Rat tau proteome consists of six tau isoforms: implication for animal models of human tauopathies

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works

Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii

Voth, D. E., & Heinzen, R. A. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00901.x · Cited by 11,773 · 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

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 · see citing works

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492 · 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

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 · see citing works

The distribution of tau in the mammalian central nervous system.

Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588 · see citing works

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · 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

Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17

Hong, M. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,003 · see citing works

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

Alonso, A. D. C., Zaidi, T., Novák, M., Grundke, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 968 · 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

Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.

Brandt, R., Léger, J. G., & Lee, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.5.1327 · Cited by 624 · see citing works

Developmentally regulated expression of specific tau sequences

Kosik, K. S., Orecchio, L. D., Bakalis, S., & Neve, R. L. (1989) · Neuron · doi:10.1016/0896-6273(89)90077-9 · Cited by 598 · 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

Tau Consists of a Set of Proteins with Repeated C-Terminal Microtubule-Binding Domains and Variable N-Terminal Domains

Himmler, A., Drechsel, D. N., Kirschner, M. W., & Martin, D. W. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1381-1388.1989 · Cited by 535 · see citing works

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 · see citing works

Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau

Goode, B., & Feinstein, S. (1994) · The Journal of cell biology · doi:10.1083/jcb.124.5.769 · Cited by 399 · 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

Tau proteins: the molecular structure and mode of binding on microtubules.

Hirokawa, N., Shiomura, Y., & Okabe, S. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.4.1449 · Cited by 389 · see citing works

Tau protein as a differential biomarker of tauopathies

Sergeant, N., Delacourte, A., & Buée, L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.020 · Cited by 312 · see citing works

Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease

Panda, D., Samuel, J. C., Massie, M., Feinstein, S. C., & Wilson, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633508100 · Cited by 280 · see citing works

Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo

Žilka, N., Filipčík, P., Koson, P., Fialová, Ľ., Škrabana, R., Žilková, M., Rolkova, G., Kontseková, E., & Novák, M. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.029 · Cited by 254 · see citing works

Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease

Mandelkow, E., Von Bergen, M., Biernat, J., & Mandelkow, E. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00053.x · Cited by 243 · see citing works

Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51.

Novak, M., Jakes, R., Edwards, P. C., Milstein, C., & Wischik, C. (1991) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.88.13.5837 · Cited by 217 · see citing works

Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation

Dayanandan, R., van Slegtenhorst, M., Mack, T. G. A., Ko, L., Yen, S. H., Leroy, K., Brion, J., Anderton, B. H., Hutton, M. L., & Lovestone, S. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00222-7 · Cited by 210 · see citing works

Selective Phosphorylation of Adult Tau Isoforms in Mature Hippocampal Neurons Exposed to Fibrillar Aβ

Ferreira, A., Lu, Q., Orecchio, L., & Kosik, K. S. (1997) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1997.0615 · Cited by 178 · see citing works

A Decade of Tau Transgenic Animal Models and Beyond

Götz, J., Deters, N. A., Doldissen, A., Bokhari, L., Ke, Y. D., Wiesner, A., Schönrock, N., & Ittner, L. M. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00051.x · Cited by 174 · see citing works

Tau and transgenic animal models

Götz, J. (2001) · Brain Research Reviews · doi:10.1016/s0165-0173(01)00055-8 · Cited by 161 · see citing works

Interaction of Tau Isoforms with Alzheimer's Disease Abnormally Hyperphosphorylated Tau and in VitroPhosphorylation into the Disease-like Protein

Alonso, A. D. C., Zaidi, T., Novák, M., Barra, H. S., Grundke, I., & Iqbal, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105365200 · Cited by 160 · see citing works

Isoforms changes of tau protein during development in various species

Takuma, H., Arawaka, S., & Mori, H. (2003) · Developmental Brain Research · doi:10.1016/s0165-3806(03)00056-7 · Cited by 157 · see citing works

Tau Phosphorylation at Serine 396 and Serine 404 by Human Recombinant Tau Protein Kinase II Inhibits Tau's Ability to Promote Microtubule Assembly

EVANS, D. B., Rank, K. B., Bhattacharya, K., Thomsen, D. R., Gurney, M. E., & Sharma, S. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000808200 · Cited by 155 · see citing works

Alzheimer paired helical filaments Restoration of the biological activity by dephosphorylation

Iqbal, K., Zaidi, T., Bancher, C., & Grundke, I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00650-4 · Cited by 150 · see citing works

Inhibitory Role for Dual Specificity Phosphatase VHR in T Cell Antigen Receptor and CD28-induced Erk and Jnk Activation

Alonso, A., Saxena, M., Williams, S., & Mustelin, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006497200 · Cited by 149 · see citing works

The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases.

Mawal-Dewan, M., Henley, J., VOORDE, A. V. D., Trojanowski, J. Q., & Lee, V. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47378-4 · Cited by 140 · see citing works

Discoveries of Tau, abnormally hyperphosphorylated tau and others of neurofibrillary degeneration: A personal historical perspective

Iqbal, K., & Grundke, I. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s325 · Cited by 110 · see citing works

Light and electron microscope localization of the microtubule- associated tau protein in rat brain

Migheli, A., Butler, M., Brown, K., & Shelanski, M. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-06-01846.1988 · Cited by 109 · see citing works

Dynamic Regulation of Expression and Phosphorylation of Tau by Fibroblast Growth Factor-2 In Neural Progenitor Cells from Adult Rat Hippocampus

Tatebayashi, Y., Iqbal, K., & Grundke, I. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-13-05245.1999 · Cited by 106 · see citing works

Phylogenetic diversity of the expression of the microtubule-associated protein tau: implications for neurodegenerative disorders

Janke, C., Beck, M., Stahl, T., Holzer, M., Brauer, K., Bigl, V., & Arendt, T. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00079-0 · Cited by 104 · see citing works

An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif

Doll, T., Meichsner, M., Riederer, B. M., Honegger, P., & Matus, A. I. (1993) · Journal of Cell Science · doi:10.1242/jcs.106.2.633 · Cited by 90 · see citing works

Truncated tau protein as a new marker for Alzheimer's disease.

Novák, M. (1994) · PubMed · Cited by 87 · see citing works

Genetic isolation of a region of chromosome 8 that exerts major effects on blood pressure and cardiac mass in the spontaneously hypertensive rat.

Křen, V., Pravenec, M., Lu, S., Krenová, D., Wang, J. M., Wang, N., Merriouns, T., Wong, A. M., Lezin, E. S., Lau, D., et al. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119198 · Cited by 87 · see citing works

Developmental changes of tau protein and mRNA in cultured rat brain oligodendrocytes

Gorath, M., Stahnke, T., Mronga, T., Goldbaum, O., & Richter‐Landsberg, C. (2001) · Glia · doi:10.1002/glia.1098 · Cited by 81 · see citing works

Tau‐4R suppresses proliferation and promotes neuronal differentiation in the hippocampus of tau knockin/ knockout mice

Sennvik, K., Boekhoorn, K., Lasrado, R., Terwel, D., Verhaeghe, S., Korr, H., Schmitz, C., Tomiyama, T., Mori, H., Krugers, H. J., et al. (2007) · The FASEB Journal · doi:10.1096/fj.06-7735com · Cited by 70 · see citing works

Postmortem changes in the phosphorylation state of tau-protein in the rat brain

Gärtner, U., Janke, C., Holzer, M., Vanmechelen, E., & Arendt, T. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00094-3 · Cited by 66 · see citing works

Postmortem changes in the levels and localization of microtubule‐associated proteins (tau, MAP2 and MAP1B) in the rat and human hippocampus

Schwab, C., Bondada, V., Sparks, D. L., Cahan, L. D., & Geddes, J. W. (1994) · Hippocampus · doi:10.1002/hipo.450040212 · Cited by 61 · see citing works

Microtubule‐associated protein tau is required for axonal neurite elaboration by neuroblastoma cells

Shea, T. B., Beermann, M. L., Nixon, R. A., & Fischer, I. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490320308 · Cited by 59 · see citing works

Organization of actin and microtubules during process formation in tau‐expressing sf9 cells

Knowles, R. B., Leclerc, N. M., & Kosik, K. S. (1994) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970280308 · Cited by 35 · 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

Tau mRNA isoforms following sciatic nerve axotomy with and without regeneration

Chambers, C. B., & Muma, N. A. (1997) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00089-2 · Cited by 28 · see citing works

The effect of amphetamine analogs on cleaved microtubule-associated protein-tau formation in the rat brain

Straiko, M. M. W., Coolen, L. M., Zemlan, F. P., & Gudelsky, G. A. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.08.073 · Cited by 27 · see citing works

MAP2d mRNA is expressed in identified neuronal populations in the developing and adult rat brain and its subcellular distribution differs from that of MAP2b in hippocampal neurones

Ferhat, L., Represa, A., Ferhat, W., Ben‐Ari, Y., & Khrestchatisky, M. (1998) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1998.00044.x · Cited by 20 · see citing works

Amyloid-β Injection in Rat Amygdala Alters Tau Protein but Not mRNA Expression

Chambers, C. B., Sigurdsson, E. M., Hejna, M. J., Lorens, S. A., Lee, J. M., & Muma, N. A. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7325 · Cited by 19 · see citing works

Rodent models in neuroscience research: is it a rat race?

Ellenbroek, B., & Youn, J. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.026120 · Cited by 627 · see citing works

A Transgenic Alzheimer Rat with Plaques, Tau Pathology, Behavioral Impairment, Oligomeric Aβ, and Frank Neuronal Loss

Cohen, R. M., Rezai-Zadeh, K. P., Weitz, T. M., Rentsendorj, A., Gate, D., Spivak, I. E., Bholat, Y., Vasilevko, V., Glabe, C. G., Breunig, J. J., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3672-12.2013 · Cited by 522 · see citing works

Effect of rapamycin on aging and age-related diseases—past and future

Selvarani, R., Mohammed, S., & Richardson, A. G. (2020) · GeroScience · doi:10.1007/s11357-020-00274-1 · Cited by 312 · 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

Atypical, non-standard functions of the microtubule associated Tau protein

Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 207 · see citing works

Modeling Alzheimer’s disease in transgenic rats

Carmo, S. D., & Cuello, A. C. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-37 · Cited by 203 · see citing works

Regulation of human MAPT gene expression

Caillet‐Boudin, M., Buée, L., Sergeant, N., & Lefebvre, B. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0025-8 · Cited by 193 · see citing works

Tau Protein and Its Role in Blood–Brain Barrier Dysfunction

Michalicová, A., Majerová, P., & Kováč, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.570045 · Cited by 179 · see citing works

Anxiety and Alzheimer’s disease: Behavioral analysis and neural basis in rodent models of Alzheimer’s-related neuropathology

Pentkowski, N. S., Rogge-Obando, K., Donaldson, T. N., Bouquin, S. J., & Clark, B. J. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.05.005 · Cited by 169 · see citing works

Overview of Transgenic Mouse Models for Alzheimer's Disease

Myers, A., & McGonigle, P. (2019) · Current Protocols in Neuroscience · doi:10.1002/cpns.81 · Cited by 140 · see citing works

An App knock-in rat model for Alzheimer’s disease exhibiting Aβ and tau pathologies, neuronal death and cognitive impairments

Pang, K., Jiang, R., Zhang, W., Yang, Z., Li, L., Shimozawa, M., Tambaro, S., Mayer, J., Zhang, B., Li, M., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00582-x · Cited by 142 · see citing works

Blood biomarkers for mild traumatic brain injury: a selective review of unresolved issues

Hier, D. B., Obafemi-Ajayi, T., Thimgan, M. S., Olbricht, G. R., Azizi, S., Allen, B., Hadi, B., & Wunsch, D. C. (2021) · Biomarker Research · doi:10.1186/s40364-021-00325-5 · Cited by 130 · see citing works

Alzheimer's Disease Mechanisms and Emerging Roads to Novel Therapeutics

Sala Frigerio, C., & De Strooper, B. (2016) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-070815-014015 · Cited by 116 · 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 & Therapy · doi:10.1186/alzrt277 · Cited by 112 · see citing works

Three Repeat Isoforms of Tau Inhibit Assembly of Four Repeat Tau Filaments

Adams, S. J., Deture, M. A., McBride, M., Dickson, D. W., & Petrucelli, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010810 · Cited by 104 · see citing works

Brain and blood biomarkers of tauopathy and neuronal injury in humans and rats with neurobehavioral syndromes following blast exposure

Dickstein, D., Gasperi, R. D., Sosa, M. G., Pérez-García, G., Short, J., Sosa, H., Perez, G. M., Tschiffely, A. E., Dams-O'Connor, K., Pullman, M., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0674-z · Cited by 86 · see citing works

Short and Long Term Behavioral and Pathological Changes in a Novel Rodent Model of Repetitive Mild Traumatic Brain Injury

McAteer, K. M., Corrigan, F., Thornton, E., Turner, R. J., & Vink, R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160220 · Cited by 97 · see citing works

Tau-mediated synaptic damage in Alzheimer’s disease

Jadhav, S., Cubinkova, V., Zimova, I., Brezováková, V., Maďari, A., Cigánková, V., & Žilka, N. (2015) · Translational Neuroscience · doi:10.1515/tnsci-2015-0023 · Cited by 92 · see citing works

Repetitive head trauma, chronic traumatic encephalopathy and tau: Challenges in translating from mice to men

Ojo, J. O., Mouzon, B., & Crawford, F. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.06.003 · Cited by 88 · see citing works

Hyperphosphorylated tau (p-tau) and drug discovery in the context of Alzheimer's disease and related tauopathies

Moore, K. B. E., Hung, T.-J., & Fortin, J. S. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103487 · Cited by 86 · see citing works

First transgenic rat model developing progressive cortical neurofibrillary tangles

Filipčík, P., Žilka, N., Bugos, O., Kučerák, J., Koson, P., Novák, P., & Novák, M. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.10.015 · Cited by 84 · see citing works

Does neuroinflammation drive the relationship between tau hyperphosphorylation and dementia development following traumatic brain injury?

Collins-Praino, L. E., & Corrigan, F. (2017) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2016.09.027 · Cited by 95 · see citing works

Modeling the β-secretase cleavage site and humanizing amyloid-beta precursor protein in rat and mouse to study Alzheimer’s disease

Serneels, L., T’Syen, D., Pérez‐Benito, L., Theys, T., Holt, M. G., & Strooper, B. D. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00399-z · Cited by 78 · see citing works

Current directions in tau research: Highlights from Tau 2020

Sexton, C. E., Snyder, H. M., Beher, D., Boxer, A. L., Brannelly, P., Brion, J., Buée, L., Cacace, A. M., Chételat, G., Citron, M., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12452 · Cited by 78 · see citing works

A Review of the Current Mammalian Models of Alzheimer’s Disease and Challenges That Need to Be Overcome

Mckean, N. E., Handley, R. R., & Snell, R. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313168 · Cited by 76 · see citing works

Truncation and Activation of Dual Specificity Tyrosine Phosphorylation-regulated Kinase 1A by Calpain I

Jin, N., Yin, X., Gu, J., Zhang, X., Shi, J., Qian, W., Ji, Y., Cao, M., Gu, X., Ding, F., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645507 · Cited by 71 · see citing works

Chronic traumatic encephalopathy-integration of canonical traumatic brain injury secondary injury mechanisms with tau pathology

Kulbe, J. R., & Hall, E. D. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.08.003 · Cited by 69 · see citing works

Expression of Tau Pathology-Related Proteins in Different Brain Regions: A Molecular Basis of Tau Pathogenesis

Hu, W. H., Wu, F., Zhang, Y., Gong, C., Iqbal, K., & Liu, F. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00311 · Cited by 61 · see citing works

Stereological estimation of neuron number and plaque load in the hippocampal region of a transgenic rat model of A lzheimer's disease

Heggland, I., Storkaas, I. S., Soligard, H., Kobro‐Flatmoen, A., & Witter, M. P. (2015) · European Journal of Neuroscience · doi:10.1111/ejn.12876 · Cited by 51 · see citing works

Bring Back the Rat!

Carter, C. S., Richardson, A., Huffman, D. M., & Austad, S. (2020) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glz298 · Cited by 51 · see citing works

Heterocellular spheroids of the neurovascular blood-brain barrier as a platform for personalized nanoneuromedicine

Kumarasamy, M., & Sosnik, A. (2021) · iScience · doi:10.1016/j.isci.2021.102183 · Cited by 51 · see citing works

Opposite changes in APP processing and human Aβ levels in rats carrying either a protective or a pathogenic APP mutation

Tambini, M. D., Norris, K. A., & D'adamio, L. (2020) · eLife · doi:10.7554/elife.52612 · Cited by 47 · see citing works

Transition of Tau Protein from Disordered to Misordered in Alzheimer’s Disease

Kovačech, B., Škrabana, R., & Novák, M. (2010) · Neurodegenerative Diseases · doi:10.1159/000283478 · Cited by 51 · see citing works

Age-dependent increases in tau phosphorylation in the brains of type 2 diabetic rats correlate with a reduced expression of p62

Jung, H.-J., Kim, Y.-J., Eggert, S., Chung, K. C., Choi, K. S., & Park, S. A. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.07.013 · Cited by 47 · see citing works

Misfolded tau protein and disease modifying pathways in transgenic rodent models of human tauopathies

Žilka, N., Korenova, M., & Novák, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0499-y · Cited by 45 · see citing works

Lentiviral Delivery of the Human Wild-type Tau Protein Mediates a Slow and Progressive Neurodegenerative Tau Pathology in the Rat Brain

Caillierez, R., Bégard, S., Lécolle, K., Deramecourt, V., Zommer, N., Dujardin, S., Loyens, A., Dufour, N., Aurégan, G., Winderickx, J., et al. (2013) · Molecular Therapy · doi:10.1038/mt.2013.66 · Cited by 43 · see citing works

Truncated tau deregulates synaptic markers in rat model for human tauopathy

Jadhav, S., Katina, S., Kováč, A., Kazmerova, Z., Novák, M., & Žilka, N. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00024 · Cited by 39 · see citing works

Anti-amyloid-beta to tau-based immunization: developments in immunotherapy for Alzheimer's disease

Lambracht‐Washington, D., & Rosenberg, R. N. (2013) · ImmunoTargets and Therapy · doi:10.2147/itt.s31428 · Cited by 38 · see citing works

Cellular and molecular mechanisms of pathological tau phosphorylation in traumatic brain injury: implications for chronic traumatic encephalopathy

Donison, N. S., Palik, J., Volkening, K., & Strong, M. J. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00842-z · Cited by 39 · see citing works

Early lysosome defects precede neurodegeneration with amyloid-β and tau aggregation in NHE6-null rat brain

Lee, Y., Miller, M. R., Fernandez, M. A., Berg, E. L., Prada, A. M., Ouyang, Q., Schmidt, M., Silverman, J. L., Young‐Pearse, T. L., & Morrow, E. M. (2021) · Brain · doi:10.1093/brain/awab467 · Cited by 35 · see citing works

Early Long-Term Memory Impairment and Changes in the Expression of Synaptic Plasticity-Associated Genes, in the McGill-R-Thy1-APP Rat Model of Alzheimer's-Like Brain Amyloidosis

Habif, M., Carmo, S. D., Báez, M. V., Colettis, N. C., Cercato, M. C., Salas, D. A., Acutain, M. F., Sister, C. L., Berkowicz, V. L., Canal, M. P., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.585873 · Cited by 31 · see citing works

The TgF344-AD rat: behavioral and proteomic changes associated with aging and protein expression in a transgenic rat model of Alzheimer's disease

Bac, B., Hicheri, C., Weiss, C., Buell, A., Vilcek, N., Späni, C. B., Geula, C., Savas, J. N., & Disterhoft, J. F. (2022) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2022.12.015 · Cited by 31 · see citing works

Gene Therapy Models of Alzheimer’s Disease and Other Dementias

Combs, B., Kneynsberg, A., & Kanaan, N. M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3271-9_25 · Cited by 31 · see citing works

A lab-on-a-chip platform for studying the subcellular functional proteome of neuronal axons

Wu, H.-I., Cheng, G.-H., Wong, Y.-Y., Lin, C.-M., Fang, W., Chow, W., & Chang, Y. (2009) · Lab on a Chip · doi:10.1039/b918217a · Cited by 30 · see citing works

The effects of mild closed head injuries on tauopathy and cognitive deficits in rodents: Primary results in wild type and rTg4510 mice, and a systematic review

Bachstetter, A. D., Morganti, J. M., Bodnar, C. N., Webster, S. J., Higgins, E. K., Roberts, K. N., Snider, H., Meier, S. E., Nation, G. K., Goulding, D. S., et al. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113180 · Cited by 29 · see citing works

Protein aggregate formation in oligodendrocytes: tau and the cytoskeleton at the intersection of neuroprotection and neurodegeneration

Richter‐Landsberg, C. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0157 · Cited by 27 · see citing works

Cellular Biology of Tau Diversity and Pathogenic Conformers

Kang, S., Eskandari‐Sedighi, G., Hromádková, L., Safar, J., & Westaway, D. A. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590199 · Cited by 27 · see citing works

Blood‐based biomarkers and traumatic brain injury—A clinical perspective

Posti, J. P., & Tenovuo, O. S. (2022) · Acta Neurologica Scandinavica · doi:10.1111/ane.13620 · Cited by 27 · see citing works

Hippocampal place cell dysfunction and the effects of muscarinic M1 receptor agonism in a rat model of Alzheimer's disease

Galloway, C. R., Ravipati, K., Singh, S., Lebois, E. P., Cohen, R. M., Levey, A. I., & Manns, J. R. (2018) · Hippocampus · doi:10.1002/hipo.22961 · Cited by 25 · see citing works

First-in-Rat Study of Human Alzheimer’s Disease Tau Propagation

Smolek, T., Jadhav, S., Brezováková, V., Cubinkova, V., Valachova, B., Novák, P., & Žilka, N. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1102-0 · Cited by 25 · see citing works

Animal Models of Alzheimer’s Disease

Newman, M., Kretzschmar, D., Khan, I., Chen, M., Verdile, G., & Lardelli, M. T. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809468-6.00040-1 · Cited by 24 · see citing works

Increased expression of three-repeat isoforms of tau contributes to tau pathology in a rat model of chronic type 2 diabetes

Jung, H. J., Park, S. S., Mok, J. O., Lee, T. K., Park, C. S., & Park, S. A. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.01.012 · Cited by 24 · see citing works

Inflammasome links traumatic brain injury, chronic traumatic encephalopathy, and Alzheimer’s disease

Seplovich, G., Bouchi, Y., Vaccari, J. P. D. R., Pareja, J. C. M., Reisner, A., Blackwell, L. S., Mechref, Y. S., Wang, K., Tyndall, J. A., Tharakan, B., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00107 · Cited by 20 · see citing works

Exploring the parity paradox: Differential effects on neuroplasticity and inflammation by APOEe4 genotype at middle age

Lee, B. H., Cevizci, M., Lieblich, S. E., Ibrahim, M., Wen, Y., Eid, R. S., Lamers, Y., Duarte‐Guterman, P., & Galea, L. A. M. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.05.019 · Cited by 19 · see citing works

Sleep/Wake Behavior and EEG Signatures of the TgF344-AD Rat Model at the Prodromal Stage

Kreuzer, M., Keating, G. L., Fenzl, T., Härtner, L., Sinon, C. G., Hajjar, I. M., Ciavatta, V. T., Rye, D. B., & García, P. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239290 · Cited by 17 · see citing works

Improving Mouse Models for Dementia. Are All the Effects in Tau Mouse Models Due to Overexpression?Preprint

Joel, Z., Izquierdo, P., Salih, D. A. M., Richardson, J. C., Cummings, D. M., & Edwards, F. A. (2018) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2018.83.037531 · Cited by 18 · see citing works

A familial Danish dementia rat shows impaired presynaptic and postsynaptic glutamatergic transmission

Yin, T., Yao, W., Norris, K. A., & D’Adamio, L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101089 · Cited by 14 · see citing works

Dose-dependent phosphorylation of endogenous Tau by intermittent hypoxia in rat brain

Marciante, A. B., Howard, J. C., Kelly, M. N., Santiago‐Moreno, J., Allen, L. L., Gonzalez‐Rothi, E. J., & Mitchell, G. S. (2022) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00332.2022 · Cited by 15 · see citing works

Tau as a fluid biomarker of concussion and neurodegeneration

Hossain, I., Blennow, K., Posti, J. P., & Zetterberg, H. (2022) · Concussion · doi:10.2217/cnc-2022-0004 · Cited by 16 · see citing works

Rodent Models for Alzheimer’s Disease in Drug Discovery

Barrett, J. E., & McGonigle, P. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802810-0.00012-x · Cited by 15 · see citing works

The three sisters of fate: Genetics, pathophysiology and outcomes of animal models of neurodegenerative diseases

Klonarakis, M., Vos, M. D., Woo, E. K., Ralph, L. T., Thacker, J. S., & Gil‐Mohapel, J. (2022) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104541 · Cited by 13 · see citing works

Humanized Tau Mice with Regionalized Amyloid Exhibit Behavioral Deficits but No Pathological Interaction

Yetman, M. J., Fowler, S., & Jankowsky, J. L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153724 · Cited by 13 · see citing works

Progressive Dysregulation of Tau Phosphorylation in an Animal Model of Temporal Lobe Epilepsy

Concepcion, F. A., Ekstrom, N. A., Khan, M. N., Estes, O., & Poolos, N. P. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.04.020 · Cited by 12 · see citing works

Potential Natural Products for Alzheimer’s Disease: Targeted Search Using the Internal Ribosome Entry Site of Tau and Amyloid-β Precursor Protein

Tasi, Y.-C., Chin, T., Chen, Y., Huang, C.-C., Lee, S.-L., & Wu, T. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16048789 · Cited by 12 · see citing works

Neuronal loss and inflammation preceding fibrillary tau pathology in a rat model with early human-like tauopathy

Emmerson, J. T., Malcolm, J. C., Carmo, S. D., Nguyen, P., Breuillaud, L., Martínez-Trujillo, J., & Cuello, A. C. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106317 · Cited by 11 · see citing works

Rat models of major neurodegenerative disorders

Novati, A., Singer, E., Yu-Taeger, L., Clemensson, E. K. H., & Nguyen, H. P. (2022) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2022.19 · Cited by 11 · see citing works

A novel rat model of Alzheimer’s disease based on lentiviral-mediated expression of mutant APP

Parsi, S., Pandamooz, S., Keshel, S. H., Naji, M., Morfini, G. A., Ahmadiani, A., & Dargahi, L. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.09.045 · Cited by 11 · see citing works

Analysis of early effects of human APOE isoforms on Alzheimer’s disease and type III hyperlipoproteinemia pathways using knock-in rat models with humanized APP and APOE

Yesiltepe, M., Yin, T., Tambini, M., Bao, H., Pan, M., d’Abramo, C., Giliberto, L., Han, X., & D’Adamio, L. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01832-2 · Cited by 10 · see citing works

Progressive human-like tauopathy with downstream neurodegeneration and neurovascular compromise in a transgenic rat model

Emmerson, J. T., Carmo, S. D., Liu, Y., Shalhoub, A., Ai, L., Bonomo, Q., Malcolm, J. C., Breuillaud, L., & Cuello, A. C. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106227 · Cited by 11 · see citing works

Rats Display Sexual Dimorphism in Phosphorylation of Brain Tau with Age

Niu, J., Iqbal, K., Liu, F., & Hu, W. H. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210341 · Cited by 9 · see citing works

Why Therapeutic Trials Fail in Primary Tauopathies

Olfati, N., Ghodsi, H., Bayram, E., & Litvan, I. (2023) · Movement Disorders · doi:10.1002/mds.29322 · Cited by 8 · see citing works

Tau isoform-specific enhancement of L-type calcium current and augmentation of afterhyperpolarization in rat hippocampal neurons

Stan, G. F., Church, T. W., Randall, E., Harvey, J. R. M., Brown, J. T., Wilkinson, K. A., Hanley, J. G., & Marrion, N. V. (2022) · Scientific Reports · doi:10.1038/s41598-022-18648-0 · Cited by 8 · see citing works

Polymeric alkylpyridinium salts permit intracellular delivery of human Tau in rat hippocampal neurons: requirement of Tau phosphorylation for functional deficits

Koss, D. J., Robinson, L., Mietelska‐Porowska, A., Gąsiorowska, A., Sepčić, K., Turk, T., Jaspars, M., Niewiadomska, G., Scott, R. H., Platt, B., et al. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1949-4 · Cited by 8 · see citing works

Anterograde and Retrograde Propagation of Inoculated Human Tau Fibrils and Tau Oligomers in a Non-Transgenic Rat Tauopathy Model

Horvat, L. L., Španić, E., Leko, M. B., Zubčić, K., Horvat, L., Mustapić, M., Hof, P. R., & Šimić, G. (2023) · Biomedicines · doi:10.3390/biomedicines11041004 · Cited by 7 · see citing works

Evaluation of Alpha-Synuclein and Tau Antiaggregation Activity of Urea and Thiourea-Based Small Molecules for Neurodegenerative Disease Therapeutics

Ganegamage, S. K., Ademoye, T. A., Patel, H., Alnakhala, H., Tripathi, A., Nguyen, C. C. D., Pham, K., Plascencia‐Villa, G., Zhu, X., Perry, G. L., et al. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00282 · Cited by 7 · see citing works

Microtubule‐associated protein tau promotes neuronal class II β‐tubulin microtubule formation and axon elongation in embryonic X enopus laevis

Liu, Y., Wang, C., Destin, G., & Szaro, B. G. (2015) · European Journal of Neuroscience · doi:10.1111/ejn.12848 · Cited by 7 · see citing works

A freeze-and-thaw-induced fragment of the microtubule-associated protein tau in rat brain extracts: implications for the biochemical assessment of neurotoxicity

Vasconcelos, I. C., de Campos, R. M., Schwaemmle, H., Masson, A. P., Ferrari, G. D., Alberici, L. C., Faça, V. M., Garcia‐Cairasco, N., & Sebollela, A. S. (2021) · Bioscience Reports · doi:10.1042/bsr20203980 · Cited by 7 · see citing works

Transfixed by transgenics: how pathology assumptions are slowing progress in Alzheimer's disease and related dementia research

D'adamio, L. (2023) · EMBO Molecular Medicine · doi:10.15252/emmm.202318479 · Cited by 6 · see citing works

Initial assessment of the spatial learning, reversal, and sequencing task capabilities of knock-in rats with humanizing mutations in the Aβ-coding region of App

Pham, H., Yin, T., & D’Adamio, L. (2022) · PLOS ONE · doi:10.1371/journal.pone.0263546 · Cited by 6 · see citing works

Exercise Improves Alzheimer’s Disease Phenotype in the TgF344-AD Rat, a Behavioral Time Course Study of Males and Females

Hall, S. E., White, Z. J., Rohn, T. T., Sudasinghe, K., & Young, M. E. (2025) · Brain Sciences · doi:10.3390/brainsci15060631 · Cited by 6 · see citing works

Intercellular signaling and synaptic deconstruction uncovered by single-cell and spatial transcriptomics in an AD tauopathy model

Ji, J. X., Giles, B. L., Bhattacharjee, S., Kautzmann, M.-A. I., Masson, A. P., Carmo, S. D., Cuello, A. C., & Bazan, N. G. (2025) · Communications Biology · doi:10.1038/s42003-025-08959-z · Cited by 6 · see citing works

A comparative study on pathological features of transgenic rat lines expressing either three or four repeat misfolded tau

Valachova, B., Brezováková, V., Bugos, O., Jadhav, S., Smolek, T., Novák, P., & Žilka, N. (2018) · The Journal of Comparative Neurology · doi:10.1002/cne.24447 · Cited by 6 · see citing works

Paradoxical attenuation of early amyloid-induced cognitive impairment and synaptic plasticity in an aged APP/Tau bigenic rat model

Emmerson, J. T., Carmo, S. D., Lavagna, A., Huang, C., Wong, T. P., Martínez-Trujillo, J., & Cuello, A. C. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01901-0 · Cited by 5 · see citing works

Repeated non-hemorrhagic and non-contusional mild traumatic brain injury in rats elicits behavioral impairment with microglial activation, astrogliosis, and tauopathy: Reproducible and quantitative model of chronic traumatic encephalopathy

Sugahara, C., Kin, K., Sasaki, T., Sasada, S., Kawauchi, S., Yabuno, S., Nagase, T., Hirayama, T., Masai, K., Hosomoto, K., et al. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149412 · Cited by 4 · see citing works

Advancements in diagnosing Post-concussion Syndrome: insights into epidemiology, pathophysiology, neuropathology, neuroimaging, and salivary biomarkers

Mavroudis, I. A., Petridis, F., Ciobica, A. S., Kamal, F. Z., Pădurariu, M., & Kazis, D. A. (2025) · Acta Neurologica Belgica · doi:10.1007/s13760-024-02695-7 · Cited by 3 · see citing works

Diverse Efficacy of Dimethyl Fumarate in Alleviating the Late Streptozotocin-Induced Cognitive Impairment and Neuropathological Features in Rat

Majkutewicz, I., Kurowska, E., Ruciński, J., Myślińska, D., Grembecka, B., Mantej, J., & Dzik, K. P. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04024-8 · Cited by 3 · see citing works

Adeno-Associated Viral Gene Delivery of Wild-Type Human Tau Induces Progressive Hyperphosphorylation and Neuronal Cell Death in the Hippocampi of Middle-Aged Rats

Gorzek, R. C., Joly‐Amado, A., Hurst-Calle, N., Gabrielson, G. L., Miller, M., Osting, S., Nash, K. R., & Bürger, C. (2025) · Cells · doi:10.3390/cells14161238 · Cited by 2 · see citing works

White matter degeneration precedes tau aggregation in rats with Alzheimer's-like tauopathy

Ai, L., Carmo, S. D., Antel, J. P., Kuhlmann, T., & Cuello, A. C. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107149 · Cited by 2 · see citing works

Isoflurane Exposure Influence on Sleep Architecture in a Rat Model of Alzheimer’s Disease

Kreuzer, M., Keating, G. L., Sinon, C. G., Fenzl, T., Schneider, G. H., Rye, D. B., & García, P. S. (2025) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000007717 · Cited by 1 · see citing works

Research progress on biomarkers of traumatic brain injury

Shen, X., Cheng, S., Chen, S., Wang, M., Li, T., Xu, W., Zhang, Y., Yuan, P., & Shi, L. (2026) · Animal Models and Experimental Medicine · doi:10.1002/ame2.70173 · Cited by 1 · see citing works

Perspective Chapter: Challenges in the Diagnosis of Post-Concussion Syndrome – Epidemiology, Pathophysiology, Neuropathology, Neuroimaging Biomarkers, and Salivary Biomarkers

Mavroudis, I. A., Petridis, F., Ciobica, A. S., Kamal, F. Z., & Pădurariu, M. (2024) · IntechOpen eBooks · doi:10.5772/intechopen.1007685 · Cited by 2 · see citing works

A freeze-and-thaw induced-fragment of the microtubule-associated protein Tau in rat brain extracts: implications for the biochemical assessment of neurotoxicityPreprint

Vasconcelos, I. C., de Campos, R. M., Schwaemmle, H. K., Masson, A. P., Ferrari, G. D., Alberici, L. C., Faça, V. M., Garcia-Cairasco, N., & Sebollela, A. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/404129 · Cited by 1 · see citing works

Keystone Symposium 2010 Highlights

Fagan, T. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101340

Past, Present, and Future: The Behavioral Sciences.

Darley, J. G. (1971) · Contemporary Psychology · doi:10.1037/014015

Potential Animal Models of Alzheimer Disease and Their Importance in Investigating the Pathogenesis of Alzheimer Disease

Farooqui, A. A. (2016) · Springer eBooks · doi:10.1007/978-3-319-15889-1_2

Optimization and Utilization of Hybrid Culture Between Rat and Fly Primary Neurons: A Novel Model for Studying Neurodegenerative Diseases

Kraus, K. L. (2016) · OhioLink ETD Center (Ohio Library and Information Network)

Characterization of Microvascular and Neuronal Injury in a Transgenic Rat Model of Alzheimer's Disease

Joo, I. L. (2017)

Familial Danish dementia young Knock-in rats expressing humanized APP and human Aβ show impaired pre and postsynaptic glutamatergic transmissionPreprint

Yin, T., Yao, W., Norris, K. A., & D'adamio, L. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.24.449787

The Neuropathology of Concussion

Mavroudis, I. A., Balmuș, I.-M., Gorgan, L., & Ciobica, A. S. (2023) · IntechOpen eBooks · doi:10.5772/intechopen.112459

Brain map of aging-induced alterations in membrane ganglioside patternPreprint

Jha, D., Dovrtělová, G., Telenský, P., Olkowicz, S., Coufalíková, K., Opálka, L., Kubíček, K., Černá, B., Hajek, R., Bělašková, S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.30.555520

Tau isoform regulation is region‐ and cell‐specific in mouse brain

McMillan, P., Korvatska, E., Poorkaj, P., Evstafjeva, Z., Robinson, L., Greenup, L., Leverenz, J., Schellenberg, G. D., & D'Souza, I. (2008) · Journal of Comparative Neurology · doi:10.1002/cne.21867 · Cited by 179 · see citing works

Distinct phenotypes of three-repeat and four-repeat human tau in a transgenic model of tauopathy

Sealey, M. A., Vourkou, E., Cowan, C. M., Bossing, T., Quraishe, S., Grammenoudi, S., Skoulakis, E. M. C., & Mudher, A. K. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.05.003 · Cited by 73 · see citing works

Differential Effects of Human Tau Isoforms to Neuronal Dysfunction and Toxicity in the Drosophila CNS

Vourkou, E., Paspaliaris, V., Bourouliti, A., Zerva, M.-C., Prifti, E., Papanikolopoulou, K., & Skoulakis, E. M. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112985 · Cited by 12 · see citing works

Transmission of tauopathy strains is independent of their isoform composition

He, Z., McBride, J. D., Xu, H. W., Changolkar, L. N., Kim, S., Zhang, B., Narasimhan, S., Gibbons, G. S., Guo, J., Kozak, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13787-x · Cited by 177 · see citing works

Isoforms changes of tau protein during development in various species

Takuma, H., Arawaka, S., & Mori, H. (2003) · Developmental Brain Research · doi:10.1016/s0165-3806(03)00056-7 · Cited by 157 · see citing works