Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

Alzheimer's Disease Is a Synaptic Failure

Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498

A simplified system for generating recombinant adenoviruses

He, T., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., & Vogelstein, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2509 · Cited by 3,209

Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160

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

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480

Stages of the Pathologic Process in Alzheimer Disease: Age Categories From 1 to 100 Years

Braak, H., Thal, D. R., Ghebremedhin, E., & Del Tredici, K. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318232a379 · Cited by 2,194

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014

Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease

Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892

Microglial physiology: unique stimuli, specialized responses

Ransohoff, R. M., & Perry, V. H. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132528 · Cited by 1,858

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821

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

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526

Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease

Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,506

Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease

Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374

Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline

Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268

The axonal transport of mitochondria

Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,218

Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease

Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207

Proteomic Analysis of the Cerebrospinal Fluid of Parkinson's Disease Patients Pre- and Post-Deep Brain Stimulation

Wang, E., Yao, H.-B., Chen, Y., Wang, G., Gao, W., Sun, Y., Guo, J., Hu, J., Jiang, C., & Hu, J. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350082 · Cited by 1,185

Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration

Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118

Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss

Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061

Tau pathology in Alzheimer disease and other tauopathies

Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037

Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17.

Hong, M., Zhukareva, V., Vogelsberg-Ragaglia, V., Wszolek, Z., Reed, L., Miller, B., Geschwind, D., Bird, T., McKeel, D., Goate, A., et al. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,024

In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis

Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015

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

Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?

Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989

Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers

Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903

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

Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress

Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885

Aβ Oligomers Induce Neuronal Oxidative Stress through an N-Methyl-D-aspartate Receptor-dependent Mechanism That Is Blocked by the Alzheimer Drug Memantine

De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878

Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules

Alonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859

Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model

Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858

Molecular motors and mechanisms of directional transport in neurons

Hirokawa, N., & Takemura, R. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1624 · Cited by 856

Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments

Alonso, A. D. C., Zaidi, T., Novak, M., Grundke-Iqbal, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 827

Tau is essential to β-amyloid-induced neurotoxicity

Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807

Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding

Biernat, J., Gustke, N., Drewes, G., Mandelkow, E., & Mandelkow, E. (1993) · Neuron · doi:10.1016/0896-6273(93)90279-z · Cited by 796

Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H., & LaFerla, F. M. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.003 · Cited by 780

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779

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

Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation

Liu, F., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04391.x · Cited by 759

Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.

Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5562 · Cited by 738

DEFECTIVE BRAIN MICROTUBULE ASSEMBLY IN ALZHEIMER'S DISEASE

Iqbal, K., Zaidi, T., Wen, G. Y., Grundke, I., MERZ, P. A., Shaikh, S., Wisniewski, H., Alafuzoff, I. I., & Winblad, B. G. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92134-3 · Cited by 737

Age-dependent neurofibrillary tangle formation, neuron loss, and memory impairment in a mouse model of human tauopathy (P301L)

Ramsden, M., Kotilinek, L., Forster, C., Paulson, J., McGowan, E., SantaCruz, K., Guimaraes, A., Yue, M., Lewis, J., Carlson, G., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.3279-05.2005 · Cited by 702

Aβ Oligomers Cause Localized Ca 2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines

Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686

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

Amyloid-β/Fyn–Induced Synaptic, Network, and Cognitive Impairments Depend on Tau Levels in Multiple Mouse Models of Alzheimer's Disease

Roberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4152-10.2011 · Cited by 654

Making New Connections

Impey, S., Obrietan, K. H., & Storm, D. R. (1999) · Neuron · doi:10.1016/s0896-6273(00)80747-3 · Cited by 616

Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons

Chen, J., Kanai, Y., Cowan, N. J., & Hirokawa, N. (1992) · Nature · doi:10.1038/360674a0 · Cited by 601

β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595

Beta amyloid protein deposition in the brain after severe head injury: implications for the pathogenesis of Alzheimer's disease.

Roberts, G. W., Gentleman, S. M., Lynch, A., Murray, L., Landon, M., & Graham, D. I. (1994) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.57.4.419 · Cited by 569

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

Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein.

Sloboda, R. D., Rudolph, S. A., Rosenbaum, J. L., & Greengard, P. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.177 · Cited by 547

Self-Assembly of Aβ 1 - 42 into Globular Neurotoxins

Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., Jones, B. W., Fernandez, S. J., Lacor, P. N., Horowitz, P., et al. (2003) · Biochemistry · doi:10.1021/bi030029q · Cited by 522

Aging renders the brain vulnerable to amyloid β-protein neurotoxicity

Guela, C., Wu, C.-K., Saroff, D., Lorenzo, A., Yuan, M., & Yankner, B. A. (1998) · Nature Medicine · doi:10.1038/nm0798-827 · Cited by 520

Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase.

Chen, H., & Guan, J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.21.10148 · Cited by 510

Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β

Hoshi, M. M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., & Sato, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1237107100 · Cited by 498

Small assemblies of unmodified amyloid $beta;-protein are the proximate neurotoxin in Alzheimer?s disease

Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 494

Alzheimer's disease: Aβ, tau and synaptic dysfunction

LaFerla, F. M., & Oddo, S. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.02.009 · Cited by 477

Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer’s disease pathology

Griffin, R. J., Moloney, A., Kelliher, M., Johnston, J. A., Ravid, R., Dockery, P., O'Connor, R., & O'Neill, C. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02949.x · Cited by 459

Multiple-motor based transport and its regulation by Tau

Vershinin, M., Carter, B. C., Razafsky, D. S., King, S. J., & Gross, S. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607919104 · Cited by 457

Tau phosphorylation: physiological and pathological consequences

Stoothoff, W. H., & Johnson, G. V. W. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.017 · Cited by 455

Mutations causing neurodegenerative tauopathies

Goedert, M., & Jakes, R. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.007 · Cited by 438

Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau

Alonso, A. D. C., Grundke-Iqbal, I., Barra, H. S., & Iqbal, K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.1.298 · Cited by 437

Measurement of Phosphorylated Tau Epitopes in the Differential Diagnosisof Alzheimer Disease: A Comparative Cerebrospinal Fluid Study

Hampel, H., Buerger, K., Zinkowski, R., Teipel, S. J., Goernitz, A., Andreasen, N., Sjoegren, M., DeBernardis, J., Kerkman, D., Ishiguro, K., et al. (2004) · Archives of General Psychiatry · doi:10.1001/archpsyc.61.1.95 · Cited by 434

Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers

De Felice, F. G., Wu, D., Lambert, M. P., Fernandez, S. J., Velasco, P. T., Lacor, P. N., Bigio, E. H., Jerecic, J., Acton, P. J., Shughrue, P. J., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.029 · Cited by 432

Reversible memory loss in a mouse transgenic model of Alzheimer’s disease

Kotilinek, L. A., Bacskai, B., Westerman, M., Kawarabayashi, T., Younkin, L., Hyman, B. T., Younkin, S., & Ashe, K. H. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06331.2002 · Cited by 420

Increased level of active GSK‐3β in Alzheimer’s disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration

Leroy, K., Yilmaz, Z., & Brion, J. ‐. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00795.x · Cited by 404

Cytoskeletal elements of chick embryo fibroblasts revealed by detergent extraction

Brown, S. S., Levinson, W. E., & Spudich, J. A. (1976) · Journal of Supramolecular Structure · doi:10.1002/jss.400050203 · Cited by 387

Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease

Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507892200 · Cited by 379

MAP2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: an immunocytochemical study of cultured rat cerebrum

Kosik, K., & Finch, E. (1987) · The Journal of Neuroscience · doi:10.1523/jneurosci.07-10-03142.1987 · Cited by 368

Structure, Microtubule Interactions, and Paired Helical Filament Aggregation by Tau Mutants of Frontotemporal Dementias

Barghorn, S., Zheng‐Fischhöfer, Q., Ackmann, M., Biernat, J., von Bergen�, M., Mandelkow�, E., & Mandelkow�, E. (2000) · Biochemistry · doi:10.1021/bi000850r · Cited by 351

Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies

Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349

Fibrillar β-Amyloid Induces Microglial Phagocytosis, Expression of Inducible Nitric Oxide Synthase, and Loss of a Select Population of Neurons in the Rat CNS In Vivo

Weldon, D. T., Rogers, S. D., Ghilardi, J. R., Finke, M. P., Cleary, J. P., O’Hare, E., Esler, W. P., Maggio, J. E., & Mantyh, P. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-06-02161.1998 · Cited by 348

Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles

Trinczek, B., Ebneth, A., Mandelkow, E.-M., & Mandelkow, E. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.14.2355 · Cited by 344

Fluorescent speckle microscopy, a method to visualize the dynamics of protein assemblies in living cells

Waterman, C. M., Desai, A. B., Bulinski, J. C., & Salmon, E. D. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00515-5 · Cited by 336

Rapid movement of axonal neurofilaments interrupted by prolonged pauses

Wang, L., Ho, C., Sun, D., Liem, R. K. H., & Brown, A. (2000) · Nature Cell Biology · doi:10.1038/35004008 · Cited by 318

Microtubule Reduction in Alzheimer's Disease and Aging Is Independent of τ Filament Formation

Cash, A., Aliev, G., Siedlak, S. L., Nunomura, A., Fujioka, H., Zhu, X., Raina, A. K., Vinters, H. V., Tabaton, M., Johnson, T., et al. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64296-4 · Cited by 317

Monoclonal antibodies that target pathological assemblies of Aβ

Lambert, M. P., Velasco, P. T., Chang, L., Viola, K. L., Fernandez, S., Lacor, P. N., Khuon, D., Gong, Y., Bigio, E. H., Shaw, P., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04157.x · Cited by 314

Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases

Andreadis, A. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.010 · Cited by 311

Molecular Interactions among Protein Phosphatase 2A, Tau, and Microtubules

Sontag, E., Nunbhakdi‐Craig, V., Lee, G. S., Brandt, R., Kamibayashi, C., Kuret, J., White, C. L., Mumby, M. C., & Bloom, G. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25490 · Cited by 305

PS1 activates PI3K thus inhibiting GSK‐3 activity and tau overphosphorylation: effects of FAD mutations

Baki, L., Shioi, J., Wen, P. H., Shao, Z., Schwarzman, A. L., Gama-Sosa, M. A., Neve, R. L., & Robakis, N. K. R. K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600251 · Cited by 294

LPS- induced inflammation exacerbates phospho-tau pathology in rTg4510 mice

Lee, D. C., Rizer, J., Selenica, M.-L. B., Reid, P., Kraft, C., Johnson, A., Blair, L., Gordon, M. N., Dickey, C. A., & Morgan, D. (2010) · Journal of Neuroinflammation · doi:10.1186/1742-2094-7-56 · Cited by 293

Induction of Tau Pathology by Intracerebral Infusion of Amyloid-β-Containing Brain Extract and by Amyloid-β Deposition in APP × Tau Transgenic Mice

Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M. C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M., & Jucker, M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070403 · Cited by 281

Stabilization and post‐translational modification of microtubules during cellular morphogenesis

Bulinski, J. C., & Gundersen, G. G. (1991) · BioEssays · doi:10.1002/bies.950130605 · Cited by 274

Requirement of Phosphatidylinositol 3-Kinase in Focal Adhesion Kinase-promoted Cell Migration

Reiske, H. R., Kao, S.-C., Cary, L. A., Guan, J., Lai, J., & Chen, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12361 · Cited by 274

A Dynamic Relationship between Intracellular and Extracellular Pools of Aβ

Oddo, S., Caccamo, A., Smith, I. F., Green, K. N., & LaFerla, F. M. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.050593 · Cited by 261

The amino terminus of tau inhibits kinesin‐dependent axonal transport: Implications for filament toxicity

LaPointe, N. E., Morfini, G. A., Pigino, G. F., Gaisina, I. N., Kozikowski, A. P., Binder, L. I., & Brady, S. T. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21850 · Cited by 251

Time Course of the Development of Alzheimer-like Pathology in the Doubly Transgenic PS1+APP Mouse

Gordon, M. N., Holcomb, L. A., Jantzen, P. T., DiCarlo, G., Wilcock, D., Boyett, K. W., Connor, K., Melachrino, J., O'Callaghan, J. P., & Morgan, D. (2002) · Experimental Neurology · doi:10.1006/exnr.2001.7754 · Cited by 247

FAK Is the Upstream Signal Protein of the Phosphatidylinositol 3-Kinase-Akt Survival Pathway in Hydrogen Peroxide-induced Apoptosis of a Human Glioblastoma Cell Line

Sonoda, Y., Watanabe, S., Matsumoto, Y., Aizu-Yokota, E., & Kasahara, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.15.10566 · Cited by 245

Neurofilaments Are Transported Rapidly But Intermittently in Axons: Implications for Slow Axonal Transport

Roy, S., Coffee, P., Smith, G. M., Liem, R. K. H., Brady, S. T., & Black, M. M. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-18-06849.2000 · Cited by 245

Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP In Vivo Is Prevented by Immunotargeting Cellular Prion Protein

Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237

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 237

MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons

Mandelkow, E.-M., Thies, E., Trinczek, B., Biernat, J., & Mandelkow, E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401085 · Cited by 236

Intracranially Administered Anti-Αβ Antibodies Reduce β-Amyloid Deposition by Mechanisms Both Independent of and Associated with Microglial Activation

Wilcock, D. M., DiCarlo, G., Henderson, D., Jackson, J., Clarke, K., Ugen, K. E., Gordon, M. N., & Morgan, D. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-09-03745.2003 · Cited by 232

Tau-Mediated Cytotoxicity in a Pseudohyperphosphorylation Model of Alzheimer's Disease

Fath, T., Eidenmüller, J., & Brandt, R. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-22-09733.2002 · Cited by 232

Rapid Tyrosine Phosphorylation of Neuronal Proteins Including Tau and Focal Adhesion Kinase in Response to Amyloid-β Peptide Exposure: Involvement of Src Family Protein Kinases

Williamson, R., Scales, T., Clark, B. R., Gibb, G., Reynolds, C. H., Kellie, S., Bird, I. N., Varndell, I. M., Sheppard, P. W., Everall, I., et al. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-01-00010.2002 · Cited by 227

Role of cytoplasmic dynein in the axonal transport of microtubules and neurofilaments

He, Y., Francis, F., Myers, K. A., Yu, W., Black, M. M., & Baas, P. W. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200407191 · Cited by 225

Overactivation of glycogen synthase kinase‐3 by inhibition of phosphoinositol‐3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory

Liu, S. J., Zhang, A. H., Li, H. L., Wang, Q., Deng, H. M., Netzer, W. J., Xu, H., & Wang, J. Z. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02070.x · Cited by 224

Intrahippocampal LPS injections reduce Aβ load in APP+PS1 transgenic mice

DiCarlo, G. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00292-5 · Cited by 223

Altered Tau and Neurofilament Proteins in Neuro‐Degenerative Diseases: Diagnostic Implications for Alzheimer's Disease and Lewy Body Dementias

Trojanowski, J. Q., Schmidt, M. L., Shin, R., Bramblett, G. T., Rao, D., & Lee, V. M. ‐. (1993) · Brain Pathology · doi:10.1111/j.1750-3639.1993.tb00725.x · Cited by 214

Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity

Alonso, A. D. C., Li, B., Grundke-Iqbal, I., & Iqbal, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603214103 · Cited by 206

Developments in neuronal cell culture

Banker, G., & Goslin, K. (1988) · Nature · doi:10.1038/336185a0 · Cited by 195

Rapid Movement of Microtubules in Axons

Wang, L., & Brown, A. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01078-3 · Cited by 183

Stabilization and the cytoplasmic ground substance in detergent-opened cells and a structural and biochemical analysis of its composition.

Schliwa, M., Blerkom, J. V., & Porter, K. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4329 · Cited by 181

Lipopolysaccharide enhances synthesis of brain-derived neurotrophic factor in cultured rat microglia

Miwa, T., Furukawa, S., Nakajima, K., Furukawa, Y., & Kohsaka, S. (1997) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19971215)50:6 · Cited by 181

Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons.

Hirokawa, N., Funakoshi, T., Sato-Harada, R., & Kanai, Y. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.4.667 · Cited by 179

Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau

Li, B., Chohan, M. O., Grundke, I., & Iqbal, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0207-8 · Cited by 173

Molecular motors implicated in the axonal transport of tau and α-synuclein

Utton, M. A., Noble, W. J., Hill, J. E., Anderton, B. H., & Hanger, D. P. (2005) · Journal of Cell Science · doi:10.1242/jcs.02558 · Cited by 172

Progressive and spatially differentiated stability of microtubules in developing neuronal cells.

Lim, S., Sammak, P. J., & Borisy, G. G. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.1.253 · Cited by 169

Protein aggregation in the pathogenesis of familial and sporadic Parkinson's disease

McNaught, K. S. P., & Olanow, C. W. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.08.012 · Cited by 166

Swimming against the Tide: Mobility of the Microtubule-Associated Protein Tau in Neurons

Konzack, S., Thies, E., Marx, A., Mandelkow, E., & Mandelkow�, E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0927-07.2007 · Cited by 165

Rapid dynamics of the microtubule binding of ensconsin in vivo

Bulinski, J. C., Odde, D. J., Howell, B. J., Salmon, T. D., & Waterman, C. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.21.3885 · Cited by 158

Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A

Gong, C., Grundke, I., & Iqbal, K. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90400-6 · Cited by 156

Restoration of biological activity of Alzheimer abnormally phosphorylated τ by dephosphorylation with protein phosphatase-2A, −2B and −1

Wang, J., Grundke, I., & Iqbal, K. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(95)00316-k · Cited by 154

Increased tau Phosphorylation in Apolipoprotein E4 Transgenic Mice Is Associated with Activation of Extracellular Signal-regulated Kinase

Harris, F. M., Brecht, W. J., Xu, Q., Mahley, R. W., & Huang, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408127200 · Cited by 151

Alzheimer's Disease Abnormally Phosphorylated τ Is Dephosphorylated by Protein Phosphatase‐2B (Calcineurin)

Gong, C., Singh, T. J., Grundke, I., & Iqbal, K. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62020803.x · Cited by 145

Sorting mechanisms of Tau and MAP2 in neurons: Suppressed axonal transit of MAP2 and locally regulated microtubule binding

Kanai, Y., & Hirokawa, N. (1995) · Neuron · doi:10.1016/0896-6273(95)90298-8 · Cited by 144

Microglial Activation is Required for Aβ Clearance After Intracranial Injection of Lipopolysaccharide in APP Transgenic Mice

Herber, D. L., Mercer, M., Roth, L. M., Symmonds, K., Maloney, J. L., Wilson, N., Freeman, M. J., Morgan, D., & Gordon, M. N. (2007) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-007-9069-z · Cited by 143

Tau Therapeutic Strategies for the Treatment of Alzheimers Disease

Churcher, I. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606776743057 · Cited by 142

Efficacy of small‐molecule glycogen synthase kinase‐3 inhibitors in the postnatal rat model of tau hyperphosphorylation

Selenica, M. L., Jensen, H. S., Larsen, A. K., Pedersen, M. L., Helboe, L., Leist, M., & Lotharius, J. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707471 · Cited by 135

Microtubules released from the neuronal centrosome are transported into the axon

Ahmad, F. J., & Baas, P. W. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.8.2761 · Cited by 132

Tau interaction with microtubules in vivo

Samsonov, A., Yu, J.-Z., Rasenick, M., & Popov, S. V. (2004) · Journal of Cell Science · doi:10.1242/jcs.01531 · Cited by 129

Amyloid β peptide alters intracellular vesicle trafficking and cholesterol homeostasis

Liu, Y., Peterson, D. A., & Schubert, D. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13266 · Cited by 128

Antibodies against β‐amyloid reduce aβ oligomers, glycogen synthase kinase‐3β activation and τ phosphorylation in vivo and in vitro

Ma, Q., Lim, G. P., Harris‐White, M. E., Yang, F., Ambegaokar, S. S., Ubeda, O. J., Glabe, C. G., Teter, B., Frautschy, S. A., & Cole, G. M. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20734 · Cited by 126

Does my mouse have Alzheimer's disease?

Dodart, J., Mathis, C., Bales, K. R., & Paul, S. M. (2002) · Genes Brain & Behavior · doi:10.1034/j.1601-183x.2002.10302.x · Cited by 126

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

Involvement of in the abnormal hyperphosphorylation of tau and its reversal by Memantine

Chohan, M. O., Khatoon, S., Iqbal, I.-G., & Iqbal, K. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.06.021 · Cited by 124

Microtubule arrays in differentiated cells contain elevated levels of a post-translationally modified form of tubulin.

Gg, G., & Bulinski, J. C. (1986) · PubMed · Cited by 124

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

Aberrant Activation of Focal Adhesion Proteins Mediates Fibrillar Amyloid β-Induced Neuronal Dystrophy

Grace, E. A., & Busciglio, J. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-02-00493.2003 · Cited by 113

Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules

Aronov, S., Aranda, G., Behar, L., & Ginzburg, I. (2002) · Journal of Cell Science · doi:10.1242/jcs.00058 · Cited by 112

Cooexpression of FTDP-17 tau and GSK-3β in transgenic mice induce tau polymerization and neurodegeneration

Engel, T., Lucas, J. J., Gómez‐Ramos, P., Morán, M. A., Ávila, J., & Hernández, F. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.010 · Cited by 111

Human amyloid β‐induced neuroinflammation is an early event in neurodegeneration

Craft, J. M., Watterson, D. M., & Eldik, L. J. V. (2005) · Glia · doi:10.1002/glia.20306 · Cited by 111

Both Src-Dependent and -Independent Mechanisms Mediate Phosphatidylinositol 3-Kinase Regulation of Colony-Stimulating Factor 1-Activated Mitogen-Activated Protein Kinases in Myeloid Progenitors

Lee, A. W. ‐., & States, D. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6779-6798.2000 · Cited by 103

Amyloid Reduction by Amyloid- Vaccination Also Reduces Mouse Tau Pathology and Protects from Neuron Loss in Two Mouse Models of Alzheimer's Disease

Wilcock, D. M., Gharkholonarehe, N., Nostrand, W. E. V., Davis, J., Vitek, M. P., & Colton, C. A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1339-09.2009 · Cited by 98

Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's A beta peptide.

Zhang, C., Lambert, M. P., Bunch, C., Barber, K., Wade, W. S., Krafft, G. A., & Klein, W. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47238-9 · Cited by 98

Slow axonal transport and the genesis of neuronal morphology

Baas, P. W., & Buster, D. W. (2003) · Journal of Neurobiology · doi:10.1002/neu.10281 · Cited by 97

Dephosphorylation of microtubule‐associated protein tau by protein phosphatase‐1 and ‐2C and its implication in Alzheimer disease

Gong, C., Grundke, I., Damuni, Z., & Iqbal, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80247-5 · Cited by 96

Three distinct axonal transport rates for tau, tubulin, and other microtubule-associated proteins: evidence for dynamic interactions of tau with microtubules in vivo

Mercken, M. H., Fischer, I., Kosik, K. S., & Nixon, R. A. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-12-08259.1995 · Cited by 92

Direct evidence for coherent low velocity axonal transport of mitochondria

Miller, K. E., & Sheetz, M. P. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200510097 · Cited by 91

Convection-enhanced delivery and systemic mannitol increase gene product distribution of AAV vectors 5, 8, and 9 and increase gene product in the adult mouse brain

Carty, N., Lee, D. C., Dickey, C. A., Ceballos‐Diaz, C., Jansen‐West, K. R., Golde, T. E., Gordon, M. N., Morgan, D., & Nash, K. R. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.10.010 · Cited by 88

Advances in the development of biomarkers for Alzheimer’s disease: from CSF total tau and Aβ1–42 proteins to phosphorylated tau protein

Hampel, H. J., Goernitz, A., & Büerger, K. (2003) · Brain Research Bulletin · doi:10.1016/s0361-9230(03)00087-x · Cited by 88

Aging Analysis Reveals Slowed Tau Turnover and Enhanced Stress Response in a Mouse Model of Tauopathy

Dickey, C. A., Kraft, C., Jinwal, U. K., Koren, J., Johnson, A. G., Anderson, L. C., Lebson, L. A., Lee, D. C., Dickson, D. W., de Silva, R., et al. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080764 · Cited by 86

Axonal transport of tubulin in tit pioneer neurons in situ

Sabry, J. H., O’Connor, T. P., & Kirschner, M. W. (1995) · Neuron · doi:10.1016/0896-6273(95)90271-6 · Cited by 86

Rapid Alzheimer‐like phosphorylation of tau by the synergistic actions of non‐proline‐dependent protein kinases and GSK‐3

Singh, T. J., Haque, N., Grundke, I., & Iqbal, K. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01445-7 · Cited by 83

β/A4‐evoked degeneration of differentiated SH‐SY5Y human neuroblastoma cells

Lambert, M. P., Stevens, G. R., Sabo, S. L., Barber, K., Wang, G., Wade, W. S., Krafft, G. A., Snyder, S. W., Holzman, T. F., & Klein, W. L. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390404 · Cited by 78

Cystatin C reduces thein vitroformation of soluble Aβ1‐42 oligomers and protofibrils

Selenica, M. B., Wang, X., Ostergaard‐Pedersen, L., Westlind‐Danielsson, A., & GRUBB, A. O. (2006) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.1080/00365510601009738 · Cited by 71

Quantitative Analysis of Microtubule Transport in Growing Nerve Processes

Ma, Y., Shakiryanova, D. M., Vardya, I., & Popov, S. V. (2004) · Current Biology · doi:10.1016/j.cub.2004.03.061 · Cited by 71

Anomalously phosphorylated tau and Aβ fragments in the CSF correlates with cognitive impairment in MCI subjects

Maccioni, R. B., Manuel Lavados, M., Guillón, M., Mújica, C. L. D., BOSCH, R., FARIAS, G., & FUENTES, P. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.01.011 · Cited by 68

The Slow Axonal Transport of the Microtubule-Associated Protein Tau and the Transport Rates of Different Isoforms and Mutants in Cultured Neurons

Utton, M. A., Connell, J. W., Asuni, A. A., van Slegtenhorst, M., Hutton, M. L., de Silva, R., Lees, A. J., Miller, C. C. J., & Anderton, B. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06394.2002 · Cited by 66

Melatonin prevents cytoskeletal alterations and oxidative stress induced by okadaic acid in n1e-115 cells

Benítez‐King, G. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00085-2 · Cited by 66

GSK3α exhibits β‐catenin and tau directed kinase activities that are modulated by Wnt

Asuni, A. A., Hooper, C., Reynolds, C. H., Lovestone, S., Anderton, B. H., & Killick, R. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05243.x · Cited by 64

Tau neurofibrillary pathology and microtubule stability

Michaelis, M., Dobrowsky, R., & Li, G. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:19:3:289 · Cited by 60

Speckle microscopic evaluation of microtubule transport in growing nerve processes

Chang, S., Svitkina, T., Borisy, G. G., & Popov, S. V. (1999) · Nature Cell Biology · doi:10.1038/15629 · Cited by 58

Posttranslational Modifications of the C-Terminus of α-Tubulin in Adult Rat Brain: α4 Is Glutamylated at Two Residues

Redeker, V., Rossier, J., & Frankfurter, A. J. (1998) · Biochemistry · doi:10.1021/bi981335k · Cited by 55

A comparative study of the in vitro polymerization of tubulin in the presence of the microtubule-associated proteins MAP2 and tau.

Sandoval, I. V., & Vandekerckhove, J. S. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68915-5 · Cited by 52

Cell cycle-dependent changes in the dynamics of MAP 2 and MAP 4 in cultured cells.

Olmsted, J. B., Stemple, D. L., Saxton, W. M., Neighbors, B., & McIntosh, J. R. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.1.211 · Cited by 51

Intracranial administration of deglycosylated C-terminal-specific anti-Aβ antibody efficiently clears amyloid plaques without activating microglia in amyloid-depositing transgenic mice

Carty, N., Wilcock, D. M., Rosenthal, A., Grimm, J., Pons, J., Ronan, V., Gottschall, P. E., Gordon, M. N., & Morgan, D. (2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-11 · Cited by 50

Tau factor polymers are similar to paired helical filaments of Alzheimer's disease

de Garcini, E. M., Carrascosa, J. L., Correas, I., Nieto, A., & Ávila, J. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80304-1 · Cited by 50

MRS in presymptomatic MAPT mutation carriers

Kantarci, K., Boeve, B. F., Wszołek, Z. K., Rademakers, R., Whitwell, J. L., Baker, M., Senjem, M. L., Samikoglu, A. R., Knopman, D. S., Petersen, R. C., et al. (2010) · Neurology · doi:10.1212/wnl.0b013e3181f073c7 · Cited by 49

Neuritogenesis and neuronal differentiation promoted by 2,4‐dinitrophenol, a novel anti‐amyloidogenic compound

Wasilewska‐Sampaio, A. P., Silveira, M. S., Holub, O., Goecking, R., Gomes, F. C. A., Moura‐Neto, V., Linden, R., Ferreira, S. T., & Felice, F. G. D. (2005) · The FASEB Journal · doi:10.1096/fj.05-3812com · Cited by 45

PGH2‐derived levuglandin adducts increase the neurotoxicity of amyloid β1–42

Boutaud, O. G., Montine, T. J., Chang, L., Klein, W. L., & Oates, J. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03586.x · Cited by 44

Okadaic acid induces JNK activation, bim overexpression and mitochondrial dysfunction in cultured rat cortical neurons

Yoon, S.-Y., Choi, J., Yoon, J., Huh, J., & Kim, D. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.10.034 · Cited by 40

Aβ peptide enhances focal adhesion kinase/Fyn association in a rat CNS nerve cell line

Zhang, C., Qiu, H. E., Krafft, G. A., & Klein, W. L. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)12761-0 · Cited by 39

Transient Phosphatidylinositol 3-Kinase Inhibition Protects Immature Primary Cortical Neurons from Oxidative Toxicity via Suppression of Extracellular Signal-regulated Kinase Activation

Levinthal, D. J., & DeFranco, D. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314261200 · Cited by 39

Hyperphosphorylation-induced self assembly of murine tau: a comparison with human tau

Chohan, M. O., Haque, N., Alonso, A., El-Akkad, E., Grundke, I., Grover, A., & Iqbal, K. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0241-9 · Cited by 36

A monoclonal antibody against synthetic Aβ dimer assemblies neutralizes brain‐derived synaptic plasticity‐disrupting Aβ

O’Nuallain, B., Klyubin, I. V., Donald, J. M. M., Foster, J. S., Welzel, A. T., Barry, A. E., Dykoski, R. K., Cleary, J. P., Gebbink, M. F. B. G., Rowan, M. J., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07389.x · Cited by 33

Deregulation of the Phosphatidylinositol-3 Kinase Signaling Cascade Is Associated with Neurodegeneration in Npc1−/− Mouse Brain

Bi, X., Liu, J., Yao, Y., Baudry, M., & LYNCH, G. S. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61197-2 · Cited by 32

β‐Amyloid Protein Precursor and τ mRNA Levels Versus β‐Amyloid Plaque and Neurofibrillary Tangles in the Aged Human Brain

Oyama, F., Shimada, H., Oyama, R., Titani, K., & Ihara, Y. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb13388.x · Cited by 28

The specificity and stability of the triton-extracted cytoskeletal framework of gerbil fibroma cells

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Untitled work

(1999) · doi:10.1002/1531-8249(199912)46:6

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