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A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.
Open accessAbstract
Paired helical filaments (PHFs) are prominent components of Alzheimer disease (AD) neurofibrillary tangles (NFTs). Rather than isolating NFTs, we selected for PHF populations that can be extracted from AD brain homogenates. About 50% of PHF immunoreactivity can be obtained in 27,200 x g supernatants following homogenization in buffers containing 0.8 M NaCl. We further enriched for PHFs by taking advantage of their insolubility in the presence of zwitterionic detergents and 2-mercaptoethanol, removal of aggregates by filtration through 0.45-microns filters, and sucrose density centrifugation. PHF-enriched fractions contained two to five proteins of 57-68 kDa that displayed the same antigenic properties as PHFs. Since the 57- to 68-kDa PHF proteins are antigenically related to tau proteins, they are similar to the tau proteins previously observed in NFTs. However, further analysis revealed that PHF-associated tau can be distinguished from normal, soluble tau by PHF antibodies that do not recognize human adult tau and by one- and two-dimensional PAGE.
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Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Cited by
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345
Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
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
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
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
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
Self-citationLife and Death of Neurons in the Aging Brain
Morrison, J. H., & Hof, P. R. (1997) · Science · doi:10.1126/science.278.5337.412 · Cited by 1,344
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998
TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
Amador‐Ortiz, C., Lin, W., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff‐Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007) · Annals of Neurology · doi:10.1002/ana.21154 · Cited by 916
Self-citationTauopathy in Drosophila : 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
Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903
Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer's Disease
Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836
Blennow, K., Wallin, A., Ågren, H., Spenger, C., Siegfried, J., & Vanmechelen, E. (1995) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815140 · Cited by 789
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
Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
Andorfer, C., Kress, Y., Espinoza, M., De Silva, R., Tucker, K. L., Barde, Y., Duff, K., & Davies, P. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01879.x · Cited by 722
Self-citationNoble, W., Planel, E., Zehr, C., Olm, V., Meyerson, J., Suleman, F., Gaynor, K., Wang, L., LaFrancois, J., Feinstein, B., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500466102 · Cited by 709
Ramsden, M., Kotilinek, L., Forster, C., Paulson, J., McGowan, E., SantaCruz, K., Guimaraes, A., Yue, M., Lewis, J., Carlson, G., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.3279-05.2005 · Cited by 702
Tau protein pathology in neurodegenerative diseases
Spillantini, M. G., & Goedert, M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01337-x · Cited by 683
Regulation of Tau Pathology by the Microglial Fractalkine Receptor
Bhaskar, K., Konerth, M., Kokiko-Cochran, O. N., Cardona, A., Ransohoff, R. M., & Lamb, B. T. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.023 · Cited by 639
“To examine the effects of CX3CR1 deficiency on MAPT aggregation in the hTau mice, 1% Sarkosyl hippocampal extracts were prepared from 6-month-old hTau-Cx3cr1 and hTau-Cx3cr1 / mice (Greenberg and Davies, 1990; Mocanu et al., 2008) to generate both Sarkosyl-soluble and -insoluble MAPT (‘‘pretangles’’) fractions (Mocanu…”
Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
Maphis, N., Xu, G., Kokiko-Cochran, O. N., Jiang, S., Cardona, A., Ransohoff, R. M., Lamb, B. T., & Bhaskar, K. (2015) · Brain · doi:10.1093/brain/awv081 · Cited by 595
β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595
Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress.
Yan, S. D., Chen, X., Schmidt, A. M., Brett, J., Godman, G., Zou, Y. S., Scott, C. W., Caputo, C., Frappier, T., & Smith, M. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7787 · Cited by 565
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
Ishihara, T., Hong, M., Zhang, B., Nakagawa, Y., Lee, M. K., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)81127-7 · Cited by 564
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
Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
Guela, C., Wu, C.-K., Saroff, D., Lorenzo, A., Yuan, M., & Yankner, B. A. (1998) · Nature Medicine · doi:10.1038/nm0798-827 · Cited by 520
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
“Ultracentrifugation and Sarkosyl extraction (30 min incubation in 1% Sarkosyl) was performed according to Greenberg and Davies (1990) to obtain insoluble fractions of tau from htau mice aged 15 months.”
MethodSelf-citationIdentification and localization of Chlamydia pneumoniae in the Alzheimer's brain
Balin, B. J., Gérard, H. C., Arking, E. J., Appelt, D. M., Branigan, P. J., Abrams, J. T., Whittum-Hudson, J. A., & Hudson, A. P. (1998) · Medical Microbiology and Immunology · doi:10.1007/s004300050071 · Cited by 506
Biernat, J., Mandelkow, E. M., Schröter, C., Lichtenberg‐Kraag, B., Steiner, B., Berling, B., Meyer, H., Mercken, M., Vandermeeren, A., & Goedert, M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05204.x · Cited by 484
Frontotemporal dementia: Clinicopathological correlations
Forman, M. S., Farmer, J., Johnson, J. K., Clark, C. M., Arnold, S. E., Coslett, H. B., Chatterjee, A., Hurtig, H. I., Karlawish, J. H., Rosen, H. J., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20873 · Cited by 478
Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., & Tan, J. (2008) · Brain Research · doi:10.1016/j.brainres.2008.02.107 · Cited by 459
Goedert, M., Jakes, R., Crowther, R. A., Six, J., Lübke, U., Vandermeeren, M., Cras, P., Trojanowski, J. Q., & Lee, V. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5066 · Cited by 446
Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain
Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41890-x · Cited by 430
Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375
p38 Kinase Is Activated in the Alzheimer's Disease Brain
Hensley, K., Floyd, R. A., Zheng, N., Nael, R., Robinson, K. A., Nguyen, X., Pye, Q. N., Stewart, C. A., Geddes, J., Markesbery, W. R., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722053.x · Cited by 373
A novel GSK-3β inhibitor reduces Alzheimer's pathology and rescues neuronal loss in vivo
Serenó, L., Coma, M., Rodríguez, M., Sánchez-Ferrer, P., Sánchez, M. B., Gich, I., Agulló, J. M., Pérez, M., Avila, J., Guardia-Laguarta, C., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.025 · Cited by 368
(1997) · Europe PMC (PubMed Central) · Cited by 354
Microglial NF-κB drives tau spreading and toxicity in a mouse model of tauopathy
Wang, C., Fan, L., Khawaja, R. R., Liu, B., Zhan, L., Kodama, L., Chin, M., Li, Y., Le, D., Zhou, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29552-6 · Cited by 333
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
Kawarabayashi, T., Shoji, M., Younkin, L. H., Wen-Lang, L., Dickson, D. W., Murakami, T., Matsubara, E., Abe, K., Ashe, K. H., & Younkin, S. G. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5543-03.2004 · Cited by 320
Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306
Self-citationCummings, B. J., Pike, C. J., Shankle, R., & Cotman, C. W. (1996) · Neurobiology of Aging · doi:10.1016/s0197-4580(96)00170-4 · Cited by 305
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
Sydow, A., Van der Jeugd, A., Zheng, F., Ahmed, T., Balschun, D., Petrova, O., Drexler, D., Zhou, L., Rune, G., Mandelkow, E., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-10.2011 · Cited by 302
Congdon, E. E., Wu, J. W., Myeku, N., Figueroa, Y. H., Herman, M., Marinec, P. S., Gestwicki, J. E., Dickey, C. A., Yu, W. H., & Duff, K. E. (2012) · Autophagy · doi:10.4161/auto.19048 · Cited by 297
Mocanu, M.-M., Nissen, A., Eckermann, K., Khlistunova, I., Biernat, J., Drexler, D., Petrova, O., Schönig, K., Bujard, H., Mandelkow, E., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2824-07.2008 · Cited by 297
Autophagic degradation of tau in primary neurons and its enhancement by trehalose
Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297
Paudel, H. K., Lew, J., Ali, Z., & Wang, J. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49492-1 · Cited by 285
Females exhibit more extensive amyloid, but not tau, pathology in an Alzheimer transgenic model
Hirata-Fukae, C., Li, H.-F., Hoe, H.-S., Gray, A. J., Minami, S. S., Hamada, K., Niikura, T., Hua, F., Tsukagoshi-Nagai, H., Horikoshi-Sakuraba, Y., et al. (2008) · Brain Research · doi:10.1016/j.brainres.2008.03.079 · Cited by 284
Goedert, M., Cohen, E. S., Jakes, R., & Cohen, P. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81418-l · Cited by 272
Theunis, C., Crespo-Biel, N., Gafner, V., Pihlgren, M., López-Deber, M. P., Reis, P., Hickman, D. T., Adolfsson, O., Chuard, N., Ndao, D. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072301 · Cited by 259
“AD2 and PHF1 among others, are located in this region [25–29].”
BackgroundLuo, W., Liu, W., Hu, X., Hanna, M., Caravaca, A., & Paul, S. M. (2015) · Scientific Reports · doi:10.1038/srep11161 · Cited by 241
Extracellular tau is toxic to neuronal cells
Gómez-Ramos, A., Díaz-Hernández, M., Cuadros, R., Hernández, F., & Avila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.078 · Cited by 241
In vivo phosphorylation sites in fetal and adult rat tau
Watanabe, A., Hasegawa, M., Suzuki, M., Takio, K., Morishima-Kawashima, M., Titani, K., Arai, T., Kosik, K. S., & Ihara, Y. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74447-0 · Cited by 231
Engel, T., Goñi‐Oliver, P., Lucas, J. J., Avila, J., & Hernández, F. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04139.x · Cited by 223
Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.
Litersky, J. M., & Johnson, G. V. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45982-0 · Cited by 201
Hyperphosphorylation of Tau in PHF
Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Watanabe, A., Titani, K., & Ihara, Y. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00027-c · Cited by 202
Transgenic Mouse Model of Tau Pathology in Astrocytes Leading to Nervous System Degeneration
Forman, M. S., Lal, D., Zhang, B., Dabir, D. V., Swanson, E., Lee, V. M.-Y., & Trojanowski, J. Q. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.0081-05.2005 · Cited by 198
Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo
Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0327 · Cited by 187
Tau – an inhibitor of deacetylase HDAC6 function
Perez, M., Santa‐Maria, I., De Barreda, E. G., Zhu, X., Cuadros, R., Cabrero, J. R., Sanchez‐Madrid, F., Dawson, H. N., Vitek, M. P., Perry, G., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06102.x · Cited by 182
Tau Proteins and Neurofibrillary Degeneration
Goedert, M., Spillantini, M. G., & Crowther, R. A. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00671.x · Cited by 178
Chatterjee, S., Sang, T.-K., Lawless, G. M., & Jackson, G. R. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddn326 · Cited by 178
Eckermann, K., Mocanu, M.-M., Khlistunova, I., Biernat, J., Nissen, A., Hofmann, A., Schönig, K., Bujard, H., Haemisch, A., Mandelkow, E., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705282200 · Cited by 168
Early association of reactive astrocytes with senile plaques in Alzheimer's disease
Pike, C. J., Cummings, B. J., & Cotman, C. W. (1995) · Experimental Neurology · doi:10.1016/0014-4886(95)90022-5 · Cited by 164
Selective suppression of the α isoform of p38 MAPK rescues late-stage tau pathology
Maphis, N., Jiang, S., Xu, G., Kokiko-Cochran, O. N., Roy, S. M., Van Eldik, L. J., Watterson, D. M., Lamb, B. T., & Bhaskar, K. (2016) · Alzheimer's Research & Therapy · doi:10.1186/s13195-016-0221-y · Cited by 147
“The Sarkosyl-insoluble fraction of MAPT was isolated from hippocampal tissues as described before [48], with minor modifications described previously [22].”
Hartigan, J. A., & Johnson, G. V. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21395 · Cited by 141
Ando, K., Brion, J.-P., Stygelbout, V., Suain, V., Authelet, M., Dedecker, R., Chanut, A., Lacor, P., Lavaur, J., Sazdovitch, V., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1111-z · Cited by 136
Roberts, M., Sevastou, I., Imaizumi, Y., Mistry, K., Talma, S., Dey, M., Gartlon, J., Ochiai, H., Zhou, Z., Akasofu, S., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0884-2 · Cited by 135
Cognitive defects are reversible in inducible mice expressing pro-aggregant full-length human Tau
Van der Jeugd, A., Hochgräfe, K., Ahmed, T., Decker, J. M., Sydow, A., Hofmann, A., Wu, D., Messing, L., Balschun, D., D’Hooge, R., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0987-3 · Cited by 135
Tau and Axonopathy in Neurodegenerative Disorders
Higuchi, M., Lee, V. M.-Y., & Trojanowski, J. Q. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:131 · Cited by 134
Differential Incorporation of Tau Isoforms in Alzheimer's Disease
Espinoza, M., de Silva, R., Dickson, D. W., & Davies, P. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-14101 · Cited by 119
Self-citationPhosphorylation of Tau at S422 is enhanced by Aβ in TauPS2APP triple transgenic mice
Grueninger, F., Bohrmann, B., Czech, C., Ballard, T. M., Frey, J. R., Weidensteiner, C., von Kienlin, M., & Ozmen, L. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.09.004 · Cited by 117
Barbero-Camps, E., Fernández, A., Martínez, L., Fernández-Checa, J. C., & Colell, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt201 · Cited by 114
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
Oh, K.-J., Perez, S. E., Lagalwar, S., Vana, L., Binder, L., & Mufson, E. J. (2010) · International Journal of Alzheimer's Disease · doi:10.4061/2010/780102 · Cited by 105
Comparison of neuropathologic criteria for the diagnosis of Alzheimer's disease
Geddes, J. W., Tekirian, T. L., Soultanian, N. S., Ashford, J. W., Davis, D. G., & Markesbery, W. R. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00063-8 · Cited by 101
Iijima, K., Gatt, A., & Iijima-Ando, K. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq200 · Cited by 96
Jiang, S., Maphis, N. M., Binder, J., Chisholm, D., Weston, L., Duran, W., Peterson, C., Zimmerman, A., Mandell, M. A., Jett, S. D., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109720 · Cited by 92
The role of tau in Alzheimer's disease
Trojanowski, J. Q., & Lee, V. M.-Y. (2002) · Medical Clinics of North America · doi:10.1016/s0025-7125(02)00002-0 · Cited by 85
O-GlcNAcase Inhibitor ASN90 is a Multimodal Drug Candidate for Tau and α-Synuclein Proteinopathies
Permanne, B., Sand, A., Ousson, S., Nény, M., Hantson, J., Schubert, R., Wiessner, C., Quattropani, A., & Beher, D. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00057 · Cited by 82
Wang, J.-W., Imai, Y., & Lu, B. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.5094-06.2007 · Cited by 80
“It becomes abnormally phosphorylated and insoluble and forms neurofibrillary tangles (NFTs) in neurodegenerative tauopathies (Grundke-Iqbal et al., 1986; Greenberg and Davies, 1990; Lee et al., 1991).”
BackgroundVoorhees, J. R., Remy, M. T., Cintrón-Pérez, C. J., El Rassi, E., Khan, M. Z., Dutca, L. M., Yin, T. C., McDaniel, L. N., Williams, N. S., Brat, D. J., et al. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.10.023 · Cited by 78
Kinase activities increase during the development of tauopathy in htau mice
Kelleher, I., Garwood, C., Hanger, D. P., Anderton, B. H., & Noble, W. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04930.x · Cited by 78
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Absence of neurodegeneration in the thalamus and caudate of elderly patients with schizophrenia
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Quantification of Tau Protein Lysine Methylation in Aging and Alzheimer’s Disease
Huseby, C. J., Hoffman, C. N., Cooper, G. L., Cocuron, J.-C., Alonso, A. P., Thomas, S. N., Yang, A. J., & Kuret, J. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190604 · Cited by 54
Thal, D. R., Arendt, T., Waldmann, G., Holzer, M., Zedlick, D., Rüb, U., & Schober, R. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00090-6 · Cited by 53
Benzing, W. C., Ikonomovic, M. D., Brady, D. R., Mufson, E. J., & Armstrong, D. M. (1993) · Journal of Comparative Neurology · doi:10.1002/cne.903340203 · Cited by 46
HERNANDEZ, F. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.002 · Cited by 41
Han, D., Qureshi, H. Y., Lu, Y., & Paudel, H. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901095200 · Cited by 40
Regional vulnerability and spreading of hyperphosphorylated tau in seeded mouse brain
Detrez, J. R., Maurin, H., Van Kolen, K., Willems, R., Colombelli, J., Lechat, B., Roucourt, B., Van Leuven, F., Baatout, S., Larsen, P., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.010 · Cited by 39
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Bailey, R. M., Howard, J., Knight, J., Sahara, N., Dickson, D. W., & Lewis, J. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-8 · Cited by 33
Levels of tau phosphorylation at different sites in Alzheimer disease brain
Ikura, Y., Kudo, T., Tanaka, T., Tanii, H., Grundke-Iqbal, I., Iqbal, K., & Takeda, M. (1998) · NeuroReport · doi:10.1097/00001756-199807130-00041 · Cited by 31
Metadata
- Authors
- Greenberg, S. G., & Davies, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1990-08
- Volume
- 87
- Issue
- 15
- Pages
- 5827-5831
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2043661712
- Cited by
- 730
- References
- 1
- FWCI
- 18.91
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.