Relevance of oxidative injury in the pathogenesis of motor neuron diseases

References

• Ghersi-Egea J-F, Perrin R, Leininger-Muller B et al. Subcellular localization of cytochrome P450, and activities of several enzymes responsible for drug metabolism in the human brain. Biochem Pharmacol 1993; 45: 647–658.
   Google Scholar
• Farrington JA, Ebert M, Land EJ, Fletcher K. Bipyridylium quaternary salts and related compounds. V. Pulse radiolysis studies of the reaction of paraquat radical with oxygen. Implications for the mode of action of bipyridyl herbicides. Biochimica et Biophysica Acta 1973; 314: 372–381.
   Google Scholar
• Lesnefsky EJ, Dauber IM, Horwitz LD. Myocardial sulfhydryl pool alterations occur during reperfusion after brief and prolonged myocardial ischemia in vivo. Circ Res 1991; 68: 605–613.
   PubMed Web of Science ®Google Scholar
• Marsala J, Sulla I, Santa M et al. Mapping of the canine lumbosacral spinal cord neurons by Nauta method at the end of the early phase of paraplegia induced by ischemia and reperfusion. Neuroscience 1991; 45: 479–494.
   Google Scholar
• Atlante A, Calissano P, Bobba A et al. Glutamate neurotoxicity, oxidative stress and mitochondria. FEBS Lett 2001; 497: 1–5.
   Google Scholar
• Perrelet D, Ferri A, MacKenzie et al. IAP family proteins delay motoneuron cell death in vivo. Eur J Neurosci 2000; 12: 2059–2067.
   PubMedGoogle Scholar
• Yim HS, Kang SO, Hah YC et al. Free radicals generated during the glycation reaction of amino acids by methylglyoxal. A model study of protein-cross-linked free radicals. J Biol Chem 1995; 270: 28228–28233.
   Google Scholar
• Mitsui A, Hirakawa T, Yodoi J. Reactive oxygen-reducing and protein-refolding activities of adult T cell leukemia-derived factor/human thioredoxin. Biochem Biophys Res Commun 1992; 186: 1220–1226.
   PubMed Web of Science ®Google Scholar
• Sies H. Oxidative stress: oxidants and antioxidants. Exp Physiol 1997; 82: 291–295.
   PubMed Web of Science ®Google Scholar
• Okado-Matsumoto A, Fridovich I. Subcellular distribution of superoxide dismutases (SOD) in rat liver, Cu/Zn SOD in mitochondria. J Biol Chem 2001; 276: 38388–38393.
   PubMed Web of Science ®Google Scholar
• Sturtz LA, Diekert K, Jensen LT et al. A fraction of yeast Cu/Zn superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria: a physiological role for SOD1 in guarding against mitochondrial oxidative damage. J Biol Chem 2001; 276: 38084–38089.
   Google Scholar
• Epstein AC, Gleadle JM, McNeill LA et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001; 107: 43–54.
   Google Scholar
• Li PF, Fang YZ, Lu X. Oxidative modification of bovine erythrocyte superoxide dismutase by hydrogen peroxide and ascorbate -Fe(III). Biochem Mol Biol Int 1993; 29: 929–937.
   Google Scholar
• Levine RL. Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue. J Biol Chem 1983; 258: 11823–11827.
   Google Scholar
• Roy J, Minotti S, Dong L et al. Glutamate potentiates the toxicity of mutant Cu/Zn superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms. J Neurosci 1998; 18: 9673–9684.
   Google Scholar
• Simpson EP, Mosier D, Appel SH. Mechanisms of disease pathogenesis in amyotrophic lateral sclerosis. A central role for calcium. Adv Neurol 2002; 88: 1–19.
   PubMedGoogle Scholar
• Philbert MA, Beiswanger CM, Waters DK et al. Cellular and regional distribution of reduced glutathione in the nervous system of the rat: Histochemical localization by mercury orange and o-Phthaldialdehyde-induced histofluorescence. Toxicol Appl Pharmacol 1991; 107: 215–227.
   Google Scholar
• Oosthuyse B, Moons L, Storkebaum E et al. Deletion of the hypoxia-response element in the vascular endothelial growth factor promoter causes motor neuron degeneration. [see comments]. Nature Genet 2001; 28: 131–138.
   Google Scholar
• Rosen DR, Siddique T, Patterson D et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyo- trophic lateral sclerosis. Nature 1993; 362: 59–62.
   Google Scholar
• Goto JJ, Gralla EB, Valentine JS. Reactions of hydrogen peroxide with familial amyotrophic lateral sclerosis, mutant human copper-zinc superoxide dismutases studied by pulse radiolysis. J Biol Chem 1998; 273: 30104–30109.
   PubMedGoogle Scholar
• Yim MB, Kang J-H, Yim H-S 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 1996; 93: 5709–5714.
   Google Scholar
• Kim SM, Eum WS, Kwon OB, Kang JH. The free radical- generating function of a familial amyotrophic lateral sclerosis- associated D90A Cu/Zn superoxide dismutase mutant. Biochem Molec Biol Int 1998; 46: 1191–1200.
   PubMedGoogle Scholar
• Bajaj NPS. Cyclin-dependent kinase-5 (CDK5) and amyo- trophic lateral sclerosis [Review]. Amyotrophic Lateral Sclerosis & Other Motor Neuron Disorders 2000; 1: 319–327.
   Web of Science ®Google Scholar
• Singh RJ, Karoui H, Gunther MR 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. Proc Natl Acad Sci USA 1998; 95: 6675–6680.
   Google Scholar
• Sankarapandi S, Zweier JL. Evidence against the generation of free hydroxyl radicals from the interaction of copper, zinc- superoxide dismutase and hydrogen peroxide. J Biol Chem 1999; 274: 34576–34583.
   Google Scholar
• Liochev SI, Chen LL, Hallewell RA, Fridovich I. The familial amyotrophic lateral sclerosis-associated amino acid substitu- tions E100G, G93A, and G93R do not influence the rate of inactivation of copper- and zinc-containing superoxide dis- mutase by hydrogen peroxide. Arch Biochem Biophys 1998; 352: 237–239.
   PubMed Web of Science ®Google Scholar
• Liochev SI, Fridovich I. The role of bicarbonate in peroxidations catalyzed by Cu/Zn superoxide dismutase. Free Rad Biol Med 1999; 27: 1444–1447.
   PubMed Web of Science ®Google Scholar
• Zhang H, Joseph J, Felix C, Kalyanaraman B. Bicarbonate enhances the hydroxylation, nitration, and peroxidation reac- tions catalyzed by copper, zinc superoxide dismutase: inter- mediacy of carbonate anion radical. J Biol Chem 2000; 275: 14038–14045.
   PubMed Web of Science ®Google Scholar
• Wiedau-Pazos M, Goto JJ, Rabizadeh S et al. Altered reactivity of superoxide dismutase in amyotrophic lateral sclerosis. Science 1996; 271: 515–518.
   Google Scholar
• Deng H-X, Hentati A, Tainer JA et al. Amyotrophic lateral sclerosis and structural defects in Cu/Zn superoxide dismutase. Science 1993; 261: 1047–1051.
   Google Scholar
• Lyons TJ, Liu HB, Goto JJ et al. Mutations in Cu/Zn superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein. Proc Natl Acad Sci USA 1996; 93: 12240–12244.
   Google Scholar
• Crow JP, Sampson JB, Zhuang YX et al. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J Neurochem 1997; 69: 1936–1944.
   Google Scholar
• Lyons TJ, Nersissian A, Huang HJ et al. The metal binding properties of the zinc site of yeast Cu/Zn superoxide dismutase: implications for amyotrophic lateral sclerosis. Archiv Biochem Biophys 2000; 5: 189–203.
   Google Scholar
• Borchelt DR, Lee MK, Slunt HS et al. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc Natl Acad Sci USA 1994; 91: 8292–8296.
   Google Scholar
• Carri MT, Battistoni A, Polizio F et al. Impaired copper binding by the H46R mutant of human Cu/Zn superoxide dismutase, involved in amyotrophic lateral sclerosis. FEBS Lett 1994; 356: 314–316.
   Google Scholar
• Wong PC, Pardo CA, Borchelt DR et al. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 1995; 14: 1105–1116.
   Google Scholar
• Beckman JS, Carson M, Smith CD, Koppenol WH. ALS, SOD and peroxynitrite. Nature 1993; 364: 584.
   PubMed Web of Science ®Google Scholar
• Este´vez AG, Spear N, Thompson JA et al. Nitric oxide- dependent production of cGMP supports the survival of rat embryonic motor neurons cultured with brain-derived neuro- trophic factor. J Neurosci 1998; 18: 3708–3714.
   Google Scholar
• Marklund SL, Andersen PM, Forsgren L et al. Normal binding and reactivity of copper in mutant superoxide dismutase isolated from amyotrophic lateral sclerosis patients. J Neurochem 1997; 69: 675–681.
   Google Scholar
• Williamson TL, Corson LB, Huang L et al. Toxicity of ALS- linked SOD1 mutants. Science 2000; 288: 399a–.
   Google Scholar
• Corson LB, Strain JJ, Culotta VC, Cleveland DW. Chaperone- facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked super- oxide dismutase mutants. Proc Natl Acad Sci USA 1998; 95: 6361–6366.
   PubMed Web of Science ®Google Scholar
• Wong PC, Waggoner D, Subramaniam JR et al. Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proc Natl Acad Sci USA 2000; 97: 2886–2891.
   Google Scholar
• Subramaniam JR, Lyons WE, Liu J et al. Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading. Nat Neurosci 2002; 5: 301–307.
   Google Scholar
• Liu RG, Narla RK, Kurinov I et al. Increased hydroxyl radical production and apoptosis in PC12 neuron cells expressing the gain-of-function mutant G93A SOD1 gene. Radiat Res 1999; 151: 133–141.
   Google Scholar
• Bogdanov M, Romos L, Xu Z, Beal MF. Elevated hydroxyl radical generation in vivo in an animal model of amyotrophic lateral sclerosis. J Neurochem 1998; 71: 1321–1324.
   PubMed Web of Science ®Google Scholar
• Liu R, Althaus JS, Ellerbrock MR et al. Enhanced oxygen radical production in a transgenic mouse model of familial amyotrophic lateral sclerosis. Ann Neurol 1998; 44: 763–770.
   Google Scholar
• Liu D, Wen J, Liu J, Li L. The roles of free radicals in amyotrophic lateral sclerosis: reactive oxygen species and elevated oxidation of protein, DNA, and membrane phospho- lipids. FASEB J 1999; 13: 2318–2328.
   PubMed Web of Science ®Google Scholar
• Ferrante RJ, Browne SE, Shinobu LA et al. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J Neurochem 1997; 69: 2064–2074.
   Google Scholar
• Andrus PK, Fleck TJ, Gurney ME, Hall ED. Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis. J Neurochem 1998; 71: 2041–2048.
   PubMed Web of Science ®Google Scholar
• Hall E, Anddrus P, Oostveen J et al. Relationship of oxygen radical-induced lipid peroxidative damage to disease onset and progression in a transgenic model of familial ALS. J Neurosci Res 2002; 53: 66–77.
   Google Scholar
• Warita H, Hayashi T, Murakami T et al. Oxidative damage to mitochondrial DNA in spinal motoneurons of transgenic ALS mice. Br Res 2001; Molecular Brain Research. 89: 147–152.
   Google Scholar
• Beal MF. Oxidatively modified proteins in aging and disease. Free Radic Biol Med 2002; 32: 797–803.
   PubMed Web of Science ®Google Scholar
• Xiao J, Perry G, Troncoso J, Monteiro MJ. a-calcium-calmodu- lin-dependent kinase II is associated with paired helical filaments of Alzheimer’s disease. J Neuropathol Exp Neurol 1996; 55: 954–963.
   Google Scholar
• Bowling AC, Schulz JB, Brown RH Jr, Beal MF. Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J Neurochem 1993; 61: 2322–2325.
   PubMed Web of Science ®Google Scholar
• Shaw PJ, Ince PG, Falkous G, Mantle D. Oxidative damage to protein in sporadic motor neuron disease spinal cord. Ann Neurol 1995; 38: 691–695.
   PubMed Web of Science ®Google Scholar
• Bruijn LI, Beal MF, Becher MW 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 1997; 94: 7606–7611.
   Google Scholar
• Bruijn LI, Becher MW, Lee MK et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 1997; 18: 327–338.
   Google Scholar
• Durham HD, Roy J, Dong L, Figlewicz DA. Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J Neuropathol Exp Neurol 1997; 56: 523–530.
   PubMed Web of Science ®Google Scholar
• Dugan LL, Turetsky DM, Du D et al. Carboxyfullerenes as neuroprotective agents. Proc Natl Acad Sci USA 1997; 94: 9434–9438.
   PubMed Web of Science ®Google Scholar
• Gurney ME, Cutting FB, Zhai P et al. Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann Neurol 1996; 39: 147–157.
   Google Scholar
• Klivenyi P, Ferrante RJ, Matthews RT et al. Neuroprotective effects of creatine in a transgenic animal model of amyotrophic lateral sclerosis. Nature Medicine 1999; 5: 347–350.
   Google Scholar
• Reinholz MM, Merkle CM, Poduslo JF. Therapeutic benefits of putrescine-modified catalase in transgenic mouse model of familial amyotrophic lateral sclerosis. Exp Neurol 1999; 159: 204–216.
   PubMed Web of Science ®Google Scholar
• Bruijn LI, Houseweart MK, Kato S et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 1998; 281: 1851–1854.
   Google Scholar
• Doroudchi MM, Minotti S, Figlewicz DA, Durham HD. Nitrotyrosination contributes minimally to toxicity of mutant SOD1 associated with ALS. Neuroreport 2001; 12: 1239–1243.
   Google Scholar
• Ghadge GD, Lee JP, Bindokas VP et al. Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: mole- cular mechanisms of neuronal death and protection. J Neurosci 1997; 17: 8756–8766.
   Google Scholar
• Facchinetti F, Sasaki M, Cutting RB et al. Lack of involvement of neuronal nitric oxide synthase in the pathogenesis of a transgenic mouse model of familial amyotrophic lateral sclerosis. Neuroscience 1999; 90: 1483–1492.
   Google Scholar
• Upton-Rice MN, Cudkowicz ME, Mathew RK et al. Adminis- tration of nitric oxide synthase inhibitors does not alter disease course of amyotrophic lateral sclerosis SOD1 mutant transgenic mice. Ann Neurol 1999; 45: 413–414.
   Google Scholar
• Beal MF, Ferrante RJ, Browne SE et al. Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann Neurol 1997; 42: 644–654.
   Google Scholar
• Chou SM, Wang HS, Taniguchi A. Role of SOD1 and nitric oxide/cyclic GMP cascade on neurofilament aggregation in ALS/ MND. J Neurol Sci 1996; 139(suppl.): 16–26.
   Google Scholar
• Cha CI, Chung YH, Shin CM et al. Immunocytochemical study on the distribution of nitrotyrosine in the brain of the transgenic mice expressing a human Cu/Zn SOD mutation. Br Res 2000; 853: 156–161.
   Google Scholar
• Dal Canto MC, Gurney ME. Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am J Pathol 1994; 145: 1271–1279.
   PubMed Web of Science ®Google Scholar
• Kong J, Xu Z. Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J Neurosci 1998; 18: 3241–3250.
   PubMed Web of Science ®Google Scholar
• Jaarsma D, Rognoni F, van Duijn W et al. Cu/Zn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations. Acta Neuropathol 2001; 102: 293–305.
   Google Scholar
• Mattiazzi M, D’Aurelio M, Gajewski CD et al. Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J Biol Chem 2002; 277: 29626–29633.
   Google Scholar
• Dal Canto MC, Gurney ME. A low expressor line of transgenic mice carrying a mutant human Cu/Zn superoxide dismutase (SOD1) gene develops pathological changes that most closely resemble those in human amyotrophic lateral sclerosis. Acta Neuropathol (Berl) 1997; 93: 537–550.
   PubMed Web of Science ®Google Scholar
• Rabizadeh S, Gralla EB, Borchelt DR et al. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc Natl Acad Sci USA 1995; 92: 3024–3028.
   Google Scholar
• Aguirre T, Van Den BL, Goetschalckx K et al. Increased sensitivity of fibroblasts from amyotrophic lateral sclerosis patients to oxidative stress. Ann Neurol 1998; 43: 452–457.
   Google Scholar
• Gabbianelli R, Ferri A, Rotilio G, Carri MT. Aberrant copper chemistry as a major mediator of oxidative stress in a human cellular model of amyotrophic lateral sclerosis. J Neurochem 2000; 73: 1175–1180.
   Google Scholar
• Lee M, Hyun DH, Halliwell B, Jenner P. Effect of over- expression of wild-type and mutant Cu/Zn superoxide dis- mutases on oxidative stress and cell death induced by hydrogen peroxide, 4-hydroxynonenal or serum deprivation: potentiation of injury by ALS-related mutant superoxide dismutases and protection by Bcl-2. J Neurochem 2001; 78: 209–220.
   PubMed Web of Science ®Google Scholar
• Oeda T, Shimohama S, Kitagawa N et al. Oxidative stress causes abnormal accumulation of familial amyotrophic lateral sclerosis-related mutant SOD1 in transgenic Caenorhabditis elegans. Hum Mol Genet 2001; 10: 2013–2023.
   Google Scholar
• Shibata N, Nagai R, Miyata S et al. Nonoxidative protein glycation is implicated in familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation. Acta Neuropathol 2000; 100: 275–284.
   Google Scholar
• Kato S, Horiuchi S, Liu J et al. Advanced glycation endproduct- modified superoxide dismutase-1 (SOD1)-positive inclusions are common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutations and transgenic mice expressing human SOD1 with a G85R mutation. Acta Neuropathol (Berl) 2000; 100: 490–505.
   Google Scholar
• Johnston JA, Dalton MJ, Gurney ME, Kopito RR. Formation of high molecular weight complexes of mutant Cu/Zn super- oxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2000; 97: 12571–12576.
   PubMed Web of Science ®Google Scholar
• Bredesen DE, Ellerby LM, Hart PJ et al. Do post-translational modifications of Cu/Zn SOD lead to sporadic amyotrophic lateral sclerosis? Ann Neurol 1997; 42: 135–137.
   Google Scholar
• Ookawara T, Kawamura N, Kitagawa Y, Taniguchi N. Site- specific and random fragmentation of Cu/Zn superoxide dismutase by glycation reaction. Implication of reactive oxygen species. J Biol Chem 1992; 267: 18505–18510.
   PubMed Web of Science ®Google Scholar
• Rakhit R, Cunningham P, Furtos-Matei A et al. Oxidation- induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis. J Biol Chem 2002; 277: 47551–47556.
   Google Scholar
• Sitte HH, Wanschitz J, Budka H, Berger ML. Autoradiography with [3H]PK11195 of spinal tract degeneration in amyotrophic lateral sclerosis. Acta Neuropathol 2001; 101: 75–78.
   PubMed Web of Science ®Google Scholar
• Pedersen WA, Weiming F, Keller JN et al. Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients. Ann Neurol 1998; 44: 819–824.
   Google Scholar
• Malaspina A, Kaushik N, De Belleroche J. Differential expres- sion of 14 genes in amyotrophic lateral sclerosis spinal cord detected using gridded cDNA arrays. Journal of Neurochemistry 2001; 77: 132–145.
   PubMed Web of Science ®Google Scholar
• Sayre LM, Smith MA, Perry G. Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr Med Chem 2001; 8: 721–738.
   PubMed Web of Science ®Google Scholar
• Stadtman ER, Levine RL. Protein oxidation. Ann N Y Acad Sci 2000; 899: 191–208.: 191–208.
   Google Scholar
• Evert BO, Wullner U, Klockgether T. Cell death in polygluta- mine diseases. Cell Tissue Res 2000; 301: 189–204.
   PubMedGoogle Scholar
• Sherman MY, Goldberg AL. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 2001; 29: 15–32.
   PubMed Web of Science ®Google Scholar
• Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001; 83: 301–310.
   PubMed Web of Science ®Google Scholar
• Urushitani M, Kurisu J, Tsukita K, Takahashi R. Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis. J Neurochem 2002; 83: 1030–1042.
   Google Scholar
• Kawamata T, Akiyama H, Yamada T, McGeer PL. Immunologic reactions in amyotrophic lateral sclerosis brain and spinal cord tissue. Am J Pathol 1992; 140: 691–707.
   PubMed Web of Science ®Google Scholar
• Alexianu ME, Kozovska M, Appel SH. Immune reactivity in a mouse model of familial ALS correlates with disease progres- sion. Neurology 2001; 57: 1282–1289.
   PubMed Web of Science ®Google Scholar
• Hall ED, Oostveen JA, Gurney ME. Relationship of microglial and astrocytic activation to disease onset and progression in a transgenic model of familial ALS. Glia 1998; 23: 249–256.
   PubMed Web of Science ®Google Scholar
• Levine JB, Kong J, Nadler M, Xu Z. Astrocytes interact intimately with degenerating motor neurons in mouse amyotrophic lateral sclerosis (ALS). Glia 1999; 28: 215–224.
   PubMed Web of Science ®Google Scholar
• Rothstein JD, Van Kammen M, Levey AI et al. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann Neurol 1995; 38: 73–84.
   Google Scholar
• Aksenova MV, Aksenov MY, Payne RM et al. Oxidation of cytosolic proteins and expression of creatine kinase BB in frontal lobe in different neurodegenerative disorders. Dement Geriatr Cogn Disord 1999; 10: 158–165.
   Google Scholar
• Ploegh HL, Dunn BM. Current Protocols in Protein Science. 2000; 14.4.16–.
   Google Scholar
• Viner RI, Williams TD, Schoneich C. Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplas- mic reticulum Ca-ATPase. Biochemistry 1999; 38: 12408–12415.
   PubMed Web of Science ®Google Scholar