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-citationWong, P. C., Pardo, C. A., Borchelt, D., Lee, M. K., Copeland, N. G., Jenkins, N. A., Sisodia, S. S., Cleveland, D. W., & Price, D. L. (1995) · Neuron · doi:10.1016/0896-6273(95)90259-7 · Cited by 1,439
Self-citationReaume, A. G., Elliott, J. L., Hoffman, E. K., Kowall, N. W., Ferrante, R. J., Siwek, D. F., Wilcox, H. M., Flood, D. G., Beal, M. F., Brown, R. H., et al. (1996) · Nature Genetics · doi:10.1038/ng0596-43 · Cited by 1,285
Cloning and expression of a rat brain L-glutamate transporter
Pines, G., Danbolt, N. C., Bjørås, M., Zhang, Y., Bendahan, A., Eide, L., Koepsell, H., Storm‐Mathisen, J., Seeberg, E. C., & Kanner, B. I. (1992) · Nature · doi:10.1038/360464a0 · Cited by 1,242
Decreased Glutamate Transport by the Brain and Spinal Cord in Amyotrophic Lateral Sclerosis
Rothstein, J. D., Martin, L. J., & Kuncl, R. W. (1992) · New England Journal of Medicine · doi:10.1056/nejm199205283262204 · Cited by 1,197
Self-citationStorck, T., Schulte, S., Hofmann, K., & Stoffel, W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10955 · Cited by 1,193
Beckman, J. S., Carson, M. A., Smith, C. D. L., & Koppenol, W. H. (1993) · Nature · doi:10.1038/364584a0 · Cited by 876
Greenlund, L. J. S., Deckwerth, T. L., & Johnson, E. M. (1995) · Neuron · doi:10.1016/0896-6273(95)90287-2 · Cited by 738
Ripps, M. E., Huntley, G. W., Hof, P. R., Morrison, J., & Gordon, J. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.689 · Cited by 725
Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
Wiedau‐Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., & Bredesen, D. E. (1996) · Science · doi:10.1126/science.271.5248.515 · Cited by 720
Self-citationAbnormal excitatory amino acid metabolism in amyotrophic lateral sclerosis
Rothstein, J. D., Tsai, G. E., Kuncl, R. W., Clawson, L., Cornblath, D. R., Drachman, D. B., Pestronk, A., Stauch, B. L., & Coyle, J. T. (1990) · Annals of Neurology · doi:10.1002/ana.410280106 · Cited by 637
Self-citationBowling, A. C., Schulz, J. B., Brown, R. H., & Beal, M. F. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07478.x · Cited by 629
Borchelt, D., Lee, M. K., Slunt, H. S., Guarnieri, M., Xu, Z. S., Wong, P. C., Brown, R. H., Price, D. L., Sisodia, S. S., & Cleveland, D. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8292 · Cited by 622
Self-citationEpstein, C. J., Avraham, K. B., Lovett, M., Smith, S. H., Elroy‐Stein, O., Rotman, G., Bry, C., & Groner, Y. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.8044 · Cited by 454
Canto, M. C. D., & Gurney, M. E. (1994) · PubMed · Cited by 395
Pardo, C. A., Xu, Z., Borchelt, D., Price, D. L., Sisodia, S. S., & Cleveland, D. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.954 · Cited by 314
Self-citationShibata, N., Hirano, A., Kobayashi, M., Siddique, T., Deng, H., Hung, W.-Y., Kato, T., & Asayama, K. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199604000-00011 · Cited by 294
Chronic inhibition of superoxide dismutase produces apoptotic death of spinal neurons.
Rothstein, J. D., Bristol, L. A., Hosler, B. A., Brown, R. H., & Kuncl, R. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4155 · Cited by 292
Self-citationLopata, M. A., & Cleveland, D. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.4.1707 · Cited by 232
Self-citationA new family of neurotransmitter transporters: the high‐affinity glutamate transporters
Kanai, Y., Smith, C. P., & Hediger, M. A. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.15.7903261 · Cited by 226
Reduction of Naturally Occurring Motoneuron Death in Vivo by a Target-Derived Neurotrophic Factor
Oppenheim, R. W., Haverkamp, L. J., Prevette, D. M., McManaman, J. L., & Appel, S. H. (1988) · Science · doi:10.1126/science.3363373 · Cited by 208
Neurofibrillary axonal swellings and amyotrophic lateral sclerosis.
Delisle, M., & Carpenter, S. (1984) · Journal of Neurological Sciences · doi:10.1016/0022-510x(84)90199-0 · Cited by 167
Robberecht, W., Sapp, P. C., Viaene, M. K., Rosen, D. R., McKenna‐Yasek, D., Haines, J. L., Horvitz, H. R., Theys, P., & Brown, R. H. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62010384.x · Cited by 163
Borchelt, D., Guarnieri, M., Wong, P. C., Lee, M. K., Slunt, H. S., Xu, Z., Sisodia, S. S., Price, D. L., & Cleveland, D. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3234 · Cited by 152
Self-citationFilaments of Lewy bodies contain insoluble cytoskeletal elements.
Galloway, P. G., Mulvihill, P., & Perry, G. L. (1992) · PubMed Central · Cited by 131
Kato, S., Shimoda, M., Watanabe, Y., Nakashima, K., Takahashi, K., & Ohama, E. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199655100-00009 · Cited by 111
Nitric oxide inhibits 3H‐glutamate transport in synaptosomes
Pöğün, Ş., Dawson, V. L., & Kuhar, M. J. (1994) · Synapse · doi:10.1002/syn.890180104 · Cited by 102
Fujii, J., Myint, T., Seo, H. G., Kayanoki, Y., Ikeda, Y., & Taniguchi, N. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64041456.x · Cited by 34
[21] Automated assay of superoxide dismutase in blood
L’Abbé, M. R., & Fischer, P. W. F. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86113-a · Cited by 33
Involvement of neurofilaments in motor neuron disease
Xu, Z., Cork, L. C., Griffin, J. W., & Cleveland, D. W. (1993) · Journal of Cell Science · doi:10.1242/jcs.1993.supplement_17.15 · Cited by 33
Self-citation
Cited by
Sorted by citations
Danbolt, N. C. (2001) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00067-8 · Cited by 4,227
Davies, S. W., Turmaine, M., Cozens, B. A., DiFiglia, M., Sharp, A. H., Ross, C. A., Scherzinger, E., Wanker, E. E., Mangiarini, L., & Bates, G. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80513-9 · Cited by 2,188
Decoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,120
Self-citationOnset and Progression in Inherited ALS Determined by Motor Neurons and Microglia
Boillée, S., Yamanaka, K., Lobsiger, C. S., Copeland, N. G., Jenkins, N. A., Kassiotis, G., Kollias, G., & Cleveland, D. W. (2006) · Science · doi:10.1126/science.1123511 · Cited by 1,623
Self-citationALS: A Disease of Motor Neurons and Their Nonneuronal Neighbors
Boillée, S., Velde, C. V., & Cleveland, D. W. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.018 · Cited by 1,476
Self-citation
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