{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:37:16Z","timestamp":1779345436471,"version":"3.51.4"},"reference-count":42,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2002,3,11]],"date-time":"2002-03-11T00:00:00Z","timestamp":1015804800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Neurosci"],"published-print":{"date-parts":[[2002,4]]},"DOI":"10.1038\/nn823","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T04:31:14Z","timestamp":1027657874000},"page":"301-307","source":"Crossref","is-referenced-by-count":217,"title":["Mutant SOD1 causes motor neuron disease independent of copper chaperone\u2013mediated copper loading"],"prefix":"10.1038","volume":"5","author":[{"given":"Jamuna R.","family":"Subramaniam","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"W. Ernest","family":"Lyons","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jian","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas B.","family":"Bartnikas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeffrey","family":"Rothstein","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Donald L.","family":"Price","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Don W.","family":"Cleveland","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonathan D.","family":"Gitlin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Philip C.","family":"Wong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2002,3,11]]},"reference":[{"key":"BFnn823_CR1","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1038\/362059a0","volume":"362","author":"DR Rosen","year":"1993","unstructured":"Rosen, D. R. et al. Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59\u201362 (1993).","journal-title":"Nature"},{"key":"BFnn823_CR2","doi-asserted-by":"publisher","first-page":"1047","DOI":"10.1126\/science.8351519","volume":"261","author":"HX Deng","year":"1993","unstructured":"Deng, H. X. et al. Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261, 1047\u20131051 (1993).","journal-title":"Science"},{"key":"BFnn823_CR3","doi-asserted-by":"publisher","first-page":"1105","DOI":"10.1016\/0896-6273(95)90259-7","volume":"14","author":"PC Wong","year":"1995","unstructured":"Wong, P. C. et al. An adverse property of a familial ALS\u2013linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105\u20131116 (1995).","journal-title":"Neuron"},{"key":"BFnn823_CR4","doi-asserted-by":"publisher","first-page":"1772","DOI":"10.1126\/science.8209258","volume":"264","author":"ME Gurney","year":"1994","unstructured":"Gurney, M. E. et al. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264, 1772\u20131775 (1994).","journal-title":"Science"},{"key":"BFnn823_CR5","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1073\/pnas.92.3.689","volume":"92","author":"ME Ripps","year":"1995","unstructured":"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\u2013693 (1995).","journal-title":"Proc. Natl. Acad. Sci."},{"key":"BFnn823_CR6","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1016\/S0896-6273(00)80272-X","volume":"18","author":"LI Bruijn","year":"1997","unstructured":"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\u2013338 (1997).","journal-title":"Neuron"},{"key":"BFnn823_CR7","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1016\/S0092-8674(01)00244-6","volume":"104","author":"J-P Julien","year":"2001","unstructured":"Julien, J.-P. Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded. Cell 104, 581\u2013591 (2001).","journal-title":"Cell"},{"key":"BFnn823_CR8","doi-asserted-by":"publisher","first-page":"806","DOI":"10.1038\/35097565","volume":"2","author":"DW Cleveland","year":"2001","unstructured":"Cleveland, D. W. & Rothstein, J. D. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2, 806\u2013819 (2001).","journal-title":"Nat. Rev. Neurosci."},{"key":"BFnn823_CR9","doi-asserted-by":"publisher","first-page":"2498","DOI":"10.1126\/science.286.5449.2498","volume":"286","author":"AG Estevez","year":"1999","unstructured":"Estevez, A. G. et al. Induction of nitric oxide\u2013dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 286, 2498\u20132500 (1999).","journal-title":"Science"},{"key":"BFnn823_CR10","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1126\/science.271.5248.515","volume":"271","author":"M Wiedau-Pazos","year":"1996","unstructured":"Wiedau-Pazos, M. et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271, 515\u2013518 (1996).","journal-title":"Science"},{"key":"BFnn823_CR11","doi-asserted-by":"crossref","unstructured":"Beckman, J. S., Carson, M., Smith, C. D. & Koppenol, W. H. ALS, SOD and peroxynitrite. Nature 364, 584 (1993).","DOI":"10.1038\/364584a0"},{"key":"BFnn823_CR12","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1126\/science.284.5415.805","volume":"284","author":"TD Rae","year":"1999","unstructured":"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\u2013808 (1999).","journal-title":"Science"},{"key":"BFnn823_CR13","doi-asserted-by":"publisher","first-page":"6836","DOI":"10.1073\/pnas.111057298","volume":"98","author":"YM Kuo","year":"2001","unstructured":"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\u20136841 (2001).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR14","doi-asserted-by":"publisher","first-page":"6842","DOI":"10.1073\/pnas.111058698","volume":"98","author":"J Lee","year":"2001","unstructured":"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\u20136847 (2001).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR15","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1007\/978-1-4615-4859-1_22","volume":"448","author":"VC Culotta","year":"1999","unstructured":"Culotta, V. C. et al. Intracellular pathways of copper trafficking in yeast and humans. Adv. Exp. Med. Biol. 448, 247\u2013254 (1999).","journal-title":"Adv. Exp. Med. Biol."},{"key":"BFnn823_CR16","doi-asserted-by":"publisher","first-page":"23469","DOI":"10.1074\/jbc.272.38.23469","volume":"272","author":"VC Culotta","year":"1997","unstructured":"Culotta, V. C. et al. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272, 23469\u201323472 (1997).","journal-title":"J. Biol. Chem."},{"key":"BFnn823_CR17","doi-asserted-by":"publisher","first-page":"38410","DOI":"10.1074\/jbc.M104790200","volume":"276","author":"AS Torres","year":"2001","unstructured":"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\u201338416 (2001).","journal-title":"J. Biol. Chem."},{"key":"BFnn823_CR18","doi-asserted-by":"publisher","first-page":"2886","DOI":"10.1073\/pnas.040461197","volume":"97","author":"PC Wong","year":"2000","unstructured":"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\u20132891 (2000).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR19","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1016\/S0076-6879(78)53044-9","volume":"53","author":"J Crapo","year":"1978","unstructured":"Crapo, J., McCord, J. M. & Fridovich, I. Preparation and assay of superoxide dismutases. Methods Enzymol. 53, 382\u2013393 (1978).","journal-title":"Methods Enzymol."},{"key":"BFnn823_CR20","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1038\/ng0596-43","volume":"13","author":"AG Reaume","year":"1996","unstructured":"Reaume, A. G. et al. Motor neurons in Cu\/Zn superoxide dismutase\u2013deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genetics 13, 43\u201347 (1996).","journal-title":"Nat. Genetics"},{"key":"BFnn823_CR21","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1016\/S0197-4580(98)00080-3","volume":"19","author":"PR Mouton","year":"1998","unstructured":"Mouton, P. R. et al. Cognitive decline strongly correlates with cortical atrophy in Alzheimer's dementia. Neurobiol. Aging 19, 371\u2013377 (1998).","journal-title":"Neurobiol. Aging"},{"key":"BFnn823_CR22","doi-asserted-by":"publisher","first-page":"2985","DOI":"10.1523\/JNEUROSCI.15-04-02985.1995","volume":"15","author":"WE Lyons","year":"1995","unstructured":"Lyons, W. E. et al. Neuronal regeneration enhances the expression of the immunophilin FKBP-12. J. Neurosci. 15, 2985\u20132994 (1995).","journal-title":"J. Neurosci."},{"key":"BFnn823_CR23","doi-asserted-by":"publisher","first-page":"399","DOI":"10.1126\/science.288.5465.399a","volume":"288","author":"TL Williamson","year":"2000","unstructured":"Williamson, T. L. et al. Toxicity of ALS-linked SOD1 mutants. Science 288, 399 (2000).","journal-title":"Science"},{"key":"BFnn823_CR24","doi-asserted-by":"publisher","first-page":"8292","DOI":"10.1073\/pnas.91.17.8292","volume":"91","author":"DR Borchelt","year":"1994","unstructured":"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\u20138296 (1994).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR25","doi-asserted-by":"publisher","first-page":"6361","DOI":"10.1073\/pnas.95.11.6361","volume":"95","author":"LB Corson","year":"1998","unstructured":"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\u2013linked superoxide dismutase mutants. Proc. Natl. Acad. Sci. USA 95, 6361\u20136366 (1998).","journal-title":"Proc. Natl. Acad. Sci."},{"key":"BFnn823_CR26","doi-asserted-by":"publisher","first-page":"1945","DOI":"10.1046\/j.1471-4159.1997.69051945.x","volume":"69","author":"JP Crow","year":"1997","unstructured":"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\u20131953 (1997).","journal-title":"J. Neurochem."},{"key":"BFnn823_CR27","doi-asserted-by":"publisher","first-page":"1239","DOI":"10.1097\/00001756-200105080-00037","volume":"12","author":"MM Doroudchi","year":"2001","unstructured":"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\u20131243 (2001).","journal-title":"Neuroreport"},{"key":"BFnn823_CR28","doi-asserted-by":"publisher","first-page":"1483","DOI":"10.1016\/S0306-4522(98)00492-8","volume":"90","author":"F Facchinetti","year":"1999","unstructured":"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\u20131492 (1999).","journal-title":"Neuroscience"},{"key":"BFnn823_CR29","doi-asserted-by":"publisher","first-page":"5709","DOI":"10.1073\/pnas.93.12.5709","volume":"93","author":"MB Yim","year":"1996","unstructured":"Yim, M. B. et al. A gain-of-function of an amyotrophic lateral sclerosis\u2013associated 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\u20135714 (1996).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR30","doi-asserted-by":"publisher","first-page":"8861","DOI":"10.1074\/jbc.272.14.8861","volume":"272","author":"HS Yim","year":"1997","unstructured":"Yim, H. S. et al. A familial amyotrophic lateral sclerosis\u2013associated 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\u20138863 (1997).","journal-title":"J. Biol. Chem."},{"key":"BFnn823_CR31","doi-asserted-by":"publisher","first-page":"6675","DOI":"10.1073\/pnas.95.12.6675","volume":"95","author":"RJ Singh","year":"1998","unstructured":"Singh, R. J. et al. Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis\u2013associated Cu,Zn superoxide dismutase mutants and H2O2 . Proc. Natl. Acad. Sci. USA 95, 6675\u20136680 (1998).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR32","doi-asserted-by":"publisher","first-page":"34576","DOI":"10.1074\/jbc.274.49.34576","volume":"274","author":"S Sankarapandi","year":"1999","unstructured":"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\u201334583 (1999).","journal-title":"J. Biol. Chem."},{"key":"BFnn823_CR33","doi-asserted-by":"publisher","first-page":"1007","DOI":"10.1074\/jbc.275.2.1007","volume":"275","author":"JJ Goto","year":"2000","unstructured":"Goto, J. J. et al. Loss of in vitro metal ion binding specificity in mutant copper\u2013zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 275, 1007\u20131014 (2000).","journal-title":"J. Biol. Chem."},{"key":"BFnn823_CR34","doi-asserted-by":"publisher","first-page":"8125","DOI":"10.1021\/bi000846f","volume":"39","author":"H Liu","year":"2000","unstructured":"Liu, H. et al. Copper2+ binding to the surface residue cysteine 111 of His46Arg human copper\u2013zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant. Biochemistry 39, 8125\u20138132 (2000).","journal-title":"Biochemistry"},{"key":"BFnn823_CR35","doi-asserted-by":"publisher","first-page":"459","DOI":"10.1097\/00005072-199905000-00005","volume":"58","author":"LJ Martin","year":"1999","unstructured":"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\u2013471 (1999).","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"BFnn823_CR36","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1126\/science.288.5464.335","volume":"288","author":"M Li","year":"2000","unstructured":"Li, M. et al. Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science 288, 335\u2013339 (2000).","journal-title":"Science"},{"key":"BFnn823_CR37","doi-asserted-by":"publisher","first-page":"13901","DOI":"10.1073\/pnas.240305897","volume":"97","author":"P Pasinelli","year":"2000","unstructured":"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\u2013mediated familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 97, 13901\u201313906 (2000).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR38","doi-asserted-by":"publisher","first-page":"1851","DOI":"10.1126\/science.281.5384.1851","volume":"281","author":"LI Bruijn","year":"1998","unstructured":"Bruijn, L. I. et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281, 1851\u20131854 (1998).","journal-title":"Science"},{"key":"BFnn823_CR39","doi-asserted-by":"publisher","first-page":"12571","DOI":"10.1073\/pnas.220417997","volume":"97","author":"JA Johnston","year":"2000","unstructured":"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\u201312576 (2000).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn823_CR40","doi-asserted-by":"publisher","first-page":"5321","DOI":"10.1523\/JNEUROSCI.20-14-05321.2000","volume":"20","author":"JM Beaulieu","year":"2000","unstructured":"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\u20135328 (2000).","journal-title":"J. Neurosci."},{"key":"BFnn823_CR41","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1093\/clinchem\/16.11.903","volume":"11","author":"FW Sunderman Jr.","year":"1970","unstructured":"Sunderman, F. W. Jr. & Nomoto, S. Measurement of human serum ceruloplasmin by its p-phenylenediamine oxidase activity. Clin. Chem. 11, 903\u2013910 (1970).","journal-title":"Clin. Chem."},{"key":"BFnn823_CR42","doi-asserted-by":"publisher","first-page":"1226","DOI":"10.1093\/jn\/123.7.1226","volume":"123","author":"JR Prohaska","year":"1993","unstructured":"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\u20131234 (1993).","journal-title":"J. Nutr."}],"container-title":["Nature Neuroscience"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nn823.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nn823","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nn823.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T20:02:48Z","timestamp":1684440168000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nn823"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,3,11]]},"references-count":42,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2002,4]]}},"alternative-id":["BFnn823"],"URL":"https:\/\/doi.org\/10.1038\/nn823","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1004980.58208","asserted-by":"object"}]},"ISSN":["1097-6256","1546-1726"],"issn-type":[{"value":"1097-6256","type":"print"},{"value":"1546-1726","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,3,11]]}}}