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Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
Abstract
We have investigated ubiquitinated paired helical filaments, which produce a proteinaceous smear in SDS-polyacrylamide gel electrophoresis and immunoblotting. The smear consisted largely of the carboxy-terminal portion of tau and ubiquitin. The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region. Most ubiquitin in paired helical filaments occurred as a monoubiquitinated form, and only a small proportion of ubiquitin formed multiubiquitin chains. There was a ubiquitin-negative smear, in which tau was much less processed in the amino-terminal portion. This strongly suggests that the amino-terminal processing of tau in paired helical filaments precedes its ubiquitination.
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“Accumulation of ubiquitin-conjugated tau at Lys254, 257, 290, 311, 317 and 353 has been identified in PHF from AD brain and in an AD mouse model [161, 163, 164].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [163]
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“Therefore, ubiquitination plays an important role in maintaining a pool of cellular tau under physiological conditions.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [163]
Citations
Cites
The molecular pathology of Alzheimer's disease
Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708
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
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATION
Hershko, A., & Ciechanover, A. J. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.003553 · Cited by 1,448
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
Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134
Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037
Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939
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
Self-citationGreenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 735
Research works printed but not linked: 1
- DeCarli, 1992, Post-mortem regional neurofibrillary tangle densities but not senile plaque densities are related to regional cerebral metabolic rates for glucose during life in Alzheimer's disease patients, Neurodegeneration, 1, 113
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Jian, C., Lv, H., Wei, G., Guo, C.-S., Deng, Y.-F., Jiang, Y., & Gao, C. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.264473 · Cited by 22
Chadwick, L., Gentle, L., Strachan, J., & Layfield, R. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01236.x · Cited by 22
Akaishi, T., Shiomi, T., Sawada, H., & Yokosawa, H. (1996) · Brain Research · doi:10.1016/0006-8993(96)00212-0 · Cited by 22
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Jia, F., & Fu, L. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04739-2 · Cited by 21
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Papanikolopoulou, K., & Skoulakis, E. M. C. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_7 · Cited by 23
New Age of Neuroproteomics in Alzheimer’s Disease Research
Kováčech, B., Žilka, N., & Novák, M. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9358-6 · Cited by 22
Flann, S., Hawkes, R. B., Riederer, B. M., Rider, C. C., & Beesley, P. W. (1997) · Neuroscience · doi:10.1016/s0306-4522(97)00196-6 · Cited by 21
Activity-dependent tau cleavage by caspase-3 promotes neuronal dysfunction and synaptotoxicity
Opland, C. K., Bryan, M. R., Harris, B., McGillion-Moore, J., Tian, X., Chen, Y., Itano, M. S., Diering, G. H., Meeker, R. B., & Cohen, T. J. (2023) · iScience · doi:10.1016/j.isci.2023.106905 · Cited by 21
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Cecarini, V., Bonfili, L., Cuccioloni, M., Mozzicafreddo, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2238-6 · Cited by 21
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Hasegawa, M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_2 · Cited by 22
Self-citationShaeffer, J. R., & Cohen, R. E. (1997) · Blood · doi:10.1182/blood.v90.3.1300 · Cited by 20
Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP
Parolini, F., Kachoie, E. A., Leo, G., Civiero, L., Bubacco, L., Arrigoni, G., Munari, F., Assfalg, M., D’Onofrio, M., & Capaldi, S. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202310230 · Cited by 18
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Feligioni, M., Marcelli, S., Knock, E., Nadeem, U., Arancio, O., & Fraser, P. E. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.4.382 · Cited by 19
Shimada, Y., Fukuda, T., Aoki, K., Yukawa, T., Iwamuro, S., Ohkawa, K., & Takada, K. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.02.031 · Cited by 19
Recent advances in experimental modeling of the assembly of tau filaments
Ko, L., Deture, M. A., Sahara, N., Chihab, R., Vega, I. E., & Yen, S.-H. C. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.004 · Cited by 19
Trivellato, D., Floriani, F., Barracchia, C. G., Munari, F., D’Onofrio, M., & Assfalg, M. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106347 · Cited by 18
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Nguyen, H. D., Kim, W.-K., & Vu, G. H. (2024) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2024.111930 · Cited by 17
Pérez, M., Medina, M., Hernández, F., & Ávila, J. (2018) · BioMolecular Concepts · doi:10.1515/bmc-2018-0001 · Cited by 20
Probing modifications of the neuronal cytoskeleton
Doering, L. C. (1993) · Molecular Neurobiology · doi:10.1007/bf02769179 · Cited by 18
Hol, E. M., Neubauer, A., de Kleijn, D. P. V., Sluijs, J. A., Ramdjielal, R. D. J., Sonnemans, M. A. F., & van Leeuwen, F. W. (1998) · Progress in brain research · doi:10.1016/s0079-6123(08)64028-5 · Cited by 18
Damage control – a possible non‐proteolytic role for ubiquitin in limiting neurodegeneration
Gray, D. A. (2001) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2001.00321.x · Cited by 17
Masuda‐Suzukake, M., Suzuki, G., Hosokawa, M., Nonaka, T., Goedert, M., & Hasegawa, M. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa091 · Cited by 16
Self-citationManipulation of microglial activity as a therapy for Alzheimer s disease
Ling, E. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s342 · Cited by 15
Thomas, S. N., & Yang, A. J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_10 · Cited by 15
Guarascio, R., Salih, D. A. M., Yasvoina, M. V., Edwards, F. A., Cheetham, M. E., & van der Spuy, J. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz255 · Cited by 16
Regulation of Tau Homeostasis and Toxicity by Acetylation
Tracy, T. E., Claiborn, K. C., & Gan, L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_4 · Cited by 17
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Kuusisto, E. (2004) · Cited by 16
Baldensperger, T., Preissler, M., & Becker, C. F. W. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00221k · Cited by 17
Guan, P.-P., & Wang, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03277-z · Cited by 15
Vulnerabilities in the Tau Network and the Role of Ultrasensitive Points in Tau Pathophysiology
Yuraszeck, T. M., Neveu, P. A., Rodriguez-Fernández, M., Robinson, A. S., Kosik, K. S., & Doyle, F. J. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000997 · Cited by 15
Masaki, T., Ishiura, S., Sugita, H., & Kwak, S. (1994) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(94)90288-7 · Cited by 15
Robinson, P. A., Leek, J. P., Thompson, J., Carr, I., Bailey, A., Moynihan, T. P., Coletta, P. L., Lench, N., & Markham, A. F. (1995) · Mammalian Genome · doi:10.1007/bf00354295 · Cited by 15
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Shinohara, M., Hirokawa, J., Shimodaira, A., Tashiro, Y., Suzuki, K., Gheni, G., Fukumori, A., Matsubara, T., Morishima, M., Saito, Y., et al. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab047 · Cited by 16
Ibarra-Bracamontes, V., Escobar‐Herrera, J., Krištofíková, Z., Řı́pová, D., Florán, B., & García‐Sierra, F. (2020) · Brain Research · doi:10.1016/j.brainres.2020.146953 · Cited by 14
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van Leeuwen, F. W., Fischer, D. F., Benne, R., & Hol, E. M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06654.x · Cited by 14
Modeling tauopathy: a range of complementary approaches
Hall, G. F., & Yao, J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.002 · Cited by 14
Biological markers in Alzheimer's disease
Grundke, I., Rolkova, G., Konstekova, E., & Iqbal, K. (2006) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.1007/bf03656854 · Cited by 13
Disruption of ubiquitin-mediated processes in diseases of the brain and bone
Layfield, R., & Searle, M. S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360469 · Cited by 12
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Corbo, C. P., & Alonso, A. D. C. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385506-0.00002-8 · Cited by 13
Park, H., Yamanaka, T., Toyama, Y., Fujita, A., Doi, H., Nirasawa, T., Murayama, S., Matsumoto, N., Shimogori, T., Ikegawa, M., et al. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01333-8 · Cited by 11
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Kumar, A., Rosa, F. G. L., Hovland, A. R., Cole, W. C., Edwards‐Prasad, J., & Prasad, K. N. (1999) · Neurochemical Research · doi:10.1023/a:1020912704404 · Cited by 10
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Catalina, M. O., Bermejo, M. C., Argent, R., Alonso, J. C., Cuenda, A., Lorenzo, M. J. V., & Centeno, F. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25579 · Cited by 10
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Ford, L. K., Fioriti, L., & Kandel, E. R. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.195 · Cited by 10
van Leeuwen, F. W., & Hol, E. M. (1999) · Springer eBooks · doi:10.1007/978-3-7091-6380-1_9 · Cited by 10
Layfield, R. (2001) · Medical Hypotheses · doi:10.1054/mehy.2000.1198 · Cited by 10
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain
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Franklin, K., Layfield, R., Landon, M., Ramage, R., Brown, A. R., Love, S. G., Muir, T. W., Urquhart, K., Bownes, M., & Mayer, R. J. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2099 · Cited by 9
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Alstyne, M. V., Pratt, J., & Parker, R. (2025) · Genes & Development · doi:10.1101/gad.352551.124 · Cited by 11
Bryan, M. R., Tian, X., Tseng, J., Evangelista, B., Ragusa, J. V., Bryan, A. F., Trotman, W., Irwin, D. J., & Cohen, T. J. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01865-1 · Cited by 10
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Almeida, M. C., & Carrettiero, D. C. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-64074-1.00044-6 · Cited by 8
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Self-citationHall, G. F. (1999) · Journal of Alzheimer s Disease · doi:10.3233/jad-1999-1603 · Cited by 7
Yuzwa, S. A., & Vocadlo, D. J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_13 · Cited by 7
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Viola, G., Trivellato, D., Meulli, L., Tira, R., Lauriola, A., Munari, F., Montagnana, M., Buffelli, M., Assfalg, M., & D’Onofrio, M. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107549 · Cited by 6
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Hall, G. F. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-788-0_15 · Cited by 6
Kang, T., Kim, J. H., Hong, I., Park, N., Heinsen, H., Lee, J., Ravid, R., Ferrer, I., Yoo, J. S., Kwon, K., et al. (2014) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-014-7933-2 · Cited by 6
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Goedert, M. (2011) · Wiley eBooks · doi:10.1002/9781444341256.ch13 · Cited by 6
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Broc, J., Piersson, C., & Fichou, Y. (2025) · FEBS Letters · doi:10.1002/1873-3468.70022 · Cited by 5
Tabassum, Z., Tseng, J., Isemann, C., Tian, X., Chen, Y., Herring, L. E., & Cohen, T. J. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101977 · Cited by 5
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Volbracht, C., & Fog, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262211062 · Cited by 4
Munari, F., Barracchia, C. G., Franchin, C., Parolini, F., Capaldi, S., Romeo, A., Bubacco, L., Assfalg, M., Arrigoni, G., & D’Onofrio, M. (2020) · Angewandte Chemie · doi:10.1002/ange.201916756 · Cited by 4
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McFarlane, O., Kozakiewicz, M., Wojciechowska, M., & Kędziora–Kornatowska, K. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45030160 · Cited by 4
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Šoltýs, K., Rolkova, G., Vechterova, L., Filipčík, P., Žilka, N., Kontseková, E., & Novák, M. (2005) · Neuroreport · doi:10.1097/01.wnr.0000181582.95764.79 · Cited by 4
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Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.02.001 · Cited by 4
Salinas, M. D., Martínez, I. M., Naranjo, E., Molina, M. L., Cuervo, A. M., Muller, S., & Valdor, R. (2026) · Autophagy · doi:10.1080/15548627.2026.2672700 · Cited by 3
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Nordbeck, A. J., Sharma, B., Garcia, C. A., & Tseng, J. (2026) · Frontiers in Dementia · doi:10.3389/frdem.2026.1834737 · Cited by 3
Stimulation of Tau Degradation
Quintanilla, R. A., Cabezas-Opazo, F., Pallo, S. P., Chesser, A. S., & Johnson, G. V. W. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00013-7 · Cited by 3
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Chen, X., Reichert, M. C., & Gan, L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802851-3.00005-x · Cited by 3
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Ihara, Y. (1994) · Archives of Gerontology and Geriatrics · doi:10.1016/0167-4943(94)90032-9 · Cited by 3
Self-citationHarrington, C. R., & Wischik, C. M. (1995) · International Review of Psychiatry · doi:10.3109/09540269509022988 · Cited by 3
τ Protein and the Neurofibrillary Pathology of Alzheimer’s Disease
Goedert, M., Trojanowski, J. Q., & Lee, V. M. ‐. (1997) · Humana Press eBooks · doi:10.1007/978-1-59259-471-9_12 · Cited by 3
Kano, M., 妙子, 木., Yanagisawa, H., Yamashita, K., Tatsumi, L., Sakai, A., Li, X., Saido, T. C., Saito, T., Takatori, S., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02407-7 · Cited by 2
Yasuaki, K. U. B. O., Kaidzu, S., Nakajima, I., Takenouchi, K., & NAKAMURA, F. (2000) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1290/1071-2690(2000)036 · Cited by 133
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Goto, S. (1994) · Archives of Gerontology and Geriatrics · doi:10.1016/0167-4943(94)90037-x · Cited by 2
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Wischik, C. M., Harrington, C. R., Lai, R. Y. K., Mukaetova-Ladinska, E. B., Xuereb, J. H., Gertz, H., Wischik, D., Edwards, P. C., Mena, R., & Roth, M. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00040-l · Cited by 2
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Kaur, V., & Sunkaria, A. (2025) · Behavioural Brain Research · doi:10.1016/j.bbr.2025.115505 · Cited by 1
Urschbach, M., Huhmann, S., Appel, D., Ferrari, L., Vogl, D. P., Martens, S., & Becker, C. F. W. (2025) · Angewandte Chemie · doi:10.1002/ange.202502638 · Cited by 1
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Sahoo, S., Padhy, A. A., Shivani, K., Misra, A., & Mishra, P. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253046 · Cited by 1
Oosterlynck, M., Fichter, L., Leroux, É., Eddarkaoui, S., Bouillet, T., Lefebvre, C., Nguyen, M., Maurage, C., Accart, B., Dupré, E., et al. (2026) · Journal of Biomedical Science · doi:10.1186/s12929-026-01250-1 · Cited by 1
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Mandelkow�, E., Friedhoff, P., Biernat, J., & Mandelkow, E. (1998) · Advances in behavioral biology · doi:10.1007/978-1-4615-5337-3_32 · Cited by 1
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Rofina, J., Eerdenburg, F. J. C. M. V., & Gruys, E. (2007) · Utrecht University Repository (Utrecht University) · Cited by 1
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Harrington, C. R. (2001) · Elsevier eBooks · doi:10.1016/b978-044450811-9/50030-6 · Cited by 1
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Hasegawa, M., Arai, T., Nonaka, T., Kametani, F., Yoshida, M., Hashizume, Y., Beach, T. G., Morita, M., Nakano, I., Oda, T., et al. (2008) · Rinsho Shinkeigaku · doi:10.5692/clinicalneurol.48.994 · Cited by 1
Self-citationSergeant, N., & Buée, L. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-6787-9_4 · Cited by 1
Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP
Parolini, F., Kachoie, E. A., Leo, G., Civiero, L., Bubacco, L., Arrigoni, G., Munari, F., Assfalg, M., D’Onofrio, M., & Capaldi, S. (2023) · Angewandte Chemie · doi:10.1002/ange.202310230 · Cited by 1
ATP-Dependent Proteases: The Cell's Degradation Machines
Bhattacharyya, S., Wilmington, S. R., & Matouschek, A. T. (2011) · Cambridge University Press eBooks · doi:10.1017/cbo9781139003704.014 · Cited by 1
Ubiquitination and SUMOylation of Amyloid and Amyloid-like Proteins in Health and Disease
Ford, L. K., Fioriti, L., & Kandel, E. R. (2019) · Caister Academic Press eBooks · doi:10.21775/9781912530120.25 · Cited by 1
Phosphorylation of Tau and Its Relationship with Alzheimer Paired Helical Filaments
Mandelkow�, E., Biernat, J., Lichtenberg-Kraag, B., Drewes, G., Wille, H., Gustke, N., Baumann, K., & Mandelkow�, E. (1995) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-79423-0_10 · Cited by 1
Posttranslational Modifications of the Tau in PHF: Phosphorylation and Ubiquitination
Morishima‐Kawashima, M., & Ihara, Y. (1995) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-79423-0_11 · Cited by 1
Self-citationGlial Changes in Aging and Alzheimer’s Disease
Morán, M. A., & Gómez‐Ramos, P. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5737-1_19 · Cited by 1
Tau and α-Synuclein in Neurodegenerative Diseases
Giasson, B. I., Wilson, C., Trojanowski, J. Q., & Lee, V. M. ‐. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-006-3_7 · Cited by 1
Choi, R. S. (2010) · Eukaryon · Cited by 1
Yeast as a Model for Studying Aβ Aggregation, Toxicity and Clearance
Bharadwaj, P. (2011) · Australasian Journal of Paramedicine · Cited by 1
Liu, K., Jones, S., Minis, A., Rodriguez, J., Molina, H., & Steller, H. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/364463 · Cited by 1
Tsagkogianni, C., Trivisonno, M., Willner, J. S., Garcia-Molinero, C., Tang, Y., Mattina, B., Latorre‐Leal, M., Wang, W., Roussarie, J.-P., & Rodriguez‐Rodriguez, P. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.15.711617 · Cited by 1
Mutant ubiquitin and the proteasome in Alzheimer's disease
de Vrij, F. M. S. (2005) · UvA-DARE (University of Amsterdam)
Grinberg, L. T. (2006) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2006.tde-04042007-082907
Metadata
- Authors
- Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y.
- Affiliations
- The University of Tokyo (JP)
- RIKEN (JP)
- Fujita Health University (JP)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 10
- Issue
- 6
- Pages
- 1151-1160
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2012781495
- Cited by
- 332
- References
- 45
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 6 · 2023: 9 · 2022: 9 · 2021: 10 · 2020: 14 · 2019: 9 · 2018: 8 · 2017: 7 · 2016: 13 · 2015: 9 · 2014: 10 · 2013: 3 · 2012: 10
- FWCI
- 10.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Ministry of Health and Welfare
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- ubiquitin, tau protein, paired helical filaments, ubiquitination, microtubule-binding region, protein aggregation, Alzheimer's disease, ubiquitin chains, post-translational modification
- MeSH terms
- Amino Acid Sequence, Antibodies, Monoclonal, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Humans, Microtubules, Molecular Sequence Data, Molecular Weight, Peptide Fragments, Peptide Mapping, Endopeptidases, Protein Binding, Mass Spectrometry, Ubiquitins, Neurofibrillary Tangles, tau Proteins
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