ALS-Linked SOD1 Mutant G85R Mediates Damage to Astrocytes and Promotes Rapidly Progressive Disease with SOD1-Containing Inclusions

Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels

Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062

Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation

Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143

GDNF: a Glial Cell Line-Derived Neurotrophic Factor for Midbrain Dopaminergic Neurons

Lin, L.-F. H., Doherty, D. H., Lile, J. D., Bektesh, S. L., & Collins, F. (1993) · Science · doi:10.1126/science.8493557 · Cited by 3,206

Free radicals, antioxidants, and human disease: curiosity, cause, or consequence?

Halliwell, B. B. (1994) · The Lancet · doi:10.1016/s0140-6736(94)92211-x · Cited by 2,926

Knockout of Glutamate Transporters Reveals a Major Role for Astroglial Transport in Excitotoxicity and Clearance of Glutamate

Rothstein, J. D., Dykes-Hoberg, M., Pardo, C. A., Bristol, L. A., Jin, L., Kuncl, R. W., Kanai, Y., Hediger, M. A., Wang, Y., Schielke, J. P., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80086-0 · Cited by 2,534

Cellular defenses against damage from reactive oxygen species

Yu, B. (1994) · Physiological Reviews · doi:10.1152/physrev.1994.74.1.139 · Cited by 2,382

Localization of neuronal and glial glutamate transporters

Rothstein, J. D., Martin, L. J., Levey, A. I., Dykes‐Hoberg, M., Jin, L., Wu, D. M., Nash, N. R., & Kuncl, R. W. (1994) · Neuron · doi:10.1016/0896-6273(94)90038-8 · Cited by 1,703

Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase

Deng, H., Hentati, A., Tainer, J. A., Iqbal, Z., Cayabyab, A., Hung, W.-Y., Getzoff, E. D., Hu, P., Herzfeldt, B., Roos, R. P., et al. (1993) · Science · doi:10.1126/science.8351519 · Cited by 1,479

Selective loss of glial glutamate transporter GLT‐1 in amyotrophic lateral sclerosis

Rothstein, J. D., Van Kammen, M., Levey, A. I., Martin, L. J., & Kuncl, R. W. (1995) · Annals of Neurology · doi:10.1002/ana.410380114 · Cited by 1,471

Astrocytes in amyotrophic lateral sclerosis: direct effects on motor neuron survival

Staats, K. A., & Bosch, L. V. D. (2009) · Journal of Biological Physics · doi:10.1007/s10867-009-9141-4 · Cited by 52

Transcriptional profile of primary astrocytes expressing ALS‐linked mutant SOD1

Vargas, M. R., Pehar, M., Díaz‐Amarilla, P., Beckman, J. S., & Barbeito, L. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21797 · Cited by 50

Toward a new role for plasma membrane sodium-dependent glutamate transporters of astrocytes: maintenance of antioxidant defenses beyond extracellular glutamate clearance

Had‐Aissouni, L. (2011) · Amino Acids · doi:10.1007/s00726-011-0863-9 · Cited by 52

New insights into the gene expression associated to amyotrophic lateral sclerosis

Recabarren-Leiva, D., & Alarcón, M. A. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.12.016 · Cited by 49

Histone Deacetylase Inhibitors: A Therapeutic Key in Neurological Disorders?

Ziemka‐Nałęcz, M., Jaworska, J., Sypecka, J., & Zalewska, T. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly073 · Cited by 53

Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases

Wang, J., Martin, E. I., Gonzales, V., Borchelt, D., & Lee, M. K. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.11.009 · Cited by 50

Presymptomatic motor neuron loss and reactive astrocytosis in the SOD1 mouse model of amyotrophic lateral sclerosis

Feeney, S. J., McKelvie, P. A., Austin, L., Jean-François, M. J. B., Kapsa, R. M. I., Tombs, S. M., & Byrne, E. (2001) · Muscle & Nerve · doi:10.1002/mus.1176 · Cited by 50

Neuromuscular accumulation of mutant superoxide dismutase 1 aggregates in a transgenic mouse model of familial amyotrophic lateral sclerosis

Turner, B. J., Lopes, E. C., & Cheema, S. S. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00893-0 · Cited by 50

Apoptosis-Inducing Factor Deficiency Induces Early Mitochondrial Degeneration in Brain Followed by Progressive Multifocal Neuropathology

Ghouzzi, V. E., Csaba, Z., Olivier, P., Lelouvier, B., Schwendimann, L., Dournaud, P., Verney, C., Rustin, P., & Gressèns, P. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318148b822 · Cited by 53

Analysis of Ubiquitination In Vivo Using a Transgenic Mouse Model

Tsirigotis, M., Thurig, S., Dubé, M., Vanderhyden, B. C., Zhang, M., & Gray, D. A. (2001) · BioTechniques · doi:10.2144/01311rr03 · Cited by 50

Toxicity of ALS-Linked SOD1 Mutants

Williamson, T. L., Corson, L., Huang, L., Burlingame, A. L., Liu, J., Bruijn, L. I., & Cleveland, D. W. (2000) · Science · doi:10.1126/science.288.5465.399a · Cited by 50

GLT1 overexpression in SOD1G93A mouse cervical spinal cord does not preserve diaphragm function or extend disease

Li, K., Hala, T. J., Seetharam, S., Poulsen, D. J., Wright, M. C., & Lepore, A. C. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.010 · Cited by 48

Involvement of quinolinic acid in the neuropathogenesis of amyotrophic lateral sclerosis

Lee, J., Tan, V. X., Lovejoy, D. B., Braidy, N., Rowe, D. B., Brew, B. J., & Guillemin, G. J. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.05.011 · Cited by 52

Membralin deficiency dysregulates astrocytic glutamate homeostasis, leading to ALS-like impairment

Jiang, L.-L., Zhu, B., Zhao, Y., Li, X., Liu, T., Piña-Crespo, J., Zhou, L., Xu, W., Gómez-Rodríguez, M. J., Yu, H., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci127695 · Cited by 51

A circuit-dependent ROS feedback loop mediates glutamate excitotoxicity to sculpt the Drosophila motor system

Peng, J.-J., Lin, S.-H., Liu, Y., Lin, H.-C., Li, T.-N., & Yao, C. (2019) · eLife · doi:10.7554/elife.47372 · Cited by 42

X‐Linked inhibitor of apoptosis protein is involved in mutant SOD1‐mediated neuronal degeneration

Ishigaki, S., Liang, Y., Yamamoto, M., Niwa, J., Ando, Y., Yoshihara, T., Takeuchi, H., Doyu, M., & Sobue, G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00998.x · Cited by 49

Absence of p53: No Effect in a Transgenic Mouse Model of Familial Amyotrophic Lateral Sclerosis

Kuntz, C., Kinoshita, Y., Beal, M. F., Donehower, L. A., & Morrison, R. S. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7464 · Cited by 49

Triggering ferroptosis in neurodegenerative diseases

Nguyen, T. P. M., Alves, F. M., Lane, D. J. R., Bush, A. I., & Ayton, S. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.06.008 · Cited by 53

Superoxide dismutase‐1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice

Bergemalm, D., Forsberg, K., Srivastava, V., Graffmo, K. S., Andersen, P. M., Brännström, T., Wingsle, G., & Marklund, S. L. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06753.x · Cited by 48

Crosstalk between astrocytes and motor neurons: What is the message?

Bosch, L. V. D., & Robberecht, W. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.01.008 · Cited by 48

Alteration of familial ALS-linked mutant SOD1 solubility with disease progression: Its modulation by the proteasome and Hsp70

Koyama, S., Arawaka, S., Ren, C.-H., Wada, M., Kawanami, T., Kurita, K., Kato, M., Nagai, M., Aoki, M., Itoyama, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.170 · Cited by 50

Deletion of Tbk1 disrupts autophagy and reproduces behavioral and locomotor symptoms of FTD-ALS in mice

Duan, W., Guo, M., Yi, L., Zhang, J., Bi, Y., Liu, Y., Li, Y., Li, Z., Ma, Y., Zhang, G., et al. (2019) · Aging · doi:10.18632/aging.101936 · Cited by 51

Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q

Winkler, D. D., Schuermann, J. P., Cao, X., Holloway, S. P., Borchelt, D., Carroll, M. C., Proescher, J. B., Culotta, V., & Hart, P. J. (2009) · Biochemistry · doi:10.1021/bi8021735 · Cited by 47

Genetics of amyotrophic lateral sclerosis

Robberecht, W. (2000) · Journal of Neurology · doi:10.1007/pl00007785 · Cited by 48

Magnetic resonance spectroscopy of regional brain metabolite markers in FALS mice and the effects of dietary creatine supplementation

Choi, J., Küstermann, E., Dedeoglu, A., & Jenkins, B. G. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07015.x · Cited by 46

Relationship between neuropathology and disease progression in the SOD1G93A ALS mouse

Yang, W. W., Sidman, R. L., Taksir, T. V., Treleaven, C. M., Fidler, J. A., Cheng, S. H., Dodge, J. C., & Shihabuddin, L. S. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.11.019 · Cited by 51

Evidence from Computer Simulations for Alterations in the Membrane Biophysical Properties and Dendritic Processing of Synaptic Inputs in Mutant Superoxide Dismutase-1 Motoneurons

Elbasiouny, S. M., Amendola, J., Durand, J., & Heckman, C. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0434-10.2010 · Cited by 47

Overexpression of manganese superoxide dismutase attenuates neuronal death in human cells expressing mutant (G37R) Cu/Zn‐superoxide dismutase

Flanagan, S. W., Anderson, R. D., Ross, M. A., & Oberley, L. W. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00812.x · Cited by 47

Absence of Nrf2 or Its Selective Overexpression in Neurons and Muscle Does Not Affect Survival in ALS-Linked Mutant hSOD1 Mouse Models

Vargas, M. R., Burton, N. C., Gan, L., Johnson, D. A., Schäfer, M., Werner, S., & Johnson, J. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056625 · Cited by 48

Functional and morphological alterations in compound transgenic mice overexpreszing Cu/Zn superoxide dismutaze and amyloid precursor protein

Harris‐Cerruti, C., Kamsler, A., Kaplan, B., Lamb, B. T., Segal, M., & Groner, Y. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03188.x · Cited by 47

Lysosomal and phagocytic activity is increased in astrocytes during disease progression in the SOD1 G93A mouse model of amyotrophic lateral sclerosis

Baker, D. J., Blackburn, D. J., Keatinge, M., Sokhi, D. S., Viskaitis, P., Heath, P. R., Ferraiuolo, L., Kirby, J., & Shaw, P. J. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00410 · Cited by 48

Mouse models for neurological disease

Hafezparast, M., Ahmad‐Annuar, A., Wood, N. W., Tabrizi, S. J., & Fisher, E. (2002) · The Lancet Neurology · doi:10.1016/s1474-4422(02)00100-x · Cited by 46

Glial restricted precursors protect against chronic glutamate neurotoxicity of motor neurons in vitro

Maragakis, N. J., Rao, M. S., Lladó, J., Wong, V., Xue, H., Pardo, A. C., Herring, J., Kerr, D. A., Coccia, C., & Rothstein, J. D. (2005) · Glia · doi:10.1002/glia.20161 · Cited by 46

Advances in the Development of Disease-Modifying Treatments for Amyotrophic Lateral Sclerosis

Moujalled, D., & White, A. R. (2016) · CNS Drugs · doi:10.1007/s40263-016-0317-8 · Cited by 48

Comparative binding of kaempferol and kaempferide on inhibiting the aggregate formation of mutant (G85R) SOD1 protein in familial amyotrophic lateral sclerosis: A quantum chemical and molecular mechanics study

Srinivasan, E., & Rajasekaran, R. (2018) · BioFactors · doi:10.1002/biof.1441 · Cited by 47

Glutamate transport alteration triggers differentiation‐state selective oxidative death of cultured astrocytes: a mechanism different from excitotoxicity depending on intracellular GSH contents

Ré, D. B., Boucraut, J., Samuel, D., Birman, S., Goff, L. K., & Had‐Aissouni, L. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01752.x · Cited by 46

Transgenic Mice in the Study of ALS: The Role of Neurofilaments

Julien, J., Couillard‐Després, S., & Meier, J. (1998) · Brain Pathology · doi:10.1111/j.1750-3639.1998.tb00199.x · Cited by 46

The Role of the Innate Immune System in ALS

Phani, S., Ré, D. B., & Przedborski, S. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00150 · Cited by 45

The Endocannabinoid System in Amyotrophic Lateral Sclerosis

Bilsland, L. G., & Greensmith, L. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208785740081 · Cited by 45

Parkin Protects Against Misfolded SOD1 Toxicity by Promoting Its Aggresome Formation and Autophagic Clearance

Yung, C., Di, S., Li, L., & Chin, L. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9537-z · Cited by 45

ALS-Linked SOD1 Mutants Enhance Neurite Outgrowth and Branching in Adult Motor Neurons

Osking, Z., Ayers, J. I., Hildebrandt, R. P., Skruber, K., Brown, H. H., Ryu, D. H., Eukovich, A. R., Golde, T. E., Borchelt, D., Read, T., et al. (2018) · iScience · doi:10.1016/j.isci.2018.12.026 · Cited by 47

Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises

McAlary, L., Chew, Y. L., Lum, J. S., Geraghty, N. J., Yerbury, J. J., & Cashman, N. R. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.581907 · Cited by 48

Mitochondrial Quality Control Strategies: Potential Therapeutic Targets for Neurodegenerative Diseases?

Hu, D., Liu, Z., & Qi, X. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.746873 · Cited by 44

Altered terminal Schwann cell morphology precedes denervation in SOD1 mice

Carrasco, D. I., Seburn, K. L., & Pinter, M. J. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.09.014 · Cited by 44

Mitochondria-Targeted Catalase Reverts the Neurotoxicity of hSOD1G93A Astrocytes without Extending the Survival of ALS-Linked Mutant hSOD1 Mice

Pehar, M., Beeson, G. C., Beeson, C., Johnson, J. A., & Vargas, M. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103438 · Cited by 44

Peripheral hyperstimulation alters site of disease onset and course in SOD1 rats

Lepore, A. C., Tolmie, C., O'Donnell, J., Wright, M. C., Dejea, C. M., Rauck, B. M., Höke, A., Ignagni, A. R., Onders, R. P., & Maragakis, N. J. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.03.021 · Cited by 44

Transplantation of clinical-grade human neural stem cells reduces neuroinflammation, prolongs survival and delays disease progression in the SOD1 rats

Zalfa, C., Nodari, L. R., Vacchi, E., Gelati, M., Profico, D. C., Boido, M., Binda, E., Filippis, L. D., Copetti, M., Garlatti, V., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1582-5 · Cited by 44

Alternative splicing of the 5′‐sequences of the mouse EAAT2 glutamate transporter and expression in a transgenic model for amyotrophic lateral sclerosis

Münch, C., Ebstein, M., Seefried, U., Zhu, B., Stamm, S., Landwehrmeyer, G. B., Ludolph, A. C., Schwalenstöcker, B., & Meyer, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01012.x · Cited by 44

Genetic Mouse Models of Neurodegenerative Diseases

Trancikova, A. K., Ramonet, D., & Moore, D. J. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-384878-9.00012-1 · Cited by 47

Expression of hepatocyte growth factor and c-Met in the anterior horn cells of the spinal cord in the patients with amyotrophic lateral sclerosis (ALS): immunohistochemical studies on sporadic ALS and familial ALS with superoxide dismutase 1 gene mutation

Kato, S., Funakoshi, H., Nakamura, T., Kato, M., Nakano, I., Hirano, A., & Ohama, E. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0708-z · Cited by 44

Aggregate Formation in Cu,Zn Superoxide Dismutase-related Proteins

Son, M., Cloyd, C. D., Rothstein, J. D., Rajendran, B., & Elliott, J. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211698200 · Cited by 44

Presence of Cu/Zn superoxide dismutase (SOD) immunoreactivity in neuronal hyaline inclusions in spinal cords from mice carrying a transgene for Gly93Ala mutant human Cu/Zn SOD

Shibata, N., Hirano, A., Kobayashi, M., Canto, M. C. D., Gurney, M. E., Komori, T., Umahara, T., & Asayama, K. (1998) · Acta Neuropathologica · doi:10.1007/s004010050777 · Cited by 44

Differential profiles of copper-induced ROS generation in human neuroblastoma and astrocytoma cells

Qian, Y., Zheng, Y., Abraham, L., Ramos, K. S., & Tiffany‐Castiglioni, E. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.11.004 · Cited by 43

Modulation of mutant superoxide dismutase 1 aggregation by co‐expression of wild‐type enzyme

Prudencio, M., Durazo, A., Whitelegge, J. P., & Borchelt, D. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05839.x · Cited by 43

Monitoring systemic oxidative stress in an animal model of amyotrophic lateral sclerosis

Mena, F. J. M., González‐Mingot, C., Larrodé, P., Muñoz, M. J., Oliván, S., Fuentes‐Broto, L., Martínez‐Ballarín, E., Reiter, R. J., Osta, R., & García, J. J. (2010) · Journal of Neurology · doi:10.1007/s00415-010-5825-8 · Cited by 43

Expression of an endoplasmic reticulum-resident chaperone, glucose-regulated stress protein 78, in the spinal cord of a mouse model of amyotrophic lateral sclerosis

Wate, R., Ito, H., Zhang, J. H., Ohnishi, S., Nakano, S., & Kusaka, H. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1080-y · Cited by 43

Rho guanine nucleotide exchange factor is an NFL mRNA destabilizing factor that forms cytoplasmic inclusions in amyotrophic lateral sclerosis

Droppelmann, C. A., Keller, B. A., Campos‐Melo, D., Volkening, K., & Strong, M. J. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.06.021 · Cited by 43

Invited Review: Decoding the pathophysiological mechanisms that underlie RNA dysregulation in neurodegenerative disorders: a review of the current state of the art

Walsh, M. J., Cooper‐Knock, J., Dodd, J. E., Stopford, M. J., Mihaylov, S. R., Kirby, J., Shaw, P. J., & Hautbergue, G. M. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12187 · Cited by 46

Insulin-like growth factor 1 in diabetic neuropathy and amyotrophic lateral sclerosis

Rauskolb, S., Dombert, B., & Sendtner, M. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.04.007 · Cited by 45

Tumor Necrosis Factor Alpha in Amyotrophic Lateral Sclerosis: Friend or Foe?

Guidotti, G., Scarlata, C., Brambilla, L., & Rossi, D. (2021) · Cells · doi:10.3390/cells10030518 · Cited by 42

Micro-RNAs Shuttled by Extracellular Vesicles Secreted from Mesenchymal Stem Cells Dampen Astrocyte Pathological Activation and Support Neuroprotection in In-Vitro Models of ALS

Provenzano, F., Nyberg, S., Giunti, D., Torazza, C., Parodi, B., Bonifacino, T., Usai, C., de Rosbo, N. K., Milanese, M., Uccelli, A., et al. (2022) · Cells · doi:10.3390/cells11233923 · Cited by 47

S100A6, a calcium- and zinc-binding protein, is overexpressed in SOD1 mutant mice, a model for amyotrophic lateral sclerosis

Hoyaux, D., Alao, J. M., Fuchs, J., Robert Kiss, A., Keller, B. U., Heizmann, C. W., Pochet, R., & Frermann, D. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00101-4 · Cited by 43

Acute intermittent hypoxia induced phrenic long-term facilitation despite increased SOD1 expression in a rat model of ALS

Nichols, N. L., Satriotomo, I., Harrigan, D. J., & Mitchell, G. S. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.08.011 · Cited by 42

Endogenous macrophage migration inhibitory factor reduces the accumulation and toxicity of misfolded SOD1 in a mouse model of ALS

Leyton-Jaimes, M. F., Benaim, C., Abu‐Hamad, S., Kahn, J., Guetta, A., Bucala, R., & Israelson, A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604600113 · Cited by 42

Genetic screening of ANXA11 revealed novel mutations linked to amyotrophic lateral sclerosis

Teyssou, E., Muratet, F., Amador, M. D. M., Ferrien, M., Lautrette, G., Machat, S., Boillée, S., Larmonier, T., Saker, S., Leguern, É., et al. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.10.015 · Cited by 40

Modelling amyotrophic lateral sclerosis in rodents

Todd, T. W., & Petrucelli, L. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00564-x · Cited by 44

Adult Olfactory Bulb Neural Precursor Cell Grafts Provide Temporary Protection From Motor Neuron Degeneration, Improve Motor Function, and Extend Survival in Amyotrophic Lateral Sclerosis Mice

Martin, L. J., & Liu, Z. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318158822b · Cited by 42

Experimental Models of Amyotrophic Lateral Sclerosis

Elliott, J. L. (1999) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0266 · Cited by 42

Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry

Nakanishi, T., Kishikawa, M., Miyazaki, A., Shimizu, A., Ogawa, Y., Sakoda, S., Ohi, T., & Shoji, H. (1998) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(98)00012-0 · Cited by 42

Genetic analysis and SOD1 mutation screening in Iranian amyotrophic lateral sclerosis patients

Alavi, A., Nafissi, S., Rohani, M., Zamani, B., Sedighi, B., Shamshiri, H., Fan, J., Ronaghi, M., & Elahi, E. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.09.006 · Cited by 41

Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention

Kishinevsky, A. C. S., & Lou, J. K. I. W. (2013) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.s10-007 · Cited by 42

Mutation of the caspase-3 cleavage site in the astroglial glutamate transporter EAAT2 delays disease progression and extends lifespan in the SOD1-G93A mouse model of ALS

Rosenblum, L. T., Markandaiah, S. S., Ghosh, B., Foran, E., Lepore, A. C., Pasinelli, P., & Trotti, D. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.03.014 · Cited by 42

Astrogliosis in ALS: possible interpretations according to pathogenetic hypotheses

Schiffer, D., & Fiano, V. (2004) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/14660820310016822 · Cited by 41

Postnatal dendritic development in lumbar motoneurons in mutant superoxide dismutase 1 mouse model of amyotrophic lateral sclerosis

Filipchuk, A., & Durand, J. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.01.046 · Cited by 45

Activation of Ets‐2 by oxidative stress induces Bcl‐xL expression and accounts for glial survival in amyotrophic lateral sclerosis

Lee, J.-H., Kannagi, M., Ferrante, R. J., Kowall, N. W., & Ryu, H. (2009) · The FASEB Journal · doi:10.1096/fj.08-121046 · Cited by 41

E6-AP association promotes SOD1 aggresomes degradation and suppresses toxicity

Mishra, A., Maheshwari, M., Chhangani, D., Fujimori-Tonou, N., Endo, F., Joshi, A. P., Jana, N. R., & Yamanaka, K. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.08.016 · Cited by 40

ALS Patient Stem Cells for Unveiling Disease Signatures of Motoneuron Susceptibility: Perspectives on the Deadly Mitochondria, ER Stress and Calcium Triad

Kaus, A. S., & Sareen, D. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00448 · Cited by 42

A faulty interaction between SOD1 and hCCS in neurodegenerative disease

Wright, G. S. A., Antonyuk, S. V., & Hasnain, S. S. (2016) · Scientific Reports · doi:10.1038/srep27691 · Cited by 40

Dysfunction of Endocytic Kinase AAK1 in ALS

Shi, B., Conner, S. D., & Liu, J. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151222918 · Cited by 41

Peripherin is not a contributing factor to motor neuron disease in a mouse model of amyotrophic lateral sclerosis caused by mutant superoxide dismutase

Larivière, R., Beaulieu, J., Nguyen, M. D., & Julien, J. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00036-6 · Cited by 40

Histidinyl Radical Formation in the Self-peroxidation Reaction of Bovine Copper-Zinc Superoxide Dismutase

Gunther, M. R., Peters, J. A., & Sivaneri, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107342200 · Cited by 40

Astrocytes as Active Participants of Glutamatergic Function and Regulators of its Homeostasis

Bezzi, P., Vesce, S., Panzarasa, P., & Volterra, A. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4685-6_6 · Cited by 40

Riluzole, unlike the AMPA antagonist RPR119990, reduces motor impairment and partially prevents motoneuron death in the wobbler mouse, a model of neurodegenerative disease

Fumagalli, E. R., Bigini, P., Barbera, S., Paola, M. D., & Mennini, T. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2005.11.010 · Cited by 40

Inter- and Intracellular Signaling in Amyotrophic Lateral Sclerosis: Role of p38 Mitogen-Activated Protein Kinase

Bendotti, C., Cutrona, M. B., Cheroni, C., Grignaschi, G., Coco, D. L., Peviani, M., Tortarolo, M., Veglianese, P., & Zennaro, E. (2005) · Neurodegenerative Diseases · doi:10.1159/000089617 · Cited by 39

Transgenic animal models of neurodegeneration based on human genetic studies

Harvey, B. K., Richie, C. T., Hoffer, B. J., & Airavaara, M. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0476-6 · Cited by 38

Tryptophan 32 mediates SOD1 toxicity in a in vivo motor neuron model of ALS and is a promising target for small molecule therapeutics

DuVal, M. G., Hinge, V. K., Snyder, N., Kanyo, R., Bratvold, J., Pokrishevsky, E., Cashman, N. R., Blinov, N., Kovalenko, A., & Allison, W. T. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.025 · Cited by 39

Neuromuscular Disease Models and Analysis

Burgess, R. W., Cox, G. A., & Seburn, K. L. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-058-8_20 · Cited by 39

Reduced VGLUT2 expression increases motor neuron viability in Sod1G93A mice

Wootz, H., Enjin, A., Wallén‐Mackenzie, Å., Lindholm, D., & Kullander, K. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.09.006 · Cited by 39

Importance of astrocytic inactivation of synaptically released glutamate for cell survival in the central nervous system—are astrocytes vulnerable to low intracellular glutamate concentrations?

Had‐Aissouni, L., Ré, D. B., Nieoullon, A. L., & Goff, L. K. (2002) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(02)00022-0 · Cited by 39

Disruption of the structure of the Golgi apparatus and the function of the secretory pathway by mutants G93A and G85R of Cu, Zn superoxide dismutase (SOD1) of familial amyotrophic lateral sclerosis

Stieber, A., Gonatas, J. O., Moore, J. S., Bantly, A., Yim, H.-S., Yim, M. B., & Gonatas, N. K. (2004) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2003.12.004 · Cited by 38

Approaches to gene modulation therapy for ALS

Meijboom, K. E., & Brown, R. H. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01285-w · Cited by 38

How do we get from hyperexcitability to excitotoxicity in amyotrophic lateral sclerosis?

Odierna, G. L., Vucic, S., Dyer, M. S., Dickson, T. C., Woodhouse, A., & Blizzard, C. A. (2024) · Brain · doi:10.1093/brain/awae039 · Cited by 36

Astrocytes: The Stars in Neurodegeneration?

Dittlau, K. S., & Freude, K. (2024) · Biomolecules · doi:10.3390/biom14030289 · Cited by 39

Neuroprotective agents target molecular mechanisms of disease in ALS

Zhu, Y., Fotinos, A., Mao, L. L. J., Atassi, N., Zhou, E., Ahmad, S., Guan, Y., Berry, J. D., Cudkowicz, M., & Wang, X. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.08.016 · Cited by 39

GABAA receptors present higher affinity and modified subunit composition in spinal motor neurons from a genetic model of amyotrophic lateral sclerosis

Carunchio, I., Mollinari, C., Pieri, M., Merlo, D., & Zona, C. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06436.x · Cited by 38

Retinoid receptors in chronic degeneration of the spinal cord: observations in a rat model of amyotrophic lateral sclerosis

Jokic, N., Ling, Y. Y., Ward, R. E., Michael-Titus, A. T., Priestley, J. V., & Malaspina, A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04893.x · Cited by 38

Reality and immortality—neural stem cells for therapies

Rothstein, J. D., & Snyder, E. Y. (2004) · Nature Biotechnology · doi:10.1038/nbt0304-283 · Cited by 38

Hydrogen Peroxide and Amyotrophic Lateral Sclerosis: From Biochemistry to Pathophysiology

Sanghai, N., & Tranmer, G. K. (2021) · Antioxidants · doi:10.3390/antiox11010052 · Cited by 37

Expression of ubiquitin and proteasome in motorneurons and astrocytes of spinal cords from patients with amyotrophic lateral sclerosis

de Mendonça, D. M. F., Chimelli, L. M. C., & Martinez, A. M. B. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.06.009 · Cited by 37

What transgenic mice tell us about neurodegenerative disease

Gurney, M. E. (2000) · BioEssays · doi:10.1002/(sici)1521-1878(200003)22:3 · Cited by 38

Astrocyte loss of mutant SOD1 delays ALS disease onset and progression in G85R transgenic mice

Wang, L., Gutmann, D. H., & Roos, R. P. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq463 · Cited by 214

SOD1 Mutations Causing Familial Amyotrophic Lateral Sclerosis Induce Toxicity in Astrocytes: Evidence for Bystander Effects in a Continuum of Astrogliosis

Wallis, N., Lau, C. L., Farg, M. A., Atkin, J. D., Beart, P. M., & O’Shea, R. D. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2385-7 · Cited by 14

Issue Cover (October 2015)

(2015) · Journal of Neurochemistry · doi:10.1111/jnc.12905

Restricted Expression of G86R Cu/Zn Superoxide Dismutase in Astrocytes Results in Astrocytosis But Does Not Cause Motoneuron Degeneration

Gong, Y. H., Parsadanian, A. S., Andreeva, A., Snider, W. D., & Elliott, J. L. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-02-00660.2000 · Cited by 387

Astrocytes from familial and sporadic ALS patients are toxic to motor neurons

Swami, M. (2011) · Nature Medicine · doi:10.1038/nm.2484 · Cited by 33