Restoration of histone acetylation ameliorates disease and metabolic abnormalities in a FUS mouse model
Open accessAbstract
Dysregulation of epigenetic mechanisms is emerging as a central event in neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS). In many models of neurodegeneration, global histone acetylation is decreased in the affected neuronal tissues. Histone acetylation is controlled by the antagonistic actions of two protein families -the histone acetyltransferases (HATs) and the histone deacetylases (HDACs). Drugs inhibiting HDAC activity are already used in the clinic as anti-cancer agents. The aim of this study was to explore the therapeutic potential of HDAC inhibition in the context of ALS. We discovered that transgenic mice overexpressing wild-type FUS ("Tg FUS+/+"), which recapitulate many aspects of human ALS, showed reduced global histone acetylation and alterations in metabolic gene expression, resulting in a dysregulated metabolic homeostasis. Chronic treatment of Tg FUS+/+ mice with ACY-738, a potent HDAC inhibitor that can cross the blood-brain barrier, ameliorated the motor phenotype and substantially extended the life span of the Tg FUS+/+ mice. At the molecular level, ACY-738 restored global histone acetylation and metabolic gene expression, thereby re-establishing metabolite levels in the spinal cord. Taken together, our findings link epigenetic alterations to metabolic dysregulation in ALS pathology, and highlight ACY-738 as a potential therapeutic strategy to treat this devastating disease.
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Genetic knockdown and pharmacological inhibition of HDACs ameliorate ALS pathology in different ALS models.
“Notably, genetic knockdown and pharmacological inhibition of HDACs have been shown to ameliorate ALS pathology in different ALS models.341–344”
From Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases (2024) · cites this paper as [341]
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STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709 · see citing works
Gene Ontology: tool for the unification of biology
Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D., Butler, H., Cherry, J. M., Davis, A. P., Dolinski, K., Dwight, S. S., Eppig, J. T., et al. (2000) · Nature Genetics · doi:10.1038/75556 · Cited by 43,206 · see citing works
Salmon provides fast and bias-aware quantification of transcript expression
Patro, R., Duggal, G., Love, M. I., Irizarry, R. A., & Kingsford, C. (2017) · Nature Methods · doi:10.1038/nmeth.4197 · Cited by 12,700 · see citing works
McCarthy, D. J., Chen, Y., & Smyth, G. K. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks042 · Cited by 5,195 · see citing works
Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6
Vance, C. A., Rogelj, B., Hortobágyi, T., Vos, K. J. D., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B. N., Ruddy, D., Wright, P. D., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,531 · see citing works
Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis
Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J. M., Kasarskis, E. J., Munsat, T. L., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,526 · see citing works
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · see citing works
A Controlled Trial of Riluzole in Amyotrophic Lateral Sclerosis
Bensimon, G., Lacomblez, L., & Meininger, V. (1994) · New England Journal of Medicine · doi:10.1056/nejm199403033300901 · Cited by 2,239 · see citing works
Mi, H., Huang, X., Muruganujan, A., Tang, H., Mills, C., Kang, D. S., & Thomas, P. D. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1138 · Cited by 1,985 · see citing works
Expansion of the Gene Ontology knowledgebase and resources
The Gene Ontology Consortium (2017) · Nucleic Acids Research · doi:10.1093/nar/gkw1108 · Cited by 1,850 · see citing works
State of play in amyotrophic lateral sclerosis genetics
Renton, A. E., Chiò, A., & Traynor, B. J. (2013) · Nature Neuroscience · doi:10.1038/nn.3584 · Cited by 1,563 · see citing works
Histone Deacetylase Inhibitors as Anticancer Drugs
Eckschlager, T., Plch, J., Stiborova, M., & Hrabeta, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071414 · Cited by 1,206 · see citing works
Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription
Wang, X., Arai, S., Song, X., Reichart, D. R., Du, K., Pascual, G., Tempst, P., Rosenfeld, M. G., Glass, C. K., & Kurokawa, R. (2008) · Nature · doi:10.1038/nature06992 · Cited by 988 · see citing works
Histone acetylation: a switch between repressive and permissive chromatin
Eberharter, A., & Becker, P. B. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf053 · Cited by 944 · see citing works
Abe, K., Aoki, M., Tsuji, S., Itoyama, Y., Sobue, G., Togo, M., Hamada, C., Tanaka, M., Akimoto, M., Nakamura, K., et al. (2017) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30115-1 · Cited by 942 · see citing works
Spandidos, A., Wang, X., Wang, H., & Seed, B. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1005 · Cited by 900 · see citing works
Proteome-wide identification of ubiquitin interactions using UbIA-MS
Zhang, X.-F., Smits, A. H., van Tilburg, G. B. A., Ovaa, H., Huber, W. K., & Vermeulen, M. (2018) · Nature Protocols · doi:10.1038/nprot.2017.147 · Cited by 813 · see citing works
MicroRNA-206 Delays ALS Progression and Promotes Regeneration of Neuromuscular Synapses in Mice
Williams, A. H., Valdez, G., Moresi, V., Qi, X., McAnally, J., Elliott, J. L., Bassel‐Duby, R., Sanes, J. R., & Olson, E. N. (2009) · Science · doi:10.1126/science.1181046 · Cited by 738 · see citing works
A new subtype of frontotemporal lobar degeneration with FUS pathology
Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., & Mackenzie, I. R. A. (2009) · Brain · doi:10.1093/brain/awp214 · Cited by 722 · see citing works
Cholesterol metabolism and homeostasis in the brain
Zhang, J., & Liu, Q. (2015) · Protein & Cell · doi:10.1007/s13238-014-0131-3 · Cited by 686 · see citing works
Mice Lacking Histone Deacetylase 6 Have Hyperacetylated Tubulin but Are Viable and Develop Normally
Zhang, Y., Kwon, S., Yamaguchi, T., Cubizolles, F., Rousseaux, S., Kneissel, M., Cao, C., Li, N., Cheng, H.-L., Chua, K., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01154-06 · Cited by 559 · cited 1× · see citing works
“First, we investigated the consequences of genetic removal of Hdac6 on the disease phenotype by crossbreeding the Tg FUS+/+ mice with Hdac6 knock-out (KO) mice [79].”
BackgroundLiu, L., MacKenzie, K. R., Putluri, N., Maletić-Savatić, M., & Bellen, H. J. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.024 · Cited by 556 · see citing works
d’Ydewalle, C. V. O., Krishnan, J., Chiheb, D., Damme, P. V., Irobi, J., Kozikowski, A. P., Berghe, P. V., Timmerman, V., Robberecht, W., & Bosch, L. V. D. (2011) · Nature Medicine · doi:10.1038/nm.2396 · Cited by 448 · see citing works
HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis
Saha, R. N., & Pahan, K. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401769 · Cited by 439 · see citing works
Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons
Wang, W., Pan, L., Su, S. C., Quinn, E. J., Sasaki, M., Jimenez, J., Mackenzie, I. R., Huang, E. J., & Tsai, L. (2013) · Nature Neuroscience · doi:10.1038/nn.3514 · Cited by 433 · see citing works
The genetics and neuropathology of amyotrophic lateral sclerosis
Al‐Chalabi, A., Jones, A., Troakes, C., King, A., Al‐Sarraj, S., & van den Berg, L. H. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1022-4 · Cited by 396 · see citing works
HDAC6 inhibition reverses axonal transport defects in motor neurons derived from FUS-ALS patients
Guo, W., Naujock, M., Fumagalli, L., Vandoorne, T., Baatsen, P., Boon, R., Ordovás, L., Patel, A., Welters, M., Vanwelden, T., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00911-y · Cited by 373 · see citing works
Self-citationRyu, H., Smith, K., Camelo, S. I., Carreras, I., Lee, J., Iglesias, A. H., Dangond, F., Cormier, K. A., Cudkowicz, M. E., H. Brown, R., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03077.x · Cited by 353 · see citing works
Deng, H., Zhai, H., Bigio, E. H., Yan, J., Fecto, F., Ajroud, K., Mishra, M., Ajroud‐Driss, S., Heller, S., Sufit, R. L., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22051 · Cited by 353 · see citing works
Trichostatin A increases SMN expression and survival in a mouse model of spinal muscular atrophy
Avila, A. M., Burnett, B. G., Taye, A. A., Gabanella, F., Knight, M. A., Hartenstein, P., Cizman, Z., Prospero, N. A. D., Pellizzoni, L., Fischbeck, K. H., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29562 · Cited by 350 · see citing works
Critical loss of CBP/p300 histone acetylase activity by caspase‐6 during neurodegeneration
Rouaux, C., Jokic, N., Mbebi, C., Boutillier, S., Loeffler, J., & Boutillier, A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg615 · Cited by 302 · see citing works
Thomas, E. A., Coppola, G., Desplats, P., Tang, B., Soragni, E., Burnett, R., Gao, F., Fitzgerald, K. M., Borok, J. F., Herman, D., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804249105 · Cited by 291 · see citing works
Mitchell, J. C., McGoldrick, P., Vance, C. A., Hortobágyi, T., Sreedharan, J., Rogelj, B., Tudor, E. L., Smith, B. N., Klasen, C., Miller, C. C. J., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1043-z · Cited by 290 · see citing works
Liu, Q., Trotter, J., Zhang, J., Peters, M. M., Cheng, H., Bao, J., Han, X., Weeber, E. J., & Bu, G. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4067-10.2010 · Cited by 268 · see citing works
Energy metabolism in ALS: an underappreciated opportunity?
Vandoorne, T., Bock, K. D., & Bosch, L. V. D. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1835-x · Cited by 260 · see citing works
Loss of astrocyte cholesterol synthesis disrupts neuronal function and alters whole-body metabolism
Ferris, H. A., Perry, R. J., Moreira, G. V., Shulman, G. I., Horton, J. D., & Kahn, C. R. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620506114 · Cited by 246 · cited 1× · see citing works
“Disturbances in either the synthesis, transport, or turnover of lipids were shown to trigger synapse loss and neurodegeneration [10, 23, 25, 35, 36].”
BackgroundAmyotrophic lateral sclerosis: mechanisms and therapeutics in the epigenomic era
Paez-Colasante, X., Figueroa‐Romero, C., Sakowski, S. A., Goutman, S. A., & Feldman, E. L. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.57 · Cited by 224 · see citing works
SAHA ameliorates the SMA phenotype in two mouse models for spinal muscular atrophy
Rießland, M., Ackermann, B., Förster, A., Jakubik, M., Hauke, J., Garbes, L., Fritzsche, I., Mende, Y., Blümcke, I., Hahnen, E., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq023 · Cited by 220 · see citing works
Rouaux, C., Panteleeva, I., René, F., de Aguilar, J. G., Echaniz‐Laguna, A., Dupuis, L., Menger, Y., Boutillier, A., & Loeffler, J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1139-07.2007 · Cited by 214 · see citing works
Benefit of valproic acid in suppressing disease progression of ALS model mice
Sugai, F., Yamamoto, Y., Miyaguchi, K., Zhou, Z., Sumi, H., Hamasaki, T., Goto, M., & Sakoda, S. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03765.x · Cited by 214 · see citing works
Membrane Lipids in Presynaptic Function and Disease.
Lauwers, E., Goodchild, R. E., & Verstreken, P. (2016) · Neuron · doi:10.1016/j.neuron.2016.02.033 · Cited by 213 · see citing works
The molecular basis of the frontotemporal lobar degeneration–amyotrophic lateral sclerosis spectrum
Langenhove, T. V., van der Zee, J., & Broeckhoven, C. V. (2012) · Annals of Medicine · doi:10.3109/07853890.2012.665471 · Cited by 192 · see citing works
HDAC inhibitor–dependent transcriptome and memory reinstatement in cognitive decline models
Benito, E., Urbanke, H., Ramachandran, B., Barth, J., Halder, R., Awasthi, A., Jain, G., Capece, V., Burkhardt, S., Navarro-Sala, M., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79942 · Cited by 190 · see citing works
Jochems, J., Boulden, J., Lee, B. G., Blendy, J. A., Jarpe, M. B., Mazitschek, R., van Duzer, J. H., Jones, S. S., & Berton, O. (2013) · Neuropsychopharmacology · doi:10.1038/npp.2013.207 · Cited by 168 · see citing works
Self-citationYang, S.-S., Zhang, R., Wang, G., & Zhang, Y.-F. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0089-1 · Cited by 163 · see citing works
Petri, S., Kiaei, M., Kipiani, K., Chen, J., Calingasan, N. Y., Crow, J. P., & Beal, M. F. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.09.013 · Cited by 161 · see citing works
Phase 2 study of sodium phenylbutyrate in ALS
Cudkowicz, M., Andres, P. L., MacDonald, S., Bedlack, R., Choudry, R., Brown, R. H., Jr., Zhang, H., Schoenfeld, D., Shefner, J. M., Matson, S. A., et al. (2008) · Amyotrophic Lateral Sclerosis · doi:10.1080/17482960802320487 · Cited by 154 · see citing works
Activity-dependent FUS dysregulation disrupts synaptic homeostasis
Sephton, C. F., Tang, A. A., Kulkarni, A., West, J. D., Brooks, M., Stubblefield, J. J., Liu, Y., Zhang, M. Q., Green, C. B., Huber, K. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406162111 · Cited by 145 · see citing works
Hdac6 deletion delays disease progression in the SOD1G93A mouse model of ALS
Taes, I., Timmers, M., Hersmus, N., Bento‐Abreu, A., Bosch, L. V. D., Damme, P. V., Auwerx, J. H., & Robberecht, W. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt028 · Cited by 139 · see citing works
Clinical efficacy of edaravone for the treatment of amyotrophic lateral sclerosis
Sawada, H. (2017) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2017.1319937 · Cited by 139 · see citing works
Bruneteau, G., Simonet, T., Bauché, S., Mandjee, N., Malfatti, E., Girard, E., Tanguy, M., Béhin, A., Khiami, F., Sariali, E., et al. (2013) · Brain · doi:10.1093/brain/awt164 · Cited by 137 · see citing works
Konsoula, Z., & Barile, F. A. (2012) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2012.08.001 · Cited by 134 · see citing works
Fused in sarcoma (FUS): An oncogene goes awry in neurodegeneration
Dormann, D., & Haass, C. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.03.006 · Cited by 134 · see citing works
Bennett, S. A., Tanaz, R., Cobos, S. N., & Torrente, M. P. (2018) · Translational research · doi:10.1016/j.trsl.2018.10.002 · Cited by 132 · see citing works
Cholesterol depletion inhibits synaptic transmission and synaptic plasticity in rat hippocampus
Frank, C., Rufini, S., Tancredi, V., Forcina, R., Grossi, D., & D’Arcangelo, G. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.04.019 · Cited by 126 · see citing works
Ebrahimi, M., Yamamoto, Y., Sharifi, K., Kida, H., Kagawa, Y., Yasumoto, Y., Islam, A., Miyazaki, H., Shimamoto, C., Maekawa, M., et al. (2015) · Glia · doi:10.1002/glia.22902 · Cited by 124 · see citing works
An ALS-associated mutation in the FUS 3′-UTR disrupts a microRNA–FUS regulatory circuitry
Modigliani, S. D., Morlando, M., Errichelli, L., Sabatelli, M., & Bozzoni, I. (2014) · Nature Communications · doi:10.1038/ncomms5335 · Cited by 123 · see citing works
Randomized sequential trial of valproic acid in amyotrophic lateral sclerosis
Piepers, S., Veldink, J. H., de Jong, S. W., van der Tweel, I., van der Pol, W. L., Uijtendaal, E. V., Schelhaas, H. J., Scheffer, H., de Visser, M., de Jong, J. M. B. V., et al. (2009) · Annals of Neurology · doi:10.1002/ana.21620 · Cited by 123 · see citing works
The promise and perils of HDAC inhibitors in neurodegeneration
Didonna, A., & Opal, P. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.147 · Cited by 120 · see citing works
A plural role for lipids in motor neuron diseases: energy, signaling and structure
Schmitt, F., Hussain, G., Dupuis, L., Loeffler, J., & Henriques, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00025 · Cited by 120 · see citing works
Yoo, Y.-E., & Ko, C. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.06.003 · Cited by 118 · see citing works
Devoy, A., Kalmár, B., Stewart, M. E., Park, H., Burke, B., Noy, S., Redhead, Y. T., Humphrey, J., Lo, K., Jaeger, J., et al. (2017) · Brain · doi:10.1093/brain/awx248 · Cited by 117 · see citing works
Sabatelli, M., Moncada, A., Conte, A., Lattante, S., Marangi, G., Luigetti, M., Lucchini, M., Massimiliano Mirabella, A., Romano, Â., Grande, A. D., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt328 · Cited by 108 · see citing works
Combined riluzole and sodium phenylbutyrate therapy in transgenic amyotrophic lateral sclerosis mice
Signore, S. J. D., Amante, D. J., Kim, J.-H., Stack, E. C., Goodrich, S., Cormier, K., Smith, K., Cudkowicz, M., & Ferrante, R. J. (2008) · Amyotrophic Lateral Sclerosis · doi:10.1080/17482960802226148 · Cited by 105 · see citing works
Differential Histone Deacetylase mRNA Expression Patterns in Amyotrophic Lateral Sclerosis
Janssen, C., Schmalbach, S., Boeselt, S., Sarlette, A., Dengler, R., & Petri, S. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181ddd404 · Cited by 100 · see citing works
So, E., Mitchell, J. C., Memmi, C., Chennell, G., Vizcay‐Barrena, G., Allison, L., Shaw, C. E., & Vance, C. A. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx415 · Cited by 91 · see citing works
Mitochondrial lipids in neurodegeneration
Aufschnaiter, A., Kohler, V., Diessl, J., Peselj, C., Carmona‐Gutiérrez, D., Keller, W., & Büttner, S. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2463-1 · Cited by 85 · see citing works
Benoy, V., Berghe, P. V., Jarpe, M. B., Damme, P. V., Robberecht, W., & Bosch, L. V. D. (2016) · Neurotherapeutics · doi:10.1007/s13311-016-0501-z · Cited by 83 · see citing works
Self-citationAmyotrophic Lateral Sclerosis and Skeletal Muscle: An Update
Pansarasa, O., Rossi, D., Berardinelli, A. L., & Cereda, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8578-4 · Cited by 79 · see citing works
ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects.
Qiu, H.-Y., Lee, S., Shang, Y., Wang, W.-Y., Au, K., Kamiya, S., Barmada, S. J., Finkbeiner, S., Lui, H., Carlton, C. E., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci72723 · Cited by 73 · see citing works
Pigna, E., Simonazzi, E., Sanna, K., Bernadzki, K. M., Proszynski, T., Heil, C., Palacios, D., Adamo, S., & Moresi, V. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.01.038 · Cited by 61 · see citing works
Majid, T., Griffin, D. M., Criss, Z. K., Jarpe, M. B., & Pautler, R. G. (2015) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2015.08.001 · Cited by 60 · see citing works
Self-citationHistone deacetylases and their role in motor neuron degeneration
Lazo-Gómez, R., Ramírez-Jarquín, U. N., Tovar‐y‐Romo, L. B., & Tapia, R. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00243 · Cited by 57 · see citing works
A novel role for central ACBP / DBI as a regulator of long‐chain fatty acid metabolism in astrocytes
Bouyakdan, K., Taïb, B., Budry, L., Zhao, S., Rodaros, D., Neess, D., Mandrup, S., Færgeman, N. J., & Alquier, T. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13035 · Cited by 56 · see citing works
Valle, C., Salvatori, I., Gerbino, V., Rossi, S., Palamiuc, L., René, F., & Carrı̀, M. T. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.247 · Cited by 52 · see citing works
Neuromuscular junction degeneration in muscle wasting
Rudolf, R., Deschenes, M. R., & Sandri, M. (2016) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000267 · Cited by 51 · see citing works
Olaharski, A. J., Ji, Z., Woo, J.-Y., Lim, S., Hubbard, A., Zhang, L., & Smith, M. T. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl068 · Cited by 49 · see citing works
Chen, K., Bennett, S. A., Rana, N., Yousuf, H., Said, M., Taaseen, S., Mendo, N., Meltser, S. M., & Torrente, M. P. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00297 · Cited by 44 · see citing works
Pigna, E., Renzini, A., Greco, E. A., Simonazzi, E., Fulle, S., Mancinelli, R., Moresi, V., & Adamo, S. (2018) · Skeletal Muscle · doi:10.1186/s13395-018-0153-2 · Cited by 42 · see citing works
Mithraprabhu, S., Khong, T., Jones, S. S., & Spencer, A. (2013) · British Journal of Haematology · doi:10.1111/bjh.12388 · Cited by 36 · see citing works
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Loh, J. S., Mak, W. Q., Tan, L. K. S., Ng, C. X., Chan, H. H., Yeow, S. H., Foo, J. B., Ong, Y. S., How, C. W., & Khaw, K. Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01743-1 · Cited by 1,193 · see citing works
Kumar, V., Kundu, S., Singh, A., & Singh, S. (2022) · Current Neuropharmacology · doi:10.2174/1570159x19666210609160017 · Cited by 210 · see citing works
HDAC6 in Diseases of Cognition and of Neurons
LoPresti, P. (2020) · Cells · doi:10.3390/cells10010012 · Cited by 105 · see citing works
A patent review of histone deacetylase 6 inhibitors in neurodegenerative diseases (2014-2019)
Shen, S., & Kozikowski, A. P. (2019) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2019.1708901 · Cited by 95 · see citing works
Shen, S., Svoboda, M., Zhang, G., Cavasin, M. A., Motlova, L., McKinsey, T. A., Eubanks, J. H., Bařinka, C., & Kozikowski, A. P. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00560 · Cited by 87 · see citing works
Dittlau, K. S., Krasnow, E. N., Fumagalli, L., Vandoorne, T., Baatsen, P., Kerstens, A., Giacomazzi, G., Pavie, B., Rossaert, E., Beckers, J., et al. (2021) · Stem Cell Reports · doi:10.1016/j.stemcr.2021.03.029 · Cited by 85 · see citing works
Self-citationWainberg, M., Andrews, S. J., & Tripathy, S. J. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01244-3 · Cited by 82 · see citing works
The role of altered protein acetylation in neurodegenerative disease
Kabir, F., Atkinson, R., Cook, A. L., Phipps, A. J., & King, A. E. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1025473 · Cited by 75 · see citing works
Calió, M. L., Henriques, E., Siena, A., Bertoncini, C. R. A., Gil-Mohapel, J., & Rosenstock, T. R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00679 · Cited by 64 · see citing works
Advances in Proteomic and Metabolomic Profiling of Neurodegenerative Diseases
Schuh, A. F. S., Bieger, A., Borelli, W. V., Portley, M. K., Awad, P. S., & Bandrés‐Ciga, S. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2021.792227 · Cited by 63 · see citing works
HDAC1 inhibition ameliorates TDP-43-induced cell death in vitro and in vivo
Sanna, S., Esposito, S., Masala, A., Sini, P., Nieddu, G., Galioto, M., Fais, M., Iaccarino, C., Cestra, G., & Crosio, C. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2580-3 · Cited by 61 · see citing works
Differentiation but not ALS mutations in FUS rewires motor neuron metabolism
Vandoorne, T., Veys, K., Guo, W., Sicart, A., Vints, K., Swijsen, A., Moisse, M., Eelen, G., Gounko, N. V., Fumagalli, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12099-4 · Cited by 59 · see citing works
Self-citationKuta, R., Larochelle, N., Fernandez, M., Pal, A., Minotti, S., Tibshirani, M., Louis, K. S., Gentil, B. J., Nalbantoglu, J. N., Hermann, A., et al. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-019-01064-1 · Cited by 57 · see citing works
Labarre, A., Guitard, E., Tossing, G., Forest, A., Bareke, E., Labrecque, M., Tétreault, M., Ruiz, M., & Parker, J. A. (2022) · Communications Biology · doi:10.1038/s42003-022-04295-8 · Cited by 53 · see citing works
Dissecting the Relationship Between Neuropsychiatric and Neurodegenerative Disorders
Gupta, R. V., Advani, D., Yadav, D., Ambasta, R. K., & Kumar, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03502-9 · Cited by 58 · see citing works
Tavares, M. T., Kozikowski, A. P., & Shen, S. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112887 · Cited by 52 · see citing works
Burg, T., Rossaert, E., Moisse, M., Van Damme, P., & Van Den Bosch, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011224 · Cited by 50 · see citing works
Self-citationFrom basic research to the clinic: innovative therapies for ALS and FTD in the pipeline
Liščić, R. M., Alberici, A., Cairns, N. J., Romano, M., & Buratti, E. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00373-9 · Cited by 45 · see citing works
Gomez-Sanchez, J. A., Patel, N., Martirena, F., Fazal, S. V., Mutschler, C., & Cabedo, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23062996 · Cited by 39 · see citing works
Amyotrophic Lateral Sclerosis, FUS and Protein Synthesis Defects
Assoni, A. F., Foijer, F., & Zatz, M. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10489-8 · Cited by 35 · see citing works
Opportunities for histone deacetylase inhibition in amyotrophic lateral sclerosis
Klingl, Y. E., Pakravan, D., & Bosch, L. V. D. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15217 · Cited by 32 · see citing works
Clinical validation of the novel HDAC6 radiotracer [18F]EKZ-001 in the human brain
Koole, M. J. B., Weehaeghe, D. V., Serdons, K., Herbots, M., Cawthorne, C., Celen, S., Schroeder, F. A., Hooker, J. M., Bormans, G. M., Hoon, J. N. J. M. D., et al. (2020) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-020-04891-y · Cited by 33 · see citing works
Milani, M., Mammarella, E., Rossi, S., Miele, C., Lattante, S., Sabatelli, M., Cozzolino, M., D’Ambrosi, N., & Apolloni, S. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02184-1 · Cited by 33 · see citing works
Molecular hallmarks of ageing in amyotrophic lateral sclerosis
Jagaraj, C. J., Shadfar, S., Kashani, S. A., Saravanabavan, S., Farzana, F., & Atkin, J. D. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05164-9 · Cited by 33 · see citing works
Beaver, M., Bhatnagar, A., Panikker, P., Zhang, H., Snook, R., Parmar, V., Vijayakumar, G., Betini, N., Akhter, S., & Elefant, F. (2020) · Scientific Reports · doi:10.1038/s41598-020-75035-3 · Cited by 32 · see citing works
Zhang, L., Liu, Y., Lu, Y., & Wang, G. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115295 · Cited by 27 · see citing works
HDAC3 Inhibition Stimulates Myelination in a CMT1A Mouse Model
Prior, R. C., Verschoren, S., Vints, K., Jaspers, T., Rossaert, E., Klingl, Y. E., Silva, A., Hersmus, N., Damme, P. V., & Bosch, L. V. D. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02782-x · Cited by 27 · see citing works
Self-citationPotential Therapeutic Role of HDAC Inhibitors in FUS-ALS
Tejido, C., Pakravan, D., & Bosch, L. V. D. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.686995 · Cited by 26 · see citing works
Chen, W., Guo, L., Li, M., Wei, C., Li, S., & Xu, R. (2022) · Brain Research · doi:10.1016/j.brainres.2022.147904 · Cited by 26 · see citing works
Hernaiz, A., Toivonen, J. M., Bolea, R., & Martín‐Burriel, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012609 · Cited by 24 · see citing works
Abnormal energy metabolism in ALS: a key player?
Burg, T., & Van Den Bosch, L. (2023) · Current Opinion in Neurology · doi:10.1097/wco.0000000000001164 · Cited by 24 · see citing works
Epigenetics of Neuromuscular Disorders
Coppedè, F. (2020) · Epigenomics · doi:10.2217/epi-2020-0282 · Cited by 23 · see citing works
Parrella, E., Porrini, V., Scambi, I., Gennari, M. M., Gussago, C., Bankole, O. O., Benarese, M., Mariotti, R., & Pizzi, M. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1017364 · Cited by 23 · see citing works
Tunca, C., Şeker, T., Akçimen, F., Coşkun, C., Bayraktar, E., Palvadeau, R. J., Zor, S., Koçoğlu, C., Kartal, E., Şen, N.-E., et al. (2020) · Human Mutation · doi:10.1002/humu.24055 · Cited by 21 · see citing works
Milani, M., Valle, I. D., Rossi, S., Fabbrizio, P., Margotta, C., Nardo, G., Cozzolino, M., D’Ambrosi, N., & Apolloni, S. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00346 · Cited by 19 · see citing works
Petrozziello, T., Dios, A. M., Mueller, K. A., Vaine, C. A., Hendriks, W. T. J., Glajch, K. E., Mills, A. N., Mangkalaphiban, K., Penney, E. B., Ito, N., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0243655 · Cited by 19 · see citing works
Seo, W. M., Yoon, J.-Y., Lee, J., Lee, Y., Lee, H.-J., Geum, D., Sun, W., & Song, M. (2022) · Scientific Reports · doi:10.1038/s41598-022-05645-6 · Cited by 18 · see citing works
Boyko, A. I., Karlina, I. S., Zavileyskiy, L. G., Aleshin, V. A., Artiukhov, A. V., Kaehne, T., Ksenofontov, A. L., Ryabov, S. I., Graf, A. V., Tramonti, A., et al. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.896263 · Cited by 17 · see citing works
Bai, Q., Shao, E., Ma, D., Jiao, B., Scheetz, S. D., Hartnett, K. A., Ильин, В. Н., Aizenman, E., Kofler, J., & Burton, E. A. (2024) · Nature Communications · doi:10.1038/s41467-024-52173-0 · Cited by 16 · see citing works
Glycerophospholipids in ALS: insights into disease mechanisms and clinical implication
Burg, T., & Bosch, L. V. D. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00876-3 · Cited by 15 · see citing works
Fisher, R. M. A., & Torrente, M. P. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1456052 · Cited by 14 · see citing works
Disruption of MAM integrity in mutant FUS oligodendroglial progenitors from hiPSCs
Zhu, Y., Burg, T., Neyrinck, K., Vervliet, T., Nami, F., Vervoort, E., Ahuja, K., Sassano, M. L., Chai, Y. C., Tharkeshwar, A. K., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02666-x · Cited by 14 · see citing works
Chhabra, R., Rockfield, S., Guergues, J., Nadeau, O. W., Hill, R. G., Stevens, S. M., & Nanjundan, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-85342-y · Cited by 12 · see citing works
Bennett, S. A., Cobos, S. N., Mirzakandova, M., Fallah, M., Son, E., Angelakakis, G., Rana, N., Hugais, M. M., & Torrente, M. P. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00455 · Cited by 12 · see citing works
Comaduran, M. F., Minotti, S., Jacob‐Tomas, S., Rizwan, J., Larochelle, N., Robitaille, R., Sephton, C. F., Vera, M., Nalbantoglu, J. N., & Durham, H. D. (2024) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2024.03.010 · Cited by 12 · see citing works
Hashimoto, K., Ide, S., Arata, M., Nakata, A., Ito, A., Ito, T. K., Kudo, N., Lin, B., Nunomura, K., Tsuganezawa, K., et al. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.2c00081 · Cited by 11 · see citing works
PP2A and GSK3 act as modifiers of FUS-ALS by modulating mitochondrial transport
Tziortzouda, P., Steyaert, J., Scheveneels, W., Sicart, A., Dittlau, K. S., Correia, A. M. B., Burg, T., Pal, A., Hermann, A., Damme, P. V., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02689-y · Cited by 11 · see citing works
Existing and Emerging Metabolomic Tools for ALS Research
Germeys, C., Vandoorne, T., Bercier, V., & Bosch, L. V. D. (2019) · Genes · doi:10.3390/genes10121011 · Cited by 11 · see citing works
Ao, C., Tang, S., Yang, Y., Liu, Y. M., Zhao, H. Y., Ban, J.-Q., & Li, J. (2024) · Epigenomics · doi:10.2217/epi-2023-0364 · Cited by 10 · see citing works
HDAC6 inhibition as a mechanism to prevent neurodegeneration in the mSOD1G93A mouse model of ALS
Phipps, A. J., Dwyer, S., Collins, J. M., Kabir, F., Atkinson, R. A. K., Chowdhury, A., Matthews, L., Dixit, D., TERRY, R. S., Smith, J. A., et al. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34587 · Cited by 10 · see citing works
Epigenetic Regulation of Ferroportin in Primary Cultures of the Rat Blood-Brain Barrier
Helgudóttir, S. S., Routhe, L. G., Burkhart, A., Jønsson, K., Pedersen, I. S., Lichota, J., & Moos, T. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01953-y · Cited by 9 · see citing works
Towards an integrated approach for understanding glia in Amyotrophic Lateral Sclerosis
Majewski, S., Klein, P., Boillée, S., Clarke, B. E., & Patani, R. (2024) · Glia · doi:10.1002/glia.24622 · Cited by 9 · see citing works
Ali, Z., Godoy-Corchuelo, J. M., Martins-Bach, A. B., García-Toledo, I., Fernández-Beltrán, L. C., Nair, R., Spring, S., Nieman, B. J., Jiménez-Coca, I., Bains, R. S., et al. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.050200 · Cited by 9 · see citing works
A next-generation HDAC6 inhibitor for amyotrophic lateral sclerosis and frontotemporal dementia
James, R. E., Bekier, M. E., Lee, P., Schroeder, F. A., Evans, L. J., Wagner, F. F., Hickman, D., Richardson, T., Hatzipetros, T., Vieira, F. G., et al. (2025) · Brain · doi:10.1093/brain/awaf380 · Cited by 7 · see citing works
Wang, S., Wang, J., Hu, Z., Wu, L., & Huang, L. (2026) · Experimental Neurology · doi:10.1016/j.expneurol.2026.115663 · Cited by 7 · see citing works
Hernán-Godoy, M., & Rouaux, C. (2024) · Cells · doi:10.3390/cells13110967 · Cited by 7 · see citing works
Epigenetics in the formation of pathological aggregates in amyotrophic lateral sclerosis
Noches, V., Campos‐Melo, D., Droppelmann, C. A., & Strong, M. J. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1417961 · Cited by 8 · see citing works
HDAC-6 inhibition ameliorates the early neuropathology in a mouse model of Krabbe disease
Bráz, S., Morgado, M. M., Pereira, M. I., Monteiro, A. C., Golonzhka, O., Jarpe, M. B., Brites, P., Sousa, M. M., & Nogueira‐Rodrigues, J. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1231659 · Cited by 6 · see citing works
Self-citationDecoding Neuromuscular Disorders: The Complex Role of Genetic and Epigenetic Regulators
Roque-Ramírez, B., Ríos-López, K. E., & López-Hernández, L. (2025) · Genes · doi:10.3390/genes16060622 · Cited by 6 · see citing works
Murine experimental models of amyotrophic lateral sclerosis: an update
Moreno‐Jiménez, L., Benito‐Martín, M. S., Sanclemente-Alamán, I., Matías-Guiu, J. A., Sancho-Bielsa, F. J., Canales-Aguirre, A. A., Mateos‐Díaz, J. C., Matías-Guiu, J., Aguilar, J., & Gómez‐Pinedo, U. (2023) · Neurología (English Edition) · doi:10.1016/j.nrleng.2021.07.004 · Cited by 6 · see citing works
Molecular targets of histone deacetylase inhibitors in neurodegeneration and neuroprotection
Park, Y., Yu, S., Hwang, S. Y., & Seo, H. (2024) · Molecular & Cellular Toxicology · doi:10.1007/s13273-024-00441-x · Cited by 5 · see citing works
Singh, A. K., & Kundu, T. K. (2026) · ACS Omega · doi:10.1021/acsomega.5c00905 · Cited by 5 · see citing works
The Promise of Epigenetic Editing for Treating Brain Disorders
González-Molina, L. A., Dolga, A. M., Rots, M. G., & Sarno, F. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-75980-2_4 · Cited by 5 · see citing works
Early epigenetic markers for precision medicine
Raj, S., & Kumar, D. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.02.003 · Cited by 4 · see citing works
Chen, Y., Wu, Y., Liu, X., Wan, J., Shen, M., & Zhang, Q. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.178721 · Cited by 3 · see citing works
Bhatnagar, A., Karnay, A. M., & Elefant, F. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91909-8.00015-3 · Cited by 3 · see citing works
Tripathi, S., & Bhawana, B. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04167-z · Cited by 4 · see citing works
Altered Lipid Homeostasis in Mutant FUSR521H Astrocytes from HiPSCs
Zhu, Y., Neyrinck, K., Burg, T., Chai, Y. C., Nami, F., Ahuja, K., Swinnen, J. V., Bosch, L. V. D., & Verfaillie, C. M. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05127-6 · Cited by 3 · see citing works
The potentiality of histone deacetylase inhibitors for diabetes and obesity
El-Serafi, A. T., & Serafi, I. E. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-816422-8.00015-5 · Cited by 3 · see citing works
Biological networks and complexity in early-onset motor neuron diseases
Butchbach, M. E. R., & Scott, R. C. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.1035406 · Cited by 2 · see citing works
Aranda, C. P. D. L. L., Tosat‐Bitrián, C., Porras, G., Dafinca, R., Muñoz‐Torrero, D., Talbot, K., Martín‐Requero, Á., Martı́nez, A., & Palomo, V. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00328 · Cited by 2 · see citing works
Evidence for a Growing Involvement of Glia in Amyotrophic Lateral Sclerosis
Radford, R. A. W., Vidal-Itriago, A., Scherer, N. M., Lee, A., Graeber, M. B., Chung, R. S., & Morsch, M. (2021) · doi:10.1002/9781119745532.ch7 · Cited by 3 · see citing works
Hou, X., Jiang, J., & Deng, M. (2025) · Journal of Neurology · doi:10.1007/s00415-025-13028-w · Cited by 2 · see citing works
The epigenetics of neurodegenerative diseases
Coppedè, F. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-18661-5.00001-4 · Cited by 1 · see citing works
Pereira‐Nunes, A., Ammarah, U., Shang, M., Charatsidou, I., Sharma, H., Sorroche, B. P., Nobis, M., Burg, T., Verschoren, S., Relaix, F., et al. (2025) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.05.003 · Cited by 1 · see citing works
Martinez, V. K., McAlpin, B. R., Singh, A. K., Heijnen, C. J., & Mahalingam, R. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05161-4 · Cited by 2 · see citing works
Scozzari, S., Columbro, S. F., Favagrossa, M., Tortarolo, M., Cagnotto, A., Salmona, M., Marco, G. D., Bendotti, C., Calvo, A., Pasetto, L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.15.628528 · Cited by 1 · see citing works
Niclosamide Targets Inflammatory and Profibrotic Pathways in Amyotrophic Lateral SclerosisPreprint
Milani, M., Mammarella, E., Rossi, S., Lattante, S., Sabatelli, M., Cozzolino, M., D’Ambrosi, N., & Apolloni, S. (2021) · doi:10.21203/rs.3.rs-138253/v1
Modelos experimentales murinos en la esclerosis lateral amiotrófica. Puesta al día
Moreno‐Jiménez, L., Benito‐Martín, M. S., Sanclemente-Alamán, I., Matías-Guiu, J. A., Sancho-Bielsa, F. J., Canales-Aguirre, A. A., Mateos‐Díaz, J. C., Matías-Guiu, J., Aguilar, J., & Gómez‐Pinedo, U. (2021) · Neurología · doi:10.1016/j.nrl.2021.07.007
Theme 07 - PRE-CLINICAL THERAPEUTIC STRATEGIES
(2021) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.1080/21678421.2021.1985793
FUSDelta14 mutation impairs normal brain development and causes systemic metabolic alterationsPreprint
Godoy-Corchuelo, J. M., Ali, Z., Martins-Bach, A. B., García-Toledo, I., Fernández-Beltrán, L. C., Nair, R., Spring, S., Nieman, B. J., Jiménez-Coca, I., Bains, R. S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.24.529858
HDAC6 inhibition as a mechanism to prevent axon degeneration in the mSOD1 G93A mouse model of ALSPreprint
Phipps, A. J., Dwyer, S., Collins, J. M., Kabir, F., Atkinson, R. A. K., Chowdhury, A., Matthews, L., Dixit, D., TERRY, R. S., Smith, J. A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.28.555025
Carboplatin restores neuronal toxicity in FUS-linked amyotrophic lateral sclerosis
Kim, K. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00489
Milani, M., Mammarella, E., Rossi, S., Miele, C., Lattante, S., Sabatelli, M., Cozzolino, M., D’Ambrosi, N., & Apolloni, S. (2021) · Figshare · doi:10.6084/m9.figshare.14775706
Ghavidel, P., Abdelmalki, Y., & Sincennes, M. (2026) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl46704
Scozzari, S., Columbro, S. F., Favagrossa, M., Tortarolo, M., Cagnotto, A., Salmona, M., Marco, G. D., Bendotti, C., Calvo, A., Pasetto, L., et al. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70493
Ao, C., Liu, H., Ban, R., Huang, T., Xiao, Y., Chen, W., Feng, Y., Zhao, H., Ban, J., & Li, J. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1883748
TDP-43 and ALS - what's wrong with my membranes?
Dahlhaus, R., Yalcin, I., Tischer, J., & Braun, R. J. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107630
Алексеевна, С. А., Beletskiy, A., Balaban, P. M., & Borodinova, A. A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27209231
Lv, X., 黄敏聪, 龙文娟, Li, X., 胡中扬, Feng, Y., Du, J., Long, Q., Chen, Y., Shi, M., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27209322
- Authors
- Rossaert, E., Pollari, E., Jaspers, T., Van Helleputte, L., Jarpe, M., Van Damme, P., De Bock, K., Moisse, M., & Van Den Bosch, L.
- Affiliations
- VIB-KU Leuven Center for Brain & Disease Research (BE)
- Corresponding author
- Moisse, Matthieu
- Venue
- Acta Neuropathologica Communications
- Published
- 2019-07-05
- Volume
- 7
- Issue
- 1
- Pages
- 107-107
- ISSN
- 2051-5960 (ISSN-L)
- PMC
- PMC6612190
- OpenAlex
- W2955740693
- Cited by
- 93
- References
- 80
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 18 · 2023: 11 · 2022: 15 · 2021: 14 · 2020: 15 · 2019: 3
- FWCI
- 8.12
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Acta Neuropathologica Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Lirias (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, cc-by)
- ETH Zürich Research Collection (cc-by)
- Funders
- Fund for Scientific Research Flanders (G.0431.12N and G.0440.12N)
- Interuniversity Attraction Poles Programme (P7/16)
- Muscular Dystrophy Association (577668)
- ALS Liga
- European Community's Health Seventh Framework Programme (FP7/2007-2013)
- ALS Therapy Alliance
- Amyotrophic Lateral Sclerosis Association (14-LGCA-181)
- Fondation Thierry Latran
- Opening the Future - KU Leuven
- Fonds Wetenschappelijk Onderzoek
- Een Hart voor ALS
- Laevers fund for ALS research
- Agentschap voor Innovatie door Wetenschap en Technologie
- Saastamoinen foundation
- Instrumentarium Science foundation
- Finnish Cultural foundation
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- amyotrophic lateral sclerosis, FUS, histone acetylation, histone deacetylase inhibition, epigenetic dysregulation, metabolic homeostasis, metabolic gene expression, motor phenotype, lifespan extension, spinal cord, neurodegeneration, transgenic mouse model
- MeSH terms
- Acetylation, Amyotrophic Lateral Sclerosis, Animals, Disease Models, Animal, Female, Histones, Humans, Hydroxamic Acids, Male, Mice, Transgenic, Pyrimidines, Random Allocation, RNA-Binding Protein FUS, Mice, Metabolomics, Histone Deacetylase Inhibitors
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 ›
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