Cited by 477Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 170 of the 171 references it cites were found in a registry or an index.

The Importance of Tau Phosphorylation for Neurodegenerative Diseases

Open access

Noble, Wendy, Hanger, Diane P., Miller, Christopher C. J., Lovestone, Simon·2013·Frontiers in Neurology

DOI 10.3389/fneur.2013.00083PMC PMC3696910

Open this paper in CoChat — free account Open PDF

Abstract

Fibrillar deposits of highly phosphorylated tau are a key pathological feature of several neurodegenerative tauopathies including Alzheimer's disease (AD) and some frontotemporal dementias. Increasing evidence suggests that the presence of these end-stage neurofibrillary lesions do not cause neuronal loss, but rather that alterations to soluble tau proteins induce neurodegeneration. In particular, aberrant tau phosphorylation is acknowledged to be a key disease process, influencing tau structure, distribution, and function in neurons. Although typically described as a cytosolic protein that associates with microtubules and regulates axonal transport, several additional functions of tau have recently been demonstrated, including roles in DNA stabilization, and synaptic function. Most recently, studies examining the trans-synaptic spread of tau pathology in disease models have suggested a potential role for extracellular tau in cell signaling pathways intrinsic to neurodegeneration. Here we review the evidence showing that tau phosphorylation plays a key role in neurodegenerative tauopathies. We also comment on the tractability of altering phosphorylation-dependent tau functions for therapeutic intervention in AD and related disorders.

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

Crossref · 10.3389/fneur.2013.00083

Cites

170 of 171 references verified1 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Chapter 12: What does the Anthropocene hold for citizenship?
(2019) · edoc (University of Basel) · doi:10.1007/978-3 · Cited by 11,533
Stages of the Pathologic Process in Alzheimer Disease: Age Categories From 1 to 100 Years
Braak, H., Thal, D. R., Ghebremedhin, E., & Del Tredici, K. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318232a379 · Cited by 2,194
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526
Propagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252
Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012

Flagged first, then by citations

Show all 169 references

Sorted by citations

Items 301–400 of 477

An emerging role for the gut microbiome in tauopathy
Zhu, Y., Self, W. K., & Holtzman, D. M. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00423 · Cited by 6
Proteomic analysis of heat-stable proteins revealed an increased proportion of proteins with compositionally biased regions
Park, H., Yamanaka, T., & Nukina, N. (2022) · Scientific Reports · doi:10.1038/s41598-022-08044-z · Cited by 6
The ataxia-telangiectasia disease protein ATM controls vesicular protein secretion via CHGA and microtubule dynamics via CRMP5
Reichlmeir, M., Duecker, R. P., Röhrich, H., Key, J., Schubert, R., Abell, K., Possemato, A. P., Stokes, M. P., & Auburger, G. W. J. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106756 · Cited by 5
Dehydroamino acids and their crosslinks in Alzheimer’s disease aggregates
Markovich, S. W., Frey, B. L., Scalf, M., Shortreed, M. R., & Smith, L. M. (2024) · Brain Communications · doi:10.1093/braincomms/fcaf019 · Cited by 5
From Better Diagnostics to Earlier Treatment: The Rapidly Evolving Alzheimer’s Disease Landscape
Bougea, A. M., Debasa‐Mouce, M., Gulkarov, S., Castro‐Mosquera, M., Reiss, A. B., & Ouro, A. (2025) · Medicina · doi:10.3390/medicina61081462 · Cited by 5
Precision Medicine in Neurodegenerative Diseases: Genomic Approaches to Target Amyloid-β, Tau, and Alpha-Synuclein Pathways
Waqar, Z., Sethi, P., Jain, D., Singh, K., Alsaidan, O. A., Alzarea, S. I., Gupta, J. K., Saxena, S., & Sharma, M. C. (2025) · Current Genomics · doi:10.2174/0113892029372437251010114053 · Cited by 6
Targeting tau hyperphosphorylation-mediated neuroinflammation in Alzheimer's disease via ABL1 kinase inhibition: Insights from microsecond MD simulation and MM/PBSA analyses
Choudhury, A., Prabha, S., Saeed, M. U., Mohammad, T., Hussain, A., Alajmi, M. F., Khan, F. I., Islam, A., & Hassan, M. I. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145785 · Cited by 5
Apolipoprotein E4 as a Novel Treatment Target for Alzheimer’s Disease
Jervies, J. L., King, S. P., & Suphioglu, C. (2021) · Cellular Physiology and Biochemistry · doi:10.33594/000000475 · Cited by 5
Infection promotes Ser‐214 phosphorylation important for generation of cytotoxic tau variants
Balczon, R., Choi, C., Deweever, A., Zhou, C., Gwin, M. S., Kolb, C., Francis, C. M., Lin, M. T., & Stevens, T. (2023) · The FASEB Journal · doi:10.1096/fj.202300620rr · Cited by 5
Sodium signal intensity of CSF using 1H‐guided 23Na‐MRI as a potential noninvasive biomarker in Alzheimer's disease
Kerl, H. U., Baazaoui, H., Herrmann, K., Adlung, A., Ludwig, N. K., Hausner, L., Frölich, L., Schad, L. R., Groden, C., & Mohamed, S. A. (2024) · Journal of Neuroimaging · doi:10.1111/jon.13216 · Cited by 5
Plasma phosphorylated tau (p-tau231) and total tau (t-tau) as prognostic markers of neurological outcome after cardiac arrest - a multicentre study
Þorgeirsdóttir, B., Sievert, T., Lybeck, A., Ashton, N. J., Blennow, K., Zetterberg, H., Friberg, H., & Frigyesi, A. (2024) · Resuscitation · doi:10.1016/j.resuscitation.2024.110450 · Cited by 5
Bioactive compound nanoparticles for Alzheimer's disease
Kshirsagar, N., Patil, A., & Suryawanshi, M. V. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01801-2 · Cited by 5
Imaging pathological tau in atypical parkinsonian disorders
Coakeley, S., & Strafella, A. P. (2015) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000210 · Cited by 5
Investigating key factors underlying neurodegeneration linked to alpha‐synuclein spread
Pang, C. C.-C., Sørensen, M. H., Lee, K., Luk, K. C., Trojanowski, J. Q., Lee, V. M. ‐., Noble, W. J., & Chang, R. C. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12829 · Cited by 4
Self-citation
Proteomic Assessment of C57BL/6 Hippocampi after Non-Selective Pharmacological Inhibition of Nitric Oxide Synthase Activity: Implications of Seizure-like Neuronal Hyperexcitability Followed by Tauopathy
Hendrickx, J. O., Adams, C., Sieben, A., Laukens, K., Dam, D. V., & Meyer, G. R. Y. D. (2022) · Biomedicines · doi:10.3390/biomedicines10081772 · Cited by 5
Toxoplasma GRA16 attenuates Tau hyperphosphorylation and enhances autophagy in thrombin-treated HT-22 hippocampal neuronal cells
Seo, S., Ham, D.-W., Lee, J.-E., & Shin, E. (2025) · Scientific Reports · doi:10.1038/s41598-025-00271-4 · Cited by 4
Molecular Mechanisms Underlying Alzheimer’s Disease Pathogenesis: Comprehensive Overview
Vecchio, F. L., la Torre, A., Gravina, C., D’Onofrio, G., & Greco, A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27104651 · Cited by 5
Preliminary evaluation of the proteomic profiling in the hippocampus of aged grazing cattle
Cozzolino, F., Canè, L., Sacchettino, L., Gatto, M. C., Iacobucci, I., GATTA, C. L., Biase, D. D., Napoli, E. D., Paciello, O., Avallone, L., et al. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1274073 · Cited by 4
A Novel Phosphorylated Tau Conformer Implicated in the Tauopathy Pathogenesis of Human Neurons
Tofigh, N., Agahi, S., Riazi, G. H., Pakdaman, H., Moazzam, M. G., & Shahpasand, K. (2025) · Biomolecules · doi:10.3390/biom15040585 · Cited by 4
Upregulation of LRRK2 following traumatic brain injury does not directly phosphorylate Thr175 tau
Donison, N. S., Hintermayer, M. A., Subramaniam, M., Santandrea, E., Volkening, K., & Strong, M. J. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1272899 · Cited by 4
α-Tocotrienol Protects Neurons by Preventing Tau Hyperphosphorylation via Inhibiting Microtubule Affinity-Regulating Kinase Activation
Liu, Y., Chen, Y., & Fukui, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158428 · Cited by 5
Pathology and pathophysiology
Dickerson, B. C. (2015) · Cambridge University Press eBooks · doi:10.1017/cbo9781316091586.016 · Cited by 4
Interplay of isoform 1N4R tau protein and amyloid-β peptide fragment 25–35 in reducing and non-reducing conditions
Mohammadi, F., Takalloo, Z., Rahmani, H., Khalili, M. A. N., Khajeh, K., Riazi, G. H., & Sajedi, R. H. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa101 · Cited by 4
Fukutin regulates tau phosphorylation and synaptic function: Novel properties of fukutin in neurons
Tsukui, R., Yamamoto, T., Okamura, Y., Kato, Y., & Shibata, N. (2022) · Neuropathology · doi:10.1111/neup.12797 · Cited by 4
Neuroimaging (Anatomical MRI)-Based Classification of Alzheimer’s Diseases and Mild Cognitive Impairment Using Convolution Neural Network
Khan, Y. F., & Kaushik, B. (2022) · Lecture notes on data engineering and communications technologies · doi:10.1007/978-981-16-8403-6_7 · Cited by 4
An Insight into the Protein Aggregation in Alzheimer’s Disease and its Inhibition
Khan, A. B., & Khan, R. H. (2023) · Protein and Peptide Letters · doi:10.2174/0109298665247757231020044633 · Cited by 4
Subcellular functions of tau mediate repair response and synaptic homeostasis in injury
Thomas, R., Zhang, D., Cronkite, C. A., Thomas, R., Singh, S. K., Bronk, L. F., Morales, R., Duman, J. G., & Grosshans, D. R. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-03029-6 · Cited by 6
Combining experiments and simulations to study the impact of multiple phosphorylations at the AT8 epitope of the Tau proteinPreprint
Lohberger, C., Marien, J., Bridot, C., Prévost, C., Allegro, D., Tatoni, M., Boll, E., Cantrelle, F., Martinho, M., Belle, V., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.22.639620 · Cited by 5
Polled Intersex Syndrome and Polledness in Goats: Molecular Aspects
Szatkowska, I., Udała, J., Zaborski, D., Czerniawska‐Piątkowska, E., Grzesiak, W., Wasielewska, M., & Wójcik, J. (2023) · Pakistan Journal of Zoology · doi:10.17582/journal.pjz/20220129110121 · Cited by 3
SUMO inhibits Tau aggregation in Alzheimer’s disease
Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.02.001 · Cited by 4
Structure‐Based Approaches for the Prediction of Alzheimer's Disease Inhibitors: Comparative Interactions Analysis, Pharmacophore Modeling and Molecular Dynamics Simulations
Zerroug, E., Belaıdı, S., Chtita, S., Tuffaha, G. O., Qais, F. A., Kciuk, M., Dubey, A., & Taha, M. O. (2024) · ChemistrySelect · doi:10.1002/slct.202303307 · Cited by 3
Neuronal Excitation Induces Tau Protein Dephosphorylation via Protein Phosphatase 1 Activation to Promote Its Binding with Stable Microtubules
Yagishita, S., Shibata, M., Furuno, A., Wakatsuki, S., & Araki, T. (2024) · Neurology International · doi:10.3390/neurolint16030049 · Cited by 3
Tau positron emission tomography in tauopathies: A narrative review
Lee, H., Gu, Y., Seo, S. W., & Moon, S. H. (2023) · Precision and Future Medicine · doi:10.23838/pfm.2023.00016 · Cited by 4
Circ_0049472 downregulation relieves Amyloid-β-induced neuronal injury by modulating PDE4A expression via targeting miR-22-3p in Alzheimer’s disease
Chen, J., Xiao, S., Cui, X., Gao, X. P., Wang, D., Li, X., Qi, W., & Wang, B. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01652-4 · Cited by 3
Perspectives on the Role of APOE4 as a Therapeutic Target for Alzheimer’s Disease
Patel, K., Srivastava, S., Kushwah, S., & Mani, A. (2021) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-210027 · Cited by 4
Nanotechnology: An Emerging Field in Protein Aggregation and Cancer Therapeutics
Jena, S., Mohanty, S., Ojha, M., Subham, K., & Jha, S. (2021) · Springer eBooks · doi:10.1007/978-981-16-2516-9_11 · Cited by 3
Mapping Alzheimer’s Molecular Pathologies in Large-Scale Connectomics Data: A Publicly Accessible Correlative Microscopy ResourcePreprint
Han, X., Li, P. H., Wang, S., Blakely, T. M., Aggarwal, S., Gopalani, B., Sanchez, M., Schalek, R. L., Meirovitch, Y., Lin, Z., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.24.563674 · Cited by 3
Endogenous tau released from human ReNCell VM cultures by neuronal activity is phosphorylated at multiple sitesPreprint
Sindi, G., Ismael, S., Uddin, R., Slepchenko, K. G., Colvin, R. A., & Lee, D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.02.597022 · Cited by 3
The Effect of the Tau Protein on D. melanogaster Lifespan Depends on GSK3 Expression and Sex
Veselkina, E. R., Trostnikov, M. V., Roshina, N. V., & PASYUKOVA, E. G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032166 · Cited by 3
The Role of Periodontitis in Increasing Cognitive Decline in Alzheimer\'s Disease
Freitas, C. M. T., Patil, S., Klonaris, N., & Murcia, J. D. G. (2025) · The Journal of Contemporary Dental Practice · doi:10.5005/jp-journals-10024-3847 · Cited by 2
PhosF3C: a feature fusion architecture with fine-tuned protein language model and conformer for prediction of general phosphorylation site
Liu, Y., Wang, X., Zhong, H., Zhai, J., Gong, X., & Lu, T. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf242 · Cited by 2
Targeting of kinases to treat neurodegenerative diseases
Shomali, T., & Trempe, J.-F. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100128 · Cited by 4
Water‐Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils
Potnuru, L. R., DuBose, A., Mon, F., Nowotarski, M. S., Vigers, M. P., Zhang, B., Han, C.-T., Straub, J. E., & Han, S. (2026) · Angewandte Chemie · doi:10.1002/ange.202521499 · Cited by 1
Molecular and environmental drivers of tau post-translational modifications and tau pathology
Price, T. M., Tucker, A. E., & Funk, K. E. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103223 · Cited by 2
Epigenetic regulons in Alzheimer's disease
Raval, M., Mishra, S., & Tiwari, A. K. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.01.012 · Cited by 2
Potent of strategic approaches for tauopathies ranging from single-cell transcriptome to microbiome
Kim, S., Yang, S., Yang, E.-J., Kang, M., & Joo, J. (2023) · Animal Cells and Systems · doi:10.1080/19768354.2023.2285826 · Cited by 2
The Interplay of Tau and Amyloid Beta Pathologies in Alzheimer's Disease
Harith, M. (2023) · Journal of Student Research · doi:10.47611/jsrhs.v12i4.5732 · Cited by 2
Deciphering the role of TYK2 in tau phosphorylation and pathology
Fröhlich, A., & Bowles, K. R. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.01.004 · Cited by 2
Mechanistic insights into the inhibition of microtubule affinity-regulating kinase 4 by Syringic acid: A computational and experimental study
Shahwan, M. J., Yadav, D. K., Khan, M. S., Choudhury, A., Shamsi, A., Hassan, M. I., & Anwar, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142812 · Cited by 2
Uncovering the Path to Neurodegeneration from Playingfield to Battlefield
Baas, F., & Ramagli, V. (2014) · InTech eBooks · doi:10.5772/57186 · Cited by 1
Secondary Metabolites of Lichens as Both Anti-aggregative and Antioxidant Agents in Tauopathies
Cornejo, A., & Areche, C. (2017) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.1000496 · Cited by 2
A low-cost, flexible extruder for liposomes synthesis and application for Murrayafoline A delivery for cancer treatment
Pham, T. D., Nguyen, L. P., Phan, Q. T. H., Pham, C. K., Pham, D. T. N., Viet, N. T., Nguyen, H. V. T., Tran, T. Q., & Nguyen, D. T. (2022) · Journal of Biomaterials Applications · doi:10.1177/08853282221112491 · Cited by 2
Phosphatidylinositol (PI) Lipids Modulate the Binding of Tau Fibrils on Lipid BilayersPreprint
Chowdhury, U. D., Paul, A., & Bhargava, B. L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.20.558589 · Cited by 2
Tau pathology reprograms glucose metabolism to support glutamatergic activity and excitatory imbalancePreprint
Irmen, R. E., Turner, S. M., Snipes, J. A., Williams, H. C., Velmurugan, G. V., Hunt, J. B., Li, J., Sullivan, P. G., Lee, D. C., Johnson, L. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.25.666872 · Cited by 2
Parameter Dependence of the Solubility Limit for Disodium Phosphate
Huang, C. J., & Pettitt, B. M. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c05343 · Cited by 1
Nanotheranostic Approach for Targeting Tauopathies in Alzheimer's Disease: Mechanistic Insight and Recent Advances
Sahu, K. K., Chaudhary, R., Farooqi, M. A., & Kaurav, M. (2024) · Drug Delivery Letters · doi:10.2174/0122103031331346241122152643 · Cited by 1
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
Maternal Bisphenol A Exposure Induces Hippocampal‐Dependent Learning and Memory Deficits Through the PI3K/Akt/mTOR Pathway in Male Offspring Rats
Ren, J., Bai, W., Guo, Y., Liu, Q., Wang, Y., & Wang, C. (2025) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70100 · Cited by 1
Rapid Microwave Fixation of the Brain Reveals Seasonal Changes in the Phosphoproteome of Hibernating Thirteen-Lined Ground Squirrels
Abid, M. S. R., Naldrett, M. J., Alvarez, S., Eichhorn, C. D., Andrews, M. T., & Checco, J. W. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00635 · Cited by 1
Cognitive-and lifestyle-related microstructural variation in the ageing human hippocampus
Agyekum, T., García, C. L., Fay, F., Parent, O., Bussy, A., Devenyi, G. A., & Chakravarty, M. M. (2025) · Brain Structure and Function · doi:10.1007/s00429-025-02908-6 · Cited by 2
Alcohol consumption in P301S mice accelerates gait impairments, modifies aggregation of pathological tau and alters microglia within the hippocampus
Maphis, N. M., Furlano, D. A., David, S. A., & Linsenbardt, D. N. (2025) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.70123 · Cited by 1
Tau Amyloid Corona‐Shelled Nanoparticle‐Based Drug Screening Platform for Discovering Tau Oligomer‐Degrading Drugs
Jung, H. G., Park, D., Bang, J., Kim, Y. H., Jang, J. W., Kim, Y.-H., Kim, H., Lee, S., Moon, W., Hwang, K. S., et al. (2025) · Aggregate · doi:10.1002/agt2.70139 · Cited by 1
Exploring pyrazolidinone and pyrazolidinedione scaffolds for Alzheimer's therapy: multitarget COX-2 inhibitors with anti-amyloid β, anti-tau, antioxidant, and neuroprotective activities
Emad, M., Waheed, R., Mostafa, Z., Darwish, S. S., Purgatorio, R., Miniero, D. V., Palma, A. D., Cheng, T., Chen, Y., Gabr, M. T., et al. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00802f · Cited by 1
Hybrid molecules with dual inhibition of acetylcholinesterase and tau hyperphosphorylation: design, inhibitory activity evaluation, apoptosis assessment, and mechanistic exploration
Hu, Q., Xu, K., Ran, Q., Zhang, W., Gan, C., Fang, Q., & Hui, A. (2025) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2025.111848 · Cited by 2
Altered gene expression associated with Alzheimer's disease in the SH-SY5Y neuroblastoma cell model: Enhanced intracellular GSK3β and Cyclophilin A, as key neuropathology-inducing factors
Pashaei, S., Mirzaei, S. Z., Mohammadi, S., Shabani, S., & Khodarahmi‬, R. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.150648 · Cited by 1
How do copper( ii ) and zinc( ii ) bind to tau protein, and how might this promote aggregation?
Balogh, B. D., Natale, G. D., Pappalardo, G., & Várnagy, K. (2026) · Dalton Transactions · doi:10.1039/d5dt03057a · Cited by 1
Toward common treatment strategies: convergent proteinopathies and mitochondrial dysfunction in Alzheimer’s and Parkinson’s diseases
Offerdahl, J. E. V., & Mor, D. E. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1846384 · Cited by 1
Caenorhabditis elegans as a Model for Studying Nrf2/SKN-1 Activation in Alzheimer’s Disease: Plant Bioactive Compounds and Therapeutic Translation
Bellver‐Sanchís, A., Ralchev, N., Romanska, P. R., Dyakova, N. K., Ivanova, K. I., Griñán‐Ferré, C., & Marchev, A. S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27177833 · Cited by 1
The potential of proteomics for in-depth molecular investigations of progressive supranuclear palsy
Romero-Murillo, S., Lee, S., Fernández‐Irigoyen, J., Martínez-Valbuena, I., & Santamaría, E. (2025) · Expert Review of Proteomics · doi:10.1080/14789450.2025.2519466 · Cited by 1
Fluid and Imaging Markers of Frontotemporal Lobar Degeneration
Prinse, F., Houwer, J. F. H. D., Dopper, E. G. P., & Seelaar, H. (2025) · Springer eBooks · doi:10.1007/978-3-031-80849-4_9 · Cited by 1
New insights into the molecular biology of Alzheimer’s-like cerebral amyloidosis achieved through multi‐omics approaches
Campanelli, L., Sendoya, J. M., Brody, S. I., Galeano, P., Carmo, S. D., Cuello, A. C., Castaño, E. M., Gonzalez-Jimenez, A., Verheul, J., Vera, D. M., et al. (2025) · PLoS ONE · doi:10.1371/journal.pone.0330859 · Cited by 1
Tau Aggregation, Conformational Selection, and Inhibition
Holden, M. R. (2018) · Digital Commons - DU (University of Denver) · Cited by 1
Racemization Hypothesis of COVID-19. Tip of the Iceberg
(2020) · Journal of Psychology and Neuroscience · doi:10.47485/2693-2490.1033 · Cited by 1
Dysfunctional vascular smooth muscle cells mediate early and late-stage neuroinflammation and Tau hyperphosphorylationPreprint
Aguilar-Pineda, J. A., Vera-López, K. J., Shrivastava, P., Nieto-Montesinos, R., Chávez‐Fumagalli, M. Á., Dávila-Del-Carpio, G., Valdez, B. G., Miller, C. L., Malhotra, R. K., Lindsay, M. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.13.439741 · Cited by 1
Self-citation
Veldwerk in het onderwijs
Doppen, P. (2007) · Utrecht University Repository (Utrecht University) · Cited by 1
Chemical Synthesis of Microtubule-Associated Protein Tau 2N4RPreprint
Powell, W. C., Jing, R., & Walczak, M. A. A. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-js9bp
Amyloid-beta deposition and reduced drainage at the cribriform plate lymphatics in APP/PS1 mouse model of Alzheimer’s DiseasePreprint
Vrba, S. M., Laaker, C. J., Limkar, A. R., Hsu, M., Ricke, W. A., Ulland, T. K., Pehar, M., Sándor, M., & Fábry, Z. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.15.654007 · Cited by 1
SORLA upregulation suppresses global pathological effects in aged tauopathy mouse brainPreprint
Huang, H., Shi, C. H., Yang, W., Piña-Crespo, J., Bhatnagar, J., Curatolo, J., Murad, R., Shah, P. M., Campos, A. R., Houser, A. K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.25.661599 · Cited by 1
SORLA up-regulation suppresses pathological effects in aged tauopathy mouse brain
Huang, H., Shi, C. H., Yang, W., Piña-Crespo, J. C., Bhatnagar, J., Curatolo, J., Murad, R., Shah, P., Campos, A., Houser, A., et al. (2026) · Science Advances · doi:10.1126/sciadv.aed6825 · Cited by 1
The role of mTor in the pathogenesis of tau-related pathologies in Alzheimer Disease
Tang, Z. (2014) · Figshare
Tauopathies
Kovács, G. G. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781107588660.008
Functional implications of tau-fyn interactions in Alzheimer's disease
Lau, H. W. D. (2015)
Inhibition of Alzheimer’s type toxic aggregates of tau with fungal secondary metabolites
Paranjape, S. R. (2015) · KU ScholarWorks (University of Kansas)
Investigating the mechanisms underlying Alzheimer's disease using a novel organotypic brain slice culture model
Croft, C. L. (2016) · Research Portal (King's College London)
Engineering antibody therapeutics and cell culture models for neurodegenerative diseases
McHugh, K. P. (2016) · Library, Museums and Press - UDSpace (University of Delaware) · doi:10.58088/9ar9-m703
The Role of Imatinib Methanesulfonate Salt-Mediated Reduction of Hippocampal Amyloid-Beta in the Hyperphosphorylation of Tau
Gardner, L. (2016)
Investigating the contribution of astrocytes and neuroinflammation to pathological tau changes in Alzheimer's disease
Phillips, E. C. (2017) · Research Portal (King's College London)
Molecular Aspects of Concussion and Chronic Traumatic Encephalopathy
Farooqui, A. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813596-9.00008-0
Rola białek motorycznych w transporcie aksonalnym
Kliszcz, B., & Kasprzak, A. A. (2018) · Kosmos · doi:10.36921/kos.2018_2371
Development of imaging-based diagnostic procedures for brain protein aging using a mouse model of tauopathy
Sahara, N. (2018) · Folia Pharmacologica Japonica · doi:10.1254/fpj.152.4
Análise de biomarcadores e déficit comportamental associados à doença de Alzheimer em um modelo animal de predisposição genética à epilepsia
Vasconcelos, I. C. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2018.tde-17042018-155058
ANALYSIS OF ATP-DEPENDENT CHAPERONE PROTEIN INTERACTIONS WITH MISFOLDED PROTEINS, AMYLOIDS, AND AGGREGATED PROTEINS
May, S. E. (2018) · Digital Commons - URI (University of Rhode Island) · doi:10.23860/diss-may-shannon-2018
Repetitive Mild Traumatic Brain Injury Increases APP and Phospho Tau within the Hippocampus of a Novel APP/Tau Mouse Model of Alzheimer’s Disease
Coschigano, N. (2019) · doi:10.13021/mars/5249
Role of Copy-Number Variations in Non-Coding Regions of Autism Spectrum Disorders
Wang, J. (2017) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
Tau proteolysis mechanisms and relevance for tauopathies
Quinn, J. P. (2019) · Research Explorer (The University of Manchester)
The Metabolic Relationship between Type 2 Diabetes and Alzheimer's Disease
Ayala, D. (2019) · UA Campus Repository (The University of Arizona)
Sustained Interleukin-1β overexpression exacerbates Tau pathology in a murine tauopathy model via cyclooxygenase-1Preprint
Ghosh, S., Shaftel, S. S., Kyrkanides, S., Olschowka, J. A., & O’Banion, M. K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.10.430570
Biomarkers of Parkinson’s Disease
Fang, F., Stewart, T., & Zhang, J. (2015) · Biomarkers in disease · doi:10.1007/978-94-007-7696-8_17
Tau peptide signals are seen in Parkinson subjects by Broderick Probe® sensors
Broderick, P. A. (2021) · MOJ Clinical & Medical Case Reports · doi:10.15406/mojcr.2021.11.00380
Development of electrochemical immunosensors for detection of Tau protein : computational and experimental studies
Harilal, C. C. (2019) · DUT Open Scholar (Durban University of Technology) · doi:10.51415/10321/3608

Authors: Noble, W., Hanger, D. P., Miller, C. C. J., & Lovestone, S.
Affiliations: King's College London (GB)
Corresponding author: Noble, Wendy
Lovestone, Simon
ORCID: Noble, Wendy
Hanger, Diane P.
Miller, Christopher C. J.
Lovestone, Simon
Venue: Frontiers in Neurology
Publisher: Frontiers Media SA
Published: 2013
Volume: 4
Pages: 83-83
ISSN: 1664-2295 (ISSN-L)
DOI: 10.3389/fneur.2013.00083
PMC: PMC3696910
OpenAlex: W2011634611
Cited by: 475
References: 169
Citations by year: 2026: 27 · 2025: 51 · 2024: 56 · 2023: 58 · 2022: 56 · 2021: 56 · 2020: 35 · 2019: 24 · 2018: 28 · 2017: 26 · 2016: 17 · 2015: 19 · 2014: 17 · 2013: 4
FWCI: 13.23
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Frontiers in Neurology (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Research Portal (King's College London) (submittedVersion)
Funders: Wellcome Trust
National Institute for Health and Care Research (NF-SI-0512-10053)
National Centre for the Replacement, Refinement and Reduction of Animals in Research (NC/K500343/1)
Directorate for Biological Sciences
Medical Research Council
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: tau phosphorylation, tauopathy, Alzheimer's disease, frontotemporal dementia, neurofibrillary tangles, soluble tau, trans-synaptic spread, extracellular tau, synaptic function, DNA stabilization, axonal transport, neurodegeneration, therapeutic target

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

The Importance of Tau Phosphorylation for Neurodegenerative Diseases

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks