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Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
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“Microtubule affinity has also been employed in the purification of other proteins such as MAP1, tau, and dynein (Vallee and Bloom, 1984; Cleveland et al., 1977; Nasr and Satir, 1985).”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Cleveland et al., 1977
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PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
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Self-citationMicrotubule-associated proteins and the stimulation of tubulin assembly in vitro
Sloboda, R. D., Dentler, W. L., & Rosenbaum, J. L. (1976) · Biochemistry · doi:10.1021/bi00665a026 · Cited by 444
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Research works printed but not linked: 6
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- Murphy, 1975, 72, 2696
- Shelanski, 1973, 70, 765
- Sloboda, 1975, 72, 177
- Weingarten, 1975, 72, 1858
- Witman, 1976, 73, 4070
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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
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Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993
“Microtubule affinity has also been employed in the purification of other proteins such as MAP~, tau, and dynein (Vallee and Bloom, 1984; Cleveland et al., 1977; Nasr and Satir, 1985).”
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
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Role of tau protein in both physiological and pathological conditions
AVILA, J., LUCAS, J. J., PÉREZ, M., & HERNÁNDEZ, F. (2004) · Physiological Reviews · doi:10.1152/physrev.00024.2003 · Cited by 1,005
“Tau is a hydrophilic protein that has been widely characterized in solution where, by analysis of the circular dichroism spectra (46), it appears as a random coiled protein.”
BackgroundModulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.
Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 1,011
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Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901
Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881
“…from microtubule protein by a combination of phosphocellulose chromatography, ammonium sulfate precipitation, and hydroxyapatite chromatography (Cleveland et al., 1977b), is seen by SDS/polyacrylamide gel electrophoresis to consist of four closely spaced bands of apparent molecular weights…”
BackgroundMethodInfluentialSelf-citationBiochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint
Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 897
“In neurons, Tau is strongly substoichiometric compared with tubulin ( 20–40 mM tubulin compared with 1 mM Tau or less [Cleveland et al. 1977b; Hiller and Weber 1978]); in vitro binding studies show saturation at Tau:tubulin ratios up to 0.”
BackgroundAmbadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00480-0 · Cited by 782
Tau and neurodegenerative disease: the story so far
Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806
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Altered microtubule organization in small-calibre axons of mice lacking tau protein
Harada, A., Oguchi, K., Okabe, S., Kuno, J., Terada, S., Ohshima, T., Sato-Yoshitake, R., Takei, Y., Noda, T., & Hirokawa, N. (1994) · Nature · doi:10.1038/369488a0 · Cited by 802
Tau protein function in living cells.
Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 766
“These include the tau proteins of 50-70 kD (Weingarten et al., 1975; Cleveland et al., 1977), microtubule-associated protein 1 (MAP1) ~ of '~330 kD, and microtubule-associated protein 2 (MAP2) of "~300 kD (for a review of MAP1 and MAP2 see Vallee et al., 1984).”
Self-citationŠimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Biomolecules · doi:10.3390/biom6010006 · Cited by 730
“Following the initial discovery of tau, two studies reported the process of tau purification and its physical and chemical properties [10,11], including the ability of tau to become phosphorylated.”
BackgroundThe Primary Structure and Heterogeneity of Tau Protein from Mouse Brain
Lee, G. S., Cowan, N. J., & Kirschner, M. W. (1988) · Science · doi:10.1126/science.3122323 · Cited by 680
Self-citationPost-translational modifications of tau protein: Implications for Alzheimer's disease
Martin, L., Latypova, X., & Terro, F. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.023 · Cited by 683
“Tau protein (tubulin-associated unit) was identified in 1975 (Cleveland et al., 1977; Weingarten et al., 1975).”
Structure and novel exons of the human .tau. gene
Andreadis, A., Brown, W. M., & Kosik, K. S. (1992) · Biochemistry · doi:10.1021/bi00158a027 · Cited by 659
Domains of tau Protein and Interactions with Microtubules
Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655
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“The four smaller ,polypeptides were similar in electrophoretic mobility and composition to the tau MAPs ( Cleveland et al., 1977 ), and the lower two bands migrated very close to alpha- and beta-tubulin.”
BackgroundProline-directed and non-proline-directed phosphorylation of PHF-tau
Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Titani, K., & Ihara, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.823 · Cited by 557
Tau protein binds to microtubules through a flexible array of distributed weak sites.
Butner, K. A., & Kirschner, M. W. (1991) · The Journal of cell biology · doi:10.1083/jcb.115.3.717 · Cited by 550
“…with eachother on binding) (McGhee and von Hipple, 1974), the molar ratio oftau protein to tubulin was never allowed to exceed 1:20, well below the saturation density of tau protein which is about 1 mole tau protein to 5 moles tubulin in polymer (Cleveland et al., 1977b ; Hirokawa et al., 1988) .”
BackgroundMethodInfluentialSelf-citationDrubin, D. G., Feinstein, S. C., Shooter, E. M., & Kirschner, M. W. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.5.1799 · Cited by 510
Self-citationAntisense oligonucleotide therapy for neurodegenerative disease
Smith, R. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25424 · Cited by 506
“43), and a -synuclein (0.5%; ref.”
InfluentialThe microtubule binding domain of tau protein
Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500
Microtubule-Associated Protein MAP2 Shares a Microtubule Binding Motif with Tau Protein
Lewis, S. A., Wang, D. H., & Cowan, N. J. (1988) · Science · doi:10.1126/science.3142041 · Cited by 483
The role of tau in neurodegeneration
Gendron, T. F., & Petrucelli, L. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-13 · Cited by 478
“Tau was first isolated in 1975 as a protein that co-purifies with tubulin and has the ability to promote microtubule assembly in vitro [2,3].”
Billingsley, M. L., & Kincaid, R. L. (1997) · Biochemical Journal · doi:10.1042/bj3230577 · Cited by 466
Alzheimer disease models and human neuropathology: similarities and differences
Duyckaerts, C., Potier, M.-C., & Delatour, B. (2008) · Acta Neuropathologica · doi:10.1007/s00401-007-0312-8 · Cited by 375
“Tau is a phosphoprotein that belongs to the family of the microtubule associated protein;microtubule-associated proteins; it binds to tubulin and facilitates tubule polymerization [61].”
BackgroundGuo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160833 · Cited by 440
“Tau is a microtubule (MT)-associated protein predominantly expressed in neuronal axons with a primary function of promoting assembly and stability of MTs (Weingarten et al., 1975; Cleveland et al., 1977b).”
BackgroundGötz, J., Probst, A., Spillantini, M. G., Schäfer, T., Jakes, R., Bürki, K., & Goedert, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07116.x · Cited by 441
Defects in Axonal Elongation and Neuronal Migration in Mice with Disrupted tau and map1b Genes
Takei, Y., Teng, J., Harada, A., & Hirokawa, N. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.5.989 · Cited by 408
“Our findings are summarized as follows: (a) dysgenesis of the axon tract with an alteration of MT constitution in vivo and suppression of axonal elongation in cultured neurons from the mutant mice; (b) MT disorganization in growth cones, which provides us new insights into the mode of action of MAPs, where and how the…”
InfluentialGoode, B., & Feinstein, S. (1994) · The Journal of cell biology · doi:10.1083/jcb.124.5.769 · Cited by 399
Tau proteins: the molecular structure and mode of binding on microtubules.
Hirokawa, N., Shiomura, Y., & Okabe, S. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.4.1449 · Cited by 389
“Tau factor is composed of four to five polypeptides (55,00062,000 mol wt) which were shown to be closely related by both peptide mapping and amino acid analysis (6), and were assumed to represent a highly asymmetric molecule by hydrodynamic data (7).”
BackgroundMethodOsborn, M., & Weber, K. K. (1982) · Methods in cell biology · doi:10.1016/s0091-679x(08)60650-0 · Cited by 383
Paullones are potent inhibitors of glycogen synthase kinase‐3β and cyclin‐dependent kinase 5/p25
Leost, M., Schultz, C., Link, A., Wu, Y., Biernat, J., Mandelkow, E., Bibb, J. A., Snyder, G. L., Greengard, P., Zaharevitz, D. W., et al. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01673.x · Cited by 383
“These structures were initially described in 1907 by Alois Alzheimer [18,19], but their major constituent was only identified in 1988 as a highly insoluble form of the microtubule-binding protein tau ([20,21]; reviewed in [22±25]).”
BackgroundMicrotubule-Associated Proteins: Structuring the Cytoskeleton
Bodakuntla, S., Jijumon, A. S., Villablanca, C., González-Billault, C. E., & Janke, C. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.07.004 · Cited by 377
“At the same time, a different biochemical purification procedure led to the discovery of tau, another protein factor essential for microtubule assembly [10-12].”
BackgroundMethodBuée, L., & Delacourte, A. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00550.x · Cited by 368
“However, microtubule assembly also depends partially upon the phosphorylation state of tau proteins: phosphorylated tau proteins are less effective than non-phosphorylated tau on microtubule polymerization (5, 8, 20, 21, 32, 80).”
BackgroundKanai, Y., Takemura, R., Oshima, T., Mori, H., Ihara, Y., Yanagisawa, M., Masaki, T., & Hirokawa, N. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.3.1173 · Cited by 360
“Tan factors are a number of proteins in the molecular mass range of 55,000-62,000, which are shown to be closely related by both peptide sequences and amino acid compositions (Cleveland et al., 1977a).”
BackgroundThe role of tau (MAPT) in frontotemporal dementia and related tauopathies
Rademakers, R., Cruts, M., & Broeckhoven, C. V. (2004) · Human Mutation · doi:10.1002/humu.20086 · Cited by 361
“The tau protein was first isolated more than 25 years ago, as an MT-binding protein that induced the assembly of MTs from purified tubulin [Weingarten et al., 1975; Cleveland et al., 1977a,b].”
BackgroundThe roles of microtubule-associated proteins in brain morphogenesis: a review
Tucker, R. P. (1990) · Brain Research Reviews · doi:10.1016/0165-0173(90)90013-e · Cited by 355
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Antisense Oligonucleotide Therapies for Neurodegenerative Diseases
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“A comparison of the effect of added XMAP on assembly with that of x-protein (a MAP from bovine brain; Cleveland et al., 1977 ) is shown in Fig. 6. Addition of x-protein produced a maximal increase of twofold in microtubule assembly rate, as evident by the length of microtubules assembled.”
BackgroundInfluentialSelf-citationMicrotubules and Microfilaments
Dillon, L. S. (1981) · Springer eBooks · doi:10.1007/978-1-4613-3147-6_2 · Cited by 341
A nucleated assembly mechanism of Alzheimer paired helical filaments
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Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333
Alternative RNA splicing in the nervous system
Grabowski, P. J., & Black, D. L. (2001) · Progress in Neurobiology · doi:10.1016/s0301-0082(01)00007-7 · Cited by 336
Rigidity of microtubules is increased by stabilizing agents.
Mickey, B., & Howard, J. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.4.909 · Cited by 333
“1 ixM (Butner and Kirschner, 1991), we expect that each microtubule's surface was saturated with tau (~1 tau per five tubulin dimers; Cleveland et al., 1977).”
BackgroundStructure of the Bovine Tau Gene: Alternatively Spliced Transcripts Generate a Protein Family
Himmler, A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1389 · Cited by 327
Tau protein as a differential biomarker of tauopathies
Sergeant, N., Delacourte, A., & Buée, L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.020 · Cited by 362
“In mice lacking the Tau gene, an increase in microtubule- associated protein 1A, which may compensate for the functions of Tau proteins, has been observed [22].”
BackgroundFractionation of Brain Microtubule‐Associated Proteins
HERZOG, W., & Weber, K. K. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12716.x · Cited by 311
Microtubule-associated Protein/Microtubule Affinity-regulating Kinase (p110mark)
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Diabetes mellitus and Alzheimer's disease: GSK-3β as a potential link
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Sapir, T., Elbaum, M., & Reiner, O. (1997) · The EMBO Journal · doi:10.1093/emboj/16.23.6977 · Cited by 304
“This was demonstrated in results obtained with a MAP, tau, that stimulated nucleation, reduced the subunit critical concentration, increased the rate of MT elongation and decreased catastrophe frequency (Cleveland et al., 1977a,b; Bre et al., 1990).”
ResultGoode, B. L., Denis, P. E., Panda, D., Radeke, M. J., Miller, H. P., Wilson, L., & Feinstein, S. C. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.2.353 · Cited by 296
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Tau phosphorylation and aggregation in Alzheimer's disease pathology
Ávila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.02.067 · Cited by 288
“Native tau can be found in the form of small oligomers [76].”
BackgroundDysregulation of human brain microtubule-associated tau mRNA maturation in myotonic dystrophy type 1
Sergeant, N. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.19.2143 · Cited by 281
“Tau protein belongs to the family of microtubule-associated proteins (27,28).”
BackgroundOxidative stress in alzheimer’s disease: A review on emergent natural polyphenolic therapeutics
Cassidy, L., Fernandez, F., Johnson, J. B., Naiker, M., Owoola, A. G., & Broszczak, D. A. (2019) · Complementary Therapies in Medicine · doi:10.1016/j.ctim.2019.102294 · Cited by 288
Baudier, J., & Cole, R. D. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45420-8 · Cited by 263
Identification and localization of a tau peptide to paired helical filaments of Alzheimer disease.
Iqbal, K., Grundke, I., Smith, A. J., George, L., Tung, Y. C., & Zaidi, T. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5646 · Cited by 256
Microtubule Assembly and Nucleation
Kirschner, M. W. (1978) · International review of cytology · doi:10.1016/s0074-7696(08)60164-3 · Cited by 256
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The interaction of actin filaments with microtubules and microtubule-associated proteins.
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Drosophila Models of Neurodegenerative Diseases
Lu, B., & Vogel, H. S. (2008) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.3.121806.151529 · Cited by 257
“The major component of the NFT is tau protein, a highly soluble, microtubule-binding protein normally enriched in axons (19).”
BackgroundGlycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites
Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266
Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro
Chirita, C. N., Necula, M., & Kuret, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301663200 · Cited by 249
Tau phosphorylation in Alzheimer's disease: pathogen or protector?
Lee, H., Perry, G. L., Moreira, P. I., Garrett, M. R., Liu, Q., Zhu, X., Takeda, A., Nunomura, A., & Smith, M. A. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.02.008 · Cited by 253
Extracellular tau is toxic to neuronal cells
Gómez-Ramos, A., Díaz-Hernández, M., Cuadros, R., Hernández, F., & Avila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.078 · Cited by 241
“Filtration chromatography analyses of different tau samples were performed on a Sepharose CL6B column [25] equilibrated in a buffer containing 0.”
BackgroundMethodCellular and pathological functions of tau
Bravo, C. P., Naguib, S. A., & Gan, L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00753-9 · Cited by 271
“Tau was discovered in 1975 and was one of the first microtubule-associated proteins (MAPs) to be characterized 1 .”
Physiology and pathology of tau protein kinases in relation to Alzheimer's disease.
Imahori, K., & Uchida, T. (1997) · PubMed · Cited by 236
Mastrangelo, M. A., & Bowers, W. J. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-81 · Cited by 242
“Tau, which is expressed as 6 soluble isoforms from a genetic locus found on chromosome 17, is a microtubuleassociated protein with numerous functions within the neuron [29-31].”
BackgroundGoing new places using an old MAP: tau, microtubules and human neurodegenerative disease
Garcia, M. L., & Cleveland, D. W. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00172-1 · Cited by 237
“As tau was initially isolated through its microtubule stabilizing properties [1], it seemed logical to assume that in vivo it would stabilize microtubules, thus providing structural support for axons.”
BackgroundSelf-citationIntrinsic disorder in proteins associated with neurodegenerative diseases
Vladimir, N. (2009) · Frontiers in bioscience · doi:10.2741/3594 · Cited by 241
“In vitro, tau binds to microtubules, promotes microtubule assembly, and affects the dynamic instability of individual microtubules [112–116].”
BackgroundYoshida, H., & Ihara, Y. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03642.x · Cited by 236
Seznec, H. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.23.2717 · Cited by 228
“Tau protein is a microtubule-associated protein produced in neurons, in which it regulates the microtubule network (35,36).”
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Role of Copper in the Onset of Alzheimer’s Disease Compared to Other Metals
Bagheri, S., Squitti, R., Haertlé, T., Siotto, M., & Saboury, A. A. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00446 · Cited by 235
“Tau proteins mostly expressed in neurons have the ability to induce microtubule assembly in vitro (Weingarten et al., 1975; Cleveland et al., 1977).”
BackgroundRösler, T. W., Marvian, A. T., Brendel, M., Nykänen, N.-P., Höllerhage, M., Schwarz, S. C., Hopfner, F., Koeglsperger, T., Respondek, G., Schweyer, K., et al. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101644 · Cited by 231
Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
Ikegami, S. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00964-7 · Cited by 221
Nitration of Tau Protein Is Linked to Neurodegeneration in Tauopathies
Horiguchi, T., Uryu, K., Giasson, B. I., Ischiropoulos, H., Lightfoot, R. T., Bellmann, C., Richter‐Landsberg, C., Lee, V. M. ‐., & Trojanowski, J. Q. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63462-1 · Cited by 220
Gustke, N., Steiner, B., Mandelkow, E., Biernat, J., Meyer, H. E., Goedert, M., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80767-b · Cited by 219
Atypical, non-standard functions of the microtubule associated Tau protein
Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 221
Transgenic Mouse Model of Tau Pathology in Astrocytes Leading to Nervous System Degeneration
Forman, M. S., Lal, D., Zhang, B., Dabir, D. V., Swanson, E., Lee, V. M.-Y., & Trojanowski, J. Q. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.0081-05.2005 · Cited by 198
“For more information, please contact digitalcommons@lmu.edu.”
BackgroundPhosphorylation of microtubule-associated proteins by a Ca2+/calmodulin- dependent protein kinase
Schulman, H. (1984) · Journal of Cell Biology · doi:10.1083/jcb.99.1.11 · Cited by 173
Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.
Litersky, J. M., & Johnson, G. V. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45982-0 · Cited by 201
Brion, J., Smith, C. J., Couck, A., Gallo, J., & Anderton, B. H. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07444.x · Cited by 202
Tau co-organizes dynamic microtubule and actin networks
Elie, A., Prezel, E., Guérin, C., Denarier, E., Ramirez-Rios, S., Serre, L., Andrieux, A., Fourest-Lieuvin, A., Blanchoin, L., & Arnal, I. (2015) · Scientific Reports · doi:10.1038/srep09964 · Cited by 200
Scott, C. W., Spreen, R. C., Herman, J. L., Chow, F. P., Davison, M. D., Young, J., & Caputo, C. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54055-2 · Cited by 202
Ramkumar, A., Jong, B. Y., & Ori-McKenney, K. M. (2017) · Developmental Dynamics · doi:10.1002/dvdy.24599 · Cited by 208
“…properties of the microtubule polymer, spacing microtubules at certain distances within the axon, and regulating microtubule motor transport (Cleveland et al., 1977; Drubin and Kirschner, 1986a; Drubin and Kirschner, 1986b; Fellous et al., 1986; Bre and Karsenti, 1990; Drechsel et al.,…”
BackgroundInhibition of tau fibrillization by oleocanthal via reaction with the amino groups of tau
Li, W., Sperry, J. B., Crowe, A., Trojanowski, J. Q., Smith, A. B., & Lee, V. M. ‐. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06224.x · Cited by 200
The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush
Wegmann, S., Medalsy, I. D., Mandelkow�, E., & Müller, D. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212100110 · Cited by 201
“The adhesion of the negatively charged, hydrophilic AFM stylus to the fuzzy coat can mimic interactions between Tau fibrils and negatively charged hydrophilic biomolecules (24), such as tubulin (≈4–5 nm in diameter), the main interaction partner of Tau (27, 28).”
BackgroundMicrotubule bundling by tau proteins in vivo: analysis of functional domains
Kanai, Y., Chen, J., & Hirokawa, N. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05489.x · Cited by 194
Metadata
- Authors
- Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W.
- Affiliations
- Princeton University (US)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1977-10
- Volume
- 116
- Issue
- 2
- Pages
- 207-225
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1971165215
- Cited by
- 915
- References
- 18
- Citations by year
- 2026: 12 · 2025: 19 · 2024: 20 · 2023: 25 · 2022: 24 · 2021: 43 · 2020: 26 · 2019: 29 · 2018: 26 · 2017: 36 · 2016: 20 · 2015: 20 · 2014: 24 · 2013: 16 · 2012: 20
- FWCI
- 11.02
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tau protein, microtubule-associated proteins, tubulin, microtubule assembly, microtubule nucleation, microtubule depolymerization, critical concentration, protein purification, phosphocellulose chromatography, ring structure
- MeSH terms
- Chromatography, Agarose, Electrophoresis, Polyacrylamide Gel, Glycoproteins, Microtubules, Molecular Weight, Proteins, Tubulin
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