C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy

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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS

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Unconventional Translation of C9ORF72 GGGGCC Expansion Generates Insoluble Polypeptides Specific to c9FTD/ALS

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The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.

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GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport

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Suppression of mutant C9orf72 expression by a potent mixed backbone antisense oligonucleotide

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Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates

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Higher-order organization of biomolecular condensates

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Axonal TDP-43 condensates drive neuromuscular junction disruption through inhibition of local synthesis of nuclear encoded mitochondrial proteins

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Mitochondrial bioenergetic deficits in C9orf72 amyotrophic lateral sclerosis motor neurons cause dysfunctional axonal homeostasis

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A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules

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Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions

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Nuclear pore complexes — a doorway to neural injury in neurodegeneration

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Biological importance of arginine: A comprehensive review of the roles in structure, disorder, and functionality of peptides and proteins

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C9orf72 -derived arginine-containing dipeptide repeats associate with axonal transport machinery and impede microtubule-based motility

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Cellular and physiological functions of C9ORF72 and implications for ALS/FTD

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Combating deleterious phase transitions in neurodegenerative disease

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Friend or foe: The role of stress granule in neurodegenerative disease

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Two FTD-ALS genes converge on the endosomal pathway to induce TDP-43 pathology and degeneration

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TDP-43 pathology: From noxious assembly to therapeutic removal

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The role of inflammation in neurodegeneration: novel insights into the role of the immune system in C9orf72 HRE-mediated ALS/FTD

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TDP-43 and Inflammation: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

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NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

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Emerging Perspectives on Dipeptide Repeat Proteins in C9ORF72 ALS/FTD

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Connecting TDP-43 Pathology with Neuropathy

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Spinal cord extracts of amyotrophic lateral sclerosis spread TDP-43 pathology in cerebral organoids

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Neuronal STING activation in amyotrophic lateral sclerosis and frontotemporal dementia

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Mitochondria, a Key Target in Amyotrophic Lateral Sclerosis Pathogenesis

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Principles and functions of condensate modifying drugs

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Traumatic injury compromises nucleocytoplasmic transport and leads to TDP-43 pathology

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Prion-Like Proteins in Phase Separation and Their Link to Disease

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Update on genetics of amyotrophic lateral sclerosis

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New developments of biofluid‐based biomarkers for routine diagnosis and disease trajectories in frontotemporal dementia

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Integrative genetic analysis illuminates ALS heritability and identifies risk genes

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Amyotrophic lateral sclerosis caused by hexanucleotide repeat expansions in C9orf72: from genetics to therapeutics

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DNA Double-Strand Breaks as Pathogenic Lesions in Neurological Disorders

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C9orf72 dipeptides disrupt the nucleocytoplasmic transport machinery and cause TDP-43 mislocalisation to the cytoplasm

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High-titer AAV disrupts cerebrovascular integrity and induces lymphocyte infiltration in adult mouse brain

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Nuclear import receptors are recruited by FG-nucleoporins to rescue hallmarks of TDP-43 proteinopathy

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Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises

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The Inflammatory Puzzle: Piecing together the Links between Neuroinflammation and Amyotrophic Lateral Sclerosis

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Proximity proteomics of C9orf72 dipeptide repeat proteins identifies molecular chaperones as modifiers of poly-GA aggregation

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PolyGR and polyPR knock-in mice reveal a conserved neuroprotective extracellular matrix signature in C9orf72 ALS/FTD neurons

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The mechanisms, hallmarks, and therapies for brain aging and age-related dementia

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Modelling amyotrophic lateral sclerosis in rodents

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Regulation of Biomolecular Condensates by Poly(ADP-ribose)

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Neuronal polyunsaturated fatty acids are protective in ALS/FTD

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Current perspectives in drug targeting intrinsically disordered proteins and biomolecular condensates

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Approaches to gene modulation therapy for ALS

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Current Concepts on Genetic Aspects of Mitochondrial Dysfunction in Amyotrophic Lateral Sclerosis

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Autophagy Dysfunction in ALS: from Transport to Protein Degradation

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Risk factors for cognitive impairment in amyotrophic lateral sclerosis: a systematic review and meta-analysis

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Mitochondria Dysfunction in Frontotemporal Dementia/Amyotrophic Lateral Sclerosis: Lessons From Drosophila Models

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Neuronal biomolecular condensates and their implications in neurodegenerative diseases

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Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD

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Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective Responses

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Proteostasis Perturbations and Their Roles in Causing Sterile Inflammation and Autoinflammatory Diseases

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SUMO2/3 conjugation of TDP-43 protects against aggregation

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Multiple pathways of toxicity induced by C9orf72 dipeptide repeat aggregates and G4C2 RNA in a cellular model

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Copper toxicity and deficiency: the vicious cycle at the core of protein aggregation in ALS

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Altered Phase Separation and Cellular Impact in C9orf72-Linked ALS/FTD

Solomon, D. A., Smikle, R., Reid, M. J., & Mizielinska, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.664151 · Cited by 33

Pathological phase transitions in ALS-FTD impair dynamic RNA–protein granules

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Poly(GR) interacts with key stress granule factors promoting its assembly into cytoplasmic inclusions

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Opposing roles of p38α-mediated phosphorylation and PRMT1-mediated arginine methylation in driving TDP-43 proteinopathy

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Aberrant Stress Granule Dynamics and Aggrephagy in ALS Pathogenesis

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Loss of C9orf72 perturbs the Ran-GTPase gradient and nucleocytoplasmic transport, generating compositionally diverse Importin β-1 granules

McGoldrick, P., Lau, A., You, Z., Durcan, T. M., & Robertson, J. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112134 · Cited by 29

Intercellular transmission of pathogenic proteins in ALS: Exploring the pathogenic wave

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TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: From pathomechanisms to therapeutic strategies

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Poly(ADP-ribose) promotes toxicity of C9ORF72 arginine-rich dipeptide repeat proteins

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Neurofilament accumulations in amyotrophic lateral sclerosis patients’ motor neurons impair axonal initial segment integrity

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Co-Aggregation of TDP-43 with Other Pathogenic Proteins and Their Co-Pathologies in Neurodegenerative Diseases

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Autoimmune response to C9orf72 protein in amyotrophic lateral sclerosis

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Updates on Disease Mechanisms and Therapeutics for Amyotrophic Lateral Sclerosis

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Brain–body mechanisms contribute to sexual dimorphism in amyotrophic lateral sclerosis

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A mouse model with widespread expression of the C9orf72-linked glycine–arginine dipeptide displays non-lethal ALS/FTD-like phenotypes

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Poly-GR repeats associated with ALS/FTD gene C9ORF72 impair translation elongation and induce a ribotoxic stress response in neurons

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Cerebrospinal fluid and blood neurofilament light chain in Parkinson's disease and atypical parkinsonian syndromes: a systematic review and Bayesian network meta-analysis

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Blocking RAN translation without altering repeat RNAs rescues C9ORF72 -related ALS and FTD phenotypes

Jiang, X., Schaeffer, L., Patni, D., Russo, T., Lee, C.-Z., Aguilar, C., Marques, C., Jansen‐West, K. R., Hruška-Plocháň, M., Ray-Soni, A., et al. (2026) · Science · doi:10.1126/science.adv2600 · Cited by 22

The porphyrin TMPyP4 inhibits elongation during the noncanonical translation of the FTLD/ALS-associated GGGGCC repeat in the C9orf72 gene

Mori, K., Gotoh, S., Yamashita, T., Uozumi, R., Kawabe, Y., Tagami, S., Kamp, F., Nuscher, B., Edbauer, D., Haass, C., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101120 · Cited by 23

Nuclear-Import Receptors Counter Deleterious Phase Transitions in Neurodegenerative Disease

Odeh, H. M., Fare, C. M., & Shorter, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167220 · Cited by 22

LSM12-EPAC1 defines a neuroprotective pathway that sustains the nucleocytoplasmic RAN gradient

Lee, J., Park, J., Kim, J.-H., Lee, G., Park, T., Yoon, K., Kim, Y. K., & Lim, C. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3001002 · Cited by 22

Multi-phaseted problems of TDP-43 in selective neuronal vulnerability in ALS

Asakawa, K., Handa, H., & Kawakami, K. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03792-z · Cited by 20

Frontotemporal Dementia and Glucose Metabolism

Garrett, L. R., & Niccoli, T. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.812222 · Cited by 20

Partners in crime: Proteins implicated in RNA repeat expansion diseases

Baud, A., Derbis, M., Tutak, K., & Sobczak, K. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1709 · Cited by 20

c-Jun N-Terminal Kinase Promotes Stress Granule Assembly and Neurodegeneration in C9orf72-Mediated ALS and FTD

Sahana, T. G., Chase, K. J., Liu, F., Lloyd, T. E., Rossoll, W., & Zhang, K. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1799-22.2023 · Cited by 21

Unraveling the impact of disrupted nucleocytoplasmic transport systems in C9orf72-associated ALS

McGoldrick, P., & Robertson, J. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1247297 · Cited by 22

Nuclear pore dysfunction and disease: a complex opportunity

Fare, C. M., & Rothstein, J. D. (2024) · Nucleus · doi:10.1080/19491034.2024.2314297 · Cited by 21

Random forest modelling demonstrates microglial and protein misfolding features to be key phenotypic markers in C9orf72 ‐ALS

Rifai, O. M., Longden, J., O’Shaughnessy, J., Sewell, M. D. E., Pate, J. A., McDade, K., Daniels, M. J. D., Abrahams, S., Chandran, S., McColl, B. W., et al. (2022) · The Journal of Pathology · doi:10.1002/path.6008 · Cited by 20

p53 Transactivation Domain Mediates Binding and Phase Separation with Poly-PR/GR

Usluer, S., Spreitzer, E., Bourgeois, B. M. R., & Madl, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111431 · Cited by 19

Enhanced motor cortex output and disinhibition in asymptomatic female mice with C9orf72 genetic expansion

Amalyan, S., Tamboli, S., Lazarevich, I. A., Topolnik, D., Bouman, L. H., & Topolnik, L. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111043 · Cited by 19

Graphene Quantum Dots Attenuate TDP-43 Proteinopathy in Amyotrophic Lateral Sclerosis

Park, N.-Y., Heo, Y., Yang, J. W., Yoo, J. M., Jang, H. J., Jo, J. H., Park, S. J., Lin, Y., Choi, J., Jeon, H., et al. (2025) · ACS Nano · doi:10.1021/acsnano.4c15283 · Cited by 20

Loss of PML nuclear bodies in familial amyotrophic lateral sclerosis-frontotemporal dementia

Antoniani, F., Cimino, M., Mediani, L., Vinet, J., Verde, E. M., Secco, V., Yamoah, A., Tripathi, P., Aronica, E., Cicardi, M. E., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01547-2 · Cited by 19

Large-scale network analysis of the cerebrospinal fluid proteome identifies molecular signatures of frontotemporal lobar degeneration

Saloner, R., Staffaroni, A. M., Dammer, E. B., Johnson, E. C. B., Paolillo, E. W., Wise, A. B., Heuer, H. W., Forsberg, L. K., Lario‐Lago, A., Webb, J. D., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00878-2 · Cited by 21

C9orf72 poly-PR forms anisotropic condensates causative of nuclear TDP-43 pathology

Hodgson, R. E., Rayment, J. A., Huang, W.-P., Avila, A. S., Ellis, B. C. S., Lin, Y.-H., Soni, N., Hautbergue, G. M., & Shelkovnikova, T. A. (2024) · iScience · doi:10.1016/j.isci.2024.110937 · Cited by 17

Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration

Copley, K. E., Mauna, J. C., Danielson, H. L., Chen, Q., Ozguney, B., Ngo, M., Xie, L., Smirnov, A., Davis, M., Mayne, L., et al. (2026) · Science · doi:10.1126/science.adv3301 · Cited by 16

Repeated mild traumatic brain injury triggers pathology in asymptomatic C9ORF72 transgenic mice

Kahriman, A., Bouley, J., Tuncali, I., Dogan, E. O., Pereira, M., Luu, T., Bosco, D. A., Jaber, S., Peters, O. M., Brown, R. H., et al. (2023) · Brain · doi:10.1093/brain/awad264 · Cited by 18

Single Acetylation-mimetic Mutation in TDP-43 Nuclear Localization Signal Disrupts Importin α1/β Signaling

Ko, Y., Lokareddy, R. K., Doll, S. G., Yeggoni, D. P., Girdhar, A., Mawn, I., Klim, J. R., Rizvi, N. F., Meyers, R. E., Gillilan, R. E., et al. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168751 · Cited by 16

C9orf72 poly(PR) aggregation in nucleus induces ALS/FTD-related neurodegeneration in cynomolgus monkeys

Xu, L., Wang, D., Zhao, L., Yang, Z., Liu, X., Li, X., Yuan, T., Wang, Y., Huang, T., Bian, N., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106197 · Cited by 16

Interaction-Dependent Secondary Structure of Peptides in Biomolecular Condensates

Lorenz-Ochoa, K. A., Cho, M., Parekh, S. H., & Baiz, C. R. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c11226 · Cited by 15

Blueprint of Collapse: Precision Biomarkers, Molecular Cascades, and the Engineered Decline of Fast-Progressing ALS

Șerban, M., Toader, C., & Covache-Busuioc, R.-A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26168072 · Cited by 17

RNA-binding protein dysfunction in neurodegeneration

Popper, B., Scheidt, T., & Schieweck, R. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210024 · Cited by 15

Gain-of-function ANXA11 mutation cause late-onset ALS with aberrant protein aggregation, neuroinflammation and autophagy impairment

Liu, Q. H., Sun, Y., He, B., Chen, H., Wang, L., Wang, G., Zhang, K., Zhao, X., Zhang, X., Shen, D., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01919-4 · Cited by 14

Repulsive vs Attractive Crowding Distinctly Regulate TDP-43 Condensates through Region-specific Structural Dynamics

Zhang, G., Feng, C., & Chu, X. (2025) · JACS Au · doi:10.1021/jacsau.5c00876 · Cited by 14

P4‐088: C9Orf72 Dipeptide Repeat Proteins Cause Intracellular Aggregation of Phosphorylated TDP‐43

Nonaka, T., & Hasegawa, M. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.06.2177

C9ORF72 dipeptide repeat poly-GA inclusions promote intracellular aggregation of phosphorylated TDP-43

Nonaka, T., Masuda‐Suzukake, M., Hosokawa, M., Shimozawa, A., Hirai, S., Okado, H., & Hasegawa, M. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy174 · Cited by 53

Modulating TDP-43 Protein Aggregation Directly and Indirectly in C. Elegans

Elshaalia, E. (2026) · Digital Commons - DU (University of Denver) · doi:10.56902/etdcrp.2026.150

C9ORF72 poly-GA inclusions promote phosphorylated TDP-43 aggregation in vitro and in vivo

Nonaka, T. (2018) · The Japanese Biochemical Society

Mitigation of TDP-43 toxic phenotype by an RGNEF fragment in amyotrophic lateral sclerosis models

Droppelmann, C. A., Campos‐Melo, D., Noches, V., McLellan, C., Szabla, R., Lyons, T. A., Amzil, H., Withers, B., Kaplanis, B., Sonkar, K. S., et al. (2024) · Brain · doi:10.1093/brain/awae078 · Cited by 15