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Effects of an Inhibitor of Poly(ADP-Ribose) Polymerase, Desmethylselegiline, Trientine, and Lipoic Acid in Transgenic ALS Mice

Andreassen, O. A., Dedeoglu, A., Friedlich, A., Ferrante, K. L., Hughes, D., Szabo, C., & Beal, M. F. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7633 · Cited by 96

Modelling brain diseases in mice: the challenges of design and analysis

Watase, K., & Zoghbi, H. Y. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1045 · Cited by 94

A polymorphism in theEAAT2promoter is associated with higher glutamate concentrations and higher frequency of progressing stroke

Mallolas, J., Hurtado, O., Castellanos, M., Blanco, M., Sobrino, T., Serena, J. L., Vivancos, J., Castillo, J., Lizasoaín, I., Moro, M. Á., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051979 · Cited by 95

The basic aspects of therapeutics in amyotrophic lateral sclerosis

Strong, M. J. (2003) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(03)00040-8 · Cited by 94

Protective effects of cardiotrophin-1 adenoviral gene transfer on neuromuscular degeneration in transgenic ALS mice

Bordet, T. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.18.1925 · Cited by 92

Cellular therapy to target neuroinflammation in amyotrophic lateral sclerosis

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Moderate exercise delays the motor performance decline in a transgenic model of ALS

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FOXO3a Is Broadly Neuroprotective In Vitro and In Vivo against Insults Implicated in Motor Neuron Diseases

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Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls

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The slow Wallerian degeneration gene, WldS, inhibits axonal spheroid pathology in gracile axonal dystrophy mice

Mi, W. (2004) · Brain · doi:10.1093/brain/awh368 · Cited by 115

GLT-1 transporter: An effective pharmacological target for various neurological disorders

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The Influence of Na+, K+-ATPase on Glutamate Signaling in Neurodegenerative Diseases and Senescence

Kinoshita, P. F., Leite, J. A., Orellana, A. M., Vasconcelos, A. R., Quintas, L. E. M., Kawamoto, E. M., & Scavone, C. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00195 · Cited by 93

Transgenic and physiological mouse models give insights into different aspects of amyotrophic lateral sclerosis

Giorgio, F. D., Maduro, C., Fisher, E., & Acevedo‐Arozena, A. (2019) · Disease Models & Mechanisms · doi:10.1242/dmm.037424 · Cited by 91

Protein interaction networks in neurodegenerative diseases: From physiological function to aggregation

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Global Loss of Na,K-ATPase and Its Nitric Oxide-Mediated Regulation in a Transgenic Mouse Model of Amyotrophic Lateral Sclerosis

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Selective ablation of proliferating astrocytes does not affect disease outcome in either acute or chronic models of motor neuron degeneration

Lepore, A. C., Dejea, C. M., Carmen, J., Rauck, B. M., Kerr, D. A., Sofroniew, M. V., & Maragakis, N. J. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.02.020 · Cited by 92

Immature Copper-Zinc Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis

Seetharaman, S. V., Prudencio, M., Karch, C. M. M., Holloway, S. P., Borchelt, D., & Hart, P. J. (2009) · Experimental Biology and Medicine · doi:10.3181/0903-mr-104 · Cited by 95

Proteasomal dysfunction induced by 4‐hydroxy‐2,3‐trans‐nonenal, an end‐product of lipid peroxidation: a mechanism contributing to neurodegeneration?

Hyun, D., Lee, M., Halliwell, B. B., & Jenner, P. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01125.x · Cited by 93

Superoxide dismutase, oxidative stress, and cell metabolism

Culotta, V. (2001) · Current topics in cellular regulation · doi:10.1016/s0070-2137(01)80005-4 · Cited by 91

A Caspase-3-cleaved Fragment of the Glial Glutamate Transporter EAAT2 Is Sumoylated and Targeted to Promyelocytic Leukemia Nuclear Bodies in Mutant SOD1-linked Amyotrophic Lateral Sclerosis

Gibb, S. L., Boston-Howes, W., Lavina, Z. S., Gustincich, S., Brown, R. H., Pasinelli, P., & Trotti, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704314200 · Cited by 91

Endoplasmic Reticulum Protein Quality Control in Neurodegenerative Disease: The Good, the Bad and the Therapy

Scheper, W., & Hoozemans, J. J. M. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787458506 · Cited by 92

Failure of protein quality control in amyotrophic lateral sclerosis

Kabashi, E., & Durham, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.006 · Cited by 90

Memantine prolongs survival in an amyotrophic lateral sclerosis mouse model

Wang, R., & Zhang, D. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04431.x · Cited by 91

The BH4 domain of Bcl-XL rescues astrocyte degeneration in amyotrophic lateral sclerosis by modulating intracellular calcium signals

Martorana, F., Brambilla, L., Valori, C. F., Bergamaschi, C., Roncoroni, C., Aronica, E., Volterra, A., Bezzi, P., & Rossi, D. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr513 · Cited by 94

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