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Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation

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Transmission and spreading of tauopathy in transgenic mouse brain

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Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease

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Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

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Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein

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Propagation of Tau Pathology in a Model of Early Alzheimer's Disease

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First-in-Rat Study of Human Alzheimer’s Disease Tau Propagation

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Emerging Developments in Targeting Proteotoxicity in Neurodegenerative Diseases

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Extracellular vesicles drive tau spreading in Alzheimer's disease

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Multifaceted Roles of Aquaporins in the Pathogenesis of Alzheimer’s Disease

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Sequence-dependent Internalization of Aggregating Peptides

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Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds

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The Pseudomonas aeruginosa Exoenzyme Y: A Promiscuous Nucleotidyl Cyclase Edema Factor and Virulence Determinant

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Mechanistic and Structural Origins of the Asymmetric Barrier to Prion-like Cross-Seeding between Tau-3R and Tau-4R

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Water-directed pinning is key to tau prion formation

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The Major Hypotheses of Alzheimer’s Disease: Related Nanotechnology-Based Approaches for Its Diagnosis and Treatment

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Tau Immunotherapy and Imaging

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Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease

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Diazaspirononane Nonsaccharide Inhibitors of O-GlcNAcase (OGA) for the Treatment of Neurodegenerative Disorders

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Recent advances in cellular biosensor technology to investigate tau oligomerization

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Spreading of Alzheimer tau seeds is enhanced by aging and template matching with limited impact of amyloid-β

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Nanotechnology for tau pathology in Alzheimer's disease

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Chronic Traumatic Encephalopathy: The cellular sequela to repetitive brain injury

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Elucidating Critical Proteinopathic Mechanisms and Potential Drug Targets in Neurodegeneration

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Targeting Tau to Treat Clinical Features of Huntington's Disease

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Recent Tau-Targeted Clinical Strategies for the Treatment of Alzheimer's Disease

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Paired Helical Filament-Forming Region of Tau (297–391) Influences Endogenous Tau Protein and Accumulates in Acidic Compartments in Human Neuronal Cells

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Detecting tau in serum of transgenic animal models after tau immunotherapy treatment

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Preclinical, phase I, and phase II investigational clinical trials for treatment of progressive supranuclear palsy

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Novel antibody against low‐n oligomers of tau protein promotes clearance of tau in cells via lysosomes

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Tau Secretion

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Cellular Models for the Study of PrionsPreprint

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A common antigenic motif recognized by naturally occurring human VH5–51/VL4–1 anti-tau antibodies with distinct functionalities

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Expression of Concern: High specificity of widely used phospho‐tau antibodies validated using a quantitative whole‐cell based assay

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Controlled and Selective Photo-oxidation of Amyloid-β Fibrils by Oligomeric p -Phenylene Ethynylenes

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Highly Specific and Sensitive Target Binding by the Humanized pS396-Tau Antibody hC10.2 Across a Wide Spectrum of Alzheimer’s Disease and Primary Tauopathy Postmortem Brains

Helboe, L., Rosenqvist, N., Volbracht, C., Pedersen, L. Ø., Pedersen, J. T., Christensen, S., Egebjerg, J., Christoffersen, C. T., Bang‐Andersen, B., Beach, T. G., et al. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220125 · Cited by 20

Harnessing the Immune System for Treatment and Detection of Tau Pathology

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α‐synuclein abnormalities trigger focal tau pathology, spreading to various brain areas in Parkinson disease

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Harnessing the immune system for the treatment of Parkinson’s disease

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Perspectives on the Tertiary Prevention Strategy for Alzheimer's Disease

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Populations of Tau Conformers Drive Prion-like Strain Effects in Alzheimer’s Disease and Related Dementias

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CSF Biomarkers of Alzheimer’s Disease: Impact on Disease Concept, Diagnosis, and Clinical Trial Design

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Endogenous Tau Aggregates in Oligodendrocytes of rTg4510 Mice Induced by Human P301L Tau

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PrionsEx Vivo: What Cell Culture Models Tell Us about Infectious Proteins

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Plant-Based Inhibitors of Protein Aggregation

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Nasal Rifampicin Halts the Progression of Tauopathy by Inhibiting Tau Oligomer Propagation in Alzheimer Brain Extract-Injected Mice

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Opportunities and Challenges for Molecular Chaperone Modulation to Treat Protein-Conformational Brain Diseases

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Glyceraldehyde 3‐phosphate dehydrogenase augments the intercellular transmission and toxicity of polyglutamine aggregates in a cell model of Huntington disease

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Secretion of full-length Tau or Tau fragments in cell culture models. Propagation of Tau in vivo and in vitro

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Intercellular Transmission of a Synthetic Bacterial Cytotoxic Prion-Like Protein in Mammalian Cells

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Tau R2 and R3 are essential regions for tau aggregation, seeding and propagation

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HIV and FIV glycoproteins increase cellular tau pathology via cGMP-dependent kinase II activation

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Amyotrophic lateral sclerosis and organ donation: Is there risk of disease transmission?

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α-Synuclein aggregates inhibit ESCRT-III through sequestration and collateral degradation

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Tau antibody 77G7 targeting microtubule binding domain suppresses proteopathic tau to seed tau aggregation

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Aβ and Tau Prions Causing Alzheimer’s Disease

Condello, C., Merz, G. E., Aoyagi, A., DeGrado, W. F., & Prusiner, S. B. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2655-9_16 · Cited by 18

Untangling Tau: Molecular Insights into Neuroinflammation, Pathophysiology, and Emerging Immunotherapies

Davidson, R., Krider, R. I., Borsellino, P., Noorda, K., Alhwayek, G., & Vida, T. A. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45110553 · Cited by 17

Tau Fibril Formation in Cultured Cells Compatible with a Mouse Model of Tauopathy

Matsumoto, G., Matsumoto, K., Kimura, T., Suhara, T., Higuchi, M., Sahara, N., & Mori, N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051497 · Cited by 17

Microtubule-modulating Agents in the Fight Against Neurodegeneration: Will it ever Work?

Soliman, A., Bakota, L., & Brandt, R. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666211201101020 · Cited by 19

Potential fluid biomarkers for pathological brain changes in Alzheimer's disease: Implication for the screening of cognitive frailty

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Recent advances in immunotherapy targeting amyloid-beta and tauopathies in Alzheimer’s disease

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Novel repertoire of tau biosensors to monitor pathological tau transformation and seeding activity in living cells

Cecon, E., Oishi, A., Luka, M., Ndiaye‐Lobry, D., François, A., Lescuyer, M., Panayi, F., Dam, J., Machado, P., & Jockers, R. (2023) · eLife · doi:10.7554/elife.78360 · Cited by 17

Influence of Tau on Neurotoxicity and Cerebral Vasculature Impairment Associated with Alzheimer’s Disease

Rather, M. A., Khan, A., Jahan, S., Siddiqui, A. J., & Wang, L. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.05.042 · Cited by 18

Recent studies of atomic‐resolution structures of tau protein and structure‐based inhibitors

Zhu, L., & Qian, Z. (2021) · Quantitative Biology · doi:10.15302/j-qb-021-0271 · Cited by 16

Clinical and biological phenotypes of frontotemporal dementia: Perspectives for disease modifying therapies

Gazzina, S., Manes, M. A., Padovani, A., & Borroni, B. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.05.056 · Cited by 21

The use of mouse models to study cell-to-cell transmission of pathological tau

Narasimhan, S., & Lee, V. M. ‐. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.009 · Cited by 16

Immunotherapeutic approaches for Alzheimer’s disease: Exploring active and passive vaccine progress

Bhadane, P., Roul, K., Belemkar, S., & Kumar, D. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149018 · Cited by 15

Understanding Biomarkers of Neurodegeneration: Novel approaches to detecting tau pathology

Cook, C. N., Murray, M. E., & Petrucelli, L. (2015) · Nature Medicine · doi:10.1038/nm.3809 · Cited by 15

Intracellular tau fragment droplets serve as seeds for tau fibrils

Soeda, Y., Yoshimura, H., Bannai, H., Koike, R., Shiiba, I., & Takashima, A. (2024) · Structure · doi:10.1016/j.str.2024.06.018 · Cited by 15

Spreading of Pathology in Alzheimer’s Disease

Lv, Z., Tan, C., Yu, J., & Tan, L. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9765-2 · Cited by 15

GAPDH-targeted therapy – A new approach for secondary damage after traumatic brain injury on rats

Lazarev, V. F., Dutysheva, E. A., Komarova, E. Y., Mikhaylova, E. R., Guzhova, I. V., & Margulis, B. A. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.05.099 · Cited by 15

C. elegans Models to Study the Propagation of Prions and Prion-Like Proteins

Sandhof, C. A., Hoppe, S. O., Tittelmeier, J., & Nussbaum-Krammer, C. I. (2020) · Biomolecules · doi:10.3390/biom10081188 · Cited by 15

Internalization of the Extracellular Full-Length Tau Inside Neuro2A and Cortical Cells Is Enhanced by Phosphorylation

Wauters, M., Wattiez, R., & Ris, L. (2016) · Biomolecules · doi:10.3390/biom6030036 · Cited by 15

Novel Cell Model for Tauopathy Induced by a Cell-Permeable Tau-Related Peptide

Veloria, J. R., Li, L., Breen, G. A. M., & Goux, W. J. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00275 · Cited by 16

Cathepsin-dependent amyloid formation drives mechanical rupture of lysosomal membranesPreprint

Li, D., Zhang, W., Medina, M., Stuke, J. F. M., Schwarz, A., Brill, J., Brenner, J., Kraus, F., Ohlerich, S., Lizarrondo, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.17.700056 · Cited by 15

Immunization targeting diseased proteins in synucleinopathy and tauopathy: insights from clinical trials

Zhan, X., Wen, G., Wu, X., & Li, J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00490-9 · Cited by 14

Quantitative live cell imaging of a tauopathy model enables the identification of a polypharmacological drug candidate that restores physiological microtubule interaction

Pinzi, L., Conze, C., Bisi, N., Torre, G. D., Soliman, A., Monteiro-Abreu, N., Trushina, N. I., Krusenbaum, A., Dolouei, M. K., Hellwig, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45851-6 · Cited by 17

Electrochemical detection of anti-tau antibodies binding to tau protein and inhibition of GSK-3β-catalyzed phosphorylation

Esteves-Villanueva, J. O., & Martić, S. (2015) · Analytical Biochemistry · doi:10.1016/j.ab.2015.12.002 · Cited by 14

Disease-modifying strategies in primary tauopathies

Rösler, T. W., Costa, M., & Höglinger, G. U. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107842 · Cited by 16

Cell-free amplification of prions: Where do we stand?

Cazzaniga, F. A., Luca, C. M. G. D., Bistaffa, E., Consonni, A., Legname, G., Giaccone, G., & Moda, F. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.005 · Cited by 14

Tau in the gut, does it really matter?

Derkinderen, P., Rolli‐Derkinderen, M., Chapelet, G., Neunlist, M., & Noble, W. J. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15320 · Cited by 16

Protein disulfide isomerases as CSF biomarkers for the neuronal response to tau pathology

Wolzak, K., Vermunt, L., del Campo, M., Jorge‐Oliva, M., van Ziel, A. M., Li, K. W., Smit, A. B., Chen‐Ploktkin, A., Irwin, D. J., Lemstra, A. W., et al. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.12978 · Cited by 14

Advanced imaging of tau pathology in Alzheimer Disease: New perspectives from super resolution microscopy and label‐free nanoscopy

Schierle, G. S. K., Michel, C. H., & Gasparini, L. (2016) · Microscopy Research and Technique · doi:10.1002/jemt.22698 · Cited by 14

Capacity for Seeding and Spreading of Argyrophilic Grain Disease in a Wild-Type Murine Model; Comparisons With Primary Age-Related Tauopathy

Ferrer, I., Andrés‐Benito, P., Sala‐Jarque, J., Gil, V., & del Rı́o, J. A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00101 · Cited by 14

The role of wild-type tau in Alzheimer’s disease and related tauopathies

Lo, C. H., & Sachs, J. N. (2020) · JoLS Journal of Life Sciences · doi:10.36069/jols/20201201 · Cited by 15

Partial Destabilization of Amyloid-β Protofibril by Methionine Photo-Oxidation: A Molecular Dynamic Simulation Study

Maghsoodi, F., Martin, T. D., & Chi, E. Y. (2023) · ACS Omega · doi:10.1021/acsomega.2c07468 · Cited by 13

FGFR3 drives Aβ-induced tau uptake

Kim, D. K., Suh, K. Y., Park, J., Lee, S., Han, J., Chang, S., Kim, Y., & Mook‐Jung, I. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01274-3 · Cited by 14

Targeted proteolytic products of τ and α-synuclein in neurodegeneration

Xia, Y., Lloyd, G. M., & Giasson, B. I. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210028 · Cited by 13

Evaluation of ferritin and transferrin binding to tau protein

Jahshan, A., Esteves-Villanueva, J. O., & Martić, S. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.06.022 · Cited by 13

Intercellular propagation of RIPK1/RIPK3 amyloid fibrils

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Macrocyclic β-arch peptides that mimic the structure and function of disease-associated tau folds

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Accumulation of C-terminal cleaved tau is distinctly associated with cognitive deficits, synaptic plasticity impairment, and neurodegeneration in aged mice

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