ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B)

A Mutation in the Vesicle-Trafficking Protein VAPB Causes Late-Onset Spinal Muscular Atrophy and Amyotrophic Lateral Sclerosis

Nishimura, A. L., Mitne-Neto, M., Silva, H. C. A., Richieri-Costa, A., Middleton, S., Cascio, D., Kok, F., Oliveira, J. R. M., Gillingwater, T., Webb, J., et al. (2004) · The American Journal of Human Genetics · doi:10.1086/425287 · Cited by 880

Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia

Skibinski, G., Parkinson, N. J., Brown, J. M., Chakrabarti, L., Lloyd, S. L., Hummerich, H., Nielsen, J. E., Hodges, J. R., Spillantini, M. G., Thusgaard, T., et al. (2005) · Nature Genetics · doi:10.1038/ng1609 · Cited by 822

Endosome-Associated Complex, ESCRT-II, Recruits Transport Machinery for Protein Sorting at the Multivesicular Body

Babst, M., Katzmann, D. J., Snyder, W. B., Wendland, B., & Emr, S. D. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00219-8 · Cited by 662

p62 Is a Common Component of Cytoplasmic Inclusions in Protein Aggregation Diseases

Zatloukal, K., Stumptner, C., Fuchsbichler, A., Heid, H., Schnoelzer, M., Kenner, L., Kleinert, R., Prinz, M., Aguzzi, A., & Denk, H. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64369-6 · Cited by 624

Frontal lobe dementia and motor neuron disease.

Neary, D., Snowden, J. S., Mann, D. M. A., Northen, B., Goulding, P., & MacDermott, N. (1990) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.53.1.23 · Cited by 437

Corticospinal tract degeneration in the progressive muscular atrophy variant of ALS

Ince, P. G., Evans, J., Knopp, M. V., Forster, G., Hamdalla, H. H. M., Wharton, S. B., & Shaw, P. J. (2003) · Neurology · doi:10.1212/01.wnl.0000058901.75728.4e · Cited by 303

ALS2, a novel guanine nucleotide exchange factor for the small GTPase Rab5, is implicated in endosomal dynamics

Otomo, A. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg184 · Cited by 250

Untitled work

Ince (1998) · doi:10.1046/j.1365-2990.1998.00108.x · Cited by 224

CHMP2B mutations are not a common cause of frontotemporal lobar degeneration

Cannon, A. D., Baker, M., Boeve, B. F., Josephs, K. A., Knopman, D. S., Petersen, R. C., Parisi, J. E., Dickison, D., Adamson, J. L., Snowden, J. S., et al. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.12.056 · Cited by 62

Disease penetrance in amyotrophic lateral sclerosis associated with mutations in the SOD1 gene

Andersen, P. M., Restagno, G., Stewart, H. G., & Chiò, A. (2004) · Annals of Neurology · doi:10.1002/ana.10850 · Cited by 25

GISP binding to TSG101 increases GABAB receptor stability by down‐regulating ESCRT‐mediated lysosomal degradation

Kantamneni, S., Holman, D., Wilkinson, K. A., Corrêa, S. A. L., Feligioni, M., Ogden, S. J., Fraser, W. D., Nishimune, A., & Henley, J. M. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05580.x · Cited by 30

Biological Spectrum of Amyotrophic Lateral Sclerosis PrionsPreprint

Polymenidou, M., & Cleveland, D. W. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024133 · Cited by 29

Amyotrophic Lateral Sclerosis Genetic Studies

He, J., Mangelsdorf, M., Fan, D., Bartlett, P. F., & Brown, M. A. (2014) · The Neuroscientist · doi:10.1177/1073858414555404 · Cited by 30

Neuronal activity regulates DROSHA via autophagy in spinal muscular atrophy

Gonçalves, I. D. C. G., Brecht, J., Thelen, M. P., Rehorst, W. A., Peters, M., Lee, H. J., Motameny, S., Torres‐Benito, L., Ebrahimi‐Fakhari, D., Kononenko, N. L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-26347-y · Cited by 29

The functional analysis of the CHMP2B missense mutation associated with neurodegenerative diseases in the endo-lysosomal pathway

Han, J. H., Ryu, H.-H., Jun, M.-H., Jang, D., & Lee, J. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.041 · Cited by 32

Gene expression analysis reveals early dysregulation of disease pathways and links Chmp7 to pathogenesis of spinal and bulbar muscular atrophy

Malik, B., Devine, H. E., Patani, R., Spada, A. R. L., Hanna, M. G., & Greensmith, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-40118-3 · Cited by 29

CHMP2B mutations are rare in French families with frontotemporal lobar degeneration

Ghanim, M., Guillot‐Noël, L., Pasquier, F., Jornéa, L., Deramecourt, V., Dubois, B., Ber, I. L., & Brice, A. (2010) · Journal of Neurology · doi:10.1007/s00415-010-5655-8 · Cited by 30

Delineating the relationship between amyotrophic lateral sclerosis and frontotemporal dementia: Sequence and structure-based predictions

Kumar, V., Islam, A., Hassan, M. I., & Ahmad, F. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.06.011 · Cited by 29

Proteinopathies as Hallmarks of Impaired Gene Expression, Proteostasis and Mitochondrial Function in Amyotrophic Lateral Sclerosis

Benson, B. C., Shaw, P. J., Azzouz, M., Highley, J. R., & Hautbergue, G. M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.783624 · Cited by 30

The converging roles of sequestosome-1/p62 in the molecular pathways of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)

Davidson, J. M., Chung, R. S., & Lee, A. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105653 · Cited by 29

Neuronal Functions of ESCRTs

Lee, J., & Gao, F. (2012) · Experimental Neurobiology · doi:10.5607/en.2012.21.1.9 · Cited by 29

Alix and ALG-2 make a link between endosomes and neuronal death

Mahul‐Mellier, A., Strappazzon, F., Chatellard, C., Blot, B., Beal, D. M., Torch, S., Hemming, F. J., Petiot, A., Verna, J., Fraboulet, S., et al. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370200 · Cited by 30

Alzheimer's Disease and the “Valley of Death”: Not Enough Guidance from Human Brain Tissue?

Beach, T. G. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129020 · Cited by 28

Pathogenic Genome Signatures That Damage Motor Neurons in Amyotrophic Lateral Sclerosis

Yousefian-Jazi, A., Seol, Y., Kim, J., Ryu, H. L., Lee, J.-H., & Ryu, H. (2020) · Cells · doi:10.3390/cells9122687 · Cited by 29

CHMP2B regulates TDP-43 phosphorylation and cytotoxicity independent of autophagy via CK1

Deng, X., Sun, X., Yue, W., Duan, Y., Hu, R., Zhang, K., Ni, J., Cui, J., Wang, Q., Chen, Y., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202103033 · Cited by 29

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Grasso, M., Piscopo, P., Crestini, A., Confaloni, A., & Denti, M. A. (2015) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-0348-0955-9_7 · Cited by 26

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Fontana, F., Siva, K., & Denti, M. A. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00009 · Cited by 30

Vps34 regulates myofibril proteostasis to prevent hypertrophic cardiomyopathy

Kimura, H., Eguchi, S., Sasaki, J., Kuba, K., Nakanishi, H., Takasuga, S., Yamazaki, M., Goto, A., Watanabe, H., Itoh, H., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.89462 · Cited by 26

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Chandía-Cristi, A., Rapuri, S., & Coyne, A. N. (2023) · FEBS Letters · doi:10.1002/1873-3468.14729 · Cited by 29

Elevated NLRP3 Inflammasome Activation Is Associated with Motor Neuron Degeneration in ALS

Cihankaya, H., Bader, V., Winklhofer, K. F., Vorgerd, M., Matschke, J., Stahlke, S., Theiß, C., & Matschke, V. (2024) · Cells · doi:10.3390/cells13120995 · Cited by 28

Endosomal sorting related protein CHMP2B is localized in Lewy bodies and glial cytoplasmic inclusions in α-synucleinopathy

Tanikawa, S., Mori, F., Tanji, K., Kakita, A., Takahashi, H., & Wakabayashi, K. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.08.035 · Cited by 27

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Udine, E., Jain, A., & van Blitterswijk, M. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00593-1 · Cited by 27

The handbook of Alzheimer's disease and other dementias

Budson, A. E., & Kowall, N. W. (2014) · Cited by 25

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Perri, E. R., Parakh, S., & Atkin, J. D. (2016) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2016.1254197 · Cited by 26

Component Interaction of ESCRT Complexes Is Essential for Endocytosis-Dependent Growth, Reproduction, DON Production and Full Virulence in Fusarium graminearum

Xie, Q., Chen, A., Zhang, Y., Yuan, M., Xie, W., Zhang, C., Zheng, W., Wang, Z., Li, G., & Zhou, J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00180 · Cited by 23

Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases

Cascella, R., Fani, G., Bigi, A., Chiti, F., & Cecchi, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153685 · Cited by 25

Neuroprotective activity of ursodeoxycholic acid in CHMP2B models of frontotemporal dementia

West, R. J. H., Ugbode, C., Fort‐Aznar, L., & Sweeney, S. T. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105047 · Cited by 27

Motor and Sensory Deficits in the teetering Mice Result from Mutation of the ESCRT Component HGS

Watson, J. A., Bhattacharyya, B. J., Vaden, J. H., Wilson, J. A., Icyuz, M., Howard, A. D., Phillips, E., DeSilva, T. M., Siegal, G. P., Bean, A. J., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005290 · Cited by 24

PIKfyve mediates the motility of late endosomes and lysosomes in neuronal dendrites

Tsuruta, F., & Dolmetsch, R. E. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.07.021 · Cited by 23

Toward precision medicine in amyotrophic lateral sclerosis.

Zou, Z., Liu, C.-Y., Che, C., & Huang, H. (2016) · PubMed · doi:10.3978/j.issn.2305-5839.2016.01.16 · Cited by 24

ALS Yeast Models—Past Success Stories and New Opportunities

Gregorio, S. E. D., & Duennwald, M. L. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00394 · Cited by 27

Is it accurate to classify ALS as a neuromuscular disorder?

van Es, M. A., Goedee, H. S., Westeneng, H., Nijboer, T. C. W., & van den Berg, L. H. (2020) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2020.1806061 · Cited by 24

The many ways to frontotemporal degeneration and beyond

Bugiani, O. (2007) · Neurological Sciences · doi:10.1007/s10072-007-0829-6 · Cited by 23

Frontotemporal Lobar Degeneration with Ubiquitin-Positive Inclusions: A Molecular Genetic Update

van der Zee, J., Gijselinck, I., Pirici, D. N., Kumar‐Singh, S., Cruts, M., & Broeckhoven, C. V. (2007) · Neurodegenerative Diseases · doi:10.1159/000101847 · Cited by 23

Gene therapy breakthroughs in ALS: a beacon of hope for 20% of ALS patients

Xie, Q., Li, K., Chen, Y., Li, Y., Jiang, W., Cao, W., Yu, H., Fan, D., & Deng, B. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00477-6 · Cited by 27

Frontotemporal Dementia: From Mendelian Genetics Towards Genome Wide Association Studies

Ferrari, R., Hardy, J., & Momeni, P. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9635-y · Cited by 23

Clinical phenotypes and genetic biomarkers of FTLD

Galimberti, D., & Scarpini, E. A. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0804-0 · Cited by 23

Meta-analysis of Genetic Modifiers Reveals Candidate Dysregulated Pathways in Amyotrophic Lateral Sclerosis

Yanagi, K. S., Wu, Z. J., Amaya, J., Chapkis, N., Duffy, A., Hajdarovic, K. H., Held, A., Mathur, A. D., Russo, K., Ryan, V. H., et al. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.10.033 · Cited by 22

Frontotemporal lobar degeneration through loss of progranulin function

Goedert, M., & Spillantini, M. G. (2006) · Brain · doi:10.1093/brain/awl291 · Cited by 23

New molecular diagnostic trends and biomarkers for amyotrophic lateral sclerosis

Pampalakis, G., Mitropoulos, K. A., Xiromerisiou, G., Dardiotis, E., Deretzi, G., Anagnostouli, M. C., Κάτσιλα, Θ., Rentzos, M., & Patrinos, G. P. (2018) · Human Mutation · doi:10.1002/humu.23697 · Cited by 20

Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degenerations: Similarities in Genetic Background

Parobková, E., & Matěj, R. (2021) · Diagnostics · doi:10.3390/diagnostics11030509 · Cited by 25

Lysosomal TRPML1 Channel: Implications in Cardiovascular and Kidney Diseases

Li, G., & Li, P. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-4254-8_13 · Cited by 22

Nuclear pore dysfunction and disease: a complex opportunity

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

Localization of CHMP2B ‐immunoreactivity in the brainstem of Lewy body disease

Kurashige, T., Takahashi, T., Yamazaki, Y., Hiji, M., Izumi, Y., Yamawaki, T., & Matsumoto, M. (2012) · Neuropathology · doi:10.1111/j.1440-1789.2012.01346.x · Cited by 21

Need an ESCRT for autophagosomal maturation?

Manil-Ségalen, M., Lefebvre, C., Culetto, E., & Legouis, R. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.21522 · Cited by 21

Phenocopy or variant: a longitudinal study of very slowly progressive frontotemporal dementia

Brodtmann, A. G., Cowie, T., McLean, C., & Darby, D. (2013) · BMJ Case Reports · doi:10.1136/bcr-2012-008077 · Cited by 22

High-Throughput Genetic Testing in ALS: The Challenging Path of Variant Classification Considering the ACMG Guidelines

Lattante, S., Marangi, G., Doronzio, P. N., Conte, A., Bisogni, G., Zollino, M., & Sabatelli, M. (2020) · Genes · doi:10.3390/genes11101123 · Cited by 21

Mutational analysis of familial and sporadic amyotrophic lateral sclerosis withOPTNmutations in Japanese population

Naruse, H., Takahashi, Y., Kihira, T., Yoshida, S., Kokubo, Y., Kuzuhara, S., Ishiura, H., Amagasa, M., Murayama, S., Tsuji, S., et al. (2012) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482968.2012.684213 · Cited by 20

TDP43 ribonucleoprotein granules: physiologic function to pathologic aggregates

Corbet, G. A., Wheeler, J. R., Parker, R., & Weskamp, K. (2021) · RNA Biology · doi:10.1080/15476286.2021.1963099 · Cited by 21

Linear Polyubiquitin Chain Modification of TDP-43-Positive Neuronal Cytoplasmic Inclusions in Amyotrophic Lateral Sclerosis

Nakayama, Y., Tsuji, K., Ayaki, T., Mori, M., Tokunaga, F., & Ito, H. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlz135 · Cited by 18

What Can Machine Learning Approaches in Genomics Tell Us about the Molecular Basis of Amyotrophic Lateral Sclerosis?

Vasilopoulou, C., Morris, A. P., Giannakopoulos, G., Duguez, S., & Duddy, W. J. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10040247 · Cited by 18

Mutations in CHMP2B are not a cause of frontotemporal lobar degeneration in Finnish patients

Kaivorinne, A.-L., Krüger, J., Udd, B., Majamaa, K., & Remes, A. M. (2010) · European Journal of Neurology · doi:10.1111/j.1468-1331.2010.03028.x · Cited by 23

Bi-allelic variants in SNF8 cause a disease spectrum ranging from severe developmental and epileptic encephalopathy to syndromic optic atrophy

Brügger, M., Lauri, A., Zhen, Y., Gramegna, L. L., Zott, B., Sekulić, N., Fasano, G., Kopajtich, R., Cordeddu, V., Radio, F. C., et al. (2024) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2024.02.005 · Cited by 17

The Use of Stem Cells to Model Amyotrophic Lateral Sclerosis and Frontotemporal Dementia: From Basic Research to Regenerative Medicine

Hedges, E. C., Mehler, V. J., & Nishimura, A. L. (2016) · Stem Cells International · doi:10.1155/2016/9279516 · Cited by 19

Ik2/TBK1 and Hook/Dynein, an adaptor complex for early endosome transport, are genetic modifiers of FTD-associated mutant CHMP2B toxicity in Drosophila

Lu, Y., West, R. J. H., Pons, M., Sweeney, S. T., & Gao, F. (2020) · Scientific Reports · doi:10.1038/s41598-020-71097-5 · Cited by 19

Heterogeneity in motoneuron disease

Lambrechts, D., Robberecht, W., & Carmeliet, P. (2007) · Trends in Neurosciences · doi:10.1016/j.tins.2007.07.002 · Cited by 18

No association of chromatin-modifying protein 2B with sporadic frontotemporal dementia

Schumacher, A., Friedrich, P., Diehl‐Schmid, J., Ibach, B., Eisele, T., Laws, S. M., Förstl, H., Kurz, A., & Riemenschneider, M. J. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.07.016 · Cited by 18

Oligodendroglial deletion of ESCRT‐I component TSG101 causes spongiform encephalopathy

Walker, W. P., Oehler, A., Edinger, A. L., Wagner, K., & Gunn, T. M. (2016) · Biology of the Cell · doi:10.1111/boc.201600014 · Cited by 18

Effect of tau-pathology on charged multivesicular body protein 2b (CHMP2B)

Midani-Kurçak, J. S., Dinekov, M., Puladi, B., Arzberger, T., & Köhler, C. N. (2018) · Brain Research · doi:10.1016/j.brainres.2018.11.008 · Cited by 17

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de Lago, E., Moreno‐Martet, M., Espejo‐Porras, F., & Fernández‐Ruíz, J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-417041-4.00005-9 · Cited by 17

Novel Missense Mutation in Charged Multivesicular Body Protein 2B in a Patient With Frontotemporal Dementia

Ferrari, R., Kapogiannis, D., Huey, E. D., Grafman, J. H., Hardy, J., & Momeni, P. (2010) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0b013e3181df20c7 · Cited by 17

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Burrell, J. R., & Hodges, J. R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091513 · Cited by 16

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

Genetic architecture of amyotrophic lateral sclerosis: a comprehensive review

Yuan, L., Yang, Y., Guo, Y., & Deng, H. (2025) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2025.05.008 · Cited by 18

Demencia frontotemporal variante conductual: biomarcadores, una aproximación a la enfermedad

Fernández‐Matarrubia, M., Matías-Guiu, J. A., Moreno‐Ramos, T., & Matías‐Guiu, J. (2013) · Neurología · doi:10.1016/j.nrl.2013.03.002 · Cited by 17

Nuclear and degradative functions of the ESCRT-III pathway: implications for neurodegenerative disease

Keeley, O., & Coyne, A. N. (2024) · Nucleus · doi:10.1080/19491034.2024.2349085 · Cited by 16

Rab-dependent cellular trafficking and amyotrophic lateral sclerosis

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

Axonal transport of Hrs is activity dependent and facilitates synaptic vesicle protein degradation

Birdsall, V., Kirwan, K., Zhu, M. J., Imoto, Y., Wilson, S. M., Watanabe, S., & Waites, C. L. (2022) · Life Science Alliance · doi:10.26508/lsa.202000745 · Cited by 16

Endocytic regulation of alkali metal transport proteins in mammals, yeast and plants

Mulet, J. M., Llopis-Torregrosa, V., Primo, C., Marqués, M. C., & Yenush, L. (2013) · Current Genetics · doi:10.1007/s00294-013-0401-2 · Cited by 14

Association between survivor motor neuron 2 (SMN2) gene homozygous deletion and sporadic lower motor neuron disease in a Korean population.

Kim, J., Lee, S.-G., Choi, Y., Kang, S., Lee, J.-B., Choi, J. R., & Lee, K. (2010) · PubMed · Cited by 14

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Galimberti, D., & Scarpini, E. A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-407824-6.00006-9 · Cited by 15

Biomarkers: a new approach to behavioural variant frontotemporal dementia

Fernández‐Matarrubia, M., Matías‐Guiu, J. A., Moreno‐Ramos, T., & Matías‐Guiu, J. (2014) · Neurología (English Edition) · doi:10.1016/j.nrleng.2013.03.007 · Cited by 13

Expression of mutant CHMP2B, an ESCRT‐III component involved in frontotemporal dementia, causes eye deformities due to Notch misregulation in Drosophila

Cheruiyot, A., Lee, J., Gao, F., & Ahmad, S. T. (2013) · The FASEB Journal · doi:10.1096/fj.13-234138 · Cited by 13

Neuropathology of Hereditary Forms of Frontotemporal Dementia and Parkinsonism

Muñoz, D. G., & Ferrer, I. (2008) · Handbook of clinical neurology · doi:10.1016/s0072-9752(07)01237-7 · Cited by 14

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

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

Transactive response DNA-binding protein 43 is enriched at the centrosome in human cells

Bodin, A., Greibill, L., Gouju, J., Letournel, F., Pozzi, S., Julien, J., Renaud, L., Bohl, D., Millecamps, S., Verny, C., et al. (2023) · Brain · doi:10.1093/brain/awad228 · Cited by 13

A comparative bioinformatic analysis of C9orf72

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

Endosomal sorting complexes required for ESCRTing cells toward death during neurogenesis, neurodevelopment and neurodegeneration

Kaul, Z., & Chakrabarti, O. (2018) · Traffic · doi:10.1111/tra.12569 · Cited by 12

CHMP2B promotes CHMP7 mediated nuclear pore complex injury in sporadic ALS

Keeley, O., Mendoza, E., Menon, D., & Coyne, A. N. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01916-7 · Cited by 11

Autophagy Dysfunction and Neurodegeneration: Where Does It Go Wrong?

Oettinger, D., & Yamamoto, A. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169219 · Cited by 10

ALS-associated genes display CNS expression in the developing zebrafish

Laboissonniere, L. A., Smith, C. L., Mesenbrink-Sainz, J., Chowdhury, R., Burney, A., Lang, M., Sierra, M., Stark, A., Maldonado-Casalduc, G., Muller, M., et al. (2018) · Gene Expression Patterns · doi:10.1016/j.gep.2018.08.003 · Cited by 11

Motoneuron Disease

Sendtner, M. (2014) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-45106-5_15 · Cited by 11

In vitro methods in autophagy research: Applications in neurodegenerative diseases and mood disorders

Sánchez-Vidaña, D. I., Li, J., Abokyi, S., Chan, J. N.-M., Ngai, S. P. C., & Lau, B. W.-M. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1168948 · Cited by 12

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Theunissen, F., Flynn, L. L., Iacoangeli, A., Khleifat, A. A., Al‐Chalabi, A., Giordano, J. J., Strømme, M., & Akkari, P. A. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00890-5 · Cited by 12

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