Dynamic association of tau with neuronal membranes is regulated by phosphorylation

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

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Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

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GSK-3α regulates production of Alzheimer's disease amyloid-β peptides

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Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

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Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase

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Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease

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

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Mechanisms of tau-induced neurodegeneration

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Tau phosphorylation in neuronal cell function and dysfunction

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Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau

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Looking for novel functions of tau

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Single‐molecule imaging reveals Tau trapping at nanometer‐sized dynamic hot spots near the plasma membrane that persists after microtubule perturbation and cholesterol depletion

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Pseudo-Phosphorylated Tau Forms Paired Helical Filaments in the Presence of High-Curvature Cholesterol-Containing Lipid Membranes

Mammeri, N. E., Duan, P., & Hong, M. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c13772 · Cited by 16

Tau in the gut, does it really matter?

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Tau–Mitochondria Interactions in Neurodegeneration: Mechanisms and Therapeutic Potential

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Serine 31 Phosphorylation-Driven Regulation of AGPase Activity: Potential Implications for Enhanced Starch Yields in Crops

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Effect of focal mild hypothermia on expression of MMP-9, TIMP-1, Tau-1 and β-APP in rats with cerebral ischaemia/reperfusion injury

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Tau Protein and Zebrafish Models for Tau-Induced Neurodegeneration

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Interaction of full-length Tau with negatively charged lipid membranes leads to polymorphic aggregates

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Unknown roles of tau pathology in neurological disorders. Challenges and new perspectives

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Partial mimicry of the microtubule binding of tau by its membrane binding

MacAinsh, M., & Zhou, H. (2023) · Protein Science · doi:10.1002/pro.4581 · Cited by 12

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

Enriched odor exposure decrease tau phosphorylation in the rat hippocampus and cortex

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C-Reactive Protein Induces Tau Hyperphosphorylation via GSK3β Signaling Pathway in SH-SY5Y Cells

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The Implication of Glial Metabotropic Glutamate Receptors in Alzheimer’s Disease

de Lima, I. B. Q., & Ribeiro, F. M. (2021) · Current Neuropharmacology · doi:10.2174/1570159x20666211223140303 · Cited by 9

Amyloids on Membrane Interfaces: Implications for Neurodegeneration

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Anesthesia promotes acute expression of genes related to Alzheimer’s disease and latent tau aggregation in transgenic mouse models of tauopathy

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EGCG modulates nuclear formaldehyde-induced Tau phosphorylation in Neuronal cellsPreprint

Sonawane, S. K., Raina, A., Majumdar, A., & Chinnathambi, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.04.325134 · Cited by 7

Peptide-based inhibitors of Tau aggregation as a potential therapeutic for Alzheimer’s disease and other TauopathiesPreprint

Aggidis, A., Chatterjee, S., Townsend, D. J., Fullwood, N. J., Ortega, E. R., Tarutani, A., Hasegawa, M., Lucas, H., Mudher, A. K., & Allsop, D. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.04.447069 · Cited by 9

Effect of Phosphorylation Sites Mutations on the Subcellular Localization and Activity of AGPase Bt2 Subunit: Implications for Improved Starch Biosynthesis in Maize

Yu, G., Shoaib, N., Yang, Y., Liu, L., Mughal, N., Mou, Y., & Huang, Y. (2023) · Agronomy · doi:10.3390/agronomy13082119 · Cited by 6

Dale Schenk One Year Anniversary: Fighting to Preserve the Memories

Overk, C., & Masliah, E. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171071 · Cited by 5

"Phosphorylation of The Tau Protein in Neurodegenerative Disease"

Chen, K. (2020) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2020.26.004393 · Cited by 6

LRP1 and SORL1 regulate tau internalization and degradation and enhance tau seedingPreprint

Cooper, J. M., Lathuilière, A., Migliorini, M. M., Arai, A. L., Wani, M. M., Dujardin, S., Muratoglu, S. C., Hyman, B. T., & Strickland, D. K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.17.386581 · Cited by 6

The promising role of bioactive congeners present in Cassytha filiformis in Alzheimer's disease: An explicative review

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Central and peripheral tau retention modulated by an anti-tau antibodyPreprint

Solorzano, A. G., Brady, M., Bhatt, N. N., Johnson, A., Burgess, B., Leyva, H., Puangmalai, N., Jerez, C., Wood, R. W., Kayed, R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.17.553682 · Cited by 4

The emerging nontraditional roles for tau in the brain

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Distribution of spleen tyrosine kinase and tau phosphorylated at tyrosine 18 in a mouse model of tauopathy and in the human hippocampus

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Tau-Centric Therapies for Treating Alzheimer’s Disease

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Risk Factors for Alzheimer’s Disease

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The role of mTor in the pathogenesis of tau-related pathologies in Alzheimer Disease

Tang, Z. (2014) · Figshare

Functional implications of tau-fyn interactions in Alzheimer's disease

Lau, H. W. D. (2015)

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)

Assembly and Disassembly of Protein Aggregates

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00006-7

Neurochemical Aspects of β-Amyloid Cascade Hypothesis for Alzheimer’s Disease

Farooqui, A. A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809937-7.00001-x · Cited by 1

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)

Tau proteolysis mechanisms and relevance for tauopathies

Quinn, J. P. (2019) · Research Explorer (The University of Manchester)

Tau forms dynamic hot spots that are resistant to microtubule perturbations and cholesterol depletionPreprint

Padmanabhan, P., Kneynsberg, A., Cruz, E., Amor, R., Sibarita, J., & Götz, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.04.479198

Etude de la dynamique de tau dans le compartiment synaptique dans un contexte physiologique et pathologique exemple de la maladie d'Alzheimer

Frandemiche, M. (2013) · theses.fr (ABES) · doi:10.70675/260ed9c4zd958z47e0za418z0f324a1b102b

Additional file 1 of Anesthesia promotes acute expression of genes related to Alzheimer’s disease and latent tau aggregation in transgenic mouse models of tauopathy

Eun, J. D., Jimenez, H. T., Adrien, L. R., Wolin, A., Marambaud, P., Davies, P., & Koppel, J. L. (2022) · Figshare · doi:10.6084/m9.figshare.20347460

Extracellular Vesicles in Tauopathies: Mechanisms and Applications

Nannuri, V., Ababneh, E., Rayes, S. E., Smith, J., Sugaya, K., & Zhao, J. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27041998

L'alpha-tubuline B et ses régulateurs chez le champignon Botrytis cinerea : régulation, rôles et interactants

Talmey, Y. F. (2014) · theses.fr (ABES) · doi:10.70675/19614ee5zadd0z4838z930cz4ac6a7f7afc4

Les nanotubes comme nouvelle voie de transfert et de propagation de la protéine Tau pathologique

Tardivel, M. (2017) · theses.fr (ABES) · doi:10.70675/0cfcd049z970ez4f2dz8417z195cfabdc00d

Rôle de la neuroinflammation et du récepteur microglial TREM2 dans la progression de deux modèles de tauopathie

Vautheny, A. (2019) · theses.fr (ABES) · doi:10.70675/1812d71aze8d9z48d6z87d1z5a23a4e81953

Neurotoxicité précoce et mécanismes de neuroprotection dans des modèles poisson‐zèbre de tauopathies

Barbereau, C. (2020) · theses.fr (ABES) · doi:10.70675/dfe1802ez70f2z4da6zb3e5z63d1de7a429c

Identification et caractérisation fonctionnelle de nouveaux sites de clivage de la protéine Tau

Derisbourg, M. J. (2015) · theses.fr (ABES) · doi:10.70675/ef5f45b0zf4e8z433fz9beaz8d2cc6de65bc

Étude du rôle de la microglie dans la propagation de la protéine Tau : mise en place de nouveaux modèles

Duwat, C. (2021) · theses.fr (ABES) · doi:10.70675/b4d3f614ze4bdz4745zb73cz5c7e662402bb

Interaction entre la protéine Tau et la protéine p54nrb : effet sur la maturation des miARN au sein des paraspeckles

Denéchaud, M. (2022) · theses.fr (ABES) · doi:10.70675/623e7224z0cb0z47b1z8a22z549acf553ac0

Full-length Tau disrupts fluid zwitterionic supported lipid bilayers

Ury‐Thiery, V., Molinari, M., Lecomte, S., & Feuillie, C. (2026) · Biophysical Chemistry · doi:10.1016/j.bpc.2026.107626

BindingDB Entry 50002158: Development of dual casein kinase 1δ/1ε (CK1δ/ε) inhibitors for treatment of breast cancer.

BindingDB (2020) · UC San Diego · doi:10.7270/q2rr21tz

P1‐362: Dynamic association of tau with neuronal membranes is regulated by phosphorylation and the tyrosine kinase fyn

Pooler, A. M., Usardi, A., & Hanger, D. P. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.916

P3‐208: Phosphorylation‐dependent association of tau with the neuronal membrane

Pooler, A. M., & Hanger, D. P. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.04.981

Tau Dephosphorylation at Tau-1 Site Correlates with its Association to Cell Membrane

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Functional implications of the association of tau with the plasma membrane

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Phosphorylation of Tau Alters Its Association with the Plasma Membrane

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