{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T02:52:10Z","timestamp":1790477530457,"version":"4.1.0"},"reference-count":92,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[1999,9,1]],"date-time":"1999-09-01T00:00:00Z","timestamp":936144000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Experimental Neurology"],"published-print":{"date-parts":[[1999,9]]},"DOI":"10.1006\/exnr.1999.7142","type":"journal-article","created":{"date-parts":[[2002,10,6]],"date-time":"2002-10-06T23:00:46Z","timestamp":1033945246000},"page":"204-216","source":"Crossref","is-referenced-by-count":51,"title":["Therapeutic Benefits of Putrescine-Modified Catalase in a Transgenic Mouse Model of Familial Amyotrophic Lateral Sclerosis"],"prefix":"10.1006","volume":"159","author":[{"given":"Monica M.","family":"Reinholz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolin M.","family":"Merkle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph F.","family":"Poduslo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1006\/exnr.1999.7142_RF1","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1080\/01616412.1997.11740784","article-title":"Upregulation of protein-tyrosine nitration in the anterior horn cells of amyotrophic lateral sclerosis","volume":"19","author":"Abe","year":"1997","journal-title":"Neurol. Res."},{"key":"10.1006\/exnr.1999.7142_RF2","series-title":"The Handbook of Oxidative Metabolism, 2.1\u20132.5, 3.1\u20133.2, 4.1\u20134.7, 5.1\u20135.13","author":"Acworth","year":"1995"},{"key":"10.1006\/exnr.1999.7142_RF3","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1038\/bjc.1957.39","article-title":"The effect of the degree of homogenization on the catalase activity of liver \u201chomogenates.\u201d","volume":"11","author":"Adams","year":"1957","journal-title":"Br. J. Cancer"},{"key":"10.1006\/exnr.1999.7142_RF4","first-page":"15.1.1","article-title":"Standard procedures and optimization","volume":"2","author":"Ausbel","year":"1997","journal-title":"Curr. Protocol. Mol. Biol."},{"key":"10.1006\/exnr.1999.7142_RF5","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1002\/ana.410420416","article-title":"Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis","volume":"42","author":"Beal","year":"1997","journal-title":"Ann. Neurol."},{"key":"10.1006\/exnr.1999.7142_RF6","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1073\/pnas.87.4.1620","article-title":"Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide","volume":"87","author":"Beckman","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF7","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/364584a0","article-title":"ALS, SOD and peroxynitrite","volume":"364","author":"Beckman","year":"1993","journal-title":"Nature"},{"key":"10.1006\/exnr.1999.7142_RF8","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/0003-9861(92)90432-V","article-title":"Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite","volume":"298","author":"Beckman","year":"1992","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1006\/exnr.1999.7142_RF9","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1056\/NEJM199403033300901","article-title":"A controlled study trial of riluzole in amyotrophic lateral sclerosis","volume":"330","author":"Benison","year":"1994","journal-title":"N. Engl. J. Med."},{"key":"10.1006\/exnr.1999.7142_RF10","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1073\/pnas.94.14.7606","volume":"94","author":"Bruijn","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF11","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/0092-8674(95)90346-1","article-title":"Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice","volume":"80","author":"Brown","year":"1995","journal-title":"Cell"},{"key":"10.1006\/exnr.1999.7142_RF12","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/0959-4388(95)80114-6","article-title":"Superoxide dismutase in familial amyotrophic lateral sclerosis: Models for gain of function","volume":"5","author":"Brown","year":"1995","journal-title":"Curr. Opin. Neurobiol."},{"key":"10.1006\/exnr.1999.7142_RF13","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1042\/bj0460402","article-title":"The enzyme-substrate compounds of bacterial catalase and peroxides","volume":"46","author":"Chance","year":"1950","journal-title":"Biochem. J."},{"key":"10.1006\/exnr.1999.7142_RF14","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1016\/S0076-6879(55)02300-8","article-title":"Assay of catalases and peroxidases","volume":"2","author":"Chance","year":"1955","journal-title":"Methods Enzymol."},{"key":"10.1006\/exnr.1999.7142_RF15","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1006\/mcne.1995.1027","article-title":"Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis","volume":"6","author":"Chiu","year":"1995","journal-title":"Mol. Cell. Neurosci."},{"key":"10.1006\/exnr.1999.7142_RF16","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/0003-2697(70)90083-7","article-title":"Measurement of catalase activity in tissue extracts","volume":"34","author":"Cohen","year":"1970","journal-title":"Anal. Biochem."},{"key":"10.1006\/exnr.1999.7142_RF17","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1126\/science.7901908","article-title":"Oxidative stress, glutamate, and neurodegenerative disorders","volume":"262","author":"Coyle","year":"1993","journal-title":"Science"},{"key":"10.1006\/exnr.1999.7142_RF18","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1046\/j.1471-4159.1997.69051936.x","article-title":"Decreased zinc affinity of amyotrophic lateral sclerosis associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite","volume":"69","author":"Crow","year":"1997","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF19","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1046\/j.1471-4159.1997.69051945.x","article-title":"Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L","volume":"69","author":"Crow","year":"1997","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF20","first-page":"332","article-title":"Comparison of pathological alterations in ALS and a murine transgenic model: Pathogenetic implications","volume":"3","author":"Dal Canto","year":"1996","journal-title":"Clin. Neurosci."},{"key":"10.1006\/exnr.1999.7142_RF21","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1007\/s004010050650","article-title":"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","volume":"93","author":"Dal Canto","year":"1997","journal-title":"Acta Neuropathol."},{"key":"10.1006\/exnr.1999.7142_RF22","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0006-8993(95)00063-V","article-title":"Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice over-expressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS)","volume":"676","author":"Dal Cantro","year":"1995","journal-title":"Brain Res."},{"key":"10.1006\/exnr.1999.7142_RF23","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1126\/science.8351519","article-title":"Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase","volume":"261","author":"Deng","year":"1993","journal-title":"Science"},{"key":"10.1006\/exnr.1999.7142_RF24","doi-asserted-by":"crossref","first-page":"9434","DOI":"10.1073\/pnas.94.17.9434","article-title":"Carboxyfullereness as neuroprotective agents","volume":"94","author":"Dugan","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF25","series-title":"Human Motor Neuron Diseases","first-page":"139","article-title":"Familial motor neuron diseases","author":"Emery","year":"1982"},{"key":"10.1006\/exnr.1999.7142_RF26","first-page":"239","article-title":"Cu,Zn-superoxide dismutase transgenic mice in the study of the role of oxidative stress in neurodegenerative disorders","author":"Epstein","year":"1994","journal-title":"Neurodegenerative Disease"},{"key":"10.1006\/exnr.1999.7142_RF27","doi-asserted-by":"crossref","first-page":"2064","DOI":"10.1046\/j.1471-4159.1997.69052064.x","article-title":"Evidence for increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis","volume":"69","author":"Ferrante","year":"1997","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF28","doi-asserted-by":"crossref","first-page":"S67","DOI":"10.1016\/S0022-510X(97)00247-5","article-title":"The use of transgenic mouse models of amyotrophic lateral sclerosis in preclinical drug studies","volume":"152","author":"Gurney","year":"1997","journal-title":"J. Neurol. Sci."},{"key":"10.1006\/exnr.1999.7142_RF29","doi-asserted-by":"crossref","first-page":"S15","DOI":"10.1007\/BF03160575","article-title":"Transgenic animal models of familial amyotrophic lateral sclerosis","volume":"244","author":"Gurney","year":"1997","journal-title":"J. Neurol."},{"key":"10.1006\/exnr.1999.7142_RF30","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1002\/ana.410390203","article-title":"Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis","volume":"39","author":"Gurney","year":"1996","journal-title":"Ann. Neurol."},{"key":"10.1006\/exnr.1999.7142_RF31","first-page":"51","article-title":"Pathogenic mechanisms in familial amyotrophic lateral sclerosis due to mutation of Cu, Zn superoxide dismutase","volume":"44","author":"Gurney","year":"1996","journal-title":"Pathol. Biol."},{"key":"10.1006\/exnr.1999.7142_RF32","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1126\/science.8209258","article-title":"Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation","volume":"264","author":"Gurney","year":"1994","journal-title":"Science"},{"key":"10.1006\/exnr.1999.7142_RF33","first-page":"199","article-title":"Comparison of tribromoethanol, ketamine\/aetylpromazine, Telazol\/xylazine, pentobarbital, and methoxyflurane anesthesia in HSD: ICR mice","volume":"45","author":"Gardner","year":"1995","journal-title":"Lab. Animal Sci."},{"key":"10.1006\/exnr.1999.7142_RF34","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1002\/(SICI)1097-4547(19980701)53:1<66::AID-JNR7>3.0.CO;2-H","article-title":"Relationship of oxygen radical-induced lipid peroxidative damage to disease onset and progression in a transgenic model of familial ALS","volume":"53","author":"Hall","year":"1998","journal-title":"J. Neurosci. Res."},{"key":"10.1006\/exnr.1999.7142_RF35","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1111\/j.1460-9568.1997.tb01511.x","article-title":"The copper chelator d-Penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis","volume":"9","author":"Hottinger","year":"1997","journal-title":"Eur. J. Neurosci."},{"key":"10.1006\/exnr.1999.7142_RF36","doi-asserted-by":"crossref","first-page":"195","DOI":"10.3109\/10715769309145868","article-title":"The reaction of NO with superoxide","volume":"18","author":"Huie","year":"1993","journal-title":"Free Radical Res. Commun."},{"key":"10.1006\/exnr.1999.7142_RF37","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/0304-3940(94)90213-5","article-title":"Iron, selenium, and glutathione peroxidase activity are elevated in sporadic motor neuron disease","volume":"82","author":"Ince","year":"1994","journal-title":"Neurosci. Lett."},{"key":"10.1006\/exnr.1999.7142_RF38","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/0003-2697(88)90554-4","article-title":"Spectrophotometric method for determination of catalase activity in small tissue samples","volume":"174","author":"Johansson","year":"1988","journal-title":"Anal. Biochem."},{"key":"10.1006\/exnr.1999.7142_RF39","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1161\/01.RES.54.3.277","article-title":"Canine myocardial reperfusion injury: Its reduction by the combined administration of superoxide dismutase and catalase","volume":"54","author":"Jolly","year":"1984","journal-title":"Circ. Res."},{"key":"10.1006\/exnr.1999.7142_RF40","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1016\/0140-6736(93)92905-9","article-title":"Cu\/Zn superoxide dismutase (SOD1) mutations and sporadic amyotrophic lateral sclerosis","volume":"342","author":"Jones","year":"1993","journal-title":"Lancet."},{"key":"10.1006\/exnr.1999.7142_RF41","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/0014-4800(92)90031-6","article-title":"Neurotoxicity of dichlorvos: Effect on antioxidant defense system in the rat central nervous system","volume":"56","author":"Julka","year":"1992","journal-title":"Exp. Mol. Pathol."},{"key":"10.1006\/exnr.1999.7142_RF42","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1126\/science.8235659","article-title":"Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species","volume":"262","author":"Kane","year":"1993","journal-title":"Science"},{"key":"10.1006\/exnr.1999.7142_RF43","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/S1016-8478(23)13272-9","article-title":"Peroxidative activity of human Cu, Zn-superoxide dismutase","volume":"7","author":"Kim","year":"1997","journal-title":"Mol. Cells"},{"key":"10.1006\/exnr.1999.7142_RF44","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1126\/science.277.5325.559","article-title":"Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis","volume":"277","author":"Kostic","year":"1997","journal-title":"Science"},{"key":"10.1006\/exnr.1999.7142_RF45","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1016\/S0140-6736(96)91680-3","article-title":"Dose-ranging study of riluzole in amyotrophic lateral sclerosis","volume":"347","author":"Lacomblez","year":"1996","journal-title":"Lancet"},{"key":"10.1006\/exnr.1999.7142_RF46","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1006\/abbi.1997.0298","article-title":"Superoxide-dependent peroxidase activity of H48Q: Oxide dismutase variant associated with amyotrophic lateral sclerosis","volume":"346","author":"Liochev","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1006\/exnr.1999.7142_RF47","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/BF02736837","article-title":"The roles of free radicals in amyotrophic lateral sclerosis","volume":"7","author":"Liu","year":"1996","journal-title":"J. Mol. Neurosci."},{"key":"10.1006\/exnr.1999.7142_RF48","first-page":"H589","article-title":"Polyethylene glycol-conjugated superoxide dismutase and catalase reduce ischemic brain injury","volume":"256","author":"Liu","year":"1989","journal-title":"Am. J. Physiol."},{"key":"10.1006\/exnr.1999.7142_RF49","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/S0165-6147(97)01062-6","article-title":"Therapeutic advances in amyotrophic lateral sclerosis","volume":"18","author":"Louvel","year":"1997","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1006\/exnr.1999.7142_RF50","first-page":"1955","article-title":"Copper- and zinc-containing superoxide dismutase, manganese-containing superoxide dismutase, catalase, and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues","volume":"42","author":"Markland","year":"1982","journal-title":"Cancer Res."},{"key":"10.1006\/exnr.1999.7142_RF51","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/0014-2999(93)90037-I","article-title":"The neuroprotective agent riluzole inhibits release of glutamate and aspartate from slices of hippocampal area CA1","volume":"250","author":"Martin","year":"1993","journal-title":"Eur. J. Pharmacol."},{"key":"10.1006\/exnr.1999.7142_RF52","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1126\/science.8209242","article-title":"Mouse model found for ALS","volume":"264","author":"Marx","year":"1994","journal-title":"Science"},{"key":"10.1006\/exnr.1999.7142_RF53","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1046\/j.1471-4159.1997.69010021.x","article-title":"Effects of wild-type and mutated copper\/zinc superoxide dismutase on neuronal survival and L-DOPA-induced toxicity in postnatal midbrain culture","volume":"69","author":"Mena","year":"1997","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF54","doi-asserted-by":"crossref","first-page":"S86","DOI":"10.1212\/WNL.47.4_Suppl_2.86S","article-title":"Clinical trials of riluzole in patients with amyotrophic lateral sclerosis (ALS)","volume":"47","author":"Miller","year":"1996","journal-title":"Neurology"},{"key":"10.1006\/exnr.1999.7142_RF55","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1006\/bbrc.1993.1599","article-title":"Nitric oxide synthase: Involvement of oxygen radicals in conversion of l-arginine to nitric oxide","volume":"193","author":"Mittal","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1006\/exnr.1999.7142_RF56","series-title":"Human Motor Neuron Diseases","first-page":"15","article-title":"Clinical limits of amyotrophic lateral sclerosis","author":"Mulder","year":"1982"},{"key":"10.1006\/exnr.1999.7142_RF57","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1212\/WNL.36.4.511","article-title":"Familial adult motor neuron disease","volume":"36","author":"Mulder","year":"1986","journal-title":"Neurology"},{"key":"10.1006\/exnr.1999.7142_RF58","first-page":"915","article-title":"Enhancement of recovery of myocardial function by oxygen free-radical scavengers after reversible regional ischemia","volume":"4","author":"Myers","year":"1985","journal-title":"Lab. Invest."},{"key":"10.1006\/exnr.1999.7142_RF59","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/0166-2236(93)90070-3","article-title":"A radical hypothesis for neurodegeneration","volume":"16","author":"Olanow","year":"1993","journal-title":"Trends Neurosci."},{"key":"10.1006\/exnr.1999.7142_RF60","first-page":"189","article-title":"Efficacy of tribromoethanol anesthesia in mice","volume":"43","author":"Papaioannou","year":"1993","journal-title":"Lab. Animal Sci."},{"key":"10.1006\/exnr.1999.7142_RF61","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1093\/infdis\/166.6.1442","article-title":"Effect of catalase on regional cerebral blood flow and brain edema during the early phase of experimental pneumococcal meningitis","volume":"166","author":"Pfister","year":"1992","journal-title":"J. Infect. Dis."},{"key":"10.1006\/exnr.1999.7142_RF62","doi-asserted-by":"crossref","first-page":"2218","DOI":"10.1073\/pnas.89.6.2218","article-title":"Increased permeability across the blood\u2013nerve barrier of albumin glycated in vitro and in vivo from patients with diabetic polyneuropathy","volume":"89","author":"Poduslo","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF63","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/0169-328X(94)90222-4","article-title":"Glycation increases the permeability of proteins across the blood nerve and blood brain barriers","volume":"23","author":"Poduslo","year":"1994","journal-title":"Mol. Brain Res."},{"key":"10.1006\/exnr.1999.7142_RF64","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1046\/j.1471-4159.1996.66041599.x","article-title":"Polyamine modification increases the permeability of proteins at the blood\u2013nerve and blood\u2013brain barriers","volume":"66","author":"Poduslo","year":"1996","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF65","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1046\/j.1471-4159.1996.67020734.x","article-title":"Increased permeability of superoxide dismutase at the blood\u2013nerve and blood\u2013brain barriers with retained enzymatic activity after covalent modification with the naturally occurring polyamine, putrescine","volume":"67","author":"Poduslo","year":"1996","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF66","doi-asserted-by":"crossref","first-page":"5705","DOI":"10.1073\/pnas.91.12.5705","article-title":"Macromolecular permeability across the blood\u2013nerve and blood\u2013brain barriers","volume":"9","author":"Poduslo","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF67","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1046\/j.1471-4159.1998.71041651.x","article-title":"Putrescine-modified nerve growth factor: Bioactivity, plasma pharmacokinetics, blood\u2013brain\/nerve barrier permeability, and nervous system biodistribution","volume":"71","author":"Poduslo","year":"1998","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF68","doi-asserted-by":"crossref","first-page":"1760","DOI":"10.1111\/j.1471-4159.1992.tb10051.x","article-title":"Superoxide dismutase activities, catalase, and glutathione peroxidase activities in copper\/zinc-superoxide dismutase transgenic mice","volume":"58","author":"Przedborski","year":"1992","journal-title":"J. Neurochem."},{"key":"10.1006\/exnr.1999.7142_RF69","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1523\/JNEUROSCI.12-05-01658.1992","article-title":"Transgenic mice with increased Cu\/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropy-ridine-induced neurotoxicity","volume":"12","author":"Pryzedborski","year":"1992","journal-title":"J. Neurosci."},{"key":"10.1006\/exnr.1999.7142_RF70","doi-asserted-by":"crossref","unstructured":"Reinholz, M. M., J. J. Haggard, G. L. Curran, and J. F. Poduslo. 1999. Plasma pharmacokinetics, nervous system biodistribution and biostability, and spinal cord permeability at the blood\u2013brain barrier of putrescine-modified catalase in the adult rat. Exp. Neurol.159: 191\u2013203.","DOI":"10.1006\/exnr.1999.7117"},{"key":"10.1006\/exnr.1999.7142_RF71","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1073\/pnas.92.3.689","article-title":"Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis","volume":"92","author":"Ripps","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF72","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"362","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"10.1006\/exnr.1999.7142_RF73","first-page":"348","article-title":"Excitotoxicity and neurodegeneration in amyotrophic lateral sclerosis","volume":"3","author":"Rothstein","year":"1996","journal-title":"Clin. Neurosci."},{"key":"10.1006\/exnr.1999.7142_RF74","doi-asserted-by":"crossref","first-page":"S19","DOI":"10.1212\/WNL.47.4_Suppl_2.19S","article-title":"Excitotoxicity hypothesis","volume":"47","author":"Rothstein","year":"1996","journal-title":"Neurology"},{"key":"10.1006\/exnr.1999.7142_RF75","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1021\/tx960037q","article-title":"Nitric oxide regulation of tissue free radical injury","volume":"9","author":"Rubbo","year":"1996","journal-title":"Chem. Res. Toxicol."},{"key":"10.1006\/exnr.1999.7142_RF76","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1016\/S0960-9822(00)00237-2","article-title":"Oxidative stress and motor neuron disease","volume":"4","author":"Sendtner","year":"1994","journal-title":"Curr. Biol."},{"key":"10.1006\/exnr.1999.7142_RF77","first-page":"219","article-title":"Familial amyotrophic lateral sclerosis","volume":"49","author":"Siddique","year":"1997","journal-title":"J. Neural Trans."},{"key":"10.1006\/exnr.1999.7142_RF78","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/0003-2697(85)90442-7","article-title":"Measurement of protein using bicinchoninic acid","volume":"150","author":"Smith","year":"1985","journal-title":"Anal. Biochem."},{"key":"10.1006\/exnr.1999.7142_RF79","first-page":"441","article-title":"Oxidative stress, mutant SOD1, and neurofilament pathology in transgenic mouse models of human motor neuron disease","volume":"76","author":"Tu","year":"1997","journal-title":"Lab. Invest."},{"key":"10.1006\/exnr.1999.7142_RF80","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1111\/j.1365-2990.1995.tb01096.x","article-title":"Apoptosis in amyotrophic lateral sclerosis is not restricted to motor neurons. Bcl-2 expression is increased in unaffected post-central gyrus","volume":"21","author":"Troost","year":"1995","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1006\/exnr.1999.7142_RF81","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1007\/BF00967704","article-title":"Superoxide dismutase, catalase, and U7851F attenuate neuronal damage in gerbils with repeated brief ischemic insults","volume":"19","author":"Truelove","year":"1994","journal-title":"Neurochem. Res."},{"key":"10.1006\/exnr.1999.7142_RF82","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/S0006-8993(97)00565-9","article-title":"Putrescine-modified catalase with preserved enzymatic activity exhibits increased permeability at the blood\u2013nerve and blood\u2013brain barriers","volume":"767","author":"Wengenack","year":"1997","journal-title":"Brain Res."},{"key":"10.1006\/exnr.1999.7142_RF83","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/S0006-8993(97)00041-3","article-title":"Postischemic, systemic administration of polyamine-modified superoxide dismutase reduces hippocampal CA1 neurodegeneration in rat global cerebral ischemia","volume":"754","author":"Wengenack","year":"1997","journal-title":"Brain Res."},{"key":"10.1006\/exnr.1999.7142_RF84","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1126\/science.271.5248.515","article-title":"Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis","volume":"271","author":"Wiedau-Pazos","year":"1996","journal-title":"Science"},{"key":"10.1006\/exnr.1999.7142_RF85","first-page":"44","article-title":"Pharmacotherapeutic options in the treatment of amyotrophic lateral sclerosis","volume":"33","author":"White","year":"1998","journal-title":"Hospital Formulary"},{"key":"10.1006\/exnr.1999.7142_RF86","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1016\/0896-6273(95)90259-7","article-title":"An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria","volume":"14","author":"Wong","year":"1995","journal-title":"Neuron"},{"key":"10.1006\/exnr.1999.7142_RF87","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1161\/01.STR.25.1.165","article-title":"Human copper-zinc superoxide dismutase transgenic mice are highly resistant to reperfusion injury after focal cerebral ischemia","volume":"25","author":"Yang","year":"1994","journal-title":"Stroke"},{"key":"10.1006\/exnr.1999.7142_RF88","doi-asserted-by":"crossref","first-page":"4099","DOI":"10.1016\/S0021-9258(18)53585-7","article-title":"Enzyme function of copper, zinc superoxide dismutase as a free radical generator","volume":"268","author":"Yim","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1006\/exnr.1999.7142_RF89","doi-asserted-by":"crossref","first-page":"5006","DOI":"10.1073\/pnas.87.13.5006","article-title":"Copper, zinc superoxide dismutase catalyzes hydroxyl production from hydrogen peroxide","volume":"87","author":"Yim","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF90","doi-asserted-by":"crossref","first-page":"8861","DOI":"10.1074\/jbc.272.14.8861","article-title":"A familial amyotrophic lateral sclerosis-associated A4V Cu,Zn-superoside dismutase mutant has a lower Km for hydrogen peroxide","volume":"272","author":"Yim","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1006\/exnr.1999.7142_RF91","doi-asserted-by":"crossref","first-page":"5709","DOI":"10.1073\/pnas.93.12.5709","article-title":"A gain-of-function of an amyotrophic lateral sclerosis-associated Cu, Zn superoxide dismutase mutation: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide","volume":"93","author":"Yim","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/exnr.1999.7142_RF92","doi-asserted-by":"crossref","first-page":"4533","DOI":"10.1073\/pnas.90.10.4533","article-title":"bcl-2 inhibits death of central neural cells induced by multiple agents","volume":"90","author":"Zhong","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Experimental Neurology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S001448869997142X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S001448869997142X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,12,2]],"date-time":"2024-12-02T23:15:01Z","timestamp":1733181301000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S001448869997142X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,9]]},"references-count":92,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1999,9]]}},"alternative-id":["S001448869997142X"],"URL":"https:\/\/doi.org\/10.1006\/exnr.1999.7142","relation":{},"ISSN":["0014-4886"],"issn-type":[{"value":"0014-4886","type":"print"}],"subject":[],"published":{"date-parts":[[1999,9]]}}}