C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS

DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936

A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD

Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409

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

Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732

Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

Elden, A. C., Kim, H.-J., Hart, M. P., Chen‐Plotkin, A. S., Johnson, B. S., Fang, X., Armakola, M., Geser, F., Greene, R. A., Lu, M. M., et al. (2010) · Nature · doi:10.1038/nature09320 · Cited by 1,361

Neurofilament light chain as a biomarker in neurological disorders

Gaetani, L., Blennow, K., Calabresi, P., Di Filippo, M., Parnetti, L., & Zetterberg, H. (2019) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2018-320106 · Cited by 1,334

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

Mori, K., Weng, S., Arzberger, T., May, S., Rentzsch, K., Kremmer, E., Schmid, B., Kretzschmar, H. A., Cruts, M., Broeckhoven, C. V., et al. (2013) · Science · doi:10.1126/science.1232927 · Cited by 1,248

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

Ash, P. E. A., Bieniek, K. F., Gendron, T. F., Caulfield, T. R., Lin, W.-L., DeJesus‐Hernandez, M., van Blitterswijk, M., Jansen‐West, K. R., Paul, J. W., Rademakers, R., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.004 · Cited by 1,127

The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.

Zhang, K., Donnelly, C. J., Haeusler, A. R., Grima, J. C., Machamer, J. B., Steinwald, P., Daley, E. L., Miller, S. J., Cunningham, K. M., Vidensky, S., et al. (2015) · Nature · doi:10.1038/nature14973 · Cited by 982

GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport

Freibaum, B. D., Lu, Y., Lopez-Gonzalez, R., Kim, N. C., Almeida, S., Lee, K.-H., Badders, N., Valentine, M., Miller, B. L., Wong, P. C., et al. (2015) · Nature · doi:10.1038/nature14974 · Cited by 841

Repeat‐Associated Non‐ AUG Translation of AGAGGG Repeats that Cause X ‐Linked Dystonia‐Parkinsonism

Reyes, C. J., Asano, K., Todd, P. K., Klein, C., & Raković, A. (2022) · Movement Disorders · doi:10.1002/mds.29183 · Cited by 14

Cytoplasmic TDP-43 accumulation drives changes in C-bouton number and size in a mouse model of sporadic Amyotrophic Lateral Sclerosis

Bak, A. N., Djukic, S., Kadlecová, M., Braunstein, T. H., Jensen, D. B., & Meehan, C. F. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103840 · Cited by 13

Hypothesis and Theory: Roles of Arginine Methylation in C9orf72-Mediated ALS and FTD

Gill, A. L., Premasiri, A. S., & Vieira, F. G. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.633668 · Cited by 12

eIF5 stimulates the CUG initiation of RAN translation of poly-GA dipeptide repeat protein (DPR) in C9orf72 FTLD/ALS

Gotoh, S., Mori, K., Fujino, Y., Kawabe, Y., Yamashita, T., Omi, T., Nagata, K., Tagami, S., Nagai, Y., & Ikeda, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105703 · Cited by 12

The role of long noncoding RNAs in amyotrophic lateral sclerosis

Rajabi, D., Khanmohammadi, S., & Rezaei, N. (2024) · Reviews in the Neurosciences · doi:10.1515/revneuro-2023-0155 · Cited by 12

C9ORF72-derived poly-GA DPRs undergo endocytic uptake in iAstrocytes and spread to motor neurons

Marchi, P. M., Marrone, L., Brasseur, L., Coens, A., Webster, C. P., Bousset, L., Destro, M., Smith, E. F., Walther, C. G., Alfred, V., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202101276 · Cited by 17

Targeting Gene C9orf72 Pathogenesis for Amyotrophic Lateral Sclerosis

Chong, Z. Z., & Souayah, N. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094276 · Cited by 11

Dissecting the stress granule RNA world: dynamics, strategies, and data

Biancon, G., Busarello, E., Cheng, M., Halene, S., & Tebaldi, T. (2025) · RNA · doi:10.1261/rna.080409.125 · Cited by 11

Challenges of modelling TDP-43 pathology in mice

Armas, J. M. B., Taoro‐González, L., Fisher, E., & Acevedo‐Arozena, A. (2025) · Mammalian Genome · doi:10.1007/s00335-025-10131-1 · Cited by 12

The nuclear envelope and nuclear pore complexes in neurodegenerative diseases

Wu, T., Xu, H., Cheng, L., Wu, R., Guo, F., & Chen, X. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1550859 · Cited by 11

Sequestration of cellular native factors by biomolecular assemblies: Physiological or pathological?

Hu, H., & Liu, Y. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119360 · Cited by 11

ALS’ Perfect Storm: C9orf72-Associated Toxic Dipeptide Repeats as Potential Multipotent Disruptors of Protein Homeostasis

Smeele, P. H., Cesare, G., & Vaccari, T. (2024) · Cells · doi:10.3390/cells13020178 · Cited by 12

Aberrant protein aggregation in amyotrophic lateral sclerosis

Wang, H., & Zeng, R. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12485-z · Cited by 11

Biological basis and psychiatric symptoms in frontotemporal dementia

Mori, K., & Ikeda, M. (2022) · Psychiatry and Clinical Neurosciences · doi:10.1111/pcn.13375 · Cited by 12

RNA-binding proteins as a common ground for neurodegeneration and inflammation in amyotrophic lateral sclerosis and multiple sclerosis

Acosta-Galeana, I., Hernandez-Martinez, R., Reyes-Cruz, T., Chiquete, E., & Buendia, J. D. J. A. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1193636 · Cited by 10

Evaluating emerging drugs in phase II & III for the treatment of amyotrophic lateral sclerosis

Li, X., & Bedlack, R. (2024) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2024.2333420 · Cited by 11

The Role of White Matter Dysfunction and Leukoencephalopathy/Leukodystrophy Genes in the Aetiology of Frontotemporal Dementias: Implications for Novel Approaches to Therapeutics

Lok, H. C., & Kwok, J. B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052541 · Cited by 10

PTPσ-mediated PI3P regulation modulates neurodegeneration in C9ORF72-ALS/FTD

Zhang, Z., Fu, X., Wright, N., Wang, W., Ye, Y., Asbury, J., Li, Y., Zhu, C., Wu, R., Wang, S., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.02.005 · Cited by 9

Is Dutasteride a Therapeutic Alternative for Amyotrophic Lateral Sclerosis?

Proaño, B., Casani-Cubel, J., Benlloch, M., Rodriguez‐Mateos, A., Navarro-Illana, E., Lajara-Romance, J. M., & Ortí, J. E. D. L. R. (2022) · Biomedicines · doi:10.3390/biomedicines10092084 · Cited by 9

Proteostasis deregulation as a driver of C9ORF72 pathogenesis

Torres, P., Cabral‐Miranda, F., Gonzalez‐Teuber, V., & Hetz, C. A. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15529 · Cited by 9

Context-dependent Interactors Regulate TDP-43 Dysfunction in ALS/FTLDPreprint

Xie, L., Zhu, Y., Hurtle, B. T., Wright, M., Robinson, J. L., Mauna, J. C., Brown, E. E., Ngo, M., Bergmann, C. A., Xu, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.07.646890 · Cited by 11

TDP-43: unveiling the hidden key to cellular fate decisions

Liu, B., Chen, X., Wang, J., Chen, J., Zhao, B., Jin, X., Jiang, M., Wang, J., Liao, W., Yang, B. X., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02442-2 · Cited by 8

Strategies in the design and development of (TAR) DNA-binding protein 43 (TDP-43) binding ligands

Rao, P. P. N., Shakeri, A., Zhao, Y., & Calon, F. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113753 · Cited by 8

The nuclear import receptor Kapβ2 modifies neurotoxicity mediated by poly(GR) in C9orf72-linked ALS/FTD

Cicardi, M. E., Kankate, V., Sriramoji, S., Krishnamurthy, K., Markandaiah, S. S., Verdone, B. M., Girdhar, A., Nelson, A. T., Rivas, L. B., Boehringer, A., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06071-2 · Cited by 8

CASP8 intronic expansion identified by poly-glycine-arginine pathology increases Alzheimer’s disease risk

Nguyen, L., Ajredini, R., Guo, S., Romano, L. E. L., Tomas, R. F., Bell, L. R., Ranum, P. T., Zu, T., Báñez-Coronel, M., Kelley, C. P., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2416885122 · Cited by 8

Proteins Associated with Neurodegenerative Diseases: Link to DNA Repair

Khodyreva, S. N., Dyrkheeva, N. S., & Lavrik, O. I. (2024) · Biomedicines · doi:10.3390/biomedicines12122808 · Cited by 7

Altered Inflammatory Signature in a C9ORF72 ‐ ALS iPSC ‐Derived Motor Neuron and Microglia Coculture Model

Gao, Y., Brothwood, J. L., Saini, H. K., O’Sullivan, G. A., Bento, C. F., McCarthy, J. M., Wallis, N. G., Daniel, E. D., Graham, B. L., & Tams, D. M. (2025) · Glia · doi:10.1002/glia.70084 · Cited by 7

TDP-43 as a potential retinal biomarker for neurodegenerative diseases

Glashutter, M., Wijesinghe, P., & Matsubara, J. A. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1533045 · Cited by 7

Lignin-carbohydrate complexes suppress SCA3 neurodegeneration via upregulating proteasomal activities

Chen, Z. S., Yan, M., Pei, W., Yan, B., Huang, C., & Chan, H. Y. E. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.07.133 · Cited by 7

Generation and characterization of monoclonal antibodies against pathologically phosphorylated TDP-43

Otero, P. C., Todd, T. W., Shao, W., Jones, C. J., Huang, K., Daughrity, L. M., Yue, M., Sheth, U., Gendron, T. F., Prudencio, M., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0298080 · Cited by 6

Recent Advances in Co-Condensation and Co-Aggregation of Amyloid Proteins Linked to Neurodegenerative Diseases

Zhang, X., Chen, Y., Tan, Y., Pan, T., & Wei, G. (2025) · Current Protein and Peptide Science · doi:10.2174/0113892037350729241129054701 · Cited by 6

Pathogenesis underlying hexanucleotide repeat expansions in C9orf72 gene in amyotrophic lateral sclerosis

Chong, Z. Z., Menkes, D. L., & Souayah, N. (2023) · Reviews in the Neurosciences · doi:10.1515/revneuro-2023-0060 · Cited by 6

Aspects of degradation and translation of the expanded C9orf72 hexanucleotide repeat RNA

Mori, K., Gotoh, S., & Ikeda, M. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15847 · Cited by 6

Sex Hormone-Binding Globulin (SHBG) in Cerebrospinal Fluid Does Not Discriminate between the Main FTLD Pathological Subtypes but Correlates with Cognitive Decline in FTLD Tauopathies

del Campo, M., Pijnenburg, Y. A. L., Chen‐Plotkin, A. S., Irwin, D. J., Grossman, M., Twaalfhoven, H. A. M., Hu, W. T., Meeter, L. H. H., Swieten, J. C. V., Vermunt, L., et al. (2021) · Biomolecules · doi:10.3390/biom11101484 · Cited by 6

Disruption of RNA-binding proteins in neurological disorders

Huang, L., Zhao, B., & Wan, Y. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.115119 · Cited by 5

NLS-binding deficient Kapβ2 reduces neurotoxicity via selective interaction with C9orf72-ALS/FTD dipeptide repeats

Kim, K. M., Girdhar, A., Cicardi, M. E., Kankate, V., Hayashi, M., Yang, R., Carey, J. L., Fare, C. M., Shorter, J., Cingolani, G., et al. (2025) · Communications Biology · doi:10.1038/s42003-024-07412-x · Cited by 5

Molecular switch of the dendrite-to-spine transport of TDP-43/FMRP-bound neuronal mRNAs and its impairment in ASD

Majumder, P., Chatterjee, B., Akter, K., Ahsan, A., Tan, S. J., Huang, C.-C. S., Chu, J.-F., & Shen, C.-K. J. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00684-5 · Cited by 6

Enhanced Acute Muscle Activation in ALS Patients Following Liposomal Curcumin, Resveratrol, and Dutasteride Administration

Martín-Ruiz, J., Maset-Roig, R., Caplliure‐Llopis, J., Villarón-Casales, C., Alarcón-Jiménez, J., de Bernardo, N., Proaño, B., Menargues-Ramírez, R., Selvi-Sabater, P., & Ortí, J. E. D. L. R. (2025) · Pharmaceuticals · doi:10.3390/ph18040497 · Cited by 6

HDAC6 Interacts With Poly (GA) and Modulates its Accumulation in c9FTD/ALS

del Rosso, G., Carlomagno, Y., Todd, T. W., Jones, C. Y., Prudencio, M., Daughrity, L. M., Yue, M., Jansen‐West, K. R., Tong, J., Shao, W., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.809942 · Cited by 5

C9orf72-associated dipeptide protein repeats form A11-positive oligomers in amyotrophic lateral sclerosis and frontotemporal dementia

Bhatt, N. N., Puangmalai, N., Sengupta, U., Jerez, C., Kidd, M., Gandhi, S. S., & Kayed, R. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105628 · Cited by 5

Cell Stress Induces Mislocalization of Transcription Factors with Mitochondrial Enrichment

Rossi, C., Fernàndez, A., Torres, P., Ramírez‐Núñez, O., Granado‐Serrano, A. B., Fontdevila, L., Povedano, M., Pamplona, R., Ferrer, I., & Portero‐Otín, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168853 · Cited by 5

Advancements in TDP-43 research: Towards biomarkers and therapeutic targets for amyotrophic lateral sclerosis

Wu, Y., Wang, J., & Zhao, Q. (2024) · Aging and Health Research · doi:10.1016/j.ahr.2024.100215 · Cited by 4

Dynamics of Onset and Progression in Amyotrophic Lateral Sclerosis

Swash, M., & de Carvalho, M. A. (2025) · Brain Sciences · doi:10.3390/brainsci15060601 · Cited by 4

Condensate protein aggregation in ALS/FTD is regulated by GGGGCC-repeat RNA scaffolds

Liu, Y., Song, M., Wan, L., Guo, P., & Han, D. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01785-9 · Cited by 4

RNA Dysmetabolism and Repeat-Associated Non-AUG Translation in Frontotemporal Lobar Degeneration/Amyotrophic Lateral Sclerosis due to C9orf72 Hexanucleotide Repeat Expansion

Mori, K., Gotoh, S., Uozumi, R., Miyamoto, T., Akamine, S., Kawabe, Y., Tagami, S., & Ikeda, M. (2023) · JMA Journal · doi:10.31662/jmaj.2022-0160 · Cited by 5

ASO-enhancement of TARDBP exitron splicing mitigates TDP-43 proteinopathiesPreprint

Yamagishi, T., Koide, S., Toyama, G., Washida, A., Yamada, Y., Hanyu, R., Nadbitova, E., Koike, Y. M., Konno, T., Ishihara, T., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.22.604579 · Cited by 4

New developments in pre-clinical models of ALS to guide translation

Cock, L. D., Bercier, V., & Bosch, L. V. D. (2024) · International review of neurobiology · doi:10.1016/bs.irn.2024.04.008 · Cited by 3

Decoding the functions of nuclear speckles in neurodegeneration

Chen, X., & Zhu, B. (2026) · Trends in Neurosciences · doi:10.1016/j.tins.2026.01.010 · Cited by 3

Effect of icaritin on autophagy-related protein expression in TDP-43-transfected SH-SY5Y cells

Zhou, Y., Huang, N., Li, Y., Ba, Z., & Luo, Y. (2022) · PeerJ · doi:10.7717/peerj.13703 · Cited by 3

Global research trends in biomarkers, therapeutic targets, and drugs for amyotrophic lateral sclerosis: a bibliometric and visualization analysis

Guo, N., Huang, W., Huang, J., Liu, Y., Zhu, K., & Gao, W. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1588968 · Cited by 4

Open Access: A Role for p53 in c9ALS/FTD?

Fare, C. M., & Shorter, J. (2021) · Trends in Genetics · doi:10.1016/j.tig.2021.01.008 · Cited by 3

Novel therapeutic approaches for motor neuron disease

Muzio, L., Ghirelli, A., Agosta, F., & Martino, G. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-98817-9.00027-2 · Cited by 3

Basic Concepts and Emergent Disease Mechanisms of Amyotrophic Lateral Sclerosis

Sirozh, O., Sáez-Mas, A., Lafarga, V., & Fernández-Capetillo, Ó. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00266-2 · Cited by 3

On the potential roles of TDP-43 in the formation of membraneless organelles and their transformation into toxic aggregates

Sergeeva, O. S., Neklesova, M. V., Reushev, V. A., Artemov, A. V., Константинович, Т. К., Константинович, Т. К., Uversky, V. N., & Fonin, A. V. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152808 · Cited by 2

PolyGR-containing aggregates link with pathology and clinical features of Alzheimer’s disease

Phuong, H. T., Tomas, R. F., Akmese, C., Mijares, A. M. P., Gerstin, I. M., Guo, S., Bell, L. R., Ellwood, R., Yegorova, S., Ng, S. K., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02954-8 · Cited by 2

Tetramethylpyrazine nitrone: a multifaceted neuroprotective agent in neurodegenerative disorders

Bahbah, E. I. (2025) · Neurodegenerative Disease Management · doi:10.1080/17582024.2025.2598227 · Cited by 2

The Chemical Regulatory Landscape of Biomolecular Condensates

Liu, D. Y., & Zhang, X. (2026) · Aggregate · doi:10.1002/agt2.70395 · Cited by 2

Reduction of RAD23A extends lifespan and mitigates pathology in a mouse model of TDP-43 proteinopathy

Guo, X., Prajapati, R. S., Chun, J., Byun, I., Gebis, K. K., Wang, Y., Ling, K., Dalton, C., Blair, J., Hamidianjahromi, A., et al. (2026) · Nature Communications · doi:10.1038/s41467-025-65104-4 · Cited by 4

Frontotemporal lobar degeneration

Kim, B., Viera-Ortiz, A., Phan, J. M., Irwin, D. J., & Lee, E. B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00041-1 · Cited by 3

Tracing neuropathological signatures: TARDBP and C9orf72 double mutations in a Sicilian family

Masrori, P., Tomé, S. O., Dedeene, L., Remiche, G., Esch, H. V., Thal, D. R., & Damme, P. V. (2025) · Human Molecular Genetics · doi:10.1093/hmg/ddaf147 · Cited by 1

TDP-43 in neurodegeneration and cancer: Decoding the mechanism of mRNA localization and translation

Pang, P., Yu, M., Ma, H., Wei, L., Huang, J., Zhao, L., & Zhang, Y.-H. (2026) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2026.102464 · Cited by 1

Decoding RNA splicing pathology: Alternative splicing in amyotrophic lateral sclerosis and its therapeutic potential

Priya, R., Tanti, G. K., & Jain, B. P. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.153723 · Cited by 1

Dysregulated neuronal mRNA transport and translation in FTD/ALS

Craig, E. J., & Ryan, V. H. (2026) · npj Dementia · doi:10.1038/s44400-026-00116-5 · Cited by 1

Plasma Proteomic Changes in GRN and C9orf72 Frontotemporal Dementia

Simrén, J., Benedet, A. L., Molfetta, G. D., Pola, I., Tan, K., Cantoni, V., Libri, I., Rivolta, J., Ghidoni, R., Zetterberg, H., et al. (2026) · European Journal of Neurology · doi:10.1111/ene.70704 · Cited by 2

Multiple motor proteins regulate TDP-43 anterograde axonal transport

Feole, M., Devoto, V. M. P., Dragišić, N., Čarná, M., Klosterman, K., Limbaek-Stokin, C., Forte, G., Moya, K. L., Smith, R. A., Svendsen, C. N., et al. (2026) · Acta Neuropathologica · doi:10.1007/s00401-026-03071-w · Cited by 1

Neurotoxicity and ALS: Insights into Pathogenesis

Vucic, S., & Kiernan, M. C. (2021) · Springer eBooks · doi:10.1007/978-3-030-71519-9_138-1 · Cited by 1

Intricate roles of spacers and stickers of Arg-rich C9ORF72 dipeptide repeat proteins; from toxicity to targeting to membraneless organelles

Miyagi, T., & Kanekura, K. (2023) · Organelle · doi:10.61747/0ifp.202311001 · Cited by 1

Neurotoxicity and ALS: Insights into Pathogenesis

Vucic, S., & Kiernan, M. C. (2022) · Springer eBooks · doi:10.1007/978-3-031-15080-7_138 · Cited by 1

Studying the Effect of TDP-43 Proteinopathy on Frontotemporal Dementia-Related Behaviors in Drosophila melanogaster

Dolbeck, E. (2021) · UA Campus Repository (The University of Arizona)

Posttranslational modifications of TDP-43

Rahman, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820066-7.20002-7

The role of TDP-43 protein in amyotrophic lateral sclerosis

Włodarczyk, P., Witczak, M., Gajewska, A., Chady, T., & Piotrowski, I. (2022) · Journal of Medical Science · doi:10.20883/medical.e710

Additional file 2 of Proximity proteomics of C9orf72 dipeptide repeat proteins identifies molecular chaperones as modifiers of poly-GA aggregation

Liu, F., Morderer, D., Wren, M. C., Vettleson-Trutza, S. A., Wang, Y., Rabichow, B. E., Salemi, M., Phinney, B. S., Oskarsson, B., Dickson, D. W., et al. (2022) · Figshare · doi:10.6084/m9.figshare.19181413

Biochemical characteristics of spacer amino acid determine phase-separating behavior and induction of nucleolar stress by arginine-rich dipeptide repeat proteins

Miyagi, T., Nawa, M., Kusakari, S., Yamazaki, R., Uji‐i, H., Hayamizu, Y., Suzuki, H., & Kanekura, K. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152252

Atypical features including acquired oculomotor apraxia in C9orf72 -associated familial primary lateral sclerosis

Hostetler, N., Zakutney, S., Pringle, C. E., Zwicker, J. C., & Breiner, A. (2025) · Journal of Neuromuscular Diseases · doi:10.1177/22143602251380427

Volumetric MRI and FDG-PET hypometabolism biomarkers of frontotemporal dementia: protocol for a systematic review and meta-analysis

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Preclinical Evaluation of the Assembly Modulator PAV-615 in a Mouse Model of C9orf72-Associated ALS/FTD

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