A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in 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 · see citing works

mTOR Signaling in Growth Control and Disease

Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509 · see citing works

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 · see citing works

Autophagy: Renovation of Cells and Tissues

Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,467 · see citing works

Autophagy fights disease through cellular self-digestion

Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452 · see citing works

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).

Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works

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 · see citing works

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 · see citing works

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

Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882 · see citing works

Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila

Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,549 · see citing works

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

Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500 · see citing works

Rab GTPases as coordinators of vesicle traffic

Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413 · see citing works

Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy

Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., Iemura, S.-I., Natsume, T., Takehana, K., Yamada, N., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1248 · Cited by 2,076 · see citing works

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · see citing works

Network organization of the human autophagy system

Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554 · see citing works

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 · see citing works

Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study

Majounie, E., Renton, A. E., Mok, K., Dopper, E. G., Waite, A., Rollinson, S., Chiò, A., Restagno, G., Nicolaou, N., Simon-Sanchez, J., et al. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70043-1 · Cited by 1,210 · see citing works

Frontotemporal dementia

Bang, J., Spina, S., & Miller, B. L. (2015) · The Lancet · doi:10.1016/s0140-6736(15)00461-4 · Cited by 1,144 · see citing works

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 1,079 · see citing works

Autophagy gone awry in neurodegenerative diseases

Wong, E. S. P., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 883 · see citing works

RNA Toxicity from the ALS/FTD C9ORF72 Expansion Is Mitigated by Antisense Intervention

Donnelly, C. J., Zhang, P.-W., Pham, J. T., Haeusler, A. R., Mistry, N. A., Vidensky, S., Daley, E. L., Poth, E. M., Hoover, B., Fines, D. M., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.015 · Cited by 877 · see citing works

RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia

Zu, T., Liu, Y., Báñez-Coronel, M., Reid, T. S., Pletniková, O., Lewis, J. M., Miller, T. M., Harms, M. B., Falchook, A. E., Subramony, S. H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315438110 · Cited by 748 · see citing works

<i>C9orf72</i> repeat expansions cause neurodegeneration in <i>Drosophila</i> through arginine-rich proteins

Mizielinska, S., Grönke, S., Niccoli, T., Ridler, C. E., Clayton, E. L., Devoy, A., Moens, T., Norona, F. E., Woollacott, I. O. C., Pietrzyk, J., et al. (2014) · Science · doi:10.1126/science.1256800 · Cited by 740 · see citing works

Lysosomal storage disorders: The cellular impact of lysosomal dysfunction

Platt, F. M., Boland, B., & van der Spoel, A. C. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201208152 · Cited by 689 · see citing works

Autophagy Inhibition Compromises Degradation of Ubiquitin-Proteasome Pathway Substrates

Korolchuk, V. I., Mansilla, A., Menzies, F. M., & Rubinsztein, D. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.021 · Cited by 657 · see citing works

Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells

Kwon, I., Xiang, S., Kato, M., Wu, L. C., Theodoropoulos, P., Wang, T., Kim, J., Yun, J., Xie, Y., & McKnight, S. L. (2014) · Science · doi:10.1126/science.1254917 · Cited by 648 · see citing works

A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: a gene identification study

Gijselinck, I., Langenhove, T. V., van der Zee, J., Sleegers, K., Philtjens, S., Kleinberger, G., Janssens, J., Bettens, K., Cauwenberghe, C. V., Pereson, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70261-7 · Cited by 635 · see citing works

Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration

Lagier‐Tourenne, C., Baughn, M. W., Rigo, F., Sun, S., Liu, P., Li, H., Jiang, J., Watt, A. T., Chun, S. J., Katz, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318835110 · Cited by 555 · see citing works

<i>C9orf72</i> is required for proper macrophage and microglial function in mice

O’Rourke, J. G., Bogdanik, L., Yáñez, A., Lall, D., Wolf, A. J., Muhammad, A. K. M. G., Ho, R., Carmona, S., Vit, J. P., Zarrow, J., et al. (2016) · Science · doi:10.1126/science.aaf1064 · Cited by 550 · see citing works

Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK

Shang, L., Chen, S., Du, F., Shen, L., Zhao, L., & Wang, X. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100844108 · Cited by 540 · see citing works

Antisense Proline-Arginine RAN Dipeptides Linked to C9ORF72-ALS/FTD Form Toxic Nuclear Aggregates that Initiate In Vitro and In Vivo Neuronal Death

Wen, X., Tan, W., Westergard, T., Krishnamurthy, K., Markandaiah, S. S., Shi, Y., Lin, S., Shneider, N. A., Monaghan, J., Pandey, U. B., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.12.010 · Cited by 513 · see citing works

Human Genome and Diseases:¶WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases

Li, D., & Roberts, R. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000838 · Cited by 497 · see citing works

Atg101, a novel mammalian autophagy protein interacting with Atg13

Hosokawa, N., Sasaki, T., Iemura, S.-I., Natsume, T., Hara, T., & Mizushima, N. (2009) · Autophagy · doi:10.4161/auto.5.7.9296 · Cited by 488 · see citing works

C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking

Farg, M. A., Sundaramoorthy, V., Sultana, J. M., Yang, S., Atkinson, R. A. K., Levina, V., Halloran, M. A., Gleeson, P. A., Blair, I. P., Soo, K. Y., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu068 · Cited by 478 · see citing works

A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy

Mercer, C. A., Kaliappan, A., & Dennis, P. B. (2009) · Autophagy · doi:10.4161/auto.5.5.8249 · Cited by 444 · see citing works

mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin

Kang, S. A. W., Pacold, M. E., Cervantes, C., Lim, D., Lou, H. J., Ottina, K. A., Gray, N. S., Turk, B. E., Yaffe, M. B., & Sabatini, D. M. (2013) · Science · doi:10.1126/science.1236566 · Cited by 432 · see citing works

Advances in understanding the molecular basis of frontotemporal dementia

Rademakers, R., Neumann, M., & Mackenzie, I. R. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.117 · Cited by 414 · see citing works

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 · see citing works

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

Webster, C. P., Smith, E. F., Bauer, C. S., Moller, A., Hautbergue, G. M., Ferraiuolo, L., Myszczynska, M. A., Higginbottom, A., Walsh, M. J., Whitworth, A. J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694401 · Cited by 404 · see citing works

Digesting the Expanding Mechanisms of Autophagy

Ktistakis, N. T., & Tooze, S. A. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.03.006 · Cited by 369 · see citing works

Expanded GGGGCC repeat RNA associated with amyotrophic lateral sclerosis and frontotemporal dementia causes neurodegeneration

Xu, Z., Poidevin, M., Li, X., Li, Y., Shu, L., Nelson, D. L., Li, H., Hales, C. M., Gearing, M., Wingo, T. S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219643110 · Cited by 334 · see citing works

Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors

Yoshimura, S., Gerondopoulos, A., Linford, A., Rigden, D. J., & Barr, F. A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201008051 · Cited by 326 · see citing works

The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs

Levine, T. P., Daniels, R. D., Gatta, A. T., Wong, L. H., & Hayes, M. J. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts725 · Cited by 321 · see citing works

C9orf72 frontotemporal lobar degeneration is characterised by frequent neuronal sense and antisense RNA foci

Mizielinska, S., Lashley, T., Norona, F. E., Clayton, E. L., Ridler, C. E., Fratta, P., & Isaacs, A. M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1200-z · Cited by 317 · see citing works

Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network.

Riederer, M. A., Soldati, T., Shapiro, A. D., Lin, J., & Pfeffer, S. R. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.125.3.573 · Cited by 310 · see citing works

The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway

Sullivan, P. M., Zhou, X., Robins, A. M., Paushter, D. H., Kim, D., Smolka, M. B., & Hu, F. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0324-5 · Cited by 295 · see citing works

Reduced C9orf72 protein levels in frontal cortex of amyotrophic lateral sclerosis and frontotemporal degeneration brain with the C9ORF72 hexanucleotide repeat expansion

Waite, A. J., Bäumer, D., East, S. Z., Neal, J., Morris, H. R., Ansorge, O., & Blake, D. J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.016 · Cited by 277 · see citing works

Mutations in RAB39B Cause X-Linked Intellectual Disability and Early-Onset Parkinson Disease with α-Synuclein Pathology

Wilson, G. R. A., Sim, J. C. H., McLean, C., Giannandrea, M., Galea, C. A., Riseley, J. R., Stephenson, S. E. M., Fitzpatrick, E., Haas, S. A., Pope, K., et al. (2014) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.10.015 · Cited by 273 · see citing works

C 9orf72 ablation in mice does not cause motor neuron degeneration or motor deficits

Koppers, M., Blokhuis, A. M., Westeneng, H., Terpstra, M. L., Zundel, C. A. C., de Sá, R. V., Schellevis, R. D., Waite, A. J., Blake, D. J., Veldink, J. H., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24453 · Cited by 268 · see citing works

DENN Domain Proteins: Regulators of Rab GTPases

Marat, A. L., Dokainish, H., & McPherson, P. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.217067 · Cited by 265 · see citing works

C9orf72 ablation causes immune dysregulation characterized by leukocyte expansion, autoantibody production and glomerulonephropathy in mice

Atanasio, A., Decman, V., White, D., Ramos, M., Ikiz, B., Lee, H.-C., Siao, C.-J., Brydges, S., LaRosa, E., Bai, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep23204 · Cited by 263 · see citing works

Discovery of Novel DENN Proteins: Implications for the Evolution of Eukaryotic Intracellular Membrane Structures and Human Disease

Zhang, D., Iyer, L. M., He, F., & Aravind, L. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00283 · Cited by 244 · see citing works

Mutations in the Small GTPase Gene RAB39B Are Responsible for X-linked Mental Retardation Associated with Autism, Epilepsy, and Macrocephaly

Giannandrea, M., Bianchi, V., Mignogna, M. L., Sirri, A., Carrabino, S., D’Elia, E., Vecellio, M. L., Russo, S., Cogliati, F., Larizza, L., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.011 · Cited by 240 · see citing works

Nucleolar stress and impaired stress granule formation contribute to C9orf72 RAN translation-induced cytotoxicity

Tao, Z., Wang, H., Qin, X., Li, K., Li, K., Jiang, X., Xu, G., Wang, G., & Ying, Z. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv005 · Cited by 233 · see citing works

Lack of Neuronal IFN-β-IFNAR Causes Lewy Body- and Parkinson’s Disease-like Dementia

Ejlerskov, P., Hultberg, J. G., Wang, J., Carlsson, R., Ambjørn, M., Kuss, M., Liu, Y., Porcu, G., Kolkova, K., Friis Rundsten, C., et al. (2015) · Cell · doi:10.1016/j.cell.2015.08.069 · Cited by 211 · see citing works

Insights into Neuroinflammation in Parkinson’s Disease: From Biomarkers to Anti-Inflammatory Based Therapies

Rocha, N. P., de Miranda, A. S., & Teixeira, A. L. (2015) · BioMed Research International · doi:10.1155/2015/628192 · Cited by 200 · see citing works

Klotho as a potential biomarker and therapy for acute kidney injury

Hu, M. C., & Moe, O. W. (2012) · Nature Reviews Nephrology · doi:10.1038/nrneph.2012.92 · Cited by 180 · see citing works

Microcephaly disease gene Wdr62 regulates mitotic progression of embryonic neural stem cells and brain size

Chen, J.-F., Zhang, Y., Wilde, J. J., Hansen, K. C., Lai, F., & Niswander, L. A. (2014) · Nature Communications · doi:10.1038/ncomms4885 · Cited by 153 · see citing works

Targeting autophagy in neurodegenerative diseases

Vidal, R. L., Matus, S., Bargsted, L., & Hetz, C. A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.09.002 · Cited by 145 · see citing works

Isoform‐specific antibodies reveal distinct subcellular localizations of C 9orf72 in amyotrophic lateral sclerosis

Xiao, S., MacNair, L., McGoldrick, P., McKeever, P. M., McLean, J. R., Zhang, M., Keith, J. L., Zinman, L. H., Rogaeva, E. A., & Robertson, J. (2015) · Annals of Neurology · doi:10.1002/ana.24469 · Cited by 139 · see citing works

Rab7b controls trafficking from endosomes to the TGN

Progida, C., Cogli, L., Piro, F., Luca, A. D., Bakke, O., & Bucci, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.051474 · Cited by 130 · see citing works

Structure of the Atg101–Atg13 complex reveals essential roles of Atg101 in autophagy initiation

SUZUKI, H., Kaizuka, T., Mizushima, N., & Noda, N. N. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3036 · Cited by 114 · see citing works

A Hereditary Spastic Paraplegia Mouse Model Supports a Role of ZFYVE26/SPASTIZIN for the Endolysosomal System

Khundadze, M., Kollmann, K., Koch, N., Biskup, C. U., Nietzsche, S., Zimmer‐Bensch, G., Hennings, J. C., Huebner, A. K., Symmank, J., Jahić, A., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003988 · Cited by 100 · see citing works

Crag Is a GEF for Rab11 Required for Rhodopsin Trafficking and Maintenance of Adult Photoreceptor Cells

Xiong, B., Bayat, V., Jaiswal, M., Zhang, K., Sandoval, H., Charng, W., Li, T., David, G., Duraine, L., Lin, Y.-Q., et al. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001438 · Cited by 98 · see citing works

Procathepsins L and D are membrane-bound in acidic microsomal vesicles

McIntyre, G., & Erickson, A. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98635-7 · Cited by 91 · see citing works

C9orf72 isoforms in Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration

Xiao, S., MacNair, L., McLean, J. R., McGoldrick, P., McKeever, P. M., Soleimani, S., Keith, J. L., Zinman, L. H., Rogaeva, E. A., & Robertson, J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.062 · Cited by 44 · see citing works

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) ¹

Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works

The molecular machinery of regulated cell death

Tang, D., Kang, R., Berghe, T. V., Vandenabeele, P., & Kroemer, G. (2019) · Cell Research · doi:10.1038/s41422-019-0164-5 · Cited by 2,595 · see citing works

The mammalian ULK1 complex and autophagy initiation

Zachari, M., & Ganley, I. G. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170021 · Cited by 789 · see citing works

C9orf72-mediated ALS and FTD: multiple pathways to disease

Balendra, R., & Isaacs, A. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0047-2 · Cited by 715 · see citing works

The role of mitochondria in amyotrophic lateral sclerosis

Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.06.052 · Cited by 556 · see citing works

ALS Genetics: Gains, Losses, and Implications for Future Therapies

Kim, G., Gautier, O., Tassoni-Tsuchida, E., Ma, X. R., & Gitler, A. D. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.022 · Cited by 370 · see citing works

A molecular perspective of mammalian autophagosome biogenesis

Mercer, T. J., Gubaš, A., & Tooze, S. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.810366 · Cited by 265 · see citing works

Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis

Root, J. T., Merino, P., Nuckols, A., Johnson, M. A., & Kukar, T. L. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105360 · Cited by 230 · see citing works

Neurobiology of axonal transport defects in motor neuron diseases: Opportunities for translational research?

Vos, K. J. D., & Hafezparast, M. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.02.004 · Cited by 238 · see citing works

Amyotrophic lateral sclerosis: translating genetic discoveries into therapies

Akçimen, F., Lopez, E. R., Landers, J. E., Nath, A., Chiò, A., Chia, R., & Traynor, B. J. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-023-00592-y · Cited by 234 · see citing works

Reduced C9ORF72 function exacerbates gain of toxicity from ALS/FTD-causing repeat expansion in C9orf72

Zhu, Q., Jiang, J., Gendron, T. F., McAlonis-Downes, M., Jiang, L., Taylor, A., Diaz Garcia, S., Ghosh Dastidar, S., Rodriguez, M. J., King, P., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0619-5 · Cited by 220 · see citing works

Dysregulated molecular pathways in amyotrophic lateral sclerosis–frontotemporal dementia spectrum disorder

Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 218 · see citing works

Heterochromatin anomalies and double-stranded RNA accumulation underlie C9orf72 poly(PR) toxicity

Zhang, Y., Guo, L. E., Gonzales, P. K., Gendron, T. F., Wu, Y., Jansen‐West, K. R., O’Raw, A. D., Pickles, S. R., Prudencio, M., Carlomagno, Y., et al. (2019) · Science · doi:10.1126/science.aav2606 · Cited by 202 · see citing works

TFEB dysregulation as a driver of autophagy dysfunction in neurodegenerative disease: Molecular mechanisms, cellular processes, and emerging therapeutic opportunities

Cortés, C. J., & Spada, A. R. L. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.012 · Cited by 197 · see citing works

The Autophagy Lysosomal Pathway and Neurodegeneration

Finkbeiner, S. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033993 · Cited by 196 · see citing works

Loss of C9orf72 Enhances Autophagic Activity via Deregulated mTOR and TFEB Signaling

Ugolino, J., Ji, Y. J., Conchina, K., Chu, J., Nirujogi, R. S., Pandey, A., Brady, N. R., Hamacher-Brady, A., & Wang, J. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1006443 · Cited by 185 · see citing works

A High-Density Human Mitochondrial Proximity Interaction Network

Antonická, H., Lin, Z., Janer, A., Aaltonen, M. J., Weraarpachai, W., Gingras, A., & Shoubridge, E. A. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.07.017 · Cited by 183 · see citing works

Autophagy and ALS: mechanistic insights and therapeutic implications

Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works

Autophagy and mitophagy in ALS

Evans, C. S., & Holzbaur, E. L. F. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.005 · Cited by 178 · see citing works

ULK1 and ULK2 Regulate Stress Granule Disassembly Through Phosphorylation and Activation of VCP/p97

Wang, B., Maxwell, B. A., Joo, J. H., Gwon, Y., Messing, J., Mishra, A., Shaw, T. I., Ward, A. L., Quan, H., Sakurada, S. M., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.027 · Cited by 174 · see citing works

C9ORF72: What It Is, What It Does, and Why It Matters

Smeyers, J., Banchi, E.-G., & Latouche, M. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.661447 · Cited by 175 · see citing works

RNA toxicity in non‐coding repeat expansion disorders

Swinnen, B., Robberecht, W., & Bosch, L. V. D. (2019) · The EMBO Journal · doi:10.15252/embj.2018101112 · Cited by 163 · see citing works

A proteomic network approach across the ALS‐FTD disease spectrum resolves clinical phenotypes and genetic vulnerability in human brain

Umoh, M. E., Dammer, E. B., Dai, J., Duong, D. M., Lah, J. J., Levey, A. I., Gearing, M., Glass, J. D., & Seyfried, N. T. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201708202 · Cited by 154 · see citing works

C9orf72 regulates energy homeostasis by stabilizing mitochondrial complex I assembly

Wang, T., Liu, H., Itoh, K., Oh, S., Zhao, L., Murata, D., Sesaki, H., Härtung, T., Na, C. H., & Wang, J. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.01.005 · Cited by 149 · see citing works

Cerebral organoid and mouse models reveal a RAB39b–PI3K–mTOR pathway-dependent dysregulation of cortical development leading to macrocephaly/autism phenotypesPreprint

Zhang, W., Ma, L., Yang, M., Shao, Q., Xu, J., Lu, Z., Zhao, Z., Chen, R., Chai, Y., & Chen, J. (2020) · Genes & Development · doi:10.1101/gad.332494.119 · Cited by 142 · see citing works

RNA metabolism in neurodegenerative disease

Liu, E. Y., Cali, C. P., & Lee, E. B. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028613 · Cited by 137 · see citing works

Reduced autophagy upon C9ORF72 loss synergizes with dipeptide repeat protein toxicity in G4C2 repeat expansion disorders

Boivin, M., Pfister, V., Gaucherot, A., Ruffenach, F., Negroni, L., Sellier, C., & Charlet‐Berguerand, N. (2020) · The EMBO Journal · doi:10.15252/embj.2018100574 · Cited by 137 · see citing works

Amyotrophic lateral sclerosis patient iPSC-derived astrocytes impair autophagy via non-cell autonomous mechanisms

Madill, M., McDonagh, K., Ma, J., Vajda, A., McLoughlin, P., O’Brien, T., Hardiman, O., & Shen, S. (2017) · Molecular Brain · doi:10.1186/s13041-017-0300-4 · Cited by 134 · see citing works

C9orf72 ALS-FTD: recent evidence for dysregulation of the autophagy-lysosome pathway at multiple levels

Beckers, J., Tharkeshwar, A. K., & Damme, P. V. (2021) · Autophagy · doi:10.1080/15548627.2021.1872189 · Cited by 124 · see citing works

Mitochondrial Fission Protein 1: Emerging Roles in Organellar Form and Function in Health and Disease

Ihenacho, U. K., Nolden, K. A., Harwig, M. C., Widlansky, M. E., & Hill, R. B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.660095 · Cited by 112 · see citing works

Autophagy as a common pathway in amyotrophic lateral sclerosis

Nguyen, D. K. H., Thombre, R., & Wang, J. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.006 · Cited by 110 · see citing works

Novel antibodies reveal presynaptic localization of C9orf72 protein and reduced protein levels in C9orf72 mutation carriers

Frick, P., Sellier, C., Mackenzie, I., Cheng, C.-Y., Tahraoui-Bories, J., Martinat, C., Pasterkamp, R., Prudlo, J., Edbauer, D., Oulad-Abdelghani, M., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0579-0 · Cited by 107 · see citing works

The spectrum of neurodevelopmental, neuromuscular and neurodegenerative disorders due to defective autophagy

Deneubourg, C., Ramm, M., Smith, L. J., Baron, O., Singh, K., Byrne, S., Duchen, M. R., Gautel, M., Eskelinen, E., Fanto, M., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1943177 · Cited by 113 · see citing works

Protein Homeostasis in Amyotrophic Lateral Sclerosis: Therapeutic Opportunities?

Webster, C. P., Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00123 · Cited by 99 · see citing works

Sex differences in autophagy-mediated diseases: toward precision medicine

Shang, D., Wang, L., Klionsky, D. J., Cheng, H., & Zhou, R. (2020) · Autophagy · doi:10.1080/15548627.2020.1752511 · Cited by 92 · see citing works

Autophagy and Its Impact on Neurodegenerative Diseases: New Roles for TDP-43 and C9orf72

Budini, M., Buratti, E., Morselli, E., & Criollo, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00170 · Cited by 91 · see citing works

RNA binding proteins and the pathological cascade in ALS/FTD neurodegeneration

Ito, D., Hatano, M., & Suzuki, N. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aah5436 · Cited by 92 · see citing works

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

Pang, W., & Hu, F. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15255 · Cited by 87 · see citing works

A C9orf72 ALS/FTD Ortholog Acts in Endolysosomal Degradation and Lysosomal Homeostasis

Corrionero, A., & Horvitz, H. R. (2018) · Current Biology · doi:10.1016/j.cub.2018.03.063 · Cited by 86 · see citing works

A C9orf72–CARM1 axis regulates lipid metabolism under glucose starvation-induced nutrient stressPreprint

Liu, Y., Wang, T., Ji, Y. J., Johnson, K., Liu, H., Johnson, K., Bailey, S., Suk, Y., Lu, Y., Liu, M., et al. (2018) · Genes & Development · doi:10.1101/gad.315564.118 · Cited by 83 · see citing works

Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration

Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79 · see citing works

Structure of the C9orf72 Arf GAP complex haploinsufficient in ALS and FTD

Su, M.-Y., Fromm, S., Zoncu, R., & Hurley, J. (2020) · Nature · doi:10.1038/s41586-020-2633-x · Cited by 67 · see citing works

Impairment of Lysosome Function and Autophagy in Rare Neurodegenerative Diseases

Darios, F. D., & Stévanin, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.033 · Cited by 77 · see citing works

Cryo-EM structure of C9ORF72–SMCR8–WDR41 reveals the role as a GAP for Rab8a and Rab11a

Tang, D., Sheng, J., Xu, L., Zhan, X., Liu, J., Jiang, H., Shu, X., Liu, X., Zhang, T., Jiang, L., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002110117 · Cited by 77 · see citing works

TFEB/Mitf links impaired nuclear import to autophagolysosomal dysfunction in C9-ALS

Cunningham, K. M., Maulding, K., Ruan, K., Şentürk, M., Grima, J. C., Sung, H., Zuo, Z., Song, H., Gao, J., Dubey, S. K., et al. (2020) · eLife · doi:10.7554/elife.59419 · Cited by 75 · see citing works

Multiplex image-based autophagy RNAi screening identifies SMCR8 as ULK1 kinase activity and gene expression regulator

Jung, J., Nayak, A., Schaeffer, V., Starzetz, T., Kirsch, A. K., Müller, S. P., Đikić, I., Mittelbronn, M. G. A., & Behrends, C. (2017) · eLife · doi:10.7554/elife.23063 · Cited by 74 · see citing works

Autophagy in Astrocytes and its Implications in Neurodegeneration

Sung, K., & Jiménez-Sánchez, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.041 · Cited by 74 · see citing works

The ALS-FTD-linked gene product, C9orf72, regulates neuronal morphogenesis via autophagy

Ho, W. Y., Tai, Y. K., Chang, J., Liang, J., Tyan, S.-H., Chen, S., Guan, J., Zhou, H., Shen, H., Koo, E. H., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1569441 · Cited by 70 · see citing works

Amyotrophic Lateral Sclerosis: Molecular Mechanisms, Biomarkers, and Therapeutic Strategies

Yang, X., Ji, Y., Wang, W., Zhang, L., Chen, Z., Yu, M., Shen, Y., Ding, F., Gu, X., & Sun, H. (2021) · Antioxidants · doi:10.3390/antiox10071012 · Cited by 71 · see citing works

C9orf72 deficiency promotes motor deficits of a C9ALS/FTD mouse model in a dose-dependent manner

Shao, Q., Chen, L., Chang, Q., Zhang, W., Yang, M., & Chen, J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0685-7 · Cited by 71 · see citing works

Reduced C9orf72 function leads to defective synaptic vesicle release and neuromuscular dysfunction in zebrafish

Butti, Z., Pan, Y. E., Giacomotto, J., & Patten, S. A. (2021) · Communications Biology · doi:10.1038/s42003-021-02302-y · Cited by 69 · see citing works

The C9orf72-interacting protein Smcr8 is a negative regulator of autoimmunity and lysosomal exocytosisPreprint

Zhang, Y., Burberry, A., Wang, J., Sandoe, J., Ghosh, S. D., Udeshi, N. D., Svinkina, T., Mordes, D. A., Mok, J., Charlton, M. E., et al. (2018) · Genes & Development · doi:10.1101/gad.313932.118 · Cited by 69 · see citing works

C9orf72 loss-of-function: a trivial, stand-alone or additive mechanism in C9 ALS/FTD?

Braems, E., Swinnen, B., & Bosch, L. V. D. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02214-x · Cited by 68 · see citing works

PQLC2 recruits the C9orf72 complex to lysosomes in response to cationic amino acid starvation

Amick, J., Tharkeshwar, A. K., Talaia, G., & Ferguson, S. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201906076 · Cited by 61 · see citing works

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 64 · see citing works

Current Advances and Limitations in Modeling ALS/FTD in a Dish Using Induced Pluripotent Stem Cells

Guo, W., Fumagalli, L., Prior, R. C., & Bosch, L. V. D. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00671 · Cited by 59 · see citing works

C9orf72 Intermediate Repeats are Associated with Corticobasal Degeneration, Increased C9orf72 Expression and Disruption of Autophagy

Cali, C. P., Patiño, M., Tai, Y., Ho, W. Y., Mclean, C., Morris, C., Seeley, W., Miller, B., Gaig, C., Vonsattel, J., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02045-5 · Cited by 55 · see citing works

The Enigmatic Role of C9ORF72 in Autophagy

Nassif, M., Woehlbier, U., & Manque, P. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00442 · Cited by 62 · see citing works

VAMP associated proteins are required for autophagic and lysosomal degradation by promoting a PtdIns4P-mediated endosomal pathway

Mao, D., Lin, G., Tepe, B., Zuo, Z., Tan, K. L., Şentürk, M., Zhang, S., Arenkiel, B. R., Sardiello, M., & Bellen, H. J. (2019) · Autophagy · doi:10.1080/15548627.2019.1580103 · Cited by 58 · see citing works

Is amyotrophic lateral sclerosis/frontotemporal dementia an autophagy disease?

Deng, Z., Sheehan, P., Chen, S., & Yue, Z. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0232-6 · Cited by 61 · see citing works

C9orf72 and smcr8 mutant mice reveal MTORC1 activation due to impaired lysosomal degradation and exocytosis

Shao, Q., Yang, M., Chen, L., Ma, L., Zhang, W., Jiang, Z., Luo, J., Lee, J., Liang, C., & Chen, J. (2019) · Autophagy · doi:10.1080/15548627.2019.1703353 · Cited by 58 · see citing works

RNA-mediated toxicity in C9orf72 ALS and FTD

McEachin, Z. T., Parameswaran, J., Raj, N., Bassell, G. J., & Jiang, J. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105055 · Cited by 57 · see citing works

Genetic models of C9orf72: what is toxic?

Moens, T. G., Partridge, L., & Isaacs, A. M. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.01.006 · Cited by 57 · see citing works

The multifaceted role of kinases in amyotrophic lateral sclerosis: genetic, pathological and therapeutic implications

Guo, W., Vandoorne, T., Steyaert, J., Staats, K. A., & Bosch, L. V. D. (2020) · Brain · doi:10.1093/brain/awaa022 · Cited by 56 · see citing works

C9orf72: At the intersection of lysosome cell biology and neurodegenerative disease

Amick, J., & Ferguson, S. M. (2017) · Traffic · doi:10.1111/tra.12477 · Cited by 55 · see citing works

Insights into C9ORF72-Related ALS/FTD from Drosophila and iPSC Models

Yuva-Aydemir, Y., Almeida, S., & Gao, F. (2018) · Trends in Neurosciences · doi:10.1016/j.tins.2018.04.002 · Cited by 55 · see citing works

Cell-autonomous immune dysfunction driven by disrupted autophagy in C9orf72 -ALS iPSC-derived microglia contributes to neurodegeneration

Banerjee, P., Mehta, A. R., Nirujogi, R. S., Cooper, J. D., James, O. G., Nanda, J., Longden, J., Burr, K., McDade, K., Salzinger, A., et al. (2023) · Science Advances · doi:10.1126/sciadv.abq0651 · Cited by 54 · see citing works

Extensive transcriptomic study emphasizes importance of vesicular transport in C9orf72 expansion carriers

Dickson, D. W., Baker, M., Jackson, J. L., DeJesus‐Hernandez, M., Finch, N. A., Tian, S., Heckman, M. G., Pottier, C. P., Gendron, T. F., Murray, M. E., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0797-0 · Cited by 50 · see citing works

Mouse Models of C9orf72 Hexanucleotide Repeat Expansion in Amyotrophic Lateral Sclerosis/ Frontotemporal Dementia

Batra, R., & Lee, C. W. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00196 · Cited by 54 · see citing works

Excessive endosomal TLR signaling causes inflammatory disease in mice with defective SMCR8-WDR41-C9ORF72 complex function

McAlpine, W., Sun, L., Wang, K.-W., Liu, A., Jain, R., Miguel, M. S., Wang, J., Zhang, Z., Hayse, B., McAlpine, S. G., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814753115 · Cited by 51 · see citing works

C9orf72 associates with inactive Rag GTPases and regulates mTORC1‐mediated autophagosomal and lysosomal biogenesis

Wang, M., Wang, H., Tao, Z., Qin, X., Hao, Z., Prehn, J. H. M., Zhen, X., Wang, G., & Ying, Z. (2020) · Aging Cell · doi:10.1111/acel.13126 · Cited by 51 · see citing works

Elevated TMEM106B levels exaggerate lipofuscin accumulation and lysosomal dysfunction in aged mice with progranulin deficiency

Zhou, X., Sun, L., Brady, O. A., Murphy, K. A., & Hu, F. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0412-1 · Cited by 49 · see citing works

Synaptic localization of C9orf72 regulates post-synaptic glutamate receptor 1 levels

Xiao, S., McKeever, P. M., Lau, A., & Robertson, J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0812-5 · Cited by 48 · see citing works

Dysfunctional Autophagy and Endolysosomal System in Neurodegenerative Diseases: Relevance and Therapeutic Options

Giovedı̀, S., Ravanelli, M. M., Parisi, B., Bettegazzi, B., & Guarnieri, F. C. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.602116 · Cited by 48 · see citing works

The papain-like protease of coronaviruses cleaves ULK1 to disrupt host autophagy

Mohamud, Y., Xue, Y. C., Liu, H., Ng, C. S., Bahreyni, A., Jan, E., & Luo, H. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.12.091 · Cited by 48 · see citing works

The endolysosomal pathway and ALS/FTD

Todd, T. W., Shao, W., Zhang, Y., & Petrucelli, L. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.09.004 · Cited by 44 · see citing works

Unaffected mosaic C9orf72 case

McGoldrick, P., Zhang, M., van Blitterswijk, M., Sato, C., Moreno, D., Xiao, S., Zhang, A. B., McKeever, P. M., Weichert, A., Schneider, R., et al. (2017) · Neurology · doi:10.1212/wnl.0000000000004865 · Cited by 46 · see citing works

UNC-51-like Kinase 1: From an Autophagic Initiator to Multifunctional Drug Target

Zhang, L., Ouyang, L., Guo, Y., Zhang, J. C., & Liu, B. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01684 · Cited by 46 · see citing works

C9orf72 is essential for neurodevelopment and motility mediated by Cyclin G1

Yeh, T., Liu, H.-F., Li, Y.-W., Lu, C.-S., Shih, H., Chiu, C., Lin, S., Huang, Y.-C., & Cheng, Y. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.03.002 · Cited by 43 · see citing works

RNA Binding Proteins and the Pathogenesis of Frontotemporal Lobar Degeneration

Hofmann, J. W., Seeley, W. W., & Huang, E. J. (2018) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012418-012955 · Cited by 42 · see citing works

Golgi-associated Rab GTPases implicated in autophagy

Lu, Q., Wang, P., & Yang, L. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00543-2 · Cited by 40 · see citing works

Pathogenic Mechanisms and Therapy Development for C9orf72 Amyotrophic Lateral Sclerosis/Frontotemporal Dementia

Jiang, J., & Ravits, J. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00797-2 · Cited by 40 · see citing works

WDR41 supports lysosomal response to changes in amino acid availability

Amick, J., Tharkeshwar, A. K., Amaya, & Ferguson, S. M. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-12-0703 · Cited by 39 · see citing works

Perturbed autophagy and DNA repair converge to promote neurodegeneration in amyotrophic lateral sclerosis and dementia

Walker, C., & El‐Khamisy, S. F. (2018) · Brain · doi:10.1093/brain/awy076 · Cited by 39 · see citing works

Using induced pluripotent stem cell neuronal models to study neurodegenerative diseases

Zhang, X., Hu, D., Shang, Y., & Qi, X. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.03.004 · Cited by 36 · see citing works

Amino acid sensing and lysosomal signaling complexes.

Cui, Z., Joiner, A., Jansen, R., & Hurley, J. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102544 · Cited by 33 · see citing works

C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated membrane tethering and fusion in mammalian autophagy

Zhang, S., Tong, M., Zheng, D., Huang, H., Li, L., Ungermann, C., Pan, Y., Luo, H., Lei, M., Tang, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42003-0 · Cited by 36 · see citing works

mTOR in metabolic homeostasis and disease.

Liu, X., Guo, B., Li, Q., & Nie, J. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.114173 · Cited by 35 · see citing works

C9ORF72-related cellular pathology in skeletal myocytes derived from ALS-patient induced pluripotent stem cells

Lynch, E. M., Semrad, T., Belsito, V. S., FitzGibbons, C., Reilly, M. L., Hayakawa, K., & Suzuki, M. (2019) · Disease Models & Mechanisms · doi:10.1242/dmm.039552 · Cited by 36 · see citing works

Emerging Evidence Highlighting the Importance of Redox Dysregulation in the Pathogenesis of Amyotrophic Lateral Sclerosis (ALS)

Jagaraj, C. J., Parakh, S., & Atkin, J. D. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.581950 · Cited by 36 · see citing works

YPD-30, a prodrug of YPD-29B, is an oral small-molecule inhibitor targeting PD-L1 for the treatment of human cancer

Lai, F., Ji, M., Huang, L., Wang, Y., Xue, N., Du, T., Dong, K., Yao, X., Jin, J., Feng, Z., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.02.031 · Cited by 35 · see citing works

Function and regulation of ULK1: From physiology to pathology

Rong, Z., Zheng, K., Chen, J., & Jin, X. (2022) · Gene · doi:10.1016/j.gene.2022.146772 · Cited by 35 · see citing works

Autophagy Dysfunction in ALS: from Transport to Protein Degradation

Cozzi, M., & Ferrari, V. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02029-3 · Cited by 35 · see citing works

C9orf72 functions in the nucleus to regulate DNA damage repair

He, L., Liang, J., Chen, C.-N., Chen, J., Shen, Y., Sun, S., & Li, L. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01074-0 · Cited by 34 · see citing works

NDST3 deacetylates α‐tubulin and suppresses V‐ATPase assembly and lysosomal acidification

Tang, Q., Liu, M., Liu, Y., Hwang, R., Zhang, T., & Wang, J. (2021) · The EMBO Journal · doi:10.15252/embj.2020107204 · Cited by 31 · see citing works

RAB39B Deficiency Impairs Learning and Memory Partially Through Compromising Autophagy

Niu, M., Zheng, N., Wang, Z., Gao, Y., Luo, X., Chen, Z., Fu, X., Wang, Y., Wang, T., Liu, M., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.598622 · Cited by 32 · see citing works

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

Frottin, F., Pérez‐Berlanga, M., Hartl, F. U., & Hipp, M. S. (2021) · eLife · doi:10.7554/elife.62718 · Cited by 31 · see citing works

The autophagy of stress granules

Ryan, L., & Rubinsztein, D. C. (2023) · FEBS Letters · doi:10.1002/1873-3468.14787 · Cited by 30 · see citing works

Autophagy and lysosomal pathways in nervous system disorders

Bingol, B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.009 · Cited by 31 · see citing works

SMCR8 negatively regulates AKT and MTORC1 signaling to modulate lysosome biogenesis and tissue homeostasis

Lan, Y., Sullivan, P. M., & Hu, F. (2019) · Autophagy · doi:10.1080/15548627.2019.1569914 · Cited by 31 · see citing works

Elucidating the disease relevance and function of the ALS/FTLD-associated protein C9orf72

Sullivan, P. M. (2017) · eCommons (Cornell University) · doi:10.7298/x4b56gwt

The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway

Sullivan, P. M., Zhou, X., Robins, A. M., Paushter, D. H., Kim, D., Smolka, M. B., & Hu, F. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0324-5 · Cited by 295 · see citing works

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

Webster, C. P., Smith, E. F., Bauer, C. S., Moller, A., Hautbergue, G. M., Ferraiuolo, L., Myszczynska, M. A., Higginbottom, A., Walsh, M. J., Whitworth, A. J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694401 · Cited by 404 · see citing works

Phosphoregulated SMCR8-FIP200 interaction connects the ALS/FTD-linked C9orf72 complex to autophagy initiation and mitochondrial quality controlPreprint

Wang, J., Davis, C. T., Kunzelmann, S., Maslen, S., Kelly, G., Skehel, M. J., & Schreiber, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.16.718395

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 68 · see citing works