The DOI matches its Crossref record; 23 of the 24 references it cites were found in a registry or an index.
Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
Abstract
Hyperphosphorylated microtubule-associated protein tau is the major component of the paired helical filament of Alzheimer's disease. Phosphorylation-dependent anti-tau antibodies are being used to identify specific amino acids that are phosphorylated in tau from normal brain and Alzheimer's disease brain. As such, monoclonal antibody AT8 is widely used. By a combination of site-directed mutagenesis of recombinant tau and in vitro phosphorylation, we show that AT8 requires tau protein to be phosphorylated at both serine 202 and threonine 205 (using the numbering of the longest human brain tau isoform.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“However, no significant difference was observed between PS19 and PS19;ApoeCh mice at both 5 and 9 mo of age (Fig. 5a-d, Supp. Figure 14a-c) [45, 67–69].”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [67]
In the citing paper
“AT8, which recognizes Tau that is phosphorylated at Ser202 and Thr205 (Goedert et al., 1995) or Ser199, Ser202, and Thr205 (Hanger et al., 2009).”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Goedert et al., 1995
In the citing paper
“their detection by this antibody is commonly used as a marker of abnormal phosphorylation in brains of Alzheimer's patients.”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Goedert et al., 1995
Citations
Cites
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
Self-citationA68: 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
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929
Self-citationBramblett, 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
Self-citationSutherland, C., Leighton, I. A., & Cohen, P. (1993) · Biochemical Journal · doi:10.1042/bj2960015 · Cited by 903
Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 769
Tau protein and the neurofibrillary pathology of Alzheimer's disease
Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 721
Self-citationMatsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588
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
Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau
Mandelkow, E.-M., Drewes, G., Biernat, J., Gustke, N., Van Lint, J., Vandenheede, J. R., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81496-9 · Cited by 515
Research works printed but not linked: 1
- Trojanowski, 1993, PHF-Tau (A68): From pathological marker to potential mediator of neuronal dysfunction and de generation in Alzheimer's disease, Clin. Neurosci., 1, 184191
Cited by
Sorted by citations
Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172
Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,142
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803
Self-citationFormation 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
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507
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
Self-citationAugustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998
Allen, B., Ingram, E., Takao, M., Smith, M. J., Jakes, R., Virdee, K., Yoshida, H., Holzer, M., Craxton, M., Emson, P. C., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-21-09340.2002 · Cited by 763
Self-citationTau protein and the neurofibrillary pathology of Alzheimer's disease
Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 721
Self-citationProteopathic tau seeding predicts tauopathy in vivo
Holmes, B. B., Furman, J. L., Mahan, T. E., Yamasaki, T. R., Mirbaha, H., Eades, W. C., Belaygorod, L., Cairns, N. J., Holtzman, D. M., & Diamond, M. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411649111 · Cited by 696
Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease
Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688
“In some control subjects, these phosphopeptides are further phosphorylated and show some of the same PTMs associated with pathological Tau (Goedert et al., 1995).”
BackgroundYanamandra, K., Kfoury, N., Jiang, H., Mahan, T. E., Ma, S., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.046 · Cited by 574
Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420640 · Cited by 543
Identification of oligomers at early stages of tau aggregation in Alzheimer's disease
Lasagna‐Reeves, C. A., Castillo‐Carranza, D. L., Sengupta, U., Sarmiento, J., Troncoso, J., Jackson, G. R., & Kayed, R. (2012) · The FASEB Journal · doi:10.1096/fj.11-199851 · Cited by 527
Kitazawa, M., Cheng, D., Tsukamoto, M. R., Koike, M. A., Wes, P. D., Vasilevko, V., Cribbs, D. H., & LaFerla, F. M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100620 · Cited by 473
Leroy, K., Yilmaz, Z., & Brion, J. ‐. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00795.x · Cited by 404
Zhang, B., Carroll, J., Trojanowski, J. Q., Yao, Y., Iba, M., Potuzak, J. S., Hogan, A.-M. L., Xie, S. X., Ballatore, C., Smith, A. B., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4922-11.2012 · Cited by 401
Liquid-liquid phase separation induces pathogenic tau conformations in vitro
Kanaan, N. M., Hamel, C., Grabinski, T., & Combs, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16580-3 · Cited by 397
Sontag, E., Nunbhakdi‐Craig, V., Lee, G. S., Bloom, G. S., & Mumby, M. C. (1996) · Neuron · doi:10.1016/s0896-6273(00)80250-0 · Cited by 397
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
Echogenicity of the Substantia Nigra
Berg, D., Roggendorf, W., Schroeder, U., Klein, R., Tatschner, T., Benz, P. M., Tucha, O. M., Preier, M., Lange, K. W., Reiners, K., et al. (2002) · Archives of Neurology · doi:10.1001/archneur.59.6.999 · Cited by 381
Progesterone and Estrogen Regulate Alzheimer-Like Neuropathology in Female 3xTg-AD Mice
Carroll, J. C., Rosario, E. R., Chang, L., Stanczyk, F. Z., Oddo, S., LaFerla, F. M., & Pike, C. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2718-07.2007 · Cited by 369
Phosphorylation Sites on Tau Identified by Nanoelectrospray Mass Spectrometry
Reynolds, C. H., Betts, J. C., Blackstock, W. P., Nebreda, Á. R., & Anderton, B. H. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741587.x · Cited by 372
Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
Probst, A., Götz, J., Wiederhold, K., Tolnay, M., Mistl, C., Jaton, A., Hong, M., Ishihara, T., Lee, V., Trojanowski, J., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010051148 · Cited by 362
Self-citationAlzheimer’s pathogenesis: is there neuron-to-neuron propagation?
Braak, H., & Tredici, K. D. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0825-z · Cited by 375
Passive Immunization with Anti-Tau Antibodies in Two Transgenic Models
Chai, X., Wu, S., Murray, T. K., Kinley, R. D., Cella, C. V., Sims, H., Buckner, N., Hanmer, J. M., Davies, P., O’Neill, M. J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.229633 · Cited by 363
Detection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau
Seubert, P., Mawal-Dewan, M., Barbour, R., Jakes, R., Goedert, M., Johnson, G. V. W., Litersky, J. M., Schenk, D., Lieberburg, I., Trojanowski, J. Q., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18917 · Cited by 345
Self-citationStimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., & Goedert, M. (2012) · Brain · doi:10.1093/brain/aws143 · Cited by 343
Self-citationSpillantini, M. G., Goedert, M., Crowther, R. A., Murrell, J. R., Farlow, M. R., & Ghetti, B. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4113 · Cited by 339
Self-citationMoloney, C. M., Lowe, V. J., & Murray, M. E. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12321 · Cited by 358
Demars, M., Hu, Y., Gadadhar, A., & Lazarov, O. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22387 · Cited by 326
Brunden, K. R., Zhang, B., Carroll, J., Yao, Y., Potuzak, J. S., Hogan, A.-M. L., Iba, M., James, M. J., Xie, S. X., Ballatore, C., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3059-10.2010 · Cited by 320
Cell cycle markers in the hippocampus in Alzheimer's disease
Nagy, Z., Esiri, M. M., Cato, A.-M., & Smith, A. D. (1997) · Acta Neuropathologica · doi:10.1007/s004010050665 · Cited by 318
Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313
Conformational change as one of the earliest alterations of tau in Alzheimer's disease
Weaver, C. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00157-3 · Cited by 310
A Human Stem Cell Model of Early Alzheimer’s Disease Pathology in Down Syndrome
Shi, Y., Kirwan, P., Smith, J., MacLean, G., Orkin, S. H., & Livesey, F. J. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003771 · Cited by 310
Illenberger, S., Zheng‐Fischhöfer, Q., Preuß, U., Stamer, K., Baumann, K., Trinczek, B., Biernat, J., Godemann, R., Mandelkow, E., & Mandelkow�, E. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.6.1495 · Cited by 305
PERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia
Radford, H. E., Moreno, J. A., Verity, N., Halliday, M., & Mallucci, G. R. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1487-z · Cited by 290
Jeganathan, S., Hascher, A., Chinnathambi, S., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805300200 · Cited by 278
Ghetti, B. F., Piccardo, P., Spillantini, M. G., Ichimiya, Y., Porro, M., Perini, F., Kitamoto, T., Tateishi, J., Seiler, C. E., Frangione, B., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.2.744 · Cited by 281
Self-citationKanaan, N. M., Morfini, G. A., LaPointe, N. E., Pigino, G. F., Patterson, K. R., Song, Y., Andreadis, A., Fu, Y., Brady, S. T., & Binder, L. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0560-11.2011 · Cited by 292
Terwel, D., Lasrado, R., Snauwaert, J., Vandeweert, E., Haesendonck, C. V., Borghgraef, P., & LEUVEN, F. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409876200 · Cited by 267
Planel, E., Miyasaka, T., Launey, T., Chui, D.-H., Tanemura, K., Sato, S., Murayama, O., Ishiguro, K., Tatebayashi, Y., & Takashima, A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5561-03.2004 · Cited by 260
Engel, T., Hernández, F., Ávila, J., & Lucas, J. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0604-06.2006 · Cited by 262
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 258
Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates
Falcon, B., Cavallini, A., Angers, R. C., Glover, S. J., Murray, T. K., Barnham, L., Jackson, S., O'Neill, M. J., Isaacs, A. M., Hutton, M. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589309 · Cited by 265
Self-citationBoth total and phosphorylated tau are increased in Alzheimer's disease
Sjögren, M. J. C. (2001) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.70.5.624 · Cited by 253
Sardi, S. P., Clarke, J. L., Viel, C., Chan, M., Tamsett, T. J., Treleaven, C. M., Bu, J., Sweet, L., Passini, M. A., Dodge, J. C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220464110 · Cited by 252
Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., YOSHIMASU, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 245
Identification of the Tau phosphorylation pattern that drives its aggregation
Despres, C., Byrne, C., Qi, H., Cantrelle, F., Huvent, I., Chambraud, B., Baulieu, É.-É., Jacquot, Y., Landrieu, I., Lippens, G. M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708448114 · Cited by 263
Ferrer, I., Blanco, R., Carmona, M., Ribera, R., Goutan, E., Puig, B., Rey, M. J., Cardozo, A., Viñals, F., & Ribalta, T. (2001) · Brain Pathology · doi:10.1111/j.1750-3639.2001.tb00387.x · Cited by 239
Insulin Dysfunction InducesIn VivoTau Hyperphosphorylation through Distinct Mechanisms
Planel, E., Tatebayashi, Y., Miyasaka, T., Liu, L., Wang, L., Herman, M., Yu, W. H., Luchsinger, J. A., Wadzinski, B. E., Duff, K., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3949-07.2007 · Cited by 242
Luna-Muñoz, J., Chávez-Macías, L., García-Sierra, F., & Mena, R. (2007) · Journal of Alzheimer's Disease · doi:10.3233/jad-2007-12410 · Cited by 233
Delacourte, A., Sergeant, N., Wattez, A., Gauvreau, D., & Robitaille, Y. (1998) · Annals of Neurology · doi:10.1002/ana.410430209 · Cited by 235
Schmidt, M., Zhukareva, V., Newell, K., Lee, V., & Trojanowski, J. (2001) · Acta Neuropathologica · doi:10.1007/s004010000330 · Cited by 230
Nagy, Z., Esiri, M. M., & Smith, A. D. (1997) · Acta Neuropathologica · doi:10.1007/s004010050617 · Cited by 225
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
Braak, H., & Braak, E. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050096 · Cited by 225
Hurtado, D. E., Molina-Porcel, L., Iba, M., Aboagye, A. K., Paul, S. M., Trojanowski, J. Q., & Lee, V. M.-Y. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.100346 · Cited by 222
P38 MAP kinase is activated at early stages in Alzheimer's disease brain
Sun, A. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00180-8 · Cited by 219
Xia, Y., Prokop, S., & Giasson, B. I. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00460-5 · Cited by 227
Bellucci, A., Westwood, A. J., Ingram, E., Casamenti, F., Goedert, M., & Spillantini, M. G. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63421-9 · Cited by 221
Self-citationRey, N. L., George, S., Steiner, J. A., Madaj, Z., Luk, K. C., Trojanowski, J. Q., Lee, V. M.-Y., & Brundin, P. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1792-9 · Cited by 215
Yeh, C., Vadhwana, B., Verkhratsky, A., & Rodriguez, J. J. (2011) · ASN NEURO · doi:10.1042/an20110025 · Cited by 221
Dayanandan, R., van Slegtenhorst, M., Mack, T. G. A., Ko, L., Yen, S. H., Leroy, K., Brion, J., Anderton, B. H., Hutton, M. L., & Lovestone, S. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00222-7 · Cited by 210
REVIEW: tau protein pathology in Alzheimer’s disease and related disorders
Tolnay, M., & Probst (1999) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.1999.00182.x · Cited by 214
Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., & Hisanaga, S.-I. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5927-11.2012 · Cited by 206
Kins, S., Crameri, A., Evans, D. R. H., Hemmings, B. A., Nitsch, R. M., & Götz, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102621200 · Cited by 203
Tau Phosphorylation at Serine 396 Residue Is Required for Hippocampal LTD
Regan, P., Piers, T., Yi, J.-H., Kim, D.-H., Huh, S., Park, S. J., Ryu, J. H., Whitcomb, D. J., & Cho, K. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2842-14.2015 · Cited by 202
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 & Experimental Neurology · doi:10.1093/jnen/64.2.104 · Cited by 199
Brion, J., Tremp, G. L., & Octave, J. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65272-8 · Cited by 203
Planel, E., Yasutake, K., Fujita, S. C., & Ishiguro, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102780200 · Cited by 201
Brückner, G., Hausen, D., Härtig, W., Drlicek, M., Arendt, T., & Brauer, K. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00071-8 · Cited by 196
Evolution of Alzheimer's disease-related cytoskeletal changes in the basal nucleus of Meynert
Sassin, I., Schultz, C., Thal, D. R., Rüb, U., Arai, K., Braak, E., & Braak, H. (2000) · Acta Neuropathologica · doi:10.1007/s004019900178 · Cited by 193
Waxman, E. A., & Giasson, B. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0297-11.2011 · Cited by 201
Pick's disease: hyperphosphorylated tau protein segregates to the somatoaxonal compartment
Probst, A., Tolnay, M., Langui, D., Goedert, M., & Spillantini, M. G. (1996) · Acta Neuropathologica · doi:10.1007/s004010050565 · Cited by 192
Self-citationTau 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
Anti‐tau antibody reduces insoluble tau and decreases brain atrophy
Yanamandra, K., Jiang, H., Mahan, T. E., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2015) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.176 · Cited by 185
Liu, B., Rasool, S., Yang, Z., Glabe, C. G., Schreiber, S. S., Ge, J., & Tan, Z. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.090159 · Cited by 182
Pathological Interface Between Oligomeric Alpha-Synuclein and Tau in Synucleinopathies
Sengupta, U., Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Lasagna‐Reeves, C. A., Gerson, J. E., Paulucci-Holthauzen, A. A., Krishnamurthy, S., Farhed, M., Jackson, G. R., & Kayed, R. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.12.019 · Cited by 187
Tauopathy-like Abnormalities and Neurologic Deficits in Mice Immunized With Neuronal Tau Protein
Rosenmann, H., Grigoriadis, N., Karussis, D., Boimel, M., Touloumi, O., Ovadia, H., & Abramsky, O. (2006) · Archives of Neurology · doi:10.1001/archneur.63.10.1459 · Cited by 178
Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
Boimel, M., Grigoriadis, N., Lourbopoulos, A., Haber, E., Abramsky, O., & Rosenmann, H. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.05.010 · Cited by 174
Yoshida, H., Watanabe, A., & Ihara, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9761 · Cited by 173
Bussière, T., Bard, F., Barbour, R., Grajeda, H., Guido, T., Khan, K., Schenk, D., Games, D., Seubert, P. A., & Buttini, M. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63360-3 · Cited by 170
Tapia‐Rojas, C., Aránguiz, F. C., Varela‐Nallar, L., & Inestrosa, N. C. (2015) · Brain Pathology · doi:10.1111/bpa.12255 · Cited by 176
. Identification of Alzheimer and vascular lesion thresholds for mixed dementia.
Gold, G., Giannakopoulos, P., Herrmann, F. R., Bouras, C., & Kovari, E. (2007) · Brain · doi:10.1093/brain/awm228 · Cited by 163
Thal, D. R., Holzer, M., Rüb, U., Waldmann, G., Günzel, S., Zedlick, D., & Schober, R. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7380 · Cited by 165
Tau and transgenic animal models
Götz, J. (2001) · Brain Research Reviews · doi:10.1016/s0165-0173(01)00055-8 · Cited by 166
Casein Kinase 1 Delta Phosphorylates Tau and Disrupts Its Binding to Microtubules
Li, G., Yin, H., & Kuret, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314116200 · Cited by 162
TauGene Mutation K257T Causes a Tauopathy Similar to Pick's Disease
Rizzini, C., Goedert, M., Hodges, J. R., Smith, M. J., Jakes, R., Hills, R., Xuereb, J. H., Crowther, R. A., & Spillantini, M. G. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.11.990 · Cited by 161
Self-citationPassive immunotherapies targeting Aβ and tau in Alzheimer's disease
Plotkin, S. S., & Cashman, N. R. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105010 · Cited by 161
Hasegawa, M., Jakes, R., Crowther, R. A., Lee, V. M.-Y., Ihara, Y., & Goedert, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00271-2 · Cited by 163
Self-citationBuée‐Scherrer, V., Condamines, O., Mourton-Gilles, C., Jakes, R., Goedert, M., Pau, B., & Delacourte, A. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(96)00003-4 · Cited by 161
Self-citationTauopathy with paired helical filaments in an aged chimpanzee
Rosen, R. F., Farberg, A. S., Gearing, M., Dooyema, J., M. Long, P., Anderson, D. C., Davis‐Turak, J., Coppola, G., Geschwind, D. H., Paré, J., et al. (2008) · Journal of Comparative Neurology · doi:10.1002/cne.21744 · Cited by 153
Koss, D. J., Jones, G., Cranston, A., Gardner, H., Kanaan, N. M., & Platt, B. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1632-3 · Cited by 155
Argyrophilic grain disease: A late‐onset dementia with distinctive features among tauopathies
Tolnay, M., & Clavaguera, F. (2004) · Neuropathology · doi:10.1111/j.1440-1789.2004.00591.x · Cited by 154
Truncation of CDK5 Activator p35 Induces Intensive Phosphorylation of Ser202/Thr205 of Human Tau
Hashiguchi, M., Saito, T., Hisanaga, S., & Hashiguchi, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207426200 · Cited by 149
Basurto‐Islas, G., Luna‐Muñoz, J., Guillozet-Bongaarts, A. L., Binder, L. I., Mena, R., & García‐Sierra, F. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31817275c7 · Cited by 163
Braak, H., & Del Tredici, K. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhy152 · Cited by 148
Ardiles, Á. O., Tapia‐Rojas, C., Mandal, M., Alexandre, F., Kirkwood, A., Inestrosa, N. C., & Palacios, A. G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201209109 · Cited by 152
Metadata
- Authors
- Goedert, M., Jakes, R., & Vanmechelen, E.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Fujirebio (Belgium) (BE)
- Corresponding author
- Goedert, M.
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1995-04
- Volume
- 189
- Issue
- 3
- Pages
- 167-170
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2062772621
- Cited by
- 608
- References
- 24
- Citations by year
- 2026: 36 · 2025: 33 · 2024: 20 · 2023: 30 · 2022: 27 · 2021: 26 · 2020: 20 · 2019: 20 · 2018: 20 · 2017: 15 · 2016: 12 · 2015: 22 · 2014: 12 · 2013: 17 · 2012: 14
- FWCI
- 11.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tau phosphorylation, paired helical filaments, Alzheimer's disease, anti-tau antibodies, site-directed mutagenesis, in vitro phosphorylation
- MeSH terms
- Amino Acid Sequence, Antibodies, Monoclonal, Cloning, Molecular, Escherichia coli, Humans, Molecular Sequence Data, Phosphorylation, Protein Kinases, Recombinant Proteins, Serine, Threonine, tau Proteins, DNA, Complementary
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 ›
Are you an author, or do you see a problem with this page? Request a review