The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo
Open accessAbstract
Tau is a microtubule binding protein implicated in a number of human neurodegenerative disorders, including Alzheimer's disease. Phosphorylation of serine-proline/threonine-proline sites, targeted by proline-directed kinases, coincides temporally with neurodegeneration in the human diseases. Recently, we demonstrated that this unique group of serines and threonines has a critical role in controlling tau toxicity in a Drosophila model of tauopathy. Here, we use a combination of genetic and biochemical approaches to examine these sites individually and to determine which of them is primarily responsible for controlling tau neurotoxicity. Despite the importance placed on individual phosphoepitopes and their contributions to disease pathogenesis, our results indicate that no single phosphorylation residue plays a dominant role in controlling tau toxicity. These findings suggest that serine-proline/threonine-proline sites cooperate to mediate neurodegeneration in vivo.
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
“in vivo fly models of tau toxicity using phosphorylation-resistant tau constructs show equivalent or even increased toxicity when compared with wild-type tau (41,42).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [41]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“when either 5 (41) or 11 (42) putative GSK-3β phosphorylation sites were mutated to alanine, tau toxicity either comparable to or more robust than the toxicity induced by wild-type tau was still observed.”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [41]
The cited source says what the claim attributes to it.
In the citing paper
“In addition, neuronal phenotypes of tau transgenic Drosophila mimic features of human Alzheimer’s disease and associated tauopathies, including but not limited to aberrant tau phosphorylation13, oxidative stress14, DNA damage15,16, decondensation of constitutive heterochromatin10, synaptic dysfunction17 and activation of the cell cycle in post-mitotic neurons18.”
From Pathogenic tau-induced piRNA depletion promotes neuronal death through transposable element dysregulation in neurodegenerative tauopathies (2018) · cites this paper as [13]
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
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
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 · cited 2×
“This abnormal hyperphosphorylation of tau induces an increase in the apparent molecular mass of the protein, which is observed in disease states (Lee et al., 1991).”
Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998
Tauopathy in Drosophila : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939
Self-citationGreenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 735
Noble, W., Planel, E., Zehr, C., Olm, V., Meyerson, J., Suleman, F., Gaynor, K., Wang, L., LaFrancois, J., Feinstein, B., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500466102 · Cited by 709
Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
Goedert, M., Jakes, R., & Vanmechelen, E. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11484-e · Cited by 608
Matsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588
Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404
Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., & Lee, V. M. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390607 · Cited by 488 · cited 9×
“Using disease-associated phospho-specific antibodies to analyze the phosphorylation status of tau AP5 , we found that reactivity with AT270, PHF1, and Tau1 was unchanged compared with tau WT (Figure 6C).”
InfluentialJackson, G. R., Wiedau-Pazos, M., Sang, T.-K., Wagle, N., Brown, C. A., Massachi, S., & Geschwind, D. H. (2002) · Neuron · doi:10.1016/s0896-6273(02)00706-7 · Cited by 488
Flagged first, then by citations
Research works printed but not linked: 1
- Kimura T., 1996, Dementia, 7, 177
Cited by
Sorted by citations
Items 101–187 of 187
The Power and Richness of Modelling Tauopathies in Drosophila
Papanikolopoulou, K., & Skoulakis, E. M. C. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8193-1 · Cited by 29
Lanzillotta, A., Sarnico, I., Benarese, M., Branca, C., Baiguera, C., Hutter‐Paier, B., Windisch, M., Spano, P., Imbimbo, B. P., & Pizzi, M. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9482-2 · Cited by 27
Studying tauopathies in Drosophila: A fruitful model
Sun, M., & Chen, L. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.03.029 · Cited by 27
Distinct systemic impacts of Aβ42 and Tau revealed by whole-organism snRNA-seq
Park, Y.-J., Lu, T., Jackson, T., Goodman, L. D., Ran, L., Chen, J., Liang, C., Harrison, E. M., Ko, C., Chen, X. X., et al. (2024) · Neuron · doi:10.1016/j.neuron.2025.04.017 · Cited by 27
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 25
Malcolm, J. C., Breuillaud, L., Carmo, S. D., Hall, H., Welikovitch, L. A., Macdonald, J. A., Goedert, M., & Cuello, A. C. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.018 · Cited by 25
Modelling Tauopathies in Drosophila : Insights from the Fruit Fly
Cowan, C. M., Sealey, M. A., Quraishe, S., Targett, M.-T., Marcellus, K. A., Allan, D. W., & Mudher, A. K. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/598157 · Cited by 26
Yao, Y., Chen, X., Bao, Y., & Wu, Y. S. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7702 · Cited by 23
Mechanism-based treatments for Alzheimer's disease
Davies, P., & Koppel, J. L. (2009) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2009.11.2/pdavies · Cited by 23
Yeboah, F., Kim, T., Bill, A., & Dettmer, U. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104543 · Cited by 22
Li, D., & Cho, Y. K. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14830 · Cited by 23
Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status
Pinzi, L., Bisi, N., Sorbi, C., Franchini, S., Tonali, N., & Rastelli, G. (2023) · Molecules · doi:10.3390/molecules28114544 · Cited by 20
New Age of Neuroproteomics in Alzheimer’s Disease Research
Kováčech, B., Žilka, N., & Novák, M. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9358-6 · Cited by 22
Schulz, L., Ramirez, P., Lemieux, A., Gonzalez, E. M., Thomson, T., & Frost, B. E. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.04.017 · Cited by 20
Non-conventional compounds with potential therapeutic effects against Alzheimer’s disease
de Castro, A. A., Soares, F. V., Pereira, A. F., Polisel, D. A., Caetano, M. S., Leal, D. H. S., da Cunha, E. F. F., Nepovimová, E., Kuča, K., & Ramalho, T. C. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1608823 · Cited by 20
Fernius, J., Starkenberg, A., Pokrzywa, M., & Thor, S. (2017) · Biology Open · doi:10.1242/bio.022749 · Cited by 21
Amini, J., Sanchooli, N., Milajerdi, M.-H., Baeeri, M., Haddadi, M., & Sanadgol, N. (2023) · International Journal of Neuroscience · doi:10.1080/00207454.2023.2210409 · Cited by 19
Yeh, P.-A., Chien, J.-Y., Chou, C.-C., Huang, Y.-F., Tang, C.-Y., Wang, H.-Y. A., & Su, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.11.089 · Cited by 19
Hoque, A., Williamson, N. A., Ameen, S. S., Ciccotosto, G. D., Hossain, M. I., Oakhill, J. S., Ng, D. C. H., Ang, C., & Cheng, H. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1445-0 · Cited by 19
Spears, W. E., Furgerson, M., Sweetnam, J. M. C., Evans, P. T., Gearing, M., Fechheimer, M., & Furukawa, R. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-74 · Cited by 19
Quantitative Analysis of MAP-Mediated Regulation of Microtubule Dynamic Instability In Vitro
Kiris, E., Ventimiglia, D., & Feinstein, S. C. (2010) · Methods in cell biology · doi:10.1016/s0091-679x(10)95024-3 · Cited by 19
Alzheimer's disease models and functional genomics—How many needles are there in the haystack?
Götz, J., Matamales, M., Götz, N. N., Ittner, L. M., & Eckert, A. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00320 · Cited by 19
New Approaches to the Pathology and Genetics of Neurodegeneration
Feany, M. Β. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.091077 · Cited by 17
Self-citationRodriguez, L., Mdzomba, J. B., Joly, S., Boudreau-Laprise, M., Planel, E., & Pernet, V. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00293 · Cited by 16
Chi, H., Lee, S., Shiu, R.-H., Han, R., Hsieh, C.-P., Wei, T.-M., Lo, C., Chang, H.-Y., & Sang, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-70423-1 · Cited by 17
Zhao, Z., Ning, Y., Li, P., Yang, N., Peng, Y., Xiong, R., Zhao, Y., Liu, D., Zeng, X., Chen, J., et al. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.02.002 · Cited by 15
Nithianandam, V., Bukhari, H., Leventhal, M. J., Battaglia, R. A., Dong, X., Fraenkel, E., & Feany, M. Β. (2023) · Nature Communications · doi:10.1038/s41467-023-42822-1 · Cited by 16
Self-citationThe Drosophila model system to study tau action
Trotter, M., Stephens, T. D., McGrath, J. P., & Steinhilb, M. L. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.006 · Cited by 15
Self-citationUsingDrosophilamodels of neurodegenerative diseases for drug discovery
Newman, T. A., Sinadinos, C., Johnston, A. H., Sealey, M. A., & Mudher, A. K. (2011) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2011.549124 · Cited by 14
Loeffler, D. A., Aasly, J. O., LeWitt, P. A., & Coffey, M. P. (2019) · Journal of Parkinson s Disease · doi:10.3233/jpd-191630 · Cited by 13
Guha, S. K., Cheng, A., Carroll, T., King, D. P., Koren, S. A., Swords, S., Nehrke, K. W., & Johnson, G. V. W. (2022) · Genetics · doi:10.1093/genetics/iyac104 · Cited by 11
Cai, J., Ruan, J., Shao, X., Ding, Y., Xie, K., Tang, C., Yan, Z., Luo, E., & Jing, D. (2021) · High Altitude Medicine & Biology · doi:10.1089/ham.2020.0218 · Cited by 11
Tau Protein: Function and Pathology
Rosenmann, H., Blum, D. L., Kayed, R., & Ittner, L. M. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/707482 · Cited by 12
Therapeutic Targets in Alzheimer's Disease and Related Tauopathies
Corbo, C. P., & Alonso, A. D. C. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385506-0.00002-8 · Cited by 13
Wang, K., Zhang, G., & Kuo, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914996 · Cited by 11
Zhang, M. Y., Lear, B. C., & Allada, R. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab303 · Cited by 11
Keramidis, I., Vourkou, E., Papanikolopoulou, K., & Skoulakis, E. M. C. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.569520 · Cited by 11
Shukla, D., Suryavanshi, A., Bharti, S. K., Asati, V., & Mahapatra, D. K. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266299847240328045737 · Cited by 10
Unraveling the Basis of Neurodegeneration using the Drosophila Eye
Fernández-Fúnez, P., Sanchez-Garcia, J., & Rincón-Limas, D. E. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8232-1_10 · Cited by 9
Altered Gut Microbial Load and Immune Activation in a Drosophila Model of Human Tauopathy
Rydbom, J., Kohl, H., Hyde, V. R., & Lohr, K. M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.731602 · Cited by 9
Expression of 1N3R-Tau Isoform Inhibits Cell Proliferation by Inducing S Phase Arrest in N2a Cells
Li, L., Xu, Z., Liu, G., Xu, C., Wang, Z.-H., Li, X., Liu, E.-J., Zeng, J., Chai, D., Yao, W., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119865 · Cited by 9
What we can learn from animal models about cerebral multi-morbidity
Baker, S. L., & Götz, J. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0097-2 · Cited by 8
Fernandez, F., Aust, C. E., Lye, S., & Griffiths, L. R. (2022) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2022.100435 · Cited by 8
Sharallah, O. A., Poddar, N. K., & Alwadan, O. A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102394 · Cited by 7
Loeffler, D. A., Smith, L. M., Klaver, A. C., & Martić, S. (2015) · Experimental Gerontology · doi:10.1016/j.exger.2015.04.010 · Cited by 7
hSOD1 Promotes Tau Phosphorylation and Toxicity in the Drosophila Model
Huang, Y., Wu, Z., & Zhou, B. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-141608 · Cited by 7
Growth arrest specific protein 7 inhibits tau fibrillogenesis
Shimizu, T., Hirose, K., Uchida, C., & Uchida, T. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.03.041 · Cited by 5
Tabassum, Z., Tseng, J., Isemann, C., Tian, X., Chen, Y., Herring, L. E., & Cohen, T. J. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101977 · Cited by 5
Bakhtiarzadeh, F., Shahpasand, K., Shojaei, A., Fathollahi, Y., & Mirnajafi‐Zadeh, J. (2023) · Behavioral and Brain Functions · doi:10.1186/s12993-023-00211-0 · Cited by 4
Neuronal Models for Studying Tau Pathology
Koechling, T., Lim, F., Hernández, F., & Ávila, J. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/528474 · Cited by 6
Kim, Y. J. (2017) · Brain & Neurorehabilitation · doi:10.12786/bn.2017.10.e4 · Cited by 5
Weir, J. S., Hanssen, K. S., Winter‐Hjelm, N., Sandvig, A., & Sandvig, I. (2024) · European Journal of Neuroscience · doi:10.1111/ejn.16625 · Cited by 3
Martínez, P., Jury, N., Patel, H., You, Y., Perkins, A., You, Y., Lee‐Gosselin, A., Vidal, R., & Lasagna‐Reeves, C. A. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251372603 · Cited by 3
Yeast surface display of full‐length human microtubule‐associated protein tau
Wang, S., & Cho, Y. K. (2019) · Biotechnology Progress · doi:10.1002/btpr.2920 · Cited by 3
Gode, D., Schmitt, C., Engel, M., & Volmer, D. A. (2014) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-014-7703-1 · Cited by 3
Peng, C.-H., Hwang, T., Hung, S.-C., Tu, H., Tseng, Y.-T., Lin, T. E., Lee, C., Tseng, Y.-C., Ko, C., Yen, S., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136860 · Cited by 3
Drosophila Models of Tauopathy
Ali, Y., Ruan, K., & Zhai, R. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00054-8 · Cited by 2
Insights into amyloid disease from fly models
Chen, K., & Crowther, D. C. (2014) · Essays in Biochemistry · doi:10.1042/bse0560069 · Cited by 2
Ávila, J., & Hernández, F. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-6787-9_3 · Cited by 2
Phospho-Tau Signature During Mitosis: AT8, p-T217 and p-S422 as Key Phospho-Epitopes
Goussard, M., Zarka, K., Denus, M., Curel, T., Claeysen, S., Lefebvre, B., Hamdane, M., Marin, P., Villeneuve, J., & Parmentier, M. (2025) · Cells · doi:10.3390/cells14201638 · Cited by 1
Hima, S., Aiswarya, N., Remya, C., Vasudevan, D. M., Dileep, K. V., & Francis, D. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.11.009 · Cited by 1
Tau Phosphorylation as a Therapeutic Target in Alzheimer’s Disease
Medina, M., & Ávila, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00012-5 · Cited by 1
Neurodegeneration models in Drosophila
Roy, B., & Jackson, G. R. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511920585.012 · Cited by 1
Schmitt, C. (2014) · Publications of the UdS (Saarland University) · doi:10.22028/d291-22977
Zheng, F., Zhang, B., Sun, Y., Qiu, M., & Su, J. (2015) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2015.1042860
Alternative Models of Prion Diseases
Fernández-Fúnez, P., Trillo, E. M., & Rincón-Limas, D. E. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5338-3_12
Pseudophosphorylation of tau modulates its function and induces AD-like changes
Sun, Q. (2009) · KU ScholarWorks (The University of Kansas)
The involvement of degradation pathways and neuron-to-neuron transmission in Alzheimer’s disease
Agholme, L. (2012) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Animal Models of Frontotemporal Dementia
Dawson, H. N., & Laskowitz, D. T. (2010) · Neuromethods · doi:10.1007/978-1-60761-898-0_28
Drosophila model of cognitive disorders: Focus on memory abnormality
Shao, L., & Zhong, Y. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511920585.013
Butzlaff, M. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-1007
Nitrate Chimeras: A New Class of Disease Modifying Agents for the Treatment of Alzheimer's Disease
VandeVrede, L. A. (2014) · Figshare
Guha, S. K., Cheng, A., Carroll, T., King, D. P., Koren, S. A., Swords, S., Nehrke, K. W., & Johnson, G. V. W. (2021) · Research Square · doi:10.21203/rs.3.rs-1096882/v1
Ahmadi, N., Steinberg, A. M., & Pynoos, R. S. (2021) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2021.08.012
Sljoka, A., Zhu, S., Shala, A., Bezginov, A., Audette, G. F., & Wilson, D. J. (2021) · doi:10.32920/14668836
Ryoo, H. D. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733685711.793549102
Sljoka, A., Zhu, S., Shala, A., Bezginov, A., Audette, G. F., & Wilson, D. J. (2021) · doi:10.32920/14668836.v1 · Cited by 2
Drosophila Models of Prion Diseases
Myers, R. R., & Fernández-Fúnez, P. (2023) · Springer eBooks · doi:10.1007/978-3-031-20565-1_17
Tang, Z., Guo, M., Ding, Y., Wen, Y., Li, B., Xiao, Y., Ni, R., Guan, Z.-Z., & Qi, X. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.24.625068 · Cited by 1
Sepulveda-Diaz, J. E. (2013) · theses.fr (ABES) · doi:10.70675/56c42bcbz41dfz432bzbb78z77110b373285
Mitochondria, neurosteroids and biological rhythms : implications in health and disease states
Grimm, A. (2015) · theses.fr (ABES) · doi:10.70675/8aac5aa9z77cdz49bdz9cf5z0ff0b5dd0f84
Identification et caractérisation fonctionnelle de nouveaux sites de clivage de la protéine Tau
Derisbourg, M. J. (2015) · theses.fr (ABES) · doi:10.70675/ef5f45b0zf4e8z433fz9beaz8d2cc6de65bc
Pescheteau, C. (2021) · theses.fr (ABES) · doi:10.70675/f258c770z5a4bz407bz9533z56a9b2b6a0f8
Lu, M. P., Rong, Y., Wang, J., Yu, X., Liu, H., Wu, Y., Zhang, M., Chen, Y., Li, Y., Yan, Y., et al. (2026) · Cells · doi:10.3390/cells15090793
Metadata
- Authors
- Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B.
- Affiliations
- Central Michigan University (US)
- Brigham and Women's Hospital (US)
- Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115; and
- Venue
- Molecular Biology of the Cell
- Published
- 2007-12
- Volume
- 18
- Issue
- 12
- Pages
- 5060-5068
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2096612
- OpenAlex
- W2165049228
- Cited by
- 187
- References
- 46
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 7 · 2023: 6 · 2022: 5 · 2021: 16 · 2020: 5 · 2019: 13 · 2018: 4 · 2017: 11 · 2016: 7 · 2015: 14 · 2014: 15 · 2013: 14 · 2012: 9
- FWCI
- 8.94
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG-19790, P50AG005134, AG 05134, R01AG019790)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau phosphorylation, proline-directed kinases, tauopathy, Alzheimer's disease, Drosophila model, neurodegeneration, microtubule-binding protein
- MeSH terms
- Amino Acids, Animals, Cell Cycle, Drosophila melanogaster, Electrophoresis, Polyacrylamide Gel, Mutation, Neurons, Phosphorylation, Protein Kinases, Signal Transduction, tau Proteins, Phosphatidylinositol 3-Kinases, Drosophila Proteins, Animals, Genetically Modified, TOR Serine-Threonine Kinases
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
