C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking
Open accessAbstract
Intronic expansion of a hexanucleotide GGGGCC repeat in the chromosome 9 open reading frame 72 (C9ORF72) gene is the major cause of familial amyotrophic lateral sclerosis (ALS) and frontotemporal dementia. However, the cellular function of the C9ORF72 protein remains unknown. Here, we demonstrate that C9ORF72 regulates endosomal trafficking. C9ORF72 colocalized with Rab proteins implicated in autophagy and endocytic transport: Rab1, Rab5, Rab7 and Rab11 in neuronal cell lines, primary cortical neurons and human spinal cord motor neurons, consistent with previous predictions that C9ORF72 bears Rab guanine exchange factor activity. Consistent with this notion, C9ORF72 was present in the extracellular space and as cytoplasmic vesicles. Depletion of C9ORF72 using siRNA inhibited transport of Shiga toxin from the plasma membrane to Golgi apparatus, internalization of TrkB receptor and altered the ratio of autophagosome marker light chain 3 (LC3) II:LC3I, indicating that C9ORF72 regulates endocytosis and autophagy. C9ORF72 also colocalized with ubiquilin-2 and LC3-positive vesicles, and co-migrated with lysosome-stained vesicles in neuronal cell lines, providing further evidence that C9ORF72 regulates autophagy. Investigation of proteins interacting with C9ORF72 using mass spectrometry identified other proteins implicated in ALS; ubiquilin-2 and heterogeneous nuclear ribonucleoproteins, hnRNPA2/B1 and hnRNPA1, and actin. Treatment of cells overexpressing C9ORF72 with proteasome inhibitors induced the formation of stress granules positive for hnRNPA1 and hnRNPA2/B1. Immunohistochemistry of C9ORF72 ALS patient motor neurons revealed increased colocalization between C9ORF72 and Rab7 and Rab11 compared with controls, suggesting possible dysregulation of trafficking in patients bearing the C9ORF72 repeat expansion. Hence, this study identifies a role for C9ORF72 in Rab-mediated cellular trafficking.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Impaired endocytic signaling has been observed during C9ORF72 mutated conditions in C9ORF72 ALS/FTD patients as well as the SH-SY5Y cell line model, suggesting that expression of C9ORF72 modulates endocytosis.
“Interestingly, the impaired endocytic signaling has been observed during C9ORF72 mutated conditions in C9ORF72 ALS/FTD patients as well as the SH-SY5Y cell line model, suggesting that the expression of C9ORF72 modulates endocytosis [172,173].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [172]
The “C9ORF72 regulates endocytosis in neuronal cell lines” section reports inhibited endocytosis after siRNA depletion of C9ORF72 in SH-SY5Y cells, supporting a role for its expression in endocytosis. The “Rab7 and Rab11 colocalize in C9ORF72 human spinal cord motor neurons” section reports increased colocalization in tissue from an ALS patient with the repeat expansion, suggesting possible trafficking dysregulation; it does not directly show impaired endocytosis in patients. The SH-SY5Y cells were depleted of C9ORF72, not described as carrying the mutation. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe C9orf72 protein belongs to the DENN family and binds the GTPases RAB7 and RAB11, which are involved in endosome maturation and recycling.
“The C9orf72 protein belongs to the DENN (differentially expressed in normal and neoplastic cells) family [143,144] and binds the GTPases RAB7 and RAB11, which are involved in endosome maturation and recycling [145].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [145]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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
Measurement of co‐localization of objects in dual‐colour confocal images
Manders, E. M. M., Verbeek, F. J., & Aten, J. A. (1993) · Journal of Microscopy · doi:10.1111/j.1365-2818.1993.tb03313.x · Cited by 2,132 · see citing works
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Kim, H. J., Kim, N. C., Wang, Y., Scarborough, E. A., Moore, J., Diaz, Z., MacLea, K. S., Freibaum, B. D., Li, S., Molliex, A., et al. (2013) · Nature · doi:10.1038/nature11922 · Cited by 1,476 · 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
Regulation of Small GTPases by GEFs, GAPs, and GDIs
Cherfils, J., & Zeghouf, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00003.2012 · Cited by 1,245 · see citing works
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
Feature-based prediction of non-classical and leaderless protein secretion
Bendtsen, J. D., Jensen, L. J., Blom, N., von HEIJNE, G., & Brunak, S. (2004) · Protein Engineering Design and Selection · doi:10.1093/protein/gzh037 · Cited by 1,179 · see citing works
Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
Deng, H.-X., Chen, W., Hong, S.-T., Boycott, K. M., Gorrie, G. H., Siddique, N., Yang, Y., Fecto, F., Shi, Y., Zhai, H., et al. (2011) · Nature · doi:10.1038/nature10353 · Cited by 1,174 · see citing works
Discovery of Atg5/Atg7-independent alternative macroautophagy
Nishida, Y., Arakawa, S., Fujitani, K., Yamaguchi, H., Mizuta, T., Kanaseki, T., Komatsu, M., Otsu, K., Tsujimoto, Y., & Shimizu, S. (2009) · Nature · doi:10.1038/nature08455 · Cited by 1,103 · see citing works
Rab7: A Key to Lysosome Biogenesis
Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J., & van Deurs, B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.467 · Cited by 1,084 · see citing works
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
Stress granules as crucibles of ALS pathogenesis
Li, Y. R., King, O. D., Shorter, J., & Gitler, A. D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302044 · Cited by 913 · see citing works
Role for Rab7 in maturation of late autophagic vacuoles
Jäger, S., Bucci, C., Tanida, I., Ueno, T., Kominami, E., Säftig, P., & Eskelinen, E. (2004) · Journal of Cell Science · doi:10.1242/jcs.01370 · Cited by 907 · see citing works
HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756 · see citing works
Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
Bosco, D. A., Morfini, G. A., Karabacak, M., Song, Y., Gros‐Louis, F., Pasinelli, P., Goolsby, H., Fontaine, B. A., Lemay, N., McKenna-Yasek, D. M., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2660 · Cited by 685 · see citing works
Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
Gutierrez, M. G., Munafó, D. B., Berón, W., & Colombo, M. I. (2004) · Journal of Cell Science · doi:10.1242/jcs.01114 · Cited by 680 · see citing works
Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis
Ferraiuolo, L., Kirby, J., Grierson, A. J., Sendtner, M., & Shaw, P. J. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.152 · Cited by 615 · see citing works
Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis
Wu, C.-H., Fallini, C., Ticozzi, N., Keagle, P. J., Sapp, P. C., Piotrowska, K., Lowe, P., Koppers, M., McKenna-Yasek, D. M., Baron, D. M., et al. (2012) · Nature · doi:10.1038/nature11280 · Cited by 603 · see citing works
Mechanisms of cross‐talk between the ubiquitin‐proteasome and autophagy‐lysosome systems
Korolchuk, V. I., Menzies, F. M., & Rubinsztein, D. C. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.047 · Cited by 565 · see citing works
LaMonte, B. H., Wallace, K. E., Holloway, B. A., Shelly, S. S., Ascaño, J., Tokito, M. K., Winkle, T. V., Howland, D., & Holzbaur, E. L. F. (2002) · Neuron · doi:10.1016/s0896-6273(02)00696-7 · Cited by 540 · see citing works
Snowden, J. S., Rollinson, S., Thompson, J. C., Harris, J. M., Stopford, C. L., Richardson, A. M. T., Jones, M., Gerhard, A., Davidson, Y. S., Robinson, A., et al. (2012) · Brain · doi:10.1093/brain/awr355 · Cited by 523 · see citing works
Bennett, E. J., Bence, N., Rajadas, J., & Kopito, R. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.021 · Cited by 509 · see citing works
Harrison, R. E., Bucci, C., Vieira, O. V., Schroer, T. A., & Grinstein, S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.18.6494-6506.2003 · Cited by 480 · see citing works
Targeting Rab GTPases to distinct membrane compartments
Pfeffer, S. R., & Aivazian, D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1500 · Cited by 462 · see citing works
Neuropathological background of phenotypical variability in frontotemporal dementia
Josephs, K. A., Hodges, J. R., Snowden, J. S., Mackenzie, I. R., Neumann, M., Mann, D. M. A., & Dickson, D. W. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0839-6 · Cited by 453 · see citing works
TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes
Longatti, A., Lamb, C. A., Razi, M., Yoshimura, S., Barr, F. A., & Tooze, S. A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201111079 · Cited by 386 · see citing works
Boeve, B. F., Boylan, K., Graff‐Radford, N. R., DeJesus‐Hernandez, M., Knopman, D. S., Pedraza, O., Vemuri, P., Jones, D. T., Lowe, V. J., Murray, M. E., et al. (2012) · Brain · doi:10.1093/brain/aws004 · Cited by 344 · see citing works
Fratta, P., Mizielinska, S., Nicoll, A. J., Zloh, M., Fisher, E., Parkinson, G. N., & Isaacs, A. M. (2012) · Scientific Reports · doi:10.1038/srep01016 · Cited by 335 · see citing works
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
hnRNP A1 Relocalization to the Stress Granules Reflects a Role in the Stress Response
Guil, S., Long, J. C., & Cáceres, J. F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00224-06 · Cited by 318 · see citing works
Autophagosome Formation Depends on the Small GTPase Rab1 and Functional ER Exit Sites
Zoppino, F. C. M., Militello, R. D., Slavin, I., Álvarez, C., & Colombo, M. I. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01086.x · Cited by 263 · see citing works
Rajagopal, R., Chen, Z.-Y., Lee, F. S., & Chao, M. V. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0010-04.2004 · Cited by 258 · see citing works
Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models
Armakola, M., Higgins, M., Figley, M. D., Barmada, S. J., Scarborough, E. A., Diaz, Z., Fang, X., Shorter, J., Krogan, N. J., Finkbeiner, S. M., et al. (2012) · Nature Genetics · doi:10.1038/ng.2434 · Cited by 250 · see citing works
Autophagy in Spinal Cord Motor Neurons in Sporadic Amyotrophic Lateral Sclerosis
Sasaki, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182160690 · Cited by 249 · see citing works
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
Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
Rothenberg, C., Srinivasan, D., Mah, L., Kaushik, S., Peterhoff, C. M., Ugolino, J., Fang, S., Cuervo, A. M., Nixon, R. A., & Monteiro, M. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq231 · Cited by 225 · see citing works
Hsiung, G. R., DeJesus-Hernandez, M., Feldman, H., Sengdy, P., Bouchard‐Kerr, P., Dwosh, E., Butler, R. K., Leung, B., Fok, A., Rutherford, N. J., et al. (2012) · Brain · doi:10.1093/brain/awr354 · Cited by 220 · see citing works
Frontotemporal dementia due toC9ORF72mutations
Sha, S. J., Takada, L. T., Rankin, K. P., Yokoyama, J. S., Rutherford, N. J., Fong, J. C., Khan, B. K., Karydas, A., Baker, M. C., DeJesus‐Hernandez, M., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e318268452e · Cited by 212 · see citing works
Spliceosome integrity is defective in the motor neuron diseases ALS and SMA
Tsuiji, H., Iguchi, Y., Furuya, A., Kataoka, A., Hatsuta, H., Atsuta, N., Tanaka, F., Hashizume, Y., Akatsu, H., Murayama, S., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201202303 · Cited by 206 · see citing works
Alsin Is a Rab5 and Rac1 Guanine Nucleotide Exchange Factor
Topp, J. D., Gray, N. W., Gerard, R. D., & Horazdovsky, B. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313504200 · Cited by 184 · see citing works
Brettschneider, J., Deerlin, V. M. V., Robinson, J. L., Kwong, L. K., Lee, E. B., Ali, Y., Safren, N., Monteiro, M. J., Toledo, J. B., Elman, L. B., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0970-z · Cited by 183 · see citing works
Aguilera, M. O., Berón, W., & Colombo, M. I. (2012) · Autophagy · doi:10.4161/auto.21459 · Cited by 166 · see citing works
Fuchs, E., Haas, A. K., Spooner, R. A., Yoshimura, S., Lord, J. M., & Barr, F. A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612068 · Cited by 161 · see citing works
Derby, M. C., Lieu, Z. Z., Brown, D. L., Stow, J. L., Goud, B., & Gleeson, P. A. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00563.x · Cited by 145 · see citing works
Self-citationLarge Scale Screening for Novel Rab Effectors Reveals Unexpected Broad Rab Binding Specificity*S
Fukuda, M., Kanno, E., Ishibashi, K., & Itoh, T. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700569-mcp200 · Cited by 140 · see citing works
Latonen, L., Moore, H. M., Bai, B., Jäämaa, S., & Laiho, M. (2010) · Oncogene · doi:10.1038/onc.2010.469 · Cited by 139 · see citing works
Hadano, S., Benn, S. C., Kakuta, S., Otomo, A., Sudo, K., Kunita, R., Suzuki-Utsunomiya, K., Mizumura, H., Shefner, J. M., Cox, G. A., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi440 · Cited by 138 · see citing works
Troakes, C., Maekawa, S., Wijesekera, L., Rogelj, B., Siklós, L., Bell, C., Smith, B., Newhouse, S., Vance, C., Johnson, L., et al. (2012) · Neuropathology · doi:10.1111/j.1440-1789.2011.01286.x · Cited by 124 · see citing works
Self-citationC9ORF72 repeat expansion in clinical and neuropathologic frontotemporal dementia cohorts
Dobson‐Stone, C., Hallupp, M., Bartley, L., Shepherd, C. E., Halliday, G. M., Schofield, P. R., Hodges, J. R., & Kwok, J. B. (2012) · Neurology · doi:10.1212/wnl.0b013e3182684634 · Cited by 117 · see citing works
A Novel Endocytic Recycling Signal Distinguishes Biological Responses of Trk Neurotrophin Receptors
Chen, Z.-Y., Ieraci, A., Tanowitz, M., & Lee, F. S. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0651 · Cited by 113 · see citing works
Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene
Meggouh, F., Bienfait, H. M. E., Weterman, M. A. J., de Visser, M., & Baas, F. (2006) · Neurology · doi:10.1212/01.wnl.0000240068.21499.f5 · Cited by 106 · see citing works
Janssens, J., Wils, H., Kleinberger, G., Joris, G., Cuijt, I., Groote, C. C., Broeckhoven, C. V., & Kumar‐Singh, S. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8427-5 · Cited by 105 · see citing works
Bekenstein, U., & Soreq, H. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.12.002 · Cited by 91 · see citing works
Thomas, M., Alegre‐Abarrategui, J., & Wade‐Martins, R. (2013) · Brain · doi:10.1093/brain/awt030 · Cited by 74 · see citing works
Sundaramoorthy, V., Walker, A. K., Yerbury, J. J., Soo, K. Y., Farg, M. A., Hoang, V., Zeineddine, R., Spencer, D. M. S., & Atkin, J. D. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1385-2 · Cited by 66 · see citing works
Self-citationOtomo, A., Pan, L., & Hadano, S. (2012) · Neurology Research International · doi:10.1155/2012/498428 · Cited by 60 · see citing works
King, A. E., Chung, R. S., Vickers, J. C., & Dickson, T. C. (2006) · The Journal of Comparative Neurology · doi:10.1002/cne.21053 · Cited by 58 · see citing works
Self-citationChronic Excitotoxin-Induced Axon Degeneration in a Compartmented Neuronal Culture Model
Hosie, K. A., King, A. E., Blizzard, C. A., Vickers, J. C., & Dickson, T. C. (2012) · ASN NEURO · doi:10.1042/an20110031 · Cited by 56 · see citing works
Self-citationTung, Y.-T., Hsu, W., Lee, H., Huang, W., & Liao, Y. (2010) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-010-9507-y · Cited by 49 · see citing works
Palmisano, R., Golfi, P., Heimann, P., Shaw, C. E., Troakes, C., Schmitt‐John, T., & Bartsch, J. W. (2011) · BMC Neuroscience · doi:10.1186/1471-2202-12-24 · Cited by 45 · see citing works
Dynein Dysfunction Induces Endocytic Pathology Accompanied by an Increase in Rab GTPases
Kimura, N., Inoue, M., Okabayashi, S., Ono, F., & Negishi, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.012625 · Cited by 41 · see citing works
Ubiquilin at a crossroads in protein degradation pathways
Rothenberg, C., & Monteiro, M. J. (2010) · Autophagy · doi:10.4161/auto.6.7.13118 · Cited by 40 · see citing works
Kittler, J. T., & Moss, S. J. (2006) · CRC Press eBooks · doi:10.1201/9780203486283 · Cited by 35 · see citing works
Low Dose Proteasome Inhibition Affects Alternative Splicing
Bieler, S., Hammer, E., Gesell-Salazar, M., Völker, U., Stangl, K., & Meiners, S. (2012) · Journal of Proteome Research · doi:10.1021/pr300435c · Cited by 11 · see citing works
FTD/ALS families are no longer orphaned
Swieten, J. C. V., & Grossman, M. (2012) · Neurology · doi:10.1212/wnl.0b013e318268471a · Cited by 4 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Manders, E.M.M., Verbeek, F.J. and Aten, J.A. (1993) Measurement of colocalization of objects in dual-color confocal images. J. Microsc-Oxford, 169, 375-382.
Cited by
Sorted by citations
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
Self-citationKlionsky, 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
Self-citationAutophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134 · see citing works
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
Compromised autophagy and neurodegenerative diseases
Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851 · see citing works
Lysosomes as a therapeutic target
Bonam, S. R., Wang, F., & Muller, S. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0036-1 · Cited by 764 · 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
ALS Genetics, Mechanisms, and Therapeutics: Where Are We Now?
Mejzini, R., Flynn, L. L., Pitout, I. L., Fletcher, S., Wilton, S. D., & Akkari, P. A. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01310 · Cited by 755 · see citing works
Haploinsufficiency leads to neurodegeneration in C9ORF72 ALS/FTD human induced motor neurons
Shi, Y., Lin, S., Staats, K. A., Li, Y., Chang, W.-H., Hung, S.-T., Hendricks, E., Linares, G. R., Wang, Y., Son, E. Y., et al. (2018) · Nature Medicine · doi:10.1038/nm.4490 · Cited by 566 · see citing works
Jiang, J., Zhu, Q., Gendron, T. F., Saberi, S., McAlonis-Downes, M., Seelman, A., Stauffer, J. E., Jafar-nejad, P., Drenner, K., Schulte, D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.006 · Cited by 536 · 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
The different autophagy degradation pathways and neurodegeneration
Fleming, A., Bourdenx, M., Fujimaki, M., Karabiyik, C., Krause, G. J., Lopez, A., Martín‐Segura, A., Puri, C., Scrivo, A., Skidmore, J., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.017 · Cited by 485 · see citing works
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
Antisense Oligonucleotide Therapies for Neurodegenerative Diseases
Bennett, C. F., Krainer, A. R., & Cleveland, D. W. (2019) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-070918-050501 · Cited by 353 · see citing works
Autophagy and neurodegeneration
Frake, R. A., Ricketts, T., Menzies, F. M., & Rubinsztein, D. C. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73944 · Cited by 332 · see citing works
Inflammation in ALS/FTD pathogenesis
McCauley, M. E., & Baloh, R. H. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1933-9 · Cited by 316 · see citing works
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
Alexander, A. G., Marfil, V., & Li, C. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00279 · Cited by 310 · see citing works
C9orf72 BAC Transgenic Mice Display Typical Pathologic Features of ALS/FTD
O’Rourke, J. G., Bogdanik, L., Muhammad, A. K. M. G., Gendron, T. F., Kim, K. J., Austin, A., Cady, J., Liu, E. Y., Zarrow, J., Grant, S., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.10.027 · Cited by 298 · see citing works
Endoplasmic reticulum stress and inflammation in the central nervous system
Sprenkle, N. T., Sims, S. G., Sánchez, C. L., & Meares, G. P. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0183-y · Cited by 299 · see citing works
Loss-of-function mutations in the <i>C9ORF72</i> mouse ortholog cause fatal autoimmune disease
Burberry, A., Suzuki, N., Wang, J.-Y., Moccia, R., Mordes, D. A., Stewart, M. H., Suzuki-Uematsu, S., Ghosh, S., Singh, A., Merkle, F. T., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf6038 · Cited by 269 · see citing works
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
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
Peters, O. M., Cabrera, G. T., Tran, H., Gendron, T. F., McKeon, J. E., Metterville, J., Weiss, A., Wightman, N., Salameh, J. S., Kim, J., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.11.018 · Cited by 259 · see citing works
on behalf of the BELNEU CONSORTIUM, Gijselinck, I., Van Mossevelde, S., van der Zee, J., Sieben, A., Engelborghs, S., De Bleecker, J., Ivanoiu, A., Deryck, O., Edbauer, D., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.159 · Cited by 242 · see citing works
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
A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy
Yang, M., Liang, C., Swaminathan, K., Herrlinger, S., Lai, F., Shiekhattar, R., & Chen, J.-F. (2016) · Science Advances · doi:10.1126/sciadv.1601167 · Cited by 238 · see citing works
Rab GTPases and Membrane Trafficking in Neurodegeneration
Kiral, F. R., Kohrs, F. E., Jin, E. J., & Hiesinger, P. R. (2018) · Current Biology · doi:10.1016/j.cub.2018.02.010 · Cited by 239 · see citing works
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
C9orf72 expansions in frontotemporal dementia and amyotrophic lateral sclerosis
Rohrer, J. D., Isaacs, A. M., Mizielinska, S., Mead, S., Lashley, T., Wray, S., Sidle, K. C. L., Fratta, P., Orrell, R. W., Hardy, J., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70233-9 · Cited by 234 · see citing works
Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 218 · see citing works
Motor Neuron Susceptibility in ALS/FTD
Ragagnin, A., Shadfar, S., Vidal, M., Jamali, M. S., & Atkin, J. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00532 · Cited by 216 · see citing works
Self-citationProsaposin facilitates sortilin-independent lysosomal trafficking of progranulin
Zhou, X., Sun, L., de Oliveira, F. M. B., Qi, X., Brown, W. J., Smolka, M. B., Sun, Y., & Hu, F. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502029 · Cited by 201 · see citing works
The expanding biology of the C9orf72 nucleotide repeat expansion in neurodegenerative disease
Haeusler, A. R., Donnelly, C. J., & Rothstein, J. D. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.38 · Cited by 202 · 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
“expressed in normal and neoplastic cells) family [143,144] and binds the GTPases RAB7 and RAB11, which are involved in endosome maturation and recycling [145].”
BackgroundLoss 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
ALS: A bucket of genes, environment, metabolism and unknown ingredients
Zufiría, M., Gil-Bea, F. J., Fernández‐Torrón, R., Poza, J. J., Muñoz-Blanco, J. L., Rojas‐García, R., Riancho, J., & de Munaín, A. L. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.05.004 · Cited by 192 · see citing works
C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling
Amick, J., Roczniak-Ferguson, A., & Ferguson, S. M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-01-0003 · Cited by 189 · see citing works
Frontotemporal dementia: latest evidence and clinical implications
Young, J. J., Lavakumar, M., Tampi, D. J., Balachandran, S., & Tampi, R. R. (2017) · Therapeutic Advances in Psychopharmacology · doi:10.1177/2045125317739818 · Cited by 183 · see citing works
Frontotemporal lobar degeneration
Grossman, M., Seeley, W. W., Boxer, A. L., Hillis, A. E., Knopman, D. S., Ljubenov, P. A., Miller, B., Piguet, O., Rademakers, R., Whitwell, J. L., et al. (2023) · Nature Reviews Disease Primers · doi:10.1038/s41572-023-00447-0 · Cited by 178 · see citing works
A complex of C9ORF72 and p62 uses arginine methylation to eliminate stress granules by autophagy
Chitiprolu, M., Jagow, C., Tremblay, V., Bondy‐Chorney, E., Paris, G., Savard, A., Palidwor, G., Barry, F. A., Zinman, L. H., Keith, J. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05273-7 · Cited by 179 · see citing works
Microglia and C9orf72 in neuroinflammation and ALS and frontotemporal dementia
Lall, D., & Baloh, R. H. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90607 · Cited by 175 · see citing works
Targeting autophagy, oxidative stress, and ER stress for neurodegenerative disease treatment
Esmaeili, Y., Yarjanli, Z., Paknia, F., Bidram, E., Łoś, M., Eshraghi, M., Klionsky, D. J., Ghavami, S., & Zarrabi, A. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.03.001 · Cited by 180 · see citing works
Rastogi, S., Sharma, V., Bharti, P. S., Rani, K., Modi, G. P., Nikolajeff, F. K., & Kumar, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010440 · Cited by 173 · 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
Remondelli, P., & Renna, M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00187 · Cited by 167 · see citing works
Laflamme, C., McKeever, P. M., Kumar, R., Schwartz, J., Kolahdouzan, M., Chen, C. X., You, Z., Benaliouad, F., Gileadi, O., McBride, H. M., et al. (2019) · eLife · doi:10.7554/elife.48363 · Cited by 155 · see citing works
Dissection of genetic factors associated with amyotrophic lateral sclerosis
Leblond, C. S., Kaneb, H., Dion, P. A., & Rouleau, G. A. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.04.013 · Cited by 163 · see citing works
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
Disrupted neuronal trafficking in amyotrophic lateral sclerosis
Burk, K., & Pasterkamp, R. J. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01964-7 · Cited by 162 · see citing works
Aoki, Y., Manzano, R., Lee, Y., Dafinca, R., Aoki, M., Douglas, A. G. L., Varela, M. A., Sathyaprakash, C., Scaber, J., Barbagallo, P., et al. (2017) · Brain · doi:10.1093/brain/awx024 · Cited by 159 · see citing works
Below the surface: The inner lives of TLR4 and TLR9
Marongiu, L., Gornati, L., Artuso, I., Zanoni, I., & Granucci, F. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mir1218-483rr · Cited by 155 · see citing works
Genetics of <scp>FTLD</scp> : overview and what else we can expect from genetic studies
Pottier, C., Ravenscroft, T. A., Sanchez‐Contreras, M., & Rademakers, R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13622 · Cited by 148 · see citing works
Endocytic membrane trafficking and neurodegenerative disease
Schreij, A. M. A., Fon, E. A., & McPherson, P. S. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2105-x · Cited by 153 · see citing works
C9ORF72 interaction with cofilin modulates actin dynamics in motor neurons
Sivadasan, R., Hornburg, D., Drepper, C., Frank, N., Jablonka, S., Hansel, A., Lojewski, X., Sterneckert, J. L., Hermann, A., Shaw, P. J., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4407 · Cited by 148 · see citing works
Neuroinflammation as a Factor of Neurodegenerative Disease: Thalidomide Analogs as Treatments
Jung, Y. J., Tweedie, D., Scerba, M. T., & Greig, N. H. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00313 · Cited by 154 · see citing works
Autophagy Dysregulation in ALS: When Protein Aggregates Get Out of Hand
Ramesh, N., & Pandey, U. B. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00263 · Cited by 150 · see citing works
Molecular and Cellular Mechanisms Affected in ALS
Gall, L. L., Anakor, E., Connolly, O., Vijayakumar, U. G., Duddy, W. J., & Duguez, S. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030101 · Cited by 147 · see citing works
C9orf72 deficiency promotes microglial-mediated synaptic loss in aging and amyloid accumulation
Lall, D., Lorenzini, I., Mota, T. A., Bell, S., Mahan, T. E., Ulrich, J. D., Davtyan, H., Rexach, J. E., Muhammad, A. K. M. G., Shelest, O., et al. (2021) · Neuron · doi:10.1016/j.neuron.2021.05.020 · Cited by 147 · see citing works
Macroautophagy in CNS health and disease
Griffey, C. J., & Yamamoto, A. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00588-3 · Cited by 144 · see citing works
Blokhuis, A. M., Koppers, M., Groen, E. J. N., van den Heuvel, D. M. A., Modigliani, S. D., Anink, J. J., Fumoto, K., van Diggelen, F., Snelting, A., Sodaar, P., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1575-8 · Cited by 139 · see citing works
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
Intercellular Spread of Protein Aggregates in Neurodegenerative Disease
Davis, A. A., Leyns, C. E. G., & Holtzman, D. M. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062636 · Cited by 131 · see citing works
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
Long Non-Coding RNA (lncRNA) Roles in Cell Biology, Neurodevelopment and Neurological Disorders
Aliperti, V., Skonieczna, J., & Cerase, A. (2021) · Non-Coding RNA · doi:10.3390/ncrna7020036 · Cited by 137 · see citing works
Hypermethylation of repeat expanded C9orf72 is a clinical and molecular disease modifier
Russ, J., Liu, E. Y., Wu, K., Neal, D., Suh, E. R., Irwin, D. J., McMillan, C. T., Harms, M. B., Cairns, N. J., Wood, E. M., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1365-0 · Cited by 128 · see citing works
Ratti, A., Gumina, V., Lenzi, P., Bossolasco, P., Fulceri, F., Volpe, C., Bardelli, D., Pregnolato, F., Maraschi, A., Fornai, F., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105051 · Cited by 128 · see citing works
Lattante, S., Ciura, S., Rouleau, G. A., & Kabashi, E. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.03.005 · Cited by 125 · see citing works
Pensalfini, A., Kim, S., Subbanna, S., Bleiwas, C., Goulbourne, C. N., Stavrides, P. H., Jiang, Y., Lee, J., Darji, S., Pawlik, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108420 · Cited by 125 · see citing works
Autophagy in Age-Associated Neurodegeneration
Metaxakis, A., Ploumi, C., & Tavernarakis, N. (2018) · Cells · doi:10.3390/cells7050037 · Cited by 121 · see citing works
Beckers, J., Tharkeshwar, A. K., & Damme, P. V. (2021) · Autophagy · doi:10.1080/15548627.2021.1872189 · Cited by 124 · see citing works
Frontotemporal Dementia, Where Do We Stand? A Narrative Review
Antonioni, A., Raho, E. M., Lopriore, P., Pace, A. P., Latino, R. R., Assogna, M., Mancuso, M., Gragnaniello, D., Granieri, E., Pugliatti, M., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411732 · Cited by 133 · see citing works
Nordin, A., Akimoto, C., Wuolikainen, A., Alstermark, H., Jonsson, P., Birve, A., Marklund, S. L., Graffmo, K. S., Forsberg, K., Brännström, T., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv064 · Cited by 120 · see citing works
Autophagosome dynamics in neurodegeneration at a glance
Wong, Y. C., & Holzbaur, E. L. F. (2015) · Journal of Cell Science · doi:10.1242/jcs.161216 · Cited by 116 · see citing works
Soo, K. Y., Halloran, M. A., Sundaramoorthy, V., Parakh, S., Toth, R. P., Southam, K. A., McLean, C., Lock, P., King, A. E., Farg, M. A., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1468-2 · Cited by 117 · see citing works
Self-citationRAB2 regulates the formation of autophagosome and autolysosome in mammalian cells
Ding, X., Jiang, X. M., Tian, R. L., Zhao, P., Lin, L., Wang, X., Chen, S., Zhu, Y., Mei, M., Bao, S., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1596478 · Cited by 117 · see citing works
STING trafficking as a new dimension of immune signaling
Jeltema, D., Abbott, K., & Yan, N. (2023) · The Journal of Experimental Medicine · doi:10.1084/jem.20220990 · Cited by 116 · see citing works
Jiang, S., & Bhaskar, K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.586731 · Cited by 113 · see citing works
Amyotrophic lateral sclerosis: Current perspectives from basic research to the clinic
Mancuso, R., & Navarro, X. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.004 · Cited by 116 · see citing works
Protein folding alterations in amyotrophic lateral sclerosis
Parakh, S., & Atkin, J. D. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.010 · Cited by 111 · see citing works
Self-citationCytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD
Khosravi, B., Hartmann, H., May, S., Möhl, C., Ederle, H., Michaelsen, M., Schludi, M. H., Dormann, D., & Edbauer, D. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw432 · Cited by 113 · 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
Stress granules at the intersection of autophagy and ALS
Monahan, Z. T., Shewmaker, F. P., & Pandey, U. B. (2016) · Brain Research · doi:10.1016/j.brainres.2016.05.022 · Cited by 105 · see citing works
Immunotherapies for Neurodegenerative Diseases
Mortada, I., Farah, R., Nabha, S. M., Ojcius, D. M., Fares, Y., Almawi, W. Y., & Sadier, N. S. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.654739 · Cited by 112 · see citing works
The genetics of amyotrophic lateral sclerosis: current insights
Kirby, J., Sultan, A. A., Waller, R., & Heath, P. R. (2016) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s84956 · Cited by 107 · see citing works
Iron and Neurodegeneration: Is Ferritinophagy the Link?
Biasiotto, G., Lorenzo, D. D., Archetti, S., & Zanella, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9473-y · Cited by 104 · see citing works
Disease Mechanisms ofC9ORF72Repeat ExpansionsPreprint
Gendron, T. F., & Petrucelli, L. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024224 · Cited by 101 · see citing works
Maharjan, N., Künzli, C., Buthey, K., & Saxena, S. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9850-1 · Cited by 99 · see citing works
Endocytosis regulates TDP-43 toxicity and turnover
Liu, G., Coyne, A. N., Pei, F., Vaughan, S., Chaung, M., Zarnescu, D. C., & Buchan, J. R. (2017) · Nature Communications · doi:10.1038/s41467-017-02017-x · Cited by 97 · see citing works
Gene Therapy for ALS—A Perspective
Cappella, M., Ciotti, C., Cohen-Tannoudji, M., & Biferi, M. G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184388 · Cited by 96 · see citing works
Rab GTPases: Switching to Human Diseases
Guadagno, N. A., & Progida, C. (2019) · Cells · doi:10.3390/cells8080909 · Cited by 95 · 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
Autophagy, Cellular Aging and Age-related Human Diseases
Cheon, S. Y., Kim, H. J., Rubinsztein, D. C., & Lee, J. E. (2019) · Experimental Neurobiology · doi:10.5607/en.2019.28.6.643 · Cited by 92 · see citing works
Autophagy receptor defects and ALS-FTLD
Majcher, V., Goode, A., James, V. H., & Layfield, R. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.01.002 · 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
Lee, Y., Baskaran, P., Gómez-Deza, J., Chen, H.-J., Nishimura, A. L., Smith, B. N., Troakes, C., Adachi, Y., Stepto, A., Petrucelli, L., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx350 · Cited by 90 · see citing works
Anđjus, P. R., Kosanović, M., Milicevic, K. D., Gautam, M., Vainio, S. J., Jagečić, D., Kozlova, E. N., Pivoriūnas, A., Chachques, J. C., Sakaj, M., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186859 · Cited by 90 · 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
- Authors
- 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., King, A. E., & Atkin, J. D.
- Affiliations
- Macquarie University (AU)
- University of Tasmania (AU)
- La Trobe University (AU)
- The University of Melbourne (AU)
- Corresponding author
- Atkin, Julie D.
- ORCID
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-02-18
- Volume
- 23
- Issue
- 13
- Pages
- 3579-3595
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC5886132
- OpenAlex
- W2102327538
- Cited by
- 478
- References
- 66
- Citations by year
- 2026: 8 · 2025: 22 · 2024: 25 · 2023: 35 · 2022: 24 · 2021: 58 · 2020: 52 · 2019: 39 · 2018: 39 · 2017: 50 · 2016: 57 · 2015: 50 · 2014: 19
- FWCI
- 38.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Human Molecular Genetics (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by-nc)
- eCite Digital Repository (University of Tasmania) (submittedVersion, cc-by-nc)
- Own your potential (DEAKIN) (submittedVersion)
- Figshare (submittedVersion, cc-by-nc)
- Funders
- Motor Neurone Disease Research Institute of Australia
- La Trobe University
- University of Wollongong
- Medical Research Council
- National Health and Medical Research Council (1004670, 1030513, 1006141)
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- C9orf72, amyotrophic lateral sclerosis, frontotemporal dementia, hexanucleotide repeat expansion, endosomal trafficking, Rab GTPases, autophagy, endocytosis, UBQLN2, hnRNP A1, HNRNPA2B1, stress granules, motor neurons, lysosomes, LC3, proteasome
- MeSH terms
- Autophagy-Related Proteins, C9orf72 Protein, rab7 GTP-Binding Proteins, rab11 GTP-Binding Proteins, Amyotrophic Lateral Sclerosis, Animals, Biological Transport, Humans, Proteins, Endosomes, Mass Spectrometry, rab GTP-Binding Proteins, Adaptor Proteins, Vesicular Transport, Heterogeneous-Nuclear Ribonucleoprotein Group A-B, Adaptor Proteins, Signal Transducing, Mice, Frontotemporal Dementia
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
