The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Tau Filament Formation in Transgenic Mice Expressing P301L Tau
Open accessAbstract
Mutations in the microtubule-associated protein tau, including P301L, are genetically coupled to hereditary frontotemporal dementia with parkinsonism linked to chromosome 17. To determine whether P301L is associated with fibril formation in mice, we expressed the longest human tau isoform, human tau40, with this mutation in transgenic mice by using the neuron-specific mouse Thy1.2 promoter. We obtained mice with high expression of human P301L tau in cortical and hippocampal neurons. Accumulated tau was hyperphosphorylated and translocated from axonal to somatodendritic compartments and was accompanied by astrocytosis and neuronal apoptosis indicated by terminal deoxynucleotidyl transferase-mediated biotinylated dUTP nick end-labeling staining. Moreover, P301L tau formed abnormal filaments. Electron microscopy of sarcosyl-insoluble protein extracts established that the filaments had a straight or twisted structure of variable length and were approximately 15 nm wide. Immunoelcecton microscopy showed that the tau filaments were phosphorylated at the TG3, AT100, AT8, and AD199 epitopes in vivo. In cortex, brain stem, and spinal cord, neurofibrillary tangles were also identified by thioflavin-S fluorescent microscopy and Gallyas silver stains. Together, our results show that expression of the P301L mutation in mice causes neuronal lesions that are similar to those seen in human tauopathies.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“transgenic mice expressing human mutated tau showed NFT formation and neuronal loss, implying a causal relationship between tau over-expression and neurodegeneration (8 -11).”
From CREB-activity and nmnat2 transcription are down-regulated prior to neurodegeneration, while NMNAT2 over-expression is neuroprotective, in a mouse model of human tauopathy (2012) · cites this paper as [8]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Genetic studies show that the development of neurodegenerative tauopathies is associated with missense mutations in the microtubule-associated tau protein (MAPT) [26].”
From Diffusion tensor imaging reveals whole-brain microstructural changes in the P301L mouse model of tauopathy. (2020) · cites this paper as [26]
In the citing paper
“Both mouse models are known to demonstrate a proinflammatory phenotype (17, 18).”
From The Transcriptional Landscape of Microglial Genes in Aging and Neurodegenerative Disease (2019) · cites this paper as [17]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Lewis, J., McGowan, E., Rockwood, J., Melrose, H., Nacharaju, P., Van Slegtenhorst, M., Gwinn-Hardy, K., Murphy, M. P., Baker, M., Yu, X., et al. (2000) · Nature Genetics · doi:10.1038/78078 · Cited by 1,371
Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122
Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929
The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease.
Delacourte, A., David, J. P., Sergeant, N., Buée, L., Wattez, A., Vermersch, P., Ghozali, F., Fallet-Bianco, C., Pasquier, F., Lebert, F., et al. (1999) · Neurology · doi:10.1212/wnl.52.6.1158 · Cited by 828
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 609
Ishihara, T., Hong, M., Zhang, B., Nakagawa, Y., Lee, M. K., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)81127-7 · Cited by 564
Götz, J., Probst, A., Spillantini, M. G., Schäfer, T., Jakes, R., Bürki, K., & Goedert, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07116.x · Cited by 441
Self-citationSpittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M. H., Sciot, R., Lommel, A. V., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 390
Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
Probst, A., Götz, J., Wiederhold, K., Tolnay, M., Mistl, C., Jaton, A., Hong, M., Ishihara, T., Lee, V., Trojanowski, J., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010051148 · Cited by 362
Self-citation
Research works printed but not linked: 1
- Gallyas, 1971, Acta Morphol. Acad. Sci. Hung., 19, 1
Cited by
Sorted by citations
Items 201–300 of 497
Tau clearance improves astrocytic function and brain glutamate-glutamine cycle
Hebron, M. L., Javidnia, M., & Moussa, C. (2018) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2018.06.005 · Cited by 50
Alzheimer's disease: Old problem, new views from transgenic and viral models
Jaworski, T., Dewachter, I., Seymour, C. M., Borghgraef, P., Devijver, H., Kügler, S., & LEUVEN, F. V. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.03.005 · Cited by 49
Tauopathy contributes to synaptic and cognitive deficits in a murine model for Alzheimer’s disease
Stancu, I., Ris, L., Vasconcelos, B., Marinangeli, C., Goeminne, L., Laporte, V., Haylani, L. E., Couturier, J., Schakman, O., Gailly, P., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-246702 · Cited by 48
ER‐mitochondria contacts and cholesterol metabolism are disrupted by disease‐associated tau protein
Szabo, L., Cummins, N., Paganetti, P., Odermatt, A., Papassotiropoulos, A., Karch, C. M. M., Götz, J., Eckert, A., & Grimm, A. (2023) · EMBO Reports · doi:10.15252/embr.202357499 · Cited by 46
Self-citationSchaeffer, V., Patte‐Mensah, C., Eckert, A., & Mensah‐Nyagan, A. G. (2006) · Journal of Neurobiology · doi:10.1002/neu.20267 · Cited by 48
Ogunsuyi, O. B., Oboh, G., Oluokun, O. O., Ademiluyi, A. O., & Ogunruku, O. O. (2019) · Oriental Pharmacy and Experimental Medicine · doi:10.1007/s13596-019-00393-x · Cited by 48
Brief update on different roles of tau in neurodegeneration
Ittner, A., Ke, Y. D., van Eersel, J., Gladbach, A., Götz, J., & Ittner, L. M. (2011) · IUBMB Life · doi:10.1002/iub.467 · Cited by 49
Self-citationUmeda, T., Yamashita, T., Kimura, T., Ohnishi, K., Takuma, H., Ozeki, T., Takashima, A., Tomiyama, T., & Mori, H. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.03.015 · Cited by 46
Ahlemeyer, B., Halupczok, S., Rodenberg-Frank, E., Valerius, K.-P., & Baumgart‐Vogt, E. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170923 · Cited by 49
Mouse models of Alzheimer's disease: The long and filamentous road
Phinney, A. L., Horne, P., Yang, J., Janus, C., Bergeron, C., & Westaway, D. A. (2003) · Neurological Research · doi:10.1179/016164103101202020 · Cited by 47
Maurage, C.-A., Sergeant, N., Ruchoux, M.-M., Hauw, J.-J., & Delacourte, A. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0608-7 · Cited by 51
Köhler, C. N., Dinekov, M., & Götz, J. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.010 · Cited by 45
Self-citationŽilka, N., Korenova, M., & Novák, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0499-y · Cited by 47
Functional Genomics meets neurodegenerative disorders
Hoerndli, F. J., David, D. C., & Götz, J. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.07.002 · Cited by 44
Self-citationNew developments in frontotemporal dementia and parkinsonism linked to chromosome 17
Rosso, S. M., & Swieten, J. C. V. (2002) · Current Opinion in Neurology · doi:10.1097/00019052-200208000-00004 · Cited by 43
Sahara, N., & Yanai, R. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1149761 · Cited by 46
Vagenknecht, P., Luzgin, A., Ono, M., Ji, B., Higuchi, M., Noaín, D., Maschio, C., Sobek, J., Chen, Z., Konietzko, U., et al. (2022) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-022-05708-w · Cited by 39
Self-citationBrainstem Alzheimer's-like pathology in the triple transgenic mouse model of Alzheimer's disease
Overk, C., Kelley, C. M., & Mufson, E. J. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.06.004 · Cited by 42
Ubhi, K. K., Rockenstein, E. M., Doppler, E., Mante, M., Adame, A., Patrick, C., Trejo, M., Crews, L. A., Paulino, A., Moessler, H., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0505-4 · Cited by 45
Compartmentalized tau hyperphosphorylation and increased levels of kinases in transgenic mice
G??tz, J., & Nitsch, R. M. (2001) · Neuroreport · doi:10.1097/00001756-200107030-00045 · Cited by 42
Self-citationPérez, P. D., Hall, G., Kimura, T., Ren, Y., Bailey, R. M., Lewis, J. M., Febo, M., & Sahara, N. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-9 · Cited by 41
Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention
Kishinevsky, A. C. S., & Lou, J. K. I. W. (2013) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.s10-007 · Cited by 42
Seed-competent tau monomer initiates pathology in a tauopathy mouse model
Mirbaha, H., Chen, D., Mullapudi, V., Terpack, S. J., White, C. L., Joachimiak, Ł. A., & Diamond, M. I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102163 · Cited by 39
Mańczak, M., & Reddy, P. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.008 · Cited by 41
Accelerated aging exacerbates a pre‐existing pathology in a tau transgenic mouse model
Bodea, L., Evans, H. T., der Jeugd, A. V., Ittner, L. M., Delerue, F., Kril, J. J., Halliday, G. M., Hodges, J. R., Kiernan, M. C., & Götz, J. (2017) · Aging Cell · doi:10.1111/acel.12565 · Cited by 41
Self-citationFunctional Genomics meets neurodegenerative disorders
David, D. C., Hoerndli, F. J., & Götz, J. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.07.001 · Cited by 39
Self-citationAn update on the toxicity of Aβ in Alzheimer’s disease
Götz, J. (2008) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s3016 · Cited by 40
Self-citationSubstrate-specific reduction of PP2A activity exaggerates tau pathology
Deters, N., Ittner, L. M., & Götz, J. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.140 · Cited by 39
Self-citationImmunotherapeutic approaches for Alzheimer’s disease in transgenic mouse models
Wısnıewskı, T., & Boutajangout, A. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0236-2 · Cited by 39
Thaker, U., McDonagh, A. M., Iwatsubo, T., Lendon, C. L., Pickering-Brown, S. M., & Mann, D. M. A. (2003) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2003.00425.x · Cited by 39
Altered phosphorylation of cytoskeletal proteins in mutant protein phosphatase 2A transgenic mice
Schild, A., Ittner, L. M., & Götz, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.066 · Cited by 38
Self-citationKnockout of p75 neurotrophin receptor attenuates the hyperphosphorylation of Tau in pR5 mouse model
Manucat-Tan, N. B., Shen, L.-L., Bobrovskaya, L., Al‐Hawwas, M., Zhou, F. H., Wang, Y., & Zhou, X. (2019) · Aging · doi:10.18632/aging.102202 · Cited by 36
Animal Models for Alzheimer’s Disease and Frontotemporal Dementia: A Perspective
Götz, J., & Götz, N. N. (2009) · ASN NEURO · doi:10.1042/an20090042 · Cited by 38
Self-citationAlzheimer's Disease Selective Vulnerability and Modeling in Transgenic Mice
Götz, J., Schönrock, N., Vissel, B., & Ittner, L. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1143 · Cited by 38
Self-citationSilva, N. M. L. E., Gonçalves, R. A., Boehnke, S. E., Forny‐Germano, L., Munoz, D. P., & Felice, F. G. D. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.03.016 · Cited by 37
Yamoah, A., Tripathi, P., Sechi, A. S., Köhler, C. N., Guo, H., Chandrasekar, A., Nolte, K. W., Wruck, C. J., Katona, I., Anink, J. J., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-190722 · Cited by 35
Is Tau Aggregation Toxic or Protective: A Sensible Question in the Absence of Sensitive Methods?
Götz, J., Ittner, L. M., Fändrich, M., & Schönrock, N. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14410 · Cited by 37
Self-citationCell-Cycle Markers in a Transgenic Mouse Model of Human Tauopathy
Delobel, P., Lavenir, I., Ghetti, B. F., Holzer, M., & Goedert, M. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.050540 · Cited by 39
Hong, X.-Y., Wan, H., Li, T., Zhang, B., Li, X., Wang, X., Li, X., Liu, Q. R., Chen, C., Yang, Y., et al. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00290-9 · Cited by 36
Aquaporin 4 is differentially increased and dislocated in association with tau and amyloid-beta
Kecheliev, V., Boss, L., Maheshwari, U., Konietzko, U., Keller, A., Razansky, D., Nitsch, R. M., Klohs, J., & Ni, R. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121593 · Cited by 36
Self-citationMitochondrial dysfunction induced by disease relevant AβPP and tau protein mutations
Keil, U., Hauptmann, S., Bonert, A., Scherping, I., Eckert, A., & Müller, W. E. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9206 · Cited by 36
Biochemical Isolation of Insoluble Tau in Transgenic Mouse Models of Tauopathies
Julien, C., Bretteville, A., & Planel, E. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-551-0_32 · Cited by 37
Frontotemporal dementia and tauopathy
Yoshiyama, Y., Lee, V. M. ‐., & Trojanowski, J. Q. (2001) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-001-0100-0 · Cited by 36
Three Postulates to Help Identify the Cause of Alzheimer's Disease
de la Torre, J. C. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101884 · Cited by 39
Glöckner, F., Meske, V., Lütjohann, D., & Ohm, T. G. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318212f185 · Cited by 35
Brain cholinesterases: III. Future perspectives of AD research and clinical practice
Shen, Z. X. (2004) · Medical Hypotheses · doi:10.1016/j.mehy.2004.03.001 · Cited by 35
Etxeberria, A., Shen, Y.-A. A., Vito, S., Silverman, S. M., Imperio, J., Lalehzadeh, G., Soung, A. L., Du, C., Xie, L., Choy, M. K., et al. (2024) · The Journal of Neuroscience · doi:10.1523/jneurosci.2347-23.2024 · Cited by 34
Distinct tau filament folds in human MAPT mutants P301L and P301T
Schweighauser, M., Shi, Y., Murzin, A. G., Garringer, H. J., Vidal, R., Murrell, J. R., Erro, M. E., Seelaar, H., Ferrer, I., Swieten, J. C. V., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01575-9 · Cited by 34
Kulic, L., Wollmer, M. A., Rhein, V. F., Pagani, L., Kuehnle, K., Cattepoel, S., Tracy, J., Eckert, A., & Nitsch, R. M. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.10.014 · Cited by 34
Self-citationAdeno‐associated virus‐based Alzheimer's disease mouse models and potential new therapeutic avenues
Ittner, L. M., Klugmann, M., & Ke, Y. D. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14637 · Cited by 36
Viney, T. J., Sárkány, B., Ozdemir, A. T., Hartwich, K., Schweimer, J. V., Bannerman, D. M., & Somogyi, P. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111646 · Cited by 37
Lambourne, S. L., Humby, T., Isles, A. R., Emson, P. C., Spillantini, M. G., & Wilkinson, L. S. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm119 · Cited by 34
Lo, A. C., Iscru, E., Blum, D. L., Tesseur, I. C., Callaerts‐Vegh, Z., Buée, L., Strooper, B. D., Balschun, D., & D’Hooge, R. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122296 · Cited by 39
Tau protein aggregation: Key features to improve drug discovery screening
Giovannini, J., Smeralda, W., Jouanne, M., Santos, J. S. O., Catto, M., & Voisin‐Chiret, A. S. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.01.009 · Cited by 33
Altered expression of brain acetylcholinesterase in FTDP-17 human tau transgenic mice
Silveyra, M. X., García‐Ayllón, M., de Barreda, E. G., Small, D. H., Martı́nez, S., Ávila, J., & Sáez‐Valero, J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.03.006 · Cited by 32
Cultured cell and transgenic mouse models for tau pathology linked to β-amyloid
Bloom, G. S., Ren, K., & Glabe, C. G. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.008 · Cited by 32
Fukushima, T., Nakamura, A., Iwakami, N., Nakada, Y., Hattori, H., Hoki, S., Yamaguchi, H., Nakagawa, M., Terashima, N., & Narita, H. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.03.091 · Cited by 31
Shin, S., Kim, D., Song, J. Y., Jeong, H., Hyeon, S. J., Kowall, N. W., Ryu, H., Pae, A. N., Lim, S., & Kim, Y. K. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101782 · Cited by 29
What Can Rodent Models Tell Us About Cognitive Decline in Alzheimer's Disease?
Davis, S., & Laroche, S. (2003) · Molecular Neurobiology · doi:10.1385/mn:27:3:249 · Cited by 32
Animal Models of Neurological Disease
Shah, A., Garzón-Muvdi, T., Mahajan, R. K., Duenas, V. J., & Quiñones-Hinojosa, A. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-5819-8_3 · Cited by 31
Modeling Alzheimer's disease and other proteopathies in vivo: Is seeding the key?
Walker, L. C., Bian, F., Callahan, M. J., Lipinski, W. J., Durham, R. A., & LeVine, H. (2002) · Amino Acids · doi:10.1007/s00726-001-0113-7 · Cited by 31
Tau Pathology Induces Intraneuronal Cholesterol Accumulation
Glöckner, F., & Ohm, T. G. (2014) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000103 · Cited by 30
Pazopanib Reduces Phosphorylated Tau Levels and Alters Astrocytes in a Mouse Model of Tauopathy
Javidnia, M., Hebron, M. L., Xin, Y., Kinney, N. G., & Moussa, C. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170429 · Cited by 30
Biochemistry and Molecular Biology of Copper in Mammals
Linder, M. C. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-288-3_1 · Cited by 29
Massalimova, A., Ni, R., Nitsch, R. M., Reisert, M., von Elverfeldt, D., & Klohs, J. (2020) · Neurodegenerative Diseases · doi:10.1159/000515754 · Cited by 28
Self-citationMartin, S. P., & Leeman-Markowski, B. A. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2023.1287545 · Cited by 30
Of mice and men: more neurobiology in dementia
Codita, A., Winblad, B. G., & Mohammed, A. H. (2006) · Current Opinion in Psychiatry · doi:10.1097/01.yco.0000245757.06374.6a · Cited by 29
Li, B., Ryder, J. W., Yuan, S., Moore, S. A., Jr., Liu, F., Solenberg, P. J., Brune, K. A., Fox, N. W., Ni, B., Liu, R., et al. (2004) · Transgenic Research · doi:10.1023/b:trag.0000040039.44899.6f · Cited by 28
Gene expression profiling of the tau mutant (P301L) transgenic mouse brain
Ho, L., Xiang, Z., Mukherjee, P., Zhang, W., Jesus, N. D., Mirjany, M., Yemul, S., & Pasinetti, G. M. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02044-4 · Cited by 28
A Rapid Gene Delivery-Based Mouse Model for Early-Stage Alzheimer Disease-Type Tauopathy
Siman, R., Lin, Y., Malthankar‐Phatak, G. H., & Dong, Y. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000006 · Cited by 27
Przybyla, M., van Eersel, J., van Hummel, A., van der Hoven, J., Sabale, M., Harasta, A. E., Müller, J., Gajwani, M., Prikas, E., Mueller, T., et al. (2020) · Brain · doi:10.1093/brain/awaa133 · Cited by 29
Ni, R., Chen, Z., Gerez, J., Shi, G., Zhou, Q., Riek, R., Nilsson, K. P. R., Razansky, D., & Klohs, J. (2020) · Biomedical Optics Express · doi:10.1364/boe.395803 · Cited by 22
Yeast growth selection system for the identification of cell-active inhibitors of β-secretase
Middendorp, O., Ortler, C., Neumann, U., Paganetti, P., Lüthi, U., & Barberis, A. (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.05.004 · Cited by 27
A role of P301L tau mutant in anti-apoptotic gene expression, cell cycle and apoptosis
Zhao, Z. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(03)00175-1 · Cited by 27
Xiong, J., Deng, I. B., Kelliny, S., Lin, L., Bobrovskaya, L., & Zhou, X. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-022-01029-x · Cited by 28
Ren, Q., Gong, W.-G., Zhou, H., Shu, H., Wang, Y., & Zhang, Z. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-00698-w · Cited by 26
In Vivo Analysis of Wild‐type and FTDP‐17 Tau Transgenic Mice
Götz, J., Barmettler, R., Ferrari, A., Goedert, M., Probst, A., & Nitsch, R. M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06914.x · Cited by 26
Self-citationAlzheimer's disease and frontotemporal dementia: prospects of a tailored therapy?
Götz, J., Ittner, L. M., & Schönrock, N. (2006) · The Medical Journal of Australia · doi:10.5694/j.1326-5377.2006.tb00615.x · Cited by 26
Self-citationMack, T. G. A., Dayanandan, R., van Slegtenhorst, M., Whone, A. L., Hutton, M. L., Lovestone, S., & Anderton, B. H. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00434-1 · Cited by 26
Ubiquitin-negative mini-pick-like bodies in the dentate gyrus in p301l tauopathy
Ferrer, I., Hernández, I., Puig, B., Rey, M. J., Ezquerra, M., TOLOSA, E. S., & Boada, M. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2003-5604 · Cited by 25
Wang, Y., Gong, W.-G., Ren, Q., & Zhang, Z. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200401 · Cited by 26
Senescence in aging and disorders of the central nervous system
Swenson, B. L., Meyer, C. F., Bussian, T. J., & Baker, D. J. (2019) · Translational Medicine of Aging · doi:10.1016/j.tma.2019.01.002 · Cited by 24
SWI and phase imaging reveal intracranial calcifications in the P301L mouse model of human tauopathy
Ni, R., Zarb, Y., Kuhn, G. A., Müller, R., Yundung, Y., Nitsch, R. M., Kulic, L., Keller, A., & Klohs, J. (2020) · Magnetic Resonance Materials in Physics, Biology and Medicine · doi:10.1007/s10334-020-00855-3 · Cited by 24
Self-citationDakson, A., Yokota, O., Esiri, M. M., Bigio, E. H., Horan, M. A., Pendleton, N., Richardson, A. M. T., Neary, D., Snowden, J. S., Robinson, A., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0798-y · Cited by 22
Seibenhener, M. L., Zhao, T., Du, Y., Calderilla-Barbosa, L., Yan, J., Jiang, J., Wooten, M. W., & Wooten, M. C. (2013) · Behavioural Brain Research · doi:10.1016/j.bbr.2013.04.006 · Cited by 22
Eskandari-Sedighi, G., Daude, N., Gapeshina, H., Sanders, D. W., Kamali-Jamil, R., Yang, J., Shi, B., Wille, H., Ghetti, B., Diamond, M. I., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0215-7 · Cited by 22
Cranston, A., Wysocka, A., Steczkowska, M., Zadrożny, M., Pałasz, E., Harrington, C. R., Theuring, F., Wischik, C. M., Riedel, G., & Niewiadomska, G. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa033 · Cited by 22
Experimental Models of Tauopathy – From Mechanisms to Therapies
Götz, J. J., & Götz, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_28 · Cited by 24
Self-citationLi, D., & Cho, Y. K. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14830 · Cited by 23
Progress in the modeling of neurodegenerative diseases in transgenic mice
Duff, K., & Rao, M. V. (2001) · Current Opinion in Neurology · doi:10.1097/00019052-200108000-00003 · Cited by 22
Olfactory dysfunction in the 3xTg-AD model of Alzheimer’s disease
Mitrano, D. A., Houle, S., Pearce, P., Quintanilla, R. M., Lockhart, B. K., Genovese, B. C., Schendzielos, R., Croushore, E. E., Dymond, E. M., Bogenpohl, J. W., et al. (2021) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2020.12.004 · Cited by 21
Transgenic Mouse Models for the Study of Neurodegenerative Diseases
Marín‐Moreno, A., Canoyra, S., Fernández‐Borges, N., Espinosa, J. C., & Torres, J. M. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2801021 · Cited by 21
Neuroendocrinology of Neurodegenerative Diseases
de Aguilar, J. G., René, F., Dupuis, L., & Loeffler, J. (2003) · Neuroendocrinology · doi:10.1159/000074445 · Cited by 22
Tau neurotoxicity without the lesions: a fly challenges a tangled web
de Silva, R., & Farrer, M. J. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)02170-7 · Cited by 21
Cassel, J., Mathis, C., Majchrzak, M. J., Moreau, P., & Dalrymple‐Alford, J. C. (2008) · Neurodegenerative Diseases · doi:10.1159/000135615 · Cited by 21
Reduced secretagogin expression in the hippocampus of P301L tau transgenic mice
Attems, J., Ittner, A., Jellinger, K. A., Nitsch, R. M., Maj, M. A., Wagner, L., Götz, J., & Heikenwälder, M. F. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0626-5 · Cited by 20
Self-citationModulation 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
Tracking white matter degeneration in asymptomatic and symptomatic MAPT mutation carriers
Chen, Q., Boeve, B. F., Schwarz, C. G., Reid, R. I., Tosakulwong, N., Lesnick, T. G., Bove, J., Brannelly, P., Brushaber, D. E., Coppola, G., et al. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.08.011 · Cited by 20
Hromádková, L., Siddiqi, M. K., Liu, H., & Safar, J. (2022) · Cells · doi:10.3390/cells11192997 · Cited by 19
Müller-Thomsen, L., Borgmann, D., Morcinek, K., Schröder, S. L., Dengler, B., Moser, N., Neumaier, F., Schneider, T., Schröder, H., & Huggenberger, S. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.03.007 · Cited by 19
Metadata
- Authors
- Götz, J., Chen, F., Barmettler, R., & Nitsch, R. M.
- Affiliations
- University of Zurich (CH)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 276
- Issue
- 1
- Pages
- 529-534
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2035156043
- Cited by
- 495
- References
- 26
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 29 · 2023: 13 · 2022: 20 · 2021: 18 · 2020: 16 · 2019: 17 · 2018: 9 · 2017: 16 · 2016: 10 · 2015: 11 · 2014: 15 · 2013: 22 · 2012: 18
- FWCI
- 18.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- transgenic mice, tau hyperphosphorylation, neurofibrillary tangles, tauopathy, neuronal apoptosis, astrocyte activation
- MeSH terms
- Animals, Brain, Gliosis, Humans, Immunohistochemistry, Mice, Transgenic, Actin Cytoskeleton, Microscopy, Electron, Microscopy, Fluorescence, Mutation, Organ Specificity, Phosphorylation, Protein Conformation, Immunoblotting, Gene Expression, Neurofibrillary Tangles, tau Proteins, Apoptosis, Amino Acid Substitution, Protein Isoforms, In Situ Nick-End Labeling, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review