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 801–900 of 1,000
Rattray, M., & Bendotti, C. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.05.001 · Cited by 26
Ré, D. B., Nafia, I., Melon, C., Shimamoto, K., Goff, L. K., & Had‐Aissouni, L. (2006) · Glia · doi:10.1002/glia.20353 · Cited by 26
Lin, H., Zhai, J., Cañete-Soler, R., & Schlaepfer, W. W. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5689-03.2004 · Cited by 26
Multiple phases of expression and regulation of mouse Hoxc8 during early embryogenesis
Belting, H., Shashikant, C. S., & Ruddle, F. H. (1998) · Journal of Experimental Zoology · doi:10.1002/(sici)1097-010x(199809/10)282:1/2 · Cited by 46
Wei, Y., Zhong, S., Yang, H., Wang, X., Lv, B., Bian, Y., Pei, Y., Xu, C., Zhao, Q., Yulan, W., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116496 · Cited by 28
Barrett, E. F., Barrett, J. N., & David, G. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9392-1 · Cited by 25
Review: Microglia in motor neuron disease
Ashford, B., Boche, D., Cooper‐Knock, J., Heath, P. R., Simpson, J. E., & Highley, J. R. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12640 · Cited by 27
Guo, Y., Duan, W., Li, Z., Huang, J., Yin, Y., Zhang, K., Wang, Q., Zhang, Z., & Li, C. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.03.025 · Cited by 25
Hoffner, G., André, W., Sandt, C., & Djian, P. (2014) · Reviews in Analytical Chemistry · doi:10.1515/revac-2014-0016 · Cited by 25
Mitochondrial ROS and Apoptosis
El-Osta, H. E., & Circu, M. L. (2016) · Springer eBooks · doi:10.1007/978-3-319-42139-1_1 · Cited by 27
Stress-Dependent Changes in the CacyBP/SIP Interacting Protein S100A6 in the Mouse Brain
Bartkowska, K., Swiatek, I., Aniszewska, A., Jurewicz, E., Turlejski, K., Filipek, A., & Djavadian, R. L. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169760 · Cited by 24
Yin, X. L., Wang, S., Qi, Y., Wang, X., Jiang, H., Wang, T., Yang, Y., Wang, Y., Zhang, C., & Feng, H. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.05.004 · Cited by 25
Jain, M. R., Ge, W., Elkabes, S., & Hong Li, A. (2008) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200780023 · Cited by 25
Mechanism and treatment of motoneuron degeneration in ALS: What have SOD1 mutants told us?
Xu, Z. (2000) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/14660820050515052 · Cited by 25
Sublethal enteroviral infection exacerbates disease progression in an ALS mouse model
Xue, Y. C., Liu, H., Mohamud, Y., Bahreyni, A., Zhang, J., Cashman, N. R., & Luo, H. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02380-7 · Cited by 24
Getter, T., Zaks, I., Barhum, Y., Ben‐Zur, T., Böselt, S., Gregoire, S., Viskind, O., Shani, T., Gottlieb, H. E., Green, O., et al. (2015) · ChemMedChem · doi:10.1002/cmdc.201500045 · Cited by 24
Motor neurones in culture as a model to study ALS
Silani, V., Braga, M., Ciammola, A., Cardin, V., & Scarlato, G. (2000) · Journal of Neurology · doi:10.1007/s004150050554 · Cited by 24
Stem Cells in Amyotrophic Lateral Sclerosis: Motor Neuron Protection or Replacement?
Silani, V., Calzarossa, C., Cova, L., & Ticozzi, N. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791292666 · Cited by 24
Amendola, J., Guéritaud, J. P., d’Incamps, B. L., Bories, C., Liabeuf, S., Allène, C., Pambo-Pambo, A. B., & Durand, J. (2007) · PubMed · Cited by 24
Overexpression of mutated Cu,Zn-SOD in neuroblastoma cells results in cytoskeletal change
Takamiya, R., Takahashi, M., Park, Y. S., Tawara, Y., Fujiwara, N., Miyamoto, Y., Gu, J., Suzuki, K., & Taniguchi, N. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00014.2004 · Cited by 24
Bruijn, L. I., & Cudkowicz, M. (2006) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.6.3.417 · Cited by 24
Self-citationFamilial amyotrophic lateral sclerosis with widespread vacuolation and hyaline inclusions
Sasaki, S., Ohsawa, Y., Yamane, K., Sakuma, H., Shibata, N., Nakano, R., Kikugawa, K., Mizutani, T., Tsuji, S., & Iwata, M. (1998) · Neurology · doi:10.1212/wnl.51.3.871 · Cited by 24
Aggregation modulating elements in mutant human superoxide dismutase 1
Karch, C. M. M., & Borchelt, D. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.07.027 · Cited by 23
Self-citationWoo, T., Yoon, M.-H., Kang, S., Park, S., Cho, J.-H., Hwang, Y. J., Ahn, J., Jang, H., Shin, Y.-J., Jung, E., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02862-z · Cited by 24
Ruffo, P., Perrone, B., & Conforti, F. L. (2022) · Genes · doi:10.3390/genes13030537 · Cited by 26
Watanabe, S., Horiuchi, M., Murata, Y., Komine, O., Kawade, N., Sobue, A., & Yamanaka, K. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106031 · Cited by 23
Abnormalities of protein kinases in neurodegenerative diseases
Wagey, R. T. E., & Krieger, C. (1998) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8845-5_4 · Cited by 23
Kiernan, M. C. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.039 · Cited by 23
Human glial progenitor engraftment and gene expression is independent of the ALS environment
Haidet-Phillips, A. M., Doreswamy, A., Gross, S. K., Tang, X., Campanelli, J. T., & Maragakis, N. J. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.12.011 · Cited by 24
Assessing the role of immuno-proteasomes in a mouse model of familial ALS
Puttaparthi, K., Kaer, L. V., & Elliott, J. L. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.03.024 · Cited by 23
Zwiegers, P., Lee, G., & Shaw, C. A. (2014) · Journal of Negative Results in BioMedicine · doi:10.1186/1477-5751-13-14 · Cited by 23
Toward precision medicine in amyotrophic lateral sclerosis.
Zou, Z., Liu, C.-Y., Che, C., & Huang, H. (2016) · PubMed · doi:10.3978/j.issn.2305-5839.2016.01.16 · Cited by 24
Watanabe, S., Komine, O., Endo, F., Wakasugi, K., & Yamanaka, K. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14285 · Cited by 23
Therapeutic developments in the treatment of amyotrophic lateral sclerosis
Jackson, M. T., Lladó, J., & Rothstein, J. D. (2002) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.11.10.1343 · Cited by 23
Self-citationMechanisms of compensatory plasticity for respiratory motor neuron death
Seven, Y. B., & Mitchell, G. S. (2019) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2019.01.001 · Cited by 22
Ting, H.-C., Yang, H.-I., Harn, H., Chiu, I., Su, H., Li, X., Chen, M., Ho, T., Liu, C.-A., Tsai, Y.-J., et al. (2021) · Cells · doi:10.3390/cells10102773 · Cited by 22
Genetic architecture of motor neuron diseases
Chaudhary, R., Agarwal, V., Rehman, M., Kaushik, A. S., & Mishra, V. (2021) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2021.120099 · Cited by 24
Pharmacological and Pathological Relevance of S100 Proteins in Neurological Disorders
Goswami, D., Anuradha, U., Angati, A., Kumari, N., & Singh, R. K. (2022) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527322666221128160653 · Cited by 22
McLean, J. R., Liu, H., Miletic, D., Weng, Y. C., Rogaeva, E. A., Zinman, L. H., Križ, J., & Robertson, J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06846.x · Cited by 22
Immunology primer for neurosurgeons and neurologists part 2: Innate brain immunity
Blaylock, R. L. (2013) · Surgical Neurology International · doi:10.4103/2152-7806.118349 · Cited by 23
Caioli, S., Curcio, L., Pieri, M., Antonini, A., Marolda, R., Severini, C., & Zona, C. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.06.008 · Cited by 24
UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review
Papaevgeniou, N., & Chondrogianni, N. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_1 · Cited by 23
Dučić, T., Stamenković, S., Lai, B. C. H., Anđjus, P. R., & Lučić, V. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04273 · Cited by 22
Ubiquitin–Synaptobrevin Fusion Protein Causes Degeneration of Presynaptic Motor Terminals in Mice
Liu, Y., Li, H., Sugiura, Y., Han, W., Gallardo, G., Khvotchev, M. V., Zhang, Y., Kavalali, E. T., Südhof, T. C., & Lin, W. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5288-14.2015 · Cited by 22
Differential effects of phytotherapic preparations in the hSOD1 Drosophila melanogaster model of ALS
Rose, F. D., Marotta, R., Talani, G., Catelani, T., Solari, P., Poddighe, S., Borghero, G., Marrosu, F., Sanna, E., Kasture, S. B., et al. (2017) · Scientific Reports · doi:10.1038/srep41059 · Cited by 22
Heilman, P. L., Song, S., Miranda, C. J., Meyer, K., Srivastava, A. K., Knapp, A., Wier, C. G., Kaspar, B. K., & Kolb, S. J. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.08.002 · Cited by 22
Andreassen, O. A., Ferrante, R. J., Klivènyi, P., Klein, A., Dedeoglu, A., Albers, D. S., Kowall, N. W., & Beal, M. F. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7627 · Cited by 22
Progress in the modeling of neurodegenerative diseases in transgenic mice
Duff, K., & Rao, M. V. (2001) · Current Opinion in Neurology · doi:10.1097/00019052-200108000-00003 · Cited by 22
Sato, T., Yamamoto, Y., Nakanishi, T., Fukada, K., Sugai, F., Zhou, Z., Okuno, T., Nagano, S., Hirata, S., Shimizu, A., et al. (2003) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2003.11.003 · Cited by 22
Park, K. H. J., & Vincent, I. J. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.04.001 · Cited by 22
Liebl, M. P., Windschmitt, J., Besemer, A. S., Schäfer, A.-K., Reber, H., Behl, C., & Clement, A. M. (2015) · Scientific Reports · doi:10.1038/srep08585 · Cited by 25
Rodríguez, M. J., & Mahy, N. (2016) · Current Medicinal Chemistry · doi:10.2174/0929867324666161123091314 · Cited by 22
Neuronal VPS35 deletion induces spinal cord motor neuron degeneration and early post-natal lethality
Sargent, D., Cunningham, L. A., Dues, D. J., Ma, Y., Kordich, J. J., Mercado, G., Brundin, P., Cowell, R. M., & Moore, D. J. (2021) · Brain Communications · doi:10.1093/braincomms/fcab208 · Cited by 21
Emerging Roles for Aberrant Astrocytic Calcium Signals in Parkinson’s Disease
Bancroft, E. A., & Srinivasan, R. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2021.812212 · Cited by 22
Widespread CNS pathology in amyotrophic lateral sclerosis homozygous for the D90A SOD1 mutation
Forsberg, K., Graffmo, K. S., Stenvall, E., Tabikh, N., Marklund, S. L., Brännström, T., & Andersen, P. M. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02519-z · Cited by 22
Why should we care about astrocytes in a motor neuron disease?
Dittlau, K. S., & Bosch, L. V. D. (2023) · Frontiers in Molecular Medicine · doi:10.3389/fmmed.2023.1047540 · Cited by 24
Endocytic pathways of pathogenic protein aggregates in neurodegenerative diseases
Hivare, P., Mujmer, K., Swarup, G., Gupta, S. K., & Bhatia, D. D. (2023) · Traffic · doi:10.1111/tra.12906 · Cited by 24
Role of Astrocytes in Neurodegenerative Diseases
George, E., González, J., Capani, F., & Morales, L. (2011) · InTech eBooks · doi:10.5772/31166 · Cited by 21
A simultaneous release of SOD1 with cytochrome c regulates mitochondria-dependent apoptosis
Li, Q., Sato, E. F., Zhu, X., & Inoue, M. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9952-9 · Cited by 21
Karch, C. M. M., & Borchelt, D. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06572.x · Cited by 21
Self-citationhling, T. M. ⁄., Duda, J., Weishaupt, J. H., Ludolph, A. C., & Liss, B. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00353 · Cited by 21
Kobatake, Y., Sakai, H., Tsukui, T., Yamato, O., Kohyama, M., Sasaki, J., Kato, S., Urushitani, M., Maeda, S., & Kamishina, H. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.10.034 · Cited by 21
Enge, T. G., Ecroyd, H. W., Jolley, D. F., Yerbury, J. J., & Dosseto, A. (2016) · Metallomics · doi:10.1039/c6mt00270f · Cited by 22
Park, J.-H., Jang, H. R., Lee, I. Y., Oh, H. K., Choi, E., Rhim, H., & Kang, S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx250 · Cited by 21
EAAT1 and EAAT2 immunoreactivity in transgenic mice with a G93A mutant SOD1 gene
Sasaki, S., Warita, H., Abe, K., Komori, T., & Iwata, M. (2001) · Neuroreport · doi:10.1097/00001756-200105250-00014 · Cited by 21
Impaired SDF1/CXCR4 signaling in glial progenitors derived from SOD1G93A mice
Luo, Y., Xue, H., Pardo, A. C., Mattson, M. P., Rao, M. S., & Maragakis, N. J. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21398 · Cited by 21
HoxB2 binds mutant SOD1 and is altered in transgenic model of ALS
Zhai, J., Lin, H., Cañete-Soler, R., & Schlaepfer, W. W. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi297 · Cited by 21
Abnormal response of distal Schwann cells to denervation in a mouse model of motor neuron disease
Carrasco, D. I., Bahr, B. A., Seburn, K. L., & Pinter, M. J. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.02.002 · Cited by 21
WILSON, J., & SHAW, C. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.09.017 · Cited by 21
Prospects for the Pharmacotherapy of Amyotrophic Lateral Sclerosis
Festoff, B. W., Suo, Z., & Citron, B. A. (2003) · CNS Drugs · doi:10.2165/00023210-200317100-00002 · Cited by 21
Differential RNA cleavage and polyadenylation of the glutamate transporter EAAT2 in the human brain
Münch, C., Schwalenstöcker, B., Hermann, C., Cirovic, S., Stamm, S., Ludolph, A. C., & Meyer, T. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00139-x · Cited by 21
Extra Axonal Neurofilaments Do Not Exacerbate Disease Caused by Mutant Cu,Zn Superoxide Dismutase
Couillard‐Després, S., Meier, J., & Julien, J. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0296 · Cited by 21
Ou, K., Jia, Q., Li, D., Li, S., Li, X., & Yin, P. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00466-9 · Cited by 23
Knockdown of GADD34 in neonatal mutant SOD1 mice ameliorates ALS
Ghadge, G. D., Sonobe, Y., Camarena, A., Drigotas, C., Rigo, F., Ling, K., & Roos, R. P. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104702 · Cited by 22
Proteostasis impairment and ALS
Lambert-Smith, I. A., Saunders, D. N., & Yerbury, J. J. (2022) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2022.06.001 · Cited by 19
Pan, L., Yoshii, Y., Otomo, A., Ogawa, H. K., Iwasaki, Y., Shang, H., & Hadano, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033409 · Cited by 20
Baptista, M. S., Duarte, C. B., & Maciel, P. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0946-0 · Cited by 19
In Vivo NMR Studies of the Brain with Hereditary or Acquired Metabolic Disorders
Sherry, E. B., Lee, P., & Choi, I.-Y. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1772-1 · Cited by 22
Stressing Out Hsp90 in Neurotoxic Proteinopathies
Inda, C., Bolaender, A., Wang, T., Gandu, S. R., & Koren, J. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160413141350 · Cited by 20
Srinivasan, E., & Rajasekaran, R. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25288 · Cited by 20
Astrocytes in Motor Neuron Diseases
Valori, C. F., Guidotti, G., Brambilla, L., & Rossi, D. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9913-8_10 · Cited by 19
Stamenković, S., Dučić, T., Stamenković, V., Kranz, A., & Anđjus, P. R. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.05.041 · Cited by 19
Creatine and coenzyme Q10 in the treatment of ALS
Strong, M. J., & Pattee, G. L. (2000) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/14660820050515665 · Cited by 20
The role of excitatory amino acid transporter 2 (EAAT2) in epilepsy and other neurological disorders
Alijanpour, S., Miryounesi, M., & Ghafouri‐Fard, S. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-022-01091-5 · Cited by 20
Neurogenetics II: complex disorders
Wright, A. F. (2005) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2004.047704 · Cited by 19
Ma, D., Shuler, J. M., Kumar, A. P. R., Stanford, Q. R., Tungtur, S. K., Nishimune, H., & Stanford, J. A. (2016) · Neurorehabilitation and neural repair · doi:10.1177/1545968316666956 · Cited by 18
Choi, S.-H., Yousefian-Jazi, A., Hyeon, S. J., Nguyen, P. T., Chu, J., Kim, S., Kim, S., Ryu, H. L., Kowall, N. W., Ryu, H., et al. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-022-00890-3 · Cited by 18
Deng, C., & Chen, H. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106377 · Cited by 18
Progress in Therapy Development for Amyotrophic Lateral Sclerosis
Venkova-Hristova, K., Christov, A., Kamaluddin, Z., Kobalka, P. J., & Hensley, K. (2012) · Neurology Research International · doi:10.1155/2012/187234 · Cited by 18
Nguyen, K. T. V., Barrett, J. N., Garcia-Chacon, L. E., David, G., & Barrett, E. F. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.031 · Cited by 19
Chhangani, D., Endo, F., Amanullah, A., Upadhyay, A., Watanabe, S., Mishra, R., Yamanaka, K., & Mishra, A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.11.017 · Cited by 18
Shijo, T., Warita, H., Suzuki, N., Ikeda, K., Mitsuzawa, S., Akiyama, T., Ono, H., Nishiyama, A., Izumi, R., Kitajima, Y., et al. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.06.009 · Cited by 18
Nefussy, B., & Drory, V. E. (2010) · The EPMA Journal · doi:10.1007/s13167-010-0027-0 · Cited by 18
Islam, R., Kumimoto, E. L., Bao, H., & Zhang, B. (2012) · F1000Research · doi:10.12688/f1000research.1-47.v1 · Cited by 18
Ge, W., Leystra‐Lantz, C., Sanelli, T. R., McLean, J. R., Wen, W., Strong, W., & Strong, M. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.03.007 · Cited by 18
Xu, G. M., Ayers, J. I., Roberts, B. L., Brown, H. H., Fromholt, S., Green, C., & Borchelt, D. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu517 · Cited by 18
Self-citationFunctional and Morphological Assessment of Diaphragm Innervation by Phrenic Motor Neurons
Martin, M., Li, K., Wright, M. C., & Lepore, A. C. (2015) · Journal of Visualized Experiments · doi:10.3791/52605 · Cited by 18
Bennett, E., Mead, R. J., Azzouz, M., Shaw, P. J., & Grierson, A. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107918 · Cited by 18
Sasaki, S., Warita, H., Abe, K., & Iwata, M. (2004) · Acta Neuropathologica · doi:10.1007/s00401-004-0838-y · Cited by 18
Matyja, E., Taraszewska, A., Nagańska, E., Rafałowska, J., & Gębarowska, J. (2006) · PubMed · Cited by 18
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