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Metals, oxidative stress and neurodegenerative disorders

  • Selkoe DJ (2001) Alzheimer’s disease: genes, proteins, and therapy. Physiol Rev 81:741–766

    PubMed  CAS  Google Scholar 

  • Barnham KJ, Masters CL, Bush AI (2004) Neurodegenerative diseases and oxidative stress. Nat Rev Drug Discov 3:205–214

    Article  PubMed  CAS  Google Scholar 

  • Bush AI (2003) The metallobiology of Alzheimer′s disease. Trends Neurosci 26:207–214

    Article  PubMed  CAS  Google Scholar 

  • Sayre LM, Smith MA, Perry G (2001) Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr Med Chem 8:721–738

    PubMed  CAS  Google Scholar 

  • Varadarajan S, Yatin S, Aksenova M, Butterfield DA (2000) Review: Alzheimer’s amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol 130:184–208

    Article  PubMed  CAS  Google Scholar 

  • Lee HG, Zhu XW, Castellani RJ, Nunomura A, Perry G, Smith MA (2007) Amyloid-beta in Alzheimer disease: the null versus the alternate hypotheses. J Pharmacol Exp Ther 321:823–829

    Article  PubMed  CAS  Google Scholar 

  • Pimplikar SW (2009) Reassessing the amyloid cascade hypothesis of Alzheimer′s disease. Int J Biochem Cell Biol 41:1261–1268

    Article  PubMed  CAS  Google Scholar 

  • Devi L, Anandatheerthavarada HK (2010) Mitochondrial trafficking of APP and alpha synuclein: relevance to mitochondrial dysfunction in Alzheimer′s and Parkinson′s diseases. Biochim Biophys Acta 1802:11–19

    PubMed  CAS  Google Scholar 

  • Tillement JP, Lecanu L, Papadopoulos V (2010) Amyloidosis and neurodegenerative diseases: current treatments and new pharmacological options. Pharmacology 85:1–17

    Article  PubMed  CAS  Google Scholar 

  • Block ML, Calderon-Garciduenas L (2009) Air pollution: mechanisms of neuroinflammation and CNS disease. Trends Neurosci 32:506–516

    Article  PubMed  CAS  Google Scholar 

  • Bush AI, Curtain CC (2008) Twenty years of metallo-neurobiology: where to now? Eur Biophys J Biophys Lett 37:241–245

    CAS  Google Scholar 

  • Jenner P, Olanow CW (1998) Understanding cell death in Parkinson′s disease. Ann Neurol 44:S72–S84

    PubMed  CAS  Google Scholar 

  • Dawson TM, Dawson VL (2003) Molecular pathways of neurodegeneration in Parkinson’s disease. Science 302:819–822

    Article  PubMed  CAS  Google Scholar 

  • Cadenas E, Davies KJA (2000) Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29:222–230

    Article  PubMed  CAS  Google Scholar 

  • Halliwell B, Gutteridge JMC (2007) Free radicals in biology and medicine, 4th edn. Oxford University Press, Oxford

    Google Scholar 

  • Liochev SI, Fridovich I (1994) The role of O2 in the production of HO: in vitro and in vivo. Free Radic Biol Med 16:29–33

    Article  PubMed  CAS  Google Scholar 

  • Valko M, Izakovic M, Mazur M, Rhodes CJ, Telser J (2004) Role of oxygen radicals in DNA damage and cancer incidence. Mol Cell Biochem 266:37–56

    Article  PubMed  CAS  Google Scholar 

  • Valko M, Leibfritz D, Moncol J, Cronin MTD, Mazur M, Telser J (2007) Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 39:44–84

    Article  PubMed  CAS  Google Scholar 

  • Ghafourifar P, Cadenas E (2005) Mitochondrial nitric oxide synthase. Trends Pharmacol Sci 26:190–195

    Article  PubMed  CAS  Google Scholar 

  • Denninger JW, Marletta MA (1999) Guanylate cyclase and the (NO)-N-/cGMP signaling pathway. Biochim Biophys Acta 1411:334–350

    Article  PubMed  CAS  Google Scholar 

  • Braak H, Braak E (1991) Neuropathological staging of Alzheimer-related changes. Acta Neuropathol 82:239–259

    Article  PubMed  CAS  Google Scholar 

  • Hardy J, Selkoe DJ (2002) Medicine—the amyloid hypothesis of Alzheimer′s disease: progress and problems on the road to therapeutics. Science 297:353–356

    Article  PubMed  CAS  Google Scholar 

  • Valko M, Morris H, Cronin MTD (2005) Metals, toxicity and oxidative stress. Curr Med Chem 11:1161–1208

    Article  Google Scholar 

  • Rajendran R, Ren MQ, Ynsa MD et al (2009) A novel approach to the identification and quantitative elemental analysis of amyloid deposits-insights into the pathology of Alzheimer’s disease. Biochem Biophys Res Commun 382:91–95

    Article  PubMed  CAS  Google Scholar 

  • Atwood CS, Moir RD, Huang XD et al (1998) Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis. J Biol Chem 273:12817–12826

    Article  PubMed  CAS  Google Scholar 

  • Chafekar SM, Hoozemans JJM, Zwart R et al (2007) Abeta (1–42) induces mild endoplasmic reticulum stress in an aggregation state-dependent manner. Antioxid Redox Signal 9:2245–2254

    Article  PubMed  CAS  Google Scholar 

  • Hung YH, Bush AI, Cherny RA (2010) Copper in the brain and Alzheimer’s disease. J Biol Inorg Chem 15:61–76

    Article  PubMed  CAS  Google Scholar 

  • Cuanjungco MP, Goldstein LE, Nunomura A et al (2000) Evidence that the beta-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of A beta by zinc. J Biol Chem 275:19439–19442

    Google Scholar 

  • Halliwell B (2001) Role of free radicals in the neurodegenerative diseases—therapeutic implications for antioxidant treatment. Drugs Aging 18:685–716

    Article  PubMed  CAS  Google Scholar 

  • Premkumar DR, Smith MA, Richey PL, Petersen RB, Castellani R, Kutty RK, Wiggert B, Perry G, Kalaria RN (1995) Induction of heme oxygenase-1 messenger-RNA and protein in neocortex and cerebral vessels in Alzheimer’s-disease. J Neurochem 65:1399–1402

    Article  PubMed  CAS  Google Scholar 

  • Nunomura A, Perry G, Zhang J, Montine TJ, Takeda A, Chiba S, Smith MA (1999) RNA oxidation in Alzheimer and Parkinson diseases. J Anti-Aging Med 2:227–230

    CAS  Google Scholar 

  • Huang XD, Cuajungco MP, Atwood CS et al (1999) Cu(II) potentiation of Alzheimer abeta neurotoxicity—correlation with cell-free hydrogen peroxide production and metal reduction. J Biol Chem 274:37111–37116

    Article  PubMed  CAS  Google Scholar 

  • Cerpa WF, Barria MI, Chacon MA, Suazo M, Gonzalez M, Opazo C, Bush AI, Inestrosa NC (2004) The N-terminal copper-binding domain of the amyloid precursor protein protects against Cu2+ neurotoxicity in vivo. FASEB J 18:1701

    PubMed  CAS  Google Scholar 

  • Pogocki D (2003) Alzheimer’s beta-amyloid peptide as a source of neurotoxic free radicals: the role of structural effects. Acta Neurobiol Exp 63:131–145

    Google Scholar 

  • Schoneich C, Pogocki D, Hug GL, Bobrowski K (2003) Free radical reactions of methionine in peptides: mechanisms relevant to beta-amyloid oxidation and Alzheimer’s disease. J Am Chem Soc 125:13700–13713

    Article  PubMed  CAS  Google Scholar 

  • da Silva GF, Lykourinou V, Angerhofer A, Ming LJ (2009) Methionine does not reduce Cu(II)-beta-amyloid!—rectification of the roles of methionine-35 and reducing agents in metal-centered oxidation chemistry of Cu(II)-beta-amyloid. Biochim Biophys Acta 1792:49–55

    PubMed  Google Scholar 

  • Hider RC, Ma Y, Molina-Holgado F et al (2008) Iron chelation as a potential therapy for neurodegenerative disease. Biochem Soc Trans 36:1304–1308

    Article  PubMed  CAS  Google Scholar 

  • Bush AI (2008) Drug development based on the metals hypothesis of Alzheimer’s disease. J Alzheimers Dis 15:223–240

    PubMed  CAS  Google Scholar 

  • Smith DG, Cappai R, Barnham KJ (2007) The redox chemistry of the Alzheimer’s disease amyloid beta peptide. Biochim Biophys Acta 1768:1976–1990

    Article  PubMed  CAS  Google Scholar 

  • White AR, Du T, Laughton KM, Volitakis I et al (2006) Degradation of the Alzheimer disease amyloid beta-peptide by metal-dependent up-regulation of metalloprotease activity. J Biol Chem 281:17670–17680

    Article  PubMed  CAS  Google Scholar 

  • Crouch PJ, Tew DJ, Du T et al (2009) Restored degradation of the Alzheimer’s amyloid-beta peptide by targeting amyloid formation. J Neurochem 108:1198–1207

    Article  PubMed  CAS  Google Scholar 

  • Ritchie CW, Bush AI, Mackinnon A (2003) Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease—a pilot phase 2 clinical trial. Arch Neurol 60:1685–1691

    Article  PubMed  Google Scholar 

  • Garai K, Sahoo B, Kaushalya SK et al (2007) Zinc lowers amyloid-beta toxicity by selectively precipitating aggregation intermediates. Biochemistry 46:10655–10663

    Article  PubMed  CAS  Google Scholar 

  • Cuajungco MP, Lees GJ (1998) Nitric oxide generators produce accumulation of chelatable zinc in hippocampal neuronal perikarya. Brain Res 799:118–129

    Article  PubMed  CAS  Google Scholar 

  • Cuajungco MP, Faget KY (2003) Zinc takes the center stage: its paradoxical role in Alzheimer’s disease. Brain Res Rev 41:44–56

    Article  PubMed  CAS  Google Scholar 

  • Ong WY, Halliwell B (2004) Iron, atherosclerosis, and neurodegeneration–a key role for cholesterol in promoting iron-dependent oxidative damage? Ann N Y Acad Sci 1012:51–64

    Article  PubMed  CAS  Google Scholar 

  • Ghribi O, Golovko MY, Larsen B et al (2006) Deposition of iron and beta-amyloid plaques is associated with cortical cellular damage in rabbits fed with long-term cholesterol-enriched diets. J Neurochem 99:438–449

    Article  PubMed  CAS  Google Scholar 

  • Kojo S (2004) Vitamin C: basic metabolism and its function as an index of oxidative stress. Curr Med Chem 11:1041–1064

    Article  PubMed  CAS  Google Scholar 

  • Carr A, Frei B (1999) Does vitamin C act as a pro-oxidant under physiological conditions? FASEB J 13:1007–1024

    PubMed  CAS  Google Scholar 

  • Kasparova S, Brezova V, Valko M et al (2005) Study of the oxidative stress in a rat model of chronic brain hypoperfusion. Neurochem Int 46:601–611

    Article  PubMed  CAS  Google Scholar 

  • Cuzzorcrea S, Thiemermann C, Salvemini D (2004) Potential therapeutic effect of antioxidant therapy in shock and inflammation. Curr Med Chem 11:1147–1162

    Google Scholar 

  • Dikalov SI, Vitek MP, Mason RP (2004) Cupric-amyloid beta peptide complex stimulates oxidation of ascorbate and generation of hydroxyl radical. Free Radic Biol Med 36:340–347

    Article  PubMed  CAS  Google Scholar 

  • Shearer J, Szalai VA (2008) The amyloid-beta peptide of Alzheimer’s disease binds Cu-I in a linear bis-his coordination environment: insight into a possible neuroprotective mechanism for the amyloid-beta peptide. J Am Chem Soc 130:17826–17835

    Article  PubMed  CAS  Google Scholar 

  • Ryglewicz D, Rodo M, Kunicki PK, Bednarska-Makaruk M et al (2002) Plasma antioxidant activity and vascular dementia. J Neurol Sci 203–204:195–197

    Article  PubMed  Google Scholar 

  • Butterfield DA, Castegna A, Pocernich ChB et al (2002) Nutritional approaches to combat oxidative stress in Alzheimer’s disease. J Nutr Biochem 13:444–461

    Article  PubMed  CAS  Google Scholar 

  • McGrath LT, McGleenon BM, Brennan S et al (2001) Increased oxidative stress in Alzheimer’s disease as assessed with 4-hydroxynonenal but not malondialdehyde. QJM 94:485–490

    Article  PubMed  CAS  Google Scholar 

  • Riviere S, Birlouez-Aragon I, Nourhashemi F (1998) Low plasma vitamin C in Alzheimer patients despite an adequate diet. Int J Geriatr Psychiatry 13:749–754

    Article  PubMed  CAS  Google Scholar 

  • Foy CJ, Passmore AP, Vahidassr MD et al (1999) Plasma chain-breaking antioxidants in Alzheimer’s disease, vascular dementia and Parkinson’s disease. QJM 92:39–45

    Article  PubMed  CAS  Google Scholar 

  • Schippling S, Kontush A, Arlt S et al (2000) Increased lipoprotein oxidation in Alzheimer’s disease. Free Radic Biol Med 28:351–360

    Article  PubMed  CAS  Google Scholar 

  • Kontush A, Mann U, Arlt S et al (2001) Influence of vitamin E and C supplementation on lipoprotein oxidation in patients with Alzheimer’s disease. Free Radic Biol Med 31:345–354

    Article  PubMed  CAS  Google Scholar 

  • Petersen RC, Thomas RG, Grundman M et al (2005) Vitamin E and donepezil for the treatment of mild cognitive impairment. N Engl J Med 352:2379–2388

    Article  PubMed  CAS  Google Scholar 

  • Kontush A, Schekatolina S (2006) Vitamin E in neurodegenerative disorders: Alzheimer’s disease. Ann N Y Acad Sci 1031:249–262

    Article  CAS  Google Scholar 

  • Azzi A, Gysin R, Kempna P, Ricciarelli R, Villacorta L, Visarius T, Zingg J-M (2003) The role of α-tocopherol in preventing disease: from epidemiology to molecular events. Mol Asp Med 24:325–336

    Article  CAS  Google Scholar 

  • Masella R, Di Benedetto R, Vari C et al (2005) Novel mechanisms of natural antioxidant compounds in biological systems: involvement of glutathione and glutathione-related enzymes. J Nutr Biochem 16:577–586

    Article  PubMed  CAS  Google Scholar 

  • Ji YB, Akerboom TPM, Sies H, Thomas JA (1999) S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione. Arch Biochem Biophys 362:67–78

    Article  PubMed  CAS  Google Scholar 

  • Karoui H, Hogg N, Frejaville C et al (1996) Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite ESR-spin trapping and oxygen uptake studies. J Biol Chem 271:6000–6009

    Article  PubMed  CAS  Google Scholar 

  • Ansari MA, Scheff SW (2010) Oxidative stress in the progression of Alzheimer disease in the frontal cortex. J Neuropathol Exp Neurol 69:155–167

    Article  PubMed  CAS  Google Scholar 

  • Packer L, Witt EH, Tritschler HJ (1995) Alfa-lipoic acid as a biological antioxidant. Free Radic Biol Med 19:227–250

    Article  PubMed  CAS  Google Scholar 

  • Smith AR, Shenvi SV, Widlansky M, Suh JH, Hagen TM (2004) Lipoic acid as a potential therapy for chronic diseases associated with oxidative stress. Curr Med Chem 11:1135–1146

    PubMed  CAS  Google Scholar 

  • Packer L, Tritschler HJ, Wessel K (1997) Neuroprotection by the metabolic antioxidant alpha-lipoic acid. Free Radic Biol Med 22:359–378

    Article  PubMed  CAS  Google Scholar 

  • Holmquist L, Stuchbury G, Berbaum K et al (2007) Lipoic acid as a novel treatment for Alzheimer′s disease and related dementias. Pharmacol Ther 113:154–164

    Article  PubMed  CAS  Google Scholar 

  • Maczurek A, Hagera K, Kenkliesa K et al (2008) Lipoic acid as an anti-inflammatory and neuroprotective treatment for Alzheimer′s disease. Adv Drug Deliv Rev 60:1463–1470

    Article  PubMed  CAS  Google Scholar 

  • Suh JH, Zhu BZ, De Szoeke E, Frei B, Hagen TM (2004) Dihydrolipoic acid lowers the redox activity of transition metal ions but does not remove them from the active site of enzymes. Redox Rep 9:57–61

    Article  PubMed  CAS  Google Scholar 

  • Cavalli A, Bolognesi ML, Minarini A et al (2008) Multi-target-directed ligands to combat at neurodegenerative diseases. J Med Chem 51:347–372

    Article  PubMed  CAS  Google Scholar 

  • Rice Evans CA, Miller NJ, Paganga G (1996) Structure-antioxidant activity relationships of flavonoids and phenolic acids. Free Radic Biol Med 20:933–956

    Article  PubMed  CAS  Google Scholar 

  • Thielecke F, Boschmann M (2009) The potential role of green tea catechins in the prevention of the metabolic syndrome–a review. Phytochemistry 70:11–24

    Article  PubMed  CAS  Google Scholar 

  • Choi YT, Jung CH, Lee SR et al (2001) The green tea polyphenol (−)-epigallocatechin gallate attenuates beta-amyloid-induced neurotoxicity in cultured hippocampal neurons. Life Sci 7:603–614

    Article  Google Scholar 

  • Guo QN, Zhao BL, Li MF, Shen SR, Xin WJ (1996) Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes. Biochim Biophys Acta 1304:210–222

    PubMed  CAS  Google Scholar 

  • Mandel S, Amit T, Reznichenko L (2006) Green tea catechins as brain-permeable, natural iron chelators-antioxidants for the treatment of neurodegenerative disorders. Mol Nutr Food Res 50:229–234

    Article  PubMed  CAS  Google Scholar 

  • Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K (2010) EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. Proc Natl Acad Sci USA 107:7710–7715

    Article  PubMed  Google Scholar 

  • Kumamoto M, Sonda T, Nagayama K et al (2001) Effects of pH and metal ions on antioxidative activities of catechins. Biosci Biotechnol Biochem 65:126–132

    Article  PubMed  CAS  Google Scholar 

  • Grinberg LN, Newmark H, Kitrossky N et al (1997) Protective effects of tea polyphenols against oxidative damage to red blood cells. Biochem Pharmacol 54:973–978

    Article  PubMed  CAS  Google Scholar 

  • Rogers JT, Randall JD, Cahill CM et al (2002) An iron-responsive element type II in the 5′-untranslated region of the Alzheimer’s amyloid precursor protein transcript. J Biol Chem 277:45518–45528

    Article  PubMed  CAS  Google Scholar 

  • Mandel SA, Amit T, Zheng H et al (2006) The essentiality of iron chelation in neuroprotection: a potential role of green tea catechins. In: Luo Y, Packer L (eds) Oxidative stress and age-related neurodegeneration. Taylor & Francis Group, Boca Raton, pp 277–299

  • Dedeoglu A, Cormier K, Payton S et al (2004) Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer’s amyloidogenesis. Exp Gerontol 39:1641–1649

    Article  PubMed  CAS  Google Scholar 

  • Hsiao K, Chapman P, Nilsen S et al (1996) Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 274:99–102

    Article  PubMed  CAS  Google Scholar 

  • Hanson ES, Rawlins ML, Leibold EA (2003) Oxygen and iron regulation of iron regulatory protein 2. J Biol Chem 278:40337–40342

    Article  PubMed  CAS  Google Scholar 

  • Wang J, Chen G, Muckenthaler M et al (2004) Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity. Mol Cell Biol 24:954–965

    Article  PubMed  CAS  Google Scholar 

  • Preetha A, Thomas SG, Kunnumakkaraa AB et al (2008) Biological activities of curcumin and its analogues (Congeners) made by man and Mother Nature. Biochem Pharmacol 76:1590–1611

    Article  CAS  Google Scholar 

  • Singhal SS, Awasthi S, Pandya U et al (1999) The effect of curcumin on glutathione-linked enzymes in K562 human leukemia cells. Toxicol Lett 109:87–95

    Article  PubMed  CAS  Google Scholar 

  • Kim DS, Park SY, Kim JK (2001) Curcuminoids from Curcuma longa L. (Zinggiveraceae) that protect PC12 rate pheochromocytoma and normal human umbilical vein endothelial cells from betaA (1–42) insult. Neurosci Lett 303:57–61

    Article  PubMed  CAS  Google Scholar 

  • Ganguli M, Chandra V, Kamboh MI (2000) Apolipoprotein E polymorphism and Alzheimer disease: the Indo-US Cross-National Dementia Study. Arch Neurol 57:824–830

    Article  PubMed  CAS  Google Scholar 

  • Lim GP, Chu T, Yang F, Beech W, Frautschy SA, Cole GM (2001) The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J Neurosci 21:8370–8377

    PubMed  CAS  Google Scholar 

  • Glenner GG, Wong CW (1984) Alzheimer’s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885–890

    Article  PubMed  CAS  Google Scholar 

  • Hardy JA, Higgins GA (1992) Alzheimer’s disease: the amyloid cascade hypothesis. Science 256:184–185

    Article  PubMed  CAS  Google Scholar 

  • Terry RD, Masliah E, Salmon DP et al (1991) Physical basis of cognitive alterations in Alzheimer’s disease: synapse loss is the major correlate of cognitive impairment. Ann Neurol 30:572–580

    Article  PubMed  CAS  Google Scholar 

  • Selkoe DJ, Wolfe MS (2007) Presenilin: running with scissors in the membrane. Cell 131:215–221

    Article  PubMed  CAS  Google Scholar 

  • Gong CX, Iqbal K (2008) Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease. Curr Med Chem 15:2321–2328

    Article  PubMed  CAS  Google Scholar 

  • Jenner P (2003) Oxidative stress in Parkinson′s disease. Ann Neurol 53:S26–S36

    Article  PubMed  CAS  Google Scholar 

  • Ebadi M, Srinivasan SK, Baxi MD (1996) Oxidative stress and antioxidant therapy in Parkinson’s disease. Prog Neurobiol 48:1–19

    Article  PubMed  CAS  Google Scholar 

  • Eriksen J, Dawson T, Dickson D, Petrucelli L (2003) Caught in the act: α-synuclein is the culprit in Parkinson’s disease. Neuron 40:453–456

    Article  PubMed  CAS  Google Scholar 

  • Gasser T (2001) Genetics of Parkinson’s disease. J Neurol 248:833–840

    Article  PubMed  CAS  Google Scholar 

  • Cooper AA, Gitler AD, Cashikar A et al (2006) Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson’s models. Science 313:324–328

    Article  PubMed  CAS  Google Scholar 

  • Winklhofer KF, Haass C (2010) Mitochondrial dysfunction in Parkinson’s disease. Biochim Biophys Acta 1802:29–44

    PubMed  CAS  Google Scholar 

  • Chinta SJ, Andersen JK (2008) Redox imbalance in Parkinson′s disease. Biochim Biophys Acta 1780:1362–1367

    PubMed  CAS  Google Scholar 

  • Kraytsberg Y, Kudryavtseva E, McKee AC et al (2006) Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nat Genet 38:518–520

    Article  PubMed  CAS  Google Scholar 

  • Bender A, Krishnan KJ, Morris CM et al (2006) High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease. Nat Genet 38:515–517

    Article  PubMed  CAS  Google Scholar 

  • Andersen JK (2004) Oxidative stress in neurodegeneration: cause or consequence? Nat Med 10:S18–S25

    Article  PubMed  Google Scholar 

  • Jenner P, Olanow CW (2006) The pathogenesis of cell death in Parkinson’s disease. Neurology 66:S24–S36

    PubMed  Google Scholar 

  • Kaur D, Yantiri F, Rajagopalan S et al (2003) Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson’s disease. Neuron 37:899–909

    Article  PubMed  CAS  Google Scholar 

  • Bogaerts V, Theuns J, van Broeckhoven C (2008) Genetic findings in Parkinson’s disease and translation into treatment: a leading role for mitochondria? Genes Brain Behav 7:129–151

    Article  PubMed  CAS  Google Scholar 

  • Henchcliffe C, Beal MF (2008) Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis. Nat Clin Pract 4:600–609

    Article  CAS  Google Scholar 

  • Paisan-Ruiz C, Jain S, Evans EW et al (2004) Cloning of the gene containing mutations that cause PARK8-linked Parkinson’s disease. Neuron 44:595–600

    Article  PubMed  CAS  Google Scholar 

  • Zimprich A, Biskup S, Leitner P et al (2004) Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 44:601–607

    Article  PubMed  CAS  Google Scholar 

  • Valente EM, Abou-Sleiman PM, Caputo V et al (2004) Hereditary early-onset Parkinson’s disease caused by mutations in PINK1. Science 304:1158–1160

    Article  PubMed  CAS  Google Scholar 

  • Gandhi S, Wood-Kaczmar A, Yao Z (2009) PINK1-associated Parkinson’s disease is caused by neuronal vulnerability to calcium-induced cell death. Mol Cell 33:627–638

    Article  PubMed  CAS  Google Scholar 

  • Moore DJ (2006) Parkin: a multifaceted ubiquitin ligase. Biochem Soc Trans 34:749–753

    Article  PubMed  CAS  Google Scholar 

  • Meulener M, Whitworth AJ, Armstrong-Gold CE et al (2005) Drosophila DJ-1 mutants are selectively sensitive to environmental toxins associated with Parkinson’s disease. Curr Biol 15:1572–1577

    Article  PubMed  CAS  Google Scholar 


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