메뉴 건너뛰기




Volumn 16, Issue 25, 2010, Pages 2799-2817

Monoamine oxidase inhibitors as neuroprotective agents in age-dependent neurodegenerative disorders

Author keywords

Alzheimer's disease; Mao inhibitors; Mitochondria; Monoamine oxidase; Neuroprotection; Neurotrophic factors; Parkinson's disease; Programmed cell death

Indexed keywords

4 [4 (4 FLUOROPHENYL) 5 (2 METHOXY 4 PYRIMIDINYL) 1 IMIDAZOLYL]CYCLOHEXANOL; ADENOSINE TRIPHOSPHATE; ANTIDEPRESSANT AGENT; BROFAROMINE; CALPASTATIN; CEP 1347; CLORGYLINE; CYCLOSPORIN; FR 255595; GLYCOSYLTRANSFERASE INHIBITOR; IPRONIAZID; ISONIAZID; K 252A; LADOSTIGIL; LEVODOPA; MOCLOBEMIDE; MONOAMINE OXIDASE INHIBITOR; N (2 PROPYNYL) 1 INDANAMINE; NEUROTRANSMITTER; PHENELZINE; RASAGILINE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; ROTTLERIN; SELEGILINE; TOLOXATONE; TRANYLCYPROMINE; TRANYLCYPROMINE DERIVATIVE; TV 1012; UNCLASSIFIED DRUG; UNINDEXED DRUG; [1 [(1 FORMYL 2 PHENYLETHYL)CARBAMOYL] 2 METHYLPROPYL]CARBAMIC ACID BENZYL ESTER;

EID: 77957968479     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161210793176527     Document Type: Article
Times cited : (107)

References (267)
  • 1
    • 0033600301 scopus 로고    scopus 로고
    • Molecular basis of the neurodegenerative disorders
    • Martin JB. Molecular basis of the neurodegenerative disorders. NEng J Med 1999; 340: 1970-1980.
    • (1999) NEng J Med , vol.340 , pp. 1970-1980
    • Martin, J.B.1
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy Physiol Rev 2001; 81: 741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 0037417254 scopus 로고    scopus 로고
    • Alzheimer's disease and Parkinson'sdisease
    • Nussbaum RL, Ellis CE. Alzheimer's disease and Parkinson'sdisease. N Eng J Med 2003; 348: 1356-1364.
    • (2003) N Eng J Med , vol.348 , pp. 1356-1364
    • Nussbaum, R.L.1    Ellis, C.E.2
  • 4
    • 33845535334 scopus 로고    scopus 로고
    • Pathologic and nicotinicreceptor binding differences between mild cognitive impairment,Alzheimer disease, and normal aging
    • Sabbagh MN, Shah F, Reid RT, et al. Pathologic and nicotinicreceptor binding differences between mild cognitive impairment,Alzheimer disease, and normal aging. Arch Neurol 2006; 63: 1771-1776.
    • (2006) Arch Neurol , vol.63 , pp. 1771-1776
    • Sabbagh, M.N.1    Shah, F.2    Reid, R.T.3
  • 5
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms andmodels
    • Dauer W, Przedborski S. Parkinson's disease: mechanisms andmodels. Neuron 2003; 39: 889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 6
    • 20444504698 scopus 로고    scopus 로고
    • The genetic epidemiology of neurodegenera-tive disease
    • Bertram L, Tanzi RE. The genetic epidemiology of neurodegenera-tive disease. J Clin Invest 2005; 115: 1449-1457.
    • (2005) J Clin Invest , vol.115 , pp. 1449-1457
    • Bertram, L.1    Tanzi, R.E.2
  • 7
    • 40749109450 scopus 로고    scopus 로고
    • Parkinson's disease: Genetic versus toxin-induced rodent models
    • Terzioglu M, Galter D. Parkinson's disease: genetic versus toxin-induced rodent models. FEBS J 2008; 275: 1384-1391.
    • (2008) FEBS J , vol.275 , pp. 1384-1391
    • Terzioglu, M.1    Galter, D.2
  • 8
    • 0030860376 scopus 로고    scopus 로고
    • α-Synuclein -a link between Parkinson andAlzheimer disease?
    • Heintz N, Zoghbi H. α-Synuclein -a link between Parkinson andAlzheimer disease? Nat Genet 1997; 17: 325-327.
    • (1997) Nat Genet , vol.17 , pp. 325-327
    • Heintz, N.1    Zoghbi, H.2
  • 9
    • 18344417178 scopus 로고    scopus 로고
    • Lewy bodies containaltered -synuclein in brains of many familial Alzheimer's diseasepatients with mutations in presenilin and amyloid precursor proteingenes
    • Lippa CF, Fujiwara H, Mann DMA, et al. Lewy bodies containaltered -synuclein in brains of many familial Alzheimer's diseasepatients with mutations in presenilin and amyloid precursor proteingenes. Am J Pathol 1998; 153: 1365-1370.
    • (1998) Am J Pathol , vol.153 , pp. 1365-1370
    • Lippa, C.F.1    Fujiwara, H.2    Mann, D.M.A.3
  • 10
    • 33748584602 scopus 로고    scopus 로고
    • Interaction between abeta peptide and alpha synuclein: Molecularmechanisms in overlapping pathology of Alzheimer's and Parkin-son's in dementia with Lewy body disease
    • Mandel PK, Pettegrew JW, Masliah E, Hamilton RL, Mandel R.Interaction between abeta peptide and alpha synuclein: molecularmechanisms in overlapping pathology of Alzheimer's and Parkin-son's in dementia with Lewy body disease. Neurochem Res 2006;31: 153-162.
    • (2006) Neurochem Res , vol.31 , pp. 153-162
    • Mandel, P.K.1    Pettegrew, J.W.2    Masliah, E.3    Hamilton, R.L.4    Mandel, R.I.5
  • 11
    • 47349093970 scopus 로고    scopus 로고
    • The α-synuclein burden hypothesis of Parkinson disease and its relationship to Alzheimer disease
    • McGeer PL, McGeer EG. The α-synuclein burden hypothesis of Parkinson disease and its relationship to Alzheimer disease. ExpNeurol 2008; 212: 235-238.
    • (2008) ExpNeurol , vol.212 , pp. 235-238
    • McGeer, P.L.1    McGeer, E.G.2
  • 12
    • 45749155306 scopus 로고    scopus 로고
    • A critical reappraisal of current staging of Lewy-related pathology in human brain
    • Jellinger KA. A critical reappraisal of current staging of Lewy-related pathology in human brain. Acta Neuropathol 2008; 116: 1-16.
    • (2008) Acta Neuropathol , vol.116 , pp. 1-16
    • Jellinger, K.A.1
  • 14
    • 0037337815 scopus 로고    scopus 로고
    • Neuronal loss isgreater in the locus coeruleus than nucleus basalis and substantianigra in Alzheimer and Parkinson diseases
    • Zarow C, Lyness SA, Mortimer JA, Chui HC. Neuronal loss isgreater in the locus coeruleus than nucleus basalis and substantianigra in Alzheimer and Parkinson diseases. Arch Neurol 2003; 60:337-341.
    • (2003) Arch Neurol , vol.60 , pp. 337-341
    • Zarow, C.1    Lyness, S.A.2    Mortimer, J.A.3    Chui, H.C.4
  • 15
    • 0028156806 scopus 로고
    • Noradrenaline, dopamine and serotonin levels and metabolism in the human hypothalamus: Observations in Parkinson's disease and normal subjects
    • Shannak K, Rajput A, Rozdilsky B, Kish G, Gilbert K, Horykiewicz O. Noradrenaline, dopamine and serotonin levels and metabolism in the human hypothalamus: observations in Parkinson's disease and normal subjects. Brain Res 1994; 639: 33-41.
    • (1994) Brain Res , vol.639 , pp. 33-41
    • Shannak, K.1    Rajput, A.2    Rozdilsky, B.3    Kish, G.4    Gilbert, K.5    Horykiewicz, O.6
  • 16
    • 0346025493 scopus 로고    scopus 로고
    • Functional neurochemistry ofAlzheimer's disease
    • Gsell W, Jungkunz G, Riederer P. Functional neurochemistry ofAlzheimer's disease. Curr Pharm Des 2004; 10: 265-293.
    • (2004) Curr Pharm Des , vol.10 , pp. 265-293
    • Gsell, W.1    Jungkunz, G.2    Riederer, P.3
  • 17
    • 58149394415 scopus 로고    scopus 로고
    • Amyloid pathology is associated with progressive monoaminergic neurodegeneration in atransgenic mouse model of Alzheimer's disease
    • Liu Y, Yoo MY, Savonenko A, et al. Amyloid pathology is associated with progressive monoaminergic neurodegeneration in atransgenic mouse model of Alzheimer's disease. J Neurosci 2008;28: 13805-13814.
    • (2008) J Neurosci , vol.28 , pp. 13805-13814
    • Liu, Y.1    Yoo, M.Y.2    Savonenko, A.3
  • 18
    • 0032914318 scopus 로고    scopus 로고
    • Monoamine oxidase: From genes tobehavior
    • Shih JC, Chen K, Ridd MJ. Monoamine oxidase: from genes tobehavior. Ann Rev Neurosci 1999; 22: 197-217.
    • (1999) Ann Rev Neurosci , vol.22 , pp. 197-217
    • Shih, J.C.1    Chen, K.2    Ridd, M.J.3
  • 20
    • 30444437749 scopus 로고    scopus 로고
    • Monoamine oxidase isoforms and inhibitors in Parkinson's disease and depressive illness
    • Youdim MBH, Bakhle YS. Monoamine oxidase isoforms and inhibitors in Parkinson's disease and depressive illness. Br J Pharmacol 2006; 147: 287-296.
    • (2006) Br J Pharmacol , vol.147 , pp. 287-296
    • Youdim, M.B.H.1    Bakhle, Y.S.2
  • 21
    • 34248549035 scopus 로고    scopus 로고
    • Involvement of type A monoamine oxidase in neurodegeneration: Regulation of mitochondrial signaling leading to cell death or neuroprotection
    • Naoi M, Maruyama W, Akao Y, Yi H, Yamaoka T. Involvement of type A monoamine oxidase in neurodegeneration: regulation of mitochondrial signaling leading to cell death or neuroprotection. J Neural Transm 2006; (Suppl 71): 67-77.
    • (2006) J Neural Transm , Issue.SUPPL. 71 , pp. 67-77
    • Naoi, M.1    Maruyama, W.2    Akao, Y.3    Yi, H.4    Yamaoka, T.5
  • 22
    • 34547698945 scopus 로고    scopus 로고
    • Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B
    • Edmondson DE, Binda C, Mattevi A. Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B.Arch Biochem Biophys 2007; 464: 269-276.
    • (2007) Arch Biochem Biophys , vol.464 , pp. 269-276
    • Edmondson, D.E.1    Binda, C.2    Mattevi, A.3
  • 23
    • 0023174117 scopus 로고
    • Localization of MAO-A and MAO-B in human brain: A step in understanding the therapeutic action of L-deprenyl
    • Riederer P, Konradi C, Schay V, et al. Localization of MAO-A and MAO-B in human brain: a step in understanding the therapeutic action of L-deprenyl. Adv Neurol 1986; 45: 111-118.
    • (1986) Adv Neurol , vol.45 , pp. 111-118
    • Riederer, P.1    Konradi, C.2    Schay, V.3
  • 24
    • 0022365018 scopus 로고
    • Increased life expectancy resulting from addition of L-deprenylto Madopar treatment in Parkinson's disease; a long-term study
    • Birkmayer W, Knoll J, Riederer P, Youdim MBH, Hars V, Marton J. Increased life expectancy resulting from addition of L-deprenylto Madopar treatment in Parkinson's disease; a long-term study. JNeural Transm 1985; 64: 113-127.
    • (1985) JNeural Transm , vol.64 , pp. 113-127
    • Birkmayer, W.1    Knoll, J.2    Riederer, P.3    Youdim, M.B.H.4    Hars, V.5    Marton, J.6
  • 25
    • 3242772321 scopus 로고    scopus 로고
    • Clinical applications of MAO-inhibitors
    • Riederer P, Lachenmayer L. Laux G. Clinical applications of MAO-inhibitors. Curr Med Chem 2004; 11: 2033-2043.
    • (2004) Curr Med Chem , vol.11 , pp. 2033-2043
    • Riederer, P.1    Lachenmayer, L.2    Laux, G.3
  • 26
    • 33645307953 scopus 로고    scopus 로고
    • The therapeutic potential of monoamine oxidase inhibitors
    • Youdim MBH, Edmondson D, Tipton KF. The therapeutic potential of monoamine oxidase inhibitors. Nat Rev Neurosci 2006; 7:295-309.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 295-309
    • Youdim, M.B.H.1    Edmondson, D.2    Tipton, K.F.3
  • 27
    • 0021224694 scopus 로고
    • Protection against the dopaminergic neurotoxiciy of 1-methyl-1,2,3,6-tetrahydropyridine (MPTP) by monoamine inhibitors
    • Heikkila RE, Manzino L, Cabbat FS, Duvoisin RC. Protection against the dopaminergic neurotoxiciy of 1-methyl-1,2,3,6-tetrahydropyridine (MPTP) by monoamine inhibitors. Nature 1984;311: 467-469.
    • (1984) Nature , vol.311 , pp. 467-469
    • Heikkila, R.E.1    Manzino, L.2    Cabbat, F.S.3    Duvoisin, R.C.4
  • 28
    • 0027530638 scopus 로고
    • Effects of tocopherol and deprenyl on progression of disability in early Parkinson's disease
    • Parkinson Study Group
    • Parkinson Study Group. Effects of tocopherol and deprenyl on progression of disability in early Parkinson's disease. N Engl JMed 1993; 328: 176-183.
    • (1993) N Engl JMed , vol.328 , pp. 176-183
  • 29
    • 0028020079 scopus 로고
    • Neuroprotective effects of some monoamine oxidase-B inhibitors against DSP-4-induced noradre-naline depletion in the mouse hippocampus
    • Yu PH, Davis BA, Boulton AA. Neuroprotective effects of some monoamine oxidase-B inhibitors against DSP-4-induced noradre-naline depletion in the mouse hippocampus. J Neurochem 1994;63: 1820-1828.
    • (1994) J Neurochem , vol.63 , pp. 1820-1828
    • Yu, P.H.1    Davis, B.A.2    Boulton, A.A.3
  • 30
    • 0031746623 scopus 로고    scopus 로고
    • Deprenyl protects human dopaminergic neuroblastoma SH-SY5Y cells from apoptosis induced by peroxynitrite and nitric oxide
    • Maruyama W, Takahashi T, Naoi M. Deprenyl protects human dopaminergic neuroblastoma SH-SY5Y cells from apoptosis induced by peroxynitrite and nitric oxide. J Neurochem 1998; 70:2510-2515.
    • (1998) J Neurochem , vol.70 , pp. 2510-2515
    • Maruyama, W.1    Takahashi, T.2    Naoi, M.3
  • 31
    • 0034603412 scopus 로고    scopus 로고
    • Monoamine oxidase-B inhibitors in the treatment ofAlzheimer's disease
    • Thomas T. Monoamine oxidase-B inhibitors in the treatment ofAlzheimer's disease. Neurobiol Aging 2000; 21: 343-348.
    • (2000) Neurobiol Aging , vol.21 , pp. 343-348
    • Thomas, T.1
  • 32
    • 0348046385 scopus 로고    scopus 로고
    • Monoamine oxidase-B inhibition in Alzheimer's disease
    • Riederer P, Danielczyk W, Grünblatt E. Monoamine oxidase-B inhibition in Alzheimer's disease. Neuro Toxicol 2004; 25: 271-277.
    • (2004) Neuro Toxicol , vol.25 , pp. 271-277
    • Riederer, P.1    Danielczyk, W.2    Grünblatt, E.3
  • 33
    • 38449116644 scopus 로고    scopus 로고
    • Neuroprotection by propargylamine in Parkinson's disease: Intracellular mechanism underlying antiapoptotic function and search for clinical markers
    • Naoi M, Maruyama W, Yi H, Akao Y, Yamaoka Y, Shamoto-Nagai M. Neuroprotection by propargylamine in Parkinson's disease: intracellular mechanism underlying antiapoptotic function and search for clinical markers. J Neural Transm 2007; (Suppl 72):121-131.
    • (2007) J Neural Transm , Issue.SUPPL. 72 , pp. 121-131
    • Naoi, M.1    Maruyama, W.2    Yi, H.3    Akao, Y.4    Yamaoka, Y.5    Shamoto-Nagai, M.6
  • 34
    • 70349314934 scopus 로고    scopus 로고
    • Functional mechanism of neuroprotection by inhibitors of type B monoamine oxidase in Parkinson's disease
    • Naoi M, Maruyama W. Functional mechanism of neuroprotection by inhibitors of type B monoamine oxidase in Parkinson's disease.Expert Rev Neurother 2009; 9: 1233-1250.
    • (2009) Expert Rev Neurother , vol.9 , pp. 1233-1250
    • Naoi, M.1    Maruyama, W.2
  • 35
    • 17644375125 scopus 로고    scopus 로고
    • CNS Targets for multi-functionaldrugs in the treatment of Alzheimer's and Parkinson's disease
    • Youdim MBH, Buccafusco JJ. CNS Targets for multi-functionaldrugs in the treatment of Alzheimer's and Parkinson's disease. J Neural Transm 2005; 112: 519-537.
    • (2005) J Neural Transm , vol.112 , pp. 519-537
    • Youdim, M.B.H.1    Buccafusco, J.J.2
  • 36
    • 34548695421 scopus 로고    scopus 로고
    • Neurorescue activity, APP regulation and amyloid-beta peptide reduction by novel multi-functional brain permeable iron-chelating-antioxidants,M-30 and green tea polyphenol, EGCG
    • Avramovich-Tirosh Y, Reznichienko L, Mit T, et al. Neurorescue activity, APP regulation and amyloid-beta peptide reduction by novel multi-functional brain permeable iron-chelating-antioxidants,M-30 and green tea polyphenol, EGCG. Curr Alzheimer Res 2007;4: 403-411.
    • (2007) Curr Alzheimer Res , vol.4 , pp. 403-411
    • Avramovich-Tirosh, Y.1    Reznichienko, L.2    Mit, T.3
  • 37
    • 20944441667 scopus 로고    scopus 로고
    • Natural products and derivatives affecting neurotransmission relevant to Alzheimer's and Parkinson's disease
    • Houghton PJ, Howes MJ. Natural products and derivatives affecting neurotransmission relevant to Alzheimer's and Parkinson's disease. Neurosignals 2005; 14: 6-22.
    • (2005) Neurosignals , vol.14 , pp. 6-22
    • Houghton, P.J.1    Howes, M.J.2
  • 38
    • 0024330311 scopus 로고
    • Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease
    • Mizuno Y, Ohta S, Tanaka M, et al. Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease. Biochem Biophys Res Commun 1989; 163: 1450-1455.
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 1450-1455
    • Mizuno, Y.1    Ohta, S.2    Tanaka, M.3
  • 41
    • 0024848034 scopus 로고
    • Abnormalities of the electron transport chain in idiopathic Parkinson's disease
    • Parker WD Jr, Boyson SJ, Parks JK. Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann Neurol 1989;26: 719-723.
    • (1989) Ann Neurol , vol.26 , pp. 719-723
    • Parker Jr., W.D.1    Boyson, S.J.2    Parks, J.K.3
  • 42
    • 0026544129 scopus 로고
    • Mitochon-drial complex I and II activities of lymphocytes and platelets in Parkinson's disease
    • Yoshino H, Nakagawa-Hattori Y, Kondo T, Mizuno Y. Mitochon-drial complex I and II activities of lymphocytes and platelets in Parkinson's disease. J Neural Transm [P-D Sect] 1992; 4: 27-34.
    • (1992) J Neural Transm [P-D Sect] , vol.4 , pp. 27-34
    • Yoshino, H.1    Nakagawa-Hattori, Y.2    Kondo, T.3    Mizuno, Y.4
  • 43
    • 33646375711 scopus 로고    scopus 로고
    • High levels of mito-chondrial DNA deletions in substantia nigra neurons in aging and Parkinson's disease
    • Bender A, Krishnan KJ, Morris CM, et alet al. High levels of mito-chondrial DNA deletions in substantia nigra neurons in aging and Parkinson's disease. Nat Genet 2006; 38: 515-517.
    • (2006) Nat Genet , vol.38 , pp. 515-517
    • Bender, A.1    Krishnan, K.J.2    Morris, C.M.3
  • 44
    • 33646351299 scopus 로고    scopus 로고
    • Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons
    • Kraytsberg Y, Kudryavtseva E, McKee AC, Geula C, Kowall NW, Khrapko K. Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. NatGenet 2006; 38: 518-520.
    • (2006) NatGenet , vol.38 , pp. 518-520
    • Kraytsberg, Y.1    Kudryavtseva, E.2    McKee, A.C.3    Geula, C.4    Kowall, N.W.5    Khrapko, K.6
  • 45
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's diseasebrain mitochondrial complex I has oxidatively damaged subunits and its functionally impaired and misassembled
    • Keeney PM, Xie J, Capaldi RA, Benett JB Jr. Parkinson's diseasebrain mitochondrial complex I has oxidatively damaged subunits and its functionally impaired and misassembled. J Neurosci 2006;26: 5256-5264.
    • (2006) J Neurosci , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Benett Jr., J.B.4
  • 46
    • 55849122639 scopus 로고    scopus 로고
    • Mitochondrial biology and oxidativestress in parkinson disease pathogenesis
    • Henchcliffe C, Beal MF. Mitochondrial biology and oxidativestress in parkinson disease pathogenesis. Nat Clin Pract Neurol 2008; 4: 600-609.
    • (2008) Nat Clin Pract Neurol , vol.4 , pp. 600-609
    • Henchcliffe, C.1    Beal, M.F.2
  • 47
    • 53149087460 scopus 로고    scopus 로고
    • Mitochondrial alterations in Parkinson's disease
    • Vila M, Ramonet D, Perier C. Mitochondrial alterations in Parkinson's disease. J Neurochem 2008; 107: 317-328.
    • (2008) J Neurochem , vol.107 , pp. 317-328
    • Vila, M.1    Ramonet, D.2    Perier, C.3
  • 48
    • 44649136091 scopus 로고    scopus 로고
    • Neuromelanin selectively induces apoptosis in dopaminergic SH-SY5Y cells by deglutathiony-lation in mitochondria: Involvement of the protein and melanin component
    • Naoi M, Maruyama W, Yi H, et al. Neuromelanin selectively induces apoptosis in dopaminergic SH-SY5Y cells by deglutathiony-lation in mitochondria: involvement of the protein and melanin component. J Neurochem 2008; 105: 2489-2500.
    • (2008) J Neurochem , vol.105 , pp. 2489-2500
    • Naoi, M.1    Maruyama, W.2    Yi, H.3
  • 49
    • 34250716407 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • Schapira AHV. Mitochondrial dysfunction in Parkinson's disease.Cell Death Differ 2007; 14: 1261-1266.
    • (2007) Cell Death Differ , vol.14 , pp. 1261-1266
    • Schapira, A.H.V.1
  • 50
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cul-tures and Parkinson disease brain
    • Devi L, Raghavendran V, Prabhu BM, Avadhani NG, Ananda-theerthavarada HK. Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cul-tures and Parkinson disease brain. J Biol Chem 2008; 283: 9089-9100.
    • (2008) J Biol Chem , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Ananda-Theerthavarada, H.K.5
  • 51
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF, Avadhani NG, Anandatheerthavarada HK. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J Neurosci 2006; 26:9057-9068.
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 52
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial functionin neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, Avadhani NG. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial functionin neuronal cells. J Cell Biol 2003; 161: 41-51.
    • (2003) J Cell Biol , vol.161 , pp. 41-51
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 53
    • 33646152108 scopus 로고    scopus 로고
    • ReddyPH. Mitochondria are a direct site of A accumulation in Alzheimer's disease neurons: Implications for free radical generationand oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, ReddyPH. Mitochondria are a direct site of A accumulation in Alzheimer's disease neurons: implications for free radical generationand oxidative damage in disease progression. Human Mol Gene 2006; 15: 1437-1449.
    • (2006) Human Mol Gene , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5
  • 54
    • 51349110166 scopus 로고    scopus 로고
    • The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
    • Petersen CAH, Alikhani N, Behbahni H, et al. The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae. Proc Natl Acad Sci USA 2008; 105: 13145-13150.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13145-13150
    • Petersen, C.A.H.1    Alikhani, N.2    Behbahni, H.3
  • 56
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang X, Su B, Lee H, et al. Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J Neurosci 2009; 29:9090-9103.
    • (2009) J Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.3
  • 57
    • 67649756320 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease
    • Brüeler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Exp Neurol 2009; 218: 235-246.
    • (2009) Exp Neurol , vol.218 , pp. 235-246
    • Brüeler, H.1
  • 58
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007; 87: 99-163.
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 59
    • 0033739282 scopus 로고    scopus 로고
    • Apoptosis and Alzheimer's disease
    • Behl C. Apoptosis and Alzheimer's disease. J Neural Transm 2000;107: 1325-1344.
    • (2000) J Neural Transm , vol.107 , pp. 1325-1344
    • Behl, C.1
  • 60
    • 0037378897 scopus 로고    scopus 로고
    • Apoptosisin parkinson's disease: Signals for neuronal degradation
    • Tatton WG, Chalmers-Redman R, Brown D, Tatton N. Apoptosisin parkinson's disease: signals for neuronal degradation. Ann Neu-rol 2003; 53 (suppl 3): S61-S72.
    • (2003) Ann Neu-rol , vol.53 , Issue.SUPPL. 3
    • Tatton, W.G.1    Chalmers-Redman, R.2    Brown, D.3    Tatton, N.4
  • 61
    • 60849136313 scopus 로고    scopus 로고
    • Caspase activation in Alzheimer's disease: Earlyto rise and late to bed
    • Rohn TT, Head E. Caspase activation in Alzheimer's disease: Earlyto rise and late to bed. Rev Neurosci 2008; 19: 383-393.
    • (2008) Rev Neurosci , vol.19 , pp. 383-393
    • Rohn, T.T.1    Head, E.2
  • 62
    • 17144425021 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, endoplasmic reticulum stress, and apoptosis in Alzheimer'sdisease
    • Takuma K, Yan SS, Stern DM, Yamada K. Mitochondrial dysfunction, endoplasmic reticulum stress, and apoptosis in Alzheimer'sdisease. J Pharmacol Sci 2005; 97: 312-316.
    • (2005) J Pharmacol Sci , vol.97 , pp. 312-316
    • Takuma, K.1    Yan, S.S.2    Stern, D.M.3    Yamada, K.4
  • 63
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neurophil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo H, Albrecht A, Bourdeau M, Petzke T, Bergeron C, LeBlanc AC. Active caspase-6 and caspase-6-cleaved tau in neurophil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am J Pathol 2004; 165: 523-531.
    • (2004) Am J Pathol , vol.165 , pp. 523-531
    • Guo, H.1    Albrecht, A.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    Leblanc, A.C.6
  • 64
    • 12944250987 scopus 로고    scopus 로고
    • Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neuronsin Parkinson's disease
    • Hartmann A, Hunot S, Michel PP, et al. Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neuronsin Parkinson's disease. Proc Natl Acad Sci USA 2000; 97: 2875-2880.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2875-2880
    • Hartmann, A.1    Hunot, S.2    Michel, P.P.3
  • 65
    • 0030842085 scopus 로고    scopus 로고
    • Nuclear translocation of NF- kb is increased in dopaminergic neurons of patients with Parkinson'sdisease
    • Hunot S, Brugg B, Ricard D, et al. Nuclear translocation of NF- kb is increased in dopaminergic neurons of patients with Parkinson'sdisease. Proc Natl Acad Sci USA 1997; 94: 7531-7536.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7531-7536
    • Hunot, S.1    Brugg, B.2    Ricard, D.3
  • 66
    • 0032509773 scopus 로고    scopus 로고
    • Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bak, Bad, ICH-1 and CPP32, in Alzheimer's disease
    • Kitamura Y, Shimohara S, Ota T, et al. Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bak, Bad, ICH-1 and CPP32, in Alzheimer's disease. Brain Res 1998; 780: 260-269.
    • (1998) Brain Res , vol.780 , pp. 260-269
    • Kitamura, Y.1    Shimohara, S.2    Ota, T.3
  • 67
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy- a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
    • Yu WH, Cuervo AM, Kumar A, et al. Macroautophagy- a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease. J Cell Biol 2005; 171: 87-98.
    • (2005) J Cell Biol , vol.171 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3
  • 68
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen D-F, Youle RJ. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy.J Clin Biol 2008; 183: 795-803.
    • (2008) J Clin Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.-F.3    Youle, R.J.4
  • 69
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2:Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2:Release of cytochrome c from mitochondria blocked. Science 1997; 275: 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 70
    • 0034884148 scopus 로고    scopus 로고
    • Transfection-enforced Bcl-2 overexpression and an anti-parkinson drug,rasagiline, prevent nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase induced by an endogenous neurotoxin,N-methyl(R)salsolinol
    • Maruyama W, Akao Y, Youdim MB, Davis BA, Naoi M. Transfection-enforced Bcl-2 overexpression and an anti-parkinson drug,rasagiline, prevent nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase induced by an endogenous neurotoxin,N-methyl(R)salsolinol. J Neurochem 2001; 78:727-735.
    • (2001) J Neurochem , vol.78 , pp. 727-735
    • Maruyama, W.1    Akao, Y.2    Youdim, M.B.3    Davis, B.A.4    Naoi, M.5
  • 71
    • 26444532918 scopus 로고    scopus 로고
    • Inhibition of mitochondrial neural cell death pathways by protein transduction of Bcl-2 family proteins
    • Soane L, Fiskum G. Inhibition of mitochondrial neural cell death pathways by protein transduction of Bcl-2 family proteins. J Bioeng Biomembr 2005; 37: 179-190.
    • (2005) J Bioeng Biomembr , vol.37 , pp. 179-190
    • Soane, L.1    Fiskum, G.2
  • 73
    • 4644333076 scopus 로고    scopus 로고
    • Protective role of Bcl-2 on β-amyloid-induced cell death of differentiated PC12 cells: Reductionof NF- KB and p38 MAP kinase activation
    • Song YS, Park HJ, Kim SY, et al. Protective role of Bcl-2 on β-amyloid-induced cell death of differentiated PC12 cells: reductionof NF- KB and p38 MAP kinase activation. Neurosci Res 2004; 49:69-80.
    • (2004) Neurosci Res , vol.49 , pp. 69-80
    • Song, Y.S.1    Park, H.J.2    Kim, S.Y.3
  • 74
    • 2642543940 scopus 로고    scopus 로고
    • Neuroprotective properties of Bcl-w in Alzheimer disease
    • Zhu X, Wang Y, Ogawa O, et al. Neuroprotective properties of Bcl-w in Alzheimer disease. J Neurochem 2004; 89: 1233-1240.
    • (2004) J Neurochem , vol.89 , pp. 1233-1240
    • Zhu, X.1    Wang, Y.2    Ogawa, O.3
  • 75
    • 0035019371 scopus 로고    scopus 로고
    • CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with Aβ-induced cortical neuron apoptosis
    • Bozyczko-Coyne D, O'Kane TM, Wu ZL, et al. CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with Aβ-induced cortical neuron apoptosis. J Neurochem 2001; 77:849-863.
    • (2001) J Neurochem , vol.77 , pp. 849-863
    • Bozyczko-Coyne, D.1    O'Kane, T.M.2    Wu, Z.L.3
  • 76
    • 0346753589 scopus 로고    scopus 로고
    • BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo
    • Sugioka R, Shimizu S, Funatsu T, et al. BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo. Oncogene 2002; 22:8432-8440.
    • (2002) Oncogene , vol.22 , pp. 8432-8440
    • Sugioka, R.1    Shimizu, S.2    Funatsu, T.3
  • 77
    • 0036677312 scopus 로고    scopus 로고
    • Mitochondrial permeability transition mediates apoptosis induced by N-methyl(R)salsolinol,an endogenous neurotoxin, and its inhibited by Bcl-2 and rasa-giline, N-propargyl-1(R)-aminoindan
    • Akao Y, Maruyama W, Shimizu S, et al. Mitochondrial permeability transition mediates apoptosis induced by N-methyl(R)salsolinol,an endogenous neurotoxin, and its inhibited by Bcl-2 and rasa-giline, N-propargyl-1(R)-aminoindan. J Neurochem 2002; 82: 913-923.
    • (2002) J Neurochem , vol.82 , pp. 913-923
    • Akao, Y.1    Maruyama, W.2    Shimizu, S.3
  • 78
    • 0037147130 scopus 로고    scopus 로고
    • K252a and CEP1347 are neuroprotective compounds that inhibit mixed-lineage kinase-3 and induce activation of Akt and ERK
    • Roux PP, Dorval G, Boudreau M, et al. K252a and CEP1347 are neuroprotective compounds that inhibit mixed-lineage kinase-3 and induce activation of Akt and ERK. J Biol Chem 2002; 277: 49473-49480.
    • (2002) J Biol Chem , vol.277 , pp. 49473-49480
    • Roux, P.P.1    Dorval, G.2    Boudreau, M.3
  • 79
    • 0038380524 scopus 로고    scopus 로고
    • Inhibition of cal-pains prevents neuronal and behavioral deficits in an MPTP mouse model of Parkinson's disease
    • Crocker SJ, Smith PD, Jackson-Lewis V, et al. Inhibition of cal-pains prevents neuronal and behavioral deficits in an MPTP mouse model of Parkinson's disease. J Neurosci 2003; 23: 4081-4091.
    • (2003) J Neurosci , vol.23 , pp. 4081-4091
    • Crocker, S.J.1    Smith, P.D.2    Jackson-Lewis, V.3
  • 80
    • 5144225191 scopus 로고    scopus 로고
    • A novel systematicallyactive caspase inhibitor attenuates the toxicities of MPTP,malonate, and 3NP in vivo
    • Yang L, Sugama S, Mischak RP, et al. A novel systematicallyactive caspase inhibitor attenuates the toxicities of MPTP,malonate, and 3NP in vivo. Neurobiol Dis 2004; 17: 250-259.
    • (2004) Neurobiol Dis , vol.17 , pp. 250-259
    • Yang, L.1    Sugama, S.2    Mischak, R.P.3
  • 81
    • 2442638936 scopus 로고    scopus 로고
    • Neuroprotective effectsof a novel poly(ADP-Ribose) polymerase-1 inhibitor, 2-{3- [4-(4-chlorophenyl)- 1-piperazinyl]propyl}-4(3H)-quinazolinone(FR255595), in an in vitro model of cell death and in mouse 1-methyl-1,2,3,6-tetrahydropyridine model of Parkinson's disease
    • Iwashita A, Yamazaki S, Mihara K, et al. Neuroprotective effectsof a novel poly(ADP-Ribose) polymerase-1 inhibitor, 2-{3- [4-(4-chlorophenyl)- 1-piperazinyl]propyl}-4(3H)-quinazolinone(FR255595), in an in vitro model of cell death and in mouse 1-methyl-1,2,3,6-tetrahydropyridine model of Parkinson's disease. J Pharmacol Exper Ther 2004; 309: 1067-1078.
    • (2004) J Pharmacol Exper Ther , vol.309 , pp. 1067-1078
    • Iwashita, A.1    Yamazaki, S.2    Mihara, K.3
  • 82
    • 36348979372 scopus 로고    scopus 로고
    • K252a prevents nigral dopaminergic cell death induced by 6-hydroxydopamine trough inhibition of both mixed-lineage kinase 3/c-Jun NH2-terminal kinase 3 (JNK3) and apoptosis-inducing kinase 1/JNK3 signaling pathways
    • Pan J, Wang G, Yang HQ, et al. K252a prevents nigral dopaminergic cell death induced by 6-hydroxydopamine trough inhibition of both mixed-lineage kinase 3/c-Jun NH2-terminal kinase 3 (JNK3) and apoptosis-inducing kinase 1/JNK3 signaling pathways. Mol Pharmacol 2007; 72: 1607-1618.
    • (2007) Mol Pharmacol , vol.72 , pp. 1607-1618
    • Pan, J.1    Wang, G.2    Yang, H.Q.3
  • 83
    • 34548101125 scopus 로고    scopus 로고
    • Neuro-protective effect of protein kinase C inhibitor rottlerin in cell cul-ture and animal models of Parkinson's disease
    • Zhang D, Anantharam V, Kanthasamy A, Kanthasamy AG. Neuro-protective effect of protein kinase C inhibitor rottlerin in cell cul-ture and animal models of Parkinson's disease. J Pharmacol Exp Ther 2007; 322: 913-922.
    • (2007) J Pharmacol Exp Ther , vol.322 , pp. 913-922
    • Zhang, D.1    Anantharam, V.2    Kanthasamy, A.3    Kanthasamy, A.G.4
  • 84
    • 58149393845 scopus 로고    scopus 로고
    • Selective activation of p38 mitogen-activated protein kinase in dopaminergic neurons of substantia nigra leads to nuclear translocation of p53 in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine treated mice
    • Karunakaran S, Saeed U, Mishra M, et al. Selective activation of p38 mitogen-activated protein kinase in dopaminergic neurons of substantia nigra leads to nuclear translocation of p53 in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine treated mice. J Neuro sci 2008;28: 1250-1259.
    • (2008) J Neuro Sci , vol.28 , pp. 1250-1259
    • Karunakaran, S.1    Saeed, U.2    Mishra, M.3
  • 85
    • 67149144477 scopus 로고    scopus 로고
    • Caspases as the rapeutic targets in Alzheimer'sdisease: Is it time to "cut" to the chase?
    • Rohn TT, Head E. Caspases as the rapeutic targets in Alzheimer'sdisease: Is it time to "cut" to the chase? Int J Clin Exp Pathol 2009;2: 108-118.
    • (2009) Int J Clin Exp Pathol , vol.2 , pp. 108-118
    • Rohn, T.T.1    Head, E.2
  • 86
    • 0014314486 scopus 로고
    • Some observations upon a new inhibitors of mono-amine oxidase in brain tissue
    • Johnston JP. Some observations upon a new inhibitors of mono-amine oxidase in brain tissue. Biochem Pharmacol 1968; 17: 1285-1297.
    • (1968) Biochem Pharmacol , vol.17 , pp. 1285-1297
    • Johnston, J.P.1
  • 87
    • 0015274536 scopus 로고
    • Some puzzling pharmacological effects of monoamine oxidase inhibitors
    • Knoll J, Magyar K. Some puzzling pharmacological effects of monoamine oxidase inhibitors. Adv Biochem Psychopharmacol 1972; 5: 393-408.
    • (1972) Adv Biochem Psychopharmacol , vol.5 , pp. 393-408
    • Knoll, J.1    Magyar, K.2
  • 88
    • 0347415718 scopus 로고    scopus 로고
    • Cloning, after cloning, knock-out mice, and physiologicalfunctions of MAO A and B
    • Shih JC. Cloning, after cloning, knock-out mice, and physiologicalfunctions of MAO A and B. Neuro Toxicol 2004; 25: 21-30.
    • (2004) Neuro Toxicol , vol.25 , pp. 21-30
    • Shih, J.C.1
  • 89
    • 0024437481 scopus 로고
    • HeinsenH, Beckmann H. Ontogenesis of monoamine oxidase-A and -B in the human brain frontal cortex
    • Kornhuber J, Konradi C, Mack-Burkhardt F, Riederer P, HeinsenH, Beckmann H. Ontogenesis of monoamine oxidase-A and -B in the human brain frontal cortex. Brain Res 1989: 499: 81-86.
    • (1989) Brain Res , vol.499 , pp. 81-86
    • Kornhuber, J.1    Konradi, C.2    Mack-Burkhardt, F.3    Riederer, P.4
  • 90
    • 0030768730 scopus 로고    scopus 로고
    • Age-related increases inbrain monoamine oxidase B in living healthy human subjects
    • Fowler JS, Volkow ND, Wang GJ, et al. Age-related increases inbrain monoamine oxidase B in living healthy human subjects. Neu-robiol Aging 1997; 18: 431-435.
    • (1997) Neu-robiol Aging , vol.18 , pp. 431-435
    • Fowler, J.S.1    Volkow, N.D.2    Wang, G.J.3
  • 91
    • 4644285991 scopus 로고    scopus 로고
    • Perspectives on MAO-B in aging and neurological disease: Where do we go from here?
    • Kumar MJ, Andersen JK. Perspectives on MAO-B in aging and neurological disease: where do we go from here? Mol Neurobiol 2004; 30: 77-89.
    • (2004) Mol Neurobiol , vol.30 , pp. 77-89
    • Kumar, M.J.1    Andersen, J.K.2
  • 92
    • 0024273128 scopus 로고
    • PlateletMAO-B activity and the psycopathology of Parkinson's disease,senile dementia and multi-infarct dementia
    • Danielczyk W, Steifler M, Konradi C, Riederer P, Moll G. PlateletMAO-B activity and the psycopathology of Parkinson's disease,senile dementia and multi-infarct dementia. Acta Psychiatr Scand 1988; 78: 730-736.
    • (1988) Acta Psychiatr Scand , vol.78 , pp. 730-736
    • Danielczyk, W.1    Steifler, M.2    Konradi, C.3    Riederer, P.4    Moll, G.5
  • 93
    • 19944429347 scopus 로고    scopus 로고
    • Oxidative stress relatedmarkers in the "VITA" and the centenarian projects
    • Grünblatt E, Schösser R, Fischer P, et al. Oxidative stress relatedmarkers in the "VITA" and the centenarian projects. Neurobiol Ageing 2005; 26: 429-438.
    • (2005) Neurobiol Ageing , vol.26 , pp. 429-438
    • Grünblatt, E.1    Schösser, R.2    Fischer, P.3
  • 94
    • 0021182244 scopus 로고
    • Pargyline prevents MPTP-induced parkinsonism in primates
    • Langston JW, Irwin I, Langston EB, Forna LS. Pargyline prevents MPTP-induced parkinsonism in primates. Science 1984; 225:1480-1482.
    • (1984) Science , vol.225 , pp. 1480-1482
    • Langston, J.W.1    Irwin, I.2    Langston, E.B.3    Forna, L.S.4
  • 95
    • 0030895917 scopus 로고    scopus 로고
    • Association of a polymor-phism in intron 13 of the monoamine oxidase B gene with Parkinson disease
    • Costa P, Checkoway H, Levy D, et al. Association of a polymor-phism in intron 13 of the monoamine oxidase B gene with Parkinson disease. Am J Med Genet 1997; 74: 154-216.
    • (1997) Am J Med Genet , vol.74 , pp. 154-216
    • Costa, P.1    Checkoway, H.2    Levy, D.3
  • 96
    • 0032543437 scopus 로고    scopus 로고
    • Detection and analysisof four polymorphic markers at the human monoamine oxidase(MAO) gene in Japanese controls and patients with Parkinson'sdisease
    • Nakamoto M, Tun Z, Shimada S, Honda K. Detection and analysisof four polymorphic markers at the human monoamine oxidase(MAO) gene in Japanese controls and patients with Parkinson'sdisease. Biochem Biophys Res Commun 1998; 247: 452-456.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 452-456
    • Nakamoto, M.1    Tun, Z.2    Shimada, S.3    Honda, K.4
  • 97
    • 33846438189 scopus 로고    scopus 로고
    • Family-based case-control study of MAOA and MAOB polymorphisms in Parkinson's disease
    • Kang SJ, Scott WK, Li YJ, et al. Family-based case-control study of MAOA and MAOB polymorphisms in Parkinson's disease. Mov Disord 2006; 21: 2175-2180.
    • (2006) Mov Disord , vol.21 , pp. 2175-2180
    • Kang, S.J.1    Scott, W.K.2    Li, Y.J.3
  • 98
    • 38949087864 scopus 로고    scopus 로고
    • Gene-gene interaction between EGF20 and MAOB in Parkinson's disease
    • Gao X, Scott WK, Wang G, et al. Gene-gene interaction between EGF20 and MAOB in Parkinson's disease. Ann Hum Genet 2008;72 (Pt 2): 157-162.
    • (2008) Ann Hum Genet , vol.72 , Issue.Pt 2 , pp. 157-162
    • Gao, X.1    Scott, W.K.2    Wang, G.3
  • 99
    • 0020963274 scopus 로고
    • Biochemical changes in dementia disorders of Alzheimer type (AD/SDAT)
    • Gottfries CG, Adoldsson R, Aquilonius SM, et al. Biochemical changes in dementia disorders of Alzheimer type (AD/SDAT).Neurobiol Aging 1983; 4: 261-271.
    • (1983) Neurobiol Aging , vol.4 , pp. 261-271
    • Gottfries, C.G.1    Adoldsson, R.2    Aquilonius, S.M.3
  • 100
    • 0037150797 scopus 로고    scopus 로고
    • Increased monoamine oxidase messenger RNA expres-sion levels in frontal cortex of Alzheimer's disease patients
    • Emilsson L, Saertre P, Balciuniene J, Castensson A, Cairns N, Jazin EE. Increased monoamine oxidase messenger RNA expres-sion levels in frontal cortex of Alzheimer's disease patients. Neu-rosci Lett 2002; 326: 56-60.
    • (2002) Neu-rosci Lett , vol.326 , pp. 56-60
    • Emilsson, L.1    Saertre, P.2    Balciuniene, J.3    Castensson, A.4    Cairns, N.5    Jazin, E.E.6
  • 101
    • 0037135289 scopus 로고    scopus 로고
    • Association of mono-amine oxidase A gene polymorphism with Alzheimer's disease andLewy body variant
    • Takehashi M, Tanaka S, Masliah E, Ueda K. Association of mono-amine oxidase A gene polymorphism with Alzheimer's disease andLewy body variant. Neurosci Lett 2002; 327: 79-82.
    • (2002) Neurosci Lett , vol.327 , pp. 79-82
    • Takehashi, M.1    Tanaka, S.2    Masliah, E.3    Ueda, K.4
  • 102
    • 34548125005 scopus 로고    scopus 로고
    • A promotor polymorphism in the monoamine oxidase gene is associated with the pineal MAOA activity in Alzheimer's disease patients
    • Wu YH, Fischer DF, Swaab DF. A promotor polymorphism in the monoamine oxidase gene is associated with the pineal MAOA activity in Alzheimer's disease patients. Brain Res 2007; 1167: 13-19.
    • (2007) Brain Res , vol.1167 , pp. 13-19
    • Wu, Y.H.1    Fischer, D.F.2    Swaab, D.F.3
  • 103
    • 0346732361 scopus 로고    scopus 로고
    • Molecular changes under-lying pineal melatonin levels in Alzheimer disease: Alterations inpreclinical and clinical stages
    • Wu YH, Feenstra MGP, Zhou JN, et al. Molecular changes under-lying pineal melatonin levels in Alzheimer disease: alterations inpreclinical and clinical stages. J Clin Endocrinol Metab 2003; 88:5898-5906.
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 5898-5906
    • Wu, Y.H.1    Feenstra, M.G.P.2    Zhou, J.N.3
  • 104
    • 0029891783 scopus 로고    scopus 로고
    • A dopaminergic neurotoxin, (R)-N-methylsalsolinol, increases in parkinsonian cerebrospinal fluid
    • Maruyama W, Abe T, Tohgi H, Dostert P, Naoi M. A dopaminergic neurotoxin, (R)-N-methylsalsolinol, increases in parkinsonian cerebrospinal fluid. Ann Neurol 1996; 40: 119-122.
    • (1996) Ann Neurol , vol.40 , pp. 119-122
    • Maruyama, W.1    Abe, T.2    Tohgi, H.3    Dostert, P.4    Naoi, M.5
  • 105
    • 0030957199 scopus 로고    scopus 로고
    • An endogenous dopa-minergic neurotoxin, N-methyl-(R)-salsolinol, induces DNA dam-age in human dopaminergic neuroblastoma SH-SY5Y cells
    • Maruyama W, Naoi M, Kasamatsu T, et al. An endogenous dopa-minergic neurotoxin, N-methyl-(R)-salsolinol, induces DNA dam-age in human dopaminergic neuroblastoma SH-SY5Y cells. J Neu-rochem 1997; 69: 322-329.
    • (1997) J Neu-rochem , vol.69 , pp. 322-329
    • Maruyama, W.1    Naoi, M.2    Kasamatsu, T.3
  • 106
    • 0030060483 scopus 로고    scopus 로고
    • Dopamine-derived en-dogenous 1(R),2(N)-dimethyl-6,7- dihydroxy-1,2,3,4-tetrahydroiso-quinoline, N-methyl-(R)-salsolinol, induced parkinsonism in rat:Biochemical, pathological and behavioral studies
    • Naoi M, Maruyama W, Dostert P, et al. Dopamine-derived en-dogenous 1(R),2(N)-dimethyl-6,7- dihydroxy-1,2,3,4-tetrahydroiso-quinoline, N-methyl-(R)-salsolinol, induced parkinsonism in rat:biochemical, pathological and behavioral studies. Brain Res 1996;709: 285-295.
    • (1996) Brain Res , vol.709 , pp. 285-295
    • Naoi, M.1    Maruyama, W.2    Dostert, P.3
  • 107
    • 33644874108 scopus 로고    scopus 로고
    • Type A monoamine oxidase is the target of an endogenous dopaminergicneurotoxin, N-methyl(R)salsolinol, leading to apoptosis in SH-SY5Y cells
    • Yi H, Akao Y, Maruyama W, Chen K, Shih J, Naoi M. Type A monoamine oxidase is the target of an endogenous dopaminergicneurotoxin, N-methyl(R)salsolinol, leading to apoptosis in SH-SY5Y cells. J Neurochem 2006; 96: 541-549.
    • (2006) J Neurochem , vol.96 , pp. 541-549
    • Yi, H.1    Akao, Y.2    Maruyama, W.3    Chen, K.4    Shih, J.5    Naoi, M.6
  • 108
    • 70449536507 scopus 로고    scopus 로고
    • Mitochondria in neurodegenerative disorders: Regulation of the redox state and death signaling leading to neuronal death and survival
    • Naoi M, Maruyama W, Yi H, Inaba K, Akao Y, Shamoto-Nagai M.Mitochondria in neurodegenerative disorders: regulation of the redox state and death signaling leading to neuronal death and survival. J Neural Transm 2009; 116: 1371-1381.
    • (2009) J Neural Transm , vol.116 , pp. 1371-1381
    • Naoi, M.1    Maruyama, W.2    Yi, H.3    Inaba, K.4    Akao, Y.5    Shamoto-Nagai, M.6
  • 109
    • 33746639596 scopus 로고    scopus 로고
    • Monoamine oxidase A and repressor R1 are involved in apoptotic signaling pathway
    • Ou X-M, Chen Km, Shih JC. Monoamine oxidase A and repressor R1 are involved in apoptotic signaling pathway. Proc Natl Acad Sci USA 2006; 103: 10923-10928.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10923-10928
    • Ou, X.-M.1    Chen, K.2    Shih, J.C.3
  • 110
    • 0002063208 scopus 로고
    • Clinical experience with iproniazid (marsilid)
    • Kline NS. Clinical experience with iproniazid (marsilid). J Clin Exp Psychopathol 1958; 19 (2, suppl 1): 72-78.
    • (1958) J Clin Exp Psychopathol , vol.19 , Issue.2 SUPPL 1 , pp. 72-78
    • Kline, N.S.1
  • 111
    • 0014189254 scopus 로고
    • Clinical trial of a new type promptly psychoergetic agent (phenyl-isopropyl-methylpropinyl-HCl, "E-250")
    • Verga E, Tringer L. Clinical trial of a new type promptly psychoergetic agent (phenyl-isopropyl-methylpropinyl-HCl, "E-250"). Acta Med Acad Sci Hung 1967; 23: 289-295.
    • (1967) Acta Med Acad Sci Hung , vol.23 , pp. 289-295
    • Verga, E.1    Tringer, L.2
  • 113
    • 0032932706 scopus 로고    scopus 로고
    • Meta-analysis of the reversi-ble inhibitors of monoamine oxidase type A moclobemide and bro-faromine for the treatment of depression
    • Lotufo-Neto F, Trivedi M, Thase ME. Meta-analysis of the reversi-ble inhibitors of monoamine oxidase type A moclobemide and bro-faromine for the treatment of depression. Neuropsychopharmacol 1999; 20: 226-247.
    • (1999) Neuropsychopharmacol , vol.20 , pp. 226-247
    • Lotufo-Neto, F.1    Trivedi, M.2    Thase, M.E.3
  • 114
    • 28444470835 scopus 로고    scopus 로고
    • MAOI efficacy and safety in advanced stage treatment-resistant depression - a retrospective study
    • Amsterdam JD, Shults J. MAOI efficacy and safety in advanced stage treatment-resistant depression - a retrospective study. J Affect Disord 2005; 89: 183-188.
    • (2005) J Affect Disord , vol.89 , pp. 183-188
    • Amsterdam, J.D.1    Shults, J.2
  • 115
    • 0016414699 scopus 로고
    • The potentiation of the anti akinetic effects after L-dopa treatment by inhibitorof MAO-B, deprenyl
    • Birkmayer W, Riederer P, Youdim MB, Linauer W. The potentiation of the anti akinetic effects after L-dopa treatment by inhibitorof MAO-B, deprenyl. J Neural Transm 1975; 36: 303-326.
    • (1975) J Neural Transm , vol.36 , pp. 303-326
    • Birkmayer, W.1    Riederer, P.2    Youdim, M.B.3    Linauer, W.4
  • 116
    • 0017345412 scopus 로고
    • Implicationsof combined treatment with Madopar and l-deprenyl in Parkinson'sdisease. A long-term study
    • Birkmayer W, Riederer P, Ambrozi L, Youdim MBH. Implicationsof combined treatment with Madopar and l-deprenyl in Parkinson'sdisease. A long-term study. Lancet 1977; 1(8009): 439-443.
    • (1977) Lancet , vol.1 , Issue.8009 , pp. 439-443
    • Birkmayer, W.1    Riederer, P.2    Ambrozi, L.3    Youdim, M.B.H.4
  • 117
    • 0346728595 scopus 로고    scopus 로고
    • Deprenyl, a selective MAO-B inhibitor,with apoptotic and anti-apoptotic properties
    • Magyar K, Szende B. Deprenyl, a selective MAO-B inhibitor,with apoptotic and anti-apoptotic properties. Neuro Toxicol 2004;25: 233-242.
    • (2004) Neuro Toxicol , vol.25 , pp. 233-242
    • Magyar, K.1    Szende, B.2
  • 118
    • 33750858897 scopus 로고    scopus 로고
    • Therapeutic efficiency ofselegiline in neurodegenerative disorders and neurological diseases
    • Ebadi M, Brown-Borg H, Ren A, et al. Therapeutic efficiency ofselegiline in neurodegenerative disorders and neurological diseases.Curr Drug Targets 2006; 7: 1513-1529.
    • (2006) Curr Drug Targets , vol.7 , pp. 1513-1529
    • Ebadi, M.1    Brown-Borg, H.2    Ren, A.3
  • 119
    • 0031019340 scopus 로고    scopus 로고
    • Hydroxyl and peroxyl radical trapping by the monoamine oxidase-B inhibitors deprenyland MDL 72,974A: Implications for protection of biological sub-strates
    • Thomas CE, Huber EW, Ohlweiler DF. Hydroxyl and peroxyl radical trapping by the monoamine oxidase-B inhibitors deprenyland MDL 72,974A: implications for protection of biological sub-strates. Free Radic Biol Med 1997; 22: 733-737.
    • (1997) Free Radic Biol Med , vol.22 , pp. 733-737
    • Thomas, C.E.1    Huber, E.W.2    Ohlweiler, D.F.3
  • 120
    • 0026074120 scopus 로고
    • Deprenyl induces activities of both superoxide dismutase and catalase but not of glutathione peroxidase in the striatum of young male rats
    • Carrillo MC, Kanai S, Nokubo M, Kitani K. Deprenyl induces activities of both superoxide dismutase and catalase but not of glutathione peroxidase in the striatum of young male rats. Life Sci1 1991; 48: 517-521.
    • (1991) Life Sci1 , vol.48 , pp. 517-521
    • Carrillo, M.C.1    Kanai, S.2    Nokubo, M.3    Kitani, K.4
  • 121
    • 27544468505 scopus 로고    scopus 로고
    • Role of the redoxprotein thioredoxin in cytoprotective mechanism evoked by deprenyl
    • Andoh T, Chock PB, Murphy DL, Chiueh CC. Role of the redoxprotein thioredoxin in cytoprotective mechanism evoked by deprenyl. Mol Pharmacol 2005; 68: 1408-1414.
    • (2005) Mol Pharmacol , vol.68 , pp. 1408-1414
    • Andoh, T.1    Chock, P.B.2    Murphy, D.L.3    Chiueh, C.C.4
  • 122
    • 0019951174 scopus 로고
    • The contri-bution of amphetamine metabolites of deprenyl to its antipark-insonian properties
    • Elsworth JD, Sandler M, Lees AJ, Ward C, Stern GM. The contri-bution of amphetamine metabolites of deprenyl to its antipark-insonian properties. J Neural Transm 1982: 54: 105-110.
    • (1982) J Neural Transm , vol.54 , pp. 105-110
    • Elsworth, J.D.1    Sandler, M.2    Lees, A.J.3    Ward, C.4    Stern, G.M.5
  • 123
    • 33645131794 scopus 로고    scopus 로고
    • Metabolic transformation playsa primary role in the psychostimulant-like discriminative-stimuluseffects of selegiline [(R)-deprenyl]
    • Yasar S, Justinova Z, Lee SH, et al. Metabolic transformation playsa primary role in the psychostimulant-like discriminative-stimuluseffects of selegiline [(R)-deprenyl]. J Pharmacol Exp Ther 2006; 317: 387-394.
    • (2006) J Pharmacol Exp Ther , vol.317 , pp. 387-394
    • Yasar, S.1    Justinova, Z.2    Lee, S.H.3
  • 124
    • 0024267460 scopus 로고
    • The striatal dopamine dependency of life span in male rats:Longevity study with deprenyl
    • Knoll J. The striatal dopamine dependency of life span in male rats:longevity study with deprenyl. Mech Age Dev 1988; 46: 237-262.
    • (1988) Mech Age Dev , vol.46 , pp. 237-262
    • Knoll, J.1
  • 125
    • 0027455791 scopus 로고
    • Chronic treatment of deprenyl prolongs the life span in male Fischer 344 rats: Further evidence
    • Kitani K, Kanai S, Sato Y, Ohta M, Ivy GO, Carrillo MC. Chronic treatment of deprenyl prolongs the life span in male Fischer 344 rats: Further evidence. Life Sci 1993; 52: 281-288.
    • (1993) Life Sci , vol.52 , pp. 281-288
    • Kitani, K.1    Kanai, S.2    Sato, Y.3    Ohta, M.4    Ivy, G.O.5    Carrillo, M.C.6
  • 126
    • 0030300160 scopus 로고    scopus 로고
    • The pharmacology of B-type selective monoamine oxidase inhibitors: Milestones in deprenyl research
    • Magyar K, Szende B, Lemgyel J, Tekes K. The pharmacology of B-type selective monoamine oxidase inhibitors: milestones in deprenyl research. J Neural Transm 1996; (Suppl 48): 29-43.
    • (1996) J Neural Transm , Issue.SUPPL. 48 , pp. 29-43
    • Magyar, K.1    Szende, B.2    Lemgyel, J.3    Tekes, K.4
  • 127
    • 0019462668 scopus 로고
    • Tyramine antagonistic properties of AGN 1135 - an irreversible inhibitor of monoamine oxidase type B
    • Finberg JPM, Tenne M, Youdim MBH. Tyramine antagonistic properties of AGN 1135 - an irreversible inhibitor of monoamine oxidase type B. Br J Pharmacol 1981; 73: 65-64.
    • (1981) Br J Pharmacol , vol.73 , pp. 65-64
    • Finberg, J.P.M.1    Tenne, M.2    Youdim, M.B.H.3
  • 129
    • 0035130289 scopus 로고    scopus 로고
    • Rasagiline [N-propargyl-1R(+)-aminoindan], a selective and potent inhibitor of mitochon-drial monoamine oxidase B
    • Youdim MBH, Gross A, Finberg JPM. Rasagiline [N-propargyl-1R(+)-aminoindan], a selective and potent inhibitor of mitochon-drial monoamine oxidase B. Br J Pharmacol 2001; 132: 500-506.
    • (2001) Br J Pharmacol , vol.132 , pp. 500-506
    • Youdim, M.B.H.1    Gross, A.2    Finberg, J.P.M.3
  • 130
    • 0031596704 scopus 로고    scopus 로고
    • Chronic TVP-1012(rasagiline) dose-activity response of monoamine oxidases A and B in the brain of the common marmoset
    • Götz ME, Breithaupt W, Sautter J, et al. Chronic TVP-1012(rasagiline) dose-activity response of monoamine oxidases A and B in the brain of the common marmoset. J Neural Transm 1998;Suppl 52: 271-278.
    • (1998) J Neural Transm , Issue.SUPPL. 52 , pp. 271-278
    • Götz, M.E.1    Breithaupt, W.2    Sautter, J.3
  • 131
    • 0032729260 scopus 로고    scopus 로고
    • Inversion of selectivity of N-substituted propar-gylamine oxidase inhibitors following structural modifications toquaternary salts
    • Yu PH, Davis BA. Inversion of selectivity of N-substituted propar-gylamine oxidase inhibitors following structural modifications toquaternary salts. Int J Biochem Cell Biol 1999; 31: 1391-1397.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1391-1397
    • Yu, P.H.1    Davis, B.A.2
  • 133
    • 0028057394 scopus 로고
    • Neurochemical and neuroprotective effects of some aliphatic propargylamines: New selective nonamphetamine-like monoamine oxidase B inhibitors
    • Yu PH, Davis BA, Durden DA, Terleckyj I, Nicklas WG, Boulton AA. Neurochemical and neuroprotective effects of some aliphatic propargylamines: New selective nonamphetamine-like monoamine oxidase B inhibitors. J Neuro chem 1994; 62: 697-704.
    • (1994) J Neuro Chem , vol.62 , pp. 697-704
    • Yu, P.H.1    Davis, B.A.2    Durden, D.A.3    Terleckyj, I.4    Nicklas, W.G.5    Boulton, A.A.6
  • 134
    • 0022378166 scopus 로고
    • Preven-tion of MPTP-induced neurotoxicity by AGN-1133 and AGN-1135, selective inhibitors of monoamine oxidase-B
    • Heikkila RE, Duvoisin RC, Finberg JPM, Youdim MBH. Preven-tion of MPTP-induced neurotoxicity by AGN-1133 and AGN-1135, selective inhibitors of monoamine oxidase-B. Eur J Pharma-col 1985; 16: 313-317.
    • (1985) Eur J Pharma-col , vol.16 , pp. 313-317
    • Heikkila, R.E.1    Duvoisin, R.C.2    Finberg, J.P.M.3    Youdim, M.B.H.4
  • 135
    • 0032722119 scopus 로고    scopus 로고
    • The effect of a sub-chronic post-lesion treatment with deprenyl on the sensitivity of6-OHDA-lesioned rats to apomorphine and d-amphetamine
    • Spooren WPJM, Walsmeier P, Gentsch C. The effect of a sub-chronic post-lesion treatment with deprenyl on the sensitivity of6-OHDA-lesioned rats to apomorphine and d-amphetamine J Neu-ral Transm 1999; 106: 825-833.
    • (1999) J Neu-ral Transm , vol.106 , pp. 825-833
    • Spooren, W.P.J.M.1    Walsmeier, P.2    Gentsch, C.3
  • 136
    • 0034871806 scopus 로고    scopus 로고
    • Monoamine oxidase-inhibitionand MPTP-induced neurotoxicity in the non-human primate: Com-parison of rasagiline (TVP1012) with selegiline
    • Kupsch A, Sautter J, Götz ME et al. Monoamine oxidase-inhibitionand MPTP-induced neurotoxicity in the non-human primate: com-parison of rasagiline (TVP1012) with selegiline. J Neural Transm 2001; 108: 985-1009.
    • (2001) J Neural Transm , vol.108 , pp. 985-1009
    • Kupsch, A.1    Sautter, J.2    Götz, M.E.3
  • 137
    • 0025171524 scopus 로고
    • Pro-tection against DSP-4-induced neurotoxicity by deprenyl is not re-layed to its inhibition of MAO B
    • Finnegan KT, Skratt JJ, Irwin I, DeLanney LE, Langston JW. Pro-tection against DSP-4-induced neurotoxicity by deprenyl is not re-layed to its inhibition of MAO B. Eur J Pharmacol 1990; 184: 119-126.
    • (1990) Eur J Pharmacol , vol.184 , pp. 119-126
    • Finnegan, K.T.1    Skratt, J.J.2    Irwin, I.3    Delanney, L.E.4    Langston, J.W.5
  • 138
    • 0028020079 scopus 로고
    • Neuroprotective effects ofsome monoamine oxidase-B inhibitors against DSP-4-inducednoradrenaline depletion in the mouse hippocampus
    • Yu PH, Davis BA, Fang J, Boulton AA. Neuroprotective effects ofsome monoamine oxidase-B inhibitors against DSP-4-inducednoradrenaline depletion in the mouse hippocampus. J Neurochem 1994; 63: 1820-1828.
    • (1994) J Neurochem , vol.63 , pp. 1820-1828
    • Yu, P.H.1    Davis, B.A.2    Fang, J.3    Boulton, A.A.4
  • 139
    • 0026492963 scopus 로고
    • Deficitsin cholinergic neurotransmission markers induced by ethylcholinemustard aziridinium (AF64A) in the rat hippocampus: Sensitivity totreatment with the monoamine oxidase-B inhibitor L-deprenyl
    • Ricci A, Mancini M, Strocchi P, Bongrani S, Bronzetti E. Deficitsin cholinergic neurotransmission markers induced by ethylcholinemustard aziridinium (AF64A) in the rat hippocampus: sensitivity totreatment with the monoamine oxidase-B inhibitor L-deprenyl.Drugs Exp Clin Res 1992; 18: 163-171.
    • (1992) Drugs Exp Clin Res , vol.18 , pp. 163-171
    • Ricci, A.1    Mancini, M.2    Strocchi, P.3    Bongrani, S.4    Bronzetti, E.5
  • 140
    • 0032101092 scopus 로고    scopus 로고
    • Sparing byrasagiline (TVP-1012) of cholinergic functions and behavior in thepostnatal anoxia rat
    • Speiser Z, Katzir O, Rehavi M, Zabarski T, Cohen S. Sparing byrasagiline (TVP-1012) of cholinergic functions and behavior in thepostnatal anoxia rat. Pharmacol Biochem Behav 1998; 60: 378-393.
    • (1998) Pharmacol Biochem Behav , vol.60 , pp. 378-393
    • Speiser, Z.1    Katzir, O.2    Rehavi, M.3    Zabarski, T.4    Cohen, S.5
  • 141
    • 0032960868 scopus 로고    scopus 로고
    • Neuronal sparing and behavioral effectsof the antiapoptotic dug, (-)deprenyl, following kainic acid admini-stration
    • Gelowitz DL, Paterson IA. Neuronal sparing and behavioral effectsof the antiapoptotic dug, (-)deprenyl, following kainic acid admini-stration. Pharmacol Biochem Behav 1999; 62: 255-262.
    • (1999) Pharmacol Biochem Behav , vol.62 , pp. 255-262
    • Gelowitz, D.L.1    Paterson, I.A.2
  • 142
    • 0032999575 scopus 로고    scopus 로고
    • Neuroprotectiveeffect of rasagiline, a selective monoamine oxidase-B inhibitor,against closed head injury in the mouse
    • Huang W, Chen Y, Shohami E, Weinstock M. Neuroprotectiveeffect of rasagiline, a selective monoamine oxidase-B inhibitor,against closed head injury in the mouse. Eur J Pharmacol 1999;366: 127-135.
    • (1999) Eur J Pharmacol , vol.366 , pp. 127-135
    • Huang, W.1    Chen, Y.2    Shohami, E.3    Weinstock, M.4
  • 143
    • 41149124377 scopus 로고    scopus 로고
    • Rasagiline is neuroprotective in a transgenic model of multiple system atrophy
    • Stefanova N, Poewe W, Wenning GK. Rasagiline is neuroprotective in a transgenic model of multiple system atrophy. Exp Neurol 2008; 210: 421-427.
    • (2008) Exp Neurol , vol.210 , pp. 421-427
    • Stefanova, N.1    Poewe, W.2    Wenning, G.K.3
  • 144
    • 0027941312 scopus 로고
    • Deprenylreduces PC12 cell apoptosis by inducing new protein synthesis
    • Tatton WG, Ju WYL, Holland D, Tai C, Kwan M. Deprenylreduces PC12 cell apoptosis by inducing new protein synthesis. J Neurochem 1994; 63: 1572-1575.
    • (1994) J Neurochem , vol.63 , pp. 1572-1575
    • Tatton, W.G.1    Ju, W.Y.L.2    Holland, D.3    Tai, C.4    Kwan, M.5
  • 145
    • 0030574241 scopus 로고    scopus 로고
    • Selegiline enhancesNGF synthesis and protects central nervous system neurons fromexcitotoxic and ischemic damage
    • Semkova I, Wolz P, Schilling M, Krieglein J. Selegiline enhancesNGF synthesis and protects central nervous system neurons fromexcitotoxic and ischemic damage. Eur J Pharmacol 1996; 315: 19-30.
    • (1996) Eur J Pharmacol , vol.315 , pp. 19-30
    • Semkova, I.1    Wolz, P.2    Schilling, M.3    Krieglein, J.4
  • 146
    • 0032498811 scopus 로고    scopus 로고
    • In-creased survival of dopaminergic neurons by rasagiline, a mono-amine oxidase B inhibitor
    • Finberg JPM, Takeshima T, Johnston JM, Commissiong JW. In-creased survival of dopaminergic neurons by rasagiline, a mono-amine oxidase B inhibitor. Neuro Report 1998; 9: 703-707.
    • (1998) Neuro Report , vol.9 , pp. 703-707
    • Finberg, J.P.M.1    Takeshima, T.2    Johnston, J.M.3    Commissiong, J.W.4
  • 147
    • 0031886449 scopus 로고    scopus 로고
    • Deprenyl and des-methylselegiline protect mesencephalic neurons from toxicity in-duced by glutathione depletion
    • Mytilieou C, Leonardi EK, Radcliffe P., et al. Deprenyl and des-methylselegiline protect mesencephalic neurons from toxicity in-duced by glutathione depletion. J Pharmcol Exp Therap 1998; 284:700-706.
    • (1998) J Pharmcol Exp Therap , vol.284 , pp. 700-706
    • Mytilieou, C.1    Leonardi, E.K.2    Radcliffe, P.3
  • 148
    • 0036206323 scopus 로고    scopus 로고
    • The anti-parkinson drug, rasagiline, prevents apoptotic DNA damage in-duced by peroxynitrite in human dopaminergic neuroblastoma SH-SY5Y cells
    • Maruyama W, Takahashi T, Youdim M, Naoi M. The anti-parkinson drug, rasagiline, prevents apoptotic DNA damage in-duced by peroxynitrite in human dopaminergic neuroblastoma SH-SY5Y cells. J Neural Transm 2002; 109: 467-481
    • (2002) J Neural Transm , vol.109 , pp. 467-481
    • Maruyama, W.1    Takahashi, T.2    Youdim, M.3    Naoi, M.4
  • 149
    • 0034676515 scopus 로고    scopus 로고
    • Apoptosisinduced by an endogenous neurotoxin, N-methyl(R)salsolinol, indopamine neurons
    • Naoi M, Maruyama W, Akao Y, Zhang J, Parvez H. Apoptosisinduced by an endogenous neurotoxin, N-methyl(R)salsolinol, indopamine neurons. Toxicology 2000; 153: 123-141.
    • (2000) Toxicology , vol.153 , pp. 123-141
    • Naoi, M.1    Maruyama, W.2    Akao, Y.3    Zhang, J.4    Parvez, H.5
  • 150
    • 0037189081 scopus 로고    scopus 로고
    • Youdim MBH,Naoi M. An anti-Parkinson's disease drug, N-propargyl-1(R)-aminoindan (rasagiline), enhances expression of anti-apoptotic Bcl-2 in human dopaminergic SH-SY5Y cells
    • Akao Y, Maruyama W, Yi H, Shamoto-Nagai M, Youdim MBH,Naoi M. An anti-Parkinson's disease drug, N-propargyl-1(R)-aminoindan (rasagiline), enhances expression of anti-apoptotic Bcl-2 in human dopaminergic SH-SY5Y cells. Neurosci Lett 2002;326: 105-108.
    • (2002) Neurosci Lett , vol.326 , pp. 105-108
    • Akao, Y.1    Maruyama, W.2    Yi, H.3    Shamoto-Nagai, M.4
  • 151
    • 34848906324 scopus 로고    scopus 로고
    • Aminoindan and hydroxyami-noindan, metabolites of rasagiline and ladostigil, respectively, exertneuroprotective properties in vitro
    • Bar-Am O, Amit T, Youdim MBH. Aminoindan and hydroxyami-noindan, metabolites of rasagiline and ladostigil, respectively, exertneuroprotective properties in vitro. J Neurochem 2007; 103: 500-508.
    • (2007) J Neurochem , vol.103 , pp. 500-508
    • Bar-Am, O.1    Amit, T.2    Youdim, M.B.H.3
  • 152
    • 16544388655 scopus 로고    scopus 로고
    • Neuroprotective functionof R-(-)1-(benzofuran-2-yl)-2-propyl- aminopentane, [R-BPAP],against apoptosis induced by N-methyl(R)salsolinol, an endogenousdopaminergic neurotoxin, in human dopaminergic neuroblastomaSH-SY5Y cells
    • Maruyama W, Yi H, Takahashi T, et al. Neuroprotective functionof R-(-)1-(benzofuran-2-yl)-2-propyl- aminopentane, [R-BPAP],against apoptosis induced by N-methyl(R)salsolinol, an endogenousdopaminergic neurotoxin, in human dopaminergic neuroblastomaSH-SY5Y cells. Life Sci 2004; 75: 107-117.
    • (2004) Life Sci , vol.75 , pp. 107-117
    • Maruyama, W.1    Yi, H.2    Takahashi, T.3
  • 153
    • 33745614941 scopus 로고    scopus 로고
    • Moclobemide upregulated Bcl-2expression and induced neural stem cell differentiation into sero-tonergic neuron via extracellular-regulated kinase pathway
    • Chiou SH, Ku HH, Tsai TH et al. Moclobemide upregulated Bcl-2expression and induced neural stem cell differentiation into sero-tonergic neuron via extracellular-regulated kinase pathway. Br J Pharmacol 2006; 148: 587-598.
    • (2006) Br J Pharmacol , vol.148 , pp. 587-598
    • Chiou, S.H.1    Ku, H.H.2    Tsai, T.H.3
  • 154
    • 0346848857 scopus 로고    scopus 로고
    • N-Propargyl-1(R)-aminoindan, rasagiline, increases glial cell line-derived neurotro-phic factor (GDNF) in neuroblastoma SH-SY5Y cells through acti-vation of NF- B transcription factor
    • Maruyama W, Nitta A, Shamoto-Nagai M, et al. N-Propargyl-1(R)-aminoindan, rasagiline, increases glial cell line-derived neurotro-phic factor (GDNF) in neuroblastoma SH-SY5Y cells through acti-vation of NF- B transcription factor. Neurochem Int 2004; 44:393-400.
    • (2004) Neurochem Int , vol.44 , pp. 393-400
    • Maruyama, W.1    Nitta, A.2    Shamoto-Nagai, M.3
  • 155
    • 33749010358 scopus 로고    scopus 로고
    • Neurotrophin-regulated signaling pathways
    • Reichardt LF. Neurotrophin-regulated signaling pathways. Phil Trans R Soc B. 2006; 361: 1545-1564.
    • (2006) Phil Trans R Soc B , vol.361 , pp. 1545-1564
    • Reichardt, L.F.1
  • 156
    • 0025993361 scopus 로고
    • Johnson SA,Winslow JW. BDNF mRNA is decreased in the hippocampus ofindividuals with Alzheimer's disease
    • Phillips HS, Hains JM, Armanini M, Laramee GR, Johnson SA,Winslow JW. BDNF mRNA is decreased in the hippocampus ofindividuals with Alzheimer's disease. Neuron 1991; 7: 695-702.
    • (1991) Neuron , vol.7 , pp. 695-702
    • Phillips, H.S.1    Hains, J.M.2    Armanini, M.3    Laramee, G.R.4
  • 157
    • 0033813571 scopus 로고    scopus 로고
    • Neurotrophic factors in Alzheimer's and Parkinson's disease brain
    • Siegel GJ, Chauhan NB. Neurotrophic factors in Alzheimer's and Parkinson's disease brain. Brian Res Rev 2000; 33: 199-227.
    • (2000) Brian Res Rev , vol.33 , pp. 199-227
    • Siegel, G.J.1    Chauhan, N.B.2
  • 158
    • 0036723891 scopus 로고    scopus 로고
    • A new brain-derived neurotrophicfactor transcript and decrease in brain-derived neurotrophic factor transcripts 1, 2 and 3 in Alzheimer's disease parietal cortex
    • Garzon D, Yu G, Fahnestock M. A new brain-derived neurotrophicfactor transcript and decrease in brain-derived neurotrophic factor transcripts 1, 2 and 3 in Alzheimer's disease parietal cortex. J Neu-rochem 2002; 82: 1058-1064.
    • (2002) J Neu-rochem , vol.82 , pp. 1058-1064
    • Garzon, D.1    Yu, G.2    Fahnestock, M.3
  • 159
    • 34547499702 scopus 로고    scopus 로고
    • Dissecting the human BDNF locus: Bidirectional transcription, complex slic-ing, and multiple promoters
    • Pruunsild P, Kazantseva A, Aid T, Palm K, Timmusk T. Dissecting the human BDNF locus: bidirectional transcription, complex slic-ing, and multiple promoters. Genomics 2007; 90: 397-406.
    • (2007) Genomics , vol.90 , pp. 397-406
    • Pruunsild, P.1    Kazantseva, A.2    Aid, T.3    Palm, K.4    Timmusk, T.5
  • 160
    • 67651171367 scopus 로고    scopus 로고
    • Decreased brain-derived neurotrophic factor depends on amyloid aggregation state in transgenic mouse models of Alzheimer's disease
    • Peng S, Garzon DJ, Marchese M, et al. Decreased brain-derived neurotrophic factor depends on amyloid aggregation state in transgenic mouse models of Alzheimer's disease. J Neurosci 2009; 29:9321-9329.
    • (2009) J Neurosci , vol.29 , pp. 9321-9329
    • Peng, S.1    Garzon, D.J.2    Marchese, M.3
  • 161
    • 62049083420 scopus 로고    scopus 로고
    • Neuroprotective effects of brain-derived neurotrophic factor in rodent and primate models of Alzheimer's disease
    • Nagahara AH, Merrill DA, Coppola G, et al. Neuroprotective effects of brain-derived neurotrophic factor in rodent and primate models of Alzheimer's disease. Nat Med 2009; 15: 331-337.
    • (2009) Nat Med , vol.15 , pp. 331-337
    • Nagahara, A.H.1    Merrill, D.A.2    Coppola, G.3
  • 162
    • 70349106433 scopus 로고    scopus 로고
    • Association between BDNF Val66Met polymorphism and Alzheimer disease,dementia with Lewy bodies, and Pick disease
    • Feher A, Juhasz A, Rimanoczy A, Kalman J, Janka Z. Association between BDNF Val66Met polymorphism and Alzheimer disease,dementia with Lewy bodies, and Pick disease. Alzheimer Dis As-soc Disord 2009; 23: 224-228.
    • (2009) Alzheimer Dis As-soc Disord , vol.23 , pp. 224-228
    • Feher, A.1    Juhasz, A.2    Rimanoczy, A.3    Kalman, J.4    Janka, Z.5
  • 163
    • 0035239020 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor in the control human brain, and in Alzheimer's disease and Parkinson's disease
    • 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 2001; 63: 71-124.
    • (2001) Prog Neurobiol , vol.63 , pp. 71-124
    • Murer, M.G.1    Yan, Q.2    Raisman-Vozari, R.3
  • 164
    • 70350495615 scopus 로고    scopus 로고
    • Glialcell-line derived neurotrophic factor (GDNF) concentrations in cerebrospinal fluid and serum of patients with early Alzheimer'sdisease and normal controls
    • Straten G, Eschweiler GW, Maetzler W, Laske C, Leyhe T. Glialcell-line derived neurotrophic factor (GDNF) concentrations in cerebrospinal fluid and serum of patients with early Alzheimer'sdisease and normal controls. J Alzheimer's Dis 2009; 18: 331-337.
    • (2009) J Alzheimer's Dis , vol.18 , pp. 331-337
    • Straten, G.1    Eschweiler, G.W.2    Maetzler, W.3    Laske, C.4    Leyhe, T.5
  • 165
    • 0032125462 scopus 로고    scopus 로고
    • Neurtur in expertspotent actions on survival and functions of midbrain dopaminergic neurons
    • Horger BA, Nishimura MC, Armanini MP, et al., Neurtur in expertspotent actions on survival and functions of midbrain dopaminergic neurons. J Neurosci 1998; 18: 4929-4937.
    • (1998) J Neurosci , vol.18 , pp. 4929-4937
    • Horger, B.A.1    Nishimura, M.C.2    Armanini, M.P.3
  • 167
    • 0142106351 scopus 로고    scopus 로고
    • Novel functions and signaling pathways forGDNF
    • Sariola H, Saarma M. Novel functions and signaling pathways forGDNF. J Cell Sci 2003; 116: 3853-3862.
    • (2003) J Cell Sci , vol.116 , pp. 3853-3862
    • Sariola, H.1    Saarma, M.2
  • 168
    • 33846501598 scopus 로고    scopus 로고
    • GDNF family receptor complexes are emerging drug targets
    • Bespalov MM, Saarma M. GDNF family receptor complexes are emerging drug targets. Trends Pharmacol Sci 2007; 28: 68-74.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 68-74
    • Bespalov, M.M.1    Saarma, M.2
  • 169
    • 0033597817 scopus 로고    scopus 로고
    • Ret-dependent and-independent mechanisms of glial cell line-derived neurotrophic factor signaling in neuronal cells
    • Trupp M, Scott R, Whittermore SR, Ibanez CF. Ret-dependent and-independent mechanisms of glial cell line-derived neurotrophic factor signaling in neuronal cells. J Biol Chem 1999; 274: 20885-20894.
    • (1999) J Biol Chem , vol.274 , pp. 20885-20894
    • Trupp, M.1    Scott, R.2    Whittermore, S.R.3    Ibanez, C.F.4
  • 170
    • 0005868926 scopus 로고    scopus 로고
    • Intracerebroven-tricular infusion of nerve growth factor in three patients with Alz-heimer's disease
    • Eriksdotter JM, Nordberg A, Amberla K, et al. Intracerebroven-tricular infusion of nerve growth factor in three patients with Alz-heimer's disease. Dement Geriatr Cogn Disord 1998; 9: 246-257.
    • (1998) Dement Geriatr Cogn Disord , vol.9 , pp. 246-257
    • Eriksdotter, J.M.1    Nordberg, A.2    Amberla, K.3
  • 171
    • 0032850453 scopus 로고    scopus 로고
    • Clinicopathological findings following intraventricular glial-derived neurotrophic factor treatment in a patient with Parkinson's disease
    • Kordower JH, Palfi S, Chen EY, et al. Clinicopathological findings following intraventricular glial-derived neurotrophic factor treatment in a patient with Parkinson's disease. Ann Neurol 1999; 46:419-424.
    • (1999) Ann Neurol , vol.46 , pp. 419-424
    • Kordower, J.H.1    Palfi, S.2    Chen, E.Y.3
  • 172
    • 0037435511 scopus 로고    scopus 로고
    • Randomized, double-blind trial of glial cell line-derived neurotrophic factor (GDNF) in PD
    • Nutt JG, Burchiel KJ, Comella CL, et al. Randomized, double-blind trial of glial cell line-derived neurotrophic factor (GDNF) in PD. Neurology 2003; 60: 69-73.
    • (2003) Neurology , vol.60 , pp. 69-73
    • Nutt, J.G.1    Burchiel, K.J.2    Comella, C.L.3
  • 173
    • 1642499508 scopus 로고    scopus 로고
    • Localized striatal delivery of GDNF as a treatment for Parkinson's disease
    • Kirik D, Georgievska B, Björklund A. Localized striatal delivery of GDNF as a treatment for Parkinson's disease. Nat Neurosci 2004;7: 105-110.
    • (2004) Nat Neurosci , vol.7 , pp. 105-110
    • Kirik, D.1    Georgievska, B.2    Björklund, A.3
  • 174
    • 33644833272 scopus 로고    scopus 로고
    • Randomized controlled trial of intraputmental glial cell line-derived neurotrophic factor infusion in Parkinson's disease
    • Lang AE, Gill S, Patel NK, et al. Randomized controlled trial of intraputmental glial cell line-derived neurotrophic factor infusion in Parkinson's disease. Ann Neurol 2006; 59: 459-466.
    • (2006) Ann Neurol , vol.59 , pp. 459-466
    • Lang, A.E.1    Gill, S.2    Patel, N.K.3
  • 176
    • 0034208461 scopus 로고    scopus 로고
    • A phase I/II trial of recombinant methionyl human brain derived neurotrophic factor administered by intrathecal infusion to patients with amyotrophic lateral sclerosis
    • Ochs G, Penn RD, York M, et al. A phase I/II trial of recombinant methionyl human brain derived neurotrophic factor administered by intrathecal infusion to patients with amyotrophic lateral sclerosis. Amyotrophic Lateral Scler Other Motor Neuron Disord 2000;1: 201-206.
    • (2000) Amyotrophic Lateral Scler Other Motor Neuron Disord , vol.1 , pp. 201-206
    • Ochs, G.1    Penn, R.D.2    York, M.3
  • 177
    • 0028874203 scopus 로고
    • GDNF protects nigral dopamine neurons against 6-hydroxydopamine in vivo
    • Kearns CM, Gash DM. GDNF protects nigral dopamine neurons against 6-hydroxydopamine in vivo. Brain Res 1995; 620: 104-111.
    • (1995) Brain Res , vol.620 , pp. 104-111
    • Kearns, C.M.1    Gash, D.M.2
  • 178
    • 13344277993 scopus 로고    scopus 로고
    • Functional recovery in park-insonian monkeys treated with GDNF
    • Gash DM, Zhang Z, Ovadia A, et al. Functional recovery in park-insonian monkeys treated with GDNF. Nature 1996; 380: 252-255.
    • (1996) Nature , vol.380 , pp. 252-255
    • Gash, D.M.1    Zhang, Z.2    Ovadia, A.3
  • 179
    • 0034721690 scopus 로고    scopus 로고
    • Neurodegeneration prevented by lentiviral vector delivery of GDNF in primate model sof Parkinson's disease
    • Kordower JH, Emborg ME, Bloch J, et al. Neurodegeneration prevented by lentiviral vector delivery of GDNF in primate model sof Parkinson's disease. Science 2000; 290: 767-773.
    • (2000) Science , vol.290 , pp. 767-773
    • Kordower, J.H.1    Emborg, M.E.2    Bloch, J.3
  • 180
    • 0037010301 scopus 로고    scopus 로고
    • Animal model of dementiainduced by entorhinal synaptic damage and partial restoration of cognitive deficients by BDNF and carnitine
    • Ando S, Kobayashi S, Waki H, et al. Animal model of dementiainduced by entorhinal synaptic damage and partial restoration of cognitive deficients by BDNF and carnitine. J Neurosci Res 2002;70: 519-527.
    • (2002) J Neurosci Res , vol.70 , pp. 519-527
    • Ando, S.1    Kobayashi, S.2    Waki, H.3
  • 181
    • 33646591536 scopus 로고    scopus 로고
    • TAT-GDNF in neurodegeneration and ischemic stroke
    • Kilic E, Kilic Ü, Hermann DM. TAT-GDNF in neurodegeneration and ischemic stroke, CNS Drug Rev 2005; 11: 369-378.
    • (2005) CNS Drug Rev , vol.11 , pp. 369-378
    • Kilic, E.1    Kilic, U.2    Hermann, D.M.3
  • 182
    • 33846577913 scopus 로고    scopus 로고
    • Pharmacologically active microcarriers releasing glial cell line-derived neurotrophic factor:Survival and differentiation of embryonic dopaminergic neuronsafter grafting in hemi parkinsonian rats
    • Tatard VM, Singji L, Branton JG, et al. Pharmacologically active microcarriers releasing glial cell line-derived neurotrophic factor:Survival and differentiation of embryonic dopaminergic neuronsafter grafting in hemi parkinsonian rats. Biomaterials 2007; 29:1978-1988.
    • (2007) Biomaterials , vol.29 , pp. 1978-1988
    • Tatard, V.M.1    Singji, L.2    Branton, J.G.3
  • 183
    • 66149086838 scopus 로고    scopus 로고
    • Clinically relevant effects of convention-enhanced delivery of AAV2-GDNF on the do-paminergic nigrostriatal pathway in aged rhesus monkeys
    • Johnston LC, Eberling J, Pivirotto P, et al. Clinically relevant effects of convention-enhanced delivery of AAV2-GDNF on the do-paminergic nigrostriatal pathway in aged rhesus monkeys. HumGene Ther 2009; 20: 497-510.
    • (2009) HumGene Ther , vol.20 , pp. 497-510
    • Johnston, L.C.1    Eberling, J.2    Pivirotto, P.3
  • 184
    • 0001155209 scopus 로고    scopus 로고
    • Enhanced glialcell line-derived neurotrophic factor mRNA expression upon deprenyl and melatonin treatment
    • Tang YP, Ma YL, Chao CC, Chen KY, Lee EHY. Enhanced glialcell line-derived neurotrophic factor mRNA expression upon deprenyl and melatonin treatment. J Neurosci Res 1998; 53: 593-604
    • (1998) J Neurosci Res , vol.53 , pp. 593-604
    • Tang, Y.P.1    Ma, Y.L.2    Chao, C.C.3    Chen, K.Y.4    Lee, E.H.Y.5
  • 185
    • 34548721105 scopus 로고    scopus 로고
    • Rasagiline promotes regeneration of substantia nigra dopaminergic neurons in post-MPTP-induced Parkinsonism via activation of tyrosine kinase receptor signaling pathway
    • Mandel SA, Sagi Y, Amit T. Rasagiline promotes regeneration of substantia nigra dopaminergic neurons in post-MPTP-induced Parkinsonism via activation of tyrosine kinase receptor signaling pathway. Neurochem Res 2007; 32: 1694-1699.
    • (2007) Neurochem Res , vol.32 , pp. 1694-1699
    • Mandel, S.A.1    Sagi, Y.2    Amit, T.3
  • 186
    • 61549111876 scopus 로고    scopus 로고
    • The novel cholines-terase-monoamine oxidase inhibitor and antioxidant, ladostigil,confers neuroprotection in neuroblastoma cells and aged rats
    • Bar-Am O, Weinreb O, Amit T, Youdim MB. The novel cholines-terase-monoamine oxidase inhibitor and antioxidant, ladostigil,confers neuroprotection in neuroblastoma cells and aged rats. J MolNeurosci 2009; 37: 135-145.
    • (2009) J MolNeurosci , vol.37 , pp. 135-145
    • Bar-Am, O.1    Weinreb, O.2    Amit, T.3    Youdim, M.B.4
  • 187
    • 70449587101 scopus 로고    scopus 로고
    • Genomic and proteomic study to survey the mechanism of action of the anti-Parkinson's disease drug, rasagiline compared with selegiline, in the rat brain
    • Weinreb O, Amit T, Sagi Y, Drigues N, Youdim MBH. Genomic and proteomic study to survey the mechanism of action of the anti-Parkinson's disease drug, rasagiline compared with selegiline, in the rat brain. J Neural Transm 2009; 116: 1456-1472.
    • (2009) J Neural Transm , vol.116 , pp. 1456-1472
    • Weinreb, O.1    Amit, T.2    Sagi, Y.3    Drigues, N.4    Youdim, M.B.H.5
  • 188
    • 77952097251 scopus 로고    scopus 로고
    • Regulation of brain-derived neurotrophic factor (BDNF) and cerebral dopamine neurotrophic factor (CDNF) by anti-parkinsonian drugtherapy in vivo
    • Gyarfas T, Kuuttila J, Lindholm P, Rantamaki T, Castren E. Regulation of brain-derived neurotrophic factor (BDNF) and cerebral dopamine neurotrophic factor (CDNF) by anti-parkinsonian drugtherapy in vivo. Cell Mol Neurobiol 2010; 30: 361-368.
    • (2010) Cell Mol Neurobiol , vol.30 , pp. 361-368
    • Gyarfas, T.1    Kuuttila, J.2    Lindholm, P.3    Rantamaki, T.4    Castren, E.5
  • 189
    • 0028121120 scopus 로고
    • Increased CTNFgene expression in process-bearing astrocytes following injury is augmented by R deprenyl
    • Seniuk NA, Henderson JT, Tatton WG, Roder JC. Increased CTNFgene expression in process-bearing astrocytes following injury is augmented by R deprenyl. J Neurosci Res 1994; 37: 278-286.
    • (1994) J Neurosci Res , vol.37 , pp. 278-286
    • Seniuk, N.A.1    Henderson, J.T.2    Tatton, W.G.3    Roder, J.C.4
  • 190
    • 0034731367 scopus 로고    scopus 로고
    • Selegiline and desmethylselegiline stimulate NGF, BDNF, and GDNF synthesis in cultured mouse as-trocytess
    • Mizuta I, Ohta M, Ohta K, et al. Selegiline and desmethylselegiline stimulate NGF, BDNF, and GDNF synthesis in cultured mouse as-trocytess. Biochem Biophys Res Commun 2000; 279: 751-755.
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 751-755
    • Mizuta, I.1    Ohta, M.2    Ohta, K.3
  • 191
    • 28844501852 scopus 로고    scopus 로고
    • Novel cytoprotective mechanism of anti-parkinsonian drug deprenyl: PI3K and Nrf2-derived induction of antioxidative proteins
    • Nakaso K, Nakamura C, Sato H, Imamura K, Takesima T, Naka-shima K. Novel cytoprotective mechanism of anti-parkinsonian drug deprenyl: PI3K and Nrf2-derived induction of antioxidative proteins. Biochem Biophys Res Commun 2006; 339: 915-922.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 915-922
    • Nakaso, K.1    Nakamura, C.2    Sato, H.3    Imamura, K.4    Takesima, T.5    Naka-Shima, K.6
  • 192
    • 57449088366 scopus 로고    scopus 로고
    • Small molecule activators of the trk receptors for neuroprotection
    • Webster NJG, Pirrung MC. Small molecule activators of the trk receptors for neuroprotection. BMC Neurosci 2008; 9 (Suppl 2): S1
    • (2008) BMC Neurosci , vol.9 , Issue.SUPPL. 2
    • Webster, N.J.G.1    Pirrung, M.C.2
  • 193
    • 0037218768 scopus 로고    scopus 로고
    • Activation of the TrkB neurotrophin receptor is induced by antidepressant drugs and is required for antidepressant-induced behavioral effects
    • Saarelainen T, Hendolin P, Lucas G, et al. Activation of the TrkB neurotrophin receptor is induced by antidepressant drugs and is required for antidepressant-induced behavioral effects. J Neurosci 2003; 23: 349-357.
    • (2003) J Neurosci , vol.23 , pp. 349-357
    • Saarelainen, T.1    Hendolin, P.2    Lucas, G.3
  • 194
    • 69249202366 scopus 로고    scopus 로고
    • Triggering neurotrophic factor action sthrough adenosine A2A receptor activation: Implications for neu-roprotection
    • Sebastiao AM, Ribeiro JA. Triggering neurotrophic factor action sthrough adenosine A2A receptor activation: implications for neu-roprotection. Br J Pharmacol 2009; 158: 15-22.
    • (2009) Br J Pharmacol , vol.158 , pp. 15-22
    • Sebastiao, A.M.1    Ribeiro, J.A.2
  • 195
    • 0037617551 scopus 로고    scopus 로고
    • Effects of dopamine agonists, bromocriptine, pergolide, cabergoline, and SKF-38393 on GDNF, NGF, and BDNF synthesis in cultured mouse astrocytes
    • Ohta K, Kuno S, Mizuta I, Fujinami A, Matsui H, Ohta M. Effects of dopamine agonists, bromocriptine, pergolide, cabergoline, and SKF-38393 on GDNF, NGF, and BDNF synthesis in cultured mouse astrocytes. Life Sci 2003; 73: 617-626.
    • (2003) Life Sci , vol.73 , pp. 617-626
    • Ohta, K.1    Kuno, S.2    Mizuta, I.3    Fujinami, A.4    Matsui, H.5    Ohta, M.6
  • 196
    • 0034720454 scopus 로고    scopus 로고
    • Apomorphine up-regulates NGF and GDNF synthesis in cultured mouse astrocytes
    • Ohta M, Mizuta I, Ohta K, et al. Apomorphine up-regulates NGF and GDNF synthesis in cultured mouse astrocytes. Biochem Bio-phys Res Commun 2000; 272: 18-22.
    • (2000) Biochem Bio-phys Res Commun , vol.272 , pp. 18-22
    • Ohta, M.1    Mizuta, I.2    Ohta, K.3
  • 197
    • 25644445917 scopus 로고    scopus 로고
    • Effects of R-BDNF on the expressions of neurotrophins and their receptors in mesen-cephalic slices
    • Hirai C, Takahata K, Shimizu S, et al. Effects of R-BDNF on the expressions of neurotrophins and their receptors in mesen-cephalic slices. Biol Pharm Bull 2005; 28:1524-1526.
    • (2005) Biol Pharm Bull , vol.28 , pp. 1524-1526
    • Hirai, C.1    Takahata, K.2    Shimizu, S.3
  • 199
    • 59449087438 scopus 로고    scopus 로고
    • Neuropro-tective effects of donepezil through inhibition of GSK-3 activity inamyloid- -induced neuronal cell death
    • Noh MY, Koh SH, Kim Y, Kim HY, Cho GW, Kim SH. Neuropro-tective effects of donepezil through inhibition of GSK-3 activity inamyloid- -induced neuronal cell death. J Neurochem 2009; 108:1116-1125.
    • (2009) J Neurochem , vol.108 , pp. 1116-1125
    • Noh, M.Y.1    Koh, S.H.2    Kim, Y.3    Kim, H.Y.4    Cho, G.W.5    Kim, S.H.6
  • 200
    • 0023184673 scopus 로고
    • L-deprenyl in Alz-heimer's disease. Preliminary evidence for behavioral change withmonoamine oxidase B inhibition
    • Tariot PN, Cohen RM, Sunderland T, et al. L-deprenyl in Alz-heimer's disease. Preliminary evidence for behavioral change withmonoamine oxidase B inhibition. Arch Gen Psychiatry 1987: 44:427-433.
    • (1987) Arch Gen Psychiatry , vol.44 , pp. 427-433
    • Tariot, P.N.1    Cohen, R.M.2    Sunderland, T.3
  • 201
    • 0030967165 scopus 로고    scopus 로고
    • A controlled trial of se-legiline, alpha tocopherol, or both as treatment for Alzheimer dis-ease
    • Sano M, Ernesto C, Thomas RG, et al. A controlled trial of se-legiline, alpha tocopherol, or both as treatment for Alzheimer dis-ease. J New Eng J Med 1997; 336: 16-22.
    • (1997) J New Eng J Med , vol.336 , pp. 16-22
    • Sano, M.1    Ernesto, C.2    Thomas, R.G.3
  • 202
    • 0032999243 scopus 로고    scopus 로고
    • Selegiline in the treatment of Alzheimer's dis-ease: A long-term randomized placebo-controlled trial. Czech andSlovak senile dementia of Alzheimer type study group
    • Filip V, Kolibas E. Selegiline in the treatment of Alzheimer's dis-ease: a long-term randomized placebo-controlled trial. Czech andSlovak senile dementia of Alzheimer type study group. J PsychiatryNeurosci 1999; 24: 134-143.
    • (1999) J PsychiatryNeurosci , vol.24 , pp. 134-143
    • Filip, V.1    Kolibas, E.2
  • 203
    • 0031943163 scopus 로고    scopus 로고
    • L-deprenyl in Alzheimer'sdisease: Cognitive and behavioral effects
    • Freedman M, Rewilak D, Terri T, et al. L-deprenyl in Alzheimer'sdisease: cognitive and behavioral effects. Neurology 1998; 50: 660-668.
    • (1998) Neurology , vol.50 , pp. 660-668
    • Freedman, M.1    Rewilak, D.2    Terri, T.3
  • 204
    • 23644440844 scopus 로고    scopus 로고
    • Ef-fects of selegiline alone or with donepezil on memory impairmentin rats
    • Takahata K, Minami A, Kusamoto H, Shimizu S, Yoneda F. Ef-fects of selegiline alone or with donepezil on memory impairmentin rats. Eur J Pharmacol 2005; 518: 140-144.
    • (2005) Eur J Pharmacol , vol.518 , pp. 140-144
    • Takahata, K.1    Minami, A.2    Kusamoto, H.3    Shimizu, S.4    Yoneda, F.5
  • 205
    • 42249083032 scopus 로고    scopus 로고
    • Syner-gistic effects of selegiline and donepezil on cognitive impairmentinduced by amyloid beta (25-35)
    • Tsunekawa H, Noda Y, Mouri A, Yoneda F, Nabeshima T. Syner-gistic effects of selegiline and donepezil on cognitive impairmentinduced by amyloid beta (25-35). Behav Brain Res 2008; 190: 224-232.
    • (2008) Behav Brain Res , vol.190 , pp. 224-232
    • Tsunekawa, H.1    Noda, Y.2    Mouri, A.3    Yoneda, F.4    Nabeshima, T.5
  • 207
    • 0037153195 scopus 로고    scopus 로고
    • Novel dual inhibitors of AChE and MAO derived from hydroxy aminoindan and phenethylamineas potential treatment for Alzheimer's disease
    • Sterling J, Herzig Y, Goren T, et al. Novel dual inhibitors of AChE and MAO derived from hydroxy aminoindan and phenethylamineas potential treatment for Alzheimer's disease. J Med Chem 2002;45: 5260-5279.
    • (2002) J Med Chem , vol.45 , pp. 5260-5279
    • Sterling, J.1    Herzig, Y.2    Goren, T.3
  • 208
    • 0034525115 scopus 로고    scopus 로고
    • TV3326, a novel neuroprotective drug with cholinesterase and monoamine oxidase inhibitory activities for thetreatment of Alzheimer's disease. J Neural Transm
    • Weinstock M, Bejar C, Wang RH, Poltyrev T, Gross A, Finberg JPM, Youdim MBH. TV3326, a novel neuroprotective drug with cholinesterase and monoamine oxidase inhibitory activities for thetreatment of Alzheimer's disease. J Neural Transm 2000; Suppl 60:157-169.
    • (2000) Suppl , vol.60 , pp. 157-169
    • Weinstock, M.1    Bejar, C.2    Wang, R.H.3    Poltyrev, T.4    Gross, A.5    Finberg, J.P.M.6    Youdim, M.B.H.7
  • 209
    • 0037507200 scopus 로고    scopus 로고
    • Potential cognitive actions of (n-propargyl-(3r)-aminoindan-5-yl)-ethyl, methyl carbamate (tv3326), a novel neuroprotective agent, as assessed inold rheusus monkeys in their performance of versions of a delayedmatching task
    • Buccafusco JJ, Terry AV Jr, Goren T, Blaugrun E. Potential cognitive actions of (n-propargyl-(3r)-aminoindan-5-yl)-ethyl, methyl carbamate (tv3326), a novel neuroprotective agent, as assessed inold rheusus monkeys in their performance of versions of a delayedmatching task. Neurosience 2003; 119: 669-678.
    • (2003) Neurosience , vol.119 , pp. 669-678
    • Buccafusco, J.J.1    Terry Jr., A.V.2    Goren, T.3    Blaugrun, E.4
  • 210
    • 0038012567 scopus 로고    scopus 로고
    • A novel cholinesterase and brain-selective monoamine oxidase inhibitor for the treatment of dementia comorbid with depression and Parkinson's disease
    • Weinstock M, Gorodetsky E, Poltyerv T, Gross A, Sagi Y, Youdim M. A novel cholinesterase and brain-selective monoamine oxidase inhibitor for the treatment of dementia comorbid with depression and Parkinson's disease. Prog Neuropsychopharmacol Biol Psy-chiatry 2003; 27: 555-561.
    • (2003) Prog Neuropsychopharmacol Biol Psy-chiatry , vol.27 , pp. 555-561
    • Weinstock, M.1    Gorodetsky, E.2    Poltyerv, T.3    Gross, A.4    Sagi, Y.5    Youdim, M.6
  • 211
    • 33846924328 scopus 로고    scopus 로고
    • Ladostigil prevents gliosis, oxidative-nitrative stress and memory deficits induced by intracerebroventricular injection of streptozoto-cin in rats
    • Shoham S, Bejar C, Kovalev E, Shorer-Apelbaun D, Weinstock M. Ladostigil prevents gliosis, oxidative-nitrative stress and memory deficits induced by intracerebroventricular injection of streptozoto-cin in rats. Neuropharmacol 2007; 52: 836-843.
    • (2007) Neuropharmacol , vol.52 , pp. 836-843
    • Shoham, S.1    Bejar, C.2    Kovalev, E.3    Shorer-Apelbaun, D.4    Weinstock, M.5
  • 212
    • 77957960863 scopus 로고    scopus 로고
    • Ladostigil prevents age-related glial activation and spatial memory deficits inrats
    • in press
    • Weintock M, Luques L, Poltyrev T, Bejar C, Shoham S. Ladostigil prevents age-related glial activation and spatial memory deficits inrats. Neurobiol Aging 2009; in press.
    • (2009) Neurobiol Aging
    • Weintock, M.1    Luques, L.2    Poltyrev, T.3    Bejar, C.4    Shoham, S.5
  • 213
    • 0345237921 scopus 로고    scopus 로고
    • Antiapop-totic action of anti-Alzheimer drug, TV3326 [(N-propargyl)-(3R)-aminoindan-5-yl]-ethyl methyl carbamate, a novel cholinesterase-monoamine oxidase inhibitor
    • Maruyama W, Weinstock M, Youdim MBH, Naoi M. Antiapop-totic action of anti-Alzheimer drug, TV3326 [(N-propargyl)-(3R)-aminoindan-5-yl]-ethyl methyl carbamate, a novel cholinesterase-monoamine oxidase inhibitor. Neurosci Lett 2003; 341: 233-236.
    • (2003) Neurosci Lett , vol.341 , pp. 233-236
    • Maruyama, W.1    Weinstock, M.2    Youdim, M.B.H.3    Naoi, M.4
  • 214
    • 50649083041 scopus 로고    scopus 로고
    • The neuroprotective effect of ladostigil against hydrogen peroxide-mediated cytotoxicity
    • Weinreb O, Bar-Am O, Amit T, Driques N, Sagi Y, Youdim MB. The neuroprotective effect of ladostigil against hydrogen peroxide-mediated cytotoxicity. Chem Biol Interact 2008; 175: 318-326.
    • (2008) Chem Biol Interact , vol.175 , pp. 318-326
    • Weinreb, O.1    Bar-Am, O.2    Amit, T.3    Driques, N.4    Sagi, Y.5    Youdim, M.B.6
  • 215
    • 33750603844 scopus 로고    scopus 로고
    • Alzheimer's centennial legacy: Prospectsfor rational therapeutic intervention targeting the A amyloid pathway
    • Masters C, Beyreuther K. Alzheimer's centennial legacy: prospectsfor rational therapeutic intervention targeting the A amyloid pathway. Brain 2006; 129: 2823-2839.
    • (2006) Brain , vol.129 , pp. 2823-2839
    • Masters, C.1    Beyreuther, K.2
  • 216
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002; 297: 352-356.
    • (2002) Science , vol.297 , pp. 352-356
    • Hardy, J.1    Selkoe, D.J.2
  • 217
    • 31744447521 scopus 로고    scopus 로고
    • Anti-Parkinsonian agents have anti-amyloidogenic activity for Alzheimer's beta-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Naiki H, Yamada M. Anti-Parkinsonian agents have anti-amyloidogenic activity for Alzheimer's beta-amyloid fibrils in vitro. Neurochem Int 2006; 48: 275-285.
    • (2006) Neurochem Int , vol.48 , pp. 275-285
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 218
    • 0036777108 scopus 로고    scopus 로고
    • The involvement of mitogen-activated protein (MAP) kinasein the regulation of amyloid precursor protein processing by novelcholinesterase inhibitors derived from rasagiline
    • Yogev-Falach M, Amit T, Bar-Am O, Weinstock M, Youdim MBH. The involvement of mitogen-activated protein (MAP) kinasein the regulation of amyloid precursor protein processing by novelcholinesterase inhibitors derived from rasagiline. FASEB J 2002;16: 1674-1676.
    • (2002) FASEB J , vol.16 , pp. 1674-1676
    • Yogev-Falach, M.1    Amit, T.2    Bar-Am, O.3    Weinstock, M.4    Youdim, M.B.H.5
  • 219
    • 6944242126 scopus 로고    scopus 로고
    • Neuroprotection via pro-survival protein kinase C isoforms associ-ated with Bcl-2 family members
    • Weinreb O, Bar-Am O, Amit T, Chillag-Talmor O, Youdim MBH.Neuroprotection via pro-survival protein kinase C isoforms associ-ated with Bcl-2 family members. FASEB J 2004; 18: 1471-1473.
    • (2004) FASEB J , vol.18 , pp. 1471-1473
    • Weinreb, O.1    Bar-Am, O.2    Amit, T.3    Chillag-Talmor, O.4    Youdim, M.B.H.5
  • 220
    • 27744486071 scopus 로고    scopus 로고
    • Regulation of Bcl-2protein family proteins, neurotrophic factors, and APP processingin the neurorescue activity of propargylamine
    • Bar-Am O, Weinreb O, Amit T, Youdim MB. Regulation of Bcl-2protein family proteins, neurotrophic factors, and APP processingin the neurorescue activity of propargylamine. FASEB J 2005; 19:1899-1901.
    • (2005) FASEB J , vol.19 , pp. 1899-1901
    • Bar-Am, O.1    Weinreb, O.2    Amit, T.3    Youdim, M.B.4
  • 221
    • 33845669856 scopus 로고    scopus 로고
    • A multifunctional, neuroprotective drug, ladostigil (TV3326), regu-lates holo-APP translocation and processing
    • Yogev-Falach M, Bar-Am O, Amit T, Weinstock M, Youdim MB. A multifunctional, neuroprotective drug, ladostigil (TV3326), regu-lates holo-APP translocation and processing. FASEB J 2006; 20:2177-2179.
    • (2006) FASEB J , vol.20 , pp. 2177-2179
    • Yogev-Falach, M.1    Bar-Am, O.2    Amit, T.3    Weinstock, M.4    Youdim, M.B.5
  • 222
    • 2642529309 scopus 로고    scopus 로고
    • Regulation of protein kinase C by the anti-Parkinson drug, MAO-Binhibitor, rasagiline and its derivatives, in vivo
    • Bar-Am O, Yogev-Falach M, Amit T, Sagi Y, Youdim MBH. Regulation of protein kinase C by the anti-Parkinson drug, MAO-Binhibitor, rasagiline and its derivatives, in vivo. J Neurochem 2004;89: 1119-1125.
    • (2004) J Neurochem , vol.89 , pp. 1119-1125
    • Bar-Am, O.1    Yogev-Falach, M.2    Amit, T.3    Sagi, Y.4    Youdim, M.B.H.5
  • 223
    • 33845291088 scopus 로고    scopus 로고
    • Mitogen activated protein kinaseand protein kinase C activation mediate promotion of sAPP secre-tion by deprenyl
    • Yang HO, Ba MW, Ren RJ, et al. Mitogen activated protein kinaseand protein kinase C activation mediate promotion of sAPP secre-tion by deprenyl. Neurochem Int 2007; 50: 74-82
    • (2007) Neurochem Int , vol.50 , pp. 74-82
    • Yang, H.O.1    Ba, M.W.2    Ren, R.J.3
  • 224
    • 4544239545 scopus 로고    scopus 로고
    • Acetylcholine in-hibitors increase ADAM10 activity by promoting its trafficking inneuroblastoma cell lines
    • Zimmermann M, Gardoni F, Marcello E, et al. Acetylcholine in-hibitors increase ADAM10 activity by promoting its trafficking inneuroblastoma cell lines. J Neurochem 2004; 90: 1489-1499.
    • (2004) J Neurochem , vol.90 , pp. 1489-1499
    • Zimmermann, M.1    Gardoni, F.2    Marcello, E.3
  • 225
    • 0642303109 scopus 로고    scopus 로고
    • The impor-tance of propargylamine moiety in the anti-Parkinson drugrasagiline and its derivatives in MAPK-dependent amyloid precur-sor protein processing
    • Yogev-Falach M, Amit T, Bar-Am O, Youdim MB. The impor-tance of propargylamine moiety in the anti-Parkinson drugrasagiline and its derivatives in MAPK-dependent amyloid precur-sor protein processing. FASEB J 2003; 17: 2325-2327
    • (2003) FASEB J , vol.17 , pp. 2325-2327
    • Yogev-Falach, M.1    Amit, T.2    Bar-Am, O.3    Youdim, M.B.4
  • 226
    • 11844255676 scopus 로고    scopus 로고
    • Design, synthesis, andevaluation of novel bifunctional iron-chelators as potential agentsfor neuroprotection in Alzheimer's, Parkinson's, and other neu-rodegenerative disease
    • Zheng H, Weiner LM, Bar-Am O, et al. Design, synthesis, andevaluation of novel bifunctional iron-chelators as potential agentsfor neuroprotection in Alzheimer's, Parkinson's, and other neu-rodegenerative disease. Bioorg Med Chem 2005; 13: 773-783.
    • (2005) Bioorg Med Chem , vol.13 , pp. 773-783
    • Zheng, H.1    Weiner, L.M.2    Bar-Am, O.3
  • 227
    • 33845879870 scopus 로고    scopus 로고
    • Fridkin M,Youdim MBH. Therapeutic targets and potential of the novel brain-permeable multifunctional iron chelator-monoamine oxidase in-hibitor drug, M-30, for the treatment of Alzheimer's disease
    • Avramovich-Tirosh Y, Amit T, Bar-Am O, Zheng H, Fridkin M,Youdim MBH. Therapeutic targets and potential of the novel brain-permeable multifunctional iron chelator-monoamine oxidase in-hibitor drug, M-30, for the treatment of Alzheimer's disease. J Neurochem 2007; 100: 490-502.
    • (2007) J Neurochem , vol.100 , pp. 490-502
    • Avramovich-Tirosh, Y.1    Amit, T.2    Bar-Am, O.3    Zheng, H.4
  • 228
    • 0025726462 scopus 로고
    • Intramusculardesferrioxamine in patients with Alzheimer's disease
    • Crapper McLachlan DR, Dalton AJ, Kruck TP, et al. Intramusculardesferrioxamine in patients with Alzheimer's disease. Lancet 1991;337: 1304-1308.
    • (1991) Lancet , vol.337 , pp. 1304-1308
    • Crapper McLachlan, D.R.1    Dalton, A.J.2    Kruck, T.P.3
  • 229
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a cop-per-zinc chelator markedly and rapidly inhibits -amyloid accumu-lation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, et al. Treatment with a cop-per-zinc chelator markedly and rapidly inhibits -amyloid accumu-lation in Alzheimer's disease transgenic mice. Neuron 2001; 30:665-676.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3
  • 230
    • 0346849912 scopus 로고    scopus 로고
    • Neuroprotection by a novel brain permeable iron chelator VK-28,against 6-hydroxydopamine lesion in rats
    • Shachar DB, Kahana N, Kampel V, Warshawsky A, Youdim MB. Neuroprotection by a novel brain permeable iron chelator VK-28,against 6-hydroxydopamine lesion in rats. Neuropharmacol 2004;46: 254-263.
    • (2004) Neuropharmacol , vol.46 , pp. 254-263
    • Shachar, D.B.1    Kahana, N.2    Kampel, V.3    Warshawsky, A.4    Youdim, M.B.5
  • 231
    • 25644452043 scopus 로고    scopus 로고
    • Novel multifunctionalneuroprotective iron chelator-monoamine oxidase inhibitor drugsfor neurodegenerative diseases. In vivo selective monoamine oxi-dase inhibition and prevention of MPTP-induced striatal dopaminedepletion
    • Gal S, Zheng H, Fridkin M, Youdim MBH. Novel multifunctionalneuroprotective iron chelator-monoamine oxidase inhibitor drugsfor neurodegenerative diseases. In vivo selective monoamine oxi-dase inhibition and prevention of MPTP-induced striatal dopaminedepletion. J Neurochem 2005; 95: 79-88.
    • (2005) J Neurochem , vol.95 , pp. 79-88
    • Gal, S.1    Zheng, H.2    Fridkin, M.3    Youdim, M.B.H.4
  • 232
    • 36849044036 scopus 로고    scopus 로고
    • Prevention and restoration of lacta-cystin-induced nigrostriatal dopamine neurons degeneration bynovel brain-permeable iron chelators
    • Zhu W, Xie W, Pan T, et al., Prevention and restoration of lacta-cystin-induced nigrostriatal dopamine neurons degeneration bynovel brain-permeable iron chelators. FASEB J 2007: 21: 3835-3844.
    • (2007) FASEB J , vol.21 , pp. 3835-3844
    • Zhu, W.1    Xie, W.2    Pan, T.3
  • 233
    • 0036304650 scopus 로고    scopus 로고
    • Modification of brain aging andneurodegenerative disorders by genes, diet, and behavior
    • Mattson MP, Chan SL, Duan W. Modification of brain aging andneurodegenerative disorders by genes, diet, and behavior. PhysiolRev 2002; 82: 637-672.
    • (2002) PhysiolRev , vol.82 , pp. 637-672
    • Mattson, M.P.1    Chan, S.L.2    Duan, W.3
  • 234
    • 47849120398 scopus 로고    scopus 로고
    • Challenges for research on polyphenols from foods in Alzheimer'sdisease: Bioavailability, metabolism, and cellular and molecularmechanisms
    • Singh M, Arseneult M, Sanderson T, Murthy V, Ramassamy C.Challenges for research on polyphenols from foods in Alzheimer'sdisease: bioavailability, metabolism, and cellular and molecularmechanisms. J Agrc Food Chem 2006; 56: 4855-4873.
    • (2006) J Agrc Food Chem , vol.56 , pp. 4855-4873
    • Singh, M.1    Arseneult, M.2    Sanderson, T.3    Murthy, V.4    Ramassamy, C.5
  • 235
    • 0141642253 scopus 로고    scopus 로고
    • YamadaM. Potent anti-amyloidogenic and fibril-destabilizing effects ofpolyphenols in vitro: Implications for the prevention and therapeu-tics of Alzheimer's disease
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, YamadaM. Potent anti-amyloidogenic and fibril-destabilizing effects ofpolyphenols in vitro: implications for the prevention and therapeu-tics of Alzheimer's disease. J Neurochem 2003; 87: 172-181.
    • (2003) J Neurochem , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5
  • 236
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril for-mation by polyphenols: Structural similarity and aromatic interac-tions as a common inhibition mechanism
    • Porat Y, Abramowitz A, Gazit E. Inhibition of amyloid fibril for-mation by polyphenols: Structural similarity and aromatic interac-tions as a common inhibition mechanism. Chem Biol Drug Des 2006; 67: 27-37.
    • (2006) Chem Biol Drug Des , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 237
    • 0038661168 scopus 로고    scopus 로고
    • Neuroprotection andneurorescue against A toxicity and PKC-dependent release ofnon-amyloidogenic soluble precursor protein by green tea polyphe-nol epigallocatechin-3-gallate
    • Levites Y, Amit T, Mandel S, Youdim MBH. Neuroprotection andneurorescue against A toxicity and PKC-dependent release ofnon-amyloidogenic soluble precursor protein by green tea polyphe-nol epigallocatechin-3-gallate. FASEB J 2003; 17: 952-954.
    • (2003) FASEB J , vol.17 , pp. 952-954
    • Levites, Y.1    Amit, T.2    Mandel, S.3    Youdim, M.B.H.4
  • 238
    • 33645294934 scopus 로고    scopus 로고
    • Reduction of iron-regulated amyloid precursor protein and -amyloid peptide by epigallocatechin-3-gallate in cell cultures: Implications for ironchelation in Alzheimer's disease
    • Reznichenko L, Amit T, Zheng H, et al. Reduction of iron-regulated amyloid precursor protein and -amyloid peptide by epigallocatechin-3-gallate in cell cultures: implications for ironchelation in Alzheimer's disease. J Neurochem 2006; 97: 527-536.
    • (2006) J Neurochem , vol.97 , pp. 527-536
    • Reznichenko, L.1    Amit, T.2    Zheng, H.3
  • 239
    • 25444500410 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavageand reduces cerebral amyloidosis in Alzheimer transgenic mice
    • Rezai-Zadeh K, Shytle D, Sun N, et al. Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavageand reduces cerebral amyloidosis in Alzheimer transgenic mice. J Neurosci 2005; 25: 8807-8814.
    • (2005) J Neurosci , vol.25 , pp. 8807-8814
    • Rezai-Zadeh, K.1    Shytle, D.2    Sun, N.3
  • 240
    • 46749123053 scopus 로고    scopus 로고
    • Grape-derived polyphenols preventA oligomerization and attenuate cognitive deterioration in amouse model of Alzheimer's disease
    • Wang J, Ho L, Zhao W, et al. Grape-derived polyphenols preventA oligomerization and attenuate cognitive deterioration in amouse model of Alzheimer's disease. J Neurochem 2008; 28:6388-6392.
    • (2008) J Neurochem , vol.28 , pp. 6388-6392
    • Wang, J.1    Ho, L.2    Zhao, W.3
  • 241
    • 27844497059 scopus 로고    scopus 로고
    • Resveratrol promotes clearanceof Alzheimer's disease amyloid- peptides
    • Marambaud P, Zhao H, Davies P. Resveratrol promotes clearanceof Alzheimer's disease amyloid- peptides. J Biol Chem 2005;280: 27377-82.
    • (2005) J Biol Chem , vol.280 , pp. 27377-27382
    • Marambaud, P.1    Zhao, H.2    Davies, P.3
  • 242
    • 33746118723 scopus 로고    scopus 로고
    • Trans-e-vinierin, a poly-phenol present in win, is an inhibitor of noradrenaline and 5-hydroxytryptamine uptake and of monoamine oxidase activity
    • Yanez M, Fraiz N, Cano E, Orallo F. Trans-e-vinierin, a poly-phenol present in win, is an inhibitor of noradrenaline and 5-hydroxytryptamine uptake and of monoamine oxidase activity. EurJ Pharmacol 2006; 542: 54-60.
    • (2006) EurJ Pharmacol , vol.542 , pp. 54-60
    • Yanez, M.1    Fraiz, N.2    Cano, E.3    Orallo, F.4
  • 243
    • 0034005306 scopus 로고    scopus 로고
    • Identification ofkaempferol as monoamine oxidase inhibitor and potential neuro-protectant in extracts of Gingo biloba leaves
    • Sloley BD, Urichuk LJ, Morley P, et al. Identification ofkaempferol as monoamine oxidase inhibitor and potential neuro-protectant in extracts of Gingo biloba leaves. J Pharm Pharmacol 2000; 52: 451-459.
    • (2000) J Pharm Pharmacol , vol.52 , pp. 451-459
    • Sloley, B.D.1    Urichuk, L.J.2    Morley, P.3
  • 244
    • 33746514329 scopus 로고    scopus 로고
    • Quercetin as the ac-tive principle of Hypericum hircinum exerts a selective inhibitoryactivity against MAO-A: Extraction, biological analysis, and com-putational study
    • Chimenti F, Cottiglia F, Bonsignore L, et al. Quercetin as the ac-tive principle of Hypericum hircinum exerts a selective inhibitoryactivity against MAO-A: Extraction, biological analysis, and com-putational study. J Nat Prod 2006; 69: 945-949.
    • (2006) J Nat Prod , vol.69 , pp. 945-949
    • Chimenti, F.1    Cottiglia, F.2    Bonsignore, L.3
  • 245
    • 58049115902 scopus 로고    scopus 로고
    • Rasmussen, Jäger AK. MAO-A inhibi-tory activity of quercetin from Calluna vulgaris (L.) Hull
    • Saaby L, Rasmussen HB, Rasmussen, Jäger AK. MAO-A inhibi-tory activity of quercetin from Calluna vulgaris (L.) Hull. J Ethno-pharmacol 2009; 121: 178-181.
    • (2009) J Ethno-pharmacol , vol.121 , pp. 178-181
    • Saaby, L.1    Rasmussen, H.B.2
  • 247
    • 21844479344 scopus 로고    scopus 로고
    • Monoamine oxidase inhibitorycomponents from the roots of sophora flavoscens
    • Hwang JS, Lee SA, Hong SS, et al. Monoamine oxidase inhibitorycomponents from the roots of sophora flavoscens. Arch Pharmacol Res 2005; 28: 190-194.
    • (2005) Arch Pharmacol Res , vol.28 , pp. 190-194
    • Hwang, J.S.1    Lee, S.A.2    Hong, S.S.3
  • 249
    • 20144386944 scopus 로고    scopus 로고
    • Ginkgo biloba affordsdose-dependent protection against 6-hydroxydopamine-inducedparkinsonism in rats: Neurobehavioral, neurochemical and immu-nohistochemical evidences
    • Ahmad M, Saleem S, Ahmad AS, et al. Ginkgo biloba affordsdose-dependent protection against 6-hydroxydopamine-inducedparkinsonism in rats: neurobehavioral, neurochemical and immu-nohistochemical evidences. J Neurochem 2005; 93: 94-104.
    • (2005) J Neurochem , vol.93 , pp. 94-104
    • Ahmad, M.1    Saleem, S.2    Ahmad, A.S.3
  • 250
    • 34547824397 scopus 로고    scopus 로고
    • EGb 761 enhancesadult hippocampal neurogenesis and phosphorylation of CREB intransgenic mouse model of Alzheimer's disease
    • Tchantchou F, Xu Y, Wu Y, Christen Y, Luo Y. EGb 761 enhancesadult hippocampal neurogenesis and phosphorylation of CREB intransgenic mouse model of Alzheimer's disease. FASEB J 2007; 2:2400-2408.
    • (2007) FASEB J , vol.2 , pp. 2400-2408
    • Tchantchou, F.1    Xu, Y.2    Wu, Y.3    Christen, Y.4    Luo, Y.5
  • 251
    • 61749103704 scopus 로고    scopus 로고
    • Protec-tive effect of quercetin in primary neurons against A (1-42): Rele-vance to Alzheimer's disease
    • Ansari MA, Abdul HM, Joshi G, Opii WO, Butterfield DA. Protec-tive effect of quercetin in primary neurons against A (1-42): rele-vance to Alzheimer's disease. J Nutr Biochem 2009; 20: 269-275.
    • (2009) J Nutr Biochem , vol.20 , pp. 269-275
    • Ansari, M.A.1    Abdul, H.M.2    Joshi, G.3    Opii, W.O.4    Butterfield, D.A.5
  • 252
    • 0033955997 scopus 로고    scopus 로고
    • Launay JM,Ohen-Salmon C. In vivo regulation of cerebral monoamine oxidaseactivity in senescent controls and chronically stress-mice by long-term treatment with Ginkgo biloba extract (EGb 761)
    • Pardon MC, Joubert C, Perez-Diaz F, Christen Y, Launay JM,Ohen-Salmon C. In vivo regulation of cerebral monoamine oxidaseactivity in senescent controls and chronically stress-mice by long-term treatment with Ginkgo biloba extract (EGb 761). Mech Age-ing Dev 2000; 113: 157-168.
    • (2000) Mech Age-ing Dev , vol.113 , pp. 157-168
    • Pardon, M.C.1    Joubert, C.2    Perez-Diaz, F.3    Christen, Y.4
  • 253
    • 42049109707 scopus 로고    scopus 로고
    • Inhibition of monoamine oxidase-B bythe polyphenolic compound, curcumin and its metabolite tetrahy-drocurcumin, in a model of Parkinson's disease induced by MPTP neurodegeneration in mice
    • Rajeswari A, Sabesan M. Inhibition of monoamine oxidase-B bythe polyphenolic compound, curcumin and its metabolite tetrahy-drocurcumin, in a model of Parkinson's disease induced by MPTP neurodegeneration in mice. Inflammopharmacol 2008; 16: 96-99.
    • (2008) Inflammopharmacol , vol.16 , pp. 96-99
    • Rajeswari, A.1    Sabesan, M.2
  • 254
    • 45749089694 scopus 로고    scopus 로고
    • Curcumin structure-function, bioavailability, and efficacy in models of neuroinflamma-tion and Alzheimer's disease
    • Begum AN, Jones MR, Lim GP, et al. Curcumin structure-function, bioavailability, and efficacy in models of neuroinflamma-tion and Alzheimer's disease. J Pharmacol Exp Ther 2008; 326:196-208.
    • (2008) J Pharmacol Exp Ther , vol.326 , pp. 196-208
    • Begum, A.N.1    Jones, M.R.2    Lim, G.P.3
  • 255
    • 23044465134 scopus 로고    scopus 로고
    • Monoamine oxidase B(MAO-B) inhibition by active principles from uncaria rhyncho-phylla
    • Hou WC, Lin RD, Chen CT, Lee MH. Monoamine oxidase B(MAO-B) inhibition by active principles from uncaria rhyncho-phylla. J Ethnopharmacol 2005; 100: 216-220.
    • (2005) J Ethnopharmacol , vol.100 , pp. 216-220
    • Hou, W.C.1    Lin, R.D.2    Chen, C.T.3    Lee, M.H.4
  • 256
    • 77649336424 scopus 로고    scopus 로고
    • Anti-depressant natural flavonols modulate BDNF and beta amy-loid in neurons and hippocampus of double TgAD mice
    • Hou Y, Aboukhatwa MA, Lei DL, Manaye K, Khan I, Luo Y.Anti-depressant natural flavonols modulate BDNF and beta amy-loid in neurons and hippocampus of double TgAD mice. Neuro-pharmacol 2009; 58: 911-920.
    • (2009) Neuro-pharmacol , vol.58 , pp. 911-920
    • Hou, Y.1    Aboukhatwa, M.A.2    Lei, D.L.3    Manaye, K.4    Khan, I.5    Luo, Y.6
  • 257
    • 0028807095 scopus 로고
    • Imidazoline/guanidinium bindingdomains on monoamine oxidase
    • Raddatz R, Parini A, Lanier SM. Imidazoline/guanidinium bindingdomains on monoamine oxidase. J Biol Chem 1995; 270: 27961-27968.
    • (1995) J Biol Chem , vol.270 , pp. 27961-27968
    • Raddatz, R.1    Parini, A.2    Lanier, S.M.3
  • 258
    • 0346785246 scopus 로고    scopus 로고
    • On the binding site of monoamineoxidase inhibitors to some sites distinct from the MAO active site,and effects thereby elicited
    • Holt A, Wieland B, Boulton AA. On the binding site of monoamineoxidase inhibitors to some sites distinct from the MAO active site,and effects thereby elicited. Neurotoxicity 2004; 25: 251-266.
    • (2004) Neurotoxicity , vol.25 , pp. 251-266
    • Holt, A.1    Wieland, B.2    Boulton, A.A.3
  • 259
    • 0037734329 scopus 로고    scopus 로고
    • Neuroprotection bydeprenyl and other propargylamines; glyceraldehydes-3-phosphatedehydrogenase rather than monoamine oxidase B
    • Tatton W, Chalmers-Redman R, Tatton N. Neuroprotection bydeprenyl and other propargylamines; glyceraldehydes-3-phosphatedehydrogenase rather than monoamine oxidase B. J Neural Transm 2003; 110: 509-515.
    • (2003) J Neural Transm , vol.110 , pp. 509-515
    • Tatton, W.1    Chalmers-Redman, R.2    Tatton, N.3
  • 260
    • 0037175058 scopus 로고    scopus 로고
    • 3H]quipirole binding by monoamine oxidase inhibitors
    • 3H]quipirole binding by monoamine oxidase inhibitors.Life Sci 2002; 71: 2691-2700.
    • (2002) Life Sci , vol.71 , pp. 2691-2700
    • Levant, B.1
  • 261
    • 0034517763 scopus 로고    scopus 로고
    • The neuroprotective effects of CGP 3466Bin the best in vivo model of Parkinson7s disease, the bilaterallyMPTP-treated rheus monkey
    • Andringa G, Cools AR. The neuroprotective effects of CGP 3466Bin the best in vivo model of Parkinson7s disease, the bilaterallyMPTP-treated rheus monkey. J Neural Transm 2000; Suppl 60:215-225.
    • (2000) J Neural Transm , Issue.SUPPL. 60 , pp. 215-225
    • Andringa, G.1    Cools, A.R.2
  • 262
    • 2342655732 scopus 로고    scopus 로고
    • A controlled, randomized, delayed-startstudy of rasagiline in early Parkinson disease
    • Parkinson Study Groups
    • Parkinson Study Groups. A controlled, randomized, delayed-startstudy of rasagiline in early Parkinson disease, Arch Neurol 2004;61: 561-6.
    • (2004) Arch Neurol , vol.61 , pp. 561-566
  • 263
    • 70349456475 scopus 로고    scopus 로고
    • A double-blind, delayed-start trial of rasagiline in Parkinson's disease
    • Olanow CW, Rascol O, Hauser R, et al. A double-blind, delayed-start trial of rasagiline in Parkinson's disease. N Eng J Med 2009;361: 1268-1278.
    • (2009) N Eng J Med , vol.361 , pp. 1268-1278
    • Olanow, C.W.1    Rascol, O.2    Hauser, R.3
  • 264
    • 1542317394 scopus 로고    scopus 로고
    • Contrasting neuroprotectiveand neurotoxic actions of respective metabolites of anti-Parkinsondrugs rasagiline and selegiline
    • Bar-Am O, Amit T, Youdim MBH. Contrasting neuroprotectiveand neurotoxic actions of respective metabolites of anti-Parkinsondrugs rasagiline and selegiline. Neurosci Lett 2004; 355: 169-172.
    • (2004) Neurosci Lett , vol.355 , pp. 169-172
    • Bar-Am, O.1    Amit, T.2    Youdim, M.B.H.3
  • 265
    • 23644437308 scopus 로고    scopus 로고
    • Comparison ofthe capacity of GDNF, BDNF, or both, to protect nigrostriatal neu-rons in a rat model of Parkinson's disease
    • Sun M, Kong L, Wang X, Lu X, Gao Q, Geller A. Comparison ofthe capacity of GDNF, BDNF, or both, to protect nigrostriatal neu-rons in a rat model of Parkinson's disease. Brain Res 2005; 1052:119-129.
    • (2005) Brain Res , vol.1052 , pp. 119-129
    • Sun, M.1    Kong, L.2    Wang, X.3    Lu, X.4    Gao, Q.5    Geller, A.6
  • 266
    • 74449085179 scopus 로고    scopus 로고
    • Regulatory role of mono-amine neurotransmitters in astrocytic NT-3 synthesis
    • Mele T, Carman-Krzan M, Juric DM. Regulatory role of mono-amine neurotransmitters in astrocytic NT-3 synthesis. Int J DevNeurosci 2010; 28: 13-19.
    • (2010) Int J DevNeurosci , vol.28 , pp. 13-19
    • Mele, T.1    Carman-Krzan, M.2    Juric, D.M.3
  • 267
    • 38449088277 scopus 로고    scopus 로고
    • Antibody-based approaches in Alz-heimer's research: Safety, pharmacokinetics, and analytical tools
    • Lichtlein P, Mohajeri MH. Antibody-based approaches in Alz-heimer's research: safety, pharmacokinetics, and analytical tools. JNeurochem 2008; 104: 859-874.
    • (2008) JNeurochem , vol.104 , pp. 859-874
    • Lichtlein, P.1    Mohajeri, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.