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

Dual transplantation of human neural stem cells into cervical and lumbar cord ameliorates motor neuron disease in SOD1 transgenic rats

Xu, L., Shen, P., Hazel, T. G., Johe, K. K., & Koliatsos, V. E. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.03.017 · Cited by 90

SIRT1 overexpression ameliorates a mouse model of SOD1-linked amyotrophic lateral sclerosis via HSF1/HSP70i chaperone system

Watanabe, S., Ageta‐Ishihara, N., Nagatsu, S., Takao, K., Komine, O., Endo, F., Miyakawa, T., Misawa, H., Takahashi, R., Kinoshita, M., et al. (2014) · Molecular Brain · doi:10.1186/s13041-014-0062-1 · Cited by 90

Amyotrophic lateral sclerosis: update and new developments

Perry, J. J. P., Pratt, A. J., & Getzoff (2012) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s19803 · Cited by 94

Mutant superoxide dismutase aggregates from human spinal cord transmit amyotrophic lateral sclerosis

Bidhendi, E. E., Bergh, J., Zetterström, P., Forsberg, K., Pakkenberg, B., Andersen, P. M., Marklund, S. L., & Brännström, T. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1915-y · Cited by 89

Neurodegeneration and neuroprotection in multiple sclerosis and other neurodegenerative diseases

Dhib-Jalbut, S. S., Arnold, D. L., Cleveland, D. W., Fisher, M., Friedlander, R. M., Mouradian, M. M., Przedborski, S., Trapp, B. D., Wyss‐Coray, T., & Yong, V. W. (2006) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2006.03.027 · Cited by 91

Mutant Profilin1 transgenic mice recapitulate cardinal features of motor neuron disease

Fil, D., DeLoach, A., Yadav, S., Alkam, D., MacNicol, M. C., Singh, A., Compadre, C. M., Goellner, J. J., O’Brien, C. A., Fahmi, T., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw429 · Cited by 88

Lack of behavioral and neuropathological effects of dietary β-methylamino-l-alanine (BMAA) in mice

Cruz-Aguado, R., Winkler, D., & Shaw, C. A. (2006) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2006.05.012 · Cited by 88

The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis

Wright, G. S. A., Antonyuk, S. V., & Hasnain, S. S. (2019) · Quarterly Reviews of Biophysics · doi:10.1017/s003358351900012x · Cited by 87

Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1

Shaw, B. F., Lelie, H., Durazo, A., Nersissian, A. M., Xu, G., Chan, P. K., Gralla, E. B., Tiwari, A., Hayward, L. J., Borchelt, D., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707751200 · Cited by 88

Global gene expression profiling of somatic motor neuron populations with different vulnerability identify molecules and pathways of degeneration and protection

Hedlund, E., Karlsson, M., Osborn, T. M., Ludwig, W. W., & Ole Isacson, A. (2010) · Brain · doi:10.1093/brain/awq167 · Cited by 93

Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: a putative mechanism of degeneration

Morrison, B. M., & Morrison, J. H. (1999) · Brain Research Reviews · doi:10.1016/s0165-0173(98)00049-6 · Cited by 88

Expression of mutant SOD1 G93A in astrocytes induces functional deficits in motoneuron mitochondria

Bilsland, L. G., Nirmalananthan, N., Yip, J., Greensmith, L., & Duchen, M. R. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05699.x · Cited by 88

Realistic Prospects for Stem Cell Therapeutics

Daley, G. Q., Goodell, M. A., & Snyder, E. Y. (2003) · Hematology · doi:10.1182/asheducation-2003.1.398 · Cited by 89

Formation of multinucleated giant cells and microglial degeneration in rats expressing a mutant Cu/Zn superoxide dismutase gene

Fendrick, S. E., Xue, Q., & Streit, W. J. (2007) · Journal of Neuroinflammation · doi:10.1186/1742-2094-4-9 · Cited by 88

Motor neuron disease, TDP-43 pathology, and memory deficits in mice expressing ALS–FTD-linked UBQLN2 mutations

Le, N. T. T., Chang, L., Kovlyagina, I., Georgiou, P., Safren, N., Braunstein, K. E., Kvarta, M. D., Dyke, A. M. V., LeGates, T. A., Philips, T., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608432113 · Cited by 96

A Novel Action of Histone Deacetylase Inhibitors in a Protein Aggresome Disease Model

Corcoran, L., Mitchison, T. J., & Liu, Q. (2004) · Current Biology · doi:10.1016/j.cub.2004.03.003 · Cited by 87

The multifaceted role of glial cells in amyotrophic lateral sclerosis

Valori, C. F., Brambilla, L., Martorana, F., & Rossi, D. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1429-7 · Cited by 88

Mapping superoxide dismutase 1 domains of non‐native interaction: roles of intra‐ and intermolecular disulfide bonding in aggregation

Wang, J., Xu, G. M., & Borchelt, D. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03642.x · Cited by 87

Of mice and men: Reconciling preclinical ALS mouse studies and human clinical trials

Rothstein, J. D. (2003) · Annals of Neurology · doi:10.1002/ana.10561 · Cited by 86

Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A

Galaleldeen, A., Strange, R. W., Whitson, L. J., Antonyuk, S. V., Narayana, N., Taylor, A. B., Schuermann, J. P., Holloway, S. P., Hasnain, S. S., & Hart, P. J. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.09.020 · Cited by 84

The neurobiology of amyotrophic lateral sclerosis

Bento‐Abreu, A., Damme, P. V., Bosch, L. V. D., & Robberecht, W. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07260.x · Cited by 89

Tryptophan 32 Potentiates Aggregation and Cytotoxicity of a Copper/Zinc Superoxide Dismutase Mutant Associated with Familial Amyotrophic Lateral Sclerosis

Taylor, D. M., Gibbs, B. F., Kabashi, E., Minotti, S., Durham, H. D., & Agar, J. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610119200 · Cited by 85

Dysregulation of intracellular copper homeostasis is common to transgenic mice expressing human mutant superoxide dismutase-1s regardless of their copper-binding abilities

Tokuda, E., Okawa, E., Watanabe, S., Ono, S.-I., & Marklund, S. L. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.001 · Cited by 83

Environmental, pharmacological, and genetic modulation of the HD phenotype in transgenic mice

Schilling, G., Savonenko, A. V., Coonfield, M. L., Morton, J. L., Vorovich, E. B., Gale, A., Neslon, C., Chan, N., Eaton, M., Fromholt, D., et al. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.01.003 · Cited by 85

Extensive exercise is not harmful in amyotrophic lateral sclerosis

Liebetanz, D., Hagemann, K., von Lewinski, F., Kahler, E., & Paulus, W. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03769.x · Cited by 85

Translational Control of Glial Glutamate Transporter EAAT2 Expression

Tian, G., Lai, L., Guo, H., Lin, Y., Butchbach, M. E. R., Chang, Y., & Lin, C. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609822200 · Cited by 85

Metallothionein Expression Is Altered in a Transgenic Murine Model of Familial Amyotrophic Lateral Sclerosis

Gong, Y. H., & Elliott, J. L. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7323 · Cited by 85

Lack of involvement of neuronal nitric oxide synthase in the pathogenesis of a transgenic mouse model of familial amyotrophic lateral sclerosis

Facchinetti, F., Sasaki, M., Cutting, F. B., Macdonald, J. E., Reif, D. W., Beal, M. F., Huang, P. L., Dawson, T. M., Gurney, M. E., Dawson, V. L., et al. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00492-8 · Cited by 85

Amyotrophic lateral sclerosis mutant vesicle-associated membrane protein-associated protein-B transgenic mice develop TAR-DNA-binding protein-43 pathology

Tudor, E. L., Galtrey, C. M., Perkinton, M. S., Lau, K., Vos, K. J. D., Mitchell, J. C., Ackerley, S., Hortobágyi, T., Vámos, E., Leigh, P. N., et al. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.02.035 · Cited by 90

Molecular Signalling Mediating the Protective Effect of A1 Adenosine and mGlu3 Metabotropic Glutamate Receptor Activation against Apoptosis by Oxygen/Glucose Deprivation in Cultured Astrocytes

Ciccarelli, R., D’Alimonte, I., Ballerini, P., D’Auro, M., Nargi, E., Buccella, S., Iorio, P. D., Bruno, V., Nicoletti, F., & Caciagli, F. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.031617 · Cited by 84

The efficacy of trientine or ascorbate alone compared to that of the combined treatment with these two agents in familial amyotrophic lateral sclerosis model mice

Nagano, S., Fujii, Y., Yamamoto, T., Taniyama, M., Fukada, K., Yanagihara, T., & Sakoda, S. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(02)00014-6 · Cited by 83

Aggregates of mutant protein appear progressively in dendrites, in periaxonal processes of oligodendrocytes, and in neuronal and astrocytic perikarya of mice expressing the SOD1G93A mutation of familial amyotrophic lateral sclerosis

Stieber, A., Gonatas, J. O., & Gonatas, N. K. (2000) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(00)00351-8 · Cited by 76

IFNγ triggers a LIGHT-dependent selective death of motoneurons contributing to the non-cell-autonomous effects of mutant SOD1

Aebischer, J., Cassina, P., Otsmane, B., Moumen, A., Seilhean, D., Meininger, V., Barbeito, L., Pettmann, B., & Raoul, C. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.143 · Cited by 83

The role of excitotoxicity in ALS - what is the evidence?

Ludolph, A. C., Meyer, T., & Riepe, M. W. (2000) · Journal of Neurology · doi:10.1007/s004150050552 · Cited by 84

Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: Mechanistic relationship and differential sensitivity to intervention

Tradewell, M. L., Cooper, L. A., Minotti, S., & Durham, H. D. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.016 · Cited by 81

Protein misfolding in the late‐onset neurodegenerative diseases: Common themes and the unique case of amyotrophic lateral sclerosis

Mulligan, V. K., & Chakrabartty, A. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24285 · Cited by 81

Altered axonal architecture by removal of the heavily phosphorylated neurofilament tail domains strongly slows superoxide dismutase 1 mutant-mediated ALS

Lobsiger, C. S., Garcia, M. L., Ward, C. M., & Cleveland, D. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503862102 · Cited by 81

Insights into Lou Gehrig's Disease from the Structure and Instability of the A4V Mutant of Human Cu,Zn Superoxide Dismutase

Cardoso, R. M. F., THAYER, M. M., DiDonato, M., Lo, T. P., Bruns, C. K., Getzoff, E. D., & Tainer, J. A. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01090-2 · Cited by 81

Selective loss of neurofilament expression in Cu/Zn superoxide dismutase (SOD1) linked amyotrophic lateral sclerosis

Menzies, F. M., Grierson, A. J., Cookson, M., Heath, P. R., Tomkins, J., Figlewicz, D. A., Ince, P. G., & Shaw, P. J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01045.x · Cited by 81

Advanced Glycation Endproducts in Neurofilament Conglomeration of Motoneurons in Familial and Sporadic Amyotrophic Lateral Sclerosis

Chou, S. M., Wang, H. S., Taniguchi, A., & Bucala, R. (1998) · Molecular Medicine · doi:10.1007/bf03401739 · Cited by 81

Identification of alternative splicing forms of GLT-1 mRNA in the spinal cord of amyotrophic lateral sclerosis patients

Nagai, M., Abe, K., Okamoto, K., & Itoyama, Y. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00158-x · Cited by 81

Metal Deficiency Increases Aberrant Hydrophobicity of Mutant Superoxide Dismutases That Cause Amyotrophic Lateral Sclerosis

Tiwari, A., Liba, A., Sohn, S. H., Seetharaman, S. V., Bilsel, O., Matthews, C. R., Hart, P. J., Valentine, J. S., & Hayward, L. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.043729 · Cited by 80

Macrophage migration inhibitory factor: A multifaceted cytokine implicated in multiple neurological diseases

Leyton-Jaimes, M. F., Kahn, J., & Israelson, A. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.06.021 · Cited by 80

The deletion of mutant SOD1 via CRISPR/Cas9/sgRNA prolongs survival in an amyotrophic lateral sclerosis mouse model

Duan, W., Guo, M., Yi, L., Liu, Y., Li, Z., Ma, Y., Zhang, G., Liu, Y., Bu, H., Song, X., et al. (2019) · Gene Therapy · doi:10.1038/s41434-019-0116-1 · Cited by 79

Synphilin-1 is present in Lewy bodies in Parkinson's disease

Wakabayashi, K., Engelender, S., Yoshimoto, M., Tsuji, S., Ross, C. A., & Takahashi, H. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200004)47:4 · Cited by 269

Cystatin C protects neuronal cells against mutant copper-zinc superoxide dismutase-mediated toxicity

Watanabe, S., Hayakawa, T., Wakasugi, K., & Yamanaka, K. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.459 · Cited by 81

Developing mouse models of aging: a consideration of strain differences in age-related behavioral and neural parameters☆

Ingram, D. K., & Jucker, M. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00033-0 · Cited by 80

From molecule to molecule and cell to cell: Prion-like mechanisms in amyotrophic lateral sclerosis

Grad, L. I., Fernando, S. M., & Cashman, N. R. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.009 · Cited by 80

Role and Therapeutic Potential of Astrocytes in Amyotrophic Lateral Sclerosis

Pehar, M., Harlan, B. A., Killoy, K. M., & Vargas, M. R. (2018) · Current Pharmaceutical Design · doi:10.2174/1381612823666170622095802 · Cited by 84

Causative Genes in Amyotrophic Lateral Sclerosis and Protein Degradation Pathways: a Link to Neurodegeneration

Maurel, C., Dangoumau, A., Marouillat, S., Brulard, C., Chami, A. A., Hergesheimer, R. C., Corcia, P., Blasco, H., Andres, C. R., & Vourc’h, P. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0856-0 · Cited by 82

Molecularly defined cortical astroglia subpopulation modulates neurons via secretion of Norrin

Miller, S., Philips, T., Kim, N., Dastgheyb, R. M., Chen, Z., Hsieh, Y.-C., Daigle, J. G., Datta, M. S., Chew, J., Vidensky, S., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0366-7 · Cited by 78

Post-translational Regulation of GLT-1 in Neurological Diseases and Its Potential as an Effective Therapeutic Target

Peterson, A. R., & Binder, D. K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00164 · Cited by 82

Early signs of motoneuron vulnerability in a disease model system: Characterization of transverse slice cultures of spinal cord isolated from embryonic ALS mice

Avossa, D., Grandolfo, M., Mazzarol, F., Zatta, M., & Ballerini, L. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2005.12.009 · Cited by 78

Amyotrophic Lateral Sclerosis-associated Copper/Zinc Superoxide Dismutase Mutations Preferentially Reduce the Repulsive Charge of the Proteins

Sandelin, E., Nordlund, A., Andersen, P. M., Marklund, S. L., & Oliveberg, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700765200 · Cited by 78

Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes

Pratt, A. J., Shin, D. S., Merz, G. E., Rambo, R. P., Lancaster, W. A., Dyer, K. N., Borbat, P. P., Poole, F. L., Adams, M. W. W., Freed, J. H., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308531111 · Cited by 80

Perspectives for Future Use of Extracellular Vesicles from Umbilical Cord- and Adipose Tissue-Derived Mesenchymal Stem/Stromal Cells in Regenerative Therapies—Synthetic Review

Lelek, J., & Zuba‐Surma, E. K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030799 · Cited by 76

Nearly 30 Years of Animal Models to Study Amyotrophic Lateral Sclerosis: A Historical Overview and Future Perspectives

Bonifacino, T., Zerbo, R. A., Balbi, M., Torazza, C., Frumento, G., Fedele, E., Bonanno, G., & Milanese, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212236 · Cited by 82

Oxidative stress and antioxidant enzyme upregulation in SOD1‐G93A mouse skeletal muscle

Mahoney, D. J., Kaczor, J. J., Bourgeois, J. M., Yasuda, N., & Tarnopolsky, M. A. (2006) · Muscle & Nerve · doi:10.1002/mus.20542 · Cited by 80

Morphological differences between wild‐type and transgenic superoxide dismutase 1 lumbar motoneurons in postnatal mice

Amendola, J., & Durand, J. (2008) · The Journal of Comparative Neurology · doi:10.1002/cne.21818 · Cited by 77

Cu/Zn-superoxide dismutase (GLY93→ALA) mutation alters AMPA receptor subunit expression and function and potentiates kainate-mediated toxicity in motor neurons in culture

Spalloni, A., Albo, F., Ferrari, F., Mercuri, N. B., Bernardi, G., Zona, C., & Longone, P. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.11.012 · Cited by 77

Calcium: the Darth Vader of ALS

Appel, S. H., Beers, D. R., Siklós, L., Engelhardt, J., & Mosier, D. R. (2001) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/146608201300079418 · Cited by 88

Progressive spinal axonal degeneration and slowness in ALS2‐deficient mice

Yamanaka, K., Miller, T. M., McAlonis‐Downes, M., Chun, S. J., & Cleveland, D. W. (2006) · Annals of Neurology · doi:10.1002/ana.20888 · Cited by 77

Aggregate formation in the spinal cord of mutant SOD1 transgenic mice is reversible and mediated by proteasomes

Puttaparthi, K., Wójcik, C., Rajendran, B., Demartino, G., & Elliott, J. L. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02028.x · Cited by 77

MAP4K4 Activation Mediates Motor Neuron Degeneration in Amyotrophic Lateral Sclerosis

Wu, C., Watts, M. E., & Rubin, L. L. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.019 · Cited by 78

Structural and kinetic analysis of protein-aggregate strains in vivo using binary epitope mapping

Bergh, J., Zetterström, P., Andersen, P. M., Brännström, T., Graffmo, K. S., Jonsson, P., Lang, L., Danielsson, J., Oliveberg, M., & Marklund, S. L. (2015) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1419228112 · Cited by 78

Metallothionein proteins expression, copper and zinc concentrations, and lipid peroxidation level in a rodent model for amyotrophic lateral sclerosis

Tokuda, E., Ono, S.-I., Ishige, K., Naganuma, A., Ito, Y., & Suzuki, T. (2006) · Toxicology · doi:10.1016/j.tox.2006.09.011 · Cited by 76

Aggregation of ubiquitin and a mutant ALS-linked SOD1 protein correlate with disease progression and fragmentation of the Golgi apparatus

Stieber, A., Gonatas, J. O., & Gonatas, N. K. (2000) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(99)00300-7 · Cited by 76

Early Functional Deficit and Microglial Disturbances in a Mouse Model of Amyotrophic Lateral Sclerosis

Gerber, Y. N., Sabourin, J.-C., Rábano, M., Vivanco, M. D., & Perrin, F. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036000 · Cited by 76

Intracellular Pathways of Copper Trafficking in Yeast and Humans

Culotta, V., Lin, S.-J., Schmidt, P. J., Klomp, L. W. J., Casareno, R. L. B., & Gitlin, J. D. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4859-1_22 · Cited by 76

Glial Cells—The Strategic Targets in Amyotrophic Lateral Sclerosis Treatment

Filipi, T., Heřmanová, Z., Turečková, J., Vaňátko, O., & Anděrová, M. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9010261 · Cited by 76

Local Unfolding in a Destabilized, Pathogenic Variant of Superoxide Dismutase 1 Observed with H/D Exchange and Mass Spectrometry

Shaw, B. F., Durazo, A., Nersissian, A. M., Whitelegge, J. P., Faull, K. F., & Valentine, J. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600623200 · Cited by 74

A Role for Copper in the Toxicity of Zinc-Deficient Superoxide Dismutase to Motor Neurons in Amyotrophic Lateral Sclerosis

Trumbull, K. A., & Beckman, J. S. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2574 · Cited by 79

PPAR gamma activation is neuroprotective in a Drosophila model of ALS based on TDP-43

Joardar, A., Menzl, J., Podolsky, T. C., Manzo, E., Estes, P. S., Ashford, S., & Zarnescu, D. C. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu587 · Cited by 76

TGFβ Trophic Factors Differentially Modulate Motor Axon Outgrowth and Protection from Excitotoxicity

Ho, T. W., Bristol, L. A., Coccia, C., Li, Y., Milbrandt, J., Johnson, E. M., Jin, L., Bar-Peled, O., Griffin, J. W., & Rothstein, J. D. (2000) · Experimental Neurology · doi:10.1006/exnr.1999.7290 · Cited by 75

The involvement of the Golgi apparatus in the pathogenesis of amyotrophic lateral sclerosis, Alzheimer's disease, and ricin intoxication

Gonatas, N. K., Gonatas, J. O., & Stieber, A. (1998) · Histochemistry and Cell Biology · doi:10.1007/s004180050257 · Cited by 75

Autophagy in Astrocytes and its Implications in Neurodegeneration

Sung, K., & Jiménez-Sánchez, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.041 · Cited by 78

Integrative role of cPLA2 with COX‐2 and the effect of non‐steriodal anti‐inflammatory drugs in a transgenic mouse model of amyotrophic lateral sclerosis

Kiaei, M., Kipiani, K., Petri, S., Choi, D., Chen, J., Calingasan, N. Y., & Beal, M. F. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03024.x · Cited by 74

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Wang, H., Ying, Z., & Wang, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.299990 · Cited by 77

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Provenzano, F., Torazza, C., Bonifacino, T., Bonanno, G., & Milanese, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015430 · Cited by 78

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Strong, M. J. (2001) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100001505 · Cited by 73

Lentiviral vectors for treating and modeling human CNS disorders

Azzouz, M., Kingsman, S. M., & Mazarakis, N. D. (2004) · The Journal of Gene Medicine · doi:10.1002/jgm.600 · Cited by 71

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Velde, C. V., Garcia, M. L., Yin, X., Trapp, B. D., & Cleveland, D. W. (2004) · NeuroMolecular Medicine · doi:10.1385/nmm:5:3:193 · Cited by 77

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Snyder, E. Y., Daley, G. Q., & Goodell, M. A. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20033 · Cited by 72

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Gill, C., Phelan, J. P., Hatzipetros, T., Kidd, J. D., Tassinari, V. R., Levine, B. A., Wang, M. Z., Moreno, A., Thompson, K., Maier, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-43164-z · Cited by 78

Impairment of axonal transport in the axon hillock and the initial segment of anterior horn neurons in transgenic mice with a G93A mutant SOD1 gene

Sasaki, S., Warita, H., Abe, K., & Iwata, M. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1021-9 · Cited by 72

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Kato, S., Horiuchi, S., Liu, J., Cleveland, D. W., Shibata, N., Nakashima, K., Nagai, R., Hirano, A., Takikawa, M., Kato, M., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010000226 · Cited by 72

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Sato, T., Nakanishi, T., Yamamoto, Y., Andersen, P. M., Ogawa, Y., Fukada, K., Zhou, Z., Aoike, F., Sugai, F., Nagano, S., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000188760.53922.05 · Cited by 72

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Wong, P. C., Rothstein, J. D., & Price, D. L. (1998) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(98)80123-2 · Cited by 72

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Lladó, J., Haenggeli, C., Pardo, A. C., Wong, V., Benson, L. M., Coccia, C., Rothstein, J. D., Shefner, J. M., & Maragakis, N. J. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.06.019 · Cited by 71

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Neusch, C., Bähr, M., & Schneider‐Gold, C. (2007) · Muscle & Nerve · doi:10.1002/mus.20768 · Cited by 69

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Ruan, Q. (2006) · Frontiers in bioscience · doi:10.2741/2111 · Cited by 71

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Rumfeldt, J., Stathopulos, P. B., Chakrabarrty, A., Lepock, J. R., & Meiering, E. M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.042 · Cited by 70

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Iłżecka, J. (2003) · Acta Neurologica Scandinavica · doi:10.1034/j.1600-0404.2003.00102.x · Cited by 70

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Grad, L. I., & Cashman, N. R. (2014) · Prion · doi:10.4161/pri.27602 · Cited by 69

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Vargas, M. R., Johnson, D. A., & Johnson, J. A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.04.025 · Cited by 70

Dismutase-competent SOD1 mutant accumulation in myelinating Schwann cells is not detrimental to normal or transgenic ALS model mice

Turner, B. J., Ackerley, S., Davies, K. E., & Talbot, K. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp550 · Cited by 69

Expression of SOD1 G93A or wild‐type SOD1 in primary cultures of astrocytes down‐regulates the glutamate transporter GLT‐1: lack of involvement of oxidative stress

Tortarolo, M., Crossthwaite, A. J., Conforti, L., Spencer, J. P. E., Williams, R. J., Bendotti, C., & Rattray, M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02208.x · Cited by 69

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Ittner, L. M., Halliday, G. M., Kril, J. J., Götz, J., Hodges, J. R., & Kiernan, M. C. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.65 · Cited by 70

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Issue Cover (October 2015)

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

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