Role of tau protein in Alzheimer’s disease: The prime pathological player

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

FKBP12‐rapamycin target TOR2 is a vacuolar protein with an associated phosphatidylinositol‐4 kinase activity.

Cardenas, M. E., & Heitman, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00277.x · Cited by 117

DNAJC5 facilitates USP19-dependent unconventional secretion of misfolded cytosolic proteins

Xu, Y., Cui, L., DiBello, A., Wang, L., Lee, J., Saidi, L. F., Lee, J., & Ye, Y. (2018) · Cell Discovery · doi:10.1038/s41421-018-0012-7 · Cited by 117

Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product, 4‐hydroxy‐2‐nonenal

Pérez, M., Cuadros, R., Smith, M. A., Perry, G. L., & Ávila, J. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02323-1 · Cited by 116

Tau Polymerization: Role of the Amino Terminus

Gamblin, T. C., Berry, R. W., & Binder, L. I. (2003) · Biochemistry · doi:10.1021/bi0272510 · Cited by 116

F-BAR Proteins of the Syndapin Family Shape the Plasma Membrane and Are Crucial for Neuromorphogenesis

Dharmalingam, E., Haeckel, A., Pinyol, R., Schwintzer, L., Koch, D. C., Kessels, M. M., & Qualmann, B. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3973-09.2009 · Cited by 115

Tau-knockout mice show reduced GSK3-induced hippocampal degeneration and learning deficits

de Barreda, E. G., Pérez, M., Gómez‐Ramos, P., de Cristóbal, J., Martín-Maestro, P., Morán, A., Dawson, H. N., Vitek, M. P., Lucas, J. J., Hernández, F., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.11.017 · Cited by 113

Internalization mechanisms of brain-derived tau oligomers from patients with Alzheimer’s disease, progressive supranuclear palsy and dementia with Lewy bodies

Puangmalai, N., Bhatt, N. N., Montalbano, M., Sengupta, U., Gaikwad, S., Ventura, F. L., McAllen, S., Ellsworth, A., García, S., & Kayed, R. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2503-3 · Cited by 113

mTor mediates tau localization and secretion: implication for Alzheimer’s disease

Tang, Z., Ioja, E., Bereczki, E., Hultenby, K., Li, C., Guan, Z., Winblad, B., & Pei, J.-J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.003 · Cited by 112

Tau-Based Therapeutic Approaches for Alzheimer's Disease - A Mini-Review

Boutajangout, A., & Wısnıewskı, T. (2014) · Gerontology · doi:10.1159/000358875 · Cited by 110

The Essential Role of Soluble Aβ Oligomers in Alzheimer’s Disease

Wang, Z.-X., Tan, L., Liu, J., & Yu, J.-T. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9143-0 · Cited by 110

Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease

Iqbal, K., & Grundke, I. (1991) · Molecular Neurobiology · doi:10.1007/bf02935561 · Cited by 108

Stabilization of Hyperdynamic Microtubules Is Neuroprotective in Amyotrophic Lateral Sclerosis

Fanara, P., Banerjee, J., Hueck, R. V., Harper, M. R., Awada, M., Turner, H., Husted, K. H., Brandt, R., & Hellerstein, M. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703434200 · Cited by 106

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

Fyn-Tau-Amyloid: A Toxic Triad

Haass, C., & Mandelkow�, E. (2010) · Cell · doi:10.1016/j.cell.2010.07.032 · Cited by 105

The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target

Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 105

Heparan sulfate proteoglycan expression in cerebrovascular amyloid β deposits in Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis (Dutch) brains

van Horssen, J., Otte‐Höller, I., David, G., Maat–Schieman, M. L. C., van den Heuvel, L. P., Wesseling, P., de Waal, R. M., & Verbeek, M. M. (2001) · Acta Neuropathologica · doi:10.1007/s004010100414 · Cited by 103

Nilotinib Induces Autophagy in Hepatocellular Carcinoma through AMPK Activation

Yu, H.-C., Lin, C., Tai, W., Liu, C., Shiau, C., & Chen, K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.446385 · Cited by 103

Synergistic interaction between amyloid and tau predicts the progression to dementia

Pascoal, T. A., Mathotaarachchi, S., Shin, M., Benedet, A. L., Mohades, S., Wang, S., Beaudry, T., Kang, M. S., Soucy, J., Labbe, A., et al. (2017) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.11.005 · Cited by 101

Ginkgolides protect against amyloid-β1–42-mediated synapse damage in vitro

Bate, C., Tayebi, M., & Williams, A. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-1 · Cited by 99

PET Imaging of Tau Pathology and Relationship to Amyloid, Longitudinal MRI, and Cognitive Change in Down Syndrome: Results from the Down Syndrome Biomarker Initiative (DSBI)

Rafii, M. S., Lukic, A. S., Andrews, R. D., Brewer, J. B., Rissman, R. A., Strother, S. C., Wernick, M. N., Pennington, C., Mobley, W. C., Ness, S. L., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170390 · Cited by 99

Transcriptional and Post-transcriptional Mechanisms Limit Heading Date 1 (Hd1) Function to Adapt Rice to High Latitudes

Goretti, D., Martignago, D., Landini, M., Brambilla, V., Gómez‐Ariza, J., Gnesutta, N., Galbiati, F., Collani, S., Takagi, H., Terauchi, R., et al. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006530 · Cited by 98

Swedish Alzheimer Mutation Induces Mitochondrial Dysfunction Mediated by HSP60 Mislocalization of Amyloid Precursor Protein (APP) and Beta-Amyloid

Walls, K. C., Coskun, P. E., Gallegos-Pérez, J.-L., Zadourian, N., Freude, K., Rasool, S., Blurton-Jones, M. M., Green, K. N., & LaFerla, F. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365890 · Cited by 95

Characteristics and consequences of muscarinic receptor activation by tau protein

Gómez‐Ramos, A., Dı́az-Hernández, M., Rubio, A., Díaz‐Hernandéz, J. I., Miras‐Portugal, M. T., & Ávila, J. (2009) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2009.04.006 · Cited by 95

Cell‐derived microparticles: a new challenge in neuroscience

Doeuvre, L., Plawinski, L., Toti, F., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06163.x · Cited by 93

Critical residues involved in tau binding to fyn: implications for tau phosphorylation in Alzheimer’s disease

Lau, D. H. W., Hogseth, M., Phillips, E. C., O’Neill, M. J., Pooler, A. M., Noble, W. J., & Hanger, D. P. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0317-4 · Cited by 93

Recent developments of protein kinase inhibitors as potential AD therapeutics

Tell, V., & Hilgeroth, A. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00189 · Cited by 92

The binding and phosphorylation of Thr231 is critical for Tau’s hyperphosphorylation and functional regulation by glycogen synthase kinase 3β

Lin, Y., Cheng, J., Liang, L., Ko, C., Lo, Y., & Lu, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04792.x · Cited by 90

Parkinsonian Neurotoxin 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and α-Synuclein Mutations Promote Tau Protein Phosphorylation at Ser262 and Destabilize Microtubule Cytoskeleton in Vitro

Qureshi, H. Y., & Paudel, H. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.178905 · Cited by 90

Trimeric Tau Is Toxic to Human Neuronal Cells at Low Nanomolar Concentrations

Tian, H., Davidowitz, E., Lopez, P., Emadi, S., Moe, J., & Sierks, M. (2013) · International Journal of Cell Biology · doi:10.1155/2013/260787 · Cited by 90

Dynactin1 depletion leads to neuromuscular synapse instability and functional abnormalities

Bercier, V., Hubbard, J. M., Fidelin, K., Duroure, K., Auer, T. O., Revenu, C., Wyart, C., & Bene, F. D. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0327-3 · Cited by 87

Amyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cells

Nie, C. L., Wang, X. S., Liu, Y. M., Perrett, S., & He, R. Q. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-9 · Cited by 86

Divergent tissue and sex effects of rapamycin on the proteasome-chaperone network of old mice

Rodriguez, K. A., Dodds, S. G., Strong, R., Galván, V., Sharp, Z. D., & Buffenstein, R. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00083 · Cited by 86

Assembly of paired helical filaments from mouse tau: implications for the neurofibrillary pathology in transgenic mouse models for Alzheimer's disease

Kampers, T., Pangalos, M. N., Geerts, H., Wiech, H., & Mandelkow, E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00522-0 · Cited by 86

The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation

Chambraud, B., Belabes, H., Fontaine‐Lenoir, V., Fellous, A., & Baulieu, E. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-7667com · Cited by 85

Interactions between Tau and Different Conformations of Tubulin: Implications for Tau Function and Mechanism

Duan, A. R., Jonasson, E. M., Alberico, E. O., Li, C., Scripture, J. P., Miller, R. A., Alber, M., & Goodson, H. V. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.018 · Cited by 85

Amyloid-β1-42 Induces Reactive Oxygen Species-Mediated Autophagic Cell Death in U87 and SH-SY5Y Cells

Wang, H., Ma, J., Tan, Y., Wang, Z., Sheng, C., Chen, S., & Ding, J. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091207 · Cited by 84

Pin1 colocalization with phosphorylated tau in Alzheimer's disease and other tauopathies

Ramakrishnan, P., Dickson, D. W., & Davies, P. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00109-8 · Cited by 84

Stimulatory effect of α‐synuclein on the tau‐phosphorylation by GSK‐3 β

Kawakami, F., Suzuki, M., Shimada, N., Kagiya, G., Ohta, E., Tamura, K., Maruyama, H., & Ichikawa, T. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08389.x · Cited by 82

Pin1 allows for differential Tau dephosphorylation in neuronal cells

Hamdane, M., Dourlen, P., Bretteville, A., Sambo, A., Ferreira, S., Ando, K., Kerdraon, O., Bégard, S., Geay, L., Lippens, G. M., et al. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.03.006 · Cited by 82

The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes

Lasagna‐Reeves, C. A., Sengupta, U., Castillo‐Carranza, D. L., Gerson, J. E., Guerrero‐Munoz, M. J., Troncoso, J. C., Jackson, G. R., & Kayed, R. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-56 · Cited by 78

Splicing of a Regulated Exon Reveals Additional Complexity in the Axonal Microtubule‐Associated Protein Tau

Wei, M., & Andreadis, A. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70041346.x · Cited by 75

Interactions between Tau and α-synuclein augment neurotoxicity in a Drosophila model of Parkinson's disease

Roy, B., & Jackson, G. R. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu011 · Cited by 75

Fyn kinase inhibition reduces protein aggregation, increases synapse density and improves memory in transgenic and traumatic Tauopathy

Tang, S. J., Fesharaki‐Zadeh, A., Takahashi, H., Nies, S. H., Smith, L. M., Luo, A., Chyung, A. S., Chiasseu, M., & Strittmatter, S. M. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00976-9 · Cited by 74

Isomerase Pin1 Stimulates Dephosphorylation of Tau Protein at Cyclin-dependent Kinase (Cdk5)-dependent Alzheimer Phosphorylation Sites

Kimura, T., Tsutsumi, K., Taoka, M., Saito, T., Masuda‐Suzukake, M., Ishiguro, K., Plattner, F., Uchida, T., Isobe, T., Hasegawa, M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.433326 · Cited by 73

Tau interacts with Golgi membranes and mediates their association with microtubules

Farah, C. A., Perreault, S., Liazoghli, D., Desjardins, M., Antón, A., Lauzon, M., Paiement, J. M., & Leclerc, N. M. (2006) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20157 · Cited by 73

Binding of Hsp90 to Tau Promotes a Conformational Change and Aggregation of Tau Protein

Tortosa, E., Santa‐María, I., Moreno, F. J., Lim, F., Pérez, M., & Ávila, J. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1049 · Cited by 72

Immunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy

Giustiniani, J., Chambraud, B., Sardin, E., Dounane, O., Guillemeau, K., Nakatani, H., Paquet, D., Kamah, A., Landrieu, I., Lippens, G. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402645111 · Cited by 72

Extensive proteomic screening identifies the obesity-related NYGGF4 protein as a novel LRP1-interactor, showing reduced expression in early Alzheimer's disease

Kajiwara, Y., Franciosi, S., Takahashi, N., Krug, L., Schmeidler, J., Taddei, K., Haroutunian, V. H., Fried, U., Ehrlich, M. E., Martins, R. N., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-1 · Cited by 72

β-Amyloid Induces Pathology-Related Patterns of Tau Hyperphosphorylation at Synaptic Terminals

Wu, H., Kuo, P.-C., Wang, Y.-T., Lin, H.-T., Roe, A. D., Wang, B. Y., Han, C., Hyman, B. T., Chen, Y., & Tai, H. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly059 · Cited by 72

Rab7A regulates tau secretion

Rodríguez, L. C. D. L. C., Mohamed, N., Desjardins, A., Lippé, R., Fon, E. A., & Leclerc, N. M. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13994 · Cited by 66

Microtubule-stabilising drugs for therapy of Alzheimer’s disease and other neurodegenerative disorders with axonal transport impairments

Trojanowski, J. Q., Smith, A. B., Huryn, D. M., & Lee, V. M. ‐. (2005) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.6.5.683 · Cited by 64

Membrane association and release of wild-type and pathological tau from organotypic brain slice cultures

Croft, C. L., Wade, M. A., Kurbatskaya, K., Mastrandreas, P., Hughes, M. M., Phillips, E. C., Pooler, A. M., Perkinton, M. S., Hanger, D. P., & Noble, W. J. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.97 · Cited by 62

Paraquat-induced inflammatory response of microglia through HSP60/TLR4 signaling

Sun, Y., Zheng, J., Xu, Y., & Zhang, X. (2018) · Human & Experimental Toxicology · doi:10.1177/0960327118758152 · Cited by 61

The neurotoxicity of amyloid β-protein oligomers is reversible in a primary neuron model

Tanokashira, D., Mamada, N., Yamamoto, F., Taniguchi, K., Tamaoka, A., Lakshmana, M. K., & Araki, W. (2017) · Molecular Brain · doi:10.1186/s13041-016-0284-5 · Cited by 59

Alternative Macroautophagic Pathways

Juenemann, K., & Reits, E. A. (2012) · International Journal of Cell Biology · doi:10.1155/2012/189794 · Cited by 58

Biochemical and functional diversity of microtubule motors in the nervous system

Brady, S. T., & Sperry, A. O. (1995) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(95)80058-1 · Cited by 57

Pathogenesis of Alzheimer's Disease: Role of Amyloid-beta and Hyperphosphorylated Tau Protein

Sajjad, R., Arif, R., Shah, A. A., Manzoor, I., & Mustafa, G. (2018) · Indian Journal of Pharmaceutical Sciences · doi:10.4172/pharmaceutical-sciences.1000397 · Cited by 57

Cancer Incidence and Mortality in Patients with Type 2 Diabetes Treated with Human Insulin: A Cohort Study in Shanghai

Gu, Y., Wang, C., Zheng, Y., Hou, X., Mo, Y., Yu, W., Zhang, L., Hu, C., Nan, H., Chen, L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053411 · Cited by 55

Hyperphosphorylation of tau protein by calpain regulation in retina of Alzheimer's disease transgenic mouse

Zhao, H., Chang, R., Che, H., Wang, J., Yang, L., Wei, F., Xia, Y., Li, N., Ma, Q., & Wang, X. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.06.026 · Cited by 53

The Binding Receptors of Aβ: an Alternative Therapeutic Target for Alzheimer’s Disease

Xia, M., Cheng, X., Yi, R., Gao, D., & Xiong, J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8994-0 · Cited by 53

A direct gateway into the extracellular space: Unconventional secretion of FGF2 through self-sustained plasma membrane pores

Steringer, J. P., & Nickel, W. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.02.010 · Cited by 53

Cytoskeletal mechanisms of neuronal degeneration

Brandt, R. (2001) · Cell and Tissue Research · doi:10.1007/s004410000334 · Cited by 52

Autophagy-Mediated Secretory Pathway is Responsible for Both Normal and Pathological Tau in Neurons

Kang, S., Son, S. M., Baik, S. H., Yang, J., & Mook‐Jung, I. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190180 · Cited by 52

Calcyclin binding protein and Siah-1 interacting protein in Alzheimer's disease pathology: neuronal localization and possible function

Wasik, U., Schneider, G., Mietelska‐Porowska, A., Mazurkiewicz, M., Fabczak, H., Weis, S., Zabke, C., Harrington, C. R., Filipek, A., & Niewiadomska, G. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.007 · Cited by 51

Tau Spreading Mechanisms; Implications for Dysfunctional Tauopathies

Fuster-Matanzo, A., Hernández, F., & Ávila, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030645 · Cited by 50

TNFα deficiency results in increased IL-1β in an early onset of spontaneous murine colitis

Santis, S. D., Kunde, D., Galleggiante, V., Liso, M., Scandiffio, L., Serino, G., Pinto, A., Campiglia, P., Sorrentino, R., Cavalcanti, E., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.397 · Cited by 49

Impaired tau–microtubule interactions are prevalent among pathogenic tau variants arising from missense mutations

Xia, Y., Sorrentino, Z. A., Kim, J. D., Strang, K. H., Riffe, C. J., & Giasson, B. I. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010178 · Cited by 48

FKBP immunophilins and Alzheimer’s disease: A chaperoned affair

Cao, W., & Konsolaki, M. (2011) · Journal of Biosciences · doi:10.1007/s12038-011-9080-7 · Cited by 46

Enhanced tau pathology via RanBP9 and Hsp90/Hsc70 chaperone complexes

Woo, J. A., Liu, T., Zhao, X., Trotter, C., Yrigoin, K., Cazzaro, S., Narvaez, E. D., Khan, H., Witas, R., Bukhari, A., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx284 · Cited by 46

Recent developments with tau-based drug discovery

Iqbal, K., Liu, F., & Gong, C. (2018) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2018.1445084 · Cited by 46

Thr175-phosphorylated tau induces pathologic fibril formation via GSK3β-mediated phosphorylation of Thr231 in vitro

Moszczynski, A. J., Gohar, M., Volkening, K., Leystra‐Lantz, C., Strong, W., & Strong, M. J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.12.001 · Cited by 42

A T-type channel-calmodulin complex triggers αCaMKII activation

Asmara, H., Micu, I., Rizwan, A. P., Sahu, G., Simms, B., Zhang, F., Engbers, J. D. T., Stys, P. K., Zamponi, G. W., & Turner, R. W. (2017) · Molecular Brain · doi:10.1186/s13041-017-0317-8 · Cited by 40

Alternative splicing of exon 10 in the taugene as a target for treatment of tauopathies

Zhou, J., Yu, Q., & Zou, T. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-s2-s10 · Cited by 39

Induction of Autophagy by a Novel Small Molecule Improves Aβ Pathology and Ameliorates Cognitive Deficits

Chu, C., Zhang, X., Ma, W., Li, L., Wang, W., Lu, S., & Fu, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065367 · Cited by 33

Pathological Role of Peptidyl-Prolyl Isomerase Pin1 in the Disruption of Synaptic Plasticity in Alzheimer’s Disease

Xu, L., Ren, Z., Chow, F. E., Tsai, R., Liu, T., Rizzolio, F., Boffo, S., Xu, Y., Huang, S., Lippa, C. F., et al. (2017) · Neural Plasticity · doi:10.1155/2017/3270725 · Cited by 33

Hsp90 Maintains the Stability and Function of the Tau Phosphorylating Kinase GSK3β

Dou, F., Chang, X., & Ma, D. (2007) · International Journal of Molecular Sciences · doi:10.3390/i8010060 · Cited by 32

The Roles of Endo-Lysosomes in Unconventional Protein Secretion

Lee, J., & Ye, Y. (2018) · Cells · doi:10.3390/cells7110198 · Cited by 32

The metamorphic nature of the Tau protein: dynamic flexibility comes at a cost

Sabbagh, J. J., & Dickey, C. A. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00003 · Cited by 31

PACSIN1, a Tau-interacting Protein, Regulates Axonal Elongation and Branching by Facilitating Microtubule Instability

Liu, Y., Lv, K., Li, Z., Yu, A. C. H., Chen, J., & Teng, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.403451 · Cited by 30

Overexpression of GSK3βS9A Resulted in Tau Hyperphosphorylation and Morphology Reminiscent of Pretangle-Like Neurons in the Brain of PDGSK3β Transgenic Mice

Li, B., Ryder, J. W., Yuan, S., Moore, S. A., Jr., Liu, F., Solenberg, P. J., Brune, K. A., Fox, N. W., Ni, B., Liu, R., et al. (2004) · Transgenic Research · doi:10.1023/b:trag.0000040039.44899.6f · Cited by 28

Recent Tau-Targeted Clinical Strategies for the Treatment of Alzheimer's Disease

Lee, H. E., Lim, D., Lee, J. Y., Lim, S. M., & Pae, A. N. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0151 · Cited by 25

Fluid biomarkers for diagnosing dementia: rationale and the Canadian Consensus on Diagnosis and Treatment of Dementia recommendations for Canadian physicians

Rosa‐Neto, P., Hsiung, G. R., Masellis, M., & participants, O. B. O. T. C. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt223 · Cited by 24

Effect of Pin1 or Microtubule Binding on Dephosphorylation of FTDP-17 Mutant Tau

Yotsumoto, K., Saito, T., Asada, A., Oikawa, T., Kimura, T., Uchida, C., Ishiguro, K., Uchida, T., Hasegawa, M., & Hisanaga, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.003277 · Cited by 23

Pathogenic Tau Protein Species: Promising Therapeutic Targets for Ocular Neurodegenerative Diseases

Mishan, M. A., Kanavi, M. R., Shahpasand, K., & Ahmadieh, H. (2019) · Journal of Ophthalmic and Vision Research · doi:10.18502/jovr.v14i4.5459 · Cited by 18

Liraglutide Treatment Ameliorates Neurotoxicity Induced by Stable Silencing of Pin1

Bianchi, M., Doria, V., Braghini, M. R., Petrini, S., & Manco, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205064 · Cited by 17

GluN2B-containing NMDA receptors are upregulated in plasma membranes by the sphingosine-1-phosphate analog FTY720P

Essis, S. A., Laurier-Laurin, M.-É., Pépin, É., Cyr, M., & Massicotte, G. (2015) · Brain Research · doi:10.1016/j.brainres.2015.07.055 · Cited by 16

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Angelucci, F., & Hort, J. (2016) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758834016665776 · Cited by 16

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Tang, L., Zhang, Y., Chen, G., Xiong, Y., Wang, X., & Zhu, B. (2017) · Neurochemical Research · doi:10.1007/s11064-016-2158-8 · Cited by 16

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Yamada, K., Holth, J. K., Liao, F., Stewart, F. R., Mahan, T. E., Jiang, H., Cirrito, J. R., Patel, T. K., Hochgräfe, K., Mandelkow, E., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.2045oia31 · Cited by 14

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Rosenmann, H., Blum, D. L., Kayed, R., & Ittner, L. M. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/707482 · Cited by 12

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Lonati, E., Sala, G., Tresoldi, V., Coco, S., Salerno, D., Milani, C., Losurdo, M., Farina, F., Botto, L., Ferrarese, C., et al. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1199-7 · Cited by 12

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Annaert, W. G. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-s1-l6 · Cited by 10

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(1997) · Transfusion Medicine Reviews · doi:10.1016/s0887-7963(97)80063-6 · Cited by 9

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Das Bhaskar, C. (2018) · Annals of Advances in Chemistry · doi:10.29328/journal.aac.1001010 · Cited by 6

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Colombino, M., Sini, M. C., Lissia, A., et al. (2014) · Journal of Translational Medicine · doi:10.1186/1479-5876-12-s1-o3 · Cited by 4

Tau pathology in Alzheimer’s disease and associated hypotheses

Dash, S. (2019) · Life Research · doi:10.53388/life2019-0725-302 · Cited by 3

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Hirokawa, N., & Takemura, R. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00434-5 · Cited by 2

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Dash, S. (2019) · Life Research · doi:10.12032/life2019-0725-302 · Cited by 1

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Batrak, G. A., & Myasoedova, S. Е. (2010) · DOAJ (DOAJ: Directory of Open Access Journals) · Cited by 1

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Rawat, P., Sehar, U., Bisht, J., Selman, A., Culberson, J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112841 · Cited by 509

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Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56

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Zhang, D., Zhang, W., Chen, M., Gao, X., Yuan, H., Lin, X., Mao, X., Wang, C., Guo, X., Du, Y., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.02.017 · Cited by 75

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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

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Engstrom, A. K., Walker, A. C., Moudgal, R. A., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/745133

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Jesús‐Cortés, H. D., Nogueras‐Ortiz, C. J., Gearing, M., Arnold, S. E., & Vega, I. E. (2012) · Neuroreport · doi:10.1097/wnr.0b013e32835982ce · Cited by 31