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

α-amino-3-hydroxy-5-methyl-isoxazole-4-propionate receptors in spinal cord motor neurons are altered in transgenic mice overexpressing human Cu,Zn superoxide dismutase (Gly93→Ala) mutation

Pieri, M., Gaetti, C., Spalloni, A., Cavalcanti, S., Mercuri, N. B., Bernardi, G., Longone, P., & Zona, C. (2003) · Neuroscience · doi:10.1016/j.neuroscience.2003.07.003 · Cited by 36

Mutant HSPB1 overexpression in neurons is sufficient to cause age-related motor neuronopathy in mice

Srivastava, A. K., Renusch, S. R., Naiman, N. E., Gu, S., Sneh, A., Arnold, W. D., Sahenk, Z., & Kolb, S. J. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.035 · Cited by 37

NO Orchestrates the Loss of Synaptic Boutons from Adult “Sick” Motoneurons: Modeling a Molecular Mechanism

Moreno‐López, B., Sunico, C. R., & González‐Forero, D. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8159-8 · Cited by 37

Flavonoids and Astrocytes Crosstalking: Implications for Brain Development and Pathology

Nones, J., Stipursky, J., Costa, S., & Gomes, F. (2010) · Neurochemical Research · doi:10.1007/s11064-010-0144-0 · Cited by 37

Genetic validation of a therapeutic target in a mouse model of ALS

de Boer, A. S., Koszka, K., Kiskinis, E., Suzuki, N., Davis‐Dusenbery, B. N., & Eggan, K. C. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009351 · Cited by 35

Regenerative medicine for neurological diseases—will regenerative neurosurgery deliver?

Burns, T. C., & Quiñones‐Hinojosa, A. (2021) · BMJ · doi:10.1136/bmj.n955 · Cited by 36

Proteasomes remain intact, but show early focal alteration in their composition in a mouse model of amyotrophic lateral sclerosis

Kabashi, E., Agar, J. N., Hong, Y. H., Taylor, D. M., Minotti, S., Figlewicz, D. A., & Durham, H. D. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05317.x · Cited by 37

Protein clearing pathways in ALS.

Ferrucci, M., Fulceri, F., Toti, L., Soldani, P., Siciliano, G., Paparelli, A., & Fornai, F. (2011) · PubMed · doi:10.4449/aib.v149i1.1258 · Cited by 35

Advances and challenges in understanding the multifaceted pathogenesis of amyotrophic lateral sclerosis

Laferrière, F., & Polymenidou, M. (2015) · Swiss Medical Weekly · doi:10.4414/smw.2015.14054 · Cited by 43

Formation of granular cytoplasmic aggregates in COS7 cells expressing mutant Cu/Zn superoxide dismutase associated with familial amyotrophic lateral sclerosis

Koide, T., Igarashi, S., Kikugawa, K., Nakano, R., Inuzuka, T., Yamada, M., Takahashi, H., & Tsuji, S. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00800-3 · Cited by 36

Temporal Response of Neural Progenitor Cells to Disease Onset and Progression in Amyotrophic Lateral Sclerosis-Like Transgenic Mice

Chi, L., Gan, L., Luo, C., Lien, L., & Liu, R. (2007) · Stem Cells and Development · doi:10.1089/scd.2006.0120 · Cited by 35

Early detachment of neuromuscular junction proteins in ALS mice with SODG93A mutation

Narai, H., Manabe, Y., Nagai, M., Nagano, I., Ohta, Y., Murakami, T., Takehisa, Y., Kamiya, T., & Abe, K. (2009) · Neurology International · doi:10.4081/ni.2009.e16 · Cited by 35

Quantitative interrogation of protein co-aggregation using multi-color fluorogenic protein aggregation sensors

Bai, Y., Wan, W., Huang, Y., Jin, W., Lyu, H., Xia, Q., Dong, X., Gao, Z., & Liu, Y. (2021) · Chemical Science · doi:10.1039/d1sc01122g · Cited by 35

Expression of Taurine Transporter (TauT) is Modulated by Heat Shock Factor 1 (HSF1) in Motor Neurons of ALS

Jung, M.-K., Kim, K.-Y., Lee, N.-Y., Kang, Y. S., Hwang, Y. J., Kim, Y., Sung, J., McKee, A. C., Kowall, N. W., Lee, J.-H., et al. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8371-9 · Cited by 35

Gene therapy for neurodegenerative and ocular diseases using lentiviral vectors

Ralph, G. S., Binley, K., Wong, L., Azzouz, M., & Mazarakis, N. D. (2005) · Clinical Science · doi:10.1042/cs20050158 · Cited by 35

Human iPSC-derived neural progenitor cells secreting GDNF provide protection in rodent models of ALS and retinal degeneration

Laperle, A., Moser, V. A., Avalos, P., Lü, B., Wu, A., Fulton, A., Ramirez, S., Garcia, V. J., Bell, S., Ho, R., et al. (2023) · Stem Cell Reports · doi:10.1016/j.stemcr.2023.03.016 · Cited by 34

Dysregulation of Astrocytic HMGB1 Signaling in Amyotrophic Lateral Sclerosis

Brambilla, L., Martorana, F., Guidotti, G., & Rossi, D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00622 · Cited by 34

γ-Oryzanol mitigates oxidative stress and prevents mutant SOD1-Related neurotoxicity in Drosophila and cell models of amyotrophic lateral sclerosis

Zhang, C., Liang, W., Wang, H., Yang, Y., Wang, T., Wang, S., Wang, X., Wang, Y., & Feng, H. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107777 · Cited by 34

Receptor-mediated endocytosis 8 (RME-8)/DNAJC13 is a novel positive modulator of autophagy and stabilizes cellular protein homeostasis

Besemer, A. S., Maus, J., Ax, M. D. A., Stein, A. H., Vo, S., Freese, C., Nalbach, K., von Hilchen, C. M., Pfalzgraf, I. F., Koziollek‐Drechsler, I., et al. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03521-y · Cited by 32

Proteomic Analysis Reveals Differentially Regulated Protein Acetylation in Human Amyotrophic Lateral Sclerosis Spinal Cord

Liu, D., Liu, C., Li, J., Azadzoi, K. M., Yang, Y., Fei, Z., Dou, K., Kowall, N. W., Choi, H.-P., Vieira, F. G., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080779 · Cited by 34

Motor Neuron Disease in Transgenic Mice With an H46R Mutant SOD1 Gene

Sasaki, S., Nagai, M., Aoki, M., Komori, T., Itoyama, Y., & Iwata, M. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000263868.84188.3b · Cited by 34

An In Vitro Model for Lewy Body-Like Hyaline Inclusion/Astrocytic Hyaline Inclusion: Induction by ER Stress with an ALS-Linked SOD1 Mutation

Yamagishi, S., Koyama, Y., Katayama, T., Taniguchi, M., Hitomi, J., Kato, M., Aoki, M., Itoyama, Y., Kato, S., & Tohyama, M. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001030 · Cited by 36

Superoxide dismutase-1 mutation-related neurotoxicity in familial amyotrophic lateral sclerosis

Shibata, N., Hirano, A., Yamamoto, T., Kato, Y., & Kobayashi, M. (2000) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/14660820050515151 · Cited by 34

Clinical and molecular aspects of motoneurone diseases: animal models, neurotrophic factors and Bcl-2 oncoprotein

Sagot, Y., Vejsada, R., & Kato, A. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)01094-8 · Cited by 34

Current developments in gene therapy for amyotrophic lateral sclerosis

Scarrott, J. M., Herranz-Martín, S., Alrafiah, A., Shaw, P. J., & Azzouz, M. (2015) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2015.1044894 · Cited by 35

Selective knockdown of mutant SOD1 in Schwann cells ameliorates disease in G85R mutant SOD1 transgenic mice

Wang, L., Pytel, P., Feltri, M. L., Wrabetz, L. G., & Roos, R. P. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.05.014 · Cited by 39

Morpholino-mediated SOD1 reduction ameliorates an amyotrophic lateral sclerosis disease phenotype

Nizzardo, M., Simoné, C., Rizzo, F., Ulzi, G., Ramirez, A., Rizzuti, M., Bordoni, A., Bucchia, M., Gatti, S., Bresolin, N., et al. (2016) · Scientific Reports · doi:10.1038/srep21301 · Cited by 33

The UPR-PERK pathway is not a promising therapeutic target for mutant SOD1-induced ALS

Dzhashiashvili, Y., Monckton, C. P., Shah, H., Kunjamma, R. B., & Popko, B. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.024 · Cited by 32

Redox susceptibility of SOD1 mutants is associated with the differential response to CCS over-expression in vivo

Son, M., Fu, Q., Puttaparthi, K., Matthews, C. M., & Elliott, J. L. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.01.005 · Cited by 33

Mice, the Motor System, and Human Motor Neuron Pathology

Nicholson, S. J., Witherden, A. S., Hafezparast, M., Martin, J. E., & Fisher, E. (2000) · Mammalian Genome · doi:10.1007/s003350010205 · Cited by 33

Composition of Soluble Misfolded Superoxide Dismutase-1 in Murine Models of Amyotrophic Lateral Sclerosis

Zetterström, P., Graffmo, K. S., Andersen, P. M., Brännström, T., & Marklund, S. L. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8204-z · Cited by 34

Modelling amyotrophic lateral sclerosis in mice

Stephenson, J., & Amor, S. (2017) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2018.10.001 · Cited by 34

Expression of a familial amyotrophic lateral sclerosis-associated mutant human superoxide dismutase in yeast leads to decreased mitochondrial electron transport

Gunther, M. R., VanGilder, R. L., Fang, J. S., & Beattie, D. S. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.08.009 · Cited by 33

Molecular dissection of ALS-associated toxicity of SOD1 in transgenic mice using an exon-fusion approach

Deng, H., Hujun, J., Fu, R., Hong, Z., Yong, S., Liu, E., Makito, H., Mauro, C. D. C., & Siddique, T. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn131 · Cited by 32

Stimulation‐Induced Mitochondrial [Ca 2+ ] Elevations in Mouse Motor Terminals: Comparison of Wild‐Type with SOD1‐G93A

Vila, L., Barrett, E. F., & Barrett, J. N. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.041905 · Cited by 32

Formation of advanced glycation end-product-modified superoxide dismutase-1 (SOD1) is one of the mechanisms responsible for inclusions common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutation, and transgenic mice expressing human SOD1 gene mutation

Kato, S., Nakashima, K., Horiuchi, S., Nagai, R., Cleveland, D. W., Liu, J., Hirano, A., Takikawa, M., Kato, M., Nakano, I., et al. (2001) · Neuropathology · doi:10.1046/j.1440-1789.2001.00359.x · Cited by 32

RNAi knockdown of Par‐4 inhibits neurosynaptic degeneration in ALS‐linked mice

Xie, J., Awad, K. S., & Guo, Q. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02834.x · Cited by 32

Clinical implications of the genetics of ALS and other motor neuron diseases

Orrell, R. W., & Figlewicz, D. A. (2001) · Neurology · doi:10.1212/wnl.57.1.9 · Cited by 32

Mutant SOD1 detoxification mechanisms in intact single cells

Ganesan, S., Rohde, G., Eckermann, K., Sroka, K., Schaefer, M. K. E., Dohm, C. P., Kermer, P., Haase, G., Wouters, F. S., Bähr, M., et al. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402262 · Cited by 31

A cysteine residue affects the conformational state and neuronal toxicity of mutant SOD1 in mice: relevance to the pathogenesis of ALS

Nagano, S., Takahashi, Y., Yamamoto, K., Masutani, H., Fujiwara, N., Urushitani, M., & Araki, T. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv093 · Cited by 31

Hyperexcitability in synaptic and firing activities of spinal motoneurons in an adult mouse model of amyotrophic lateral sclerosis

Jiang, M. C., Adimula, A., Birch, D. V., & Heckman, C. J. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.08.041 · Cited by 31

Levels of membrane fluidity in the spinal cord and the brain in an animal model of amyotrophic lateral sclerosis

Mena, F. J. M., Piedrafita, E., González‐Mingot, C., Larrodé, P., Muñoz, M. J., Martínez‐Ballarín, E., Reiter, R. J., Osta, R., & García, J. J. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9348-5 · Cited by 30

Methylene blue administration fails to confer neuroprotection in two amyotrophic lateral sclerosis mouse models

Audet, J., Soucy, G., & Julien, J. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2011.12.047 · Cited by 30

Astrocytes As the Main Players in Primary Degenerative Disorders of the Human Central Nervous System

Capani, F., Quarracino, C., Caccuri, R. L., & Sica, R. E. P. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00045 · Cited by 30

Fasciculation intensity and disease progression in amyotrophic lateral sclerosis

Tsugawa, J., Dharmadasa, T., Ma, Y., Huynh, W., Vucic, S., & Kiernan, M. C. (2018) · Clinical Neurophysiology · doi:10.1016/j.clinph.2018.07.015 · Cited by 31

Imaging spinal cord activity in behaving animals

Nelson, N. A., Wang, X., Cook, D., Carey, E. M., & Nimmerjahn, A. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.112974 · Cited by 30

Astrocytes: Dissecting Their Diverse Roles in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Valori, C. F., Sulmona, C., Brambilla, L., & Rossi, D. (2023) · Cells · doi:10.3390/cells12111450 · Cited by 30

Changes in the Spinal Cord Proteome of an Amyotrophic Lateral Sclerosis Murine Model Determined by Differential In-gel Electrophoresis

Bergemalm, D., Forsberg, K., Jonsson, P. A., Graffmo, K. S., Brännström, T., Andersen, P. M., Antti, H., & Marklund, S. L. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900046-mcp200 · Cited by 30

Phenotypic heterogeneity of astrocytes in motor neuron disease

Trías, E., Barbeito, L., & Yamanaka, K. (2018) · Clinical and Experimental Neuroimmunology · doi:10.1111/cen3.12476 · Cited by 31

Amyotrophic lateral sclerosis: pathogenesis.

Robberecht, W., Bosch, L. V. D., & Vleminckx, V. (2000) · PubMed · Cited by 30

Targeted stem cell transplantation strategies in ALS

Lepore, A. C., & Maragakis, N. J. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.09.005 · Cited by 30

Synaptic sprouting increases the uptake capacities of motoneurons in amyotrophic lateral sclerosis mice

Millecamps, S., Nicolle, D. M., Ceballos-Picot, I., Mallet, J. J., & Barkats, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.131031098 · 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

A liquid-to-solid phase transition of Cu/Zn superoxide dismutase 1 initiated by oxidation and disease mutation

Gu, S., Xu, M., Chen, L., Shi, X., & Luo, S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102857 · Cited by 32

Amyotrophic Lateral Sclerosis

Jackson, M., & Rothstein, J. D. (2002) · Handbook of experimental pharmacology · doi:10.1007/978-3-662-06274-6_16 · Cited by 29

Boosting the peripheral immune response in the skeletal muscles improved motor function in ALS transgenic mice

Trolese, M. C., Scarpa, C., Melfi, V., Fabbrizio, P., Sironi, F. M., Rossi, M., Bendotti, C., & Nardo, G. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.04.018 · Cited by 27

The Cell Autonomous and Non-Cell Autonomous Aspects of Neuronal Vulnerability and Resilience in Amyotrophic Lateral Sclerosis

Schweingruber, C., & Hedlund, E. (2022) · Biology · doi:10.3390/biology11081191 · Cited by 29

Wild-type human SOD1 overexpression does not accelerate motor neuron disease in mice expressing murine Sod1G86R

Audet, J., Gowing, G., & Julien, J. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.031 · Cited by 29

Recent advances in amyotrophic lateral sclerosis research

Przedborski, S., Mitsumoto, H., & Rowland, L. P. (2003) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-003-0041-x · Cited by 29

Neuronal Loss and Decreased GLT-1 Expression Observed in the Spinal Cord of Pembroke Welsh Corgi Dogs With Canine Degenerative Myelopathy

Ogawa, M., Uchida, K., Yamato, O., Inaba, M., Uddin, M. M., & Nakayama, H. (2013) · Veterinary Pathology · doi:10.1177/0300985813495899 · Cited by 29

Prediction of Misfolding-Specific Epitopes in SOD1 Using Collective Coordinates

Peng, X., Cashman, N. R., & Plotkin, S. S. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b07680 · Cited by 29

Evidence Linking Protein Misfolding to Quality Control in Progressive Neurodegenerative Diseases

Kabir, M. T., Uddin, M. S., Abdeen, A., Ashraf, G. M., Perveen, A., Hafeez, A., Bin-Jumah, M. N., & Abdel‐Daim, M. M. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200618114924 · Cited by 29

Light-induced Retinal Damage in Mice Carrying a Mutated SOD I Gene

Mittag, T. W., Bayer, A. U., & Vail, M. M. L. (1999) · Experimental Eye Research · doi:10.1006/exer.1999.0748 · Cited by 29

Transgenic Mouse Models of Alzheimer's Disease and Amyotrophic Lateral Sclerosis

Borchelt, D., Wong, P. C., Sisodia, S. S., & Price, D. L. (1998) · Brain Pathology · doi:10.1111/j.1750-3639.1998.tb00198.x · Cited by 29

Glutamatergic receptors regulate expression, phosphorylation and accumulation of neurofilaments in spinal cord neurons

Vartiainen, N., Tikka, T., Keinänen, R., Chan, P. H., & Koıstınaho, J. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00200-6 · Cited by 29

Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations

Wang, L., Ma, Y., Zhang, M.-Y., Yuan, H., Li, X.-N., Xia, W., Zhao, K., Huang, X., Chen, J., 邹良玉, et al. (2024) · Science Advances · doi:10.1126/sciadv.ado8499 · Cited by 30

Links between Electrophysiological and Molecular Pathology of Amyotrophic Lateral Sclerosis

Quinlan, K. A. (2011) · Integrative and Comparative Biology · doi:10.1093/icb/icr116 · Cited by 29

Effects of Cellular Pathway Disturbances on Misfolded Superoxide Dismutase-1 in Fibroblasts Derived from ALS Patients

Keskin, I., Forsgren, E., Lange, D. J., Weber, M., Birve, A., Synofzik, M., Gilthorpe, J. D., Andersen, P. M., & Marklund, S. L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0150133 · Cited by 29

A small-molecule inhibitor of SOD1-Derlin-1 interaction ameliorates pathology in an ALS mouse model

Tsuburaya, N., Homma, K., Higuchi, T., Balia, A. G., Yamakoshi, H., Shibata, N., Nakamura, S., Nakagawa, H., Ikeda, S., Umezawa, N., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05127-2 · Cited by 29

Interactions of amyloid coaggregates with biomolecules and its relevance to neurodegeneration

Murakami, K., & Ono, K. (2022) · The FASEB Journal · doi:10.1096/fj.202200235r · Cited by 28

Activation of a glycine transporter on spinal cord neurons causes enhanced glutamate release in a mouse model of amyotrophic lateral sclerosis

Raiteri, L., Paolucci, E., Prisco, S., Raiteri, M., & Bonanno, G. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705142 · Cited by 28

Proteomic analysis of mitochondrial dysfunction in neurodegenerative diseases

Rodolfo, C., Ciccosanti, F., Giacomo, G. D., Piacentini, M., & Fimia, G. M. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.43 · Cited by 29

Structures of mouse SOD1 and human/mouse SOD1 chimeras

Seetharaman, S. V., Taylor, A. B., Holloway, S., & Hart, P. J. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.08.014 · Cited by 28

Intraspinal Cell Transplantation for Targeting Cervical Ventral Horn in Amyotrophic Lateral Sclerosis and Traumatic Spinal Cord Injury

Lepore, A. C. (2011) · Journal of Visualized Experiments · doi:10.3791/3069 · Cited by 25

A comparison of in vitro properties of resting SOD1 transgenic microglia reveals evidence of reduced neuroprotective function

Sargsyan, S. A., Blackburn, D. J., Barber, S. C., Großkreutz, J., Vos, K. J. D., Monk, P. N., & Shaw, P. J. (2011) · BMC Neuroscience · doi:10.1186/1471-2202-12-91 · Cited by 28

The in vivo contribution of motor neuron TrkB receptors to mutant SOD1 motor neuron disease

Zhai, J., Zhou, W., Li, J., Hayworth, C. R., Zhang, L., Misawa, H., Klein, R., Scherer, S. S., Balice‐Gordon, R. J., & Kalb, R. G. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr335 · Cited by 28

Amyotrophic Lateral Sclerosis Pathogenesis Converges on Defects in Protein Homeostasis Associated with TDP-43 Mislocalization and Proteasome-Mediated Degradation Overload

Lin, G., Mao, D., & Bellen, H. J. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.004 · Cited by 29

Spatiotemporal progression of ubiquitin-proteasome system inhibition after status epilepticus suggests protective adaptation against hippocampal injury

Engel, T., de Villarreal, J. M., Henke, C., Jimenez-Mateos, E. M., Sanz‐Rodriguez, A., Alves, M., Hernandez-Santana, Y., Brennan, G. P., Kenny, A., Campbell, A., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0163-2 · Cited by 28

Examining the relationship between astrocyte dysfunction and neurodegeneration in ALS using hiPSCs

Halpern, M., Brennand, K., & Gregory, J. A. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104562 · Cited by 30

Early and Selective Pathology of Light Chain Neurofilament in the Spinal Cord and Sciatic Nerve of G86R Mutant Superoxide Dismutase Transgenic Mice

Morrison, B. M., Shu, I.-W., Wilcox, A. L., Gordon, J. W., & Morrison, J. H. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7457 · Cited by 28

Therapeutic gene silencing in neurological disorders, using interfering RNA

Ralph, G. S., Mazarakis, N. D., & Azzouz, M. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0649-1 · Cited by 28

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Ghadge, G. D., Wang, L., Sharma, K., Monti, A. L., Bindokas, V. P., Stevens, F. J., & Roos, R. P. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.07.006 · Cited by 28

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Houseweart, M. K., & Cleveland, D. W. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-15-06446.1999 · Cited by 28

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Kadekawa, J., Fujimura, H., Ogawa, Y., Hattori, N., Kaido, M., Nishimura, T., Yoshikawa, H., Shirahata, N., Sakoda, S., & Yanagihara, T. (1997) · Acta Neuropathologica · doi:10.1007/s004010050758 · Cited by 28

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Barnett, D., Bohmbach, K., Grelot, V., Charlet, A., Dallérac, G. M., Ju, Y. H., Nagai, J., & Orr, A. G. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1376-23.2023 · Cited by 27

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Cha, J. R. C., Louis, K. S., Tradewell, M. L., Gentil, B. J., Minotti, S., Jaffer, Z. M., Chen, R., Rubenstein, A. E., & Durham, H. D. (2013) · Cell Stress and Chaperones · doi:10.1007/s12192-013-0467-2 · Cited by 25

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Issue Cover (October 2015)

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

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