Neurodegenerative Tauopathies

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, 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

Prions

Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice

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

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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 protein factor essential for microtubule assembly

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Amyloid deposition as the central event in the aetiology of Alzheimer’s disease

Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538

Clinical research criteria for the diagnosis of progressive supranuclear palsy (Steele-Richardson-Olszewski syndrome): Report of the NINDS-SPSP International Workshop*

Litvan, I., Agid, Y., Calne, D., Campbell, G., Dubois, B., Duvoisin, R. C., Goetz, C. G., Golbe, L. I., Grafman, J., Growdon, J. H., et al. (1996) · Neurology · doi:10.1212/wnl.47.1.1 · Cited by 2,538

Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein

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Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492

Cell-Mediated Neuroprotection in a Mouse Model of Human Tauopathy

Hampton, D. W., Webber, D. J., Bilican, B., Goedert, M., Spillantini, M. G., & Chandran, S. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0834-10.2010 · Cited by 127

The Role of the Lipid Bilayer in Tau Aggregation

Elbaum‐Garfinkle, S., Ramlall, T. F., & Rhoades, E. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.03.013 · Cited by 127

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

Tau Phosphorylation, Tangles, and Neurodegeneration

Geschwind, D. H. (2003) · Neuron · doi:10.1016/s0896-6273(03)00681-0 · Cited by 129

Protein phosphatase 2A methylation: a link between elevated plasma homocysteine and Alzheimer's Disease

Vafai, S. B., & Stock, J. B. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02702-3 · Cited by 129

Hyperphosphorylated tau in parahippocampal cortex impairs place learning in aged mice expressing wild‐type human tau

Kimura, T., Yamashita, S., Fukuda, T., Park, J., Murayama, M., Mizoroki, T., Yoshiike, Y., Sahara, N., & Takashima, A. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601917 · Cited by 144

Genetic markers for diagnosis and pathogenesis of Alzheimer's disease

Kim, D., Yeo, S. H., Park, J.-M., Choi, J. Y., Lee, T.-H., Park, S. Y., Ock, M. S., Eo, J., Kim, H., & Cha, H. (2014) · Gene · doi:10.1016/j.gene.2014.05.031 · Cited by 133

Polyphenols Beyond Barriers: A Glimpse into the Brain

Figueira, I., Menezes, R., Macedo, D., Costa, I., & dos Santos, C. N. (2016) · Current Neuropharmacology · doi:10.2174/1570159x14666161026151545 · Cited by 134

Alternative polyadenylation and miR‐34 family members regulate tau expression

Dickson, J. R., Kruse, C., Montagna, D. R., Finsen, B. R., & Wolfe, M. S. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12437 · Cited by 128

Axonal Degeneration Induced by Targeted Expression of Mutant Human Tau in Oligodendrocytes of Transgenic Mice That Model Glial Tauopathies

Higuchi, M., Zhang, B., Forman, M. S., Yoshiyama, Y., Trojanowski, J. Q., & Lee, V. M. ‐. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2691-05.2005 · Cited by 133

TFEB regulates lysosomal exocytosis of tau and its loss of function exacerbates tau pathology and spreading

Xu, Y., Du, S., Marsh, J. A., Horie, K., Sato, C., Ballabio, A., Karch, C. M. M., Holtzman, D. M., & Zheng, H. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0738-0 · Cited by 124

Assembly of tau in transgenic animals expressing P301L tau: alteration of phosphorylation and solubility

Sahara, N., Lewis, J. M., Deture, M. A., McGowan, E. M., Dickson, D. W., Hutton, M., & Yen, S.-H. C. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01241.x · Cited by 127

Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations

Liu, Q., Smith, M. A., Ávila, J., DeBernardis, J. F., Kansal, M. M., Takeda, A., Zhu, X., Nunomura, A., Honda, K., Moreira, P. I., et al. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.005 · Cited by 129

Nucleation-dependent Tau Filament Formation

Congdon, E. E., Kim, S., Bonchak, J., Songrug, T., Anastasios Matzavinos, A., & Kuret, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800247200 · Cited by 126

U‐box protein carboxyl terminus of Hsc70‐interacting protein (CHIP) mediates poly‐ubiquitylation preferentially on four‐repeat Tau and is involved in neurodegeneration of tauopathy

Hatakeyama, S., Matsumoto, M., Kamura, T., Murayama, M., Chui, D.-H., Planel, E., Takahashi, R., Nakayama, K. I., & Takashima, A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02713.x · Cited by 127

Obesity, leptin, and Alzheimer's disease

Lee, E. B. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06274.x · Cited by 126

General aspects of neurodegeneration

Jellinger, K. A. (2003) · Journal of Neural Transmission. Supplementa · doi:10.1007/978-3-7091-0643-3_7 · Cited by 126

Pathophysiological importance of aggregated damaged proteins

Höhn, A., Jung, T., & Grune, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.028 · Cited by 130

White Matter Tauopathy With Globular Glial Inclusions: A Distinct Sporadic Frontotemporal Lobar Degeneration

Kovács, G. G., Majtényi, K., Spina, S., Murrell, J. R., Gelpí, E., Höftberger, R., Fraser, G. M., Crowther, R. A., Goedert, M., Budka, H., et al. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318187a80f · Cited by 130

Acetylated Tau Neuropathology in Sporadic and Hereditary Tauopathies

Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., McCarty-Wood, E., Van Deerlin, V. M., Lee, V. M.-Y., & Trojanowski, J. Q. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.04.025 · Cited by 125

Sex difference in pathology and memory decline in rTg4510 mouse model of tauopathy

Yue, M., Hanna, A., Wilson, J., Roder, H. M., & Janus, C. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.04.006 · Cited by 125

Rifampicin is a candidate preventive medicine against amyloid-β and tau oligomers

Umeda, T., Ono, K., Sakai, A., Yamashita, M., Mizuguchi, M., Klein, W. L., Yamada, M., Mori, H., & Tomiyama, T. (2016) · Brain · doi:10.1093/brain/aww042 · Cited by 124

1,2,4-Triazolo[1,5-a]pyrimidines in drug design

Oukoloff, K., Lucero, B., Francisco, K. R., Brunden, K. R., & Ballatore, C. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.01.027 · Cited by 125

Evidence that Non-Fibrillar Tau Causes Pathology Linked to Neurodegeneration and Behavioral Impairments

Brunden, K. R., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14406 · Cited by 125

Drosophila models of neurodegenerative disease

Sang, T., & Jackson, G. R. (2005) · NeuroRx · doi:10.1602/neurorx.2.3.438 · Cited by 128

Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau

Lin, W.-L., Lewis, J. M., Yen, S.-H. C., Hutton, M. L., & Dickson, D. W. (2003) · Journal of Neurocytology · doi:10.1023/b:neur.0000021904.61387.95 · Cited by 125

Genetic zebrafish models of neurodegenerative diseases

Bandmann, O., & Burton, E. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.017 · Cited by 125

Mutations in the tau gene that cause an increase in three repeat tau and frontotemporal dementia

Stanford, P. M. (2003) · Brain · doi:10.1093/brain/awg090 · Cited by 125

Magnetic resonance imaging-based volumetry differentiates progressive supranuclear palsy from corticobasal degeneration

Gröschel, K., Hauser, T.-K., Luft, A., Patronas, N., Dichgans, J., Litvan, I., & Schulz, J. B. (2004) · NeuroImage · doi:10.1016/j.neuroimage.2003.09.070 · Cited by 125

Microglia in Alzheimer’s Disease in the Context of Tau Pathology

Perea, J. R., Bolós, M., & Ávila, J. (2020) · Biomolecules · doi:10.3390/biom10101439 · Cited by 134

Infectious agents and Alzheimer's disease

Piekut, T., Hurła, M., Banaszek, N., Szejn, P., Dorszewska, J., Kozubski, W., & Prendecki, M. (2022) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2102073 · Cited by 123

Tau: It’s Not What You Think

Baas, P. W., & Qiang, L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.007 · Cited by 123

Multiplex SILAC Analysis of a Cellular TDP-43 Proteinopathy Model Reveals Protein Inclusions Associated with SUMOylation and Diverse Polyubiquitin Chains

Seyfried, N. T., Gozal, Y. M., Dammer, E. B., Xia, Q., Duong, D. M., Cheng, D., Lah, J. J., Levey, A. I., & Peng, J. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800390-mcp200 · Cited by 127

Trends in the Molecular Pathogenesis and Clinical Therapeutics of Common Neurodegenerative Disorders

Choonara, Y. E., Pillay, V., du Toit, L. C., Modi, G., Naidoo, D., Ndesendo, V. M. K., & Sibambo, S. R. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10062510 · Cited by 126

Analysis of Tau Phosphorylation and Truncation in a Mouse Model of Human Tauopathy

Delobel, P., Lavenir, I., Fraser, G. M., Ingram, E., Holzer, M., Ghetti, B. F., Spillantini, M. G., Crowther, R. A., & Goedert, M. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070627 · Cited by 124

α-Internexin Is Present in the Pathological Inclusions of Neuronal Intermediate Filament Inclusion Disease

Cairns, N. J., Zhukareva, V. A., Uryu, K., Zhang, B., Bigio, E. H., Mackenzie, I. R., Gearing, M., Duyckaerts, C. J., Yokoo, H., Nakazato, Y., et al. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63773-x · Cited by 123

Genetic Correction of Tauopathy Phenotypes in Neurons Derived from Human Induced Pluripotent Stem Cells

Fong, H., Wang, C., Knoferle, J., Walker, D., Balestra, M. E., Tong, L. M., Leung, L., Ring, K. L., Seeley, W. W., Karydas, A., et al. (2013) · Stem Cell Reports · doi:10.1016/j.stemcr.2013.08.001 · Cited by 122

Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets

Lee, V. M.-Y., Brunden, K. R., Hutton, M., & Trojanowski, J. Q. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006437 · Cited by 122

Phosphorus Dendrimers Affect Alzheimer’s (Aβ1–28) Peptide and MAP-Tau Protein Aggregation

Wasiak, T., Йонов, М., Nieznański, K., Nieznańska, H., Klementieva, O. L., Granell, M., Cladera, J., Majoral, J., Caminade, A., & Klajnert‐Maculewicz, B. (2011) · Molecular Pharmaceutics · doi:10.1021/mp2005627 · Cited by 125

An overview of concussion in sport

Khurana, V. G., & Kaye, A. H. (2011) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2011.08.002 · Cited by 140

The behavioural and neuropathologic sexual dimorphism and absence of MIP-3α in tau P301S mouse model of Alzheimer’s disease

Sun, Y., Guo, Y., Feng, X., Jia, M., Ai, N., Dong, Y., Zheng, Y., Fu, L., Yu, B., Zhang, H., et al. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01749-w · Cited by 122

Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions

Chee, F. C., Mudher, A. K., Cuttle, M. F., Newman, T. A., Mackay, D., Lovestone, S., & Shepherd, D. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.05.029 · Cited by 119

Knock-out and transgenic mouse models of tauopathies

Denk, F., & Wade‐Martins, R. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.05.010 · Cited by 128

Expression of the Small Heat-Shock Protein αB-Crystallin in Tauopathies with Glial Pathology

Dabir, D. V., Trojanowski, J. Q., Richter‐Landsberg, C., Lee, V. M. ‐., & Forman, M. S. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63106-9 · Cited by 120

Disease-Modifying Therapies for Alzheimer’s Disease: More Questions than Answers

Golde, T. E. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01201-2 · Cited by 119

New perspectives on the role of tau in Alzheimer's disease. Implications for therapy

Medina, M., & Ávila, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.013 · Cited by 123

LRRK2 Kinase Regulates Synaptic Morphology through Distinct Substrates at the Presynaptic and Postsynaptic Compartments of theDrosophilaNeuromuscular Junction

Lee, S., Liu, H., Lin, W., Guo, H.-F., & Lu, B. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1807-10.2010 · Cited by 117

Tau Binds to Lipid Membrane Surfaces via Short Amphipathic Helices Located in Its Microtubule-Binding Repeats

Georgieva, E. R., Xiao, S., Borbat, P. P., Freed, J. H., & Eliezer, D. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.07.046 · Cited by 124

The Human Tau Interactome: Binding to the Ribonucleoproteome, and Impaired Binding of the Proline-to-Leucine Mutant at Position 301 (P301L) to Chaperones and the Proteasome

Gunawardana, C. G., Mehrabian, M., Wang, X., Mueller, I., Lubambo, I., Jonkman, J. E. N., Wang, H., & Schmitt‐Ulms, G. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.050724 · Cited by 127

Hyperphosphorylated tau mediates neuronal death by inducing necroptosis and inflammation in Alzheimer’s disease

Dong, Y., Yu, H., Li, X., Bian, K., Zheng, Y., Dai, M., Feng, X., Sun, Y., He, Y. T., Yu, B., et al. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02567-y · Cited by 127

Chronic lithium treatment decreases tau lesions by promoting ubiquitination in a mouse model of tauopathies

Nakashima, H., Ishihara, T., Suguimoto, S. P., Yokota, O., Oshima, E., Kugo, A., Terada, S., Hamamura, T., Trojanowski, J. Q., Lee, V. M. ‐., et al. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1087-4 · Cited by 119

Genomic features defining exonic variants that modulate splicing

Woolfe, A., Mullikin, J. C., & Elnitski, L. L. (2010) · Genome biology · doi:10.1186/gb-2010-11-2-r20 · Cited by 119

Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders

Layfield, R., Cavey, J. R., & Lowe, J. S. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(03)00025-4 · Cited by 118

Increased basal ganglia binding of 18F‐AV‐1451 in patients with progressive supranuclear palsy

Smith, R., Schain, M., Nilsson, C., Strandberg, O., Olsson, T., Hägerström, D., Jögi, J., Borroni, E., Schöll, M., Honer, M., et al. (2017) · Movement Disorders · doi:10.1002/mds.26813 · Cited by 118

Is synaptic loss a unique hallmark of Alzheimer’s disease?

Scheff, S. W., Neltner, J. H., & Nelson, P. T. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.028 · Cited by 118

ApoE4 induces Aβ42, tau, and neuronal pathology in the hippocampus of young targeted replacement apoE4 mice

Liraz, O., Boehm-Cagan, A., & Michaelson, D. M. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-16 · Cited by 118

Association between cerebrospinal fluid and plasma neurodegeneration biomarkers with brain atrophy in Alzheimer's disease

Pereira, J. B., Westman, E., & Hansson, O. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.06.002 · Cited by 120

Modeling neurodegenerative diseases in Caenorhabditis elegans

Li, J., & Le, W. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.09.024 · Cited by 125

Synapses and Dendritic Spines as Pathogenic Targets in Alzheimer’s Disease

Yu, W., & Lu, B. (2012) · Neural Plasticity · doi:10.1155/2012/247150 · Cited by 123

Neural stem cells transplantation in cortex in a mouse model of Alzheimer’s disease

Wang, Q., Matsumoto, Y., Shindo, T., Miyake, K., Shindo, A., Kawanishi, M., Kawai, N., Tamiya, T., & Nagao, S. (2006) · The Journal of Medical Investigation · doi:10.2152/jmi.53.61 · Cited by 118

Disease modifying therapy for AD?1

Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117

Alzheimer disease

Nussbaum, J. M., Seward, M. E., & Bloom, G. S. (2013) · Prion · doi:10.4161/pri.22118 · Cited by 128

Protein Semisynthesis Provides Access to Tau Disease-Associated Post-translational Modifications (PTMs) and Paves the Way to Deciphering the Tau PTM Code in Health and Diseased States

Haj‐Yahya, M., & Lashuel, H. A. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b02668 · Cited by 118

Evidence for two distinct binding sites for tau on microtubules

Makrides, V., Massie, M. R., Feinstein, S. C., & Lew, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400992101 · Cited by 117

A mutation affecting the sodium/proton exchanger, SLC9A6, causes mental retardation with tau deposition

Garbern, J. Y., Neumann, M., Trojanowski, J. Q., Lee, V. M. ‐., Feldman, G. L., Norris, J. W., Friez, M. J., Schwartz, C. E., Stevenson, R. E., & Sima, A. A. F. (2010) · Brain · doi:10.1093/brain/awq071 · Cited by 117

A novel, ultrasensitive assay for tau: potential for assessing traumatic brain injury in tissues and biofluids.

Rubenstein, R., Chang, B., Davies, P., Wagner, A. K., Robertson, C. S., & Wang, K. K. W. (2015) · Journal of Neurotrauma · doi:10.1089/neu.2014.3548 · Cited by 116

Epigenetics: A novel therapeutic approach for the treatment of Alzheimer's disease

Adwan, L. I., & Zawia, N. H. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.03.010 · Cited by 118

Vitamin E and Alzheimer’s disease: what do we know so far?

Browne, D., McGuinness, B., Woodside, J. V., & McKay, G. J. (2019) · Clinical Interventions in Aging · doi:10.2147/cia.s186760 · Cited by 119

Degradation and Transmission of Tau by Autophagic-Endolysosomal Networks and Potential Therapeutic Targets for Tauopathy

Jiang, S., & Bhaskar, K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.586731 · Cited by 119

Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy

Lim, J., Balaštík, M., Lee, T. H., Nakamura, K., Liou, Y., Sun, A., Finn, G., Pastorino, L., Lee, V. M. ‐., & Lu, K. P. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34308 · Cited by 117

SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans

Guthrie, C. R., Schellenberg, G. D., & Kraemer, B. C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp099 · Cited by 116

Synchrotron X-ray Diffraction Study of Microtubules Buckling and Bundling under Osmotic Stress: A Probe of Interprotofilament Interactions

Needleman, D. J., Ojeda-López, M. A., Raviv, U., Ewert, K. K., Jones, J. B., Miller, H. P., Wilson, L., & Safinya, C. R. (2004) · Physical Review Letters · doi:10.1103/physrevlett.93.198104 · Cited by 116

Astroglia and Tau: New Perspectives

Kovacs, G. G. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00096 · Cited by 115

Tau as a therapeutic target in neurodegenerative disease

Himmelstein, D. S., Ward, S., Lancia, J. K., Patterson, K. R., & Binder, L. I. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.07.001 · Cited by 122

Progressive neurodegeneration in C. elegans model of tauopathy

Miyasaka, T., Ding, Z., Gengyo-Ando, K., Oue, M., Yamaguchi, H., Mitani, S., & Ihara, Y. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.03.017 · Cited by 115

Alternative splicing of mRNA in the molecular pathology of neurodegenerative diseases

Mills, J. D., & Janitz, M. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.10.030 · Cited by 118

The neuritic plaque facilitates pathological conversion of tau in an Alzheimer’s disease mouse model

Li, T., Braunstein, K. E., Zhang, J., Lau, A., Sibener, L., Deeble, C., & Wong, P. C. (2016) · Nature Communications · doi:10.1038/ncomms12082 · Cited by 114

Phospho-Tau Bar Code: Analysis of Phosphoisotypes of Tau and Its Application to Tauopathy

Kimura, T., Sharma, G., Ishiguro, K., & Hisanaga, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00044 · Cited by 116

Parkinson’s disease-linked D620N VPS35 knockin mice manifest tau neuropathology and dopaminergic neurodegeneration

Chen, X., Kordich, J. K., Williams, E. T., Levine, N. D., Cole-Strauss, A., Marshall, L. L., Labrie, V., Ma, J., Lipton, J. W., & Moore, D. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814909116 · Cited by 114

A non-toxic Hsp90 inhibitor protects neurons from Aβ-induced toxicity

Ansar, S., Burlison, J. A., Hadden, M. K., Yu, X. M., Desino, K. E., Bean, J. L., Neckers, L., Audus, K. L., Michaelis, M. L., & Blagg, B. S. J. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.01.017 · Cited by 114

Abnormal tau induces cognitive impairment through two different mechanisms: synaptic dysfunction and neuronal loss

Di, J., Cohen, L. S., Corbo, C. P., Phillips, G. R., Idrissi, A. E., & Alonso, A. D. C. (2016) · Scientific Reports · doi:10.1038/srep20833 · Cited by 120

Therapeutic strategies for the treatment of tauopathies: Hopes and challenges

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The role of overexpressed DYRK1A protein in the early onset of neurofibrillary degeneration in Down syndrome

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