The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351

Image processing with ImageJ

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AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1

Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227

Induction of the Vitamin D Receptor Attenuates Autophagy Dysfunction-Mediated Cell Death Following Traumatic Brain Injury

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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 · cited 5×

p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

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

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Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

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Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila

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Loss of autophagy in the central nervous system causes neurodegeneration in mice

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Focus on the Small GTPase Rab1: A Key Player in the Pathogenesis of Parkinson’s Disease

Martínez‐Menárguez, J. A., Martínez‐Alonso, E., Cara‐Esteban, M., & Tomás, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222112087 · Cited by 24

The RNA exosome complex degrades expanded hexanucleotide repeat RNA in C9orf72 FTLD/ALS

Kawabe, Y., Mori, K., Yamashita, T., Gotoh, S., & Ikeda, M. (2020) · The EMBO Journal · doi:10.15252/embj.2019102700 · Cited by 25

Deregulated expression of a longevity gene, Klotho, in the C9orf72 deletion mice with impaired synaptic plasticity and adult hippocampal neurogenesis

Ho, W. Y., Navakkode, S., Liu, F., Soong, T. W., & Ling, S. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01030-4 · Cited by 26

Mechanistic Insights of Mitochondrial Dysfunction in Amyotrophic Lateral Sclerosis: An Update on a Lasting Relationship

Candelise, N., Salvatori, I., Scaricamazza, S., Nesci, V., Zenuni, H., Ferri, A., & Valle, C. (2022) · Metabolites · doi:10.3390/metabo12030233 · Cited by 25

The human autophagy-initiating complexes ULK1C and PI3KC3-C1

Chen, M., & Hurley, J. H. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110391 · Cited by 25

C9ORF72 protein function and immune dysregulation in amyotrophic lateral sclerosis

Lai, J. D., & Ichida, J. K. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134523 · Cited by 25

The Proteasomal Deubiquitinating Enzyme PSMD14 Regulates Macroautophagy by Controlling Golgi-to-ER Retrograde Transport

Bustamante, H. A., Cereceda, K., González, A., Valenzuela, G., Cheuquemilla, Y., Hernández, S., Arias‐Muñoz, E., Cerda‐Troncoso, C., Bandau, S., Soza, A., et al. (2020) · Cells · doi:10.3390/cells9030777 · Cited by 20

Significance and prognostic role of human epidermal growth factor receptor 2 and RAB1A expression in gastric cancer

Xu, B., Huang, C., Yang, X., Li, X., Li, L., & Ding, Y. (2018) · Oncology Letters · doi:10.3892/ol.2018.7992 · Cited by 21

Molecular mechanisms of autophagy and implications in liver diseases

Wu, Y., Tan, H. W. S., Lin, J.-Y., Shen, H., Wang, H., & Lu, G. X. (2023) · Liver Research · doi:10.1016/j.livres.2023.02.002 · Cited by 24

Neurodegenerative diseases: model organisms, pathology and autophagy

Suresh, S., Verma, V., Sateesh, S., Clement, J. P., & Manjithaya, R. R. (2018) · Journal of Genetics · doi:10.1007/s12041-018-0955-3 · Cited by 22

C9orf72/ALFA-1 controls TFEB/HLH-30-dependent metabolism through dynamic regulation of Rag GTPases

Ji, Y. J., Ugolino, J., Zhang, T., Lu, J., Kim, D., & Wang, J. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008738 · Cited by 22

Genetic forms of frontotemporal lobar degeneration: Current diagnostic approach and new directions in therapeutic strategies

Sellami, L., Saracino, D., & Ber, I. L. (2020) · Revue Neurologique · doi:10.1016/j.neurol.2020.02.008 · Cited by 23

C9orf72-associated SMCR8 protein binds in the ubiquitin pathway and with proteins linked with neurological disease

Goodier, J. L., Soares, A. O., Pereira, G., Devine, L. R., Sánchez, L., Cole, R. N., & Garcia-Perez, J. L. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00982-x · Cited by 21

Proteostasis impairment and ALS

Lambert-Smith, I. A., Saunders, D. N., & Yerbury, J. J. (2022) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2022.06.001 · Cited by 19

C9ORF72 hexanucleotide repeat expansion: From ALS and FTD to a broader pathogenic role?

Sellier, C., Corcia, P., Vourc’h, P., & Dupuis, L. (2024) · Revue Neurologique · doi:10.1016/j.neurol.2024.03.008 · Cited by 24

Human Induced Pluripotent Stem Cell Models of Neurodegenerative Disorders for Studying the Biomedical Implications of Autophagy

Seranova, E., Palhegyi, A. M., Verma, S., Dimova, S., Lasry, R., Naama, M., Sun, C., Barrett, T. G., Rosenstock, T. R., Kumar, D., et al. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.024 · Cited by 20

Smcr8 deficiency disrupts axonal transport-dependent lysosomal function and promotes axonal swellings and gain of toxicity in C9ALS/FTD mouse models

Chen, L., Shao, Q., Zhang, W., Yang, M., Chang, Q., Chen, R., & Chen, J. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz230 · Cited by 20

Simple model systems reveal conserved mechanisms of Alzheimer’s disease and related tauopathies

Jiang, Y., & MacNeil, L. T. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00664-x · Cited by 22

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

Riku, Y. (2020) · Neuropathology · doi:10.1111/neup.12644 · Cited by 19

The essential and downstream common proteins of amyotrophic lateral sclerosis: A protein-protein interaction network analysis

Mao, Y., Kuo, S.-W., Chen, L., Heckman, C. J., & Jiang, M. C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172246 · Cited by 19

Establishment of the phagophore–ERES membrane contact site initiates phagophore elongation

Gómez‐Sánchez, R., Ramirez, S. C., Duarte, P. V., Hu, Y. P., Mari, M. C., Olschewski, K., Hardenberg, R., Fromme, J. C., Ungermann, C., & Reggiori, F. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01621-6 · Cited by 18

The Classification and Prediction of Ferroptosis-Related Genes in ALS: A Pilot Study

Zhang, Q., Zhao, H., Luo, M., Cheng, X., Li, Y., Li, Q., Wang, Z., & Niu, Q. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.919188 · Cited by 19

C9orf72 regulates the unfolded protein response and stress granule formation by interacting with eIF2α

Zheng, W., Wang, K., Wu, Y., Ge, Y., Zhang, C., Li, Z., Wang, L., & Chen, S. (2022) · Theranostics · doi:10.7150/thno.76138 · Cited by 18

Mechanisms of IRF2BPL-related disorders and identification of a potential therapeutic strategy

Ray, S. S., Dutta, D., Dennys, C. N., Powers, S., Roussel, F. S., Lisowski, P., Glažar, P., Zhang, X., Biswas, P., Caporale, J. R., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111751 · Cited by 19

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

High frequency of C9orf72 hexanucleotide repeat expansion in amyotrophic lateral sclerosis patients from two founder populations sharing the same risk haplotype

Goldstein, O., Gana‐Weisz, M., Nefussy, B., Vainer, B., Nayshool, O., Bar‐Shira, A., Traynor, B. J., Drory, V. E., & Orr‐Urtreger, A. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.12.015 · Cited by 17

Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy

Barz, S., Kriegenburg, F., Sánchez‐Martín, P., & Kraft, C. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119064 · Cited by 17

Disease Mechanisms and Therapeutic Approaches in C9orf72 ALS-FTD

Mayl, K., Shaw, C. E., & Lee, Y. (2021) · Biomedicines · doi:10.3390/biomedicines9060601 · Cited by 18

FTLD Patient–Derived Fibroblasts Show Defective Mitochondrial Function and Accumulation of p62

Leskelä, S., Hoffmann, D. B., Rostalski, H., Huber, N., Wittrahm, R., Hartikainen, P. H., Korhonen, V. E., Leinonen, V., Hiltunen, M. O., Solje, E., et al. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02475-x · Cited by 16

Unraveling the multifaceted insights into amyotrophic lateral sclerosis: Genetic underpinnings, pathogenesis, and therapeutic horizons

Sharma, R., Khan, Z., Mehan, S., Gupta, G. D., & Narula, A. S. (2024) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2024.108518 · Cited by 18

Advanced Gene-Targeting Therapies for Motor Neuron Diseases and Muscular Dystrophies

Chamakioti, M., Karantzelis, N., & Taraviras, S. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094824 · Cited by 17

Sec16 in conventional and unconventional exocytosis: Working at the interface of membrane traffic and secretory autophagy?

Tang, B. L. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25842 · Cited by 15

Small molecule inhibition of PIKFYVE kinase rescues gain- and loss-of-function C9ORF72 ALS/FTD disease processes in vivo

Staats, K. A., Seah, C., Sahimi, A., Wang, Y., Koutsodendris, N., Lin, S., Kim, D., Chang, W.-H., Gray, K. A., Shi, Y., et al. (2019) · doi:10.1101/685800 · Cited by 16

Force-induced dephosphorylation activates the cochaperone BAG3 to coordinate protein homeostasis and membrane traffic

Ottensmeyer, J., Esch, A., Baeta, H., Sieger, S., Gupta, Y., Rathmann, M. F., Jeschke, A., Jacko, D., Schaaf, K., Schiffer, T., et al. (2024) · Current Biology · doi:10.1016/j.cub.2024.07.088 · Cited by 18

The role of autophagy in the pathogenesis and treatment of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)

Beckers, J., & Damme, P. V. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2474796 · Cited by 19

Non-muscle MYH10/myosin IIB recruits ESCRT-III to participate in autophagosome closure to maintain neuronal homeostasis

Jun, Y., Lee, S., Ban, B.-K., Lee, J., & Gao, F. (2023) · Autophagy · doi:10.1080/15548627.2023.2169309 · Cited by 16

Modeling the C9ORF72 repeat expansion mutation using human induced pluripotent stem cells

Selvaraj, B. T., Livesey, M. R., & Chandran, S. (2017) · Brain Pathology · doi:10.1111/bpa.12520 · Cited by 14

Modelling C9orf72-Related Amyotrophic Lateral Sclerosis in Zebrafish

Fortier, G., Butti, Z., & Patten, S. A. (2020) · Biomedicines · doi:10.3390/biomedicines8100440 · Cited by 15

A Review of APOE Genotype-Dependent Autophagic Flux Regulation in Alzheimer’s Disease

Chen, H., Chen, F., Zhang, M., Chen, Y., Cui, L., & Liang, C. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210602 · Cited by 15

A monocarboxylate transporter rescues frontotemporal dementia and Alzheimer’s disease models

Xu, D., Vincent, A. J., González‐Gutiérrez, A., Aleyakpo, B., Anoar, S., Giblin, A., Atilano, M. L., Adams, M. L., Shen, D., Thoeng, A., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010893 · Cited by 15

Rab-dependent cellular trafficking and amyotrophic lateral sclerosis

Parakh, S., Perri, E. R., Jagaraj, C. J., Ragagnin, A., & Atkin, J. D. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1553926 · Cited by 15

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

Smcr8 deficiency disrupts axonal transport-dependent lysosomal function and promotes axonal swellings and gain of toxicity in C9ALS/FTD mouse models

Chen, L., Shao, Q., Zhang, W., Yang, M., Chang, Q., Chen, R., & Chen, J. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa012 · Cited by 14

C9orf72 Intermediate Repeats Confer Genetic Risk for Severe COVID-19 Pneumonia Independently of Age

Zanella, I., Zacchi, E., Piva, S., Filosto, M., Beligni, G., Alaverdian, D. A., Amitrano, S., Fava, F., Baldassarri, M., Frullanti, E., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136991 · Cited by 14

Autophagy in Tumor Immunity and Viral-Based Immunotherapeutic Approaches in Cancer

Amiri, A. Z., Malone, K., Beug, S. T., Alain, T., & Yeganeh, B. (2021) · Cells · doi:10.3390/cells10102672 · Cited by 14

Deficiency of RAB39B Activates ER Stress-Induced Pro-apoptotic Pathway and Causes Mitochondrial Dysfunction and Oxidative Stress in Dopaminergic Neurons by Impairing Autophagy and Upregulating α-Synuclein

Chiu, C., Weng, Y.-H., Yeh, T., Lu, J., Chen, W.-S., Li, A. H.-R., Chen, Y.-L., Wei, K., & Wang, H. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03238-6 · Cited by 13

Pluripotent stem cells for neurodegenerative disease modeling: an expert view on their value to drug discovery

Chen, S.-D., Li, H., Cui, M., Dong, Q., & Yu, J. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1767579 · Cited by 15

Loss of TMEM106B exacerbates C9ALS/FTD DPR pathology by disrupting autophagosome maturation

Bauer, C. S., Webster, C. P., Shaw, A. C., Kok, J. R., Castelli, L. M., Lin, Y.-H., Smith, E. F., Illanes-Álvarez, F., Higginbottom, A., Shaw, P. J., et al. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1061559 · Cited by 15

Rab41-mediated ESCRT machinery repairs membrane rupture by a bacterial toxin in xenophagy

Nozawa, T., Toh, H., Iibushi, J., Kogai, K., Minowa‐Nozawa, A., Satoh, J., Ito, S., Murase, K., & Nakagawa, I. (2023) · Nature Communications · doi:10.1038/s41467-023-42039-2 · Cited by 13

Regulation of autophagy by protein lipidation

Shao, Y., Hu, J., Li, H., & Lu, K. (2024) · Advanced Biotechnology · doi:10.1007/s44307-024-00040-w · Cited by 14

Dysfunction of RNA/RNA-Binding Proteins in ALS Astrocytes and Microglia

Rossi, S., & Cozzolino, M. (2021) · Cells · doi:10.3390/cells10113005 · Cited by 15

Reduced C9orf72 expression exacerbates polyGR toxicity in patient iPSC-derived motor neurons and a Type I protein arginine methyltransferase inhibitor reduces that toxicity

Dane, T. L., Gill, A. L., Vieira, F. G., & Denton, K. R. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1134090 · Cited by 15

The Interplay Between Autophagy and RNA Homeostasis: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Houghton, O. H., Mizielinska, S., & Gómez‐Suaga, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.838402 · Cited by 12

C9orf72 protein quality control by UBR5‐mediated heterotypic ubiquitin chains

Jülg, J., Edbauer, D., & Behrends, C. (2023) · EMBO Reports · doi:10.15252/embr.202255895 · 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

Hippocampal aggregation signatures of pathogenic UBQLN2 in amyotrophic lateral sclerosis and frontotemporal dementia

Thumbadoo, K. M., Dieriks, B. V., Murray, H. C., Swanson, M. E. V., Yoo, J. H., Mehrabi, N. F., Turner, C. P., Dragunow, M., Faull, R. L. M., Curtis, M. A., et al. (2024) · Brain · doi:10.1093/brain/awae140 · Cited by 13

C9orf72-Associated Dipeptide Repeat Expansions Perturb ER-Golgi Vesicular Trafficking, Inducing Golgi Fragmentation and ER Stress, in ALS/FTD

Sultana, J., Ragagnin, A., Parakh, S., Saravanabavan, S., Soo, K. Y., Vidal, M., Jagaraj, C. J., Ding, K., Wu, S., Shadfar, S., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04187-4 · Cited by 12

Multifaceted role of SMCR8 as autophagy regulator

Jung, J., & Behrends, C. (2017) · Small GTPases · doi:10.1080/21541248.2017.1346553 · Cited by 13

Hereditary Motor Neuropathies and Amyotrophic Lateral Sclerosis: a Molecular and Clinical Update

García-Santibáñez, R., Burford, M. J., & Bucelli, R. C. (2018) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-018-0901-z · Cited by 14

The progress inC9orf72research: ALS/FTD pathogenesis, functions and structure

Jiang, L., Zhang, T., Lu, K., & Qi, S. (2021) · Small GTPases · doi:10.1080/21541248.2021.1892443 · Cited by 13

C9ORF72 knockdown triggers FTD-like symptoms and cell pathology in mice

Lopez-Herdoiza, M.-B., Bauché, S., Wilmet, B., Duigou, C. L., Roussel, D., Frah, M., Béal, J., Devely, G., Boluda, S., Frick, P., et al. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1155929 · Cited by 13

A comparative bioinformatic analysis of C9orf72

Iyer, S., Acharya, K. R., & Subramanian, V. (2018) · PeerJ · doi:10.7717/peerj.4391 · Cited by 13

Cell-Clearing Systems Bridging Repeat Expansion Proteotoxicity and Neuromuscular Junction Alterations in ALS and SBMA

Limanaqi, F., Busceti, C. L., Biagioni, F., Cantini, F., Lenzi, P., & Fornai, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114021 · Cited by 11

C9orf72 controls hepatic lipid metabolism by regulating SREBP1 transport

Wu, Y., Zheng, W., Xu, G., Zhu, L., Li, Z., Chen, J., Wang, L., & Chen, S. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01312-7 · Cited by 11

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

Amyotrophic Lateral Sclerosis Risk Genes and Suppressor

Ponnusamy, K., Haider, S., Kumar, R., Malik, M. Z., Singh, M., Rachana, R., & Mani, S. (2022) · Current Gene Therapy · doi:10.2174/1566523223666221108113330 · Cited by 11

A conjoint analysis of bulk RNA-seq and single-nucleus RNA-seq for revealing the role of ferroptosis and iron metabolism in ALS

Fu, X., He, Y., Xie, Y., & Lu, Z. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1113216 · Cited by 11

Mitochondrial Dysfunction in Repeat Expansion Diseases

Giménez-Bejarano, A., Alegre-Cortés, E., Yakhine-Diop, S. M. S., Gómez‐Suaga, P., & Fuentes, J. M. (2023) · Antioxidants · doi:10.3390/antiox12081593 · Cited by 12

Autophagy induced by Rab1a-ULK1 interaction promotes porcine reproductive and respiratory syndrome virus replication

Jiang, C., Diao, F., Ma, Z., Zhang, J., Bai, J., Nauwynck, H., Jiang, P., & Liu, X. (2022) · Virus Research · doi:10.1016/j.virusres.2022.198989 · Cited by 10

Identifying FUS amyotrophic lateral sclerosis disease signatures in patient dermal fibroblasts

Kumbier, K., Roth, M. A., Li, Z., Lazzari-Dean, J. R., Waters, C., Hammerlindl, S., Rinaldi, C., Huang, P., Korben, V. A., Phatnani, H. P., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.05.011 · Cited by 10

Role of the C9ORF72 Gene in the Pathogenesis of Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Hao, Z., Wang, R., Ren, H., & Wang, G. (2020) · Neuroscience Bulletin · doi:10.1007/s12264-020-00567-7 · Cited by 11

Identification of Potential Diagnoses Based on Immune Infiltration and Autophagy Characteristics in Major Depressive Disorder

Sun, Y., Li, J., Wang, L., Cong, T., Zhai, X., Li, L., Wu, H., Li, S., & Xiao, Z. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.702366 · Cited by 10

ALS-linked C9orf72 dipeptide repeats inhibit starvation-induced autophagy through modulating BCL2–BECN1 interaction

Xu, S., Ma, Q., Shen, J., Li, N., Sun, S., Wang, N., Chen, Y., Dong, C., Tam, K. Y., Prehn, J. H. M., et al. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.02.004 · Cited by 9

Simple models to understand complex disease: 10 years of progress from Caenorhabditis elegans models of amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Eck, R. J., Stair, J. G., Kraemer, B. C., & Liachko, N. F. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1300705 · Cited by 10

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

Drosophila as a model to study autophagy in neurodegenerative diseases and digestive tract

Tzou, F., Wen, J., Yeh, J., Huang, S., Chen, G., & Chan, C. (2021) · IUBMB Life · doi:10.1002/iub.2583 · Cited by 9

The impact of proteostasis dysfunction secondary to environmental and genetic causes on neurodegenerative diseases progression and potential therapeutic intervention

Elmatboly, A. M., Sherif, A., Deeb, D. A., Benmelouka, A. Y., Bin-Jumah, M. N., Aleya, L., & Abdel‐Daim, M. M. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-07914-1 · Cited by 9

ALS-Associated TDP-43 Dysfunction Compromises UPF1-Dependent mRNA Metabolism Pathways Including Alternative Polyadenylation and 3’UTR LengthPreprint

Alessandrini, F., Wright, M., Kurosaki, T., Maquat, L. E., & Kiskinis, E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.31.578311 · Cited by 9

C9orf72 deficiency impairs the autophagic response to aggregated TDP-25 and exacerbates TDP-25-mediated neurodegeneration in vivo

Lin, L. T., Shenouda, M., McGoldrick, P., Lau, A., & Robertson, J. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02061-5 · Cited by 8

Soluble CD83 Regulates Dendritic Cell–T Cell Immunological Synapse Formation by Disrupting Rab1a-Mediated F-Actin Rearrangement

Lin, W., Zhou, S., Feng, M., Yu, Y., Su, Q., & Li, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.605713 · Cited by 8

Expression of C9orf72 hexanucleotide repeat expansion leads to formation of RNA foci and dipeptide repeat proteins but does not influence autophagy or proteasomal function in neuronal cells

Leskelä, S., Huber, N., Hoffmann, D. B., Rostalski, H., Remes, A. M., Takalo, M., Hiltunen, M., & Haapasalo, A. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119021 · Cited by 10

Bioenergetic and Autophagic Characterization of Skin Fibroblasts from C9orf72 Patients

Álvarez‐Mora, M. I., Garrabou, G., Barcos, T., Garcia‐García, F., Grillo-Risco, R., Peruga, E., Gort, L., Borrego‐Écija, S., Sánchez‐Valle, R., Cantó, J., et al. (2022) · Antioxidants · doi:10.3390/antiox11061129 · Cited by 8

Patient-Derived iPSCs and iNs—Shedding New Light on the Cellular Etiology of Neurodegenerative Diseases

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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

Distinctive autophagy/mitophagy biomarker profiles in frontotemporal lobar degeneration and Alzheimer’s disease

Veverová, K., Katonová, A., Horáková, H., Laczó, J., Angelucci, F., Hort, J., Lautrup, S., Fang, E. F., & Vyhnálek, M. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-01954-9 · Cited by 7

Drug repurposing candidates for amyotrophic lateral sclerosis using common and rare genetic variants

Gerring, Z. F., Bhalala, O. G., Fearnley, L. G., Oikari, L. E., White, A. R., Derks, E. M., Watson, R., Yassi, N., Bahlo, M., & Reay, W. R. (2025) · Brain Communications · doi:10.1093/braincomms/fcaf184 · Cited by 6

TDP-43 dysfunction compromises UPF1-dependent mRNA metabolism in ALS

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Inflammatory diseases: Function of LncRNAs in their emergence and the role of mesenchymal stem cell secretome in their treatment

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Current neuroprotective therapies and future prospects for motor neuron disease

Evans, L. J., O’Brien, D., & Shaw, P. J. (2024) · International review of neurobiology · doi:10.1016/bs.irn.2024.04.003 · Cited by 5

Rsp5/NEDD4 and ESCRT regulate TDP-43 toxicity and turnover via an endolysosomal clearance mechanism

Byrd, A. T., Marmorale, L. J., Marcinowski, S., Dykstra, M. M., Addison, V., Barmada, S. J., & Buchan, J. R. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202212064 · Cited by 7

Loss of C9orf72 function leads to autoimmunity

Sakkas, L. I., Bogdanos, D. P., & Kousvelari, E. E. (2017) · Annals of Translational Medicine · doi:10.21037/atm.2017.01.33 · Cited by 6

Neurons Induced From Fibroblasts of c9ALS/FTD Patients Reproduce the Pathology Seen in the Central Nervous System

Bauer, P. O., Dunmore, J., Sasaguri, H., & Maťoška, V. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00935 · Cited by 6

Autophagy in motor neuron diseases

Rodríguez‐Muela, N. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.03.009 · Cited by 7

C9ORF72 hexanucleotide repeat expansion frequency in patients with Paget's disease of bone

Rubino, E., Stefano, M. D., Galimberti, D., Serpente, M., Scarpini, E. A., Fenoglio, C., Bo, M., & Rainero, I. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.08.014 · Cited by 6

BV-2 Microglial Cells Overexpressing C9orf72 Hexanucleotide Repeat Expansion Produce DPR Proteins and Show Normal Functionality but No RNA Foci

Rostalski, H., Hietanen, T., Leskelä, S., Beháňová, A., Abdollahzadeh, A., Wittrahm, R., Mäkinen, P. M., Huber, N., Hoffmann, D. B., Solje, E., et al. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.550140 · Cited by 5

Molecular interactions between C9ORF72 and SMCR8: A local energetic frustration perspective

Kumar, V. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.07.016 · Cited by 6

Autophagy-Lysosome Dysfunction in Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration

Sullivan, P. M., Zhou, X., & Hu, F. (2017) · InTech eBooks · doi:10.5772/intechopen.69371 · Cited by 6

Defects in early secretory pathway transport machinery components and neurodevelopmental disorders

Tang, B. L. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2021-0020 · Cited by 7

Propranolol reduces the accumulation of cytotoxic aggregates in C9orf72-ALS/FTD in vitro models

Seidel, M., Rajkumar, S., Steffke, C., Noeth, V., Agarwal, S., Roger, K., Lipecka, J., Ludolph, A. C., Guerrera, I. C., Boeckers, T. M., et al. (2023) · Current Research in Neurobiology · doi:10.1016/j.crneur.2023.100105 · Cited by 5

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

C9orf72 plays a central role in Rab GTPase-dependent regulation of autophagy

Webster, C. P., Smith, E. F., Grierson, A. J., & Vos, K. J. D. (2016) · Small GTPases · doi:10.1080/21541248.2016.1240495 · Cited by 70

C9orf72’s Interaction with Rab GTPases—Modulation of Membrane Traffic and Autophagy

Tang, B. L. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00228 · Cited by 38

C9ORF72 is a GDP/GTP exchange factor for Rab8 and Rab39 and regulates autophagy

Corbier, C., & Sellier, C. (2016) · Small GTPases · doi:10.1080/21541248.2016.1212688 · Cited by 73

Investigations into the cellular function of C9orf72

Webster, C. P. (2016) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin‐2 to induce motor neuron dysfunction and cell death

Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593350 · Cited by 414