Mitochondrial proteomics as a selective tool for unraveling Parkinsons disease pathogenesis

Expert Review of Proteomics

Volumn 7, Issue 2, 2010, Pages 205-226

  Pienaar, Ilse Sanet ^a   Dexter, David Trevor ^b   Burkhard, Pierre Roland ^c,d  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

^c UNIVERSITY OF GENEVA   (Switzerland)

^d GENEVA UNIVERSITY HOSPITALS   (Switzerland)

Author keywords

Biomarker; Mitochondrial electron transport chain; Mitochondrial function; Mitochondrial proteomics; Parkinsons disease

Indexed keywords

LEVODOPA; PROTEOME; RASAGILINE; ROTENONE; SELEGILINE; TOXIN;

CELL FUNCTION; COMPREHENSION; DISORDERS OF MITOCHONDRIAL FUNCTIONS; DYNAMICS; GENE MUTATION; GENETIC ANALYSIS; GENETICS; HUMAN; INTROSPECTION; MITOCHONDRION; NONHUMAN; PARKINSON DISEASE; PATHOGENESIS; PROTEOMICS; REVIEW; SAMPLE;

ANIMALS; HUMANS; MITOCHONDRIA; MODELS, BIOLOGICAL; PARKINSON DISEASE; PROTEOMICS;

ANIMALIA;

EID: 77950834717     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/epr.10.8     Document Type: Review

References (212)

1. De Rijk MC, Launer LJ, Berger K et al. Prevalence of Parkinson's disease in Europe: a collaborative study of population-based cohorts. Neurological diseases in the elderly research group. Neurology 54, S21-S23 (2000). (Pubitemid 30390601)
2. Marsden CD. Parkinson's disease. Lancet 335, 948-952 (1990). (Pubitemid 20134975)
3. Braak H, Del Tredici K, Rub U, de Vos RA, Jansen Steur EN, Braak E. Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol. Aging 24, 197-211 (2003). (Pubitemid 36007810)
4. Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M. a-synuclein in Lewy bodies. Nature 388, 839-840 (1997).
5. Kawaja MD. A proteomic approach to assess intraneuronal inclusions associated with neurodegenerative disorders. Curr. Opin. Mol. Ther. 7, 565-568 (2005).
6. Sas K, Robotka H, Toldi J, Vécsei, L. Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J. Neurol. Sci. 257, 221-239 (2007). (Pubitemid 46856508)
7. Elbaz A, Tranchant C. Epidemiologic studies of environmental exposures in Parkinson's disease. J. Neurol. Sci. 262, 37-44 (2007). (Pubitemid 47398893)
8. Bonifati V, Rizzu P, van Baren MJ et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299, 256-259 (2003). (Pubitemid 36131051)
9. Schapira AH. Etiology and pathogenesis of Parkinson's disease. Neurol. Clin. 27, 583-603 (2009).
10. Tanner CM, Ben-Shlomo Y. Epidemiology of Parkinson's disease. Adv. Neurol. 80, 153-159 (1999).
11. Scheffler IE. A century of mitochondrial research: achievements and perspectives. Mitochondrion 1, 3-31 (2001). (Pubitemid 33586018)
12. Chan CS, Gertler TS, Surmeier DJ. Calcium homeostasis, selective vulnerability and Parkinson's disease. Trends Neurosci. 32, 249-256 (2009).
13. Blandini F, Armentero MT, Martignoni E. The 6-hydroxydopamine model: news from the past. Parkinsonism Relat. Disord. 14(suppl. 2), S124-S129 (2008).
14. Simola N, Morelli M, Carta AR. The 6-hydroxydopamine model of Parkinson's disease. Neurotox. Res. 11, 151-167 (2007).
15. Glinka YY, Youdim MBH. Inhibition of mitochondrial complexes I and IV by 6-hydroxydopamine. Eur. J. Pharmacol. 292, 329-332 (1995).
16. Glinka YY, Tipton KF, Youdim MBH. Nature of inhibition of mitochondrial respiratory complex I by 6-hydroxydopamine. J. Neurochem. 66, 2004-2010 (1996). (Pubitemid 26118791)
17. Kumar R, Agarwal AK, Seth PK. Free radical-generated neurotoxicity of 6-hydroxydopamine. J. Neurochem. 64, 1703-1707 (1995).
18. Pezzella A, D'Ischia M, Napolitano A, Misuraca G, Prota G. Iron-mediated generation of the neurotoxin 6-hydroxydopamine quinone by reaction of fatty acid hydoperoxides with dopamine: a possible contributory mechanism for neuronal degeneration in Parkinson's disease. J. Med. Chem. 40, 2211-2216 (1997). (Pubitemid 27284359)
19. Graham DG, Tiffany SM, Bell WR Jr, Gutknecht WF. Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro. Mol. Pharmacol. 14, 644-653 (1978).
20. Gorman AM, Szegezdi E, Quigney DJ, Samali A. Hsp27 inhibits 6-hydroxydopamine-induced cytochrome C release and apoptosis in PC12 cells. Biochem. Biophys. Res. Commun. 327, 801-810 (2005). (Pubitemid 40092820)
21. Soto-Otero R, Méndez-Álvarez E, Sánchez-Iglesias S et al. Inhibition of 6-hydroxydopamine-induced oxidative damage by 4,5-dihydro-3H-2-benzazepine N-oxides. Biochem. Pharmacol. 75, 1526-1537 (2008).
22. Dauer W, Przedborski S. Parkinson's disease: mechanisms and models. Neuron 39, 889-909 (2003). (Pubitemid 37130207)
23. Przedborski S, Vila M. The 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model: a tool to explore the pathogenesis of Parkinson's disease. Ann. NY Acad. Sci. 991, 189-198 (2003). (Pubitemid 36793814)
24. Krueger MJ, Singer TP, Casida JE, Ramsay RR. Evidence that the blockade of mitochondrial respiration by the neurotoxin 1-methyl-4-phenylpyridinium (MPP+) involves binding at the same site as the respiratory inhibitor, rotenone. Biochem. Biophys. Res. Commun. 169, 123-128 (1990).
25. Chiba K, Trevor A, Castagnoli N Jr. Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine oxidase. Biochem. Biophys. Res. Commun. 120, 574-578 (1984). (Pubitemid 14101750)
26. Heikkila RE, Manzino L, Cabbat FS, Duvoisin RC. Protection against the dopaminergic neurotoxicity of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine by monoamine oxidase inhibitors. Nature 311, 467-469 (1984). (Pubitemid 14035453)
27. Nicklas WJ, Vyas I, Heikkila RE. Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. Life Sci. 36, 2503-2508 (1985). (Pubitemid 15072756)
28. Ramsay RR, Salach JI, Dadgar J, Singer TP. Inhibition of mitochondrial NADH dehydrogenase by pyridine derivatives and its possible relation to experimental and idiopathic parkinsonism. Biochem. Biophys. Res. Commun. 135, 269-275 (1986). (Pubitemid 16063998)
29. Mizuno Y, Sone N, Suzuki K, Saitoh T. Studies on the toxicity of 1-methyl-4-phenylpyridinium ion (MPP+) against mitochondria of mouse brain. J. Neurol. Sci. 86, 97-110 (1988).
30. Mizuno Y, Suzuki K, Sone N, Saitoh T. Inhibition of mitochondrial respiration by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) in mouse brain in vivo. Neurosci. Lett. 91, 349-353 (1988).
31. Hertzman C, Wiens M, Bowering D, Snow B, Calne D. Parkinson's disease: a case-control study of occupational and environmental risk factors. Am. J. Ind. Med. 17, 349-355 (1990). (Pubitemid 20155397)
32. Bonneh-Barkay D, Reaney SH, Langston WJ, Di Monte DA. Redox cycling of the herbicide paraquat in microglial cultures. Brain Res. Mol. Brain Res. 134, 52-56 (2005). (Pubitemid 40403639)
33. Ramachandiran S, Hansen JM, Jones DP, Richardson JR, Miller GW. Divergent mechanisms of paraquat, MPP+, and rotenone toxicity: oxidation of thioredoxin and caspase-3 activation. Toxicol. Sci. 95, 163-171 (2007). (Pubitemid 44970055)
34. Castello PR, Drechsel DA, Patel M. Mitochondria are a major source of paraquat-induced reactive oxygen species production in the brain. J. Biol. Chem. 282, 14186-14193 (2007). (Pubitemid 47100444)
35. Betarbet R, Sherer TB, MacKenzie G, Garcia-Osuna M, Panov AV, Greenamyre JT. Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat. Neurosci. 3, 1301-1306 (2000).
36. Alam M, Schmidt WJ. Rotenone destroys dopaminergic neurons and induces parkinsonian symptoms in rats. Behav. Brain Res. 136, 317-324 (2002). (Pubitemid 35246417)
37. Sherer TB, Kim JH, Brbet R, Greenamyre JT. Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and a-synuclein aggregation. Exp. Neurol. 179, 9-16 (2003).
38. Radad K, Rausch WD, Gille G. Rotenone induces cell death in primary dopaminergic culture by increasing ROS production and inhibiting mitochondrial respiration. Neurochem. Int. 49, 379-386 (2006). (Pubitemid 44119044)
39. Janetzky B, Hauck S, Youdim MB et al. Unaltered aconitase activity, but decreased complex I activity in substantia nigra pars compacta of patients with Parkinson's disease. Neurosci. Lett. 169, 126-128 (1994). (Pubitemid 24108879)
40. Orth M, Schapira AH. Mitochondrial involvement in Parkinson's disease. Neurochem. Int. 40, 533-541 (2002). (Pubitemid 34159154)
41. Schapira AH, Cooper JM, Dexter D, Clark JB, Jenner P, Marsden CD. Mitochondrial complex I deficiency in Parkinson's disease. J. Neurochem. 54, 823-827 (1990). (Pubitemid 20087661)
42. Keeney PM, Xie X, Capaldi RA, Bennett JP. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neuroscience 26, 5256-5264 (2006).
43. Shoffner JM, Watts RL, Juncos JL, Torroni A, Wallace DC. Mitochondrial oxidative phosphorylation defects in Parkinson's disease. Ann. Neurol. 30, 332-339 (1991).
44. Swerdlow RH, Parks JK, Cassarino DS et al. Biochemical analysis of cybrids expressing mitochondrial DNA from Contursi kindred Parkinson's subjects. Exp. Neurol. 169, 479-485 (2001).
45. Hanagasi HA, Ayribas D, Baysal K, Emre M. Mitochondrial complex I, II/III, and IV activities in familial and sporadic Parkinson's disease. Int. J. Neurosci. 115, 479-493 (2005). (Pubitemid 40460680)
46. Yoshino H, Nakagawa-Hattori Y, Kondo T, Mizuno Y. Mitochondrial complex I and II activities of lymphocytes and platelets in Parkinson's disease. J. Neural Transm. Parkinson's Dis. Dement. Sect. 4, 27-34 (1992).
47. Shinde S, Pasupathy K. Respiratory-chain enzyme activities in isolated mitochondria of lymphocytes from patients with Parkinson's disease: preliminary study. Neurol. India 54, 390-393 (2006). (Pubitemid 44870691)
48. Martin MA, Molina JA, Jimenez-Jimenez FJ et al. Respiratory-chain enzyme activities in isolated mitochondria of lymphocytes from untreated Parkinson's disease patients. Grupo-Centro de Trastornos del Movimiento. Neurology 46, 1343-1346 (1996).
49. Büeler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Exp. Neurol. 218, 235-246 (2009).
50. Sherer TB, Brbet R, Greenamyre JT. Environment, mitochondria, and Parkinson's disease. Neuroscientist 8, 192-197 (2002).
51. Beal F. Mitchondria, oxidative damage, and inflammation in Parkinson's disease. Ann. NY Acad. Sci. 991, 120-131 (2003). (Pubitemid 36793808)
52. Lenaz G, Bovina C, D'Aurelio M et al. Role of mitochondria in oxidative stress and aging. Ann. NY Acad. Sci. 959, 199-213 (2002). (Pubitemid 34457563)
53. Bulteau AL, Szweda LI, Friguet B. Mitochondrial protein oxidation and degradation in response to oxidative stress and aging. Exp. Gerontol. 41, 653-657 (2006). (Pubitemid 43866355)
54. Thyagarajan D, Bressman S, Bruno C et al. A novel mitochondrial 12SrRNA point mutation in parkinsonism, deafness, and neuropathy. Ann. Neurol. 48, 730-736 (2000).
55. Van der Walt JM, Nicodemus KK, Martin ER et al. Mitochondrial polymorphisms significantly reduce the risk of Parkinson's disease. Am. J. Hum. Genet. 72, 804-811 (2003). (Pubitemid 36403301)
56. Autere J, Moilanen JS, Finnila S et al. Mitochondrial DNA polymorphisms as risk factors for Parkinson's disease and Parkinson's disease dementia. Hum. Genet. 115, 29-35 (2004). (Pubitemid 38787215)
57. Hattori N, Yoshino H, Tanaka M, Suzuki H, Mizuno Y. Genotype in the 24-kDa subunit gene (NDUFV2) of mitochondrial complex I and susceptibility to Parkinson disease. Genomics 49, 52-58 (1998). (Pubitemid 28194436)
58. Bender A, Krishnan KJ, Morris CM et al. High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease. Nat. Genet. 38, 515-517 (2006).
59. Alvarez V, Corao AI, Sanchez-Ferrero E et al. Mitochondrial transcription factor A (TFAM) gene variation in Parkinson's disease. Neurosci. Lett. 432, 79-82 (2008). (Pubitemid 352039031)
60. Luoma PT, Eerola J, Ahola S et al. Mitochondrial DNA polymerase g variants in idiopathic sporadic Parkinson's disease. Neurology 69, 1152-1159 (2007). (Pubitemid 47517561)
61. Davidzon G, Greene P, Mancuso M et al. Early-onset familial parkinsonism due to POLG mutations. Ann. Neurol. 59, 859-862 (2006). (Pubitemid 43673164)
62. Invernezzi F, Varanese S, Thomas A, Carrara A, Onofrj M, Zeviani M. Two novel POLG1 mutations in a patient with progressive external ophthalmoplegia, levodopa-responsive pseudo-orthostatic tremor and parkinsonism. Neuromuscul. Disord. 18, 460-464 (2008).
63. Filosto M, Mancuso M, Nishigaki Y et al. Clinical and genetic heterogeneity in progressive external ophthalmoplegia due to mutations in polymerase g. Arch. Neurol. 60, 1279-1284 (2003). (Pubitemid 37099636)
64. Dodson MW, Guo M. Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease. Curr. Opin. Neurobiol. 17331-17337 (2009). (Pubitemid 46880329)
65. Valente EM, Abou-Sleiman PM, Caputo V et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304, 1158-1160 (2004). (Pubitemid 38661852)
66. Ibanez P, Lesage S, Lohmann E et al. Mutational analysis of the PINK1 gene in early-onset parkinsonism in Europe and North Africa. Brain 129, 686-694 (2006). (Pubitemid 43278230)
67. Chu CT. Tickled PINK1: mitochondrial homeostasis and autophagy in recessive Parkinsonism. Biochim. Biophys. Acta 1802, 20-28 (2010).
68. Greene JC, Whitworth AJ, Kuo I, Andrews LA, Feany MB, Pallanck LJ. Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc. Natl. Acad. Sci. USA 100, 4078-4083 (2003). (Pubitemid 36418160)
69. Clark IE, Dodson MW, Jiang C et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441, 1162-1166 (2006). (Pubitemid 43990738)
70. Palacino JJ, Sagi D, Goldberg MS et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J. Biol. Chem. 279, 18614-18622 (2004). (Pubitemid 38623283)
71. Gasser T. Update on the genetics of Parkinson's disease. Mov. Disord. 22, S343-S350 (2007). (Pubitemid 350134187)
72. Zhang L, Shimoji M, Thomas B et al. Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis. Hum. Mol. Genet. 14, 2063-2073 (2005). (Pubitemid 41418042)
73. Parker WD Jr, Parks JK. Mitochondrial ND5 mutations in idiopathic Parkinson's disease. Biochem. Biophys. Res. Commun. 326, 667-669 (2005). (Pubitemid 39642776)
74. Jones JM, Datta P, Srinivasula SM et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature 425, 721-727 (2003). (Pubitemid 37314315)
75. Martins LM. Neuroprotective role of the reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Nature 425, 721-727 (2004).
76. Strauss KM, Martins LM, Plun-Favreau H et al. Loss-of-function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease. Hum. Mol. Genet. 14, 2099-2111 (2005). (Pubitemid 41418010)
77. Simon-Sanchez J, Singleton AB. Sequencing analysis of OMI/HTRA2 shows previously reported pathogenic mutations in neurologically normal controls. Hum. Mol. Genet. 17, 1988-1993 (2008). (Pubitemid 351865847)
78. Ross OA, Soto AI, Vilarino-Guell C et al. Genetic variation of Omi/ HtrA2 and Parkinson's disease. Parkinsonism Relat. Disord. 14, 539-543 (2008).
79. Simon DK, Mayeux R, Marder K, Kowall NW, Beal MF, Johns DR. Mitochondrial DNA mutations in complex I and tRNA genes in Parkinson's disease. Neurology 54, 703-709 (2000). (Pubitemid 30082942)
80. Vives-Bauza C, Andreu AL, Manfredi G et al. Sequence analysis of the entire mitochondrial genome in Parkinson's disease. Biochem. Biophys. Res. Commun. 290, 1593-1601 (2002). (Pubitemid 34687441)
81. Soane L, Kahraman S, Kristian T, Fiskum G. Mechanisms of impaired mitochondrial energy metabolism in acute and chronic neurodegenerative disorders. J. Neurosci. Res. 85, 3407-3415 (2007). (Pubitemid 350058529)
82. Frei B, Richter C. N-methyl-4-phenylpyridine (MPP+) together with 6-hydroxydopamine or dopamine stimulates Ca2+ release from mitochondria. FEBS Lett. 198, 99-102 (1986). (Pubitemid 16055176)
83. Cassarino DS, Parks JK, Parker WD Jr, Bennett JP Jr. The parkinsonian neurotoxin MPP+ opens the mitochondrial permeability transition pore and releases cytochrome C in isolated mitochondria via an oxidative mechanism. Biochim. Biophys.Acta 1453, 49-62 (1999).
84. Packer MA, Miesel R, Murphy MP. Exposure to the parkinsonian neurotoxin 1-methyl-4-phenylpyridinium (MPP+) and nitric oxide simultaneously causes cyclosporin A-sensitive mitochondrial calcium efflux and depolarization. Biochem. Pharmacol. 51, 267-273 (1996). (Pubitemid 26054434)
85. Stavrovskaya IG, Narayanan MV, Zhang W et al. Clinically approved heterocyclics act on a mitochondrial target and reduce stroke-induced pathology. J. Exp. Med. 200, 211-222 (2004). (Pubitemid 38982180)
86. Cleren C, Starkov AA, Callingasan NY, Lorenzo BJ, Chen J, Beal MF. Promethazine protects against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxicity. Neurobiol. Dis. 20, 701-708 (2005). (Pubitemid 41619346)
87. Fontaine E, Bernardi P. Progress on the mitochondrial permeability transition pore: regulation by complex I and ubiquinone analogs. J. Bioenerg. Biomembranes 31, 335-345 (1999). (Pubitemid 30058569)
88. Lemasters JJ, Nieminen AL, Qian T et al. The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochim. Biophys. Acta 1366, 177-196 (1998). (Pubitemid 28467031)
89. Di Lisa F, Menoba R, Canton M, Barile M, Bernardi P. Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD+ and is a causative event in the death of myocytes in postischemic reperfusion of the heart. J. Biol. Chem. 27, 2571-2575 (2001). (Pubitemid 37376632)
90. Anderson MF, Sims NR. The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions. J. Neurochem. 81, 541-549 (2002).
91. Cheng EH, Sheiko TV, Fisher JK, Craigen WJ, Korsmeyer SJ. VDAC2 inhibits BAK activation and mitochondrial apoptosis. Science 301, 513-517 (2003). (Pubitemid 36900308)
92. Shoshan-Barmatz V, Israelson A, Brdiczka D, Sheu SS. The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death. Curr. Pharm. Des. 12, 2249-2270 (2006). (Pubitemid 43891398)
93. Banerjee R, Starkov AA, Beal MF, Thomas B. Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis. Biochim. Biophys. Acta 1792, 651-663 (2009).
94. Chalmers S, Nicholls DG. The relationship between free and total calcium concentrations in the matrix of liver and brain mitochondria. J. Biol. Chem. 278, 19062-19070 (2003). (Pubitemid 36799293)
95. Panov A, Dikalov S, Shalbuyeva N, Hemendinger R, Greenamyre JT, Rosenfeld J. Species-and tissue-specific relationships between mitochondrial permeability transition and generation of ROS in brain and liver mitochondria of rats and mice. Am. J. Physiol. Cell. Physiol. 292, C708-C718 (2007). (Pubitemid 46263470)
96. Frantseva MV, Carlen PL, Perez Velazquez JL. Dynamics of intracellular calcium and free radical production during ischemia in pyramidal neurons. Free Radic. Biol. Med. 3, 1216-1227 (2001).
97. Leung AW, Halestrap AP. Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore. Biochim. Biophys. Acta 1777, 946-952 (2008).
98. Johnson MD, Yu LR, Corads TP et al. The proteomics of neurodegeneration. Am. J. Pharmacogenom. 5, 259-270 (2005).
99. Moreira PI, Zhu X, Wang X et al. Mitochondria: a therapeutic target in neurodegeneration. Biochim. Biophys. Acta 1802, 212-220 (2010).
100. Pienaar IS, Daniels WMU, Götz J. Neuroproteomics as a promising tool in Parkinson's disease research. J. Neural Transm. 115, 1413-1430 (2007).
101. Lopez MF, Melov S. Applied proteomics: mitochondrial proteins and effect on function. Circ. Res. 90, 380-389 (2002). (Pubitemid 34633906)
102. Basso M, Giraudo S, Corpillo D, Bergamasco B, Lopiano L, Fasano M. Proteome analysis of human substantia nigra in Parkinson's disease. Proteomics 4, 3943-3952 (2004). (Pubitemid 39657469)
103. Trojanowski JQ, Lee VM. Aggregation of neurofilament and a-synuclein proteins in Lewy bodies: implications for the pathogenesis of Parkinson disease and Lewy body dementia. Arch. Neurol. 55, 151-152 (1998). (Pubitemid 28110056)
104. Chiasson K, Lahaie-Collins V, Bournival J, Delapierre B, Gélinas S, Martinoli M-G. Oxidative stress and 17-a-and 17-b-estradiol modulate neurofilaments differently. J. Mol. Neurosci. 30, 297-310 (2006). (Pubitemid 46568348)
105. Werner CJ, Heyny-von Haussen R, Mall G, Wolf S. Proteome analysis of human substantia nigra in Parkinson's disease. Proteome Sci. 6, 8 (2008). (Pubitemid 351385673)
106. Unschuld PG, Dächsel J, Darios F et al. Parkin modulates gene expression in control and ceramide-treated PC12 cells. Mol. Biol. Rep. 33, 13-32 (2006).
107. Davison EJ, Pennington K, Hung CC et al. Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9, 4284-4297 (2009).
108. Von Coelln R, Dawson VL, Dawson TM. Parkin-associated Parkinson's disease. Cell Tissue Res. 318, 175-184 (2004). (Pubitemid 39362637)
109. Chin MH, Qian W-J, Wang H et al. Mitochondrial dysfunction, oxidative stress, and apoptosis revealed by proteomic and transcriptomic analyses of the striata in two mouse models of Parkinson's disease. J. Prot. Res. 7, 666-667 (2008). (Pubitemid 351294029)
110. Fukae J, Mizuno Y, Hattori N. Mitochondrial dysfunction in Parkinson's disease. Mitochondrion 7, 58-62 (2007). (Pubitemid 46351976)
111. Boger HA, Middaugh LD, Patrick KS et al. Long-term consequences of methamphetamine exposure in young adults are exacerbated in glial cell line-derived neurotrophic factor heterozygous mice. J. Neurosci. 27, 8816-8825 (2007).
112. Tsuchiya K, Tajima H, Kuwae T et al. Pro-apoptotic protein glyceraldehyde-3-phosphate dehydrogenase promotes the formation of Lewy body-like inclusions. Eur. J. Neurosci. 21, 317-326 (2005). (Pubitemid 40204236)
113. Perier C, Tieu K, Guegan C et al. Complex I deficiency primes Bax-dependent neuronal apoptosis through mitochondrial oxidative damage. Proc. Natl Acad. Sci. USA 102, 19126-19131 (2005). (Pubitemid 43049577)
114. Galter D, Buervenich S, Carmine A, Anvret M, Olson L. ALDH1 mRNA: presence in human dopamine neurons and decreases in substantia nigra in Parkinson's disease and in the ventral tegmental area in schizophrenia. Neurobiol. Dis. 14, 637-647 (2003). (Pubitemid 37547970)
115. Ran Q, Liang H, Gu M et al. Transgenic mice overexpressing glutathione peroxidase 4 are protected against oxidative stress-induced apoptosis. J. Biol. Chem. 279, 55137-55146 (2004). (Pubitemid 40066507)
116. Sacksteder CA, Qian WJ, Knyushko TV et al. Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease. Biochemistry 45, 8009-8022 (2006).
117. Wolfer DP, Mohajeri HM, Lipp HP, Schachner M. Increased flexibility and selectivity in spatial learning of transgenic mice ectopically expressing the neural cell adhe sion molecule L1 in astrocytes. Eur. J. Neurosci. 10, 708-717 (1998). (Pubitemid 28325493)
118. Law JW, Lee AY, Sun M et al. Decreased anxiety, altered place learning, and increased CA1 basal excitatory synaptic transmission in mice with conditional ablation of the neural cell adhesion molecule L1. J. Neurosci. 23, 10419-10432 (2003). (Pubitemid 37444619)
119. Hulley P, Schachner M, Lubbert H. L1 neural cell adhesion molecule is a survival factor for fetal dopaminergic neurons. J. Neurosci. Res. 53, 129-134 (1998). (Pubitemid 28300118)
120. Diedrich M, Mao L, Bernreuther C et al. Proteome analysis of ventral midbrain in MPTP-treated normal and L1cam transgenic mice. Animal Proteomics 8, 1266-1275 (2008). (Pubitemid 351462932)
121. De Iuliis A, Grigoletto J, Recchia A, Giusti P, Arslan P. A proteomic approach in the study of an animal model of Parkinson's disease. Clin. Chim. Acta 357, 202-209 (2005). (Pubitemid 40894638)
122. Poon HF, Shepherd HM, Reed TT et al. Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis. Neurobiol. Aging 27, 1020-1034 (2006).
123. Youdim MB, Gross A, Finberg JP. Rasagiline [N-propargyl-1R(+)-aminoindan] , a selective and potent inhibitor of mitochondrial monoamine oxidase B. Br. J. Pharmacol. 132, 500-506 (2001). (Pubitemid 32142364)
124. Riederer P, Youdim MB. Monoamine oxidase activity and monoamine metabolism in brains of parkinsonian patients treated with l-deprenyl. J. Neurochem. 46, 1359-1365 (1986). (Pubitemid 16062531)
125. Kupsch A, Sautter J, Gotz ME et al. Monoamine oxidase-inhibition and MPTP-induced neurotoxicity in the non-human primate: comparison of rasagiline (TVP 1012) with selegiline. J. Neural Transm. 108, 985-1009 (2001). (Pubitemid 32802096)
126. Blandini F, Armentero MT, Fancellu R, Blaugrund E, Nappi G. Neuroprotective effect of rasagiline in a rodent model of Parkinson's disease. Exp. Neurol. 18, 455-459 (2004). (Pubitemid 38610291)
127. Olanow CW, Rascol O, Hauser R et al. A double-blind, delayed-start trial of rasagiline in Parkinson's disease. N. Engl. J. Med. 361, 1268-1278 (2009).
128. Maruyama W, Takahashi T, Youdim M, Naoi M. The anti-Parkinson drug, rasagiline, prevents apoptotic DNA damage induced by peroxynitrite in human dopaminergic neuroblastoma SH-SYSY cells. J. Neural Transm. 109, 467-481 (2002). (Pubitemid 34280405)
129. Akao Y, Maruyama W, Yi H et al. An anti-Parkinson's disease drug, N-propargyl-1 (R)-aminoindan (rasagiline), enhances expression of antiapoptotic bcl-2 in human dopaminergic SH-SY5Y cells. Neurosci. Lett. 326, 105-108 (2002). (Pubitemid 34607570)
130. Maruyama W, Akao Y, Youdim MB et al. Transfection-enforced Bcl-2 overexpression and an anti-Parkinson drug, rasagiline, prevent nuclear accumulation of glyceraldehyde-3 phosphate dehydrogenase induced by an endogenous dopaminergic neurotoxin, N-methyl(R)salsolinol. J. Neurochem. 78, 727-735 (2001). (Pubitemid 32777974)
131. Weinreb O, Bar-Am O, Amit T et al. Neuroprotection via pro-survival protein kinase C isoforms associated with Bcl-2 family members. FASEB J. 18, 1471-1473 (2004). (Pubitemid 39561618)
132. Carrillo MC, Minami C, Kitani K et al. Enhancing effect of rasagiline on superoxide dismutase and catalase activities in the dopaminergic system in the rat. Life Sci. 67, 577-585 (2000). (Pubitemid 30431547)
133. Magyar K, Palfi M, Tabi T et al. Pharmacological aspects of (-)-deprenyl. Curr. Med. Chem. 11, 2017-2031 (2004). (Pubitemid 38967727)
134. Am OB, AmitT, Youdim MB. Contrasting neuroprotective and neurotoxic actions of respective metabolites of anti-Parkinson drugs rasagiline and selegiline. Neurosci. Lett. 355, 169-172 (2004). (Pubitemid 38368730)
135. Ricaurte GA, Seiden LS, Schuster CR. Further evidence that amphetamines produce long-lasting dopamine neurochemical deficits by destroying dopamine nerve fibers. Brain Res. 303, 358-364 (1984).
136. Moszczynska A, Fitzmaurice P, Ang L et al. Why is parkinsonism not a feature of human methamphetamine users? Brain 127, 363-370 (2004). (Pubitemid 38160321)
137. Palhagen S, Heinonen E, Hagglund J et al. for the Swedish Parkinson Study Group. Selegiline slows the progression of the symptoms of Parkinson disease. Neurology 66, 1200-1206 (2006). (Pubitemid 43739704)
138. Abu-Raya S, Tabakman R, Blaugrund E et al. Neuroprotective and neurotoxic effects of monoamine oxidase-B inhibitors and derived metabolites under ischemia in PC12 cells. Eur. J. Pharmacol. 434, 109-116 (2002). (Pubitemid 34056569)
139. Jenner P. Preclinical evidence for neuroprotection with monoamine oxidase-B inhibitors in Parkinson's disease. Neurology 63(Suppl. 2), S13-S22 (2004). (Pubitemid 39346707)
140. Tabakman R, Lecht S, Lazarovici P. Neuroprotection by monoamine oxidase B inhibitors: a therapeutic strategy monoamine oxidase B inhibitors: a therapeutic strategy for Parkinson's disease? Bioessays 26, 80-90 (2004).
141. Weinreb O, Amit T, Sagi Y, Drigues N, Youdim MB. Genomic and proteomic study to survey the mechanism of action of the anti-Parkinson's disease drug, rasagiline compared with selegiline, in the rat midbrain. J. Neural. Transm. 116, 1457-1472 (2009).
142. Weinreb O, Amit T, Bar-Am O, Youdim MB. Induction of neurotrophic factors GDNF and BDNF associated with the mechanism of neurorescue action of rasagiline and ladostigil: new insights and implications for therapy. Ann. NY Acad. Sci. 1122, 155-168 (2007). (Pubitemid 350249546)
143. Bar-Am O, Amit T, Youdim MB. Contrasting neuroprotective and neurotoxic actions of respective metabolites of anti-Parkinson drugs rasagiline and selegiline. Neurosci. Lett. 35, 169-172 (2004). (Pubitemid 38368730)
144. Maruyama W, Nitta A, Shamoto-Nagai M et al. N-Propargyl-1 (R)-aminoiddan. rasagiline, increases glial cell line-derived neurotrophic factor (GDNF) in neuroblastoma SH-SY5Y cells through activation of NF-kB trabscription factor. Neurochem. Int. 44, 393-400 (2004). (Pubitemid 37548404)
145. Murer MG, Yan Q, Raisman-Vozari R. Brain-derived neurotrophic factor in the control human brain, and in Alzheimer's disease and Parkinson's disease. Prog. Neurobiol. 63, 71-124 (2001).
146. Parain K, Murer MG, Yan O et al. Reduced expression of brain-derived neurotrophic factor protein in Parkinson's disease substantia nigra. NeuroReport 10, 557-561 (1999). (Pubitemid 29333282)
147. Sole C, Dolcet X, Segura MF et al. The death receptor antagonist FAIM promotes neurite outgrowth by a mechanism that depends on ERK and NF-kB signaling. J. Cell Biol. 167, 479-492 (2004). (Pubitemid 39489056)
148. Shimoji M, Zhang L, Mandir AS et al. Absence of inclusion body formation in the MPTP mouse model of Parkinson's disease. Brain Res. Mol. Brain Res.134, 103-108 (2005). (Pubitemid 40403642)
149. Jin J, Meredith GE, Chen L et al. Quantitative proteomic analysis of mitochondrial proteins: relevance to Lewy body formation and Parkinson's disease. Brain Res. Mol. Brain Res. 134, 119-138 (2005). (Pubitemid 40403644)
150. Alvarez-Fischer D, Guerreiro S, Hunot S et al. Modelling Parkinson-like neurodegeneration via osmotic minipump delivery of MPTP and probenecid. J. Neurochem.107, 701-711 (2008).
151. Muqit MM, Abou-Sleiman PM, Saurin AT et al. Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress. J. Neurochem. 98, 156-169 (2006).
152. Ashley AK, Hanneman WH, Katoh T et al. Analysis of targeted mutation in DJ-1 on cellular function in primary astrocytes. Toxicol. Lett. 184, 186-191 (2009).
153. Spencer JP, Jenner P, Daniel SE, Lees AJ, Marsden DC, Halliwell B. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 71, 2112-2122 (1998). (Pubitemid 28491568)
154. Berman SB, Hastings TG. Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson's disease. J. Neurochem. 73, 1127-1137 (1999).
155. Van Laar VS, Dukes AA, Cascio M, Hastings TG. Proteomic analysis of rat brain mitochondria following exposure to dopamine quinone: implications for Parkinson disease. Neurobiol. Dis. 29, 477-489 (2008).
156. Schlattner U, Forstner M, Eder M, Stachowiak O, Fritz-Wolf K, Wallimann T. Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach. Mol. Cell. Biochem. 184, 125-140 (1998). (Pubitemid 28398605)
157. Lenz H, Schmidt M, Welge V et al. Inhibition of cytosolic and mitochondrial creatine kinase by siRNA in HaCaT-and HeLaS3-cells affects cell viability and mitochondrial morphology. Mol. Cell Biochem. 306, 153-162 (2007). (Pubitemid 350001827)
158. Speer O, Back N, Buerklen T et al. Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane. Biochem. J. 385, 445-450 (2005). (Pubitemid 40165077)
159. Dolder M, Wendt S, Wallimann T. Mitochondrial creatine kinase in contact sites: interaction with porin and adenine nucleotide translocase, role in permeability transition and sensitivity to oxidative damage. Biol. Signals Recept. 10, 93-111 (2001). (Pubitemid 32171161)
160. Wendt S, Schlattner U, Wallimann T. Differential effects of peroxynitrite on human mitochondrial creatine kinase isoenzymes. Inactivation, octamer destabilization and identification of involved residues. J. Biol. Chem. 278, 1125-1130 (2003). (Pubitemid 36790793)
161. Brdiczka DG, Zorov DB, Sheu SS. Mitochondrial contact sites: their role in energy metabolism and apoptosis. Biochim. Biophys. Acta 1762, 148-163 (2006). (Pubitemid 43006022)
162. Geissler A, Rassow J, Pfanner N, Voos W. Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins. Mol. Cell. Biol. 21, 7097-7104 (2001). (Pubitemid 32911268)
163. John GB, Shang Y, Li L et al. The mitochondrial inner membrane protein mitofilin controls cristae morphology. Mol. Biol. Cell 16, 1543-1554 (2005). (Pubitemid 40349586)
164. Xie J, Marusich MF, Souda P, Whitelegge J, Capaldi RA. The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxisn 1 and 2, coiled-coil helix domain-containing protein 3 and 6 and DnaJC11. FEBS Lett. 581, 3545-3549 (2007). (Pubitemid 47048194)
165. Jin J, Hulette C, Wang Y et al. Proteomic identification of a stress protein, mortalin/ mthsp70/GRP75: relevance to Parkinson disease. Mol. Cell Proteomics 5, 1193-1204 (2006). (Pubitemid 44103391)
166. Zhou Y, Gu G, Goodlett DR et al. Analysis of a-synuclein-associated proteins by quantitative proteomics. J. Biol. Chem. 279, 39155-39164 (2004). (Pubitemid 39296079)
167. Zhou Y, Wang Y, Kovacs MI, Jin J, Zhang J. Microglial activation induced by neurodegeneration. A proteomic analysis. Mol. Cell. Proteomics 4, 1471-1479 (2005). (Pubitemid 41555473)
168. Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999 (1999). (Pubitemid 29474856)
169. Haqqani AS, Kelly JF, Stanimirovic DB. Quantitative protein profiling by mass spectrometry using isotope-coded affinity tags. Methods Mol. Biol. 439, 225-240 (2008).
170. von Haller PD, Yi E, Donohoe S et al. The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: II. Evaluation of tandem mass spectrometry methodologies for large-scale protein analysis, and the application of statistical tools for data analysis and interpretation. Mol. Cell. Proteomics 2, 428-442 (2003).
171. Maries E, Dass B, Collier TJ et al. The role of a-synuclein in Parkinson's disease: insights from animal models. Nat. Rev. Neurosci. 4, 727-738 (2003). (Pubitemid 37280152)
172. Feany MB, Bender WW. A Drosophila model of Parkinson's disease. Nature 404, 394-398 (2000).
173. Xun Z, Sowell RA, Kaufman TC et al. Protein expression in a Drosophila model of Parkinson's disease. J. Proteome Res. 6, 348-357 (2007). (Pubitemid 46173686)
174. Xun Z, Sowell RA, Kaufman TC, Clemmer DE. Quantitative proteomics and presymptomatic A53T a-synuclein Drosophila model of Parkinson's disease. Mol. Cell. Proteomics 7, 1191-1203 (2008). (Pubitemid 352038266)
175. Chakraborty A, Regnier FE. Global internal standard technology for comparative proteomics. J. Chromatogr. A 949, 173-184 (2002). (Pubitemid 34183425)
176. Poon HF, Frasier M, Shreve N, Calabrese V, Wolozin B, Butterfield DA. Mitochondrial associated metabolic proteins are selectively oxidized in A30P a-synuclein transgenic mice-a model of familial Parkinson's disease. Neurobiol. Dis. 18, 492-498 (2005). (Pubitemid 40332708)
177. Conway KA, Harper JD, Lansbury PT. Accelerated in vitro fibril formation by a mutant a-synuclein linked to early-onset Parkinson disease. Nat. Med. 4, 1318-1320 (1998).
178. Li J, Uversky VN, Fink AL. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human a-synuclein. Biochem. 40, 11604-11613 (2001). (Pubitemid 32911305)
179. Li J, Uversky VN, Fink AL. Conformational behavior of human a-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T. Neurotoxicology 23, 553-567 (2002). (Pubitemid 36527676)
180. Narhi L, Wood SJ, Steavenson S. Both familial Parkinson's disease mutations accelerate a-synuclein aggregation. J. Biol. Chem. 274, 9843-9846 (1999). (Pubitemid 129517964)
181. Lee M, Hyun D, Halliwell B, Jenner P. Effect of the overexpression of wild-type or mutant a-synuclein on cell susceptibility to insult. J. Neurochem. 76, 998-1009 (2001). (Pubitemid 32167373)
182. Giege P, Heazlewood JL, Roessner-Tunali U et al. Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells. Plant Cell 15, 2140-2151 (2003). (Pubitemid 37144066)
183. Shah GN, Hewett-Emmett D, Grubb JH et al. Mitochondrial carbonic anhydrase CA VB: differences in tissue distribution and pattern of evolution from those of CA VA suggest distinct physiological roles. Proc. Natl Acad. Sci. USA 97, 1677-1682 (2000). (Pubitemid 30118502)
184. Darios F, Corti O, Lucking CB et al. Parkin prevents mitochondrial swelling and cytochrome C release in mitochondria-dependent cell death. Hum. Mol. Genet. 12, 517-526 (2003). (Pubitemid 36305590)
185. Hasegawa T, Treis A, Patenge N, Fiesel FC, Springer W, Kahle PJ. Parkin protects against tyrosinase-mediated dopamine neurotoxicity by suppressing stress-activated protein kinase pathways. J. Neurochem. 105, 1700-1715 (2008). (Pubitemid 351678502)
186. Kuroda Y, Mitsui T, Kunishige M et al. Parkin enhances mitochondrial biogenesis in proliferating cells. Hum. Mol. Genet. 15, 883-895 (2006). (Pubitemid 43338230)
187. Kitada T, Asakawa S, Hattori N et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392, 605-608 (1998). (Pubitemid 28207717)
188. Periquet M, Corti O, Jacquier S, Brice A. Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function. J. Neurochem. 95, 1259-1276 (2005). (Pubitemid 41779252)
189. Pesah Y, Pham T, Burgess H et al. Parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 131, 2183-2194 (2004). (Pubitemid 38702049)
190. Xun Z, Kaufman TC, Clemmer DE. Stable isotope labelling and label-free proteomics of Drosophila parkin null mutants. J. Proteome Res. 8, 4500-4510 (2009).
191. Bondarenko PV, Chelius D, Shaler TA. Identification and relative quantification of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid-chromatography-tandem mass spectrometry. Anal. Chem. 74, 4741-4749 (2002).
192. Paschen SA, Waizenegger T, Stan T et al. Evolutionary conservation of biogenesis of b barrel membrane proteins. Nature 426, 862-866 (2003). (Pubitemid 38056874)
193. Martens GJ, Piosik PA, Danen EH. Evolutionary conservation of the 14-13-3 protein. Biochem. Biophys. Res. Commun. 184, 1456-1459 (1992).
194. Li J, Cai T, Wu P et al. Proteomic analysis of mitochondria from Caenorhabditis elegans. Proteomics 9, 4539-4553 (2009).
195. Grad LI, Sayles LC, Lemire BD. Isolation and functional analysis of mitochondria from the nematode Caenorhabditis elegans. Methods Mol. Biol. 372, 51-66 (2007).
196. Kanehisa M, Goto S. KEGG: Kyoto encyclopaedia of genes and genomes. Nucleic Acids Res. 28, 27-30 (2000). (Pubitemid 30047706)
197. Gibson BW. The human mitochondrial proteome: oxidative stress, protein modifications and oxidative phosphorylation. Int. J. Biochem. Cell Biol. 37, 927-934 (2005). (Pubitemid 40311735)
198. Hinerfeld D, Traini MD, Weinberger RP et al. Endogenous mitochondrial oxidative stress: neurodegeneration, proteome analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice. J. Neurochem. 88, 657-667 (2004). (Pubitemid 38140210)
199. Lebovitz RM, Zhang H, Vogel H et al. Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc. Natl. Acad. Sci. USA 93, 9782-9787 (1996). (Pubitemid 26296686)
200. Melov S, Schneider JA, Day BJ et al. A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase. Nat. Genet. 18, 159-163 (1998). (Pubitemid 28082464)
201. Fernéndez-Silva P, Enriquez JA, Montoya J. Replication and transcription of mammalian mitochondrial DNA. Exp. Physiol. 88, 41-56 (2003). (Pubitemid 36150058)
202. Ozawa T, Sako Y, Sato M, Kitamura T, Umezawa Y. A genetic approach to identifying mitochondrial proteins. Nat. Biotechnol. 21, 287-293 (2003). (Pubitemid 36314813)
203. Isaaq HJ. The role of separation science in proteomics research. Electophoresis 22, 3629-3638 (2001).
204. Fountoulakis M, Juranville J-F, Roeder D, Evers S, Berndt P, Langen H. Reference map of the low-molecular-mass proteins of Haemophilus influenzae. Electrophoresis 19, 1819-1827 (1998). (Pubitemid 28396267)
205. Smith AC, Robinson AJ. MitoMiner: an integrated database for the storage and analysis of mitochondrial proteomics data. Mol. Cell Proteomics 8, 1324-1337 (2009).
206. Hamosh A, Scott AF, Amberger JS, Bocchini CA, McKusick VA. Online Mendelian Inheritance in Man (OMIM), a knowledge-base of human genes and genetic disorders. Nucleic Acids Res. 33, D514-D517 (2005). (Pubitemid 40207927)
207. Silvestri L, Caputo V, Bellacchio E et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum. Mol. Genet. 14, 3477-3492 (2005). (Pubitemid 41672130)
208. Park J, Lee SB, Lee S et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441, 1157-1161 (2006). (Pubitemid 43990737)
209. Abou-Sleiman PM, Mugit MM, McDonald NQ et al. A heterozygous effect for PINK1 mutations in Parkinson's disease? Ann. Neurol. 60, 414-419 (2006). (Pubitemid 44684977)
210. Casarejos MJ, Menéndez J, Solano RM et al. Susceptibility to rotenone is increased in neurons from parkin null mice and is reduced by minocycline. J. Neurochem. 97, 934-946 (2006).
211. Bandopadhyay R, Kingsbury AE, Cookson MR et al. The expression of DJ-1 (PARK7) in normal human CNS and idiopathic Parkinson's disease. Brain 127, 420-430 (2004). (Pubitemid 38160326)
212. Kim RH, Smith PD, Aleyasin H et al. Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress. Proc. Natl. Acad. Sci. USA 102, 5215-5220 (2005). (Pubitemid 40503765)