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Mechanisms of Heparin-Induced Tau Aggregation Revealed by a Single Nanopore

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To target Tau pathologies, we must embrace and reconstruct their complexities

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C1 Inhibits Liquid–Liquid Phase Separation and Oligomerization of Tau and Protects Neuroblastoma Cells against Toxic Tau Oligomers

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Critical Molecular and Cellular Contributors to Tau Pathology

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Alzheimer’s disease seeded tau forms paired helical filaments yet lacks seeding potential

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Heparin remodels the microtubule-binding repeat R3 of Tau protein towards fibril-prone conformations

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Programmable DNA Nanodevices for Applications in Neuroscience

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Polysaccharides: potential bioactive macromolecules for Alzheimer’s disease

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Key Physicochemical and Biological Factors of the Phase Behavior of Tau

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Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP

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Intrinsically disordered proteins (IDPs) studied by EPR and in-cell EPR

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NMR Studies of Tau Protein in Tauopathies

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Molecular Dynamics Simulations of the Tau Amyloid Fibril Core Dimer at the Surface of a Lipid Bilayer Model: I. In Alzheimer’s Disease

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Targeting the Intrinsically Disordered Proteome Using Small-Molecule Ligands

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Water-directed pinning is key to tau prion formation

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In vitro Tau Aggregation Inducer Molecules Influence the Effects of MAPT Mutations on Aggregation Dynamics

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MAP2 caps tau fibrils and inhibits aggregation

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Detecting the Undetectable: Advances in Methods for Identifying Small Tau Aggregates in Neurodegenerative Diseases

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Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau protein

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Quantitative Assays for Catalytic Photo-Oxygenation of Alzheimer Disease-Related Tau Proteins

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An amphiphilic material arginine–arginine–bile acid promotes α-synuclein amyloid formation

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Direct Observation of the Self‐Aggregation of R3R4 Bi‐repeat of Tau Protein

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Pathogenic MAPT mutations Q336H and Q336R have isoform‐dependent differences in aggregation propensity and microtubule dysfunction

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Short-chain polyphosphates induce tau fibrillation and neurotoxicity in human iPSC-derived retinal neurons

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Specific Peptide from the Novel W-Tau Isoform Inhibits Tau and Amyloid β Peptide Aggregation In Vitro

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Drug Discovery and Screening Tool Development for Tauopathies by Focusing on Pathogenic Tau Repeat 3 Oligomers

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Fungally Derived Isoquinoline Demonstrates Inducer-Specific Tau Aggregation Inhibition

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An Additive-Free Model for Tau Self-Assembly

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Making tau amyloid models in vitro: a crucial and underestimated challenge

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Optical signature of retinal Tau fibrillation

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Effective Reduction of Tau Amyloid Aggregates in the Presence of Cyclophilin from Platanus orientalis Pollens; An Alternative Mechanism of Action of the Allergen

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Design and application of a Tau seed amplification assay for screening inhibitors of Tau seeding

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Illuminating the Structural Basis of Tau Aggregation by Intramolecular Distance Tracking: A Perspective on Methods

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α‐Synuclein Drives Tau's Cytotoxic Aggregates Formation through Hydrophobic Interactions

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Shapeshifting tau: from intrinsically disordered to paired-helical filaments

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Tau Inclusions in Alzheimer's, Chronic Traumatic Encephalopathy and Pick's Disease. A Speculation on How Differences in Backbone Polarization Underlie Divergent Pathways of Tau Aggregation

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Passaging Human Tauopathy Patient Samples in Cells Generates Heterogeneous Fibrils with a Subpopulation Adopting Disease FoldsPreprint

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Inhibiting Disulfide Bonding in Truncated Tau297–391 Results in Enhanced Self-Assembly of Tau into Seed-Competent Assemblies

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Extension of the SUGRES-1P Coarse-Grained Model of Polysaccharides to Heparin

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The impact of caffeine on tau-tau interaction: LSPR detection, structural modification and molecular dynamics simulation

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Conformation pattern changes in R1-pS262 tau peptide induced endogenous tau aggregation, synaptic damage, and cognitive impairments

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Biophysical Studies of Amyloid-Binding Fluorophores to Tau AD Core Fibrils Formed without Cofactors

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Effect of PHF-1 hyperphosphorylation on the seeding activity of C-terminal Tau fragments

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Polyamine and tau: a chemical framework for understanding the hyperphosphorylated tau condensation

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Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP

Parolini, F., Kachoie, E. A., Leo, G., Civiero, L., Bubacco, L., Arrigoni, G., Munari, F., Assfalg, M., D’Onofrio, M., & Capaldi, S. (2023) · Angewandte Chemie · doi:10.1002/ange.202310230 · Cited by 1 · see citing works

Drug Discovery and Screening Tool Development for Tauopathies by Focusing on Pathogenic Tau Repeat 3 Oligomers

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Protein shapes at the core of chronic traumatic encephalopathy

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Alzheimer's disease neurotoxic peptides : towards a comprehension of their modes of action on model membranes.

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The molecular mechanism of Hsp90-induced oligomerization of TauPreprint

Weickert, S., Wawrzyniuk, M., John, L., Rüdiger, S., & Drescher, M. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/614289

Mechanistic Insight into Tau Fibril Cross-Seeding Barriers: Structural Order and Disorder

Weismiller, H. A. (2019) · Digital Commons - DU (University of Denver)

Additional file 12 of Impact of APOE genotype on prion-type propagation of tauopathy

Williams, T., Ruiz, A. J., Ruiz, A. M., Vo, Q., Tsering, W., Xu, G., McFarland, K., Giasson, B. I., Sullivan, P. M., Borchelt, D. R., et al. (2022) · Figshare · doi:10.6084/m9.figshare.19619142

Study of the Neuron-Astrocyte Relationship in a Rodent Model of Tauopathy

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Caractérisation d'anticorps à domaine unique dirigés contre la protéine Tau

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

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Study of 3-O-sulfated heparan sulfates on tauopathy development in AD : neuropathologic and cellular approach

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Full-length Tau disrupts fluid zwitterionic supported lipid bilayers

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From Food Additives to Neurodegeneration: The Emerging Role of Polyphosphates in Tauopathies

Barolo, L., Farina, M. V., Cimaglia, G., Gigante, Y., Mirone, A., Mautone, L., Boffi, A., Angelantonio, S. D., & Baiocco, P. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00915

Phosphorylation of S396 and S400 Promotes Tau Self-Assembly and Favors the Chronic Traumatic Encephalopathy (CTE) Protofilament FoldPreprint

Powell, W. C., Yan, N., Tse, E., Melo, A. A., Sin, N., Southworth, D. R., & Gestwicki, J. E. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.19.726321

Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control

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Protocol for efficient purification of endotoxin-free human recombinant tau protein

Karabova, M. K., del Ser‐Badia, A., James, W., & Cowley, S. A. (2026) · STAR Protocols · doi:10.1016/j.xpro.2026.104800

Early Hetero-Oligomerization of Tau Fragments Redirects Cofactor-Free Tau Assembly and Fibril Morphology

Safoah, H. A., Hirschbeck, S. S., Chen, J., Domingo, N., Sogolovsky-Bard, I., Sams, A., Harish, A., Melkonian, M. J., Cantrell, K. L., Bar‐Yosef, D. L., et al. (2026) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6c05345

P4‐146: NOVEL HEPARINOIDS TO STUDY TAU AGGREGATION

Nadji, S., Dahr, R., Darvish, E., & Ren, Y. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.06.3807

Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases

Zhang, W., Falcon, B., Murzin, A. G., Fan, J., Crowther, R. A., Goedert, M., & Scheres, S. H. W. (2019) · eLife · doi:10.7554/elife.43584 · Cited by 500 · see citing works

Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

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Conformational Features of Tau Fibrils from Alzheimer’s Disease Brain Are Faithfully Propagated by Unmodified Recombinant Protein

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Aggregation Kinetics and Filament Structure of a Tau Fragment Are Influenced by the Sulfation Pattern of the Cofactor Heparin

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