Tau-directed approaches for the treatment of Alzheimer’s disease: focus on leuco-methylthioninium

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works

Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade

Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70299-6 · Cited by 4,806 · see citing works

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

Tracking pathophysiological processes in Alzheimer's disease: an updated hypothetical model of dynamic biomarkers

Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396 · see citing works

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works

Clinical and biomarker changes in dominantly inherited Alzheimer's disease

Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814 · see citing works

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 · see citing works

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 · see citing works

Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature

Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · see citing works

Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.

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

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979 · see citing works

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 · see citing works

Transmission and spreading of tauopathy in transgenic mouse brain

Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works

Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories

Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656 · see citing works

2015 Alzheimer's disease facts and figures

Alzheimer's Association (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.02.003 · Cited by 1,641 · see citing works

The roles of intracellular protein-degradation pathways in neurodegeneration

Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625 · see citing works

Propagation of Tau Pathology in a Model of Early Alzheimer's Disease

de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works

Propagation of Tau Misfolding from the Outside to the Inside of a Cell

Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · see citing works

Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms

Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,114 · see citing works

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939 · see citing works

O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775 · see citing works

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724 · see citing works

Evolution of the neuropathology of Alzheimer's disease

Braak, H., & Braak, E. (1996) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1996.tb05866.x · Cited by 710 · see citing works

Amyloid-β and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice

Rhein, V., Song, X., Wiesner, A., Ittner, L. M., Baysang, G., Meier, F., Ozmen, L., Bluethmann, H., Dröse, S., Brandt, U., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905529106 · Cited by 655 · see citing works

Clinical trials and late‐stage drug development for <scp>A</scp>lzheimer's disease: an appraisal from 1984 to 2014

Schneider, L. S., Mangialasche, F., Andreasen, N., Feldman, H., Giacobini, E., Jones, R., Mantua, V., Mecocci, P., Pani, L., Winblad, B., et al. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12191 · Cited by 651 · see citing works

Tau protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631 · see citing works

Mechanisms of tau-induced neurodegeneration

Iqbal, K., Liu, F., Gong, C.-X., Alonso, A. D. C., & Grundke-Iqbal, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0486-3 · Cited by 628 · see citing works

Structural characterization of the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novák, M., Edwards, P. C., Klug, A., Tichelaar, W., & Crowther, R. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4884 · Cited by 597 · see citing works

Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress.

Yan, S. D., Chen, X., Schmidt, A. M., Brett, J., Godman, G., Zou, Y. S., Scott, C. W., Caputo, C., Frappier, T., & Smith, M. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7787 · Cited by 565 · see citing works

Preclinical Alzheimer's disease and its outcome: a longitudinal cohort study

Vos, S. J., Xiong, C., Visser, P. J., Jasielec, M. S., Hassenstab, J., Grant, E. A., Cairns, N. J., Morris, J. C., Holtzman, D. M., & Fagan, A. M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70194-7 · Cited by 564 · see citing works

Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration

Wang, J., Grundke, I., & Iqbal, K. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05226.x · Cited by 553 · see citing works

Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines.

Wischik, C. M., Edwards, P. C., Lai, R. Y., Roth, M., & Harrington, C. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.11213 · Cited by 547 · see citing works

Effects of α-Synuclein Immunization in a Mouse Model of Parkinson’s Disease

Masliah, E., Rockenstein, E., Adame, A., Alford, M., Crews, L., Hashimoto, M., Seubert, P., Lee, M., Goldstein, J., Chilcote, T., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.010 · Cited by 542 · see citing works

Inhibition of Heparin-induced Tau Filament Formation by Phenothiazines, Polyphenols, and Porphyrins

Taniguchi, S., Suzuki, N., Masuda, M., Hisanaga, S., Iwatsubo, T., Goedert, M., & Hasegawa, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408714200 · Cited by 540 · see citing works

A Phase II Trial of Tideglusib in Alzheimer's Disease

Lovestone, S., for the ARGO investigators, Boada, M., Dubois, B., Hüll, M., Rinne, J. O., Huppertz, H.-J., Calero, M., Andrés, M. V., Gómez-Carrillo, B., et al. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-141959 · Cited by 536 · see citing works

Inhibition of nitric oxide synthesis by methylene blue

Mayer, B., Brünner, F., & Schmidt, K. (1993) · Biochemical Pharmacology · doi:10.1016/0006-2952(93)90072-5 · Cited by 536 · see citing works

Clinical core of the Alzheimer's disease neuroimaging initiative: Progress and plans

Aisen, P. S. S., Petersen, R. C., Donohue, M., Gamst, A. C., Raman, R., Thomas, R. G., Walter, S., Trojanowski, J. Q., Shaw, L. M. J., Beckett, L. A., et al. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.03.006 · Cited by 516 · see citing works

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works

Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms

Andorfer, C., Acker, C. M., Kress, Y., Hof, P. R., Duff, K., & Davies, P. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4637-04.2005 · Cited by 511 · see citing works

Immunotherapy Targeting Pathological Tau Conformers in a Tangle Mouse Model Reduces Brain Pathology with Associated Functional Improvements

Asuni, A. A., Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2361-07.2007 · Cited by 506 · see citing works

Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport

Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L. (2010) · Science · doi:10.1126/science.1194653 · Cited by 486 · 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

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 · see citing works

Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death.

Stadelmann, C., Deckwerth, T., Srinivasan, A., Bancher, C., Brück, W., Jellinger, K. A., & Lassmann, H. (1999) · American Journal of Pathology · doi:10.1016/s0002-9440(10)65460-0 · Cited by 449 · see citing works

Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies

Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2959 · Cited by 440 · see citing works

“Lest we forget you — methylene blue …”

Schirmer, R. H., Adler, H., Pickhardt, M., & Mandelkow�, E. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.12.012 · Cited by 416 · see citing works

Azaphilones: Chemistry and Biology

Gao, J., Yang, S., & Qin, J. (2013) · Chemical Reviews · doi:10.1021/cr300402y · Cited by 409 · see citing works

The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice

Zhang, B., Carroll, J., Trojanowski, J. Q., Yao, Y., Iba, M., Potuzak, J. S., Hogan, A.-M. L., Xie, S. X., Ballatore, C., Smith, A. B., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4922-11.2012 · Cited by 401 · see citing works

Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament

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

Complete Sequence of a Novel Protein Containing a Femtomolar‐Activity‐Dependent Neuroprotective Peptide

Bassan, M., Zamostiano, R., Davidson, A., Pinhasov, A., Giladi, E., Perl, O., Bassan, H., Blat, C., Gibney, G., Glazner, G. W., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0721283.x · Cited by 394 · see citing works

Pharmacokinetics and organ distribution of intravenous and oral methylene blue

Peter, C., Hongwan, D., Kupfer, A., & Lauterburg, B. H. (2000) · European Journal of Clinical Pharmacology · doi:10.1007/s002280000124 · Cited by 374 · see citing works

Small Molecule Inhibitors of α-Synuclein Filament Assembly

Masuda, M., Suzuki, N., Taniguchi, S., Oikawa, T., Nonaka, T., Iwatsubo, T., Hisanaga, S., Goedert, M., & Hasegawa, M. (2006) · Biochemistry · doi:10.1021/bi0600749 · Cited by 367 · see citing works

The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine

Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28741 · Cited by 361 · see citing works

Cerebrospinal Fluid Tau and β-Amyloid: How Well Do These Biomarkers Reflect Autopsy-Confirmed Dementia Diagnoses?

Clark, C. M., Xie, S., Chittams, J., Ewbank, D., Peskind, E., Galasko, D., Morris, J. C., McKeel, D. W., Farlow, M., Weitlauf, S. L., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1696 · Cited by 357 · see citing works

Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells

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

Treatment of Alzheimer's Disease with the GSK-3 Inhibitor Tideglusib: A Pilot Study

del Ser, T., Steinwachs, K. C., Gertz, H. J., Andrés, M. V., Gómez-Carrillo, B., Medina, M., Vericat, J. A., Redondo, P., Fleet, D., & León, T. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-120805 · Cited by 329 · see citing works

A phase 2 trial of the GSK‐3 inhibitor tideglusib in progressive supranuclear palsy

Tolosa, E., Litvan, I., Höglinger, G. U., Burn, D., Lees, A., Andrés, M. V., Gómez‐Carrillo, B., León, T., del Ser, T., & for the TAUROS Investigators (2014) · Movement Disorders · doi:10.1002/mds.25824 · Cited by 320 · see citing works

A data-driven model of biomarker changes in sporadic Alzheimer’s disease

Young, A. L., Oxtoby, N. P., Daga, P., Cash, D. M., Fox, N. C., Ourselin, S., Schott, J. M., & Alexander, D. C. (2014) · Brain · doi:10.1093/brain/awu176 · Cited by 308 · see citing works

Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306 · see citing works

Brain Levels of Microtubule‐Associated Protein τ Are Elevated in Alzheimer's Disease: A Radioimmuno‐Slot‐Blot Assay for Nanograms of the Protein

Khatoon, S., Grundke, I., & Iqbal, K. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09432.x · Cited by 304 · see citing works

Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo

Congdon, E. E., Wu, J. W., Myeku, N., Figueroa, Y. H., Herman, M., Marinec, P. S., Gestwicki, J. E., Dickey, C. A., Yu, W. H., & Duff, K. E. (2012) · Autophagy · doi:10.4161/auto.19048 · Cited by 297 · see citing works

Longitudinal Cerebrospinal Fluid Biomarker Changes in Preclinical Alzheimer Disease During Middle Age

Sutphen, C. L., Jasielec, M. S., Shah, A. R., Macy, E. M., Xiong, C., Vlassenko, A. G., Benzinger, T. L. S., Stoops, E., Vanderstichele, H., Brix, B., et al. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.1285 · Cited by 294 · see citing works

Davunetide in patients with progressive supranuclear palsy: a randomised, double-blind, placebo-controlled phase 2/3 trial

Boxer, A. L., Lang, A. E., Grossman, M., Knopman, D. S., Miller, B. L., Schneider, L. S., Doody, R. S., Lees, A., Golbe, L. I., Williams, D. R., et al. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70088-2 · Cited by 294 · see citing works

Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins

Sinha, S., Lopes, D., Du, Z., Pang, E. S., Shanmugam, A., Lomakin, A., Talbiersky, P., Tennstaedt, A., McDaniel, K., Bakshi, R., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206279b · Cited by 280 · see citing works

Passive Immunization with Tau Oligomer Monoclonal Antibody Reverses Tauopathy Phenotypes without Affecting Hyperphosphorylated Neurofibrillary Tangles

Castillo-Carranza, D. L., Sengupta, U., Guerrero-Muñoz, M. J., Lasagna-Reeves, C. A., Gerson, J. E., Singh, G., Estes, D. M., Barrett, A. D. T., Dineley, K. T., Jackson, G. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3192-13.2014 · Cited by 278 · cited 1× · see citing works

Methylene blue and serotonin toxicity: inhibition of monoamine oxidase A (MAO A) confirms a theoretical prediction

Ramsay, R. R., Dunford, C., & Gillman, P. K. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707430 · Cited by 276 · see citing works

Immunotherapy Targeting Pathological Tau Prevents Cognitive Decline in a New Tangle Mouse Model

Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4363-10.2010 · Cited by 272 · see citing works

Tau Aggregation Inhibitor Therapy: An Exploratory Phase 2 Study in Mild or Moderate Alzheimer's Disease

Wischik, C. M., Staff, R. T., Wischik, D. J., Bentham, P., Murray, A. D., Storey, J. M. D., Kook, K. A., & Harrington, C. R. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-142874 · Cited by 269 · see citing works

Tau-aggregation inhibitor therapy for Alzheimer's disease

Wischik, C. M., Harrington, C. R., & Storey, J. M. D. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.008 · Cited by 263 · see citing works

Efficacy and Safety of A Liposome-Based Vaccine against Protein Tau, Assessed in Tau.P301L Mice That Model Tauopathy

Theunis, C., Crespo-Biel, N., Gafner, V., Pihlgren, M., López-Deber, M. P., Reis, P., Hickman, D. T., Adolfsson, O., Chuard, N., Ndao, D. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072301 · Cited by 259 · see citing works

Tau truncation during neurofibrillary tangle evolution in Alzheimer’s disease

Guillozet-Bongaarts, A. L., Garcia-Sierra, F., Reynolds, M. R., Horowitz, P. M., Fu, Y., Wang, T., Cahill, M. E., Bigio, E. H., Berry, R. W., & Binder, L. I. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.09.019 · Cited by 256 · see citing works

Alternative Mitochondrial Electron Transfer as a Novel Strategy for Neuroprotection

Wen, Y., Li, W., Poteet, E. C., Xie, L., Tan, C., Yan, L., Ju, X., Liu, R., Qian, H., Marvin, M. A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208447 · Cited by 251 · see citing works

First-in-man tau vaccine targeting structural determinants essential for pathological tau–tau interaction reduces tau oligomerisation and neurofibrillary degeneration in an Alzheimer’s disease model

Kontseková, E., Žilka, N., Kováčech, B., Novák, P., & Novák, M. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt278 · Cited by 248 · see citing works

Tau immunotherapy for Alzheimer's disease

Pedersen, J. T., & Sigurdsson, E. M. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.03.003 · Cited by 247 · see citing works

Caspase-9 Activation and Caspase Cleavage of tau in the Alzheimer's Disease Brain

Rohn, T. T., Rissman, R. A., Davis, M. C., Kim, Y., Cotman, C. W., & Head, E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0549 · Cited by 242 · see citing works

Memory and mental status correlates of modified Braak staging

Grober, E. H., Dickson, D. W., Sliwinski, M. J., Herman Buschke, L., Katz, M., Crystal, H., & Lipton, R. B. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00063-9 · Cited by 235 · see citing works

Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability

Jinwal, U. K., Miyata, Y., Koren, J., Jones, J. R., Trotter, J. H., Chang, L., O’Leary, J. C., Morgan, D., Lee, D. C., Shults, C. L., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3345-09.2009 · Cited by 231 · see citing works

Human secreted tau increases amyloid-beta production

Bright, J., Hussain, S., Dang, V., Wright, S., Cooper, B., Byun, T., Ramos, C., Singh, A., Parry, G., Stagliano, N., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.09.007 · Cited by 230 · see citing works

Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia

Ittner, L. M., Fath, T., Ke, Y. D., Bi, M., van Eersel, J., Li, K. M., Gunning, P. W., & Götz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808084105 · Cited by 219 · see citing works

Activity-Dependent Neuroprotective Protein Snippet NAP Reduces Tau Hyperphosphorylation and Enhances Learning in a Novel Transgenic Mouse Model

Vulih-Shultzman, I., Pinhasov, A., Mandel, S., Grigoriadis, N., Touloumi, O., Pittel, Z., & Gozes, I. (2007) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.129551 · Cited by 219 · see citing works

Methylene Blue Inhibits Amyloid Aβ Oligomerization by Promoting Fibrillization

Necula, M., Breydo, L., Milton, S., Kayed, R., van der Veer, W. E., Tone, P., & Glabe, C. G. (2007) · Biochemistry · doi:10.1021/bi700411k · Cited by 213 · see citing works

Towards a Pharmacophore for Amyloid

Landau, M., Sawaya, M. R., Faull, K. F., Laganowsky, A. D., Jiang, L., Sievers, S. A., Liu, J., Barrio, J. R., & Eisenberg, D. S. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001080 · Cited by 209 · see citing works

Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice

Kins, S., Crameri, A., Evans, D. R. H., Hemmings, B. A., Nitsch, R. M., & Götz, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102621200 · Cited by 203 · see citing works

Neuronal uptake of tau/pS422 antibody and reduced progression of tau pathology in a mouse model of Alzheimer‘s disease

Collin, L., Bohrmann, B., Göpfert, U., Oroszlan‐Szovik, K., Ozmen, L., & Grüninger, F. (2014) · Brain · doi:10.1093/brain/awu213 · Cited by 203 · see citing works

The green tea polyphenol (−)‐epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios

Wobst, H. J., Sharma, A. M., Diamond, M. I., Wanker, E. E., & Bieschke, J. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.11.026 · Cited by 202 · see citing works

Inhibition 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

Antibody Uptake into Neurons Occurs Primarily via Clathrin-dependent Fcγ Receptor Endocytosis and Is a Prerequisite for Acute Tau Protein Clearance

Congdon, E. E., Gu, J., Sait, H. B. R., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491001 · Cited by 195 · see citing works

Methylene Blue Reduces Aβ Levels and Rescues Early Cognitive Deficit by Increasing Proteasome Activity

Medina, D. X., Caccamo, A., & Oddo, S. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2010.00430.x · Cited by 194 · see citing works

Color and Constitution: One Hundred Years of Research

Dähne, S. (1978) · Science · doi:10.1126/science.199.4334.1163 · Cited by 194 · see citing works

Adverse Effects of Methylene Blue on the Central Nervous System

Vutskits, L., Briner, A., Klauser, P., Gascon, E., Dayer, A. G., Kiss, J. Z., Müller, D., Licker, M. J., & Morel, D. R. (2008) · Anesthesiology · doi:10.1097/aln.0b013e3181684be4 · Cited by 188 · see citing works

The Glutathione System: A New Drug Target in Neuroimmune Disorders

Morris, G., Anderson, G., Dean, O. M., Berk, M., Gałecki, P., Martín-Subero, M., & Maes, M. H. J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8705-x · Cited by 187 · see citing works

Staging of Cytoskeletal and β-Amyloid Changes in Human Isocortex Reveals Biphasic Synaptic Protein Response during Progression of Alzheimer’s Disease

Mukaetova‐Ladinska, E. B., García‐Sierra, F., Hurt, J., Gertz, H.-J., Xuereb, J. H., Hills, R., Brayne, C., Huppert, F. A., Paykel, E. S., McGee, M. A., et al. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64573-7 · Cited by 187 · see citing works

Curcumin Prevents Aggregation in α-Synuclein by Increasing Reconfiguration Rate

Ahmad, B., & Lapidus, L. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.325548 · Cited by 185 · see citing works

Tau protein and tau aggregation inhibitors

Bulic, B., Pickhardt, M., Mandelkow, E., & Mandelkow�, E. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.01.016 · Cited by 179 · see citing works

Tauopathy-like Abnormalities and Neurologic Deficits in Mice Immunized With Neuronal Tau Protein

Rosenmann, H., Grigoriadis, N., Karussis, D., Boimel, M., Touloumi, O., Ovadia, H., & Abramsky, O. (2006) · Archives of Neurology · doi:10.1001/archneur.63.10.1459 · Cited by 178 · see citing works

Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden

O’Leary, J. C., Li, Q., Marinec, P. S., Blair, L. J., Congdon, E. E., Johnson, A. G., Jinwal, U. K., Koren, J., Jones, J. R., Kraft, C., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-45 · Cited by 176 · see citing works

Cinnamon extract inhibits tau aggregation associated with Alzheimer’s disease in vitro

Peterson, D. W., George, R. C., Scaramozzino, F., LaPointe, N. E., Anderson, R. A., Graves, D. J., & Lew, J. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1083 · Cited by 171 · see citing works

Two Novel Tau Antibodies Targeting the 396/404 Region Are Primarily Taken Up by Neurons and Reduce Tau Protein Pathology

Gu, J., Congdon, E. E., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494922 · Cited by 163 · see citing works

Methylene blue upregulates Nrf2/ARE genes and prevents tau-related neurotoxicity

Stack, C., Jainuddin, S., Elipenahli, C., Gerges, M., Starkova, N. N., Starkov, A. A., Jové, M., Portero‐Otín, M., Launay, N., Pujol, A., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu080 · Cited by 159 · see citing works

Convergence of Amyloid-β and Tau Pathologies on Mitochondria In Vivo

Eckert, A., Schulz, K. L., Rhein, V. F., & Götz, J. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8109-5 · Cited by 158 · see citing works

Rhodanine‐Based Tau Aggregation Inhibitors in Cell Models of Tauopathy

Bulic, B., Pickhardt, M., Khlistunova, I., Biernat, J., Mandelkow, E., Mandelkow�, E., & Waldmann, H. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200704051 · Cited by 158 · see citing works

Activity-Dependent Neurotrophic Factor: Intranasal Administration of Femtomolar-Acting Peptides Improve Performance in a Water Maze

Gozes, I., Giladi, E., Pinhasov, A., Bardea, A., & Brenneman, D. E. (2000) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)39336-x · Cited by 157 · see citing works

Phosphorylated Tau Interacts with c-Jun N-terminal Kinase-interacting Protein 1 (JIP1) in Alzheimer Disease

Ittner, L. M., Ke, Y. D., & Götz, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014472 · Cited by 156 · see citing works

Mechanistic Basis of Phenothiazine‐Driven Inhibition of Tau Aggregation

Akoury, E., Pickhardt, M., Gajda, M. J., Biernat, J., Mandelkow�, E., & Zweckstetter, M. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208290 · Cited by 151 · see citing works

Site-Specific Nitration and Oxidative Dityrosine Bridging of the τ Protein by Peroxynitrite: Implications for Alzheimer's Disease

Reynolds, M. R., Berry, R. W., & Binder, L. I. (2005) · Biochemistry · doi:10.1021/bi047982v · Cited by 149 · see citing works

Neuroprotective Actions of Methylene Blue and Its Derivatives

Poteet, E. C., Winters, A., Yan, L., Shufelt, K., Green, K. N., Simpkins, J. W., Wen, Y., & Yang, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048279 · Cited by 148 · see citing works

Interplay between Cyclin-Dependent Kinase 5 and Glycogen Synthase Kinase 3β Mediated by Neuregulin Signaling Leads to Differential Effects on Tau Phosphorylation and Amyloid Precursor Protein Processing

Wen, Y., Planel, E., Herman, M., Figueroa, H. Y., Wang, L., Liu, L., Lau, L.-F., Yu, W. H., & Duff, K. E. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-07.2008 · Cited by 145 · see citing works

Aminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation

Crowe, A., James, M. J., Lee, V. M.-Y., Smith, A. B., Trojanowski, J. Q., Ballatore, C., & Brunden, K. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.436006 · Cited by 143 · see citing works

Tau Nitration Occurs at Tyrosine 29 in the Fibrillar Lesions of Alzheimer's Disease and Other Tauopathies

Reynolds, M. R., Reyes, J. F., Fu, Y., Bigio, E. H., Guillozet-Bongaarts, A. L., Berry, R. W., & Binder, L. I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2143-06.2006 · Cited by 140 · see citing works

Preventive methylene blue treatment preserves cognition in mice expressing full-length pro-aggregant human Tau

Hochgräfe, K., Sydow, A., Matenia, D., Cadinu, D., Könen, S., Petrova, O. M., Pickhardt, M., Goll, P., Morellini, F., Mandelkow�, E., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0204-4 · Cited by 137 · see citing works

Strong Gametocytocidal Effect of Methylene Blue-Based Combination Therapy against Falciparum Malaria: A Randomised Controlled Trial

Coulibaly, B., Zoungrana, A., Mockenhaupt, F. P., Schirmer, R. H., Klose, C., Mansmann, U., Meissner, P. E., & Müller, O. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005318 · Cited by 133 · see citing works

Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy

Arai, T., Hasegawa, M., Nonoka, T., Kametani, F., Yamashita, M., Hosokawa, M., Niizato, K., Tsuchiya, K., Kobayashi, Z., Ikeda, K., et al. (2010) · Neuropathology · doi:10.1111/j.1440-1789.2009.01089.x · Cited by 132 · see citing works

Complex Disposition of Methylthioninium Redox Forms Determines Efficacy in Tau Aggregation Inhibitor Therapy for Alzheimer’s Disease

Baddeley, T. C., McCaffrey, J., Storey, J. M. D., Cheung, J. K. S., Melis, V., Horsley, D., Harrington, C. R., & Wischik, C. M. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.219352 · Cited by 128 · see citing works

Immunotherapy for Alzheimer‘s Disease: From Anti-β-Amyloid to Tau-Based Immunization Strategies

Panza, F., Frisardi, V., Solfrizzi, V., Imbimbo, B. P., Logroscino, G., Santamato, A., Greco, A., Seripa, D., & Pilotto, A. (2012) · Immunotherapy · doi:10.2217/imt.11.170 · Cited by 125 · see citing works

Phenylthiazolyl-Hydrazide and Its Derivatives Are Potent Inhibitors of τ Aggregation and Toxicity in Vitro and in Cells

Pickhardt, M., Larbig, G., Khlistunova, I., Çoksezen, A., Meyer, B., Mandelkow, E., Schmidt, B., & Mandelkow�, E. (2007) · Biochemistry · doi:10.1021/bi700878g · Cited by 125 · see citing works

Phosphoprotein Phosphatase 2A: A Novel Druggable Target for Alzheimer’s Disease

Voronkov, M. V., Braithwaite, S. P., & Stock, J. B. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.47 · Cited by 121 · 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

Interaction of Cinnamaldehyde and Epicatechin with Tau: Implications of Beneficial Effects in Modulating Alzheimer's Disease Pathogenesis

George, R. C., Lew, J., & Graves, D. J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122113 · Cited by 112 · see citing works

Identification of structural determinants on tau protein essential for its pathological function: novel therapeutic target for tau immunotherapy in Alzheimer’s disease

Kontsekova, E., Zilka, N., Kovacech, B., Skrabana, R., & Novak, M. (2014) · Alzheimer's Research &amp; Therapy · doi:10.1186/alzrt277 · Cited by 112 · see citing works

Methylene blue and dimebon inhibit aggregation of TDP‐43 in cellular models

Yamashita, M., Nonaka, T., Arai, T., Kametani, F., Buchman, V. L., Ninkina, N. N., Бачурин, С. О., Akiyama, H., Goedert, M., & Hasegawa, M. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.06.042 · Cited by 110 · see citing works

τ Protein from Alzheimer's Disease Patients Is Glycated at Its Tubulin‐Binding Domain

Ledesma, M. D., Bonay, P., & Avila, J. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65041658.x · Cited by 109 · see citing works

Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease

Iqbal, K., & Grundke, I. (1991) · Molecular Neurobiology · doi:10.1007/bf02935561 · Cited by 108 · see citing works

Cellular Models of Aggregation-dependent Template-directed Proteolysis to Characterize Tau Aggregation Inhibitors for Treatment of Alzheimer Disease

Harrington, C. R., Storey, J. M. D., Clunas, S., Harrington, K. A., Horsley, D., Ishaq, A., Kemp, S. J., Larch, C. P., Marshall, C., Nicoll, S. L., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616029 · Cited by 107 · see citing works

Natural Products As A Rich Source Of Tau-Targeting Drugs For Alzheimer’s Disease

Calcul, L., Zhang, B., Jinwal, U. K., Dickey, C. A., & Baker, B. J. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.124 · Cited by 107 · see citing works

Review: The phenothiazinium chromophore and the evolution of antimalarial drugs

WAINWRIGHT, M. S., & Amaral, L. (2005) · Tropical Medicine & International Health · doi:10.1111/j.1365-3156.2005.01417.x · Cited by 107 · see citing works

Towards Disease-Modifying Treatment of Alzheimers Disease: Drugs Targeting β -Amyloid

Frisardi, V., Solfrizzi, V., Imbimbo, B. P., Capurso, C. A., D’Introno, A., Colacicco, A. M., Vendemiale, G., Seripa, D., Pilotto, A., Capurso, C. A., et al. (2010) · Current Alzheimer Research · doi:10.2174/156720510790274400 · Cited by 107 · see citing works

Methylthioninium chloride reverses cognitive deficits induced by scopolamine: comparison with rivastigmine

Deiana, S., Harrington, C. R., Wischik, C. M., & Riedel, G. (2008) · Psychopharmacology · doi:10.1007/s00213-008-1394-2 · Cited by 106 · see citing works

Ligand-Dependent Inhibition and Reversal of Tau Filament Formation

Chirita, C. N., Necula, M., & Kuret, J. (2004) · Biochemistry · doi:10.1021/bi036094h · Cited by 104 · see citing works

Stimulation of respiration by methylene blue in rat liver mitochondria

Visarius, T. M., Stucki, J. W., & Lauterburg, B. H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00767-9 · Cited by 103 · see citing works

High throughput screening for small molecule inhibitors of heparin-induced tau fibril formation

Crowe, A., Ballatore, C., Hyde, E. G., Trojanowski, J. Q., & Lee, V. M. ‐. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.056 · Cited by 101 · see citing works

Identification of Aminothienopyridazine Inhibitors of Tau Assembly by Quantitative High-Throughput Screening

Crowe, A., Huang, W., Ballatore, C., Johnson, R. L., Hogan, A. L., Huang, R., Wichterman, J., McCoy, J. G., Huryn, D. M., Auld, D. S., et al. (2009) · Biochemistry · doi:10.1021/bi9006435 · Cited by 101 · see citing works

Methylene Blue Modulates Huntingtin Aggregation Intermediates and Is Protective in Huntington's Disease Models

Sontag, E. M., Lotz, G. P., Agrawal, N., Tran, A., Aron, R., Yang, G., Necula, M., Lau, A., Finkbeiner, S. M., Glabe, C. G., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0895-12.2012 · Cited by 101 · 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

Molecular Basis for Preventing α-Synuclein Aggregation by a Molecular Tweezer

Acharya, S., Safaie, B. M., Wongkongkathep, P., Ivanova, M. I., Attar, A., Klärner, F. G., Schrader, T. H., Loo, J. A., Bitan, G., & Lapidus, L. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.524520 · Cited by 97 · see citing works

Aggregation of Detergent-insoluble Tau Is Involved in Neuronal Loss but Not in Synaptic Loss

Kimura, T., Fukuda, T., Sahara, N., Yamashita, S., Murayama, M., Mizoroki, T., Yoshiike, Y., Lee, B., Sotiropoulos, I., Maeda, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136630 · Cited by 97 · see citing works

Protection of primary neurons and mouse brain from Alzheimer's pathology by molecular tweezers

Attar, A., Ripoli, C., Riccardi, E., Maiti, P., Puma, D. D. L., Liu, T., Hayes, J. D., Jones, M. R., Lichti-Kaiser, K., Yang, F., et al. (2012) · Brain · doi:10.1093/brain/aws289 · Cited by 93 · see citing works

Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion

Ahmad, B., Chen, Y., & Lapidus, L. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109526109 · Cited by 92 · see citing works

Effects of oxidized and reduced forms of methylthioninium in two transgenic mouse tauopathy models

Melis, V., Magbagbeolu, M., Rickard, J. E., Horsley, D., Davidson, K., Harrington, K. A., Goatman, K. A., Goatman, E. A., Deiana, S., Close, S., et al. (2015) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000133 · Cited by 91 · see citing works

Cyanine Dye N744 Inhibits Tau Fibrillization by Blocking Filament Extension: Implications for the Treatment of Tauopathic Neurodegenerative Diseases

Necula, M., Chirita, C. N., & Kuret, J. (2005) · Biochemistry · doi:10.1021/bi050387o · Cited by 89 · see citing works

The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics

Pritchard, S. M., Dolan, P. J., Vitkus, A., & Johnson, G. V. W. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01273.x · Cited by 89 · see citing works

Methylene Blue Reduced Abnormal Tau Accumulation in P301L Tau Transgenic Mice

Hosokawa, M., Arai, T., Masuda‐Suzukake, M., Nonaka, T., Yamashita, M., Akiyama, H., & Hasegawa, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052389 · Cited by 89 · see citing works

Modulation of Tau Protein Fibrillization by Oleocanthal

Monti, M. C., Margarucci, L., Riccio, R., & Casapullo, A. (2012) · Journal of Natural Products · doi:10.1021/np300384h · Cited by 88 · see citing works

“Clicked” Sugar–Curcumin Conjugate: Modulator of Amyloid-β and Tau Peptide Aggregation at Ultralow Concentrations

Dolai, S., Shi, W., Corbo, C. P., Sun, C., Averick, S. E., Obeysekera, D., Farid, M., Alonso, A. D. C., Banerjee, P., & Raja, K. S. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200088r · Cited by 87 · see citing works

The carboxy‐terminal fragment of inhibitor‐2 of protein phosphatase‐2A induces Alzheimer disease pathology and cognitive impairment

Wang, X., Blanchard, J., Kohlbrenner, E., Clement, N., Linden, R. M., Radu, A., Grundke, I., & Iqbal, K. (2010) · The FASEB Journal · doi:10.1096/fj.10-158477 · Cited by 81 · see citing works

Tangle-Bearing Neurons Survive Despite Disruption of Membrane Integrity in a Mouse Model of Tauopathy

de Calignon, A., Spires-Jones, T. L., Pitstick, R., Carlson, G. A., & Hyman, B. T. (2009) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e3181a9fc66 · Cited by 81 · see citing works

Methylene blue fails to inhibit Tau and polyglutamine protein dependent toxicity in zebrafish

van Bebber, F., Paquet, D., Hruscha, A., Schmid, B., & Haass, C. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.03.023 · Cited by 77 · see citing works

Inhibition of Tau Filament Formation by Conformational Modulation

Akoury, E., Gajda, M. J., Pickhardt, M., Biernat, J., Pornsuwan, S., Griesinger, C., Mandelkow�, E., & Zweckstetter, M. (2013) · Journal of the American Chemical Society · doi:10.1021/ja312471h · Cited by 76 · see citing works

Microtubule-associated protein tau as a therapeutic target in Alzheimer's disease

Iqbal, K., Gong, C., & Liu, F. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.870156 · Cited by 76 · see citing works

Amyloid-directed monoclonal antibodies for the treatment of Alzheimer’s disease: the point of no return?

Panza, F., Solfrizzi, V., Imbimbo, B. P., & Logroscino, G. (2014) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2014.935332 · Cited by 75 · see citing works

Tau Phosphorylation and Cleavage in Ethanol-Induced Neurodegeneration in the Developing Mouse Brain

Saito, M., Chakraborty, G., Mao, R.-F., Paik, S.-M., Vadász, C., & Saito, M. (2010) · Neurochemical Research · doi:10.1007/s11064-009-0116-4 · Cited by 72 · see citing works

Role of monoamine oxidase, nitric oxide synthase and regional brain monoamines in the antidepressant-like effects of methylene blue and selected structural analogues

Harvey, B. H., Duvenhage, I., Viljoen, F. P., Scheepers, N., Malan, S. F., Wegener, G., Brink, C. B., & Petzer, J. P. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.07.037 · Cited by 70 · see citing works

Molecular Implication of PP2A and Pin1 in the Alzheimer's Disease Specific Hyperphosphorylation of Tau

Landrieu, I., Smet‐Nocca, C., Amniai, L., Louis, J. V., Wieruszeski, J., Goris, J., Janssens, V., & Lippens, G. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021521 · Cited by 69 · see citing works

Immunochemical Properties of Ubiquitin Conjugates in the Paired Helical Filaments of Alzheimer Disease

Perry, G. L., Mulvihill, P., Fried, V. A., Smith, H. T., Grundke, I., & Iqbal, K. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb09203.x · Cited by 69 · see citing works

Oleuropein Aglycone: A Possible Drug against Degenerative Conditions. In Vivo Evidence of its Effectiveness against Alzheimer's Disease

Casamenti, F., Grossi, C., Rigacci, S., Pantano, D., Luccarini, I., & Stefani, M. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142850 · Cited by 68 · see citing works

Tau pathology in children and young adults: can you still be unconditionally baptist?

Duyckaerts, C. J. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0794-7 · Cited by 68 · see citing works

Microtubule-stabilizing agent prevents protein accumulation-induced loss of synaptic markers

Butler, D., Bendiske, J., Michaelis, M. L., Karanian, D. A., & Bahr, B. A. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.01.053 · Cited by 64 · see citing works

The interaction between methylene blue and the cholinergic system

Pfaffendorf, M., Bruning, T. A., Batink, H. D., & van Zwieten, P. A. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701355 · Cited by 62 · see citing works

Therapeutic and preventive effects of methylene blue on Alzheimer's disease pathology in a transgenic mouse model

Paban, V., Manrique, C., Filali, M., Maunoir-Regimbal, S., Fauvelle, F., & Alescio‐Lautier, B. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.06.033 · Cited by 58 · see citing works

Screening for Inhibitors of Tau Protein Aggregation into Alzheimer Paired Helical Filaments: A Ligand Based Approach Results in Successful Scaffold Hopping

Larbig, G., Pickhardt, M., Lloyd, D. G., & Schmidt, B. (2007) · Current Alzheimer Research · doi:10.2174/156720507781077250 · Cited by 58 · see citing works

Beneficial network effects of methylene blue in an amnestic model

Riha, P. D., Rojas, J. C., & Gonzalez-Lima, F. (2010) · NeuroImage · doi:10.1016/j.neuroimage.2010.11.023 · Cited by 58 · see citing works

NAP (Davunetide) Provides Functional and Structural Neuroprotection

Gozes, I. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211795589373 · Cited by 57 · see citing works

Structure−Activity Relationship of Cyanine Tau Aggregation Inhibitors

Chang, E. S., Congdon, E. E., Honson, N. S., Duff, K., & Kuret, J. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900116d · Cited by 56 · see citing works

Methylene Blue Improves Brain Mitochondrial ABAD Functions and Decreases Aβ in a Neuroinflammatory Alzheimer’s Disease Mouse Model

Zakaria, A., Hamdi, N., & Abdel-Kader, R. M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-014-9088-8 · Cited by 53 · see citing works

N-Phenylamine Derivatives as Aggregation Inhibitors in Cell Models of Tauopathy

Pickhardt, M., Biernat, J., Khlistunova, I., Wang, Y.-P., Gažová, Z., Mandelkow�, E., & Mandelkow�, E. (2007) · Current Alzheimer Research · doi:10.2174/156720507781788765 · Cited by 53 · see citing works

Different pathways of molecular pathophysiology underlie cognitive and motor tauopathy phenotypes in transgenic models for Alzheimer’s disease and frontotemporal lobar degeneration

Melis, V., Zabke, C., Stamer, K., Magbagbeolu, M., Schwab, K., Marschall, P., Veh, R. W., Bachmann, S., Deiana, S., Moreau, P., et al. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1804-z · Cited by 52 · see citing works

New insights into the role of glycogen synthase kinase-3 in Alzheimer's disease

Medina, M., & Ávila, J. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.843670 · Cited by 49 · see citing works

Methylene Blue Modulates β-Secretase, Reverses Cerebral Amyloidosis, and Improves Cognition in Transgenic Mice

Mori, T., Koyama, N., Segawa, T., Maeda, M., Maruyama, N., Kinoshita, N., Hou, H., Tan, J., & Town, T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.568212 · Cited by 49 · see citing works

Leucine Carboxyl Methyltransferase 1 (LCMT1)-dependent Methylation Regulates the Association of Protein Phosphatase 2A and Tau Protein with Plasma Membrane Microdomains in Neuroblastoma Cells

Sontag, J., Nunbhakdi‐Craig, V., & Sontag, E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490102 · Cited by 47 · see citing works

Azaphilones Inhibit Tau Aggregation and Dissolve Tau Aggregates in Vitro

Paranjape, S. R., Riley, A. P., Somoza, A. D., Oakley, C. E., Wang, C. C. C., Prisinzano, T. E., Oakley, B. R., & Gamblin, T. C. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00013 · Cited by 46 · see citing works

Glycogen synthase kinase-3β and the p25 activator of cyclin dependent kinase 5 increase pausing of mitochondria in neurons

Morel, M., Authelet, M., Dedecker, R., & Brion, J. P. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.02.077 · Cited by 46 · see citing works

Structural Determinants of Tau Aggregation Inhibitor Potency

Schafer, K. N., Cisek, K. K., Huseby, C. J., Chang, E. S., & Kuret, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.503474 · Cited by 45 · see citing works

Truncated tau at D421 is associated with neurodegeneration and tangle formation in the brain of Alzheimer transgenic models

Zhang, Q., Zhang, X., & Sun, A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0491-6 · Cited by 43 · see citing works

Binding of methylene blue to a surface cleft inhibits the oligomerization and fibrillization of prion protein

Cavaliere, P., Torrent, J., Prigent, S., Granata, V., Pauwels, K., Pastore, A., Rezaei, H., & Zagari, A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.09.005 · Cited by 43 · see citing works

The crystalline state of methylene blue: a zoo of hydrates

Rager, T., Geoffroy, A., Hilfiker, R., & Storey, J. M. D. (2012) · Physical Chemistry Chemical Physics · doi:10.1039/c2cp40128b · Cited by 42 · see citing works

Early investigational drugs targeting tau protein for the treatment of Alzheimer’s disease

Anand, K., & Sabbagh, M. N. (2015) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2015.1075002 · Cited by 41 · see citing works

Further understanding of tau phosphorylation: implications for therapy

Medina, M., & Avila, J. (2015) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.1000864 · Cited by 41 · see citing works

Methylene blue does not reverse existing neurofibrillary tangle pathology in the rTg4510 mouse model of tauopathy

Spires‐Jones, T. L., Friedman, T., Pitstick, R., Polydoro, M., Roe, A. D., Carlson, G. A., & Hyman, B. T. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.01.013 · Cited by 41 · see citing works

Novel Types of Frontotemporal Lobar Degeneration: Beyond Tau and TDP-43

Mackenzie, I. R., Neumann, M., Cairns, N. J., Muñoz, D. G., & Isaacs, A. M. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9551-1 · Cited by 40 · see citing works

Pharmacologic reductions of total tau levels; implications for the role of microtubule dynamics in regulating tau expression.

Dickey, C. A., Ash, P. E. A., Klosak, N., Lee, C. W., Petrucelli, L., Hutton, M. L., & Eckman, C. B. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-6 · Cited by 40 · see citing works

A brief history of tau: the evolving view of the microtubule-associated protein tau in neurodegenerative diseases

Lace, G., Wharton, S. B., & Ince, P. G. (2007) · Clinical Neuropathology · doi:10.5414/npp26043 · Cited by 37 · see citing works

Inhibition of Tau Aggregation by Three Aspergillus nidulans Secondary Metabolites: 2,ω-Dihydroxyemodin, Asperthecin, and Asperbenzaldehyde

Paranjape, S., Chiang, Y., Sanchez, J. F., Entwistle, R., Wang, C. C. C., Oakley, B. R., & Gamblin, T. C. (2014) · Planta Medica · doi:10.1055/s-0033-1360180 · Cited by 37 · see citing works

Methylene blue induces macroautophagy through 5′ adenosine monophosphate-activated protein kinase pathway to protect neurons from serum deprivation

Xie, L., Li, W., Winters, A., Yuan, F., Jin, K., & Yang, S. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00056 · Cited by 36 · see citing works

Methylene Blue Protects Astrocytes against Glucose Oxygen Deprivation by Improving Cellular Respiration

Choudhury, G. R., Winters, A., Rich, R. M., Ryou, M., Gryczynski, Z. K., Yuan, F., Yang, S., & Liu, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123096 · Cited by 34 · see citing works

Chaperone-like Antibodies Targeting Misfolded Tau Protein: New Vistas in the Immunotherapy of Neurodegenerative Foldopathies

Žilka, N., Kontseková, E., & Novák, M. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-15203 · Cited by 31 · see citing works

Effects of different anti‐tau antibodies on tau fibrillogenesis: RTA‐1 and RTA‐2 counteract tau aggregation

Taniguchi, T., Sumida, M., Hiraoka, S., Tomoo, K., Kakehi, T., Minoura, K., Sugiyama, S., Inaka, K., Ishida, T., Saito, N., et al. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.039 · Cited by 30 · see citing works

Determination of Methylene Blue and Leucomethylene Blue in Male and Female Fischer 344 Rat Urine and B6C3F1 Mouse Urine

Gaudette, N. F., & Lodge, J. W. (2005) · Journal of Analytical Toxicology · doi:10.1093/jat/29.1.28 · Cited by 30 · see citing works

Aminothienopyridazine inhibitors of tau aggregation: Evaluation of structure–activity relationship leads to selection of candidates with desirable in vivo properties

Ballatore, C., Crowe, A., Piscitelli, F., James, M., Lou, K., Rossidivito, G., Yao, Y., Trojanowski, J. Q., Lee, V. M. ‐., Brunden, K. R., et al. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.05.027 · Cited by 29 · see citing works

NAP Alpha-Aminoisobutyric Acid (IsoNAP)

Gozes, I., Schirer, Y., Idan-Feldman, A., David, M. P., & Furman-Assaf, S. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0103-8 · Cited by 28 · see citing works

Nontoxic singlet oxygen generator as a therapeutic candidate for treating tauopathies

Mohideen, S. S., Yamasaki, Y., Omata, Y., Tsuda, L., & Yoshiike, Y. (2015) · Scientific Reports · doi:10.1038/srep10821 · Cited by 26 · see citing works

Tau Immunotherapy and Imaging

Sigurdsson, E. M. (2013) · Neurodegenerative Diseases · doi:10.1159/000354491 · Cited by 23 · see citing works

Modulation and Detection of Tau Aggregation with Small-Molecule Ligands

Chang, E. S., Honson, N. S., Bandyopadhyay, B., Funk, K. E., Jensen, J. R., Kim, S., Naphade, S. B., & Kuret, J. (2009) · Current Alzheimer Research · doi:10.2174/156720509789207976 · Cited by 20 · see citing works

Chaperone-Like Antibodies in Neurodegenerative Tauopathies: Implication for Immunotherapy

Kontseková, E., Ivanovova, N. P., Handzusova, M., & Novák, M. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9355-9 · Cited by 19 · see citing works

Methylene blue supravital staining: an evaluation of its applicability to the mammalian brain and pineal gland.

Müller, T. (1998) · PubMed · doi:10.14670/hh-13.1019 · Cited by 18 · see citing works

Methylene Blue Inhibits the Function of α7-Nicotinic Acetylcholine Receptors

Mansouri, A. S. A., Lorke, D. E., Nurulain, S. M., Ashoor, A., Keun-Hang, S. Y., Petroianu, G. A., Isaev, D. S., & Öz, M. (2012) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152712803581010 · Cited by 15 · see citing works

Pharmacological evidence that methylene blue inhibits noradrenaline neuronal uptake in the rat vas deferens.

Chies, A. B., Custodio, R. C., Souza, G. L. D., Corrêa, F. M. D. A., & Pereira, O. C. M. (2003) · PubMed · Cited by 12 · see citing works

Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies

Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258 · see citing works

Current and future therapeutic strategies for Alzheimer’s disease: an overview of drug development bottlenecks

Peng, Y., Jin, H., Xue, Y.-H., Chen, Q., Yao, S., Du, M., & Liu, S. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1206572 · Cited by 176 · see citing works

Development of disease-modifying drugs for frontotemporal dementia spectrum disorders

Panza, F., Lozupone, M., Seripa, D., Daniele, A., Watling, M., Giannelli, G., & Imbimbo, B. P. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0330-x · Cited by 122 · see citing works

Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau

Rayaprolu, S., Higginbotham, L., Bagchi, P., Watson, C. M., Zhang, T., Levey, A. I., Rangaraju, S., & Seyfried, N. T. (2021) · Neuropsychopharmacology · doi:10.1038/s41386-020-00840-3 · Cited by 118 · see citing works

Diabetes as a risk factor for Alzheimer’s disease in the Middle East and its shared pathological mediators

Jayaraj, R. L., Azimullah, S., & Beiram, R. (2019) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2019.12.028 · Cited by 105 · see citing works

How Can Insulin Resistance Cause Alzheimer’s Disease?

Yoon, J. H., Hwang, J., Son, S. U., Choi, J., You, S.-W., Park, H., Cha, S.-Y., & Maeng, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043506 · Cited by 104 · see citing works

Molecular properties of methylene blue, a common probe in sorption and degradation studies: a review

Bollinger, J., Lima, E. C., Mouni, L., Salvestrini, S., & Tran, H. N. (2025) · Environmental Chemistry Letters · doi:10.1007/s10311-025-01856-1 · Cited by 100 · see citing works

Developments with multi-target drugs for Alzheimer’s disease: An overview of the current discovery approaches

González, J. F., Alcántara, A. R., Doadrio, A. L., & Sánchez-Montero, J. M. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1623201 · Cited by 98 · see citing works

New Features about Tau Function and Dysfunction

Medina, M., Hernández, F., & Ávila, J. (2016) · Biomolecules · doi:10.3390/biom6020021 · Cited by 92 · see citing works

Two decades of new drug discovery and development for Alzheimer's disease

Liu, Z., Zhang, A., Sun, H. J., Han, Y., Kong, L. D., & Wang, X. (2017) · RSC Advances · doi:10.1039/c6ra26737h · Cited by 83 · see citing works

Anti-amyloid-β protein agents for the treatment of Alzheimer’s disease: an update on emerging drugs

Lozupone, M., Solfrizzi, V., D’Urso, F., Di Gioia, I., Sardone, R., Dibello, V., Stallone, R., Liguori, A., Ciritella, C., Daniele, A., et al. (2020) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2020.1808621 · Cited by 77 · see citing works

Emerging drugs to reduce abnormal β-amyloid protein in Alzheimer’s disease patients

Panza, F., Seripa, D., Solfrizzi, V., Imbimbo, B. P., Lozupone, M., Leo, A., Sardone, R., Gagliardi, G., Lofano, L., Creanza, B. C., et al. (2016) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2016.1241232 · Cited by 59 · see citing works

Self-assembly hollow manganese Prussian white nanocapsules attenuate Tau-related neuropathology and cognitive decline

Cai, X., Zhang, K., Xie, X., Zhu, X., Feng, J., Jin, Z., Zhang, H., Tian, M., & Chen, H. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119678 · Cited by 59 · see citing works

From dual binding site acetylcholinesterase inhibitors to allosteric modulators: A new avenue for disease-modifying drugs in Alzheimer's disease

Chierrito, T. P. C., Mantoani, S. P., Roca, C., Requena-Triguero, C., Sebastián-Pérez, V., Ordoñez, W. O. C., Moreira, N. C. D. S., Pérez, C., Sakamoto‐Hojo, E. T., Takahashi, C. S., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.08.051 · Cited by 54 · see citing works

Tau Related Pathways as a Connecting Link between Epilepsy and Alzheimer’s Disease

Paudel, Y. N., Angelopoulou, E., Jones, N. C., O'Brien, T. J., Kwan, P., Piperi, C., Othman, I., & Shaikh, M. F. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00460 · Cited by 42 · see citing works

The potential of solanezumab and gantenerumab to prevent Alzheimer’s disease in people with inherited mutations that cause its early onset

Panza, F., Seripa, D., Lozupone, M., Solfrizzi, V., Imbimbo, B. P., Barulli, M. R., Tortelli, R., Capozzo, R., Bisceglia, P., Dimitri, A., et al. (2018) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2018.1389885 · Cited by 41 · see citing works

Targeting β-Amyloid Plaques and Oligomers: Development of Near-Ir Fluorescence Imaging Probes

Liu, H., Yang, J., Wang, L., Xu, Y., Zhang, S., Lv, J., Ran, C., & Li, Y. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0185 · Cited by 32 · see citing works

Pharmacological Management of Psychiatric Symptoms in Frontotemporal Dementia: A Systematic Review

Buoli, M., Serati, M., Caldiroli, A., Galimberti, D., Scarpini, E. A., & Altamura, A. C. (2017) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988717700506 · Cited by 27 · see citing works

Promising therapies for the treatment of frontotemporal dementia clinical phenotypes: from symptomatic to disease-modifying drugs

Logroscino, G., Imbimbo, B. P., Lozupone, M., Sardone, R., Capozzo, R., Battista, P., Zecca, C., Dibello, V., Giannelli, G., Bellomo, A., et al. (2019) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2019.1598377 · Cited by 28 · see citing works

The Structure Biology of Tau and Clue for Aggregation Inhibitor Design

Wang, D., Huang, X., Yan, L., Zhou, L., Chang, Y., Wu, J., Su, Z., & Huang, Y. (2021) · The Protein Journal · doi:10.1007/s10930-021-10017-6 · Cited by 26 · see citing works

Glutamate Metabolism in Mitochondria is Closely Related to Alzheimer’s Disease

Song, J., Yang, X., Zhang, M., Wang, C., & Chen, L. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210595 · Cited by 27 · see citing works

Molecular Role of Protein Phosphatases in Alzheimer’s and Other Neurodegenerative Diseases

Hassan, M., Yasir, M., Shahzadi, S., Chun, W., & Kloczkowski, A. (2024) · Biomedicines · doi:10.3390/biomedicines12051097 · Cited by 28 · see citing works

Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C., & Yang, Y. (2022) · Chinese Medicine · doi:10.1186/s13020-022-00698-1 · Cited by 27 · see citing works

The epigenetics of frailty.

Lozupone, M., Solfrizzi, V., Sardone, R., Dibello, V., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Daniele, A., & Panza, F. (2023) · Epigenomics · doi:10.2217/epi-2023-0279 · Cited by 17 · see citing works

Methylene blue activates the PMCA activity and cross-interacts with amyloid β-peptide, blocking Aβ-mediated PMCA inhibition

Berrocal, M., Corbacho‐Cuello, I., Gutiérrez‐Merino, C., & Mata, A. M. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.07.012 · Cited by 20 · see citing works

Disease-modifying therapies for tauopathies: agents in the pipeline

Panza, F., Imbimbo, B. P., Lozupone, M., Greco, A., Seripa, D., Logroscino, G., Daniele, A., & Colosimo, C. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1606715 · Cited by 19 · see citing works

Tau proteins and senescent Cells: Targeting aging pathways in Alzheimer’s disease

Singh, M., Ali, H., Jyothi, S. R., Kaur, I., Kumar, S., Sharma, N., Prasad, G. V. S., Pramanik, A., Almalki, W. H., & Imran, M. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149165 · Cited by 18 · see citing works

The development of peptide- and oligonucleotide-based drugs to prevent the formation of abnormal tau in tauopathies

Lozupone, M., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Stallone, R., Altamura, M., Bellomo, A., et al. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2200245 · Cited by 19 · see citing works

Structural Proteomic Profiling of Cerebrospinal Fluids to Reveal Novel Conformational Biomarkers for Alzheimer’s Disease

Wang, B., Zhong, X., Fields, L. G., Lu, H., Zhu, Z., & Li, L. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00332 · Cited by 15 · see citing works

Alzheimer's disease approaches - Focusing on pathology, biomarkers and clinical trial candidates

Hroudová, J., & Fišar, Z. (2024) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2024.111069 · Cited by 13 · see citing works

Alzheimer's Disease and Vascular Dementia, Connecting and Differentiating Features

Hurła, M., Banaszek, N., Kozubski, W. P., & Dorszewska, J. (2024) · Current Alzheimer Research · doi:10.2174/0115672050319219240711103459 · Cited by 9 · see citing works

Implications of Successful Symptomatic Treatment in Parkinson’s Disease for Therapeutic Strategies of Alzheimer’s Disease

Zhao, L., Cheng, X., & Zhong, C. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00450 · Cited by 9 · see citing works

Methylene Blue Exerts Anticonvulsant and Neuroprotective Effects on Self-Sustaining Status Epilepticus (SSSE) Induced by Prolonged Basolateral Amygdala Stimulation in Wistar Rats

Cui, Z., Li, W., Luo, Y., Yang, J., Qu, Z., & Zhao, W. (2018) · Medical Science Monitor · doi:10.12659/msm.907758 · Cited by 6 · see citing works

Targeted Drug Delivery: Amyloid Beta Targeting Drugs, Immunotherapy, Anti-Tau and Aggregation Inhibitor, Microtubule-Stabilizing, and Neuroinflammation Modulation

Chintamaneni, P. K., Pindiprolu, S. K. S. S., Krishnamurthy, P. T., & Varshini, M. S. (2024) · Springer eBooks · doi:10.1007/978-981-96-0259-9_12 · Cited by 3 · see citing works

Green Nanotechnology for High-performance Impurity Detection and Water Treatment

Li, B., Wang, N., Zheng, J., Zhu, H., Wang, S., Ye, E., & Li, Z. (2022) · Royal Society of Chemistry eBooks · doi:10.1039/9781839165771-00033 · Cited by 2 · see citing works

Neuroprotektive Therapien bei Tauopathien

Respondek, G., Krey, L., Huber, M. K., Pflugrad, H., Wegner, F., & Höglinger, G. U. (2021) · Der Nervenarzt · doi:10.1007/s00115-021-01210-0 · Cited by 2 · see citing works

Tau-Centric Therapies for Treating Alzheimer’s Disease

Quraishe, S., Cowan, C. M., & Mudher, A. K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00005-3 · Cited by 1 · see citing works

Tauopathies and its therapeutic interventions in Alzheimer’s disease

Sonawane, S. K., Rangappa, N., Chidambaram, H., & Chinnathambi, S. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2025.12.001 · Cited by 1 · see citing works

Anti-Tau-Therapien – was können wir erwarten?

Fließbach, K., McCormick, C., Kaulen, B., & Schneider, A. (2019) · Der Nervenarzt · doi:10.1007/s00115-019-0758-7 · Cited by 1 · see citing works

α5-GABA-A Receptor Positive Allosteric Modulation prevents neuronal atrophy and cognitive decline independently of p-Tau accumulation in the PS19 mouse modelPreprint

Dharavath, R. N., Bernardo, A. M., Marceau-Linhares, C., Marcotte, M. D., Mezo‐González, C. E., Wong, K. D., Pina‐Leblanc, C., Bouchet, A., Sharmin, D., Pandey, K. P., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.07.611810 · Cited by 1 · see citing works

Advanced Drug Discovery for Alzheimer’s Disease: Challenges and Strategies

Haque, R., & Nazir, A. (2017) · Springer eBooks · doi:10.1007/978-981-10-5187-6_2

Immunotherapy for the Treatment of Alzheimer’s Disease

Farooqui, A. A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809937-7.00009-4

Additional file 3 of Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C. Y., & Yang, Y. X. (2023) · Figshare · doi:10.6084/m9.figshare.22600132

Additional file 5 of Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C. Y., & Yang, Y. X. (2023) · Figshare · doi:10.6084/m9.figshare.22600138

Additional file 6 of Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C. Y., & Yang, Y. X. (2023) · Figshare · doi:10.6084/m9.figshare.22600141

Additional file 7 of Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C. Y., & Yang, Y. X. (2023) · Figshare · doi:10.6084/m9.figshare.22600144

Additional file 2 of Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C. Y., & Yang, Y. X. (2023) · Figshare · doi:10.6084/m9.figshare.22600129

Additional file 4 of Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C. Y., & Yang, Y. X. (2023) · Figshare · doi:10.6084/m9.figshare.22600135

Additional file 1 of Integrating network pharmacology, UPLC-Q–TOF–MS and molecular docking to investigate the effect and mechanism of Chuanxiong Renshen decoction against Alzheimer's disease

Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C. Y., & Yang, Y. X. (2023) · Figshare · doi:10.6084/m9.figshare.22600126

The neuro-immune axis of Tau pathology in Alzheimer’s disease

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