, C. M., Galimberti, D., Olivecrona, G., Klein, R. S., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1388-1 · Cited by 296

Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly.

Goode, B. L., Denis, P. E., Panda, D., Radeke, M. J., Miller, H. P., Wilson, L., & Feinstein, S. C. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.2.353 · Cited by 296

Changes in brain oxysterols at different stages of Alzheimer’s disease: Their involvement in neuroinflammation

Testa, G., Staurenghi, E., Zerbinati, C., Gargiulo, S., Iuliano, L., Giaccone, G., Fantò, F., Poli, G., Leonarduzzi, G., & Gamba, P. (2016) · Redox Biology · doi:10.1016/j.redox.2016.09.001 · Cited by 270

Axonal injury: a universal consequence of fatal closed head injury?

Gentleman, S. M., Roberts, G. W., Gennarelli, T. A., Maxwell, W. L., Adams, J. H., Kerr, S., & Graham, D. I. (1995) · Acta Neuropathologica · doi:10.1007/bf00571509 · Cited by 296

Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models

Wan, Y.-W., Al-Ouran, R., Mangleburg, C. G., Perumal, T. M., Lee, T. V., Allison, K., Swarup, V., Funk, C. C., Gaiteri, C., Allen, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107908 · Cited by 295

When Immune Cells Turn Bad—Tumor-Associated Microglia/Macrophages in Glioma

Roesch, S., Rapp, C., Dettling, S., & Herold‐Mende, C. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020436 · Cited by 305

Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids

Scheres, S. H. W., Falcon, B., & Goedert, M. (2023) · Nature · doi:10.1038/s41586-023-06437-2 · Cited by 308

Presynaptic dystrophic neurites surrounding amyloid plaques are sites of microtubule disruption, BACE1 elevation, and increased Aβ generation in Alzheimer’s disease

Sadleir, K. R., Kandalepas, P. C., Buggia-Prévot, V., Nicholson, D. A., Thinakaran, G., & Vassar, R. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1558-9 · Cited by 294

PERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia

Radford, H. E., Moreno, J. A., Verity, N., Halliday, M., & Mallucci, G. R. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1487-z · Cited by 290

Blood–brain barrier impairment in Alzheimer disease

Bowman, G. L., Kaye, J. A., Moore, M., Waichunas, D., Carlson, N. E., & Quinn, J. F. (2007) · Neurology · doi:10.1212/01.wnl.0000262031.18018.1a · Cited by 294

Link between type 2 diabetes and Alzheimer’s disease: from epidemiology to mechanism and treatment

Li, X., Leng, S. X., & Song, D. (2015) · Clinical Interventions in Aging · doi:10.2147/cia.s74042 · Cited by 314

Amyloid-β peptide levels in brain are inversely correlated with insulysin activity levels in vivo

Miller, B. C., Eckman, E. A., Sambamurti, K., Dobbs, N., Chow, K. M., Eckman, C. B., Hersh, L. B., & Thiele, D. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031520100 · Cited by 294

A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration

Walsh, D. M., & Selkoe, D. J. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.13 · Cited by 301

Repurposed drugs targeting eIF2α-P-mediated translational repression prevent neurodegeneration in mice

Halliday, M., Radford, H., Zents, K. A. M., Molloy, C., Moreno, J. A., Verity, N. C., Smith, E., Ortori, C. A., Barrett, D. A., Bushell, M., et al. (2017) · Brain · doi:10.1093/brain/awx074 · Cited by 293

Missorting of Tau in Neurons Causes Degeneration of Synapses That Can Be Rescued by the Kinase MARK2/Par-1

Thies, E., & Mandelkow, E.-M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4674-06.2007 · Cited by 293

Tau Pathology in Two Dutch Families with Mutations in the Microtubule-Binding Region of Tau

Spillantini, M. G., Crowther, R. A., Kamphorst, W., Heutink, P., & Swieten, J. C. V. (1998) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65721-5 · Cited by 293

Clinicopathologic Correlations in a Large Alzheimer Disease Center Autopsy Cohort: Neuritic Plaques and Neurofibrillary Tangles "Do Count" When Staging Disease Severity

Nelson, P. T., Jicha, G. A., Schmitt, F. A., Liu, H., Davis, D. G., Mendiondo, M. S., Abner, E. L., & Markesbery, W. R. (2007) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/nen.0b013e31815c5efb · Cited by 292

Alzheimer’s-related endosome dysfunction in Down syndrome is Aβ-independent but requires APP and is reversed by BACE-1 inhibition

Jiang, Y., Mullaney, K. A., Peterhoff, C. M., Che, S., Schmidt, S. D., Boyer‐Boiteau, A., Ginsberg, S. D., Cataldo, A. M., Mathews, P. M., & Nixon, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908953107 · Cited by 293

Role of Microglia TLRs in Neurodegeneration

Fiebich, B. L., Batista, C. R. A., Saliba, S. W., Yousif, N. M., & de Oliveira, A. C. P. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00329 · Cited by 291

Activation of c-Jun N-Terminal Kinase and p38 in an Alzheimer's Disease Model Is Associated with Amyloid Deposition

Savage, M. J., Lin, Y.-G., Ciallella, J. R., Flood, D. G., & Scott, R. W. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-09-03376.2002 · Cited by 291

Hyperphosphorylated tau in patients with refractory epilepsy correlates with cognitive decline: a study of temporal lobe resections.

Tai, X. Y., Koepp, M., Duncan, J. S., Fox, N., Thompson, P., Baxendale, S., Liu, J. Y. W., Reeves, C., Michalak, Z., & Thom, M. (2016) · Brain · doi:10.1093/brain/aww187 · Cited by 291

Targeting protein kinases in central nervous system disorders

Chico, L. K., Eldik, L. J. V., & Watterson, D. M. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2999 · Cited by 298

Desmin-related cardiomyopathy in transgenic mice: A cardiac amyloidosis

Sanbe, A., Osińska, H. E., Saffitz, J. E., Glabe, C. G., Kayed, R., Maloyan, A., & Robbins, J. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401900101 · Cited by 291

Alpha-synuclein and tau: teammates in neurodegeneration?

Moussaud, S., Jones, D. R., Moussaud-Lamodière, E. L., Delenclos, M., Ross, O. A., & McLean, P. J. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-43 · Cited by 301

Monoaminergic neuropathology in Alzheimer’s disease

Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.04.001 · Cited by 297

A walk through tau therapeutic strategies

Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 299

Alzheimer Disease Pathogenesis: Insights From Molecular and Cellular Biology Studies of Oligomeric Aβ and Tau Species

Chen, X., & Mobley, W. C. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00659 · Cited by 302

Beta-amyloid deposition in chronic traumatic encephalopathy

Stein, T. D., Montenigro, P. H., Alvarez, V. E., Xia, W., Crary, J. F., Tripodis, Y., Daneshvar, D. H., Mez, J., Solomon, T., Meng, G., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1435-y · Cited by 291

BACE1 gene deletion prevents neuron loss and memory deficits in 5XFAD APP/PS1 transgenic mice

Ohno, M., Cole, S. L., Yasvoina, M., Zhao, J., Citron, M., Berry, R., Disterhoft, J. F., & Vassar, R. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.12.008 · Cited by 290

Defective Neuromuscular Synapses in Mice Lacking Amyloid Precursor Protein (APP) and APP-Like Protein 2

Wang, P., Yang, G., Mosier, D. R., Chang, P., Zaidi, T., Gong, Y.-D., Zhao, N.-M., Dominguez, B., Lee, K.-F., Gan, W.-B., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4660-04.2005 · Cited by 290

Oxidative damage in neurodegeneration: roles in the pathogenesis and progression of Alzheimer disease

Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 322

Aging in Down Syndrome and the Development of Alzheimer's Disease Neuropathology

Head, E., T. Lott, I., M. Wilcock, D., & A. Lemere, C. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666151020114607 · Cited by 289

Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation

Ruggeri, F. S., Longo, G., Faggiano, S., Lipiec, E. W., Pastore, A., & Dietler, G. (2015) · Nature Communications · doi:10.1038/ncomms8831 · Cited by 288

Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer’s disease.

Zhang, Z., Song, M., Liu, X., Su Kang, S., Duong, D. M., Seyfried, N. T., Cao, X., Cheng, L., Sun, Y. E., Ping Yu, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9762 · Cited by 277

Sodium rutin ameliorates Alzheimer’s disease–like pathology by enhancing microglial amyloid-β clearance

Pan, R., Ma, J., Kong, X.-X., Wang, X., Li, S., Qi, X., Yan, Y., Cheng, J., Liu, Q., Jin, W., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau6328 · Cited by 293

Certain Inhibitors of Synthetic Amyloid β-Peptide (Aβ) Fibrillogenesis Block Oligomerization of Natural Aβ and Thereby Rescue Long-Term Potentiation

Walsh, D. M., Townsend, M., Podlisny, M. B., Shankar, G. M., Fadeeva, J. V., El‐Agnaf, O. M. A., Hartley, D. M., & Selkoe, D. J. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4391-04.2005 · Cited by 295

Age-Dependent Neurodegeneration and Alzheimer-Amyloid Plaque Formation in Transgenic Drosophila

Greeve, I., Kretzschmar, D., Tschäpe, J., Beyn, A., Brellinger, C., Schweizer, M., Nitsch, R. M., & Reifegerste, R. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0283-04.2004 · Cited by 293

Anthocyanins Reversed D-Galactose-Induced Oxidative Stress and Neuroinflammation Mediated Cognitive Impairment in Adult Rats

Rehman, S. U., Shah, S. A., Ali, T., Chung, J. I., & Kim, M. O. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9604-5 · Cited by 290

The role of microglia in processing and spreading of bioactive tau seeds in Alzheimer’s disease

Hopp, S. C., Lin, Y., Oakley, D., Roe, A. D., DeVos, S. L., Hanlon, D., & Hyman, B. T. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1309-z · Cited by 286

Timing-Dependent Septal Cholinergic Induction of Dynamic Hippocampal Synaptic Plasticity

Gu, Z., & Yakel, J. L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.026 · Cited by 287

Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape

Miller, Y., Ma, B., & Nussinov, R. (2010) · Chemical Reviews · doi:10.1021/cr900377t · Cited by 288

Advances in developing novel therapeutic strategies for Alzheimer’s disease

Cao, J., Hou, J., Ping, J., & Cai, D. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0299-8 · Cited by 283

Immunotherapeutic Approaches for Alzheimer’s Disease

Wisniewski, T., & Goñi, F. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.064 · Cited by 284

Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer’s disease models

van Eersel, J., Ke, Y. D., Liu, X., Delerue, F., Kril, J. J., Götz, J., & Ittner, L. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009038107 · Cited by 284

Progressive inflammation‐mediated neurodegeneration after traumatic brain or spinal cord injury

Faden, A. I., Wu, J., Stoica, B. A., & Loane, D. J. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13179 · Cited by 299

Beta‐amyloid 1‐42 monomers, but not oligomers, produce PHF ‐like conformation of Tau protein

Manassero, G., Guglielmotto, M., Zamfir, R. I., Borghi, R., Colombo, L., Salmona, M., Perry, G. L., Odetti, P. R., Arancio, O., Tamagno, E., et al. (2016) · Aging Cell · doi:10.1111/acel.12500 · Cited by 32

Antibodies against β‐amyloid reduce aβ oligomers, glycogen synthase kinase‐3β activation and τ phosphorylation in vivo and in vitro

Ma, Q., Lim, G. P., Harris‐White, M. E., Yang, F., Ambegaokar, S. S., Ubeda, O. J., Glabe, C. G., Teter, B., Frautschy, S. A., & Cole, G. M. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20734 · Cited by 126

O4‐05‐01: Intraneuronal accumulation of Aβ oligomers causes abnormal tau phosphorylation, glial activation and neuronal loss in transgenic mice with APP E693Δ mutation

Tomiyama, T., Umeda, T., Sakama, N., Lambert, M. P., Klein, W. L., & Mori, H. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.488

Amyloid β accelerates phosphorylation of tau and neurofibrillary tangle formation in an amyloid precursor protein and tau double‐transgenic mouse model

Seino, Y., Kawarabayashi, T., Wakasaya, Y., Watanabe, M., Takamura, A., Yamamoto‐Watanabe, Y., Kurata, T., Abe, K., Ikeda, M., Westaway, D. A., et al. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22516 · Cited by 31

ER stress is involved in Aβ‐induced GSK‐3β activation and tau phosphorylation

Resende, R., Ferreiro, E. B., Pereira, C., & Oliveira, C. R. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21648 · Cited by 142