TDP-43 is intercellularly transmitted across axon terminals

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TDP-43 differentially propagates to induce antero- and retrograde degeneration in the corticospinal circuits in mouse focal ALS models

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Using Tetracysteine-Tagged TDP-43 with a Biarsenical Dye To Monitor Real-Time Trafficking in a Cell Model of Amyotrophic Lateral Sclerosis

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Is LRP2 Involved in Leptin Transport over the Blood-Brain Barrier and Development of Obesity?

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The unique neuropathological vulnerability of the human brain to aging

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Tandem Detergent-Extraction and Immunoprecipitation of Proteinopathy (TDiP): Scalable Enrichment of ALS-Associated TDP-43 Aggregates

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Targeting amyotrophic lateral sclerosis by neutralizing seeding-competent TDP-43 in CSF

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The spectrum of behavioral disorders in amyotrophic lateral sclerosis: current view

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Targeting RACK1 to alleviate TDP-43 and FUS proteinopathy-mediated suppression of protein translation and neurodegeneration

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Present and future use of exosomes containing proteins and RNAs in neurodegenerative diseases for synaptic function regulation: A comprehensive review

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Prion-like Spreading of Disease in TDP-43 Proteinopathies

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Unveiling exosomal biomarkers in neurodegenerative diseases: LC-MS-based profiling

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Spreading of pathological TDP-43 along corticospinal tract axons induces ALS-like phenotypes in Atg5+/- mice

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Ubiquitin-like 3 as a new protein-sorting factor for small extracellular vesicles

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Divergent Histopathological Networks of Frontotemporal Degeneration Proteinopathy Subytpes

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Emerging perspectives of synaptic biomarkers in ALS and FTD

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Relationship Between Homodimeric Glucocorticoid Receptor and Transcriptional Regulation Assessed via an In Vitro Fluorescence Correlation Spectroscopy-Microwell System

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Conditioned Medium from Cells Overexpressing TDP-43 Alters the Metabolome of Recipient Cells

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Is there a glucose metabolic signature of spreading TDP-43 pathology in amyotrophic lateral sclerosis?

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Dominant Heterogeneity of Upper and Lower Motor Neuron Degeneration to Motor Manifestation of Involved Region in Amyotrophic Lateral Sclerosis

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De novo design of RNA-binding proteins with a prion-like domain related to ALS/FTD proteinopathies

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Neutral sphingomyelinase 2: A promising drug target for CNS disease

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The role of microglia in the prion-like transmission of protein aggregates in neurodegeneration

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<Original Article>TDP-43 in the skin of amyotrophic lateral sclerosis patients.

Abe, K., Ohkubo, T., & Yokota, T. (2017) · PubMed · doi:10.11480/jmds.640102 · Cited by 10

When sleep fails, brain clearance suffers: the role of glymphatic impairment in clinical neurology

la Herrán-Arita, A. K. D. (2025) · Acta Neurologica Belgica · doi:10.1007/s13760-025-02959-w · Cited by 11

Potential of Microfluidics and Lab-on-Chip Platforms to Improve Understanding of “prion-like” Protein Assembly and Behavior

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Deciphering the prion-like behavior of pathogenic protein aggregates in neurodegenerative diseases

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Big versus small: The impact of aggregate size in disease

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Neuronal-enriched small extracellular vesicles trigger a PD-L1-mediated broad suppression of T cells in Parkinson’s disease

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Computational Insights Into the Mechanism of EGCG's Binding and Inhibition of the TDP‐43 Aggregation

Meshram, V. D., Balaji, R., Saravanan, P., Subbamanda, Y., Deeksha, W., Bajpai, A., Joshi, H., Bhargava, A., & Patel, B. K. (2024) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14640 · Cited by 8

Neuron-Derived Extracellular Vesicles: Emerging Regulators in Central Nervous System Disease Progression

Liu, S., Feng, A., & Li, Z. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05010-4 · Cited by 8

Cytoplasmic RNA granules, ribostasis, and neurodegeneration

Benarroch, E. E. (2018) · Neurology · doi:10.1212/wnl.0000000000005172 · Cited by 8

Enhanced secretion of the amyotrophic lateral sclerosis ALS-associated misfolded TDP-43 mediated by the ER-ubiquitin specific peptidase USP19

Picard, F., Nonaka, T., Belotti, E., Osseni, A., Errazuriz-Cerda, E., Jost-Mousseau, C., Bernard, E., Conjard‐Duplany, A., Bohl, D., Hasegawa, M., et al. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05589-w · Cited by 7

Membrane Charge Drives the Aggregation of TDP-43 Pathological Fragments

Corucci, G., Vadukul, D. M., Paracini, N., Laux, V., Batchu, K. C., Aprile, F. A., & Pastore, A. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c00594 · Cited by 7

TDP-43 mutants with different aggregation properties exhibit distinct toxicity, axonal transport, and secretion for disease progression in a mouse ALS/FTLD model

Mori, H., Sato, T., Tsuboguchi, S., Takahashi, M., Nakamura, Y., Hoshina, K., Kato, T., Fujii, M., Onodera, O., & Ueno, M. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106988 · Cited by 7

TFEB overexpression alleviates autophagy-lysosomal deficits caused by progranulin insufficiency

Nader, W. O., Brown, K. S., Boyle, N. R., Kaplelach, A. K., Abdelaziz, S. M., Davis, S. E., Aljabi, Q., Hakim, A. R., Davidson, A. G., Vollmer, G. A., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-12268-0 · Cited by 8

Glymphatic dysfunction and neurodegeneration in ALS: Longitudinal insights from rNLS8 TDP-43 mice

Zamani, A., Walker, A. K., & Wright, D. K. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106832 · Cited by 6

TDP-43 Proteinopathies in ALS and FTLD: Mechanistic Insights and Therapeutic Approaches

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Searching for the cellular underpinnings of the selective vulnerability to tauopathic insults in Alzheimer’s disease

Torok, J., Maia, P. D., Anand, C., & Raj, A. (2025) · Communications Biology · doi:10.1038/s42003-025-07575-1 · Cited by 8

Extracellular Vesicles in Chronic Demyelinating Diseases: Prospects in Treatment and Diagnosis of Autoimmune Neurological Disorders

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Current Perspectives in Human Papillomavirus

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The Regulation of TDP-43 Structure and Phase Transitions: A Review

Liu, Y., Xiang, J., Gong, H., Yu, T., Gao, M., & Huang, Y. (2025) · The Protein Journal · doi:10.1007/s10930-025-10261-0 · Cited by 8

TDP-43 pathology is associated with divergent protein profiles in ALS brain and spinal cord

Feneberg, E., Thompson, A. G., Charles, P. D., Vendrell, I., Kessler, B. M., Fischer, R., Ansorge, O., Gray, E., Talbot, K., & Turner, M. R. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02084-y · Cited by 5

Inhibition of amyloid beta oligomer accumulation by NU-9: A unifying mechanism for the treatment of neurodegenerative diseases

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Exosomal Transport and Progression of Neurodegeneration in Amyotrophic Lateral Sclerosis

Mv, I., Олеговна, Ч. Е., Belugin, B. V., Тутыхина, И. Л., Dolzhikova, I. V., Владимировна, З. И., Васильев, А. В., & Zakharova, M. N. (2019) · Neurochemical Journal · doi:10.1134/s1819712419030085 · Cited by 5

Roles of glia-derived extracellular vesicles in central nervous system diseases: an update

Sun, H., Su, X., Li, S., Mu, D., & Qu, Y. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2020-0144 · Cited by 5

Electrostatics Choreographs the Aggregation Dynamics of Full-Length TDP-43 via a Monomeric Amyloid Precursor

Doke, A. A., & Jha, S. K. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00060 · Cited by 5

The promise and challenges of extracellular vesicles in the diagnosis of neurodegenerative diseases

Hagey, D. W., & Andaloussi, S. E. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-85555-6.00014-x · Cited by 5

Somatic gene mutations in the motor cortex of patients with sporadic amyotrophic lateral sclerosis

González-Velasco, Ó., Parlato, R., Yilmaz, R., Decker, L., Menge, S., Freischmidt, A., Yang, X., Tulasi, N., Brenner, D., Andersen, P. M., et al. (2025) · Brain · doi:10.1093/brain/awaf460 · Cited by 5

Brain-derived extracellular vesicles potentially mediate crosstalk with peripheral organs in neurodegenerative diseases

Hamdalla, R. H., Bhaskar, V. B., & Tian, C. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1710150 · Cited by 5

Attenuation of amyotrophic lateral sclerosis via stem cell and extracellular vesicle therapy: An updated review

Lockard, G., Gordon, J., Schimmel, S. J., Sayed, B. E., Monsour, M., Garbuzova-Davis, S. N., & Borlongan, C. V. (2023) · Neuroprotection/Neuroprotection (Chichester, England. Print) · doi:10.1002/nep3.26 · Cited by 4

Role of Triggers on the Structural and Functional Facets of TAR DNA-binding Protein 43

Camilus, N. S., Arias, C. Q., & Martić, S. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.11.027 · Cited by 4

Role of Extracellular Vesicles in Human Papillomavirus-Induced Tumorigenesis

Mangino, G., Chiantore, M. V., Iuliano, M., Capriotti, L., Accardi, L., Bonito, P. D., Fiorucci, G., & Romeo, G. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.80654 · Cited by 4

Protein Aggregation in Amyotrophic Lateral Sclerosis

Chisholm, C. G., Yerbury, J. J., & McAlary, L. (2021) · Wiley eBooks · doi:10.1002/9781119745532.ch6 · Cited by 5

Synapse loss in the prefrontal cortex is associated with cognitive decline in amyotrophic lateral sclerosis

Henstridge, C. M., & Spires‐Jones, T. L. (2018) · doi:10.26226/morressier.5b31ec442afeeb001345a7e4 · Cited by 4

Exploring Protein Misfolding in Amyotrophic Lateral Sclerosis: Structural and Functional Insights

Ivantsik, O., Exarchos, T. P., Vrahatis, A. G., Vlamos, P., & Krokidis, M. G. (2025) · Biomedicines · doi:10.3390/biomedicines13051146 · Cited by 3

Applying available knowledge and resources to alleviate familial and sporadic neurodegenerative disorders

Mattson, M. P. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.09.001 · Cited by 3

Testing Amyloid Cross-Toxicity in the Vertebrate Brain

Henrı́quez, G., Méndez, L., Schmid, A. N., Guerrero, E. D., Collins, S. A., Castañeda, E., & Narayan, M. (2020) · ACS Omega · doi:10.1021/acsomega.0c01819 · Cited by 3

How network-based approaches can complement gene identification studies in frontotemporal dementia

Koçoğlu, C., Broeckhoven, C. V., & van der Zee, J. (2022) · Trends in Genetics · doi:10.1016/j.tig.2022.05.005 · Cited by 3

Prion-Like Propagation in Neurodegenerative Diseases

Peelaerts, W., Baekelandt, V., & Brundin, P. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00008-0 · Cited by 3

Which TDP-43 aggregates are toxic in ALS?

Valle, C., & Carrì, M. T. (2016) · Oncotarget · doi:10.18632/oncotarget.13461 · Cited by 4

Stress induced TDP-43 mobility loss independent of stress granulesPreprint

Streit, L. M., Kuhn, T., Vomhof, T., Ludolph, A. C., Weishaupt, J. H., Gebhardt, J. C. M., Michaelis, J., & Danzer, K. M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.28.482242 · Cited by 3

Herpes simplex virus infection promotes ALS pathology through ICP0-mediated PML body disruptionPreprint

Freisem, D., Rombach, D., Brockmann, S. J., Fink, A., Engels, Z., Luna, A. D., Acharya, D., Hoenigsperger, H., Goreth, A., Tigges, S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.27.714707 · Cited by 4

Identification of a Hidden, Highly Aggregation-Prone Intermediate of Full-Length TDP-43 That Triggers its Misfolding and Amyloid Aggregation

Doke, A. A., & Jha, S. K. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00389 · Cited by 2

Novel subcellular regulatory mechanisms of protein homeostasis and its implications in amyotrophic lateral sclerosis

Zhan, A., Zhong, K., & Zhang, K. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151582 · Cited by 2

Modeling amyotrophic lateral sclerosis (ALS) in vitro : from mechanistic studies to translatable drug discovery

Maskell, K. G., Cook, A. L., King, A. E., Dickson, T. C., & Blizzard, C. L. (2026) · Lab on a Chip · doi:10.1039/d5lc00577a · Cited by 2

Autophagy–exosome crosstalk in neurodegeneration: Mechanisms and therapeutic opportunities

Sedighi, S., Guan, T., Michetti, F., Cordani, M., Behrooz, A. B., Sabouni, F., Eshraghi, M., Saleem, A., Ghavami, S., & Aghanoori, M. (2026) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2026.109025 · Cited by 3

Übergreifende Konzepte der Neurodegeneration

Becktepe, J. S., Gövert, F., & Deuschl, G. (2017) · Aktuelle Neurologie · doi:10.1055/s-0042-123500 · Cited by 2

Preclinical Model to Evaluate Outcomes of Amyloid Cross-Toxicity in the Rodent Brain

Henrı́quez, G., Méndez, L., Castañeda, E., Wagler, A. E., Jeon, S., & Narayan, M. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00419 · Cited by 2

The Role of Extracellular Vesicles in the Progression of ALS and Their Potential as Biomarkers and Therapeutic Agents with Which to Combat the Disease

Chun, C., Smith, A. S. T., Bothwell, M. A., & Mack, D. L. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.91388 · Cited by 2

In silico and in vitro studies suggest epigallocatechin gallate (EGCG), a polyphenol in green tea, can bind and modulate the aggregation and cytotoxicity of the full-length TDP-43 protein implicated in TDP-43 proteinopathiesPreprint

Meshram, V. D., Balaji, R., Saravanan, P., Subbamanda, Y., Deeksha, W., Bajpai, A., Joshi, H., Bhargava, A., & Patel, B. K. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.22.573011 · Cited by 2

The infectious potential of protein misfolding: insights from cross-over studies of prion diseases and common neurodegenerative disorders

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Amyloidogenic oligomers derived from TDP-43 LCD promote the condensation and phosphorylation of TDP-43

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Co‐localization of tau and TDP ‐43 after extracellular vesicle delivery to cells

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TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain

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Regenerative strategies for ALS: stem cells and extracellular vesicles

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Retromer deficiency in amyotrophic lateral sclerosis

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Neuron-derived exosomes trigger a PD-L1-mediated broad suppression of T cells in Parkinson’s diseasePreprint

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Direct binding of TDP-43 and Tau drives their co-condensation, but suppresses Tau fibril formation and seedingPreprint

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Using Bioengineering Approaches to Generate a Three-Dimensional (3D) Human Pluripotent Stem Cell (hPSC)-Based Model for Neurodegenerative Diseases

Petty, F. J. (2016)

Development of a cellular model for C9ORF72-related Amyotrophic Lateral Sclerosis

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Elucidating the effect of aggregated SOD1 on microglia and astrocytes in ALS

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Breitet sich die sporadisch auftretende amyotrophe Lateralsklerose über axonale Verbindungen aus?

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Basal Forebrain Deep Brain Stimulation Impacts the Regulation of Extracellular Vesicle Related Proteins in the Rat BrainPreprint

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Investigation of the intercellular transmission of α-synuclein, amyloid-β and TDP-43

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Neuropathologie de la sclérose latérale amyotrophique sporadique

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Motoneuronerkrankungen

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TDP-43: A Key of Neurodegenerative Disease

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Cellular underpinnings of the selective vulnerability to tauopathic insults in Alzheimer’s diseasePreprint

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Somatic mutations in ALS genes in the motor cortex of sporadic ALS patientsPreprint

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Reappraisal of the anatomical spreading and propagation hypothesis about TDP‐43 aggregation in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

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Prion-like mechanisms of TDP-43 in ALS

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TDP-43 Is Efficiently Transferred Between Neuron-Like Cells in a Manner Enhanced by Preservation of Its N-Terminus but Independent of Extracellular Vesicles

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The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis

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The effects of clusterin on the aggregation and pathogenicity of TDP-43, a protein implicated in amyotrophic lateral sclerosis

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