Crossref
journal-article
Springer Science and Business Media LLC
Nature Neuroscience (297)
References
42
Referenced
213
-
Rosen, D. R. et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59–62 (1993).
(
10.1038/362059a0) / Nature by DR Rosen (1993) -
Deng, H. X. et al. Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261, 1047–1051 (1993).
(
10.1126/science.8351519) / Science by HX Deng (1993) -
Wong, P. C. et al. An adverse property of a familial ALS–linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105–1116 (1995).
(
10.1016/0896-6273(95)90259-7) / Neuron by PC Wong (1995) -
Gurney, M. E. et al. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264, 1772–1775 (1994).
(
10.1126/science.8209258) / Science by ME Gurney (1994) -
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. 92, 689–693 (1995).
(
10.1073/pnas.92.3.689) / Proc. Natl. Acad. Sci. by ME Ripps (1995) -
Bruijn, L. I. et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 18, 327–338 (1997).
(
10.1016/S0896-6273(00)80272-X) / Neuron by LI Bruijn (1997) -
Julien, J.-P. Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded. Cell 104, 581–591 (2001).
(
10.1016/S0092-8674(01)00244-6) / Cell by J-P Julien (2001) -
Cleveland, D. W. & Rothstein, J. D. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2, 806–819 (2001).
(
10.1038/35097565) / Nat. Rev. Neurosci. by DW Cleveland (2001) -
Estevez, A. G. et al. Induction of nitric oxide–dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 286, 2498–2500 (1999).
(
10.1126/science.286.5449.2498) / Science by AG Estevez (1999) -
Wiedau-Pazos, M. et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271, 515–518 (1996).
(
10.1126/science.271.5248.515) / Science by M Wiedau-Pazos (1996) -
Beckman, J. S., Carson, M., Smith, C. D. & Koppenol, W. H. ALS, SOD and peroxynitrite. Nature 364, 584 (1993).
(
10.1038/364584a0) -
Rae, T. D., Schmidt, P. J., Pufahl, R. A., Culotta, V. C. & O'Halloran, T. V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284, 805–808 (1999).
(
10.1126/science.284.5415.805) / Science by TD Rae (1999) -
Kuo, Y. M., Zhou, B., Cosco, D. & Gitschier, J. The copper transporter CTR1 provides an essential function in mammalian embryonic development. Proc. Natl. Acad. Sci. USA 98, 6836–6841 (2001).
(
10.1073/pnas.111057298) / Proc. Natl. Acad. Sci. USA by YM Kuo (2001) -
Lee, J., Prohaska, J. R. & Thiele, D. J. Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development. Proc. Natl. Acad. Sci. USA 98, 6842–6847 (2001).
(
10.1073/pnas.111058698) / Proc. Natl. Acad. Sci. USA by J Lee (2001) -
Culotta, V. C. et al. Intracellular pathways of copper trafficking in yeast and humans. Adv. Exp. Med. Biol. 448, 247–254 (1999).
(
10.1007/978-1-4615-4859-1_22) / Adv. Exp. Med. Biol. by VC Culotta (1999) -
Culotta, V. C. et al. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272, 23469–23472 (1997).
(
10.1074/jbc.272.38.23469) / J. Biol. Chem. by VC Culotta (1997) -
Torres, A. S., Petri, V., Rae, T. D. & O'Halloran, T. V. Copper-stabilized heterodimer of the yCCS metallochaperone and its target superoxide dismutase. J. Biol. Chem. 276, 38410–38416 (2001).
(
10.1074/jbc.M104790200) / J. Biol. Chem. by AS Torres (2001) -
Wong, P. C. et al. Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proc. Natl. Acad. Sci. USA 97, 2886–2891 (2000).
(
10.1073/pnas.040461197) / Proc. Natl. Acad. Sci. USA by PC Wong (2000) -
Crapo, J., McCord, J. M. & Fridovich, I. Preparation and assay of superoxide dismutases. Methods Enzymol. 53, 382–393 (1978).
(
10.1016/S0076-6879(78)53044-9) / Methods Enzymol. by J Crapo (1978) -
Reaume, A. G. et al. Motor neurons in Cu/Zn superoxide dismutase–deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genetics 13, 43–47 (1996).
(
10.1038/ng0596-43) / Nat. Genetics by AG Reaume (1996) -
Mouton, P. R. et al. Cognitive decline strongly correlates with cortical atrophy in Alzheimer's dementia. Neurobiol. Aging 19, 371–377 (1998).
(
10.1016/S0197-4580(98)00080-3) / Neurobiol. Aging by PR Mouton (1998) -
Lyons, W. E. et al. Neuronal regeneration enhances the expression of the immunophilin FKBP-12. J. Neurosci. 15, 2985–2994 (1995).
(
10.1523/JNEUROSCI.15-04-02985.1995) / J. Neurosci. by WE Lyons (1995) -
Williamson, T. L. et al. Toxicity of ALS-linked SOD1 mutants. Science 288, 399 (2000).
(
10.1126/science.288.5465.399a) / Science by TL Williamson (2000) -
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).
(
10.1073/pnas.91.17.8292) / Proc. Natl. Acad. Sci. USA by DR Borchelt (1994) -
Corson, L. B, Strain, J. J., Culotta, V. C. & Cleveland, D. W. Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis–linked superoxide dismutase mutants. Proc. Natl. Acad. Sci. USA 95, 6361–6366 (1998).
(
10.1073/pnas.95.11.6361) / Proc. Natl. Acad. Sci. by LB Corson (1998) -
Crow, J. P. et al. Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L. J. Neurochem. 69, 1945–1953 (1997).
(
10.1046/j.1471-4159.1997.69051945.x) / J. Neurochem. by JP Crow (1997) -
Doroudchi, M. M., Minotti, S., Figlewicz, D. A. & Durham, H. D. Nitrotyrosination contributes minimally to toxicity of mutant SOD1 associated with ALS. Neuroreport 12, 1239–1243 (2001).
(
10.1097/00001756-200105080-00037) / Neuroreport by MM Doroudchi (2001) -
Facchinetti, F. et al. Lack of involvement of neuronal nitric oxide synthase in the pathogenesis of a transgenic mouse model of familial amyotrophic lateral sclerosis. Neuroscience 90, 1483–1492 (1999).
(
10.1016/S0306-4522(98)00492-8) / Neuroscience by F Facchinetti (1999) -
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).
(
10.1073/pnas.93.12.5709) / Proc. Natl. Acad. Sci. USA by MB Yim (1996) -
Yim, H. S. et al. 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).
(
10.1074/jbc.272.14.8861) / J. Biol. Chem. by HS Yim (1997) -
Singh, R. J. et al. Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis–associated Cu,Zn superoxide dismutase mutants and H2O2 . Proc. Natl. Acad. Sci. USA 95, 6675–6680 (1998).
(
10.1073/pnas.95.12.6675) / Proc. Natl. Acad. Sci. USA by RJ Singh (1998) -
Sankarapandi, S. & Zweier, J. L. Evidence against the generation of free hydroxyl radicals from the interaction of copper, zinc-superoxide dismutase and hydrogen peroxide. J. Biol. Chem. 274, 34576–34583 (1999).
(
10.1074/jbc.274.49.34576) / J. Biol. Chem. by S Sankarapandi (1999) -
Goto, J. J. et al. Loss of in vitro metal ion binding specificity in mutant copper–zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 275, 1007–1014 (2000).
(
10.1074/jbc.275.2.1007) / J. Biol. Chem. by JJ Goto (2000) -
Liu, H. et al. Copper2+ binding to the surface residue cysteine 111 of His46Arg human copper–zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant. Biochemistry 39, 8125–8132 (2000).
(
10.1021/bi000846f) / Biochemistry by H Liu (2000) -
Martin, L. J. Neuronal death in amyotrophic lateral sclerosis is apoptosis: possible contribution of a programmed cell death mechanism. J. Neuropathol. Exp. Neurol. 58, 459–471 (1999).
(
10.1097/00005072-199905000-00005) / J. Neuropathol. Exp. Neurol. by LJ Martin (1999) -
Li, M. et al. Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science 288, 335–339 (2000).
(
10.1126/science.288.5464.335) / Science by M Li (2000) -
Pasinelli, P., Houseweart, M. K., Brown, R. H. Jr. & Cleveland, D. W. Caspase-1 and -3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase–mediated familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 97, 13901–13906 (2000).
(
10.1073/pnas.240305897) / Proc. Natl. Acad. Sci. USA by P Pasinelli (2000) -
Bruijn, L. I. et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281, 1851–1854 (1998).
(
10.1126/science.281.5384.1851) / Science by LI Bruijn (1998) -
Johnston, J. A, Dalton, M. J., Gurney, M. E. & Kopito, R. R. Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 97, 12571–12576 (2000).
(
10.1073/pnas.220417997) / Proc. Natl. Acad. Sci. USA by JA Johnston (2000) -
Beaulieu, J. M., Jacomy, H. & Julien, J. P. Formation of intermediate filament protein aggregates with disparate effects in two transgenic mouse models lacking the neurofilament light subunit. J. Neurosci. 20, 5321–5328 (2000).
(
10.1523/JNEUROSCI.20-14-05321.2000) / J. Neurosci. by JM Beaulieu (2000) -
Sunderman, F. W. Jr. & Nomoto, S. Measurement of human serum ceruloplasmin by its p-phenylenediamine oxidase activity. Clin. Chem. 11, 903–910 (1970).
(
10.1093/clinchem/16.11.903) / Clin. Chem. by FW Sunderman Jr. (1970) -
Prohaska, J. R & Bailey, W. R. Persistent regional changes in brain copper, cuproenzymes and catecholamines following perinatal copper deficiency in mice. J. Nutr. 123, 1226–1234 (1993).
(
10.1093/jn/123.7.1226) / J. Nutr. by JR Prohaska (1993)
Dates
| Type | When |
|---|---|
| Created | 23 years, 1 month ago (July 26, 2002, 4:31 a.m.) |
| Deposited | 2 years, 3 months ago (May 18, 2023, 8:02 p.m.) |
| Indexed | 1 month ago (July 24, 2025, 7:37 a.m.) |
| Issued | 23 years, 5 months ago (March 11, 2002) |
| Published | 23 years, 5 months ago (March 11, 2002) |
| Published Online | 23 years, 5 months ago (March 11, 2002) |
| Published Print | 23 years, 4 months ago (April 1, 2002) |
@article{Subramaniam_2002, title={Mutant SOD1 causes motor neuron disease independent of copper chaperone–mediated copper loading}, volume={5}, ISSN={1546-1726}, url={http://dx.doi.org/10.1038/nn823}, DOI={10.1038/nn823}, number={4}, journal={Nature Neuroscience}, publisher={Springer Science and Business Media LLC}, author={Subramaniam, Jamuna R. and Lyons, W. Ernest and Liu, Jian and Bartnikas, Thomas B. and Rothstein, Jeffrey and Price, Donald L. and Cleveland, Don W. and Gitlin, Jonathan D. and Wong, Philip C.}, year={2002}, month=mar, pages={301–307} }