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

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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

Tau elevations in the brain extracellular space correlate with reduced amyloid-β levels and predict adverse clinical outcomes after severe traumatic brain injury

Magnoni, S., Esparza, T. J., Conte, V., Carbonara, M., Carrabba, G. G., Holtzman, D. M., Zipfel, G. J., Stocchetti, N., & Brody, D. L. (2011) · Brain · doi:10.1093/brain/awr286 · Cited by 169

Nonhuman Primate Models of Alzheimer-Like Cerebral Proteopathy

Heuer, E., F. Rosen, R., Cintron, A., & C. Walker, L. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315885 · Cited by 169

Oleuropein and derivatives from olives as Tau aggregation inhibitors

Daccache, A., Lion, C. J., Sibille, N., Gérard, M., Slomianny, C., Lippens, G. M., & Cotelle, P. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.02.010 · Cited by 173

Molecular Neuropathology of TDP-43 Proteinopathies

Neumann, M. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10010232 · Cited by 172

Tau Mutations in Neurodegenerative Diseases

Wolfe, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800013200 · Cited by 172

LRRK2 G2019S Mutation Induces Dendrite Degeneration through Mislocalization and Phosphorylation of Tau by Recruiting Autoactivated GSK3β

Lin, C., Tsai, P.-I., Wu, R., & Chien, C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1737-10.2010 · Cited by 172

Cell‐specific blood–brain barrier regulation in health and disease: a focus on hypoxia

Engelhardt, S., Patkar, S., & Ogunshola, O. O. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12489 · Cited by 168

The β-Propensity of Tau Determines Aggregation and Synaptic Loss in Inducible Mouse Models of Tauopathy

Eckermann, K., Mocanu, M.-M., Khlistunova, I., Biernat, J., Nissen, A., Hofmann, A., Schönig, K., Bujard, H., Haemisch, A., Mandelkow, E., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705282200 · Cited by 168

Tau and Tauopathies

Lee, G. S., & Leugers, C. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00004-7 · Cited by 173

Distinct α-Synuclein strains and implications for heterogeneity among α-Synucleinopathies

Peng, C., Gathagan, R. J., & Lee, V. M. ‐. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.07.018 · Cited by 173

Association analysis of MAPT H1 haplotype and subhaplotypes in Parkinson's disease

Zabetian, C. P., Hutter, C. M., Factor, S. A., Nutt, J. G., Higgins, D. S., Griffith, A., Roberts, J. W., Leis, B. C., Kay, D. M., Yearout, D., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21157 · Cited by 165

Curcumin Inhibits Tau Aggregation and Disintegrates Preformed Tau Filaments in vitro

Rane, J. S., Bhaumik, P., & Panda, D. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170351 · Cited by 169

Biological links between traumatic brain injury and Parkinson’s disease

Delic, V., Beck, K. D., Pang, K. C. H., & Citron, B. A. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00924-7 · Cited by 165

Inhibition of O-GlcNAcase leads to elevation of O-GlcNAc tau and reduction of tauopathy and cerebrospinal fluid tau in rTg4510 mice

Hastings, N. B., Wang, X., Song, L., Butts, B. D., Grotz, D., Hargreaves, R., Fred Hess, J., Hong, K.-L. K., Huang, C. R.-R., Hyde, L., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0181-0 · Cited by 164

Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168

Transgenic mouse models of amyotrophic lateral sclerosis

Julien, J., & Križ, J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.03.006 · Cited by 162

H UMAN N EURODEGENERATIVE D ISEASE M ODELING U SING D ROSOPHILA

Bonini, N. M., & Fortini, M. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131425 · Cited by 169

Cdk5 is involved in NFT-like tauopathy induced by transient cerebral ischemia in female rats

Wen, Y., Yang, S.-H., Liu, R., Perez, E. J., Brun-Zinkernagel, A. M., Koulen, P., & Simpkins, J. W. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.011 · Cited by 162

The characterization of microtubule-stabilizing drugs as possible therapeutic agents for Alzheimer's disease and related tauopathies

Brunden, K. R., Yao, Y., Potuzak, J. S., Ferrer, N. I., Ballatore, C., James, M. J., Hogan, A. L., Trojanowski, J. Q., Smith, A. B., & Lee, V. M. ‐. (2010) · Pharmacological Research · doi:10.1016/j.phrs.2010.12.002 · Cited by 159

Intranuclear Aggregation of Mutant FUS/TLS as a Molecular Pathomechanism of Amyotrophic Lateral Sclerosis

Nomura, T., Watanabe, S., Kaneko, K., Yamanaka, K., Nukina, N., & Furukawa, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.516492 · Cited by 160

Trafficking regulation of proteins in Alzheimer’s disease

Jiang, S., Li, Y., Zhang, X., Bu, G., Xu, H., & Zhang, Y. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-6 · Cited by 164

The role of PAR-1 in regulating the polarised microtubule cytoskeleton in theDrosophilafollicular epithelium

Doerflinger, H., Benton, R., Shulman, J. M., & Johnston, D. S. (2003) · Development · doi:10.1242/dev.00616 · Cited by 168

Antioxidant Therapy in Alzheimers Disease: Theory and Practice

Aliev, G., Obrenovich, M. E., Reddy, V. P., Shenk, J. C., Moreira, P. I., Nunomura, A., Zhu, X., Smith, M. A., & Perry, G. L. (2008) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955708786369582 · Cited by 160

Parkinson's disease-linked mutations in VPS35 induce dopaminergic neurodegeneration

Tsika, E., Glauser, L., Moser, R., Fiser, A., Daniel, G., Sheerin, U.-M., Lees, A., Troncoso, J. C., Lewis, P. A., Bandopadhyay, R., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu178 · Cited by 159

Tau accumulation in the retina promotes early neuronal dysfunction and precedes brain pathology in a mouse model of Alzheimer’s disease

Chiasseu, M., Alarcón-Martínez, L., Belforte, N., Quintero, H., Dotigny, F., Destroismaisons, L., Velde, C. V., Panayi, F., Louis, C., & Polo, A. D. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0199-3 · Cited by 158

Jun NH2-terminal Kinase (JNK) Interacting Protein 1 (JIP1) Binds the Cytoplasmic Domain of the Alzheimer's β-Amyloid Precursor Protein (APP)

Scheinfeld, M. H., Roncarati, R., Vito, P., Lopez, P., Abdallah, M., & D'adamio, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108357200 · Cited by 160

Molecular motors implicated in the axonal transport of tau and α-synuclein

Utton, M. A., Noble, W. J., Hill, J. E., Anderton, B. H., & Hanger, D. P. (2005) · Journal of Cell Science · doi:10.1242/jcs.02558 · Cited by 172

Swimming against the Tide: Mobility of the Microtubule-Associated Protein Tau in Neurons

Konzack, S., Thies, E., Marx, A., Mandelkow, E., & Mandelkow�, E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0927-07.2007 · Cited by 165

Neurons associated with aggrecan-based perineuronal nets are protected against tau pathology in subcortical regions in Alzheimer's disease

Morawski, M., Brückner, G., Jäger, C., Seeger, G., & Arendt, T. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.05.022 · Cited by 156

Phosphorylated Tau Interacts with c-Jun N-terminal Kinase-interacting Protein 1 (JIP1) in Alzheimer Disease

Ittner, L. M., Ke, Y. D., & Götz, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014472 · Cited by 156

Functions of lipoprotein receptors in neurons

Beffert, U., Stolt-Bergner, P. C., & Herz, J. (2004) · Journal of Lipid Research · doi:10.1194/jlr.r300017-jlr200 · Cited by 164

Preliminary Study of Plasma Exosomal Tau as a Potential Biomarker for Chronic Traumatic Encephalopathy

Stern, R. A., Tripodis, Y., Baugh, C. M., Fritts, N. G., Martin, B. M., Chaisson, C., Cantu, R. C., Joyce, J. A., Shah, S., Ikezu, T., et al. (2016) · Journal of Alzheimer’s Disease · doi:10.3233/jad-151028 · Cited by 155

Learning and Memory Deficits Upon TAU Accumulation in Drosophila Mushroom Body NeuronsPreprint

Mershin, A., Pavlopoulos, E., Fitch, O., Braden, B. C., Nanopoulos, D. V., & Skoulakis, E. M. C. (2004) · Learning & Memory · doi:10.1101/lm.70804 · Cited by 158

Lithium and Autophagy

Motoi, Y., Shimada, K., Ishiguro, K., & Hattori, N. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500056q · Cited by 157

Tauopathy with paired helical filaments in an aged chimpanzee

Rosen, R. F., Farberg, A. S., Gearing, M., Dooyema, J., M. Long, P., Anderson, D. C., Davis‐Turak, J., Coppola, G., Geschwind, D. H., Paré, J., et al. (2008) · Journal of Comparative Neurology · doi:10.1002/cne.21744 · Cited by 153

Pharmacological inhibition of O-GlcNAcase (OGA) prevents cognitive decline and amyloid plaque formation in bigenic tau/APP mutant mice

Yuzwa, S. A., Shan, X., Jones, B. A., Zhao, G., Woodward, M. L., Li, X., Zhu, Y., McEachern, E. J., Silverman, M. A., Watson, N. V., et al. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-42 · Cited by 156

Role for glyoxalase I in Alzheimer's disease

Chen, F., Wollmer, M. A., Hoerndli, F. J., Münch, G. W., Kuhla, B., Rogaev, E. I., Tsolaki, M., Papassotiropoulos, A., & Götz, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402338101 · Cited by 151

Disease‐specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain

Fischer, D. F., de Vos, R. A. I., van Dijk, R., de Vrij, F. M. S., Proper, E. A., Sonnemans, M. A. F., Verhage, M. C., Sluijs, J. A., Hobo, B., Zouambia, M., et al. (2003) · The FASEB Journal · doi:10.1096/fj.03-0205com · Cited by 154

Atypical Progressive Supranuclear Palsy With Corticospinal Tract Degeneration

Josephs, K. A., Katsuse, O., Beccano-Kelly, D. A., Lin, W.-L., Uitti, R. J., Fujino, Y., Boeve, B. F., Hutton, M. L., Baker, M., & Dickson, D. W. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000218446.38158.61 · Cited by 152

Regulation of tau isoform expression and dementia

D’Souza, I., & Schellenberg, G. D. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.009 · Cited by 151

Increased tau Phosphorylation in Apolipoprotein E4 Transgenic Mice Is Associated with Activation of Extracellular Signal-regulated Kinase

Harris, F. M., Brecht, W. J., Xu, Q., Mahley, R. W., & Huang, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408127200 · Cited by 151

Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans

Kraemer, B. C., Burgess, J. K., Chen, J. H., Thomas, J. H., & Schellenberg, G. D. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl067 · Cited by 150

Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases

Chang, A., Xiang, X., Wang, J., Lee, C., Arakhamia, T., Simjanoska, M., Wang, C., Carlomagno, Y., Zhang, G., Dhingra, S., et al. (2022) · Cell · doi:10.1016/j.cell.2022.02.026 · Cited by 150

Sustained elevation of extracellular dopamine causes motor dysfunction and selective degeneration of striatal GABAergic neurons

Cyr, M., Beaulieu, J., Laakso, A., Sotnikova, T. D., Yao, W., Bohn, L., Gainetdinov, R. R., & Caron, M. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1831768100 · Cited by 150

Argyrophilic grain disease: A late‐onset dementia with distinctive features among tauopathies

Tolnay, M., & Clavaguera, F. (2004) · Neuropathology · doi:10.1111/j.1440-1789.2004.00591.x · Cited by 154

Identification of an Aggregation-Prone Structure of Tau

Elbaum-Garfinkle, S., & Rhoades, E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305206m · Cited by 149

The microtubule-associated tau protein has intrinsic acetyltransferase activity

Cohen, T. J., Friedmann, D., Hwang, A. W., Marmorstein, R., & Lee, V. M. Y. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2555 · Cited by 149

Signature Tau Neuropathology in Gray and White Matter of Corticobasal Degeneration

Forman, M. S., Zhukareva, V. A., Bergeron, C., Chin, S. S., Grossman, M., Clark, C. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61154-6 · Cited by 149

Transgenic Mouse Model of Tauopathies with Glial Pathology and Nervous System Degeneration

Higuchi, M., Ishihara, T., Zhang, B., Hong, M., Andreadis, A., Trojanowski, J. Q., & Lee, V. M. ‐. (2002) · Neuron · doi:10.1016/s0896-6273(02)00789-4 · Cited by 149

Truncation of CDK5 Activator p35 Induces Intensive Phosphorylation of Ser202/Thr205 of Human Tau

Hashiguchi, M., Saito, T., Hisanaga, S., & Hashiguchi, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207426200 · Cited by 149

Lysosomal Dysfunction Promotes Cleavage and Neurotoxicity of Tau In Vivo

Khurana, V., Elson‐Schwab, I., Fulga, T. A., Sharp, K. A., Loewen, C. A., Mulkearns-Hubert, E. E., Tyynelä, J., Scherzer, C. R., & Feany, M. Β. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001026 · Cited by 152

A Genomic Screen for Modifiers of Tauopathy Identifies Puromycin-Sensitive Aminopeptidase as an Inhibitor of Tau-Induced Neurodegeneration

Karsten, S. L., Sang, T.-K., Gehman, L. T., Chatterjee, S., Liu, J., Lawless, G. M., Sengupta, S., Berry, R. W., Pomakian, J., Oh, H. S., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.019 · Cited by 147

Hyperphosphorylation and Cleavage at D421 Enhance Tau Secretion

Plouffe, V., Mohamed, N., Rivest‐McGraw, J., Bertrand, J., Lauzon, M., & Leclerc, N. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036873 · Cited by 159

From Alzheimer to Huntington: why is a structural understanding so difficult?

Temussi, P. A., Masino, L., & Pastore, A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg044 · Cited by 147

Plaques, Tangles, and Memory Loss in Mouse Models of Neurodegeneration

Eriksen, J. L., & Janus, C. G. (2007) · Behavior Genetics · doi:10.1007/s10519-006-9118-z · Cited by 146

Interaction of Tau Protein with Model Lipid Membranes Induces Tau Structural Compaction and Membrane Disruption

Jones, E. M., Dubey, M. K., Camp, P. J., Vernon, B. C., Biernat, J., Mandelkow�, E., Majewski, J. P., & Chi, E. Y. (2012) · Biochemistry · doi:10.1021/bi201857v · Cited by 149

Is aging part of Alzheimer's disease, or is Alzheimer's disease part of aging?

Swerdlow, R. H. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.021 · Cited by 154

Discovery of MK-8719, a Potent O-GlcNAcase Inhibitor as a Potential Treatment for Tauopathies

Selnick, H. G., Hess, J. F., Tang, C., Liu, K., Schachter, J. B., Ballard, J. E., Marcus, J., Klein, D. J., Wang, X., Pearson, M. S., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01090 · Cited by 144

Aminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation

Crowe, A., James, M. J., Lee, V. M.-Y., Smith, A. B., Trojanowski, J. Q., Ballatore, C., & Brunden, K. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.436006 · Cited by 143

Templated misfolding of Tau by prion-like seeding along neuronal connections impairs neuronal network function and associated behavioral outcomes in Tau transgenic mice

Stancu, I.-C., Vasconcelos, B., Ris, L., Wang, P., Villers, A., Peeraer, E., Buist, A., Terwel, D., Baatsen, P., Oyelami, T., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1413-4 · Cited by 143

Inhibition and Modulation of γ-Secretase for Alzheimer's Disease

Wolfe, M. S. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.010 · Cited by 146

Tau‐tubulin kinase 1 (TTBK1), a neuron‐specific tau kinase candidate, is involved in tau phosphorylation and aggregation

Sato, S., Cerny, R. L., Buescher, J. L., & Ikezu, T. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04059.x · Cited by 143

Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells

Gómez‐Ramos, A., Díaz‐Nido, J., Smith, M. A., Perry, G. L., & Ávila, J. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10525 · Cited by 146

Loss of Axonal Mitochondria Promotes Tau-Mediated Neurodegeneration and Alzheimer's Disease–Related Tau Phosphorylation Via PAR-1

Iijima-Ando, K., Sekiya, M., Maruko-Otake, A., Ohtake, Y., Suzuki, E., Lu, B., & Iijima, K. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002918 · Cited by 142

The role of tau phosphorylation and cleavage in neuronal cell death

Chun, W. (2006) · Frontiers in bioscience · doi:10.2741/2097 · Cited by 144

Amyloid‐induced neurofibrillary tangle formation in Alzheimer's disease: insight from transgenic mouse and tissue‐culture models

Götz, J., Schild, A., Hoerndli, F. J., & Pennanen, L. (2004) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2004.07.013 · Cited by 146

Autosomal dominant VCP hypomorph mutation impairs disaggregation of PHF-tau

Darwich, N. F., Phan, J. M., Kim, B., Suh, E. R., Papatriantafyllou, J. D., Changolkar, L. N., Nguyen, A. T., O’Rourke, C. M., He, Z., Porta, S., et al. (2020) · Science · doi:10.1126/science.aay8826 · Cited by 132

Surface-decoration of Microtubules by Human Tau

Santarella, R. A., Skiniotis, G., Goldie, K. N., Tittmann, P., Gross, H., Mandelkow, E., Mandelkow, E., & Hoenger, A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.008 · Cited by 141

A role for FKBP52 in tau protein function

Chambraud, B., Sardin, E., Giustiniani, J., Dounane, O., Schumacher, M., Goedert, M., & Baulieu, E.-E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914957107 · Cited by 140

Proteolytic processing of tau

Wang, Y., Garg, S., Mandelkow, E., & Mandelkow�, E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380955 · Cited by 145

Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies

Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815357 · Cited by 124

A comparison of amyloid fibrillogenesis using the novel fluorescent compound K114

Crystal, A., Giasson, B. I., Crowe, A., Kung, M., Zhuang, Z., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01949.x · Cited by 138

Discovery of AZD3839, a Potent and Selective BACE1 Inhibitor Clinical Candidate for the Treatment of Alzheimer Disease

Jeppsson, F., Eketjäll, S., Janson, J., Karlström, S., Gustavsson, S., Olsson, L., Radesäter, A., Ploeger, B. A., Cebers, G., Kolmodin, K., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.409110 · Cited by 138

Behavioral deficit, oxidative stress, and mitochondrial dysfunction precede tau pathology in P301S transgenic mice

Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N. N., Yang, L., Starkov, A. A., & Beal, F. M. (2011) · The FASEB Journal · doi:10.1096/fj.11-186650 · Cited by 139

Tau Nitration Occurs at Tyrosine 29 in the Fibrillar Lesions of Alzheimer's Disease and Other Tauopathies

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

Astrocytes in mouse models of tauopathies acquire early deficits and lose neurosupportive functions

Sidoryk‐Wȩgrzynowicz, M., Gerber, Y. N., Ries, M., Sastre, M., Tolkovsky, A. M., & Spillantini, M. G. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0478-9 · Cited by 137

Tau PET Imaging in Neurodegenerative Disorders

Groot, C., Villeneuve, S., Smith, R., Hansson, O., & Ossenkoppele, R. (2022) · Journal of Nuclear Medicine · doi:10.2967/jnumed.121.263196 · Cited by 137

Transgenic animal models of tauopathies

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