The DOI matches its Crossref record; 64 of the 66 references it cites were found in a registry or an index.
The microtubule binding domain of tau protein
Abstract
Tau protein is a microtubule-associated protein implicated in the spatial and temporal specification of microtubules and has been found in the neurofibrillary tangles of Alzheimer's disease. Determination of tau protein structure has revealed three 18 amino acid repeated sequences hypothesized to be tubulin binding sites. Using tau cDNA clones from human fetal brain, we employed E. coli expression systems to synthesize tau protein and fragments of tau protein in order to identify the microtubule binding site. A fragment containing the three repeated sequences binds microtubules, while the amino-terminal half of the protein does not bind. Fragments containing two or one repeat are also capable of binding, indicating that the basic tubulin interacting unit is one repeat.
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
“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 [122]
Citations
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
A new method for sequencing DNA.
Maxam, A. M., & Gilbert, W. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.2.560 · Cited by 7,929
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
Merril, C. R., Goldman, D. A., Sedman, S. A., & Ebert, M. H. (1981) · Science · doi:10.1126/science.6162199 · Cited by 2,933
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780
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
Self-citationGoedert, 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
Dale, R. M. K., McClure, B., & Houchins, J. P. (1985) · Plasmid · doi:10.1016/0147-619x(85)90053-8 · Cited by 1,043
Cited by
Sorted by citations
Items 101–200 of 501
Structural and Functional Organization of Tubulin
Fosket, D. E., & Morejohn, L. C. (1992) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.43.060192.001221 · Cited by 129
Wei, Y., Qu, M.-H., Wang, X.-S., Chen, L., Wang, D.-L., Liu, Y., Hua, Q., & He, R.-Q. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002600 · Cited by 129
The Role of the Lipid Bilayer in Tau Aggregation
Elbaum‐Garfinkle, S., Ramlall, T. F., & Rhoades, E. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.03.013 · Cited by 127
West, R. R., Tenbarge, K. M., & Olmsted, J. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54720-7 · Cited by 127
Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease
Terwel, D., Dewachter, I., & Van Leuven, F. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:151 · Cited by 146
Wang, J., Gao, Q., Wang, Y., Lafyatis, R., Stamm, S., & Andreadis, A. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02232.x · Cited by 125
Diverse Distribution and Function of Fibrous Microtubule-Associated Proteins in the Nervous System
Schoenfeld, T. A., & Obar, R. A. (1994) · International review of cytology · doi:10.1016/s0074-7696(08)62631-5 · Cited by 128
Missense and splice site mutations in tau associated with FTDP-17: Multiple pathogenic mechanisms
Hutton, M. L. (2001) · Neurology · doi:10.1212/wnl.56.suppl_4.s21 · Cited by 125
Microglia in Alzheimer’s Disease in the Context of Tau Pathology
Perea, J. R., Bolós, M., & Ávila, J. (2020) · Biomolecules · doi:10.3390/biom10101439 · Cited by 134
Baas, P. W., & Qiang, L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.007 · Cited by 123
Phosphorylated tau and the neurodegenerative foldopathies
Kosik, K. S., & Shimura, H. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.011 · Cited by 124
Self-citationTau isoform composition influences rate and extent of filament formation
Zhong, Q., Congdon, E. E., Nagaraja, H. N., & Kuret, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.364067 · Cited by 122
Competition for Microtubule-binding with Dual Expression of Tau Missense and Splice Isoforms
Lü, M., & Kosik, K. S. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.171 · Cited by 122
Self-citationKar, A. N., Fushimi, K., Zhou, X., Ray, P., Chen, S., Chen, X., Liu, Z., Chen, S., & Wu, J. Y. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01149-10 · Cited by 132
Padmanabhan, J., Levy, M. M., Dickson, D. W., & Potter, H. (2006) · Brain · doi:10.1093/brain/awl255 · Cited by 124
Doublecortin mutations cluster in evolutionarily conserved functional domains
Sapir, T. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.5.703 · Cited by 125
New perspectives on the role of tau in Alzheimer's disease. Implications for therapy
Medina, M., & Ávila, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.013 · Cited by 123
Pathogenesis of the Tauopathies
Goedert, M., & Spillantini, M. G. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9593-4 · Cited by 126
Wang, P., Joberty, G., Buist, A., Vanoosthuyse, A., Stancu, I., Vasconcelos, B., Pierrot, N., Faelth-Savitski, M., Kienlen‐Campard, P., Octave, J., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1663-9 · Cited by 120
Synaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 128
Untangling tau-related dementia
Heutink, P. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.6.979 · Cited by 117
Potential Contribution of Exosomes to the Prion-Like Propagation of Lesions in Alzheimer’s Disease
Vingtdeux, V., Sergeant, N., & Buée, L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00229 · Cited by 116
The Molecular and Cellular Biology of Tau
Kosik, K. S. (1993) · Brain Pathology · doi:10.1111/j.1750-3639.1993.tb00724.x · Cited by 116
Self-citationMolecular structure of microtubule-associated protein 2b and 2c from rat brain.
Kindler, S., Schulz, B., Goedert, M., & Garner, C. C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45425-1 · Cited by 114
Kalbfuss, B., Mabon, S. A., & Misteli, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105113200 · Cited by 114
A Role for Glial Cells in Activity-Dependent Development of the Vertebrate Nervous System
Fields, R. D., & Nelson, P. G. (1992) · International review of neurobiology · doi:10.1016/s0074-7742(08)60098-7 · Cited by 113
The effect of insomnia on development of Alzheimer’s disease
Sadeghmousavi, S., Eskian, M., Rahmani, F., & Rezaei, N. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01960-9 · Cited by 122
The ‘jaws’ model of tau-microtubule interaction examined in CHO cells
Preuß, U., Biernat, J., Mandelkow�, E., & Mandelkow�, E. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.6.789 · Cited by 115
Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation
Grinberg, L. T., Wang, X., Wang, C., Sohn, P., Theofilas, P., Sidhu, M., Arevalo, J. B., Heinsen, H., Huang, E. J., Rosen, H. J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1080-2 · Cited by 110
Peng, Y., Gao, P., Shi, L., Chen, L., Liu, J., & Long, J. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2019.7763 · Cited by 110
Insights into Disease-Associated Tau Impact on Mitochondria
Szabo, L., Eckert, A., & Grimm, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176344 · Cited by 107
The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer′s Disease (AD)
Mroczko, B., Groblewska, M., & Litman‐Zawadzka, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194661 · Cited by 111
Tubulin-G protein interactions involve microtubule polymerization domains
Wang, N., & Rasenick, M. M. (1991) · Biochemistry · doi:10.1021/bi00109a021 · Cited by 103
Prion-like Spreading in Tauopathies
Ayers, J. I., Giasson, B. I., & Borchelt, D. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.04.003 · Cited by 106
Levy, S. F., LeBoeuf, A. C., Massie, M. R., Jordan, M. A., Wilson, L., & Feinstein, S. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413490200 · Cited by 102
Microtubule-dependent Oligomerization of Tau
Makrides, V., Shen, T. E., Bhatia, R., Smith, B. L., Thimm, J. C., Lal, R., & Feinstein, S. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305207200 · Cited by 102
Chapin, S. J., & Bulinski, J. C. (1992) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970230403 · Cited by 100
Protein coding of neurodegenerative dementias: the neuropathological basis of biomarker diagnostics
Kovács, G. G., Botond, G., & Budka, H. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0658-1 · Cited by 102
Stress‐induced hyperphosphorylation of tau in the mouse brain
Okawa, Y., Ishiguro, K., & Fujita, S. C. (2003) · FEBS Letters · doi:10.1016/s0014-5793(02)03883-8 · Cited by 98
Kim, B. M., You, M.-H., Chen, C.-H., Lee, S., Hong, Y., Hong, Y., Kimchi, A., Zhou, X. Z., & Lee, T. H. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.216 · Cited by 98
Tau mis-splicing in the pathogenesis of neurodegenerative disorders
Park, S. A., Ahn, S. I., & Gallo, J. (2016) · BMB Reports · doi:10.5483/bmbrep.2016.49.8.084 · Cited by 100
Tau gene expression in rat sensory neurons during development and regeneration
Oblinger, M., Argasinski, A., Wong, J., & Kosik, K. S. (1991) · Journal of Neuroscience · doi:10.1523/jneurosci.11-08-02453.1991 · Cited by 98
Self-citationWęgiel, J., Kaczmarski, W., Barua, M., Kuchna, I., Nowicki, K., Wang, K.-C., Wegiel, J., Mazur‐Kolecka, B., Frackowiak, J., Mazur‐Kolecka, B., et al. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318202bfa1 · Cited by 98
The Evolution of Tau Phosphorylation and Interactions
Trushina, N. I., Bakota, L., Mulkidjanian, A. Y., & Brandt, R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00256 · Cited by 99
Review: Alternative Splicing (AS) of Genes As An Approach for Generating Protein Complexity
Roy, B., Haupt, L. M., & Griffiths, L. R. (2013) · Current Genomics · doi:10.2174/1389202911314030004 · Cited by 102
Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS
Callister, J. B., & Pickering-Brown, S. M. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.06.001 · Cited by 103
Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI‐TOF MS, CD, and NMR
Ma, Q., Li, Y., Du, J., Kanazawa, K., Nemoto, T., Nakanishi, H., & Zhao, Y. (2005) · Biopolymers · doi:10.1002/bip.20335 · Cited by 96
The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target
Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 105
Alz-50 recognizes a phosphorylated epitope of tau protein
Ueda, K., Masliah, E., Saitoh, T., Bakalis, S., Scoble, H. A., & Kosik, K. S. (1990) · Journal of Neuroscience · doi:10.1523/jneurosci.10-10-03295.1990 · Cited by 96
Self-citationCollins-Praino, L. E., & Corrigan, F. (2017) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2016.09.027 · Cited by 95
Molecular Genetics of Chromosome 17 Tauopathies
HUTTON, M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06906.x · Cited by 92
Structural Plasticity of the Hippocampus in Neurodegenerative Diseases
Weerasinghe-Mudiyanselage, P. D. E., Ang, M. J., Kang, S., Kim, J., & Moon, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063349 · Cited by 97
Analysis of tauopathies with transgenic mice
Hutton, M., Lewis, J., Dickson, D., Yen, S.-H., & McGowan, E. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02123-2 · Cited by 91
The L266V tau mutation is associated with frontotemporal dementia and Pick-like 3R and 4R tauopathy
Hogg, M. C., Grujic, Z., Baker, M. C., Demirci, S., Guillozet-Bongaarts, A. L., Sweet, A. P., Herzog, L. L., Weıntraub, S., Mesulam, M. M., LaPointe, N. E., et al. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0734-x · Cited by 93
Brandt, R., Lee, G. S., Teplow, D. B., Shalloway, D. I., & Abdel-Ghany, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32639-x · Cited by 90
Self-citationÁvila, J. (1992) · Life Sciences · doi:10.1016/0024-3205(92)90433-p · Cited by 91
Cyclic AMP-dependent Protein Kinase Regulates the Alternative Splicing of Tau Exon 10
Shi, J., Qian, W., Yin, X., Iqbal, K., Grundke, I., Gu, X., Ding, F., Gong, C., & Liu, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204453 · Cited by 87
Complex Regulation of Tau Exon 10, Whose Missplicing Causes Frontotemporal Dementia
Gao, Q., Memmott, J. E., Lafyatis, R., Stamm, S., Screaton, G. R., & Andreadis, A. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.740490.x · Cited by 87
Greenwood, J. A., Scott, C. W., Spreen, R. C., Caputo, C. B., & Johnson, G. V. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41790-x · Cited by 86
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
Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles
Prezel, E., Elie, A., Delaroche, J., Stoppin-Mellet, V., Bosc, C., Serre, L., Fourest-Lieuvin, A., Andrieux, A., Vantard, M., & Arnal, I. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0429 · Cited by 83
Yoshida, H., & Goedert, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04052.x · Cited by 87
Side Chain-dependent Stacking Modulates Tau Filament Structure
Margittai, M., & Langen, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605336200 · Cited by 84
van Herpen, E., Rosso, S. M., Serverijnen, L., Yoshida, H., Breedveld, G. J., van de Graaf, R., Kamphorst, W., Ravid, R., Willemsen, R., Dooijes, D., et al. (2003) · Annals of Neurology · doi:10.1002/ana.10721 · Cited by 83
Choi, M. C., Raviv, U., Miller, H. P., Gaylord, M. R., Kiris, E., Ventimiglia, D., Needleman, D. J., Kim, M. W., Wilson, L., Feinstein, S. C., et al. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.04.047 · Cited by 80
Tau protein: An update on structure and function
Lee, G. S. (1990) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970150402 · Cited by 80
Self-citationGong, C., Liu, F., Grundke, I., & Iqbal, K. (2006) · BioMed Research International · doi:10.1155/jbb/2006/31825 · Cited by 81
A Soluble Oligomer of Tau Associated with Fiber Formation Analyzed by NMR
Peterson, D. W., Zhou, H., Dahlquist, F. W., & Lew, J. (2008) · Biochemistry · doi:10.1021/bi702466a · Cited by 76
Buée‐Scherrer, V., & Goedert, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02460-2 · Cited by 76
Tau mutants bind tubulin heterodimers with enhanced affinity
Elbaum‐Garfinkle, S., Cobb, G., Compton, J. T., Li, X., & Rhoades, E. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315983111 · Cited by 76
Pacheco, C. D., Elrick, M. J., & Lieberman, A. P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn423 · Cited by 77
Wang, Y., Wang, J., Gao, L., Lafyatis, R., Stamm, S., & Andreadis, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413846200 · Cited by 75
A critical appraisal of tau‐targeting therapies for primary and secondary tauopathies
Imbimbo, B. P., Ippati, S., Watling, M., & Balducci, C. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12453 · Cited by 76
Zhou, K., Yuan, C., Dai, B., Wang, K., Chen, Y., Ma, D., Dai, J., Liang, Y., Tan, H., & Cui, M. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00672 · Cited by 73
Misregulation of Tau Alternative Splicing in Neurodegeneration and Dementia
Andreadis, A. (2006) · Progress in molecular and subcellular biology · doi:10.1007/978-3-540-34449-0_5 · Cited by 72
Functional implications of the association of tau with the plasma membrane
Pooler, A. M., & Hanger, D. P. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381012 · Cited by 72
Folding of the Repeat Domain of Tau Upon Binding to Lipid Surfaces
Barré, P., & Eliezer, D. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.018 · Cited by 69
Wu, G., Lin, Y.-T., Wei, R. L.-H., Chen, Y., Shan, Z., & Lee, W. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01923-07 · Cited by 67
Preuß, U., & Mandelkow, E. (1998) · European Journal of Cell Biology · doi:10.1016/s0171-9335(98)80032-0 · Cited by 66
Neuronal differentiation triggered by blocking cell proliferation.
LoPresti, P., Poluha, W., Poluha, D. K., Drinkwater, E., & Ross, A. H. (1992) · PubMed · Cited by 66
Non-motor microtubule-associated proteins
Olmsted, J. B. (1991) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(91)90165-u · Cited by 65
Role of Tau Protein in Neuronal Damage in Alzheimer's Disease and Down Syndrome
Cárdenas, A. M., Ardiles, Á. O., Barraza, N., Báez‐Matus, X., & Caviedes, P. A. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.012 · Cited by 68
Niewidok, B., Igaev, M., Sündermann, F., Janning, D., Bakota, L., & Brandt, R. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-06-0402 · Cited by 62
Membrane-mediated fibrillation and toxicity of the tau hexapeptide PHF6
Fanni, A. M., Zanden, C. M. V., Majewska, P. V., Majewski, J. P., & Chi, E. Y. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010003 · Cited by 63
Clavaguera, F., Grueninger, F., & Tolnay, M. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.037 · Cited by 68
Death-Associated Protein Kinase 1 as a Promising Drug Target in Cancer and Alzheimer’s Disease
Chen, D., Zhou, X. Z., & Lee, T. H. (2018) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/1574892814666181218170257 · Cited by 61
Ainsztein, A. M., & Purich, D. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46950-5 · Cited by 61
Mapping of the Alz 50 epitope in microtubule‐associated proteins tau
Ksiezak‐Reding, H., Chien, C.-H., LEE, V. M.-Y., & Yen, S.-H. C. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490250319 · Cited by 61
Phospho-dependent association of neurofilament proteins with kinesin in situ
Yabe, J. T., Jung, C., Chan, W. K. ‐., & SHEA, T. B. (2000) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(200004)45:4 · Cited by 116
Brandt, R., & Lee, G. S. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03613.x · Cited by 60
Self-citationChen, D., Mei, Y., Kim, N., Lan, G., Gan, C., Fan, F., Zhang, T., Xia, Y., Wang, L., Lin, C., et al. (2020) · Journal of Pineal Research · doi:10.1111/jpi.12665 · Cited by 59
Peptidyl-Prolyl Cis/Trans Isomerase Pin1 and Alzheimer’s Disease
Wang, L., Zhou, Y., Chen, D., & Lee, T. H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00355 · Cited by 66
Cross, D. C., Vial, C., & Maccioni, R. B. (1993) · Journal of Cell Science · doi:10.1242/jcs.105.1.51 · Cited by 59
The molecular mechanism, targets, and novel molecules in the treatment of Alzheimer’s disease
Verma, A., Waiker, D. K., Bhardwaj, B., Saraf, P., & Shrivastava, S. K. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105562 · Cited by 58
Gao, L., Wang, J., Wang, Y., & Andreadis, A. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.10.004 · Cited by 59
Dynamics of microtubules bundled by microtubule associated protein 2C (MAP2C).
Umeyama, T., Okabe, S., Kanai, Y., & Hirokawa, N. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.120.2.451 · Cited by 57
Vanbesien-Mailliot, C., Podevin-Dimster, V., Rosenthal, R. E., Sergeant, N., Delacourte, A., Fiskum, G. M., & Buée, L. (2000) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200003000-00013 · Cited by 57
Monte Carlo Simulations of Tau Proteins: Effect of Phosphorylation
Jho, Y., Zhulina, E. B., Kim, M. W., & Pincus, P. A. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.06.056 · Cited by 55
Expression of specific tau exons in normal and tumoral pancreatic acinar cells
Vanier, M., Neuville, P., Michalik, L., & Launay, J. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.10.1419 · Cited by 54
Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy
Gigant, B., Landrieu, I., Fauquant, C., Barbier, P., Huvent, I., Wieruszeski, J., Knossow, M., & Lippens, G. M. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504864m · Cited by 54
Metadata
- Authors
- Lee, G., Neve, R. L., & Kosik, K. S.
- Affiliations
- Brigham and Women's Hospital (US)
- Boston Children's Hospital (US)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1989-06
- Volume
- 2
- Issue
- 6
- Pages
- 1615-1624
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1972355725
- Cited by
- 500
- References
- 66
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 13 · 2023: 19 · 2022: 12 · 2021: 19 · 2020: 14 · 2019: 17 · 2018: 13 · 2017: 13 · 2016: 8 · 2015: 12 · 2014: 13 · 2013: 13 · 2012: 13
- FWCI
- 14.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r29gm039300-05, 5r01ag006601-13)
- National Institute on Aging (R01 AG06601-01)
- National Institute of General Medical Sciences (R29 GM39300-01)
- 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, microtubule-binding site, microtubule-associated proteins, tubulin binding, neurofibrillary tangles, Alzheimer's disease, protein structure
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, DNA, Humans, Microtubule-Associated Proteins, Microtubules, Molecular Sequence Data, Protein Binding, Recombinant Fusion Proteins, Repetitive Sequences, Nucleic Acid, Sequence Homology, Nucleic Acid, Tubulin, tau Proteins
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