Mechanisms of tau-induced neurodegeneration

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 · see citing works

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668 · see citing works

THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASES

Cohen, P. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.002321 · Cited by 2,547 · see citing works

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 · see citing works

Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works

Observations on the brains of demented old people

Tomlinson, B. E., Blessed, G., & Roth, M. (1970) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(70)90063-8 · Cited by 2,084 · see citing works

Memantine in Moderate-to-Severe Alzheimer's Disease

Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043 · see citing works

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works

Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities

Kim, I., Xu, W., & Reed, J. C. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2755 · Cited by 1,816 · see citing works

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · see citing works

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works

Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474 · see citing works

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · cited 2× · see citing works

Long-term effects of Aβ42 immunisation in Alzheimer's disease: follow-up of a randomised, placebo-controlled phase I trial

Holmes, C., Boche, D., Wilkinson, D., Yadegarfar, G., Hopkins, V., Bayer, A., Jones, R. W., Bullock, R., Love, S., Neal, J. W., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61075-2 · Cited by 1,416 · cited 1× · see citing works

Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type

Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,380 · see citing works

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374 · see citing works

Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein

Lewis, J., McGowan, E., Rockwood, J., Melrose, H., Nacharaju, P., Van Slegtenhorst, M., Gwinn-Hardy, K., Murphy, M. P., Baker, M., Yu, X., et al. (2000) · Nature Genetics · doi:10.1038/78078 · Cited by 1,371 · see citing works

Molecular cloning and expression of glycogen synthase kinase‐3/factor A.

Woodgett, J. R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07419.x · Cited by 1,362 · see citing works

Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells

Stambolic, V., Ruel, L., & Woodgett, J. R. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70790-2 · Cited by 1,321 · see citing works

Clinical, pathological, and neurochemical changes in dementia: a subgroup with preserved mental status and numerous neocortical plaques

Katzman, R., Terry, R., DeTeresa, R., Brown, T., Davies, P., Fuld, P., Renbing, X., & Peck, A. (1988) · Annals of Neurology · doi:10.1002/ana.410230206 · Cited by 1,225 · see citing works

Occurrence of neuropathological changes and dementia of Alzheimer’s disease in Down’s syndrome

Wisniewski, K. E., Wisniewski, H. M., & Wen, G. Y. (1985) · Annals of Neurology · doi:10.1002/ana.410170310 · Cited by 1,159 · see citing works

Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms

Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,114 · see citing works

Tau pathology in Alzheimer disease and other tauopathies

Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037 · see citing works

Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036 · see citing works

Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( ³⁰⁶ VQIVYK ³¹¹ ) forming β structure

von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E.-M., & Mandelkow, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5129 · Cited by 1,021 · see citing works

Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease

Oddo, S. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.08.012 · Cited by 980 · see citing works

Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments

Alonso, A. D. C., Zaidi, T., Novák, M., Grundke, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 968 · see citing works

Tauopathy in <i>Drosophila</i> : Neurodegeneration Without Neurofibrillary Tangles

Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · see citing works

Decreased nuclear β‐catenin, tau hyperphosphorylation and neurodegeneration in GSK‐3β conditional transgenic mice

Lucas, J. J., Hernández, F., Gómez‐Ramos, P., Morán, M. A., Hen, R., & Avila, J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.27 · Cited by 903 · see citing works

Phosphorylation affects the ability of tau protein to promote microtubule assembly.

Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878 · see citing works

Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules

Alonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859 · see citing works

Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843 · see citing works

Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works

Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's disease

Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., & Wisniewski, H. M. (1989) · Brain Research · doi:10.1016/0006-8993(89)91396-6 · Cited by 818 · see citing works

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works

O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775 · see citing works

Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation

Liu, F., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04391.x · Cited by 759 · see citing works

Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.

Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5562 · Cited by 738 · see citing works

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 735 · cited 1× · see citing works

DEFECTIVE BRAIN MICROTUBULE ASSEMBLY IN ALZHEIMER'S DISEASE

Iqbal, K., Zaidi, T., Wen, G. Y., Grundke, I., MERZ, P. A., Shaikh, S., Wisniewski, H., Alafuzoff, I. I., & Winblad, B. G. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92134-3 · Cited by 727 · see citing works

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo

Yuzwa, S. A., Macauley, M. S., Heinonen, J. E., Shan, X., Dennis, R. J., He, Y., Whitworth, G. E., Stubbs, K. A., McEachern, E. J., Davies, G. J., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.96 · Cited by 717 · see citing works

Identification of normal and pathological aging in prospectively studied nondemented elderly humans

Dickson, D. W., Crystal, H. A., Mattiace, L. A., Masur, D. M., Blau, A. D., Davies, P., Yen, S.-H., & Aronson, M. K. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90027-u · Cited by 643 · see citing works

Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains.

Perry, G., Friedman, R., Shaw, G., & Chau, V (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.3033 · Cited by 623 · see citing works

Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles

Cruz, J. C., Tseng, H.-C., Goldman, J. A., Shih, H., & Tsai, L.-H. (2003) · Neuron · doi:10.1016/s0896-6273(03)00627-5 · Cited by 609 · see citing works

A brain-specific activator of cyclin-dependent kinase 5

Lew, J., Huang, Q.-Q., Qi, R. Z., Winkfein, R. J., Aebersold, R. H., Hunt, T., & Wang, J. H.-C. (1994) · Nature · doi:10.1038/371423a0 · Cited by 580 · see citing works

Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.

Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565 · see citing works

Phosphorylation that Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical Filaments

Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E., & Mandelkow, E.-M. (1999) · Biochemistry · doi:10.1021/bi981874p · Cited by 564 · see citing works

A Prospective Study of Alzheimer Disease in Down Syndrome

Lai, F., & Williams, R. S. (1989) · Archives of Neurology · doi:10.1001/archneur.1989.00520440031017 · Cited by 561 · see citing works

Proline-directed and non-proline-directed phosphorylation of PHF-tau

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Titani, K., & Ihara, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.823 · Cited by 557 · see citing works

Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration

Wang, J., Grundke, I., & Iqbal, K. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05226.x · Cited by 553 · see citing works

RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01386-5 · Cited by 548 · see citing works

Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein.

Sloboda, R. D., Rudolph, S. A., Rosenbaum, J. L., & Greengard, P. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.177 · Cited by 547 · see citing works

Association of high-molecular-weight proteins with microtubules and their role in microtubule assembly in vitro.

Murphy, D. B., & Borisy, G. G. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.7.2696 · Cited by 537 · see citing works

Tau Consists of a Set of Proteins with Repeated C-Terminal Microtubule-Binding Domains and Variable N-Terminal Domains

Himmler, A., Drechsel, D. N., Kirschner, M. W., & Martin, D. W. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1381-1388.1989 · Cited by 535 · see citing works

Protein Phosphorylation and Neuronal Function

Browning, M. D., Huganir, R. L., & Greengard, P. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb05468.x · Cited by 528 · see citing works

Phosphoprotein Phosphatase Activities in Alzheimer Disease Brain

Gong, C., Singh, T. J., Grundke‐Iqbal, I., & Iqbal, K. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03603.x · Cited by 527 · see citing works

Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms

Andorfer, C., Acker, C. M., Kress, Y., Hof, P. R., Duff, K., & Davies, P. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4637-04.2005 · Cited by 511 · cited 1× · see citing works

Cdk5 Is a Key Factor in Tau Aggregation and Tangle Formation In Vivo

Noble, W. J., Olm, V., Takata, K., Casey, E., Mary, O., Meyerson, J. L., Gaynor, K., LaFrancois, J. J., Wang, L., Kondo, T., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00259-9 · Cited by 511 · see citing works

DYNAMIC O-LINKED GLYCOSYLATION OF NUCLEAR AND CYTOSKELETAL PROTEINS

Hart, G. W. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.315 · Cited by 503 · see citing works

The Myeloid Leukemia-associated Protein SET Is a Potent Inhibitor of Protein Phosphatase 2A

Li, M., Makkinje, A., & Damuni, Z. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11059 · Cited by 479 · see citing works

Lithium Reduces Tau Phosphorylation by Inhibition of Glycogen Synthase Kinase-3

Hong, M., Chen, D. C. R., Klein, P. S., & Lee, V. M. ‐. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25326 · Cited by 470 · see citing works

Distribution of Active Glycogen Synthase Kinase 3β (GSK-3β) in Brains Staged for Alzheimer Disease Neurofibrillary Changes

Pei, J.-J., Braak, E., Braak, H., Grundke-Iqbal, I., Iqbal, K., Winblad, B., & Cowburn, R. F. (1999) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/00005072-199909000-00011 · Cited by 459 · see citing works

Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system

Tsai, L., Takahashi, T., Caviness, V. S., & Harlow, E. (1993) · Development · doi:10.1242/dev.119.4.1029 · Cited by 457 · see citing works

Phosphatase Activity Toward Abnormally Phosphorylated τ: Decrease in Alzheimer Disease Brain

Gong, C., Shaikh, S., Wang, J., Zaidi, T., Grundke, I., & Iqbal, K. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65020732.x · Cited by 440 · see citing works

Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau

Alonso, A. D. C., Grundke-Iqbal, I., Barra, H. S., & Iqbal, K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.1.298 · Cited by 437 · see citing works

[37] Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle

Cohen, P., Alemany, S., Therese, B. A., Resink, J., Strålfors, P., & Tung, H. Y. L. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)59039-0 · Cited by 411 · see citing works

Phosphorylation of Microtubule-associated Protein Tau Is Regulated by Protein Phosphatase 2A in Mammalian Brain

Gong, C.-X., Lidsky, T., Wegiel, J., Zuck, L., Grundke-Iqbal, I., & Iqbal, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5535 · Cited by 405 · see citing works

Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.

Lindern, M. V., van Baal, S., Wiegant, J. C. A. G., Raap, A. K., Hagemeijer, A., & Grosveld, G. C. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.8.3346 · Cited by 389 · see citing works

Microtubule-associated Protein/Microtubule Affinity-regulating Kinase (p110mark)

Meyer, H. E., Mandelkow, E.-M., Drewes, G., Trinczek, B., Illenberger, S., Biernat, J., Schmitt-Ulms, G., & Mandelkow, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7679 · Cited by 388 · see citing works

Anesthesia Leads to Tau Hyperphosphorylation through Inhibition of Phosphatase Activity by Hypothermia

Planel, E., Richter, K. E. G., Nolan, C. E., Finley, J. E., Liu, L., Wen, Y., Krishnamurthy, P., Herman, M., Wang, L., Schachter, J. B., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4854-06.2007 · Cited by 386 · see citing works

Alzheimer's disease. A double-labeling immunohistochemical study of senile plaques.

Dickson, D. W., Farlo, J., Davies, P., Crystal, H., Fuld, P. A., & Yen, S. H. (1988) · PubMed Central · Cited by 383 · see citing works

Calpain-dependent Proteolytic Cleavage of the p35 Cyclin-dependent Kinase 5 Activator to p25

Kusakawa, G.-I., Saito, T., Onuki, R., Ishiguro, K., Kishimoto, T., & Hisanaga, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m907757199 · Cited by 381 · see citing works

New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament‐Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry

Hanger, D. P., Betts, J. C., Loviny, T. L. F., Blackstock, W. P., & Anderton, B. H. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71062465.x · Cited by 378 · see citing works

Distribution, Levels, and Activity of Glycogen Synthase Kinase-3 in the Alzheimer Disease Brain

PEI, J.-J., TANAKA, T., TUNG, Y.-C., BRAAK, E., IQBAL, K., & GRUNDKE-IQBAL, I. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199701000-00007 · Cited by 371 · see citing works

Neurons May Live for Decades with Neurofibrillary Tangles

Morsch, R., Simon, W., & Coleman, P. D. (1999) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199902000-00008 · Cited by 370 · see citing works

The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine

Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28741 · Cited by 361 · see citing works

Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease

Wang, J.-Z., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0896-871 · Cited by 360 · see citing works

Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals

Arendt, T., Stieler, J., Strijkstra, A. M., Hut, R. A., Rüdiger, J., Van der Zee, E. A., Harkany, T., Holzer, M., & Härtig, W. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-18-06972.2003 · Cited by 357 · see citing works

Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

Pérez, M., Valpuesta, J., Medina, M., de Garcini, E. M., & Ávila, J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031183.x · Cited by 355 · see citing works

The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bɛ at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase

Woods, Y. L., Cohen, P., Becker, W. B., Jakes, R., Goedert, M., Wang, X., & Proud, C. G. (2001) · Biochemical Journal · doi:10.1042/bj3550609 · Cited by 343 · see citing works

Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90063-w · Cited by 332 · see citing works

Promotion of Hyperphosphorylation by Frontotemporal Dementia Tau Mutations

Alonso, A. D. C., Mederlyova, A., Novák, M., Grundke, I., & Iqbal, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405131200 · Cited by 330 · see citing works

Glycogen Synthase Kinase-3β Phosphorylates Protein Tau and Rescues the Axonopathy in the Central Nervous System of Human Four-repeat Tau Transgenic Mice

Spittaels, K., den Haute, C. V., Dorpe, J. V., Geerts, H., Mercken, M. H., Bruynseels, K., Lasrado, R., Vandezande, K., Laenen, I., Boon, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006219200 · Cited by 317 · see citing works

Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation

Cripps, D., Thomas, S. N., Jeng, Y., Yang, F., Davies, P., & Yang, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512786200 · Cited by 312 · see citing works

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 · see citing works

Microtubule Reduction in Alzheimer's Disease and Aging Is Independent of τ Filament Formation

Cash, A., Aliev, G. M., Siedlak, S. L., Nunomura, A., Fujioka, H., Zhu, X., Raina, A. K., Vinters, H. V., Tabaton, M., Johnson, T., et al. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64296-4 · Cited by 309 · see citing works

Phosphorylation of microtubule‐associated protein tau: identification of the site for Ca2(+)‐calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles.

Steiner, B., Mandelkow�, E., Biernat, J., Gustke, N., Meyer, H. E., Schmidt, B., Mieskes, G., Söling, H., Drechsel, D. N., & Kirschner, M. W. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07563.x · Cited by 304 · see citing works

Brain Levels of Microtubule‐Associated Protein τ Are Elevated in Alzheimer's Disease: A Radioimmuno‐Slot‐Blot Assay for Nanograms of the Protein

Khatoon, S., Grundke, I., & Iqbal, K. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09432.x · Cited by 304 · see citing works

Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease

Maeda, S., Sahara, N., Saito, Y., Murayama, S., Ikai, A., & Takashima, A. (2006) · Neuroscience Research · doi:10.1016/j.neures.2005.11.009 · Cited by 301 · see citing works

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 · see citing works

PS1 activates PI3K thus inhibiting GSK‐3 activity and tau overphosphorylation: effects of FAD mutations

Baki, L., Shioi, J., Wen, P. H., Shao, Z., Schwarzman, A. L., Gama-Sosa, M. A., Neve, R. L., & Robakis, N. K. R. K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600251 · Cited by 289 · see citing works

Population-based study of the prevalence and presentation of dementia in adults with Down's syndrome

Holland, A. J., Hon, J., Huppert, F. A., Stevens, F., & Watson, P. (1998) · The British Journal of Psychiatry · doi:10.1192/bjp.172.6.493 · Cited by 288 · see citing works

Microtubule-Associated Protein Tau

Yen, S.-H. C., Nacharaju, P., Ko, L., Kenessey, Á., & Liu, W.-K. (1998) · Elsevier eBooks · doi:10.1016/b978-012734610-6/50012-9 · Cited by 284 · see citing works

Reduction of Soluble Aβ and Tau, but Not Soluble Aβ Alone, Ameliorates Cognitive Decline in Transgenic Mice with Plaques and Tangles

Oddo, S., Vasilevko, V., Caccamo, A., Kitazawa, M., Cribbs, D. H., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608485200 · Cited by 282 · see citing works

The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between β-amyloid production and tau phosphorylation in Alzheimer disease

Kimura, R., Kamino, K., Yamamoto, M., Nuripa, A., Kida, T., Kazui, H., Hashimoto, R., Tanaka, T., Kudo, T., Yamagata, H., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl437 · Cited by 281 · see citing works

Overexpression of Dyrk1A contributes to neurofibrillary degeneration in down syndrome

Liu, F., Liang, Z., Wegiel, J., Hwang, Y., Iqbal, K., Grundke‐Iqbal, I., Ramakrishna, N., & Gong, C. (2008) · The FASEB Journal · doi:10.1096/fj.07-104539 · Cited by 272 · see citing works

Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B

Wang, J.-Z., Gong, C.-X., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4854 · Cited by 269 · see citing works

Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites

Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266 · see citing works

Histopathological criteria for progressive dementia disorders: clinical-pathological correlation and classification by multivariate data analysis

Alafuzoff, I. I., Iqbal, K., Fridén, H., Adolfsson, R., & Winblad, B. G. (1987) · Acta Neuropathologica · doi:10.1007/bf00688184 · Cited by 265 · see citing works

A Conformation‐ and Phosphorylation‐Dependent Antibody Recognizing the Paired Helical Filaments of Alzheimer's Disease

Jicha, G. A., Lane, E., Vincent, I. J., Ötvös, L., Hoffmann, R., & Davies, P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69052087.x · Cited by 264 · see citing works

Identification and localization of a tau peptide to paired helical filaments of Alzheimer disease.

Iqbal, K., Grundke, I., Smith, A. J., George, L., Tung, Y. C., & Zaidi, T. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5646 · Cited by 260 · see citing works

Dyrk, a Dual Specificity Protein Kinase with Unique Structural Features Whose Activity Is Dependent on Tyrosine Residues between Subdomains VII and VIII

Kentrup, H., Becker, W. B., Heukelbach, J., Wilmes, A., Schürmann, A., Huppertz, C., Kainulainen, H., & Joost, H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.7.3488 · Cited by 259 · see citing works

Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubules and microtubule organisation

Wagner, U., Utton, M. A., Gallo, J., & Miller, C. C. J. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.6.1537 · Cited by 255 · see citing works

Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo

Žilka, N., Filipčík, P., Koson, P., Fialová, Ľ., Škrabana, R., Žilková, M., Rolkova, G., Kontseková, E., & Novák, M. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.029 · Cited by 252 · see citing works

Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration

Pei, J.-J., Grundke-Iqbal, I., Iqbal, K., Bogdanovic, N., Winblad, B., & Cowburn, R. F. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00296-0 · Cited by 226 · see citing works

Akt and CHIP coregulate tau degradation through coordinated interactions

Dickey, C. A., Koren, J., Zhang, Y.-J., Xu, Y.-F., Jinwal, U. K., Birnbaum, M. J., Monks, B., Sun, M., Cheng, J. Q., Patterson, C., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709180105 · Cited by 226 · see citing works

Purification and Characterization of Two Potent Heat-Stable Protein Inhibitors of Protein Phosphatase 2A from Bovine Kidney

Li, M., Guo, H., & Damuni, Z. (1995) · Biochemistry · doi:10.1021/bi00006a020 · Cited by 224 · see citing works

Disease-related Modifications in Tau Affect the Interaction between Fyn and Tau

Bhaskar, K., Yen, S.-H. C., & Lee, G. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505895200 · Cited by 223 · see citing works

Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer’s disease

Tanimukai, H., Grundke-Iqbal, I., & Iqbal, K. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62486-8 · Cited by 220 · see citing works

Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51.

Novak, M., Jakes, R., Edwards, P. C., Milstein, C., & Wischik, C. (1991) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.88.13.5837 · Cited by 217 · see citing works

In vivo evidence of CHIP up‐regulation attenuating tau aggregation

Sahara, N., Murayama, M., Mizoroki, T., Urushitani, M., Imai, Y., Takahashi, R., Murata, S., Tanaka, K., & Takashima, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03272.x · Cited by 208 · see citing works

Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity

Alonso, A. D. C., Li, B., Grundke-Iqbal, I., & Iqbal, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603214103 · Cited by 206 · see citing works

Alzheimer-like Changes in Microtubule-associated Protein Tau Induced by Sulfated Glycosaminoglycans

Hasegawa, M., Crowther, R. A., Jakes, R., & Goedert, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.33118 · Cited by 205 · see citing works

Phosphorylation of tau by glycogen synthase kinase-3β in intact mammalian cells: The effects on the organization and stability of microtubules

Lovestone, S., Hartley, C. L., Pearce, J., & Anderton, B. H. (1996) · Neuroscience · doi:10.1016/0306-4522(96)00126-1 · Cited by 201 · see citing works

Phosphorylation of recombinant tau by cAMP-dependent protein kinase. Identification of phosphorylation sites and effect on microtubule assembly.

Scott, C. W., Spreen, R. C., Herman, J. L., Chow, F. P., Davison, M. D., Young, J., & Caputo, C. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54055-2 · Cited by 200 · see citing works

The Role of Caspase Cleavage of Tau in Alzheimer Disease Neuropathology

Cotman, C. W., Poon, W. W., Rissman, R. A., & Blurton-Jones, M. (2005) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1093/jnen/64.2.104 · Cited by 199 · see citing works

τ is phosphorylated by GSK‐3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A‐kinase

Wang, J.-Z., Wu, Q., Smith, A., Grundke, I., & Iqbal, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01090-4 · Cited by 199 · see citing works

Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK‐3β

Liu, F., Iqbal, K., Grundke, I., & Gong, C. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03487-7 · Cited by 197 · see citing works

Physiologic importance of protein phosphatase inhibitors

Shenolikar, S. (1998) · Frontiers in bioscience · doi:10.2741/a336 · Cited by 195 · see citing works

Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease

Ledesma, M. D., Correas, I., Ávila, J., & Díaz‐Nido, J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81278-t · Cited by 189 · see citing works

Tau Becomes a More Favorable Substrate for GSK-3 When It Is Prephosphorylated by PKA in Rat Brain

Liu, S. J., Zhang, J. Y., Li, H. L., Fang, Z., Wang, Q., Deng, H. M., Gong, C. X., Grundke, I., Iqbal, K., & Wang, J. Z. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406109200 · Cited by 186 · see citing works

Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer disease

Bancher, C., Grundke, I., Iqbal, K., Fried, V. A., Smith, H. T., & Wisniewski, H. M. (1991) · Brain Research · doi:10.1016/0006-8993(91)90681-k · Cited by 185 · see citing works

Increased Dosage of Dyrk1A Alters Alternative Splicing Factor (ASF)-regulated Alternative Splicing of Tau in Down Syndrome

Shi, J., Zhang, T., Zhou, C., Chohan, M. O., Gu, X., Węgiel, J., Zhou, J., Hwang, Y., Iqbal, K., Grundke, I., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802645200 · Cited by 181 · see citing works

Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model

Pérez, M., Hernández, F., Lim, F., Díaz‐Nido, J., & Ávila, J. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2003-5405 · Cited by 180 · see citing works

Structural Impact of Heparin Binding to Full-Length Tau As Studied by NMR Spectroscopy

Sibille, N., Sillen, A., Leroy, A., Wieruszeski, J., Mulloy, B., Landrieu, I., & Lippens, G. M. (2006) · Biochemistry · doi:10.1021/bi060964o · Cited by 175 · see citing works

Molecular Identification of I1PP2A, a Novel Potent Heat-Stable Inhibitor Protein of Protein Phosphatase 2A

Li, M., Makkinje, A., & Damuni, Z. (1996) · Biochemistry · doi:10.1021/bi960581y · Cited by 174 · see citing works

Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress

Poppek, D., Keck, S., Ermak, G., Jung, T., Stolzing, A., Ullrich, O., Davies, K. J. A., & Grune, T. (2006) · Biochemical Journal · doi:10.1042/bj20060463 · Cited by 174 · see citing works

Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau

Li, B., Chohan, M. O., Grundke, I., & Iqbal, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0207-8 · Cited by 173 · see citing works

Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease

Liu, F., Zaidi, T., Iqbal, K., Grundke-Iqbal, I., Merkle, R. K., & Gong, C.-X. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02228-7 · Cited by 167 · see citing works

Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains

Khatoon, S., Grundke, I., & Iqbal, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00829-9 · Cited by 167 · see citing works

Localization of active forms of C-jun kinase (JNK) and p38 kinase in Alzheimer's disease brains at different stages of neurofibrillary degeneration

Pei, J.-J., Braak, E., Braak, H., Grundke-Iqbal, I., Iqbal, K., Winblad, B., & Cowburn, R. F. (2001) · Journal of Alzheimer's Disease · doi:10.3233/jad-2001-3107 · Cited by 165 · see citing works

ALZHEIMER'S DISEASE: PAIRED HELICAL FILAMENTS AND CYTOMEMBRANES

Gray, E. G., Paula-Barbosa, M., & Roher, A. (1987) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1987.tb00174.x · Cited by 165 · see citing works

Subgroups of Alzheimer's disease based on cerebrospinal fluid molecular markers

Iqbal, K., Flory, M. J., Khatoon, S., Soininen, H. S., Pirttilä, T., Lehtovirta, M., Alafuzoff, I. I., Blennow, K., Andreasen, N., Vanmechelen, E., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20639 · Cited by 163 · see citing works

Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5

Sengupta, A., Wu, Q., Grundke, I., Iqbal, K., & Singh, T. J. (1997) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006883924775 · Cited by 160 · see citing works

Interaction of Tau Isoforms with Alzheimer's Disease Abnormally Hyperphosphorylated Tau and in VitroPhosphorylation into the Disease-like Protein

Alonso, A. D. C., Zaidi, T., Novák, M., Barra, H. S., Grundke, I., & Iqbal, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105365200 · Cited by 160 · see citing works

Neurofibrillary tangle-predominant dementia: comparison with classical Alzheimer disease

Jellinger, K. A., & Attems, J. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0156-7 · Cited by 157 · see citing works

Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice

Kins, S., Kurosinski, P., Nitsch, R. M., & Götz, J. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63444-x · Cited by 155 · see citing works

Tau Protein in Normal and Alzheimer's Disease Brain: An Update

Johnson, G. V. W., & Hartigan, J. A. (1999) · Journal of Alzheimer s Disease · doi:10.3233/jad-1999-14-512 · Cited by 154 · see citing works

Restoration of biological activity of Alzheimer abnormally phosphorylated τ by dephosphorylation with protein phosphatase-2A, −2B and −1

Wang, J., Grundke, I., & Iqbal, K. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(95)00316-k · Cited by 154 · see citing works

Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration

Li, L., Sengupta, A., Haque, N., Grundke, I., & Iqbal, K. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.04.047 · Cited by 151 · see citing works

Alzheimer paired helical filaments Restoration of the biological activity by dephosphorylation

Iqbal, K., Zaidi, T., Bancher, C., & Grundke, I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00650-4 · Cited by 150 · see citing works

The Down Syndrome critical region

Shapiro, B. L. (1999) · Springer eBooks · doi:10.1007/978-3-7091-6380-1_3 · Cited by 149 · see citing works

PKA modulates GSK‐3β‐ and cdk5‐catalyzed phosphorylation of tau in site‐ and kinase‐specific manners

Liu, F., Liang, Z., Shi, J., Yin, D., El-Akkad, E., Grundke, I., Iqbal, K., & Gong, C. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.033 · Cited by 149 · see citing works

Inhibitory Role for Dual Specificity Phosphatase VHR in T Cell Antigen Receptor and CD28-induced Erk and Jnk Activation

Alonso, A., Saxena, M., Williams, S., & Mustelin, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006497200 · Cited by 149 · see citing works

Calpain-mediated Cleavage of the Cyclin-dependent Kinase-5 Activator p39 to p29

Patzke, H., & Tsai, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109645200 · Cited by 143 · see citing works

Okadaic-Acid-Induced Inhibition of Protein Phosphatase 2A Produces Activation of Mitogen-Activated Protein Kinases ERK1/2, MEK1/2, and p70 S6, Similar to That in Alzheimer's Disease

Pei, J.-J., Gong, C., An, W., Winblad, B. G., Cowburn, R. F., Grundke, I., & Iqbal, K. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63445-1 · Cited by 142 · see citing works

O-GlcNAcylation of key nuclear and cytoskeletal proteins: reciprocity with O-phosphorylation and putative roles in protein multimerization

Hart, G. W., Kreppel, L. K., Comer, F. I., Arnold, C. S., Snow, D. M., Ye, Z., Cheng, X., Manna, D. L. D., Caine, D. S., Earles, B. J., et al. (1996) · Glycobiology · doi:10.1093/glycob/6.7.711 · Cited by 140 · see citing works

Protein phosphorylation and neuronal function.

Walaas, S. I., & Greengard, P. (1991) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)06666-9 · Cited by 137 · see citing works

A New Molecular Link between the Fibrillar and Granulovacuolar Lesions of Alzheimer's Disease

Ghoshal, N., Smiley, J. F., DeMaggio, A. J., Hoekstra, M. F., Cochran, E. J., Binder, L. I., & Kuret, J. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65219-4 · Cited by 135 · see citing works

Down's Syndrome: Up‐Regulation of β‐Amyloid Protein Precursor and τ mRNAs and Their Defective Coordination

Oyama, F., Cairns, N. J., Shimada, H., Oyama, R., Titani, K., & Ihara, Y. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62031062.x · Cited by 129 · see citing works

Impaired brain glucose metabolism leads to Alzheimer neurofibrillary degeneration through a decrease in tau O-GlcNAcylation

Gong, C., Liu, F., Grundke-Iqbal, I., & Iqbal, K. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9101 · Cited by 128 · see citing works

Microtubule-associated polypeptides tau are altered in Alzheimer paired helical filaments

Grundke, I., VORBRODT, A. W., Iqbal, K., Tung, Y. C., Wang, G. P., & Wisniewski, H. M. (1988) · Molecular Brain Research · doi:10.1016/0169-328x(88)90017-4 · Cited by 128 · see citing works

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 126 · see citing works

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 · see citing works

Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease

Jicha, G. A., Berenfeld, B., & Davies, P. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990315)55:6 · Cited by 123 · see citing works

Involvement of in the abnormal hyperphosphorylation of tau and its reversal by Memantine

Chohan, M. O., Khatoon, S., Iqbal, I.-G., & Iqbal, K. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.06.021 · Cited by 120 · see citing works

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 120 · see citing works

P70 S6 kinase mediates tau phosphorylation and synthesis

Pei, J.-J., An, W., Zhou, X., Nishimura, T., Norberg, J., Benedikz, E., Götz, J., & Winblad, B. G. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.059 · Cited by 119 · see citing works

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 · see citing works

O3‐04–07: Tau aggregation inhibitor (TAI) therapy with rember™ arrests disease progression in mild and moderate Alzheimer's disease over 50 weeks

Wischik, C. M., Bentham, P., Wischik, D., & Seng, K. M. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.438 · Cited by 118 · see citing works

Role of Calcineurin and Protein Phosphatase‐2A in the Regulation of DARPP‐32 Dephosphorylation in Neostriatal Neurons

Nishi, A., Snyder, G. L., Nairn, A. C., & Greengard, P. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722015.x · Cited by 117 · see citing works

Concurrent alterations of O‐GlcNAcylation and phosphorylation of tau in mouse brains during fasting

Li, X., Fen, L., Wang, J., & Gong, C. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04735.x · Cited by 116 · see citing works

Polymerization of tau peptides into fibrillar structures. The effect of FTDP‐17 mutations

Arrasate, M., Pérez, M., Armas-Portela, R., & Ávila, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00210-0 · Cited by 116 · see citing works

BAG-1 Associates with Hsc70·Tau Complex and Regulates the Proteasomal Degradation of Tau Protein

Elliott, E., Tsvetkov, P., & Ginzburg, I. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706379200 · Cited by 114 · see citing works

Anesthesia Induces Phosphorylation of Tau

Run, X., Liang, Z., Zhang, L., Iqbal, K., Grundke, I., & Gong, C. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1003 · Cited by 114 · see citing works

Calpain‐Induced Proteolysis of Normal Human Tau and Tau Associated with Paired Helical Filaments

Yang, L., & Ksiezak‐Reding, H. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.009_1.x · Cited by 113 · see citing works

The regulation of phosphorylation of τ in SY5Y neuroblastoma cells: the role of protein phosphatases

Tanaka, T., Zhong, J., Iqbal, K., Trenkner, E., & Grundke, I. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00346-9 · Cited by 113 · see citing works

Decrease in levels and rates of synthesis of tubulin and actin in developing rat brain

Schmitt, H., Gozes, I., & Littauer, U. Z. (1977) · Brain Research · doi:10.1016/0006-8993(77)90155-x · Cited by 111 · see citing works

Brain Protein Kinase PK40erk Converts TAU into a PHF-like Form as Found in Alzheimer′s Disease

Roder, H. M., Eden, P. A., & Ingram, V. M. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1672 · Cited by 110 · see citing works

Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease

Luna‐Muñoz, J., García‐Sierra, F., Falcón, V., Menéndez, I., Chávez-Macías, L., & Mena, R. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-8104 · Cited by 109 · see citing works

Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies

Yoshida, M. (2006) · Neuropathology · doi:10.1111/j.1440-1789.2006.00743.x · Cited by 108 · see citing works

Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5

Liu, F., Zaidi, T., Iqbal, K., Grundke, I., & Gong, C. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00510-9 · Cited by 106 · see citing works

Inhibition of PP‐2A upregulates CaMKII in rat forebrain and induces hyperphosphorylation of tau at Ser 262/356

Bennecib, M., Gong, C., Grundke, I., & Iqbal, K. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02127-5 · Cited by 105 · see citing works

Nature of mental retardation and dementia in down syndrome: Study with PET, CT, and neuropsychology

Schapiro, M. B., Haxby, J. V., & Grady, C. L. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90096-g · Cited by 103 · see citing works

Sites of phosphorylation in tau and factors affecting their regulation

Anderton, B. H., Betts, J. C., Blackstock, W. P., Brion, J., Chapman, S., Connell, J. W., Dayanandan, R., Gallo, J., Gibb, G., Hanger, D. P., et al. (2001) · Biochemical Society Symposia · doi:10.1042/bss0670073 · Cited by 99 · see citing works

Role of tau phosphorylation by glycogen synthase kinase-3β in the regulation of organelle transport

Tatebayashi, Y., Haque, N., Tung, Y. C., Iqbal, K., & Grundke, I. (2004) · Journal of Cell Science · doi:10.1242/jcs.01018 · Cited by 92 · see citing works

Metabolic/signal transduction hypothesis of Alzheimer?s disease and other tauopathies

Iqbal, K., & Grundke, I. (2005) · Acta Neuropathologica · doi:10.1007/s00401-004-0951-y · Cited by 91 · see citing works

Physiological regulation of tau phosphorylation during hibernation

Su, B., Wang, X., Drew, K. L., Perry, G. L., Smith, M. A., & Zhu, X. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05294.x · Cited by 91 · see citing works

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 · see citing works

Protein expression in Down syndrome brain

Engidawork, E., & Lübec, G. (2001) · Amino Acids · doi:10.1007/s007260170001 · Cited by 85 · see citing works

I PP2A 1 Affects Tau Phosphorylation via Association with the Catalytic Subunit of Protein Phosphatase 2A

Chen, S., Li, B., Grundke, I., & Iqbal, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709852200 · Cited by 84 · see citing works

Identification and Isolation of a Hyperphosphorylated, Conformationally Changed Intermediate of Human Protein Tau Expressed in Yeast

Vandebroek, T., Vanhelmont, T., Terwel, D., Borghgraef, P., Lemaire, K., Snauwaert, J., Wera, S., LEUVEN, F. V., & Winderickx, J. (2005) · Biochemistry · doi:10.1021/bi0506775 · Cited by 82 · see citing works

Calcium/calmodulin‐dependent protein kinase II phosphorylates tau at Ser‐262 but only partially inhibits its binding to microtubules

Singh, T. J., Wang, J., Novák, M., Kontzekova, E., Grundke, I., & Iqbal, K. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00485-1 · Cited by 82 · see citing works

Phosphorylation of τ Protein by Casein Kinase‐1 Converts It to an Abnormal Alzheimer‐Like State

Singh, T. J., Grundke‐Iqbal, I., & Iqbal, K. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64031420.x · Cited by 81 · see citing works

Regulation between O‐GlcNAcylation and phosphorylation of neurofilament‐M and their dysregulation in Alzheimer disease

Deng, Y., Li, B., Liu, F., Iqbal, K., Grundke, I., Brandt, R., & Gong, C. (2007) · The FASEB Journal · doi:10.1096/fj.07-8309com · Cited by 80 · see citing works

Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau

Tsujio, I., Zaidi, T., Xu, J., Kotula, L., Grundke-Iqbal, I., & Iqbal, K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2004.11.097 · Cited by 80 · see citing works

FAD mutants unable to increase neurotoxic Aβ 42 suggest that mutation effects on neurodegeneration may be independent of effects on Aβ

Shioi, J., Georgakopoulos, A., Mehta, P. D., Kouchi, Z., Litterst, C. M., Baki, L., & Robakis, N. K. R. K. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04391.x · Cited by 78 · see citing works

Proteolytic Stress Causes Heat Shock Protein Induction, Tau Ubiquitination, and the Recruitment of Ubiquitin to Tau-Positive Aggregates in Oligodendrocytes in Culture

Goldbaum, O., & Richter‐Landsberg, C. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1307-04.2004 · Cited by 75 · see citing works

Ser‐262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK

Sironi, J., Yen, S.-H. C., Gondal, J. A., Wu, Q., Grundke, I., & Iqbal, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01185-5 · Cited by 73 · see citing works

Regulation of phosphorylation of tau by cyclin‐dependent kinase 5 and glycogen synthase kinase‐3 at substrate level

Sengupta, A., Novák, M., Grundke, I., & Iqbal, K. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.09.060 · Cited by 70 · see citing works

Fragmentation of the Golgi Apparatus Induced by the Overexpression of Wild-Type and Mutant Human Tau Forms in Neurons

Liazoghli, D., Perreault, S., Micheva, K. D., Desjardins, M., & Leclerc, N. M. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62366-8 · Cited by 70 · see citing works

Immunochemical Properties of Ubiquitin Conjugates in the Paired Helical Filaments of Alzheimer Disease

Perry, G. L., Mulvihill, P., Fried, V. A., Smith, H. T., Grundke, I., & Iqbal, K. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb09203.x · Cited by 69 · see citing works

The microtubule-associated protein tau forms a triple-stranded left-hand helical polymer.

Ruben, G. C., Iqbal, K., Grundke, I., Wisniewski, H. M., Ciardelli, T. L., & Johnson, J. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54739-6 · Cited by 67 · see citing works

Microtubule Binding and Clustering of Human Tau-4R and Tau-P301L Proteins Isolated from Yeast Deficient in Orthologues of Glycogen Synthase Kinase-3β or cdk5

Vandebroek, T., Terwel, D., Vanhelmont, T., Gysemans, M., Haesendonck, C. V., Engelborghs, Y., Winderickx, J., & LEUVEN, F. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602792200 · Cited by 57 · see citing works

Oxidative Stress and the Pathogenesis of Alzheimer's Disease

Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855 · see citing works

The pathological process underlying Alzheimer’s disease in individuals under thirty

Braak, H., & Del Tredici, K. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0789-4 · Cited by 812 · see citing works

Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works

Alzheimer's disease as homeostatic responses to age-related myelin breakdown

Bartzokis, G. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.08.007 · Cited by 546 · see citing works

Trans-cellular Propagation of Tau Aggregation by Fibrillar Species

Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552 · see citing works

Invited review: Neuropathology of tauopathies: principles and practice

Kovacs, G. G. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12208 · Cited by 492 · see citing works

The epigenetics of aging and neurodegeneration

Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381 · see citing works

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 · see citing works

VDAC1, mitochondrial dysfunction, and Alzheimer’s disease

Shoshan-Barmatz, V., Nahon-Crystal, E., Shteinfer-Kuzmine, A., & Gupta, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.03.010 · Cited by 286 · see citing works

Site-specific phosphorylation of tau inhibits amyloid-β toxicity in Alzheimer’s mice

Ittner, A., Chua, S. W., Bertz, J., Volkerling, A., van der Hoven, J., Gladbach, A., Przybyla, M., Bi, M., van Hummel, A., Stevens, C. H., et al. (2016) · Science · doi:10.1126/science.aah6205 · Cited by 263 · see citing works

Contributions of Brain Insulin Resistance and Deficiency in Amyloid-Related Neurodegeneration in Alzheimerʼs Disease

de la Monte, S. M. (2012) · Drugs · doi:10.2165/11597760-000000000-00000 · Cited by 265 · see citing works

Does Alzheimer's disease begin in the brainstem?

Simic, G., Stanic, G., Mladinov, M., Jovanov‐Milosevic, N., Kostovic, I., & Hof, P. R. (2009) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2009.01038.x · Cited by 204 · see citing works

Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo

Cowan, C. M., Bossing, T., Page, A., Shepherd, D., & Mudher, A. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0716-8 · Cited by 156 · see citing works

Methamphetamine-induced neuroinflammation and neuronal dysfunction in the mice hippocampus: preventive effect of indomethacin

Gonçalves, J., Baptista, S., Martins, T., Milhazes, N., Borges, F., Ribeiro, C. F., Malva, J. O., & Silva, A. P. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07059.x · Cited by 152 · see citing works

Spreading of Tau Pathology in Sporadic Alzheimer’s Disease Along Cortico-cortical Top-Down Connections

Braak, H., & Del Tredici, K. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhy152 · Cited by 148 · see citing works

Dynamic association of tau with neuronal membranes is regulated by phosphorylation

Pooler, A. M., Usardi, A., Evans, C. J., Philpott, K. L., Noble, W., & Hanger, D. P. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.01.005 · Cited by 148 · see citing works

The influence of phospho-tau on dendritic spines of cortical pyramidal neurons in patients with Alzheimer’s disease

Merino-Serrais, P., Benavides-Piccione, R., Blazquez-Llorca, L., Kastanauskaite, A., Rábano, A., Avila, J., & DeFelipe, J. (2013) · Brain · doi:10.1093/brain/awt088 · Cited by 134 · see citing works

Cancer and Alzheimer’s disease inverse relationship: an age-associated diverging derailment of shared pathways

Lanni, C., Masi, M., Racchi, M., & Govoni, S. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-0760-2 · Cited by 130 · see citing works

Developing Effective Alzheimer’s Disease Therapies: Clinical Experience and Future Directions

Elmaleh, D. R., Farlow, M. R., Conti, P. S., Tompkins, R. G., Kundakovic, L., & Tanzi, R. E. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190507 · Cited by 129 · see citing works

Sodium selenate retards epileptogenesis in acquired epilepsy models reversing changes in protein phosphatase 2A and hyperphosphorylated tau.

Liu, S.-J., Zheng, P., Wright, D. K., Dezsi, G., Braine, E., Nguyen, T., Corcoran, N. M., Johnston, L. A., Hovens, C. M., Mayo, J. N., et al. (2016) · Brain · doi:10.1093/brain/aww116 · Cited by 127 · see citing works

Cellular, synaptic, and biochemical features of resilient cognition in Alzheimer’s disease

Arnold, S. E., Louneva, N., Cao, K., Wang, L.-S., Han, L.-Y., Wolk, D. A., Negash, S., Leurgans, S. E., Schneider, J. A., Buchman, A. S., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.03.004 · Cited by 123 · see citing works

Amyloid generation and dysfunctional immunoproteasome activation with disease progression in animal model of familial Alzheimer’s disease

Aso, E., Lomoio, S., López‐González, I., Joda, L., Carmona, M., Fernández‐Yagüe, N., Moreno, J., Juvés, S., Pujol, A., Pamplona, R., et al. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00560.x · Cited by 118 · see citing works

Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies

Gaikwad, S., Senapati, S., Haque, M. A., & Kayed, R. (2024) · Alzheimer's &amp; Dementia · doi:10.1002/alz.13490 · Cited by 117 · see citing works

Amyloid, tau, pathogen infection and antimicrobial protection in Alzheimer’s disease –conformist, nonconformist, and realistic prospects for AD pathogenesis

Li, H., Liu, C.-C., Zheng, H., & Huang, T. Y. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0139-3 · Cited by 103 · see citing works

The Proteasome and Oxidative Stress in Alzheimer's Disease

Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99 · see citing works

The &amp;#x201C;Aged Garlic Extract&amp;#x201D; (AGE) and One of its Active Ingredients S-Allyl-LCysteine (SAC) as Potential Preventive and Therapeutic Agents for Alzheimer's Disease (AD)

Ray, B., B. Chauhan, N., & K. Lahiri, D. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711796504664 · Cited by 100 · see citing works

mTOR in Down syndrome: Role in Aß and tau neuropathology and transition to Alzheimer disease-like dementia

Di Domenico, F., Tramutola, A., Foppoli, C., Head, E., Perluigi, M., & Butterfield, D. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.009 · Cited by 89 · see citing works

Stimulatory effect of <b>α</b>‐synuclein on the tau‐phosphorylation by GSK‐3<b>β</b>

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 · see citing works

Alzheimer’s-like pathology in aging rhesus macaques: Unique opportunity to study the etiology and treatment of Alzheimer’s disease

Arnsten, A. F. T., Datta, D., Leslie, S., Yang, S.-T., Wang, M., & Nairn, A. C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903671116 · Cited by 74 · see citing works

Infantile tauopathies: Hemimegalencephaly; tuberous sclerosis complex; focal cortical dysplasia 2; ganglioglioma

Sarnat, H. B., & Flores-Sarnat, L. (2015) · Brain and Development · doi:10.1016/j.braindev.2014.08.010 · Cited by 73 · see citing works

Metabolic syndrome as a risk factor for Alzheimer's disease: Is Aβ a crucial factor in both pathologies?

Campos-Peña, V., Toral-Rios, D., Becerril-Pérez, F., Sánchez-Torres, C., Delgado-Namorado, Y., Torres-Ossorio, E., Franco-Bocanegra, D., & Carvajal, K. (2017) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2016.6768 · Cited by 58 · see citing works

High-fat diet-induced activation of SGK1 promotes Alzheimer’s disease-associated tau pathology

Elahi, M., Motoi, Y., Shimonaka, S., Ishida, Y., Hioki, H., Takanashi, M., Ishiguro, K., Imai, Y., & Hattori, N. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab115 · Cited by 57 · see citing works

Molecular mechanism of prion‐like tau‐induced neurodegeneration

Alonso, A. D., Beharry, C., Corbo, C. P., & Cohen, L. S. (2016) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2015.12.014 · Cited by 53 · see citing works

Caspase-3-Dependent Proteolytic Cleavage of Tau Causes Neurofibrillary Tangles and Results in Cognitive Impairment During Normal Aging

Means, J. C., Gerdes, B. C., Kaja, S., Sumien, N., Payne, A. J., Stark, D. A., Borden, P. K., Price, J. L., & Koulen, P. (2016) · Neurochemical Research · doi:10.1007/s11064-016-1942-9 · Cited by 54 · see citing works

A multifactorial model of pathology for age of onset heterogeneity in familial Alzheimer’s disease

Sepulveda-Falla, D., Chavez-Gutierrez, L., Portelius, E., Vélez, J. I., Dujardin, S., Barrera-Ocampo, A., Dinkel, F., Hagel, C., Puig, B., Mastronardi, C., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02249-0 · Cited by 54 · see citing works

Reduction of the immunostainable length of the hippocampal dentate granule cells’ primary cilia in 3xAD-transgenic mice producing human Aβ1-42 and tau

Chakravarthy, B., Gaudet, C., Ménard, M., Brown, L., Atkinson, T., LaFerla, F. M., Ito, S., Armato, U., Dal Prà, I., & Whitfield, J. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.09.056 · Cited by 52 · see citing works

Tau-directed approaches for the treatment of Alzheimer’s disease: focus on leuco-methylthioninium

Seripa, D., Solfrizzi, V., Imbimbo, B. P., Daniele, A., Santamato, A., Lozupone, M., Zuliani, G., Greco, A., Logroscino, G., & Panza, F. (2016) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2016.1140039 · Cited by 50 · see citing works

Tau phosphorylation in human brain: relationship to behavioral disturbance in dementia

Guadagna, S., Esiri, M. M., Williams, R. J., & Francis, P. T. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.01.015 · Cited by 48 · see citing works

Validation of the Movement Disorder Society Criteria for the Diagnosis of 4‐Repeat Tauopathies

Respondek, G., Grimm, M., Piot, I., Arzberger, T., Compta, Y., Englund, E. M., Ferguson, L. W., Gelpí, E., Roeber, S., Giese, A., et al. (2019) · Movement Disorders · doi:10.1002/mds.27872 · Cited by 73 · see citing works

4-repeat tauopathy sharing pathological and biochemical features of corticobasal degeneration and progressive supranuclear palsy

Katsuse, O., Iseki, E., Arai, T., Akiyama, H., Togo, T., Uchikado, H., Kato, M., de Silva, R., Lees, A. J., & Kosaka, K. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0728-8 · Cited by 46 · see citing works

Novel tau filament fold in corticobasal degeneration, a four-repeat tauopathyPreprint

Zhang, W., Tarutani, A., Newell, K. L., Murzin, A. G., Matsubara, T., Falcon, B., Vidal, R., Garringer, H. J., Shi, Y., Ikeuchi, T., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/811703 · Cited by 19 · see citing works

A clinical and neuropathological study of an unusual case of sporadic tauopathy. A variant of corticobasal degeneration?

Ohara, S., Tsuyuzaki, J., Oide, T., Arai, H., Higuchi, S., Hasegawa, M., & Iwatsubo, T. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00616-x · Cited by 15 · see citing works

Clinical and Pathologic Evidence of Corticobasal Degeneration and Progressive Supranuclear Palsy in Familial Tauopathy

Tuite, P., Clark, H. B., Bergeron, C., Bower, M., George‐Hyslop, P. S., Mateva, V., Anderson, J. H., & Knopman, D. S. (2005) · Archives of Neurology · doi:10.1001/archneur.62.9.1453 · Cited by 29 · see citing works