The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
ALS-Linked SOD1 Mutant G85R Mediates Damage to Astrocytes and Promotes Rapidly Progressive Disease with SOD1-Containing Inclusions
Open accessAbstract
High levels of familial Amyotrophic Lateral Sclerosis (ALS)-linked SOD1 mutants G93A and G37R were previously shown to mediate disease in mice through an acquired toxic property. We report here that even low levels of another mutant, G85R, cause motor neuron disease characterized by an extremely rapid clinical progression, without changes in SOD1 activity. Initial indicators of disease are astrocytic inclusions that stain intensely with SOD1 antibodies and ubiquitin and SOD1-containing aggregates in motor neurons, features common with some cases of SOD1 mutant-mediated ALS. Astrocytic inclusions escalate markedly as disease progresses, concomitant with a decrease in the glial glutamate transporter (GLT-1). Thus, the G85R SOD1 mutant mediates direct damage to astrocytes, which may promote the nearly synchronous degeneration of motor neurons.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“implying that astrocytes are both necessary and sufficient for neurodegeneration in this ALS model.”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [414]
In the citing paper
“Selective clearance of SOD1-positive inclusions from astrocytes is sufficient to slow disease progression [414]”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [414]
In the citing paper
“In transgenic mice overexpressing mutant SOD1 associated with ALS, astrocytes display more SOD1-positive inclusions than do neurons, and at an earlier stage [414].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [414]
Citations
Cites
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
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
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
Self-citationCellular 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
Self-citationAmyotrophic 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
Self-citation
Cited by
Sorted by citations
Items 501–600 of 1,000
Exciting Complexity: The Role of Motor Circuit Elements in ALS Pathophysiology
Gunes, Z. I., Kan, V. W. Y., Ye, X., & Liebscher, S. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00573 · Cited by 74
Wood-Allum, C. A. (2006) · Brain · doi:10.1093/brain/awl118 · Cited by 67
Do oxidatively modified proteins cause ALS?
Valentine, J. S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01080-8 · Cited by 68
Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states
Prudencio, M., & Borchelt, D. R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-77 · Cited by 63
Self-citationSharp, P. S., Dick, J. R. T., & Greensmith, L. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.09.069 · Cited by 67
Lithium prevents excitotoxic cell death of motoneurons in organotypic slice cultures of spinal cord
Calderó, J., Brunet, N., Tarabal, O., Piedrafita, L., Hereu, M., Ayala, V., & Esquerda, J. E. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.11.034 · Cited by 67
An update on human astrocytes and their role in development and disease
de Majo, M., Koontz, M., Rowitch, D. H., & Ullian, E. M. (2020) · Glia · doi:10.1002/glia.23771 · Cited by 69
Wengenack, T. M., Holasek, S. S., Montaño, C., Gregor, D. M., Curran, G. L., & Poduslo, J. F. (2004) · Brain Research · doi:10.1016/j.brainres.2004.08.054 · Cited by 67
Heterogeneous astrocytes: Active players in CNS
Hu, X., Yuan, Y., Wang, D., & Su, Z. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.03.017 · Cited by 73
Non-neuronal induction of immunoproteasome subunits in an ALS model: Possible mediation by cytokines
Puttaparthi, K., & Elliott, J. L. (2005) · Experimental Neurology · doi:10.1016/j.expneurol.2005.08.027 · Cited by 66
Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R
Seetharaman, S. V., Winkler, D. D., Taylor, A. B., Cao, X., Whitson, L. J., Doucette, P. A., Valentine, J. S., Schirf, V. R., Demeler, B., Carroll, M. C., et al. (2010) · Biochemistry · doi:10.1021/bi100314n · Cited by 66
Kim, Y., Nakatomi, R., Akagi, T., Hashikawa, T., & Takahashi, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502230200 · Cited by 68
Nguyen, M. D., Larivière, R., & Julien, J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.12306 · Cited by 66
Nguyen, K. T. V., Garcia-Chacon, L. E., Barrett, J. N., Barrett, E. F., & David, G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810934106 · Cited by 65
Duplan, L., Bernard‐Marissal, N., Casseron, W., Dudley, K., Thouvenot, É., Honnorat, J., Rogemond, V., de Bovis, B., Aebischer, P., Marin, P., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5411-09.2010 · Cited by 65
Caenorhabditis elegans as a model system for studying aging-associated neurodegenerative diseases
Pelt, K. M. V., & Truttmann, M. C. (2020) · Translational Medicine of Aging · doi:10.1016/j.tma.2020.05.001 · Cited by 62
Meehan, C. F., Moldovan, M., Marklund, S. L., Graffmo, K. S., Nielsen, J. B., & Hultborn, H. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02188.x · Cited by 64
Mitochondrial Involvement in Amyotrophic Lateral Sclerosis: Trigger or Target?
Bacman, S. R., Bradley, W. G., & Moraes, C. T. (2006) · Molecular Neurobiology · doi:10.1385/mn:33:2:113 · Cited by 66
Genetic Rodent Models of Amyotrophic Lateral Sclerosis
Bosch, L. V. D. (2011) · BioMed Research International · doi:10.1155/2011/348765 · Cited by 70
Mitochondrial Degeneration in Amyotrophic Lateral Sclerosis
Xu, Z., Jung, C., Higgins, C. M. J., Levine, J. B., & Kong, J. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041774.12654.e1 · Cited by 64
Holasek, S. S., Wengenack, T. M., Kandimalla, K. K., Montaño, C., Gregor, D. M., Curran, G. L., & Poduslo, J. F. (2005) · Brain Research · doi:10.1016/j.brainres.2005.03.037 · Cited by 67
Stieber, A., Chen, Y. J., Wei, S., Mourelatos, Z., Gonatas, J. O., Okamoto, K., & Gonatas, N. K. (1998) · Acta Neuropathologica · doi:10.1007/s004010050794 · Cited by 64
Gene‐based treatment of motor neuron diseases
Federici, T., & Boulis, N. M. (2005) · Muscle & Nerve · doi:10.1002/mus.20439 · Cited by 64
Farah, C. A., Nguyen, M. D., Julien, J., & Leclerc, N. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01505.x · Cited by 64
Autophagy in neuroinflammatory diseases
Muller, S., Brun, S., René, F., Seze, J. D., Loeffler, J., & Jeltsch‐David, H. (2017) · Autoimmunity Reviews · doi:10.1016/j.autrev.2017.05.015 · Cited by 66
Steinruecke, M., Lonergan, R. M., Selvaraj, B. T., Chandran, S., Castro, B. D., & Stavrou, M. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231153281 · Cited by 63
Miro1 deficiency in amyotrophic lateral sclerosis
Zhang, F., Wang, W., Siedlak, S. L., Liu, Y., Liu, J., Jiang, K., Perry, G. L., Zhu, X., & Wang, X. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00100 · Cited by 64
FUS-related proteinopathies: Lessons from animal models
Lanson, N. A., & Pandey, U. B. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.039 · Cited by 66
Defective axonal transport of neurofilament proteins in neurons overexpressing peripherin
Millecamps, S., Robertson, J., Larivière, R., Mallet, J. J., & Julien, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03932.x · Cited by 62
Nardo, G., Trolese, M. C., Verderio, M., Mariani, A., Paola, M. D., Riva, N., Dina, G., Panini, N., Erba, E., Quattrini, A., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0271-7 · Cited by 62
Defective Neurofilament Transport in Mouse Models of Amyotrophic Lateral Sclerosis: A Review
Rao, M. V., & Nixon, R. A. (2003) · Neurochemical Research · doi:10.1023/a:1023259207015 · Cited by 62
Martin, L. J. (2007) · Reviews in the Neurosciences · doi:10.1515/revneuro.2007.18.2.115 · Cited by 61
EAAT2 and the Molecular Signature of Amyotrophic Lateral Sclerosis
Rosenblum, L. T., & Trotti, D. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-55769-4_6 · Cited by 66
Komine, O., Yamashita, H., Fujimori-Tonou, N., Koike, M., Jin, S., Moriwaki, Y., Endo, F., Watanabe, S., Uematsu, S., Akira, S., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0098-3 · Cited by 66
Early abnormalities in transgenic mouse models of amyotrophic lateral sclerosis
Durand, J., Amendola, J., Bories, C., & d’Incamps, B. L. (2006) · Journal of Physiology-Paris · doi:10.1016/j.jphysparis.2005.12.014 · Cited by 67
Fukada, K., Nagano, S., Satoh, M., Tohyama, C., Nakanishi, T., Shimizu, A., Yanagihara, T., & Sakoda, S. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01828.x · Cited by 61
From nucleation to widespread propagation: A prion-like concept for ALS
Maniecka, Z., & Polymenidou, M. (2015) · Virus Research · doi:10.1016/j.virusres.2014.12.032 · Cited by 65
ALS pathogenesis: Recent insights from genetics and mouse models
Swarup, V., & Julien, J. (2010) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2010.08.006 · Cited by 65
Sathornsumetee, S., McGavern, D. B., Ure, D., & Rodriguez, M. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64650-0 · Cited by 59
Zhang, H., Andrekopoulos, C., Joseph, J., Crow, J., & Kalyanaraman, B. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.038 · Cited by 59
Hoyaux, D., Boom, A., Bosch, L. V. D., Belot, N., Martin, J., Heizmann, C. W., Robert Kiss, A., & Pochet, R. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.8.736 · Cited by 59
Protein Quality Control and the Amyotrophic Lateral Sclerosis/Frontotemporal Dementia Continuum
Shahheydari, H., Ragagnin, A., Walker, A. K., Toth, R. P., Vidal, M., Jagaraj, C. J., Perri, E. R., Konopka, A., Sultana, J. M., & Atkin, J. D. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00119 · Cited by 61
Maxwell, M. M., Pasinelli, P., Kazantsev, A. G., & Brown, R. H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308726100 · Cited by 59
Ström, A., Shi, P., Zhang, F., Gál, J., Kilty, R., Hayward, L. J., & Zhu, H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800276200 · Cited by 58
Sealing one's fate: control of cell death in neurons
Bergeron, L., & Yuan, J. (1998) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(98)80008-1 · Cited by 57
Alexander, G. M., Deitch, J. S., Seeburger, J. L., Valle, L. D., & Heiman-Patterson, T. D. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741666.x · Cited by 58
Calcium Ions Promote Superoxide Dismutase 1 (SOD1) Aggregation into Non-fibrillar Amyloid
Leal, S. S., Cardoso, I., Valentine, J. S., & Gomes, C. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470740 · Cited by 60
Vaz, A. R., Cunha, C., Gomes, C., Schmucki, N., Barbosa, M., & Brites, D. M. T. O. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8731-8 · Cited by 57
Vitamin D as a Potential Therapy in Amyotrophic Lateral Sclerosis
Gianforcaro, A., & Hamadeh, M. J. (2014) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12204 · Cited by 61
Chen, J., Bassot, A., Giuliani, F., & Simmen, T. (2021) · Cells · doi:10.3390/cells10071789 · Cited by 58
Genetic Mapping of a Mouse Modifier Gene That Can Prevent ALS Onset
Kunst, C. B., Messer, L. H., Gordon, J. W., Haines, J. L., & Patterson, D. (2000) · Genomics · doi:10.1006/geno.2000.6379 · Cited by 57
Wilson, J. M. B., Khabazian, I., Pow, D. V., Craig, U. K., & Shaw, C. A. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:3:2:105 · Cited by 57
IN VITRO AND IN VIVO MODELS OF AMYOTROPHIC LATERAL SCLEROSIS: AN UPDATED OVERVIEW
de Gois, A. M., de Mendonça, D. M. F., Freire, M. A. M., & dos Santos, J. R. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.03.012 · Cited by 63
Excessive and precocious glutamate release in a mouse model of amyotrophic lateral sclerosis
Raiteri, L., Stigliani, S., Zappettini, S., Mercuri, N. B., Raiteri, M., & Bonanno, G. (2004) · Neuropharmacology · doi:10.1016/j.neuropharm.2003.11.025 · Cited by 56
Trías, E., Díaz‐Amarilla, P., Olivera‐Bravo, S., Isasi, E., Drechsel, D. A., Lopez, N. I., Bradford, C. S., Ireton, K. E., Beckman, J. S., & Barbeito, L. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00274 · Cited by 62
Sagot, Y., Toni, N., Perrelet, D., Lurot, S., King, B., Rixner, H., Mattenberger, L., Waldmeier, P. C., & Kato, A. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703633 · Cited by 56
Benedusi, V., Martorana, F., Brambilla, L., Maggi, A. C., & Rossi, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366419 · Cited by 58
The Neuroprotective Role of Creatine
Klein, A., & Ferrante, R. J. (2007) · Springer eBooks · doi:10.1007/978-1-4020-6486-9_11 · Cited by 56
Induction of motor neuron apoptosis by free 3‐nitro‐ l ‐tyrosine
Peluffo, H., Shacka, J. J., Ricart, K. C., Bisig, C. G., Palma, L. M., Pritsch, O., Kamaid, A., Eiserich, J. P., Crow, J. P., Barbeito, L., et al. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2004.02363.x · Cited by 56
Copray, J. C. V. M., Jaarsma, D., Kst, B. M., Bruggeman, R., Mantingh-Otter, I., Brouwer, N., & Boddeke, H. W. G. M. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00755-8 · Cited by 56
Zona, C., Pieri, M., & Carunchio, I. (2006) · Journal of Neurophysiology · doi:10.1152/jn.00566.2006 · Cited by 56
Kim, S. H., Henkel-Tigges, J., Beers, D. R., Şengün, İ. Ş., Simpson, E. P., Goodman, J. C., Engelhardt, J. I., Siklós, L., & Appel, S. H. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.1.88 · Cited by 56
Shibata, N., Nagai, R., Miyata, S., Jono, T., Horiuchi, S., Hirano, A., Kato, S., Sasaki, S., Asayama, K., & Kobayashi, M. (2000) · Acta Neuropathologica · doi:10.1007/s004019900173 · Cited by 56
Vanoni, C., Massari, S., Losa, M., Carrega, P., Perego, C., Conforti, L., & Pietrini, G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01411 · Cited by 56
Wang, J., Caruano-Yzermans, A. L., Rodriguez, A., Scheurmann, J. P., Slunt, H. H., Cao, X., Gitlin, J. D., Hart, P. J., & Borchelt, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604503200 · Cited by 55
Self-citationAstrocyte signaling and neurodegeneration
Brambilla, L., Martorana, F., & Rossi, D. (2013) · Prion · doi:10.4161/pri.22512 · Cited by 58
Gomes, C., Escrevente, C., & Costa, J. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.03.065 · Cited by 55
Altered sensorimotor development in a transgenic mouse model of amyotrophic lateral sclerosis
Amendola, J., Verrier, B., Roubertoux, P. L., & Durand, J. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03745.x · Cited by 55
Yagami, T., Yamamoto, Y., & Koma, H. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1277-4 · Cited by 56
Yamashita, H., Kawamata, J., Okawa, K., Kanki, R., Nakamizo, T., Hatayama, T., Yamanaka, K., Takahashi, R., & Shimohama, S. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04534.x · Cited by 54
Glia-specific autophagy dysfunction in ALS
Strohm, L., & Behrends, C. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.024 · Cited by 57
Pan, Y., & Nicolazzo, J. A. (2022) · British Journal of Pharmacology · doi:10.1111/bph.15802 · Cited by 49
Neuroinflammation and brain infections: Historical context and current perspectives
Bentivoglio, M., Mariotti, R., & Bertini, G. (2010) · Brain Research Reviews · doi:10.1016/j.brainresrev.2010.09.008 · Cited by 53
Misawa, H., Nakata, K., Matsuura, J., Moriwaki, Y., Kawashima, K., Shimizu, T., Shirasawa, T., & Takahashi, R. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.02.014 · Cited by 53
Qiu, L., Qiao, T., Beers, M. A., Tan, W., Wang, H., Yang, B., & Xu, Z. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-1 · Cited by 53
Stathmin 1/2-triggered microtubule loss mediates Golgi fragmentation in mutant SOD1 motor neurons
Bellouze, S., Baillat, G., Buttigieg, D., de la Grange, P., Rabouille, C., & Haase, G. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0111-6 · Cited by 54
The Value of Transgenic Models for the Study of Neurodegenerative Diseases
Price, D. L., Wong, P. C., Markowska, A. L., Lee, M. K., THINAKAREN, G., Cleveland, D. W., Sisodia, S. S., & Borchelt, D. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06920.x · Cited by 52
Self-citationMotor neuron–immune interactions: the vicious circle of ALS
Barbeito, A. G., Mesci, P., & Boillée, S. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0429-0 · Cited by 57
Watanabe, S., Nagano, S., Duce, J. A., Kiaei, M., Li, Q.-X., Tucker, S. M., Tiwari, A., Brown, R. H., Beal, M. F., Hayward, L. J., et al. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.02.004 · Cited by 52
Physical Activity and Neuroprotection in Amyotrophic Lateral Sclerosis
McCrate, M., & Kaspar, B. K. (2008) · NeuroMolecular Medicine · doi:10.1007/s12017-008-8030-5 · Cited by 52
A patient-derived stem cell model of hereditary spastic paraplegia with SPAST mutations
Abrahamsen, G., Fan, Y., Matigian, N., Wali, G., Bellette, B., Sutharsan, R., Raju, J., Wood, S. A., Veivers, D., Sue, C. M., et al. (2012) · Disease Models & Mechanisms · doi:10.1242/dmm.010884 · Cited by 56
Experimental models for the study of neurodegeneration in amyotrophic lateral sclerosis
Tovar‐y‐Romo, L. B., Santa-Cruz, L. D., & Tapia, R. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-31 · Cited by 52
Vonk, W. I. M., Kakkar, V., Bartuzi, P., Jaarsma, D., Berger, R., Hofker, M. H., Klomp, L. W. J., Wijmenga, C., Kampinga, H. H., & van de Sluis, B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092408 · Cited by 52
Shobha, K., Vijayalakshmi, K., Alladi, P. A., Nalini, A., Sathyaprabha, T. N., & Raju, T. R. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2006.12.004 · Cited by 52
Zhang, J., Ito, H., Wate, R., Ohnishi, S., Nakano, S., & Kusaka, H. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0130-4 · Cited by 52
Biochemical and Molecular Pathways in Neurodegenerative Diseases: An Integrated View
Sanghai, N., & Tranmer, G. K. (2023) · Cells · doi:10.3390/cells12182318 · Cited by 60
Advances in stem cell research for Amyotrophic Lateral Sclerosis
Papadeas, S. T., & Maragakis, N. J. (2009) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2009.09.003 · Cited by 51
Emerging drugs for amyotrophic lateral sclerosis
Habib, A. A., & Mitsumoto, H. (2011) · Expert Opinion on Emerging Drugs · doi:10.1517/14728214.2011.604312 · Cited by 52
Antinone, S. E., Ghadge, G. D., Lam, T. T., Wang, L., Roos, R. P., & Green, W. N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.487231 · Cited by 51
Gouix, E., Buisson, A., Nieoullon, A., Goff, L. K.-L., Tauskela, J., Blondeau, N., & Had‐Aissouni, L. (2014) · Pharmacological Research · doi:10.1016/j.phrs.2014.06.002 · Cited by 53
Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane
Ahtoniemi, T., Jaronen, M., Keksa-Goldsteine, V., Goldsteins, G., & Koıstınaho, J. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.08.010 · Cited by 51
Motor neuron disease: Classification and nomenclature
Swash, M. (2000) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/14660820050515403 · Cited by 51
In Vitro Modeling of Nerve–Muscle Connectivity in a Compartmentalized Tissue Culture Device
Machado, C. B., Pluchon, P., Harley, P., Rigby, M., Sabater, V. G., Stevenson, D. C., Hynes, S., Lowe, A., Burrone, J., Viasnoff, V., et al. (2019) · Advanced Biosystems · doi:10.1002/adbi.201800307 · Cited by 55
Tummala, H., Jung, C., Tiwari, A., Higgins, C. M. J., Hayward, L. J., & Xu, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501705200 · Cited by 51
Shibata, N., Hirano, A., Hedley-Whyte, T. E., Canto, M. C. D., Nagai, R., Uchida, K., Horiuchi, S., Kawaguchi, M., Yamamoto, T., & Kobayashi, M. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0537-5 · Cited by 51
Early glial responses in murine models of multiple sclerosis
Ayers, M. M., Hazelwood, L. J., Catmull, D. V., Wang, D., McKormack, Q., Bernard, C. C. A., & Orian, J. M. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2003.08.018 · Cited by 51
Impaired post‐translational folding of familial ALS‐linked Cu, Zn superoxide dismutase mutants
Bruns, C. K., & Kopito, R. R. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601528 · Cited by 51
Regulation of Glutamate, GABA and Dopamine Transporter Uptake, Surface Mobility and Expression
Ryan, R. M., Ingram, S., & Scimemi, A. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.670346 · Cited by 54
You, J., Youssef, M., Santos, J. R., Lee, J., & Park, J. (2023) · Biology · doi:10.3390/biology12101307 · Cited by 60
Xia, G., Benmohamed, R., Kim, J., Arvanites, A. C., Morimoto, R. I., Ferrante, R. J., Kirsch, D. R., & Silverman, R. B. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101549k · Cited by 50
Metadata
- Authors
- Bruijn, L. I., Becher, M. W., Lee, M. K., Anderson, K. L., Jenkins, N. A., Copeland, N. G., Sisodia, S. S., Rothstein, J. D., Borchelt, D. R., Price, D. L., & Cleveland, D. W.
- Affiliations
- University of California San Diego (US)
- Johns Hopkins University (US)
- National Cancer Institute (US)
- Corresponding author
- Cleveland, D.W.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1997-02
- Volume
- 18
- Issue
- 2
- Pages
- 327-338
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2012851706
- Cited by
- 1,341
- References
- 39
- Citations by year
- 2026: 10 · 2025: 22 · 2024: 23 · 2023: 30 · 2022: 41 · 2021: 40 · 2020: 36 · 2019: 35 · 2018: 36 · 2017: 40 · 2016: 47 · 2015: 44 · 2014: 52 · 2013: 52 · 2012: 64
- FWCI
- 37.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuron (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Muscular Dystrophy Association
- National Institute on Aging (P50AG005146, AG 05146)
- National Institute of Neurological Disorders and Stroke (NS10580, NS 27036)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- amyotrophic lateral sclerosis, SOD1 G93A, astrocyte damage, motor neuron degeneration, disease progression, glutamate transporter GLT-1, ubiquitin, familial ALS
- MeSH terms
- Amyotrophic Lateral Sclerosis, Animals, Astrocytes, Axons, Disease Models, Animal, Genes, Dominant, Humans, Mice, Transgenic, Microscopy, Electron, Nerve Degeneration, Neurons, Spinal Cord, Superoxide Dismutase, Ubiquitins, Point Mutation, ATP-Binding Cassette Transporters, Amino Acid Transport System X-AG, Mice
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 ›
Are you an author, or do you see a problem with this page? Request a review