Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 373

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter

Trotti, Davide, Rolfs, Andreas, Danbolt, Niels C., Brown, Robert H., Hediger, Matthias A.·1999·Nature Neuroscience
DOI 10.1038/8091
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/8091

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 46

  1. Gurney, M. E. et al. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science 264, 1772–1775 (1994). · DOI · Paper page
  2. Bruijn, L. I. et al. Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc. Natl. Acad. Sci. USA 94, 7606– 7611 (1997). · DOI · Paper page
  3. Bogdanov, M. B., Ramos, L. E., Xu, Z. & Beal, M. F. Elevated hydroxyl radical generation in vivo in an animal model of amyotrophic lateral sclerosis. J. Neurochem. 71, 1321– 1324 (1998). · DOI
  4. Ferrante, R. J. et al. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J. Neurochem. 69, 2064–2074 (1997). · DOI · Paper page
  5. Borchelt, D. R. et al. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl. Acad. Sci. USA 91, 8292–8296 ( 1994). · DOI · Paper page
  6. Borchelt, D. R. et al. Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J. Biol. Chem. 270, 3234–3238 (1995). · DOI
  7. Deng, H-X. et al. Amyotrophic lateral sclerosis and structural defects in Cu, Zn superoxide dismutase. Science 261, 1047– 1051 (1993). · DOI · Paper page
  8. Yim, H-S., Kang, J-H., Chock, P. B., Stadtman, E. R. & Yim, M. B. A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value. J. Biol. Chem. 272, 8861– 8863 (1997). · DOI
  9. Wiedau-Pazos, M. et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271, 515– 518 (1996). · DOI · Paper page
  10. Yim, M. B. et al. A gain of function of an amyotrophic lateral sclerosis-associated Cu, Zn superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Km for hydrogen peroxide. Proc. Natl. Acad. Sci. USA 93, 5709–5714 (1996). · DOI · Paper page
  11. Rothstein, J. D. et al. Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate. Neuron 16, 675–686 ( 1996). · DOI · Paper page
  12. Haugeto, O. et al. Brain glutamate transporter proteins form homomultimers. J. Biol. Chem. 271, 27715–27722 (1996). · DOI · Paper page
  13. Lehre, K. P. & Danbolt, N. C. The number of glutamate transporter subtype molecules at glutamatergic synapses: chemical and stereological quantification in young adult rat brain. J. Neurosci. 18, 8751–8757 (1998). · DOI · Paper page
  14. Rothstein, J. D., Martin, L. J. & Kuncl, R. W. Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis. N. Engl. J. Med. 326, 1464–1468 (1992). · DOI · Paper page
  15. Rothstein, J. D., Van Kammen, M., Levey, A. I., Martin, L. J. & Kuncl, R. W. Selective loss of glial glutamate transporter GLT1 in amyotrophic lateral sclerosis. Ann. Neurol. 38, 73–84 ( 1995). · DOI · Paper page
  16. Bristol, L. A. & Rothstein, J. D. Glutamate transporter gene expression in amyotrophic lateral sclerosis motor cortex. Ann. Neurol. 39, 676–679 (1996). · DOI
  17. Aoki, M. et al. Mutations in the glutamate transporter EAAT2 gene do not cause abnormal EAAT2 transcripts in amyotrophic lateral sclerosis. Ann. Neurol. 43, 645–653 ( 1998). · DOI
  18. Lin, C-L. G. et al. Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. Neuron 20, 589–602 (1998). · DOI · Paper page
  19. Canton, T., Pratt, J., Stutzmann, J-M., Imperato, A. & Boireau, A. Glutamate uptake is decreased tardively in the spinal cord of FALS mice. Neuroreport 9, 775–778 (1998). · DOI
  20. Pedersen, W. A. et al. Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients. Ann. Neurol. 44, 819–824 (1998). · DOI · Paper page
  21. Trotti, D. et al. Peroxynitrite inhibits glutamate transporter subtypes. J. Biol. Chem. 271, 5976–5979 (1996). · DOI · Paper page
  22. Trotti, D., Nussberger, S., Volterra, A. & Hediger, M. A. Differential modulation of the uptake currents by redox interconversion of cysteine residues in the human neuronal glutamate transporter EAAC1. Eur. J. Neurosci. 9, 2207–2212 (1997). · DOI
  23. Trotti, D., Danbolt, N. C. & Volterra, A. Glutamate transporters are oxidant-vulnerable: a molecular link between oxidative and excitotoxic neurodegeneration? Trends Pharmacol. Sci. 19, 328–334 (1998). · DOI · Paper page
  24. Taylor, P. M., Kaur, S., Mackenzie, B. & Peter, G. J. Amino-acid-dependent modulation of amino acid transporter in Xenopus laevis oocytes. J. Exp. Biol. 199, 923–931 (1996). · DOI
  25. Robberecht, W. et al. Cu/Zn superoxide dismutase activity in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 62, 384–387 (1994). · DOI
  26. Tu, P-H., Gurney, M. E., Julien, J-P., Lee, V. M. & Trojanowski, J. Q. Oxidative stress, mutant SOD1, and neurofilament pathology in transgenic mouse models of human motor neuron disease. Lab. Invest. 76, 441– 456 (1997).
  27. Siddique, T. & Deng, H. X. Genetics of amyotrophic lateral sclerosis. Hum. Mol. Gen. 5, 1465– 1470 (1996). · DOI
  28. Gillis, K. D. in Single Channel Recording 2nd edn. (eds. Sakmann, B. & Neher, E.) 155–198 (Plenum, New York, 1995). · DOI · Paper page
  29. Davies, K. J., Delsignore, M. E. & Lin, S. W. Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J. Biol. Chem. 262 , 9902–9907 (1987). · DOI · Paper page
  30. Zerangue, N. & Kavanaugh, M. P. Flux coupling in a neuronal glutamate transporter. Nature 383, 634– 637 (1996). · DOI · Paper page
  31. Davies, K. J. Protein damage and degeneration by oxygen radicals. I. General aspects. J. Biol. Chem. 262, 9895–9901 (1987). · DOI · Paper page
  32. Grunewald, M., Bendahan, A. & Kanner, B. I. Biotinylation of single cysteine mutants of the glutamate transporter GLT1 from rat brain reveals its unusual topology. Neuron 21, 623–632 ( 1998). · DOI
  33. Day, B. J., Fridovich, I. & Crapo, J. D. Manganic porphyrins possess catalase activity and protect endothelial cells against hydrogen peroxide-mediated injury. Arch. Biochem. Biophys. 347, 256–262 (1997). · DOI · Paper page
  34. Batinic-Haberle, I., Liochev, S. I., Spasojevic, I. & Fridovich, I. A potent superoxide dismutase mimic: Manganese β-octabromo-meso-etrakis-(N-methylpyridinium-4-yl) porphyrin. Arch. Biochem. Biophys. 343, 225–233 (1997). · DOI
  35. Mu, X., He, J., Anderson, D. W., Trojanowski, J. Q. & Springer, J. E. Altered expression of bcl-2 and bax mRNA in amyotrophic lateral sclerosis spinal cord motor neurons. Ann. Neurol. 40, 379–386 (1996). · DOI
  36. Eisen, A. Amyotrophic lateral sclerosis is a multifactorial disease. Muscle Nerve 18, 741–752 ( 1995). · DOI
  37. Brown, R. H. Jr. Free radicals, programmed cell death and muscular dystrophy. Curr. Opin. Neurol. 8, 373– 378 (1995). · DOI
  38. Brown, R. H. Jr. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 80, 687– 692 (1995). · DOI · Paper page
  39. van Iwaarden, P. R., Driessen, A. J. & Koning, W. N. What we can learn from the effects of thiol reagents on transport proteins. Biochem. Biophys. Acta 1113, 161–170 (1992).
  40. Davies, K. J. A. & Delsignore, M. E. Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure. J. Biol. Chem. 262, 9908–9913 (1987). · DOI · Paper page
  41. Davies, K. J. A., Lin, S. W. & Pacifici, R. E. Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. J. Biol. Chem. 262, 9914–9920 (1987). · DOI · Paper page
  42. Tanaka, K. et al. Epilepsy and exacerbation of brain injury in mice lacking the glutamate transporter GLT1. Science 276, 1699–1702 (1997). · DOI · Paper page
  43. Bensimon, G., Lacomblez, L. & Meininger, V. A controlled trial of riluzole in amyotrophic lateral sclerosis. ALS/riluzole study group. N. Engl. J. Med. 330, 585–591 (1994). · DOI · Paper page
  44. Lacomblez, L., Bensimon, G., Leigh, P. N., Guillet, P. & Meininger, V. Dose-ranging study of riluzole in amyotrophic lateral sclerosis. Amyotrophic lateral sclerosis/riluzole study group II. Lancet 347, 1425– 1431 (1996). · DOI · Paper page
  45. Gurney, M. E., Fleck, T. J., Himes, C. S. & Hall, E. D. Riluzole preserves motor function in a transgenic model of familial amyotrophic lateral sclerosis. Neurology 50, 62– 66 (1998). · DOI
  46. Arriza, J. L. et al. Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. J. Neurosci. 14, 5559–5569 (1994). · DOI · Paper page

Cited by

See all 373

Metadata

Authors
Trotti, D., Rolfs, A., Danbolt, N. C., Brown, R. H., & Hediger, M. A.
Venue
Nature Neuroscience
Publisher
Springer Science and Business Media LLC
Published
1999-05
Volume
2
Issue
5
Pages
427-433
ISSN
  • 1097-6256 (ISSN-L)
  • 1546-1726
DOI
10.1038/8091
OpenAlex
W1555605403
Cited by
373
References
2
FWCI
20.98
Type
journal article
Language
en
Update notices
erratum (1999-09-01)
Open access
closed
Licence

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

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.