Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
Abstract
Alzheimer's disease is characterized by aggregates of tau protein. Attempts to study the conditions for aggregation in vitro have led to different experimental systems, some of which appear mutually exclusive (e.g., oxidative vs reductive conditions, induction by polyanions vs fatty acids). We show here that different approaches and pathways can be viewed in a common framework, and that apparent differences can be explained by variations in the kinetics of subreactions. A unified view of PHF aggregation should help to analyze the causes of PHF aggregation and devise methods to prevent it.
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K18 aggregates significantly faster than K19.
“This protein aggregates significantly faster than K19, the corresponding three-repeat version (38, 39) (Fig. 1B).”
From MAP2 caps tau fibrils and inhibits aggregation (2023) · cites this paper as [38]
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
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 2,007 · see citing works
Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998 · see citing works
Self-citationBancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., & Wisniewski, H. M. (1989) · Brain Research · doi:10.1016/0006-8993(89)91396-6 · Cited by 818 · see citing works
Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 773 · see citing works
Self-citationvon Bergen�, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E., & Mandelkow�, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105196200 · Cited by 590 · see citing works
Self-citationSchweers, O., Schönbrunn, E., Marx, A., & Mandelkow�, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51080-8 · Cited by 569 · see citing works
Self-citationKampers, T., Friedhoff, P., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01386-5 · Cited by 548 · see citing works
Self-citationBiernat, J., Mandelkow, E. M., Schröter, C., Lichtenberg‐Kraag, B., Steiner, B., Berling, B., Meyer, H., Mercken, M., Vandermeeren, A., & Goedert, M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05204.x · Cited by 484 · see citing works
Self-citationWille, H., Drewes, G., Biernat, J., Mandelkow�, E., & Mandelkow�, E. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.118.3.573 · Cited by 477 · see citing works
Self-citationRizzu, P., Swieten, J. C. V., Joosse, M., Hasegawa, M., Stevens, M., Tibben, A., Niermeijer, M. F., Hillebrand, M., Ravid, R., Oostra, B. A., et al. (1999) · The American Journal of Human Genetics · doi:10.1086/302256 · Cited by 428 · see citing works
The Structural Basis of Monoclonal Antibody Alz50's Selectivity for Alzheimer's Disease Pathology
Carmel, G., Mager, E. M., Binder, L. I., & Kuret, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32789 · Cited by 402 · see citing works
Goode, B., & Feinstein, S. (1994) · The Journal of cell biology · doi:10.1083/jcb.124.5.769 · Cited by 399 · see citing works
Novak, M., Kabat, J., & Wischik, C. M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05665.x · Cited by 398 · see citing works
Pérez, M., Valpuesta, J., Medina, M., de Garcini, E. M., & Ávila, J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031183.x · Cited by 355 · see citing works
Jicha, G. A., Lane, E., Vincent, I. J., Ötvös, L., Hoffmann, R., & Davies, P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69052087.x · Cited by 264 · see citing works
Structural and Functional Differences between 3-Repeat and 4-Repeat Tau Isoforms
Goode, B. L., Chau, M. F., Denis, P. E., & Feinstein, S. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007489200 · Cited by 241 · see citing works
Going 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 235 · see citing works
Yoshida, H., & Ihara, Y. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03642.x · Cited by 232 · see citing works
Ackmann, M., Wiech, H., & Mandelkow�, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002590200 · Cited by 131 · see citing works
Self-citationBhattacharya, K., Rank, K. B., EVANS, D. B., & Sharma, S. K. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5116 · Cited by 74 · see citing works
In Vitro Assembly of Alzheimer-like Filaments
DeTure, M. A., Di Noto, L., & Purich, D. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201201200 · Cited by 21 · see citing works
An improved voltage measurement device for gel electrophoresis in tube apparatus
Orbán, L., Fawcett, J. S., Sullivan, J. V., Chidakel, B. E., & Chrambach, A. (1988) · Electrophoresis · doi:10.1002/elps.1150090107 · Cited by 19 · see citing works
Disulfide-cross-linked tau and MAP2 homodimers readily promote microtubule assembly.
Noto, L. D., Deture, M., & Purich, D. (1999) · Molecular Cell Biology Research Communications · doi:10.1006/mcbr.1999.0153 · Cited by 17 · see citing works
Modeling of a periodic instability in paired helical filaments reveals an axial repeat
Pollanen, M. S., & Bergeron, C. (2000) · Acta Neuropathologica · doi:10.1007/s004010051157 · Cited by 2 · see citing works
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AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
Conchillo‐Solé, O., de Groot, N. S., Avilés, F. X., Vendrell, J., Daura, X., & Ventura, S. (2007) · BMC Bioinformatics · doi:10.1186/1471-2105-8-65 · Cited by 1,058 · see citing works
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 · see citing works
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works
Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., & Selkoe, D. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017033108 · Cited by 876 · see citing works
Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
Selkoe, D. J. (2004) · Nature Cell Biology · doi:10.1038/ncb1104-1054 · Cited by 863 · see citing works
Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works
Self-citationBarghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559 · see citing works
Self-citationCaspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420640 · Cited by 543 · see citing works
Zhang, W., Falcon, B., Murzin, A. G., Fan, J., Crowther, R. A., Goedert, M., & Scheres, S. H. W. (2019) · eLife · doi:10.7554/elife.43584 · Cited by 500 · see citing works
Structural insights into a yeast prion illuminate nucleation and strain diversity
Krishnan, R., & Lindquist, S. L. (2005) · Nature · doi:10.1038/nature03679 · Cited by 470 · see citing works
Structure and Pathology of Tau Protein in Alzheimer Disease
Kolarova, M., García‐Sierra, F., Bartoš, A., Říčný, J., & Řı́pová, D. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731526 · Cited by 473 · see citing works
Post-translational modifications of tau protein in Alzheimer’s disease
Gong, C.-X., Liu, F., Grundke-Iqbal, I., & Iqbal, K. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-004-0221-0 · Cited by 437 · see citing works
Global Hairpin Folding of Tau in Solution
Jeganathan, S., von Bergen, M., Brutlach, H., Steinhoff, H.-J., & Mandelkow, E. (2006) · Biochemistry · doi:10.1021/bi0521543 · Cited by 432 · see citing works
Self-citationMAPT mutations, tauopathy, and mechanisms of neurodegeneration
Strang, K. H., Golde, T. E., & Giasson, B. I. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0197-x · Cited by 424 · see citing works
Tau aggregation is driven by a transition from random coil to beta sheet structure.
von Bergen, M., Barghorn, S., Biernat, J., Mandelkow, E., & Mandelkow, E. (2005) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2004.09.010 · Cited by 376 · see citing works
Self-citationPreparation and Characterization of Neurotoxic Tau Oligomers
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359 · see citing works
Characterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease
Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 354 · see citing works
Pickhardt, M., Gažová, Z., von Bergen�, M., Khlistunova, I., Wang, Y., Hascher, A., Mandelkow, E., Biernat, J., & Mandelkow�, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410984200 · Cited by 334 · see citing works
Self-citationSites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions
Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501565200 · Cited by 324 · see citing works
Self-citationCripps, D., Thomas, S. N., Jeng, Y., Yang, F., Davies, P., & Yang, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512786200 · Cited by 312 · see citing works
Template-assisted filament growth by parallel stacking of tau
Margittai, M., & Langen, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401911101 · Cited by 276 · see citing works
Jouanne, M., Rault, S., & Voisin‐Chiret, A. S. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.07.070 · Cited by 252 · see citing works
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 244 · see citing works
Coppola, G., Chinnathambi, S., Lee, J. J., Dombroski, B. A., Baker, M. C., Soto-Ortolaza, A. I., Lee, S. E., Klein, E., Huang, A. Y., Sears, R., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds161 · Cited by 240 · see citing works
Self-citationInterplay of pathogenic forms of human tau with different autophagic pathways
Caballero, B., Wang, Y., Diaz, A., Tasset, I., Juste, Y. R., Stiller, B., Mandelkow, E., Mandelkow, E., & Cuervo, A. M. (2018) · Aging Cell · doi:10.1111/acel.12692 · Cited by 213 · see citing works
Self-citationProtein amyloids develop an intrinsic fluorescence signature during aggregation
Chan, F. T. S., Schierle, G. S. K., Kumita, J. R., Bertoncini, C. W., Dobson, C. M., & Kaminski, C. F. (2013) · The Analyst · doi:10.1039/c3an36798c · Cited by 230 · see citing works
The Formation of Straight and Twisted Filaments from Short Tau Peptides
Goux, W. J., Kopplin, L., Nguyen, A. D., Leak, K., Rutkofsky, M., Shanmuganandam, V. D., Sharma, D., Inouye, H., & Kirschner, D. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402379200 · Cited by 227 · see citing works
Tau alteration and neuronal degeneration in tauopathies: mechanisms and models
Brandt, R., Hundelt, M., & Shahani, N. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.018 · Cited by 222 · see citing works
β-Sheet Core of Tau Paired Helical Filaments Revealed by Solid-State NMR
Daebel, V., Chinnathambi, S., Biernat, J., Schwalbe, M., Habenstein, B., Loquet, A., Akoury, E., Tepper, K., Müller, H., Baldus, M., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305470p · Cited by 219 · see citing works
Self-citationAre tau aggregates toxic or protective in tauopathies?
Cowan, C. M., & Mudher, A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00114 · Cited by 215 · see citing works
Tau phosphorylation by GSK-3β promotes tangle-like filament morphology
Rankin, C. A., Sun, Q., & Gamblin, T. C. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-12 · Cited by 214 · see citing works
Domain Conformation of Tau Protein Studied by Solution Small-Angle X-ray Scattering
Mylonas, E., Hascher, A., Bernadó, P., Blackledge, M. J., Mandelkow�, E., & Svergun, D. I. (2008) · Biochemistry · doi:10.1021/bi800900d · Cited by 211 · see citing works
Self-citationBarghorn, S., Davies, P., & Mandelkow�, E. (2004) · Biochemistry · doi:10.1021/bi0357006 · Cited by 209 · see citing works
Self-citationInhibition 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 197 · see citing works
A mechanistic model of tau amyloid aggregation based on direct observation of oligomers
Shammas, S. L., Garcia, G. A., Kumar, S., Kjærgaard, M., Horrocks, M. H., Shivji, N., Mandelkow, E., Knowles, T. P. J., Mandelkow�, E., & Klenerman, D. (2015) · Nature Communications · doi:10.1038/ncomms8025 · Cited by 195 · see citing works
Self-citationIbuprofen reduces Aβ, hyperphosphorylated tau and memory deficits in Alzheimer mice
McKee, A. C., Carreras, I., Hossain, L., Ryu, H., Klein, W. L., Oddo, S., LaFerla, F. M., Jenkins, B. G., Kowall, N. W., & Dedeoglu, A. (2008) · Brain Research · doi:10.1016/j.brainres.2008.01.095 · Cited by 196 · see citing works
Tau oligomers and aggregation in Alzheimer’s disease
Meraz‐Ríos, M. A., León, K. I. L.-D., Campos‐Peña, V., Anda-Hernández, M. A. D., & Mena‐López, R. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06511.x · Cited by 193 · see citing works
Barghorn, S., Biernat, J., & Mandelkow�, E. (2005) · Humana Press eBooks · doi:10.1385/1-59259-874-9:035 · Cited by 193 · see citing works
Self-citationAssembly of two distinct dimers and higher‐order oligomers from full‐length tau
Sahara, N., Maeda, S., Murayama, M., Suzuki, T., Dohmae, N., Yen, S.-H. C., & Takashima, A. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05555.x · Cited by 192 · see citing works
Low Micromolar Zinc Accelerates the Fibrillization of Human Tau via Bridging of Cys-291 and Cys-322
Mo, Z., Zhu, Y.-Z., Zhu, H., Fan, J.-B., Chen, J., & Liang, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.058883 · Cited by 189 · see citing works
A Label‐Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence
Pinotsi, D., Buell, A. K., Dobson, C. M., Schierle, G. S. K., & Kaminski, C. F. (2013) · ChemBioChem · doi:10.1002/cbic.201300103 · Cited by 175 · see citing works
Zeller, M. V., Dias, D., Sebastião, A. M., & Valente, C. A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210268 · Cited by 173 · see citing works
Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease
Guerrero-Muñoz, M. J., Gerson, J., & Castillo-Carranza, D. L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00464 · Cited by 168 · see citing works
Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein Pathology
Michel, C. H., Kumar, S., Pinotsi, D., Tunnacliffe, A., St. George-Hyslop, P., Mandelkow, E., Mandelkow, E.-M., Kaminski, C. F., & Kaminski Schierle, G. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515445 · Cited by 165 · see citing works
Self-citationLimorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 162 · see citing works
Amyloidogenesis of Tau protein
Niżyński, B., Dzwolak, W., & Nieznański, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 157 · see citing works
Identification of an Aggregation-Prone Structure of Tau
Elbaum-Garfinkle, S., & Rhoades, E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305206m · Cited by 149 · see citing works
Ghag, G., Bhatt, N. N., Cantu, D. V., Guerrero‐Munoz, M. J., Ellsworth, A., Sengupta, U., & Kayed, R. (2018) · Protein Science · doi:10.1002/pro.3499 · Cited by 156 · see citing works
Oligomer Formation of Tau Protein Hyperphosphorylated in Cells
Tepper, K., Biernat, J., Kumar, S., Wegmann, S., Timm, T., Hübschmann, S., Redecke, L., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611368 · Cited by 154 · see citing works
Self-citationBunker, J. M., Wilson, L., Jordan, M. A., & Feinstein, S. C. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-01-0062 · Cited by 154 · see citing works
Regulation of tau isoform expression and dementia
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Jones, E. M., Dubey, M. K., Camp, P. J., Vernon, B. C., Biernat, J., Mandelkow�, E., Majewski, J. P., & Chi, E. Y. (2012) · Biochemistry · doi:10.1021/bi201857v · Cited by 145 · see citing works
Self-citationAminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation
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Derry, P. J., Hegde, M. L., Jackson, G. R., Kayed, R., Tour, J. M., Tsai, A.-L., & Kent, T. A. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101716 · Cited by 142 · see citing works
Ramachandran, G., & Udgaonkar, J. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.271874 · Cited by 140 · see citing works
Formation and Propagation of Tau Oligomeric Seeds
Gerson, J. E., & Kayed, R. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00093 · Cited by 137 · see citing works
Roberts, M., Sevastou, I., Imaizumi, Y., Mistry, K., Talma, S., Dey, M., Gartlon, J., Ochiai, H., Zhou, Z., Akasofu, S., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0884-2 · Cited by 135 · see citing works
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 129 · see citing works
Nucleation-dependent Tau Filament Formation
Congdon, E. E., Kim, S., Bonchak, J., Songrug, T., Anastasios Matzavinos, A., & Kuret, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800247200 · Cited by 126 · see citing works
Pathways of tau fibrillization
Kuret, J., Chirita, C. N., Congdon, E. E., Kannanayakal, T. J., Li, G., Necula, M., Yin, H., & Zhong, Q. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.016 · Cited by 124 · see citing works
Tau 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 · see citing works
Amyloid structure and assembly: Insights from scanning transmission electron microscopy
Goldsbury, C. S., Baxa, U., Simon, M. N., Steven, A. C., Engel, A. H., Wall, J. S., Aebi, U., & Müller, S. A. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.09.018 · Cited by 122 · see citing works
Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets
Lee, V. M.-Y., Brunden, K. R., Hutton, M., & Trojanowski, J. Q. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006437 · Cited by 122 · see citing works
Jiang, L., Yao, T., Zhu, Z.-L., Wang, C., & Ji, L. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.08.014 · Cited by 117 · see citing works
Haj‐Yahya, M., & Lashuel, H. A. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b02668 · Cited by 117 · see citing works
Progress and Developments in Tau Aggregation Inhibitors for Alzheimer Disease
Bulic, B., Pickhardt, M., & Mandelkow�, E. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3017317 · Cited by 116 · see citing works
Self-citationSynaptic 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 117 · see citing works
Evaluating triggers and enhancers of tau fibrillization
Kuret, J., Congdon, E. E., Li, G., Yin, H., Yu, X., & Zhong, Q. (2005) · Microscopy Research and Technique · doi:10.1002/jemt.20187 · Cited by 110 · see citing works
Luo, Y., Ma, B., Nussinov, R., & Wei, G. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz501457f · Cited by 107 · see citing works
Sahara, N., Deture, M. A., Ren, Y., Ebrahim, A.-S., Kang, D., Knight, J. A., Volbracht, C., Pedersen, J. T., Dickson, D. W., Yen, S.-H. C., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121093 · Cited by 107 · see citing works
Haj‐Yahya, M., Gopinath, P., Rajasekhar, K., Mirbaha, H., Diamond, M. I., & Lashuel, H. A. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201913001 · Cited by 104 · see citing works
Three Repeat Isoforms of Tau Inhibit Assembly of Four Repeat Tau Filaments
Adams, S. J., Deture, M. A., McBride, M., Dickson, D. W., & Petrucelli, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010810 · Cited by 104 · see citing works
Variations in filament conformation dictate seeding barrier between three- and four-repeat Tau
Dinkel, P. D., Siddiqua, A., Huynh, H., Shah, M., & Margittai, M. (2011) · Biochemistry · doi:10.1021/bi2004685 · Cited by 104 · see citing works
Quantitative Characterization of Heparin Binding to Tau Protein
Zhu, H., Fernández, C., Fan, J.-B., Shewmaker, F. P., Chen, J., Minton, A. P., & Liang, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035691 · Cited by 102 · see citing works
Echeverrı́a, V., Ducatenzeiler, A., Dowd, E., Jänne, J., Grant, S. M., Szyf, M., Wandosell, F. G., Ávila, J., Grimm, H. S., Dunnett, S. B., et al. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.07.036 · Cited by 101 · see citing works
Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration
Sahara, N., Maeda, S., & Takashima, A. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898442 · Cited by 99 · see citing works
Kaniyappan, S., Chandupatla, R., Mandelkow, E., & Mandelkow, E. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.04.002 · Cited by 95 · see citing works
Self-citationThe mechanism of Hsp90-induced oligomerizaton of Tau
Weickert, S., Wawrzyniuk, M., John, L., Rüdiger, S., & Drescher, M. (2020) · Science Advances · doi:10.1126/sciadv.aax6999 · Cited by 95 · see citing works
Structure and Mechanism of Action of Tau Aggregation Inhibitors
Cisek, K. K., Cooper, G., Huseby, C. J., & Kuret, J. (2014) · Current Alzheimer Research · doi:10.2174/1567205011666141107150331 · Cited by 98 · see citing works
Paired helical filaments contain small amounts of cholesterol, phosphatidylcholine and sphingolipids
Gellermann, G. P., Appel, T. R., Davies, P., & Diekmann, S. (2006) · Biological Chemistry · doi:10.1515/bc.2006.157 · Cited by 97 · see citing works
Lin, Y., Fichou, Y., Zeng, Z., Hu, N. Y., & Han, S. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00627 · Cited by 96 · see citing works
Al‐Hilaly, Y. K., Pollack, S. J., Vadukul, D. M., Citossi, F., Rickard, J. E., Simpson, M. C., Storey, J. M. D., Harrington, C. R., Wischik, C. M., & Serpell, L. C. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.09.007 · Cited by 91 · see citing works
Pseudo-phosphorylation of tau at Ser202 and Thr205 affects tau filament formation
Rankin, C. A., Sun, Q., & Gamblin, T. C. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.04.012 · Cited by 95 · see citing works
Nguyen, T. V., Shen, L., Griend, L. V., Quach, L. N., Belichenko, N. P., Saw, N. L., Yang, T., Shamloo, M., Wyss‐Coray, T., Massa, S. M., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140036 · Cited by 94 · see citing works
Calfío, C., González, A., Singh, S. K., Rojo, L. E., & Maccioni, R. B. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200443 · Cited by 93 · see citing works
Hyperphosphorylation Renders Tau Prone to Aggregate and to Cause Cell Death
Liu, M., Sui, D., Dexheimer, T. S., Hovde, S., Deng, X., Wang, K., Lin, H. L., Hagar, H. C., Kweon, H. K., Kuo, N. S., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02034-w · Cited by 97 · see citing works
FTDP-17 Mutations Compromise the Ability of Tau to Regulate Microtubule Dynamics in Cells
Bunker, J. M., Kamath, K., Wilson, L., Jordan, M. A., & Feinstein, S. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509420200 · Cited by 90 · see citing works
Kumar, S., Tepper, K., Kaniyappan, S., Biernat, J., Wegmann, S., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554725 · Cited by 86 · see citing works
Self-citationMorozova, O. A., March, Z. M., Robinson, A. S., & Colby, D. W. (2013) · Biochemistry · doi:10.1021/bi400866w · Cited by 87 · see citing works
Copper (II) modulates in vitro aggregation of a tau peptide
Zhou, L., Du, J., Zeng, Z., Wu, W., Zhao, Y., Kanazawa, K., Ishizuka, Y., Nemoto, T., Nakanishi, H., & Li, Y. (2007) · Peptides · doi:10.1016/j.peptides.2007.08.022 · Cited by 87 · see citing works
Cell-based Models To Investigate Tau Aggregation
Lim, S., Haque, M. M., Kim, D., Kim, D. J., & Kim, Y. K. (2014) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2014.09.011 · Cited by 84 · see citing works
RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth
Dinkel, P. D., Holden, M. R., Matin, N., & Margittai, M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00453 · Cited by 84 · see citing works
Characteristics of Tau Oligomers
Ren, Y., & Sahara, N. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00102 · Cited by 86 · see citing works
Esteves-Villanueva, J. O., Trzeciakiewicz, H., & Martić, S. (2014) · The Analyst · doi:10.1039/c4an00204k · Cited by 85 · see citing works
Signature of an aggregation-prone conformation of tau
Eschmann, N. A., Georgieva, E. R., Ganguly, P., Borbat, P. P., Rappaport, M. D., Akdoğan, Y., Freed, J. H., Shea, J., & Han, S. (2017) · Scientific Reports · doi:10.1038/srep44739 · Cited by 82 · see citing works
Takashima, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130653 · Cited by 80 · see citing works
Vandebroek, T., Vanhelmont, T., Terwel, D., Borghgraef, P., Lemaire, K., Snauwaert, J., Wera, S., LEUVEN, F. V., & Winderickx, J. (2005) · Biochemistry · doi:10.1021/bi0506775 · Cited by 82 · see citing works
Transcriptional and conformational changes of the tau molecule in Alzheimer's disease
Hyman, B. T., Augustinack, J. C., & Ingelsson, M. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.015 · Cited by 79 · see citing works
Pavlova, À., Cheng, C., Kinnebrew, M., Lew, J., Dahlquist, F. W., & Han, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504415113 · Cited by 79 · see citing works
α-Linolenic acid inhibits Tau aggregation and modulates Tau conformation
Desale, S. E., Dubey, T., & Chinnathambi, S. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.10.226 · Cited by 77 · see citing works
- Authors
- Barghorn, S., & Mandelkow, E.
- Affiliations
- Max Planck Unit for Structural Molecular Biology (DE)
- Max-Planck-Unit for Structural Molecular Biology, Notkestrasse 85, 22607 Hamburg, Germany
- ORCID
- Barghorn, S.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-11-20
- Volume
- 41
- Issue
- 50
- Pages
- 14885-14896
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2006051211
- Cited by
- 341
- References
- 25
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 12 · 2023: 9 · 2022: 17 · 2021: 18 · 2020: 19 · 2019: 18 · 2018: 14 · 2017: 19 · 2016: 11 · 2015: 11 · 2014: 21 · 2013: 23 · 2012: 16
- FWCI
- 8.79
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- tau protein, paired helical filaments, Alzheimer's disease, protein aggregation, aggregation kinetics, oxidative conditions, reducing conditions, aggregation pathways
- MeSH terms
- Polyelectrolytes, Alzheimer Disease, Anions, Cross-Linking Reagents, Cysteine, Disulfides, Heparin, Humans, Polymers, Protein Processing, Post-Translational, Spectrometry, Fluorescence, Mutagenesis, Site-Directed, Arachidonic Acid, Neurofibrillary Tangles, tau Proteins, Protein Isoforms
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