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. 1995 Feb 28;92(5):1251–1253. doi: 10.1073/pnas.92.5.1251

Amyotrophic lateral sclerosis: human challenge for neuroscience.

L P Rowland 1
PMCID: PMC42496  PMID: 7877963

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aoki M., Ogasawara M., Matsubara Y., Narisawa K., Nakamura S., Itoyama Y., Abe K. Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R mutation in Cu/Zn superoxide dismutase gene: a possible new subtype of familial ALS. J Neurol Sci. 1994 Oct;126(1):77–83. doi: 10.1016/0022-510x(94)90097-3. [DOI] [PubMed] [Google Scholar]
  2. Aoki M., Ogasawara M., Matsubara Y., Narisawa K., Nakamura S., Itoyama Y., Abe K. Mild ALS in Japan associated with novel SOD mutation. Nat Genet. 1993 Dec;5(4):323–324. doi: 10.1038/ng1293-323. [DOI] [PubMed] [Google Scholar]
  3. Beckman J. S., Carson M., Smith C. D., Koppenol W. H. ALS, SOD and peroxynitrite. Nature. 1993 Aug 12;364(6438):584–584. doi: 10.1038/364584a0. [DOI] [PubMed] [Google Scholar]
  4. Bergeron C., Beric-Maskarel K., Muntasser S., Weyer L., Somerville M. J., Percy M. E. Neurofilament light and polyadenylated mRNA levels are decreased in amyotrophic lateral sclerosis motor neurons. J Neuropathol Exp Neurol. 1994 May;53(3):221–230. doi: 10.1097/00005072-199405000-00002. [DOI] [PubMed] [Google Scholar]
  5. Borchelt D. R., Lee M. K., Slunt H. S., Guarnieri M., Xu Z. S., Wong P. C., Brown R. H., Jr, Price D. L., Sisodia S. S., Cleveland D. W. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8292–8296. doi: 10.1073/pnas.91.17.8292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bowling A. C., Schulz J. B., Brown R. H., Jr, Beal M. F. Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J Neurochem. 1993 Dec;61(6):2322–2325. doi: 10.1111/j.1471-4159.1993.tb07478.x. [DOI] [PubMed] [Google Scholar]
  7. Bracco F., Scarpa M., Rigo A., Battistin L. Determination of superoxide dismutase activity by the polarographic method of catalytic currents in the cerebrospinal fluid of aging brain and neurologic degenerative diseases. Proc Soc Exp Biol Med. 1991 Jan;196(1):36–41. doi: 10.3181/00379727-196-43160. [DOI] [PubMed] [Google Scholar]
  8. Brown R. H. A transgenic-mouse model of amyotrophic lateral sclerosis. N Engl J Med. 1994 Oct 20;331(16):1091–1092. doi: 10.1056/NEJM199410203311613. [DOI] [PubMed] [Google Scholar]
  9. Côté F., Collard J. F., Julien J. P. Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell. 1993 Apr 9;73(1):35–46. doi: 10.1016/0092-8674(93)90158-m. [DOI] [PubMed] [Google Scholar]
  10. Dal Canto M. C., Gurney M. E. Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am J Pathol. 1994 Dec;145(6):1271–1279. [PMC free article] [PubMed] [Google Scholar]
  11. Elshafey A., Lanyon W. G., Connor J. M. Identification of a new missense point mutation in exon 4 of the Cu/Zn superoxide dismutase (SOD-1) gene in a family with amyotrophic lateral sclerosis. Hum Mol Genet. 1994 Feb;3(2):363–364. doi: 10.1093/hmg/3.2.363. [DOI] [PubMed] [Google Scholar]
  12. Esteban J., Rosen D. R., Bowling A. C., Sapp P., McKenna-Yasek D., O'Regan J. P., Beal M. F., Horvitz H. R., Brown R. H., Jr Identification of two novel mutations and a new polymorphism in the gene for Cu/Zn superoxide dismutase in patients with amyotrophic lateral sclerosis. Hum Mol Genet. 1994 Jun;3(6):997–998. doi: 10.1093/hmg/3.6.997. [DOI] [PubMed] [Google Scholar]
  13. Eyer J., Peterson A. Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-beta-galactosidase fusion protein. Neuron. 1994 Feb;12(2):389–405. doi: 10.1016/0896-6273(94)90280-1. [DOI] [PubMed] [Google Scholar]
  14. Figlewicz D. A., Krizus A., Martinoli M. G., Meininger V., Dib M., Rouleau G. A., Julien J. P. Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum Mol Genet. 1994 Oct;3(10):1757–1761. doi: 10.1093/hmg/3.10.1757. [DOI] [PubMed] [Google Scholar]
  15. 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. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science. 1994 Jun 17;264(5166):1772–1775. doi: 10.1126/science.8209258. [DOI] [PubMed] [Google Scholar]
  16. Gurney M. E. Response. Science. 1994 Dec 2;266(5190):1587–1587. doi: 10.1126/science.266.5190.1587. [DOI] [PubMed] [Google Scholar]
  17. Hirano A. Cytopathology of amyotrophic lateral sclerosis. Adv Neurol. 1991;56:91–101. [PubMed] [Google Scholar]
  18. Iwasaki Y., Ikeda K., Kinoshita M. Decreased cerebrospinal-fluid superoxide dismutase in amyotrophic lateral sclerosis. Lancet. 1993 Oct 30;342(8879):1118–1118. doi: 10.1016/0140-6736(93)92104-2. [DOI] [PubMed] [Google Scholar]
  19. Jones C. T., Brock D. J., Chancellor A. M., Warlow C. P., Swingler R. J. Cu/Zn superoxide dismutase (SOD1) mutations and sporadic amyotrophic lateral sclerosis. Lancet. 1993 Oct 23;342(8878):1050–1051. doi: 10.1016/0140-6736(93)92905-9. [DOI] [PubMed] [Google Scholar]
  20. Jones C. T., Swingler R. J., Brock D. J. Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others. Hum Mol Genet. 1994 Apr;3(4):649–650. doi: 10.1093/hmg/3.4.649. [DOI] [PubMed] [Google Scholar]
  21. Kostrzewa M., Burck-Lehmann U., Müller U. Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene. Hum Mol Genet. 1994 Dec;3(12):2261–2262. doi: 10.1093/hmg/3.12.2261. [DOI] [PubMed] [Google Scholar]
  22. Lee M. K., Marszalek J. R., Cleveland D. W. A mutant neurofilament subunit causes massive, selective motor neuron death: implications for the pathogenesis of human motor neuron disease. Neuron. 1994 Oct;13(4):975–988. doi: 10.1016/0896-6273(94)90263-1. [DOI] [PubMed] [Google Scholar]
  23. Lowe J. New pathological findings in amyotrophic lateral sclerosis. J Neurol Sci. 1994 Jul;124 (Suppl):38–51. doi: 10.1016/0022-510x(94)90175-9. [DOI] [PubMed] [Google Scholar]
  24. Lynch T., Sano M., Marder K. S., Bell K. L., Foster N. L., Defendini R. F., Sima A. A., Keohane C., Nygaard T. G., Fahn S. Clinical characteristics of a family with chromosome 17-linked disinhibition-dementia-parkinsonism-amyotrophy complex. Neurology. 1994 Oct;44(10):1878–1884. doi: 10.1212/wnl.44.10.1878. [DOI] [PubMed] [Google Scholar]
  25. Majoor-Krakauer D., Ottman R., Johnson W. G., Rowland L. P. Familial aggregation of amyotrophic lateral sclerosis, dementia, and Parkinson's disease: evidence of shared genetic susceptibility. Neurology. 1994 Oct;44(10):1872–1877. doi: 10.1212/wnl.44.10.1872. [DOI] [PubMed] [Google Scholar]
  26. McCord J. M. Mutant mice, Cu,Zn superoxide dismutase, and motor neuron degeneration. Science. 1994 Dec 2;266(5190):1586–1587. [PubMed] [Google Scholar]
  27. McNamara J. O., Fridovich I. Human genetics. Did radicals strike Lou Gehrig? Nature. 1993 Mar 4;362(6415):20–21. doi: 10.1038/362020a0. [DOI] [PubMed] [Google Scholar]
  28. Migheli A., Cavalla P., Marino S., Schiffer D. A study of apoptosis in normal and pathologic nervous tissue after in situ end-labeling of DNA strand breaks. J Neuropathol Exp Neurol. 1994 Nov;53(6):606–616. doi: 10.1097/00005072-199411000-00008. [DOI] [PubMed] [Google Scholar]
  29. Mitchell J. D., Gatt J. A., Phillips T. M., Houghton E., Rostron G., Wignall C., Whittington J., Shaw I. C. Cu/Zn superoxide dismutase free radicals, and motoneuron disease. Lancet. 1993 Oct 23;342(8878):1051–1052. doi: 10.1016/0140-6736(93)92906-a. [DOI] [PubMed] [Google Scholar]
  30. Orrell R. W., deBelleroche J. S. Superoxide dismutase and ALS. Lancet. 1994 Dec 17;344(8938):1651–1652. doi: 10.1016/s0140-6736(94)90452-9. [DOI] [PubMed] [Google Scholar]
  31. Pardo C. A., Xu Z., Borchelt D. R., Price D. L., Sisodia S. S., Cleveland D. W. Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):954–958. doi: 10.1073/pnas.92.4.954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Pramatarova A., Goto J., Nanba E., Nakashima K., Takahashi K., Takagi A., Kanazawa I., Figlewicz D. A., Rouleau G. A. A two basepair deletion in the SOD 1 gene causes familial amyotrophic lateral sclerosis. Hum Mol Genet. 1994 Nov;3(11):2061–2062. [PubMed] [Google Scholar]
  33. Price D. L., Cleveland D. W., Koliatsos V. E. Motor neurone disease and animal models. Neurobiol Dis. 1994 Nov;1(1-2):3–11. doi: 10.1006/nbdi.1994.0002. [DOI] [PubMed] [Google Scholar]
  34. Przedborski S., Jackson-Lewis V., Kostic V., Carlson E., Epstein C. J., Cadet J. L. Superoxide dismutase, catalase, and glutathione peroxidase activities in copper/zinc-superoxide dismutase transgenic mice. J Neurochem. 1992 May;58(5):1760–1767. doi: 10.1111/j.1471-4159.1992.tb10051.x. [DOI] [PubMed] [Google Scholar]
  35. Przedborski S., Kostic V., Jackson-Lewis V., Naini A. B., Simonetti S., Fahn S., Carlson E., Epstein C. J., Cadet J. L. Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity. J Neurosci. 1992 May;12(5):1658–1667. doi: 10.1523/JNEUROSCI.12-05-01658.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Puymirat J., Cossette L., Gosselin F., Bouchard J. P. Red blood cell Cu/Zn superoxide dismutase activity in sporadic amyotrophic lateral sclerosis. J Neurol Sci. 1994 Dec 1;127(1):121–123. doi: 10.1016/0022-510x(94)90145-7. [DOI] [PubMed] [Google Scholar]
  37. Ripps M. E., Huntley G. W., Hof P. R., Morrison J. H., Gordon J. W. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):689–693. doi: 10.1073/pnas.92.3.689. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Robberecht W., Sapp P., Viaene M. K., Rosen D., McKenna-Yasek D., Haines J., Horvitz R., Theys P., Brown R., Jr Cu/Zn superoxide dismutase activity in familial and sporadic amyotrophic lateral sclerosis. J Neurochem. 1994 Jan;62(1):384–387. doi: 10.1046/j.1471-4159.1994.62010384.x. [DOI] [PubMed] [Google Scholar]
  39. Rosen D. R., Bowling A. C., Patterson D., Usdin T. B., Sapp P., Mezey E., McKenna-Yasek D., O'Regan J., Rahmani Z., Ferrante R. J. A frequent ala 4 to val superoxide dismutase-1 mutation is associated with a rapidly progressive familial amyotrophic lateral sclerosis. Hum Mol Genet. 1994 Jun;3(6):981–987. doi: 10.1093/hmg/3.6.981. [DOI] [PubMed] [Google Scholar]
  40. 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. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993 Mar 4;362(6415):59–62. doi: 10.1038/362059a0. [DOI] [PubMed] [Google Scholar]
  41. Rothstein J. D., Bristol L. A., Hosler B., Brown R. H., Jr, Kuncl R. W. Chronic inhibition of superoxide dismutase produces apoptotic death of spinal neurons. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4155–4159. doi: 10.1073/pnas.91.10.4155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Rowland L. P. Amyotrophic lateral sclerosis. Curr Opin Neurol. 1994 Aug;7(4):310–315. doi: 10.1097/00019052-199408000-00006. [DOI] [PubMed] [Google Scholar]
  43. Troy C. M., Shelanski M. L. Down-regulation of copper/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6384–6387. doi: 10.1073/pnas.91.14.6384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Uchino M., Ando Y., Tanaka Y., Nakamura T., Uyama E., Mita S., Murakami T., Ando M. Decrease in Cu/Zn- and Mn-superoxide dismutase activities in brain and spinal cord of patients with amyotrophic lateral sclerosis. J Neurol Sci. 1994 Dec 1;127(1):61–67. doi: 10.1016/0022-510x(94)90136-8. [DOI] [PubMed] [Google Scholar]
  45. Xu Z., Cork L. C., Griffin J. W., Cleveland D. W. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell. 1993 Apr 9;73(1):23–33. doi: 10.1016/0092-8674(93)90157-l. [DOI] [PubMed] [Google Scholar]

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