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Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.
Open accessAbstract
We have expressed six previously cloned isoforms of human microtubule-associated tau protein in Escherichia coli and purified them to homogeneity in a biologically active form. They range from 352 to 441 amino acids in length and differ from each other by the presence of three or four tandem repeats in the carboxy-terminal half and by the presence or absence of 29 or 58 amino acid inserts in the amino-terminus. When mixed together they gave a set of six bands on SDS-PAGE gels with apparent molecular weights of 48-67 kd and with a characteristic pattern of spacings. Four of these bands aligned with the major tau bands found in adult human cerebral cortex following perchloric acid extraction and alkaline phosphatase treatment. They consisted of isoforms with three repeats and no insertions, four repeats and no amino-terminal insertions and three- and four-repeat containing isoforms with the 29 amino acid insertion. In fetal human brain extracts treated with alkaline phosphatase one of the two major tau bands aligned with the three-repeat containing isoform with no insertions, whereas the molecular nature of the second major tau band remains to be established. The recombinant tau isoforms were biologically active at micromolar concentrations, as assessed by their ability to promote microtubule assembly. The rates of assembly were 2.5-3.0 times faster for isoforms containing four repeats when compared with three-repeat containing isoforms, with no significant contribution by the amino-terminal insertions.
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“Since tau binds to microtubules through C-terminal repeats within the microtubule-binding domain, 4R tau isoforms show a higher propensity to promote microtubule assembly compared to 3R tau isoforms [122, 123].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [123]
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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
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
[6] Use of T7 RNA polymerase to direct expression of cloned genes
Studier, F. W., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562
Matsudaira, P. T. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61070-1 · Cited by 4,951
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
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-citationMicrotubule-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
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588
Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491
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
Self-citation
Research works printed but not linked: 7
- Goedert,M., Wischik,C.M., Crowther,R.A., Walker,J.E. and Klug,A. (1988) Proc. Natl. Acad. Sci. USA, 85, 4051-4055.
- Hirel,P.H., Schmitter,J.M., Dessen,P., Fayat,G. and Blanquet,S. (1989) Proc. Natl. Acad. Sci. USA, 86, 8247-8251.
- Kosik,K.S., Joachim,C.L. and Selkoe,D.J. (1986) Proc. Natl. Acad. Sci. USA, 83, 4044-4048.
- Weingarten,M.D., Lockwood,A.H., Hwo,S.Y. and Kirschner,M.W. (1975) Proc. Natl. Acad. Sci. USA, 72, 1858-1862.
- Wischik,C.M., Novak,M., Th0gersen,H.C., Edwards,P.C., Runswick,M.J., Jakes,R., Walker,J.E., Milstein,C., Roth,M. and Klug,A. (1988a) Proc. Natl. Acad. Sci. USA, 85, 4506-4510.
- Wischik,C.M., Novak,M., Edwards,P.C., Klug,A., Tichelaar,W. and Crowther,R.A. (1988b) Proc. Natl. Acad. Sci. USA, 85, 4884-4888.
- Wood,J.G., Mirra,S.S., Pollock,N.J. and Binder,L.I. (1986) Proc. Natl. Acad. Sci. USA, 83, 4040-4043. Received on August 28, 1990 4230 14602075, 1990, 13, Downloaded from https://www.embopress.org/doi/10.1002/j.1460-2075.1990.tb07870.x by Readcube (Labtiva Inc.), Wiley Online Library on [14/08/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License · DOI
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Items 701–800 of 929
Selective dimerization of cysteines in glycopeptides and phosphopeptides
Hoffmann, R., & Ötvös, L. (1997) · Letters in Peptide Science · doi:10.1007/bf00127968 · Cited by 7
Misfolded proteins as a therapeutic target in Alzheimer's disease
Liyanage, S. I., & Weaver, D. F. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.003 · Cited by 8
Modulated induction of tau proteins in cultured human neuroblastoma cells
Ko, L., Liu, W.-K., Georgieff, I. S., & Yen, S.-H. C. (1996) · Brain Research · doi:10.1016/0006-8993(95)01268-0 · Cited by 7
Halverson, R. A., Chambers, C. B., & Muma, N. A. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7637 · Cited by 7
Aggidis, A., Chatterjee, S., Townsend, D. J., Fullwood, N. J., Ortega, E. R., Tarutani, A., Hasegawa, M., Lucas, H., Mudher, A. K., & Allsop, D. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.04.447069 · Cited by 9
Hedna, R., Maio, A. D., Robin, M., Allegro, D., Tatoni, M., Peyrot, V., Barbier, P., Kovacic, H., & Breuzard, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015050 · Cited by 6
“In adults, there are six predominant Tau isoforms, resulting from alternative splicing of mRNA of a single gene MAPT , each with three or four microtubule-binding repeats located in the C-terminal half of the protein, and with zero to two inserts located in the N-terminal portion [15].”
BackgroundIlluminating Tau Aggregates: Multiscale Approaches for Detection, Imaging, and Understanding
Bhuskute, K. R., Fan, J., & Kaur, A. (2025) · Aggregate · doi:10.1002/agt2.70133 · Cited by 6
“During neurodevelopment, the brain is predominantly populated by the 3R isoforms, whereas the balanced expression of 3R and 4R isoforms is characteristic of the adult brain [35, 36].”
Shiravi, S., Yufa, A., Papavasileiou, P., Lotz, S., Murphy, D., Bertucci, T. B., Temple, S., & Finan, J. D. (2025) · Journal of Neurotrauma · doi:10.1177/08977151251374286 · Cited by 6
“55 Microtubule fracture is an important initiating pathology in neurotrauma 56 and stabilizing microtubules with taxol protects them against trauma in vitro.”
Finding MAPT Mutations in Frontotemporal Dementia and Other Tauopathies
Dobson‐Stone, C., & Kwok, J. B. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_19 · Cited by 6
“3R and 4R tau differ in their interaction strength with microtubules [6] and the concentrations of 3R and 4R tau are roughly equal in normal adult brain [7].”
BackgroundGazarian, K. G., Ramírez-García, L. R., Orozco, L. T., Luna‐Muñoz, J., & Pacheco‐Herrero, M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.612657 · Cited by 6
“An RT-PCR assay (Figure 2B) revealed the RNA copies of MAPT gene known to encode the amino acid sequences of the six tau isoforms in the brain of AD persons (66, 67).”
MethodZou, Y. F., Qi, B., Tan, J., Guan, L., Zhang, Q., Sun, Y., & Huang, F. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00434 · Cited by 6
Yakout, D. W., Shroff, A., Wei, W., Thaker, V. S., Allen, Z. D., Sajish, M., Nazarko, T. Y., & Mabb, A. M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107237 · Cited by 8
“5 to 3 times faster compared to 3R isoforms (97).”
Zhu, T., Xu, F., Zhang, L., Zhang, Y., Yang, C., Cheng, M., Chen, F., & Wang, K. (2017) · Oncotarget · doi:10.18632/oncotarget.19686 · Cited by 6
“Tau protein interacts with tubulin to stabilize microtubules [9] and binds to the inner and outer surfaces of microtubules.”
BackgroundAlterations of cytoskeletal tau protein of SH-SY5Y human neuroblastoma cells after exposure to MPTP.
Song, X., & Ehrich, M. F. (1998) · PubMed · Cited by 6
Kenner, L., Zatloukal, K., Stumptner, C., Eferl, R., & Denk, H. (1999) · Hepatology · doi:10.1002/hep.510290325 · Cited by 6
Introduction to the Tauopathies
Goedert, M. (2011) · Wiley eBooks · doi:10.1002/9781444341256.ch13 · Cited by 6
Self-citationControl of microtubule polymerization and stability
Ávila, J., & Díaz‐Nido, J. (1995) · The Cytoskeleton · doi:10.1016/s1874-6020(06)80005-4 · Cited by 6
Shang, H., Duan, M., Da, C., Fu, X., & Zhang, T. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144651 · Cited by 5
Rational Modulation of Liquid–Liquid Phase Separation Offers Novel Ways to Combat Tauopathies
Zhang, X., Wang, L., Lin, N., Gao, M. Y., & Huang, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146709 · Cited by 7
“Since the 4R tau isoforms contain one more binding repeat than the 3R isoforms, the 4R tau isoforms show a higher affinity for microtubules and promote microtubule assembly more efficiently [45].”
Progressive Supranuclear Palsy
Morris, H. R. (2009) · Blue books of neurology · doi:10.1016/b978-1-4160-6641-5.00021-0 · Cited by 5
Hassan, M. S. O., Vahid, A. A., Sahayaraj, A. E., Viswanathan, R., & Vijayan, V. (2023) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.3c00912 · Cited by 5
Villa-González, M., & Pérez-Álvarez, M. J. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.313027 · Cited by 5
“3R-Tau, which has lost exon 10, has three microtubule-binding 2402 ｜NEURAL REGENERATION RESEARCH｜Vol 16｜No. 12｜December 2021 domains, thus making its binding to microtubules more labile and conferring greater dynamism to the cytoskeleton network (Goedert and Jakes, 1990).”
BackgroundInfluentialFenouil, T., Fourier, A., Quadrio, I., Streichenberger, N., Bernardini, S., Zima, T., Perret‐Liaudet, A., & Meyronet, D. (2019) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2019.06.004 · Cited by 5
Abeta(1-42) induces abnormal alternative splicing of tau exons 2/3 in NGF-induced PC12 cells
LAGUNES, T., Herrera-Rivero, M., Hernández‐Aguilar, M. E., & Aranda-Abreu, G. E. (2014) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765201420130333 · Cited by 5
“Six tau isoforms ranging from 352 to 441 amino acid residues are found in the human brain (Goedert and Jakes 1990) as a result of the alternative splicing of exons 2, 3 and 10 (Figure 1) (Andreadis et al.”
BackgroundBush, M. S., Eagles, P. A. M., & Gordon‐Weeks, P. R. (1996) · The Cytoskeleton · doi:10.1016/s1874-6020(96)80009-7 · Cited by 5
Quick purification of recombinant human truncated tau proteins for immunoanalysis
Kontseková, E., Cattaneo, A., & Novák, M. (1995) · Journal of Immunological Methods · doi:10.1016/0022-1759(95)00120-y · Cited by 5
Prasad, V., Jordan, M. A., & Ludueña, R. F. (1992) · Journal of Protein Chemistry · doi:10.1007/bf01025028 · Cited by 5
SUMO2 Protects Against Tau-induced Synaptic and Cognitive DysfunctionPreprint
Orsini, F., Argyrousi, E. K., Restelli, E., Ford, L. K., Takamura, H., Matsuzaki, S., Zentilin, L., Pascente, R., Kanaan, N. M., Soni, R. K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.11.516192 · Cited by 5
Zhou, X., Lu, Y., Cui, X., Li, N., Wei, Y., Li, H., & Feng, L. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c02255 · Cited by 4
Tau and Alzheimer’s Disease: Molecular Mechanisms and Treatment Approaches
Reiss, A. B., Muhieddine, D., Leon, A. Z. D., Voloshyna, I., Gomolin, I. H., & Pinkhasov, A. (2021) · SN Comprehensive Clinical Medicine · doi:10.1007/s42399-021-01092-y · Cited by 4
Smith, E. D., Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2025) · NeuroMolecular Medicine · doi:10.1007/s12017-025-08850-4 · Cited by 7
“cDNAs encoding the 6 full-length human tau isoforms were cloned into bacterial expression vector pRK172, expressed in Escherichia coli , and purified by Mono S chromatography as previously described (Giasson et al., 2003; Goedert & Jakes, 1990; Hong et al., 1998; Waxman & Giasson, 2011).”
Dickerson, B. C. (2015) · Cambridge University Press eBooks · doi:10.1017/cbo9781316091586.016 · Cited by 4
Cooper, G. L., Huseby, C. J., Chandler, C. N., Cocuron, J., Alonso, A. P., & Kuret, J. (2018) · Analytical Biochemistry · doi:10.1016/j.ab.2018.01.018 · Cited by 4
“(A) Coomassie-blue stained SDS-PAGE gel of input protein standards calmodulin (lane 1, 1 μg), MBP (lane 2, 2 μg) and mixed histones (lane 3, 3 μg).”
BackgroundInfluentialChaudhary, N., & Nagaraj, R. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_4 · Cited by 4
Chemical Genetic Identification of PKC Epsilon Substrates in Mouse Brain
Dugan, M. P., Ferguson, L. B., Hertz, N. T., Chalkley, R. J., Burlingame, A. L., Shokat, K. M., Parker, P. J., & Messing, R. O. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100522 · Cited by 5
“Tau is abundant in neurons, plays a primary role in the assembly and stabilization of microtubules, and is key to the pathogenesis of several neurodegenerative disorders known as tauopathies (101 – 103).”
[Phosphorylation of tau and Alzheimer's disease].
García, T., & Jay, D. (2004) · PubMed · Cited by 4
Genetics of Alzheimer´S Disease
Campos‐Peña, V., Gmez, R., & Antônio, M. (2014) · InTech eBooks · doi:10.5772/58286 · Cited by 5
“Each isoform differs from each other by the presence or absence of a 29-aminoacid or 58-aminoacid inserts in the amino-terminal half and by the inclusion or not in the carboxy-terminal half of the protein of a 31-aminoacid repeat encoded by exon 10 of MAPT [25, 29-30].”
BackgroundMolecular Pathobiology of Alzheimer’s Disease
Harrington, C. R., & Wischik, C. M. (1994) · Springer eBooks · doi:10.1007/978-1-4615-6805-6_13 · Cited by 4
Polled Intersex Syndrome and Polledness in Goats: Molecular Aspects
Szatkowska, I., Udała, J., Zaborski, D., Czerniawska‐Piątkowska, E., Grzesiak, W., Wasielewska, M., & Wójcik, J. (2023) · Pakistan Journal of Zoology · doi:10.17582/journal.pjz/20220129110121 · Cited by 3
14-3-3ζ protein prevents formation of GSK3β-phosphorylated Tau protein fibrils
Kučinskas, G., Kozeleková, A., Králová, K., Volko, V., Šedo, O., & Hritz, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148222 · Cited by 4
Multivalency in Tau–Microtubule Interactions: Heterogeneous Association and Functional Implications
Naveh-Tassa, S., & Levy, Y. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169600 · Cited by 3
Polymerization of recombinant tau core fragments in vitro and seeding studies in cultured cells
Paterno, G., Bell, B. M., Riley-DiPaolo, A., LaVoie, M. J., & Giasson, B. I. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1268360 · Cited by 3
“Additionally, 3R tau isoforms also exhibit decreased affinity for MTs compared to 4R (Goedert and Jakes, 1990; Xia et al., 2021), lending credence to the hypothesis that MT dissociated tau is perhaps causal for aggregation.”
BackgroundMethodZhang, P., Taghavi, A., Abe, M., Aikawa, H., Akahori, Y., Chen, J. L., Tong, Y., Baisden, J. T., Cameron, M. D., Childs‐Disney, J. L., et al. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00260 · Cited by 3
Rotake, D. R., Patle, S. K., & Singh, S. G. (2024) · Smart nanomaterials technology · doi:10.1007/978-981-99-6597-7_12 · Cited by 3
Relave, E. T., Hedna, R., Maio, A. D., Devred, F., Kovacic, H., Robin, M., & Breuzard, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111785 · Cited by 3
“In adults, the alternative splicing of mRNA of a single gene MAPT can generate six predominant Tau isoforms, each with three or four MT-binding repeats located in the C -terminal half of the protein, and with zero to two inserts located in the N-terminal region [3].”
BackgroundFrontotemporal dementia with parkinsonism linked to Chromosome 17
Forman, M. S., Lee, V. M. ‐., & Trojanowski, J. Q. (2005) · Cambridge University Press eBooks · doi:10.1017/cbo9780511544873.036 · Cited by 3
Brion, J., Couck, A. M., Conreur, J.-L., & Octave, J. N. (1995) · Springer eBooks · doi:10.1007/978-3-642-79423-0_13 · Cited by 3
Regulation of tau exon 10 splicing by a double stem–loop structure in mouse intron 10
Yamashita, T., Tomiyama, T., Li, Q., Numata, H., & Mori, H. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.11.090 · Cited by 3
“microtubules more avidly than 3R-tau due to its additional microtubule-binding domain encoded with E10 [5,6].”
BackgroundTau Protein in Drug-Resistant Epilepsy and Cognitive Decline
Thom, M., & Koepp, M. J. (2021) · Progress in inflammation research · doi:10.1007/978-3-030-67403-8_7 · Cited by 3
Development of the Axonal and Dendritic Cytoskeleton
Riederer, B. M. (1995) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60261-1 · Cited by 3
Ayubcha, C., Moghbel, M. C., Borja, A. J., Newberg, A. B., Werner, T. J., Alavi, A. A., & Revheim, M.-E. R. (2021) · PET Clinics · doi:10.1016/j.cpet.2020.12.009 · Cited by 3
“The 3R and 4R isoforms are equally expressed in the cerebral cortex of healthy adults(8); otherwise, there is a notable discrepancy in the prevalence of N-terminal variants; for example, 0N, 1N, and 2N tau represent 40%, 50%, and 10% of the total CNS tau, respectively.(9) With respect to the proportions of tau protein…”
BackgroundThe microtubule cytoskeleton in neuronal development and degeneration
Ávila, J., Correas, I., de Ancos, J. G., Ledesma, D., Ulloa, L., de Garcini, E. M., & Díaz‐Nido, J. (1993) · Elsevier eBooks · doi:10.1016/b978-0-444-81470-8.50010-7 · Cited by 3
Neves‐Carvalho, A., Duarte‐Silva, S., Silva, J. M., Meireles-Costa, L., Monteiro‐Fernandes, D., Correia, J. S., Rodrigues, B., Heetveld, S., Almeida, B., Savytska, N., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/711424 · 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
Self-citationA novel pThr217 tau monoclonal antibody reveals neuropathological heterogeneity in tauopathies
Paterno, G., Bell, B. M., Gorion, K.-M. M., Quintin, S. S., Prokop, S., & Giasson, B. I. (2025) · Scientific Reports · doi:10.1038/s41598-025-04291-y · Cited by 2
Gorzek, R. C., Joly‐Amado, A., Hurst-Calle, N., Gabrielson, G. L., Miller, M., Osting, S., Nash, K. R., & Bürger, C. (2025) · Cells · doi:10.3390/cells14161238 · Cited by 2
“4R tau is particularly relevant in studies of microtubule dynamics, neuronal transport, and cytoskeletal integrity, as it binds microtubules more tightly and stabilizes them more effectively than 3R tau [29].”
Spilling the T: T cells in tauopathy mechanisms, disease progression, and therapeutic horizons
Bosch, M. E., & Ulrich, J. D. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00020-5 · Cited by 3
“This further amplifies neuroinflammation and contributes to a neurotoxic milieu human brain, only 0N3R isoform is present but in the adult human brain all six isoforms are expressed at an approximate 1:1 ratio of 3R to 4R tau [11].”
Efficient tag-less purification of recombinant human tau proteins
Pettis, J. A., Orshoski, M., Pal, S., Allen, A., Zepeda, M. O., Wysocki, V. H., & Kuret, J. (2026) · Analytical Biochemistry · doi:10.1016/j.ab.2026.116095 · Cited by 2
RNA-based therapeutics for Alzheimer’s disease and related tauopathies: challenges and opportunities
Rajbanshi, B., Brentari, I., Denti, M. A., Cummings, J. L., & Guruacharya, A. (2026) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2026.100585 · Cited by 2
“The complexity of tau biology arises from its existence as multiple splice variants that generate six distinct isoforms [14], each isoform undergoing extensive post-translational modifications.”
Alzheimer's disease pathology in aged chimpanzees
Edler, M. K. (2016) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 2
Drosophila Models of Tauopathy
Ali, Y., Ruan, K., & Zhai, R. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00054-8 · Cited by 2
Behrens, A., Anderberg, P., Berglund, J. S., Cianchetta‐Sivoriceruti, M., & Dallora, A. L. (2025) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1002/dad2.70181 · Cited by 2
“32,33 This size disparity suggests that A β can more readily cross the BBB, explaining its lesser sensitivity to BBB integrity.”
Mueller, R. L., Combs, B., & Kanaan, N. M. (2025) · Scientific Reports · doi:10.1038/s41598-025-21920-8 · Cited by 2
“In contrast to adult expression patterns, only 3R tau is expressed during development in humans and mice 62–64 .”
Vingtdeux, V., Buée, L., & Sergeant, N. (2011) · InTech eBooks · doi:10.5772/20567 · Cited by 1
“It has been demonstrated that adult Tau isoforms with 4R (R1-R4) are more efficient at promoting microtubule assembly than the fetal isoform with 3R (R1, R3-R4) (Butner and Kirschner, 1991; Goedert and Jakes, 1990; Gustke et al., 1994).”
Chen, C., Lv, Y., Shi, Q. W., Zhang, B., Chen, L., Xiao, K., Sun, J., & Dong, X. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2235 · Cited by 2
Kurkó, D., Boros, A. M., Dezső, P., Urbányi, Z., Sárvári, M., Nagy, J., Szombathelyi, Z., & Szendrei, G. I. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2005.11.010 · Cited by 2
Effects of Formaldehyde on Protein (Tau) Aggregation and Cytotoxicity
He, R. (2017) · Springer eBooks · doi:10.1007/978-94-024-1177-5_7 · Cited by 2
Neurodegeneration and the Ordered Assembly of Tau
Goedert, M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00004-3 · Cited by 3
Self-citationTau in Health and Neurodegenerative Diseases
Chu, D., & Liu, F. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.101299 · Cited by 2
In Vitro Amplification of Pathogenic Tau Seeds from Neurodegenerative Disease Patient Brains
Xu, H. W., & Lee, V. M. Y. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2655-9_15 · Cited by 3
Novel Conformation-Dependent Tau Antibodies Are Modulated by Adjacent Phosphorylation Sites
Paterno, G., Torrellas, J., Bell, B. M., Gorion, K.-M. M., Quintin, S. S., Hery, G. P., Prokop, S., & Giasson, B. I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813676 · Cited by 2
“Human tau isoforms 2N/4R, 0N/4R, and 0N/3R, and truncated tau protein 1–253 ∆ 45–102 of 2N/3R, and human tau 0N/4R phospho-mimetic (12E and 4E(210–217)) constructs were expressed from the bacterial plasmid pRK172 [76] in BL21 (DE3) Escherichia coli (Agilent Technologies, Santa Clara, CA, USA) and purified as previousl…”
MethodBachmann, S., Bell, M., Klimek, J., & Zempel, H. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.16.154757 · Cited by 2
Progressive Supranuclear Palsy
Morris, H. R. (2017) · Neurodegeneration · doi:10.1002/9781118661895.ch8 · Cited by 2
Biochemical and biophysical features of disease-associated tau mutants V363A and V363I
Luigi, A. D., Colombo, L., Russo, L., Ricci, C., Bastone, A., Cimini, S., Tagliavini, F., Rossi, G., Cantú, L., Favero, E. D., et al. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140755 · Cited by 1
Quantification of Methylation and Phosphorylation Stoichiometry
Ayoub, C. A., Moore, K. I., & Kuret, J. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_13 · Cited by 1
Scalable human neuronal models of tauopathy producing endogenous seed-competent 4R tau
Tsefou, E., Bez, S., Birkle, T. J. Y., Foiani, M. S., Watamura, N., Bourdenx, M., Gavriouchkina, D., Turkes, E., Crawford, S., Coneys, R., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeg1445 · Cited by 1
Arar, S. H., Haque, M. A., Kayed, A., Khan, S., Bhatt, N. N., Zhao, Y., & Kayed, R. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00122 · Cited by 1
From Protein Tangles to Genetic Variants: The Central Role of Tau in Neurodegenerative Disease
Julia, H., & Wade‐Martins, R. (2011) · InTech eBooks · doi:10.5772/29839 · Cited by 1
“It has been shown that 4R tau isoforms are more efficient promoters of tubulin polymerisation than 3R isoforms, hinting at different functions of the different isoforms (Goedert & Jakes, 1990).”
Viskontas, I. V., & Miller, B. L. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511581410.004 · Cited by 1
Cerebrospinal Fluid Tau and Phosphotau As Biomarkers in Alzheimer's Disease Diagnosis
Ahmadian, N., Talebi, M., Mahmoudi, J., Etegad, S. S., & Aghili, A. (2019) · Basic and Clinical Neuroscience Journal · doi:10.32598/bcn.9.10.445 · Cited by 1
Sergeant, N., & Buée, L. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-6787-9_4 · Cited by 1
Peng, C., Wei, W., Zhang, H., Wang, Y., Chang, B., Zhao, W., Jia, L., Li, L., Lu, F., & Liu, F. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09231-z · Cited by 1
Malyshka, D., Jimenez-Harrison, D., & Kuret, J. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_7 · Cited by 1
Lorenzo, D. D., Bisi, N., Bucci, R., Ennen, I., Presti, L. L., Dodero, V. I., Brandt, R., Ongeri, S., Gelmi, M. L., & Tonali, N. (2025) · iScience · doi:10.1016/j.isci.2025.112272 · Cited by 1
Takashima, A. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-6787-9_5 · Cited by 1
Tau Aggregation, Conformational Selection, and Inhibition
Holden, M. R. (2018) · Digital Commons - DU (University of Denver) · Cited by 1
Tau, Tangles and Tauopathies: Insights from Drosophila Disease Models
Nisha, N., Pragati, Tandon, S., Aqsa, A., Aggarwal, P., & Sarkar, S. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_8 · Cited by 1
Delacourte, A., Sergeant, N., & Buée, L. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-336-3_20 · Cited by 1
Bernardes, C. P., dos Santos, N. A. G., Costa, T. R., Menaldo, D. L., Sisti, F., Amstalden, M. K., Ribeiro, D. L., Antunes, L. M. G., Sampaio, S. V., & dos Santos, A. C. (2023) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-023-10517-2 · Cited by 1
“Different subunits of α- and β-tubulin, including β-III-tubulin, form the microtubules, which are the major components of the neuronal cytoskeleton (Goedert and Jakes 1990; Li and Yang 2015).”
BackgroundDiversity of microtubule-associated Tau proteins and neuronal polarity
Nunez, J., Langkopf, A., & Couchie, D. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00009-4 · Cited by 1
Proteomic strategies for analysis of cerebrospinal fluid in neurodegenerative disorders
Hansson, S. (2008) · Gothenburg University Publications Electronic Archive (Gothenburg University) · Cited by 1
Lovestone, S. (1996) · International Journal of Geriatric Psychiatry · doi:10.1002/(sici)1099-1166(199604)11:4 · 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
Lee, V. M. Y., & Trojanowski, J. Q. (2000) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-662-04056-0_7 · Cited by 1
Lyu, C., Vela, S. D., Al‐Hilaly, Y. K., Marshall, K. E., Thorogate, R., Svergun, D. I., Serpell, L. C., Pastore, A., & Hanger, D. P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.08.451675 · Cited by 1
Langston, J. W., Forno, L. S., Tetrud, J., Reeves, A. G., Kaplan, J. A., & Karluk, D. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199910)46:4 · Cited by 1
Kordower (1999) · doi:10.1002/1531-8249(199909)46:3
Higgins, J. J. (2003) · Elsevier eBooks · doi:10.1016/b978-012566652-7/50032-0
Tau Phosphorylation and Dephosphorylation in the Pathogenesis of Alzheimer’s Disease
Mawal-Dewan, M., Trojanowski, J. Q., & Lee, V. M.-Y. (1996) · Springer eBooks · doi:10.1007/978-3-662-03248-0_7 · Cited by 1
Wider, C. W., Dickson, D. W., Rademakers, R., & Wszołek, Z. K. (2009) · Blue books of neurology · doi:10.1016/b978-1-4160-6641-5.00023-4
Metadata
- Authors
- Goedert, M., & Jakes, R.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- ORCID
- Goedert, M.
- Venue
- The EMBO Journal
- Published
- 1990-12-01
- Volume
- 9
- Issue
- 13
- Pages
- 4225-4230
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC552204
- OpenAlex
- W1509571186
- Cited by
- 929
- References
- 46
- Citations by year
- 2026: 23 · 2025: 29 · 2024: 50 · 2023: 39 · 2022: 40 · 2021: 53 · 2020: 34 · 2019: 39 · 2018: 42 · 2017: 41 · 2016: 27 · 2015: 37 · 2014: 18 · 2013: 21 · 2012: 25
- FWCI
- 15.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tau isoforms, microtubule-associated proteins, microtubule assembly, tandem repeats, recombinant protein expression, cerebral cortex, fetal brain
- MeSH terms
- Aged, Alkaline Phosphatase, Alzheimer Disease, Amino Acid Sequence, Brain, Escherichia coli, Humans, Isomerism, Microtubule-Associated Proteins, Middle Aged, Molecular Sequence Data, Recombinant Proteins, Repetitive Sequences, Nucleic Acid, RNA Splicing, RNA, Messenger, Tubulin, Mutagenesis, Site-Directed, tau Proteins
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