메뉴 건너뛰기




Volumn 41, Issue 6, 2005, Pages 369-391

Neuropharmacological, neuroprotective and amyloid precursor processing properties of selective MAO-B inhibitor antiparkinsonian drug, rasagiline

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; AMINE OXIDASE (FLAVIN CONTAINING); AMPHETAMINE; AMYLOID PRECURSOR PROTEIN; CLORGYLINE; DOPAMINE; FLUOXETINE; LADOSTIGIL; LAZABEMIDE; LEVODOPA; META TYRAMINE; METHAMPHETAMINE; MILACEMIDE; MONOAMINE OXIDASE B INHIBITOR; NEUROTOXIN; NOMIFENSINE; RASAGILINE; RESERPINE; SELEGILINE; SOLUBLE AMYLOID PRECURSOR PROTEIN ALPHA; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 23144441835     PISSN: 16993993     EISSN: 16994019     Source Type: Journal    
DOI: 10.1358/dot.2005.41.6.893613     Document Type: Review
Times cited : (63)

References (159)
  • 1
    • 0014965307 scopus 로고
    • Multiple forms of human brain mitochondrial monoamine oxidase
    • Collins, G.G., Sandler, M., Williams, E.D., Youdim, M.B. Multiple forms of human brain mitochondrial monoamine oxidase. Nature 1970, 225:817-20.
    • (1970) Nature , vol.225 , pp. 817-820
    • Collins, G.G.1    Sandler, M.2    Williams, E.D.3    Youdim, M.B.4
  • 2
    • 0015272059 scopus 로고
    • Multiple forms of monoamine oxidase in intact mitochondria as characterized by selective inhibitors and thermal stability: A comparison of eight mammalian species
    • Squires, R.F. Multiple forms of monoamine oxidase in intact mitochondria as characterized by selective inhibitors and thermal stability: a comparison of eight mammalian species. Adv Biochem Psychopharmacol 1972, 5: 355-7.
    • (1972) Adv Biochem Psychopharmacol , vol.5 , pp. 355-357
    • Squires, R.F.1
  • 4
    • 0015274536 scopus 로고
    • Some puzzling pharmacological effects of monoamine oxidase inhibitors
    • Knoll and Magyar. Some puzzling pharmacological effects of monoamine oxidase inhibitors. Adv Biochem Psychopharmacol 1972, 5: 393-408.
    • (1972) Adv Biochem Psychopharmacol , vol.5 , pp. 393-408
    • Knoll1    Magyar2
  • 5
    • 0016414699 scopus 로고
    • The potentiation of the anti akinetic effect after L-dopa treatment by an inhibitor of MAO-B, Deprenil
    • Birkmayer, W., Riederer, P., Youdim, M.B., Linauer, W. The potentiation of the anti akinetic effect after L-dopa treatment by an inhibitor of MAO-B, Deprenil. J Neural Transm 1975, 36: 303-26.
    • (1975) J Neural Transm , vol.36 , pp. 303-326
    • Birkmayer, W.1    Riederer, P.2    Youdim, M.B.3    Linauer, W.4
  • 6
    • 0017345412 scopus 로고
    • Implications of combined treatment with 'Madopar' and L-deprenil in Parkinson's disease. A long-term study
    • Birkmayer, W., Riederer, P., Ambrozi, L., Youdim, M.B. Implications of combined treatment with 'Madopar' and L-deprenil in Parkinson's disease. A long-term study. Lancet 1977, 1: 439-43.
    • (1977) Lancet , vol.1 , pp. 439-443
    • Birkmayer, W.1    Riederer, P.2    Ambrozi, L.3    Youdim, M.B.4
  • 7
    • 0017729733 scopus 로고
    • Deprenyl in Parkinson's disease
    • Lees, A.J., Shaw, K.M., Kohout, L.J. et al. Deprenyl in Parkinson's disease. Lancet 1977, 2: 791-5.
    • (1977) Lancet , vol.2 , pp. 791-795
    • Lees, A.J.1    Shaw, K.M.2    Kohout, L.J.3
  • 8
    • 0006093024 scopus 로고
    • Selegiline and Parkinson's disease
    • Parkinson Study Group (Datatop). Selegiline and Parkinson's disease. N Engl J Med 1989, 321: 1364-71.
    • (1989) N Engl J Med , vol.321 , pp. 1364-1371
  • 9
    • 0022365018 scopus 로고
    • Increased life expectancy resulting from addition of L-deprenyl to Madopar treatment in Parkinson's disease: A long-term study
    • Birkmayer, W., Knoll, J., Riederer, P., Youdim, M.B., Hars, V., Marton, J. Increased life expectancy resulting from addition of L-deprenyl to Madopar treatment in Parkinson's disease: A long-term study. J Neural Transm 1985, 64: 113-27.
    • (1985) J Neural Transm , vol.64 , pp. 113-127
    • Birkmayer, W.1    Knoll, J.2    Riederer, P.3    Youdim, M.B.4    Hars, V.5    Marton, J.6
  • 10
    • 0006122290 scopus 로고
    • Selegiline in Parkinson's Disease: An update
    • Riederer, P., Rinne U.K. Selegiline in Parkinson's Disease: An update. Mov Disords 1992, 8 (Suppl. 1): 51-44.
    • (1992) Mov Disords , vol.8 , Issue.SUPPL. 1 , pp. 51-144
    • Riederer, P.1    Rinne, U.K.2
  • 11
    • 0017186551 scopus 로고
    • The action of acetylenic inhibitors on mitochondrial monoamine oxidase: Structure of the flavin site in the inhibited enzyme
    • Elsevier, Amsterdam
    • Maycock, A.L., Abeles, R.H., Salach, J., Singer, T.P. The action of acetylenic inhibitors on mitochondrial monoamine oxidase: Structure of the flavin site in the inhibited enzyme. Ciba Foundation Symposium, Elsevier, Amsterdam 1976, 39: 33-49.
    • (1976) Ciba Foundation Symposium , vol.39 , pp. 33-49
    • Maycock, A.L.1    Abeles, R.H.2    Salach, J.3    Singer, T.P.4
  • 13
    • 0018068203 scopus 로고
    • Amphetamine and 2-phenylethylamine in post mortem Parkinson brains after I-deprenyl administration
    • Reynolds, G.P., Riederer, P., Sandler, N.R., Jellinger, K., Seemali, D. Amphetamine and 2-phenylethylamine in post mortem Parkinson brains after I-deprenyl administration. J Neural Transm 1978, 3: 271-8.
    • (1978) J Neural Transm , vol.3 , pp. 271-278
    • Reynolds, G.P.1    Riederer, P.2    Sandler, N.R.3    Jellinger, K.4    Seemali, D.5
  • 14
    • 0016829477 scopus 로고
    • Effects of monoamine oxidase inhibition by clorgyline, deprenil or tranylcypromine on 5-hydroxytryptamine concentrations in rat brain and hyperactivity following subsequent tryptophan administration
    • Green, A.R., Youdim, M.B. Effects of monoamine oxidase inhibition by clorgyline, deprenil or tranylcypromine on 5-hydroxytryptamine concentrations in rat brain and hyperactivity following subsequent tryptophan administration. Br J Pharmacol 1975, 55: 415-22.
    • (1975) Br J Pharmacol , vol.55 , pp. 415-422
    • Green, A.R.1    Youdim, M.B.2
  • 15
    • 0018139965 scopus 로고
    • Evidence that deprenyl, a type B monoamine oxidase inhibitor is an indirectly acting sympathomimetic amine
    • Simpson, L.L. Evidence that deprenyl, a type B monoamine oxidase inhibitor is an indirectly acting sympathomimetic amine. Biochem Pharmacol 1978, 27: 1591-5.
    • (1978) Biochem Pharmacol , vol.27 , pp. 1591-1595
    • Simpson, L.L.1
  • 16
    • 0019462668 scopus 로고
    • Tyramine antagonistic properties of AGN 1135, an irreversible inhibitor of monoamine oxidase type B
    • Finberg, J.P.M., Tenne, M., Youdim, M.B.H. Tyramine antagonistic properties of AGN 1135, an irreversible inhibitor of monoamine oxidase type B. Br J Pharmacol 1981, 73: 65-74.
    • (1981) Br J Pharmacol , vol.73 , pp. 65-74
    • Finberg, J.P.M.1    Tenne, M.2    Youdim, M.B.H.3
  • 17
    • 84878744562 scopus 로고    scopus 로고
    • R-Enantiomers of N-propargyl-aminoindan compounds. Their preparation and pharmaceutical composition containing them. US Patent 1995, 5: 457, 133; NCI 1420, 1-8
    • Youdim, M.B.H., Finberg, J.P.M., Levy, R. et al. R-Enantiomers of N-propargyl-aminoindan compounds. Their preparation and pharmaceutical composition containing them. US Patent 1995, 5: 457, 133; NCI 1420, 1-8.
    • Youdim, M.B.H.1    Finberg, J.P.M.2    Levy, R.3
  • 18
    • 0031596711 scopus 로고    scopus 로고
    • (R) (+)-N-propargyl-1-aminoindan (rasagiline) and derivatives: Highly selective and potent inhibitors of monoamine oxidase B
    • Sterling, J., Veinberg, A., Lerner, D. et al. (R) (+)-N-propargyl-1- aminoindan (rasagiline) and derivatives: Highly selective and potent inhibitors of monoamine oxidase B. J Neural Transm Suppl 1998, 52: 301-5.
    • (1998) J Neural Transm Suppl , vol.52 , pp. 301-305
    • Sterling, J.1    Veinberg, A.2    Lerner, D.3
  • 19
    • 0037153195 scopus 로고    scopus 로고
    • Novel dual inhibitors of AChE and MAO derived from hydroxy aminoindan and phenethylamine as 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 phenethylamine as potential treatment for Alzheimer's disease. J Med Chem 2002, 45: 5260-79.
    • (2002) J Med Chem , vol.45 , pp. 5260-5279
    • Sterling, J.1    Herzig, Y.2    Goren, T.3
  • 20
    • 0000031465 scopus 로고
    • Selective inhibition of monoamine oxidase type B by propargyl-containing drugs
    • Sabbagh, A., Youdim, M.B.H. Selective inhibition of monoamine oxidase type B by propargyl-containing drugs. Israel J Med Sci 1978, 14: 1097.
    • (1978) Israel J Med Sci , vol.14 , pp. 1097
    • Sabbagh, A.1    Youdim, M.B.H.2
  • 21
    • 0019429465 scopus 로고
    • Selective "suicide" acetylenic and reversible inhibitors of monoamine oxidase A and B
    • Kalir, A., Sabbagh, A., Youdim, M.B.H. Selective "suicide" acetylenic and reversible inhibitors of monoamine oxidase A and B. Br J Pharmacol 1981, 73: 55-64.
    • (1981) Br J Pharmacol , vol.73 , pp. 55-64
    • Kalir, A.1    Sabbagh, A.2    Youdim, M.B.H.3
  • 22
    • 0035130289 scopus 로고    scopus 로고
    • Rasagiline [N-Propargyl-1R(+)-aminoindant], a selective and potent inhibitor of mitochondrial monoamine oxidase B
    • Youdim, M.B.H., Gross, A., Finberg, J.P.M. Rasagiline [N-Propargyl-1R(+)-aminoindant], A selective and potent inhibitor of mitochondrial monoamine oxidase B. Br J Pharmacol 2001, 132: 500-6.
    • (2001) Br J Pharmacol , vol.132 , pp. 500-506
    • Youdim, M.B.H.1    Gross, A.2    Finberg, J.P.M.3
  • 23
    • 0023209438 scopus 로고
    • MAO type B inhibitors as adjunct to L-dopa therapy
    • Youdim, M.B., Finberg, J.P. MAO type B inhibitors as adjunct to L-dopa therapy. Adv Neurol 1987, 45: 127-36.
    • (1987) Adv Neurol , vol.45 , pp. 127-136
    • Youdim, M.B.1    Finberg, J.P.2
  • 24
    • 0031596702 scopus 로고    scopus 로고
    • Increased striatal dopamine production from L-DOPA following selective inhibition of monoamine oxidase B by R(+)-N-propargyl-1-aminoindan (rasagiline) in the monkey
    • Finberg, J.P., Wang, J., Bankiewicz, K., Harvey-White, J., Kopin, I.J., Goldstein, D.S. Increased striatal dopamine production from L-DOPA following selective inhibition of monoamine oxidase B by R(+)-N-propargyl-1-aminoindan (rasagiline) in the monkey. J Neural Transm 1998, 52: 279-85.
    • (1998) J Neural Transm , vol.52 , pp. 279-285
    • Finberg, J.P.1    Wang, J.2    Bankiewicz, K.3    Harvey-White, J.4    Kopin, I.J.5    Goldstein, D.S.6
  • 26
    • 0036894795 scopus 로고    scopus 로고
    • A controlled trial of rasagiline in early Parkinson disease: The TEMPO Study
    • Parkinson Study Group. A controlled trial of rasagiline in early Parkinson disease: The TEMPO Study. Arch Neurol 2002, 59: 1937-43.
    • (2002) Arch Neurol , vol.59 , pp. 1937-1943
  • 27
    • 2342655732 scopus 로고    scopus 로고
    • A controlled, randomized, delayed-start study of rasagiline in early Parkinson disease
    • Parkinson Study Group. A controlled, randomized, delayed-start study of rasagiline in early Parkinson disease. Arch Neurol 2004, 61: 561-6.
    • (2004) Arch Neurol , vol.61 , pp. 561-566
  • 28
    • 0022401727 scopus 로고
    • Modification of blood pressure and nictitating membrane response to sympathetic amines by selective monoamine oxidase inhibitors of types a and B in the cat
    • Finberg, J.P.M., Youdim, M.B.H. Modification of blood pressure and nictitating membrane response to sympathetic amines by selective monoamine oxidase inhibitors of types A and B in the cat. Br J Pharmacol 1985, 85: 541-6.
    • (1985) Br J Pharmacol , vol.85 , pp. 541-546
    • Finberg, J.P.M.1    Youdim, M.B.H.2
  • 29
    • 0034519674 scopus 로고    scopus 로고
    • Rasagiline mesylate, a new MAO-B inhibitor for the treatment of Parkinson's disease: A double-blind study as adjunctive therapy to levodopa
    • Rabey, J.M., Sagi, I., Huberman, M. et al.; Rasagiline Study Group. Rasagiline mesylate, a new MAO-B inhibitor for the treatment of Parkinson's disease: A double-blind study as adjunctive therapy to levodopa. Clin Neuropharmacol 2000, 23: 324-30.
    • (2000) Clin Neuropharmacol , vol.23 , pp. 324-330
    • Rabey, J.M.1    Sagi, I.2    Huberman, M.3
  • 30
    • 33544464417 scopus 로고    scopus 로고
    • unpublished data
    • Largo Study Group, 2003 (unpublished data).
    • (2003)
  • 31
    • 13444302612 scopus 로고    scopus 로고
    • A randomized placebo-controlled trial of rasagiline in levodopa-treated patients with Parksinson disease and motor fluctuations. The PRESTO Study
    • Parkinson Study Group. A randomized placebo-controlled trial of rasagiline in levodopa-treated patients with Parksinson disease and motor fluctuations. The PRESTO Study. Arch Neurol 2005, 62: 241-8.
    • (2005) Arch Neurol , vol.62 , pp. 241-248
  • 34
    • 0015186769 scopus 로고
    • The covalently bound flavin of hepatic monoamine oxidase I. Isolation and sequence of a flavin peptide and evidence for binding to the 8-position
    • Kearney, FB., Salach, J.I., Walker, W.H. et al. The covalently bound flavin of hepatic monoamine oxidase I. Isolation and sequence of a flavin peptide and evidence for binding to the 8-position. Eur J Biochem 1971, 24: 321-7.
    • (1971) Eur J Biochem , vol.24 , pp. 321-327
    • Kearney, F.B.1    Salach, J.I.2    Walker, W.H.3
  • 35
    • 0024042954 scopus 로고
    • CDNA cloning of human liver monoamine oxidase a and B: Molecular basis of differences in enzymatic properties
    • Bach, A.W.J., Lan, N.C., Johnson, D.L. et al. cDNA cloning of human liver monoamine oxidase A and B: Molecular basis of differences in enzymatic properties. Proc Nat Acad Sci USA 1988, 85: 4934-8.
    • (1988) Proc Nat Acad Sci USA , vol.85 , pp. 4934-4938
    • Bach, A.W.J.1    Lan, N.C.2    Johnson, D.L.3
  • 37
    • 0015690527 scopus 로고
    • The oestrous cycle and monoamine oxidase activity
    • Holzbauer, M., Youdim, M.B. The oestrous cycle and monoamine oxidase activity. Br J Pharmacol 1973, 48: 600-8.
    • (1973) Br J Pharmacol , vol.48 , pp. 600-608
    • Holzbauer, M.1    Youdim, M.B.2
  • 38
    • 0027981209 scopus 로고
    • Slow recovery of human brain MAO B after deprenyl (selegiline) withdrawal
    • Fowler, J.S., Volkow, N.D., Logan, J. et al. Slow recovery of human brain MAO B after deprenyl (selegiline) withdrawal. Synapse 1994, 18: 86-93.
    • (1994) Synapse , vol.18 , pp. 86-93
    • Fowler, J.S.1    Volkow, N.D.2    Logan, J.3
  • 39
    • 0024556215 scopus 로고
    • Steroid regulation of monoamine oxidase activity in the adrenal medulla
    • Youdim, M.B., Banerjee, D.K., Keiner, K., Offutt, L., Pollard, H.B. Steroid regulation of monoamine oxidase activity in the adrenal medulla. FASEB J 1989, 3: 1753-9.
    • (1989) FASEB J , vol.3 , pp. 1753-1759
    • Youdim, M.B.1    Banerjee, D.K.2    Keiner, K.3    Offutt, L.4    Pollard, H.B.5
  • 40
    • 0027496797 scopus 로고
    • The relevance of glial monoamine oxidase-B and polyamines to the action of selegiline in Parkinson's disease
    • Youdim, M.B., Riederer, P. The relevance of glial monoamine oxidase-B and polyamines to the action of selegiline in Parkinson's disease. Mov Disord 1993, 8 (Suppl. 1): S8-S13.
    • (1993) Mov Disord , vol.8 , Issue.SUPPL. 1
    • Youdim, M.B.1    Riederer, P.2
  • 41
    • 0036162584 scopus 로고    scopus 로고
    • Rat striatal monoamine oxidase-B inhibition by i-deprenyl and rasagiline: Its relationship to 2-phenylethylamine-induced stereotypy and Parkinson's disease
    • Youdim, M.B., Tipton, K.F. Rat striatal monoamine oxidase-B inhibition by i-deprenyl and rasagiline: Its relationship to 2-phenylethylamine-induced stereotypy and Parkinson's disease. Parkinsonism Relat Disord 2002, 8: 247-53.
    • (2002) Parkinsonism Relat Disord , vol.8 , pp. 247-253
    • Youdim, M.B.1    Tipton, K.F.2
  • 42
    • 0034941767 scopus 로고    scopus 로고
    • The anti-Parkinson drug rasagiline and its cholinesterase inhibitor derivatives exert neuroprotection unrelated to MAO inhibition in cell culture and in vivo
    • Youdim, M.B.H., Wadia, A., Tatton, N.A., Weinstock, M. The anti-Parkinson drug rasagiline and its cholinesterase inhibitor derivatives exert neuroprotection unrelated to MAO inhibition in cell culture and in vivo. Ann NY Acad Sci 2001, 939: 450-8.
    • (2001) Ann NY Acad Sci , vol.939 , pp. 450-458
    • Youdim, M.B.H.1    Wadia, A.2    Tatton, N.A.3    Weinstock, M.4
  • 43
    • 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
    • Gotz, M.E., 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, 52(Suppl.): 271-8.
    • (1998) J Neural Transm , vol.52 , Issue.SUPPL. , pp. 271-278
    • Gotz, M.E.1    Breithaupt, W.2    Sautter, J.3
  • 44
    • 0022496317 scopus 로고
    • Monoamine oxidase activity and monoamine metabolism in brains of parkinsonian patients treated with I-deprenyl
    • Riederer, P., Youdim, M.B. Monoamine oxidase activity and monoamine metabolism in brains of parkinsonian patients treated with I-deprenyl. J Neurochem 1986, 46: 1359-65.
    • (1986) J Neurochem , vol.46 , pp. 1359-1365
    • Riederer, P.1    Youdim, M.B.2
  • 45
    • 0017755902 scopus 로고
    • Evidence for dopamine deamination by both type a and type B monoamine oxidase in rat brain in vivo and for degree of inhibition of enzyme necessary for increased function and activity of dopamine and 5-hydroxytryptamine
    • Green, A.R., Tordoff, A., Mitchel, B., Youdim, M.B.H. Evidence for dopamine deamination by both type A and type B monoamine oxidase in rat brain in vivo and for degree of inhibition of enzyme necessary for increased function and activity of dopamine and 5-hydroxytryptamine. Br J Pharmacol 1977, 60: 343-9.
    • (1977) Br J Pharmacol , vol.60 , pp. 343-349
    • Green, A.R.1    Tordoff, A.2    Mitchel, B.3    Youdim, M.B.H.4
  • 46
    • 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: 111-8.
    • (1986) Adv Neurol , vol.45 , pp. 111-118
    • Riederer, P.1    Konradi, C.2    Schay, V.3
  • 47
    • 0015270743 scopus 로고
    • Neuronal monoamine oxidase: Specific enzyme types and their rates of formation
    • Neff, N.H., Gordis, C. Neuronal monoamine oxidase: Specific enzyme types and their rates of formation. Adv Biochem Psychopharmacol 1972, 5: 307-24.
    • (1972) Adv Biochem Psychopharmacol , vol.5 , pp. 307-324
    • Neff, N.H.1    Gordis, C.2
  • 48
    • 0018844749 scopus 로고
    • The turnover of the a and B-forms of monoamine oxidase in rat liver
    • Della Corte, L., Tipton, K.F. The turnover of the A and B-forms of monoamine oxidase in rat liver. Biochem Pharmacol 1980, 29: 811-5.
    • (1980) Biochem Pharmacol , vol.29 , pp. 811-815
    • Della Corte, L.1    Tipton, K.F.2
  • 49
    • 0036914093 scopus 로고    scopus 로고
    • Pharmacological properties of the anti-Parkinson drug rasagiline, modification of endogenous brain amines, reserpine reversal, serotonergic and dopaminergic behaviours
    • Finberg, J.P., Youdim, M.B. Pharmacological properties of the anti-Parkinson drug rasagiline, modification of endogenous brain amines, reserpine reversal, serotonergic and dopaminergic behaviours. Neuropharmacology 2002, 43: 1110-18.
    • (2002) Neuropharmacology , vol.43 , pp. 1110-1118
    • Finberg, J.P.1    Youdim, M.B.2
  • 50
    • 0019944455 scopus 로고
    • Relationship between tyramine potentiation and selective inhibition of monoamine oxidase types a and B in the rat vas deferens
    • Finberg, J.P., Tenne, M. Relationship between tyramine potentiation and selective inhibition of monoamine oxidase types A and B in the rat vas deferens. Br J Pharmacol 1982, 77: 13-21.
    • (1982) Br J Pharmacol , vol.77 , pp. 13-21
    • Finberg, J.P.1    Tenne, M.2
  • 51
    • 0345308381 scopus 로고    scopus 로고
    • Rasagiline - An anti-Parkinson drug with neuroprotective activity
    • Youdim, M.B.H. Rasagiline - An anti-Parkinson drug with neuroprotective activity. Fut Drug Expert Neurotherap Rev 2003, 3: 737-49.
    • (2003) Fut Drug Expert Neurotherap Rev , vol.3 , pp. 737-749
    • Youdim, M.B.H.1
  • 52
    • 0029832455 scopus 로고    scopus 로고
    • Effect of long-term treatment with selective monoamine oxidase a and B inhibitors on dopamine release from rat striatum in vivo
    • Lamensdorf, I., Youdim, M.B., Finberg, J.P. Effect of long-term treatment with selective monoamine oxidase A and B inhibitors on dopamine release from rat striatum in vivo. J Neurochem 1996, 67: 1532-9.
    • (1996) J Neurochem , vol.67 , pp. 1532-1539
    • Lamensdorf, I.1    Youdim, M.B.2    Finberg, J.P.3
  • 53
    • 0032498811 scopus 로고    scopus 로고
    • Increased survival of dopaminergic neurons by rasagiline, a monoamine oxidase B inhibitor
    • Finberg, J.P., Takeshima, T., Johnston, J.M., Commissiong, J.W. Increased survival of dopaminergic neurons by rasagiline, a monoamine oxidase B inhibitor. Neuroreport 1998, 9: 703-7.
    • (1998) Neuroreport , vol.9 , pp. 703-707
    • Finberg, J.P.1    Takeshima, T.2    Johnston, J.M.3    Commissiong, J.W.4
  • 54
    • 0029832455 scopus 로고    scopus 로고
    • Effect of long-term treatment with selective monoamine oxidase a and B inhibitors on dopamine release from rat striatum in vivo
    • Lamensdorf, L., Youdim, M.B., Finberg, J.P. Effect of long-term treatment with selective monoamine oxidase A and B inhibitors on dopamine release from rat striatum in vivo. J Neurochem 1996, 67: 1532-9.
    • (1996) J Neurochem , vol.67 , pp. 1532-1539
    • Lamensdorf, L.1    Youdim, M.B.2    Finberg, J.P.3
  • 55
    • 0032955147 scopus 로고    scopus 로고
    • Effect of low-dose treatment with selegiline on dopamine transporter (DAT) expression and amphetamine-induced dopamine release in vivo
    • Lamensdorf, I., Porat, S., Simantov, R., Finberg, J.P. Effect of low-dose treatment with selegiline on dopamine transporter (DAT) expression and amphetamine-induced dopamine release in vivo. Br J Pharmacol 1999, 126: 997-1002.
    • (1999) Br J Pharmacol , vol.126 , pp. 997-1002
    • Lamensdorf, I.1    Porat, S.2    Simantov, R.3    Finberg, J.P.4
  • 56
    • 0015763585 scopus 로고
    • Beta-phenylethylamine: A specific substrate for type B monoamine oxidase of brain
    • Yang, H.Y., Neff, N.H. Beta-phenylethylamine: A specific substrate for type B monoamine oxidase of brain. J Pharmacol Exp Ther 1973, 187: 365-71.
    • (1973) J Pharmacol Exp Ther , vol.187 , pp. 365-371
    • Yang, H.Y.1    Neff, N.H.2
  • 59
    • 0016333002 scopus 로고
    • The use of selective monoamine oxidase inhibitor drugs to modify amine metabolism in brain
    • Neff, N.H., Yang, H.Y., Fuentes, J.A. The use of selective monoamine oxidase inhibitor drugs to modify amine metabolism in brain. Adv Biochem Psychopharmacol 1974, 12: 49-57.
    • (1974) Adv Biochem Psychopharmacol , vol.12 , pp. 49-57
    • Neff, N.H.1    Yang, H.Y.2    Fuentes, J.A.3
  • 60
    • 0024418295 scopus 로고
    • The novel neuropsychotropic agent milacemide is a specific enzyme-activated inhibitor of brain monoamine oxidase B
    • Janssens de Varebeke, P., Pauwels, G., Buyse, C. et al. The novel neuropsychotropic agent milacemide is a specific enzyme-activated inhibitor of brain monoamine oxidase B. J Neurochem 1989, 53: 1109-16.
    • (1989) J Neurochem , vol.53 , pp. 1109-1116
    • Janssens De Varebeke, P.1    Pauwels, G.2    Buyse, C.3
  • 61
    • 0027264145 scopus 로고
    • Dopamine metabolism and neurotransmission in primate brain in relationship to monoamine oxidase A and B inhibition
    • Youdim, M.B., Riederer, P. Dopamine metabolism and neurotransmission in primate brain in relationship to monoamine oxidase A and B inhibition. J Neural Transm Gen Sect 1993, 91: 181-95.
    • (1993) J Neural Transm Gen Sect , vol.91 , pp. 181-195
    • Youdim, M.B.1    Riederer, P.2
  • 62
    • 0022378166 scopus 로고
    • Prevention of MPTP neurotoxicity by AGN1133 and AGN-1135, selective inhibitors of monoamine oxidase
    • Heikkila, R.E., Duvoisin, R.C., Finberg, J.P., Youdim, M.B.H. Prevention of MPTP neurotoxicity by AGN1133 and AGN-1135, selective inhibitors of monoamine oxidase. B Eur J Pharmacol 1985, 116:3 13-7.
    • (1985) B Eur J Pharmacol , vol.116 , pp. 313-317
    • Heikkila, R.E.1    Duvoisin, R.C.2    Finberg, J.P.3    Youdim, M.B.H.4
  • 63
    • 0032101092 scopus 로고    scopus 로고
    • Sparing by rasagiline (TVP-1012) of cholinergic functions and behavior in the postnatal anoxia rat
    • Speiser, Z., Katzir, O., Rehavi, M., Zabarski, T., Cohen, S. Sparing by rasagiline (TVP-1012) of cholinergic functions and behavior in the postnatal anoxia rat. Pharmacol Biochem Behav 1998, 60: 387-93.
    • (1998) Pharmacol Biochem Behav , vol.60 , pp. 387-393
    • Speiser, Z.1    Katzir, O.2    Rehavi, M.3    Zabarski, T.4    Cohen, S.5
  • 64
    • 0031596710 scopus 로고    scopus 로고
    • Effects of N-propargyl-1-(R)aminoindan (rasagiline) in models of motor and cognition disorders
    • Speiser, Z., Levy, R., Cohen, S. Effects of N-propargyl-1-(R)aminoindan (rasagiline) in models of motor and cognition disorders. J Neural Transm Suppl 1998, 52: 287-300.
    • (1998) J Neural Transm Suppl , vol.52 , pp. 287-300
    • Speiser, Z.1    Levy, R.2    Cohen, S.3
  • 65
    • 0032999575 scopus 로고    scopus 로고
    • Neuroprotective effect of rasagiline, a selective monoamine oxidase-B inhibitor, against closed head injury in the mouse
    • Huang, W., Chen, Y., Shohami, E., Weinstock, M. Neuroprotective effect of rasagiline, a selective monoamine oxidase-B inhibitor, against closed head injury in the mouse. Eur J Pharmacol 1999, 366: 127-35.
    • (1999) Eur J Pharmacol , vol.366 , pp. 127-135
    • Huang, W.1    Chen, Y.2    Shohami, E.3    Weinstock, M.4
  • 66
    • 4644225112 scopus 로고    scopus 로고
    • Rasagiline alone and in combination with riluzole prolongs survival in an ALS mouse model
    • Waibel, S., Reuter, A., Malessa, S., Blaugrund, E., Ludolph, A.C. Rasagiline alone and in combination with riluzole prolongs survival in an ALS mouse model. J Neurol 2004, 251: 1080-4.
    • (2004) J Neurol , vol.251 , pp. 1080-1084
    • Waibel, S.1    Reuter, A.2    Malessa, S.3    Blaugrund, E.4    Ludolph, A.C.5
  • 67
    • 2342547676 scopus 로고    scopus 로고
    • Neuroprotective effect of rasagiline in a rodent model of Parkinson's disease
    • Blandini, F., Armentero, M.T., Fancellu, R., Blaugrund, E., Nappi, G. Neuroprotective effect of rasagiline in a rodent model of Parkinson's disease. Exp Neurol 2004, 187: 455-9.
    • (2004) Exp Neurol , vol.187 , pp. 455-459
    • Blandini, F.1    Armentero, M.T.2    Fancellu, R.3    Blaugrund, E.4    Nappi, G.5
  • 68
    • 0037461309 scopus 로고    scopus 로고
    • Neuroprotective agents for clinical trials in Parkinson's disease: A systematic assessment
    • Ravina, B.M., Fagan, S.C., Hart, R.G. et al. Neuroprotective agents for clinical trials in Parkinson's disease: A systematic assessment. Neurology 2003, 22, 60: 1234-40.
    • (2003) Neurology , vol.22-60 , pp. 1234-1240
    • Ravina, B.M.1    Fagan, S.C.2    Hart, R.G.3
  • 69
    • 0032726944 scopus 로고    scopus 로고
    • Neuroprotection by (-)-deprenyl and related compounds
    • Maruyama, W., Naoi, M. Neuroprotection by (-)-deprenyl and related compounds. Mech Ageing Dev 1999, 111: 189-200.
    • (1999) Mech Ageing Dev , vol.111 , pp. 189-200
    • Maruyama, W.1    Naoi, M.2
  • 70
    • 0034939146 scopus 로고    scopus 로고
    • Anti-apoptotic function of N-propargylamine-1(R)-and (S)-aminoindan, Rasagiline and TV1022
    • Maruyama, W., Youdim, M.B.H., Naoi, M. Anti-apoptotic function of N-propargylamine-1(R)-and (S)-aminoindan, Rasagiline and TV1022. Ann NY Acad Sci 2000, 939: 320-9.
    • (2000) Ann NY Acad Sci , vol.939 , pp. 320-329
    • Maruyama, W.1    Youdim, M.B.H.2    Naoi, M.3
  • 71
    • 0034525891 scopus 로고    scopus 로고
    • Neurotoxins induce apoptosis in dopamine neurons: Protection by N-propargylamine 1(R)-and (S)-aminoindan, rasagiline and TV1022
    • Maruyama, W., Akao, Y., Youdim, M.B.H., Naoi, M. Neurotoxins induce apoptosis in dopamine neurons: Protection by N-propargylamine 1(R)-and (S)-aminoindan, rasagiline and TV1022. J Neural Transm 2000, 60: 171-86.
    • (2000) J Neural Transm , vol.60 , pp. 171-186
    • Maruyama, W.1    Akao, Y.2    Youdim, M.B.H.3    Naoi, M.4
  • 72
    • 0034928655 scopus 로고    scopus 로고
    • Enantio-specific induction of apoptosis by an endogenous neurotoxin, N-methyl(R)salsolinol, in dopaminergic SH-SY5Y cells: Suppression of apoptosis by N-(2-heptyl)-N-methylpropargylamine
    • Maruyama, W., Boulton, A. A., Davis, B.A., Dostert, P., Naoi, M. Enantio-specific induction of apoptosis by an endogenous neurotoxin, N-methyl(R)salsolinol, in dopaminergic SH-SY5Y cells: Suppression of apoptosis by N-(2-heptyl)-N-methylpropargylamine. J Neural Transm 2001, 108: 11-24.
    • (2001) J Neural Transm , vol.108 , pp. 11-24
    • Maruyama, W.1    Boulton, A.A.2    Davis, B.A.3    Dostert, P.4    Naoi, M.5
  • 73
    • 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 dopaminergicneurotoxin, N-methyl(R)salsolinol
    • Maruyama, W., Akao, Y., Youdim, M.B., Davis, B.A., 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 dopaminergicneurotoxin, N-methyl(R)salsolinol. J Neurochem 2001, 78: 727-35.
    • (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
  • 74
    • 0036719861 scopus 로고    scopus 로고
    • Neuroprotection by propargylamines in Parkinson's disease: Suppression of apoptosis and induction of prosurvival genes
    • Maruyama, W., Akao, Y., Carrillo, M.C., Kitani, K., Youdium, M.B., Naoi, M. Neuroprotection by propargylamines in Parkinson's disease: Suppression of apoptosis and induction of prosurvival genes. Neurotoxicol Teratol 2002, 24: 675-82.
    • (2002) Neurotoxicol Teratol , vol.24 , pp. 675-682
    • Maruyama, W.1    Akao, Y.2    Carrillo, M.C.3    Kitani, K.4    Youdium, M.B.5    Naoi, M.6
  • 75
    • 0036206323 scopus 로고    scopus 로고
    • The anti-Parkinson drug, rasagiline, prevents apoptotic DNA damage induced 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 induced by peroxynitrite in human dopaminergic neuroblastoma SH-SY5Y cells. J Neural Transm 2002, 109:467-81.
    • (2002) J Neural Transm , vol.109 , pp. 467-481
    • Maruyama, W.1    Takahashi, T.2    Youdim, M.3    Naoi, M.4
  • 76
    • 0035568344 scopus 로고    scopus 로고
    • Molecular basis of neuroprotective activities of rasagiline and the anti-Alzheimer drug, TV3326, [(N-propargyl-(3R)aminoindan-5-yl)-ethyl methyl carbamate]
    • Youdim, M.B.H., Weinstock, M. Molecular basis of neuroprotective activities of rasagiline and the anti-Alzheimer drug, TV3326, [(N-propargyl-(3R)aminoindan-5-yl)-ethyl methyl carbamate]. Cell Mol Neurobiol 2002, 21: 555-73.
    • (2002) Cell Mol Neurobiol , vol.21 , pp. 555-573
    • Youdim, M.B.H.1    Weinstock, M.2
  • 77
    • 0033756901 scopus 로고    scopus 로고
    • Increased caspase 3 and Bax immunoreactivity accompany nuclear GAPDH translocation and neuronal apoptosis in Parkinson's disease
    • Tatton, N.A. Increased caspase 3 and Bax immunoreactivity accompany nuclear GAPDH translocation and neuronal apoptosis in Parkinson's disease. Exp Neurol 2000, 166: 29-43.
    • (2000) Exp Neurol , vol.166 , pp. 29-43
    • Tatton, N.A.1
  • 78
    • 0036229947 scopus 로고    scopus 로고
    • Propargylamines induce anti-apoptotic new protein synthesis in serum- and nerve growth factor (NGF)-withdrawn, NGF-differentiated PC-12 cells
    • Tatton, W.G., Chalmers-Redman, R.M., Ju, W.J. et al. Propargylamines induce anti-apoptotic new protein synthesis in serum- and nerve growth factor (NGF)-withdrawn, NGF-differentiated PC-12 cells. J Pharmacol Exp Therap 2002, 301, 753-64.
    • (2002) J Pharmacol Exp Therap , vol.301 , pp. 753-764
    • Tatton, W.G.1    Chalmers-Redman, R.M.2    Ju, W.J.3
  • 79
    • 0345237921 scopus 로고    scopus 로고
    • Anti-apoptotic 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, M.B., Nagai, M., Naoi, M. Anti-apoptotic 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: 233-6.
    • (2003) Neurosci Lett , vol.341 , pp. 233-236
    • Maruyama, W.1    Weinstock, M.2    Youdim, M.B.3    Nagai, M.4    Naoi, M.5
  • 80
    • 0036719861 scopus 로고    scopus 로고
    • Neuroprotection by propargylamines in Parkinson's disease: Suppression of apoptosis and induction of prosurvival genes
    • Maruyama, W., Akao, Y., Carrillo, M.C., Kitani, K., Youdium, M.B., Naoi, M. Neuroprotection by propargylamines in Parkinson's disease: Suppression of apoptosis and induction of prosurvival genes. Neurotoxicol Teratol 2002, 24: 675-82.
    • (2002) Neurotoxicol Teratol , vol.24 , pp. 675-682
    • Maruyama, W.1    Akao, Y.2    Carrillo, M.C.3    Kitani, K.4    Youdium, M.B.5    Naoi, M.6
  • 81
    • 0027530638 scopus 로고
    • Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease
    • Parkinson Study Group. Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease. N Engl J Med 1993, 328: 176-83.
    • (1993) N Engl J Med , vol.328 , pp. 176-183
  • 82
    • 0033231244 scopus 로고    scopus 로고
    • Rosagiline, a monoamine oxidase-B inhibitor, protects NGF-differentiated PC12 cells against oxygen-glucose deprivation
    • Abu-Raya, S., Blaugrund, E., Trembovler, V., Shilderman-Bloch, E., Shohami, E., Lazarovici, P. Rosagiline, a monoamine oxidase-B inhibitor, protects NGF-differentiated PC12 cells against oxygen-glucose deprivation. J Neurosci Res 1999, 58: 456-63.
    • (1999) J Neurosci Res , vol.58 , pp. 456-463
    • Abu-Raya, S.1    Blaugrund, E.2    Trembovler, V.3    Shilderman-Bloch, E.4    Shohami, E.5    Lazarovici, P.6
  • 83
    • 0037059430 scopus 로고    scopus 로고
    • Neuroprotective and neurotoxic effects of monoamine oxidase-B inhibitors and derived metabolites under ischemia in PC12 cells
    • Abu-Raya, S., Tabakman, R., Blaugrund, E., Trembovler, V., Lazarovici, P. Neuroprotective and neurotoxic effects of monoamine oxidase-B inhibitors and derived metabolites under ischemia in PC12 cells. Eur J Pharmacol 2002, 434: 109-16P.
    • (2002) Eur J Pharmacol , vol.434
    • Abu-Raya, S.1    Tabakman, R.2    Blaugrund, E.3    Trembovler, V.4    Lazarovici, P.5
  • 84
    • 1542317394 scopus 로고    scopus 로고
    • Contrasting neuroprotective and neurotoxic actions of respective metabolites of antiparkinson drugs rasagiline and selegiline
    • in press
    • Bar Am, O., Amit, T., Youdim, M.B.H. Contrasting neuroprotective and neurotoxic actions of respective metabolites of antiparkinson drugs rasagiline and selegiline. Neurosci Lett 2004, in press.
    • (2004) Neurosci Lett
    • Bar Am, O.1    Amit, T.2    Youdim, M.B.H.3
  • 85
    • 0032807402 scopus 로고    scopus 로고
    • Studies with rasagiline, a MAO-B inhibitor, in experimental focal ischemia in the rat
    • Speiser, Z., Mayk, A., Eliash, S., Cohen, S. Studies with rasagiline, a MAO-B inhibitor, in experimental focal ischemia in the rat. J Neural Transm 1999, 106: 59.
    • (1999) J Neural Transm , vol.106 , pp. 59
    • Speiser, Z.1    Mayk, A.2    Eliash, S.3    Cohen, S.4
  • 86
    • 0028181797 scopus 로고
    • (-)-Deprenyl alters the survival of adult murine facial motoneurons after axotomy: Increases in vulnerable C57BL strain but decreases in motor neuron degeneration mutants
    • Oh, C., Murray, B., Bhattacharya, N., Holland, D., Tatton, W.G. (-)-Deprenyl alters the survival of adult murine facial motoneurons after axotomy: Increases in vulnerable C57BL strain but decreases in motor neuron degeneration mutants. J Neurosci Res 1994, 38: 64-74.
    • (1994) J Neurosci Res , vol.38 , pp. 64-74
    • Oh, C.1    Murray, B.2    Bhattacharya, N.3    Holland, D.4    Tatton, W.G.5
  • 87
    • 0037198060 scopus 로고    scopus 로고
    • Novel neuroprotective anti-Alzheimer drugs with anti-depressant activity derived from the anti-Parkinson drug, rasagiline
    • Youdim, M.B., Weinstock, M. Novel neuroprotective anti-Alzheimer drugs with anti-depressant activity derived from the anti-Parkinson drug, rasagiline. Mech Ageing Dev 2002, 123: 1081-6.
    • (2002) Mech Ageing Dev , vol.123 , pp. 1081-1086
    • Youdim, M.B.1    Weinstock, M.2
  • 88
    • 0034705512 scopus 로고    scopus 로고
    • Enhancing effect of rasagiline on superoxide dismutase and catalase activities in the dopaminergic system in the rat
    • Carrillo, M.C., Minami, C., Kitani, K. et al. Enhancing effect of rasagiline on superoxide dismutase and catalase activities in the dopaminergic system in the rat. Life Sci 2000, 67: 577-85.
    • (2000) Life Sci , vol.67 , pp. 577-585
    • Carrillo, M.C.1    Minami, C.2    Kitani, K.3
  • 89
    • 0023029305 scopus 로고
    • Contrasting monoamine oxidase activity and tyramine induced catecholamine release in PC12 and chromaffin cells
    • Youdim, M.B., Heldman, E., Pollard, H.B., Fleming, P., McHugh, E. Contrasting monoamine oxidase activity and tyramine induced catecholamine release in PC12 and chromaffin cells. Neuroscience 1986, 19: 1311-8.
    • (1986) Neuroscience , vol.19 , pp. 1311-1318
    • Youdim, M.B.1    Heldman, E.2    Pollard, H.B.3    Fleming, P.4    McHugh, E.5
  • 90
    • 0036329996 scopus 로고    scopus 로고
    • Mitochondria determine the survival and death in apoptosis by an endogenous neurotoxin, N-methyl(R)salsolinol, and neuroprotection by propargylamines
    • Naoi, M., Maruyama, W., Akao, Y., Yi, H. Mitochondria determine the survival and death in apoptosis by an endogenous neurotoxin, N-methyl(R)salsolinol, and neuroprotection by propargylamines. J Neural Transm 2002, 109: 607-21.
    • (2002) J Neural Transm , vol.109 , pp. 607-621
    • Naoi, M.1    Maruyama, W.2    Akao, Y.3    Yi, H.4
  • 91
    • 0037321610 scopus 로고    scopus 로고
    • Attenuation of methamphetamine induced dopaminergic neurotoxicity by flupirtine: Microdialysis study on dopamine release and free radical generation
    • Gassen, M., Lamensdorf, I., Armony, T., Finberg, J.P., Youdim, M.B. Attenuation of methamphetamine induced dopaminergic neurotoxicity by flupirtine: Microdialysis study on dopamine release and free radical generation. J Neural Transm 2003, 110: 171-82.
    • (2003) J Neural Transm , vol.110 , pp. 171-182
    • Gassen, M.1    Lamensdorf, I.2    Armony, T.3    Finberg, J.P.4    Youdim, M.B.5
  • 92
    • 0032885411 scopus 로고    scopus 로고
    • Protection with metabotropic glutamate 1 receptor antagonists in models of ischemic neuronal death: Time-course and mechanisms
    • Pellegrini-Giampietro, D.E., Peruginelli, F., Meli, E. et al. Protection with metabotropic glutamate 1 receptor antagonists in models of ischemic neuronal death: Time-course and mechanisms. Neuropharmacology 1999, 38: 1607-19.
    • (1999) Neuropharmacology , vol.38 , pp. 1607-1619
    • Pellegrini-Giampietro, D.E.1    Peruginelli, F.2    Meli, E.3
  • 93
    • 23144451035 scopus 로고    scopus 로고
    • Genomic and proteomic profiling of the neuroprotective mechanism of rasagiline in the mouse model of PD
    • Sagi, Y., Mandel, S., Youdim, M.B.H. Genomic and proteomic profiling of the neuroprotective mechanism of rasagiline in the mouse model of PD. Neural Plsticity 2003, 10: 227.
    • (2003) Neural Plsticity , vol.10 , pp. 227
    • Sagi, Y.1    Mandel, S.2    Youdim, M.B.H.3
  • 94
    • 0141649550 scopus 로고    scopus 로고
    • The adenine nucleotide translocator: A new potential chemotherapeutic target
    • review
    • Belzacq, A.S., Brenner, C. The adenine nucleotide translocator: A new potential chemotherapeutic target. Curr Drug Targets 2003, 7: 517-24, review.
    • (2003) Curr Drug Targets , vol.7 , pp. 517-524
    • Belzacq, A.S.1    Brenner, C.2
  • 95
  • 96
  • 97
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: Another view
    • Halestrap, A.P., McStay, G.P., Clarke, S.J. The permeability transition pore complex: Another view. Biochimie 2002, 84: 153-66.
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 99
    • 0036677312 scopus 로고    scopus 로고
    • Mitochondrial permeability transition mediates apoptosis induced by N-methyl(R)salsolinol, an endogenous neurotoxin, and is inhibited by Bc1-2 and rasagiline, 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 is inhibited by Bc1-2 and rasagiline, N-propargyl-1 (R)-aminoindan. J Neurochem 2002, 82: 913-23.
    • (2002) J Neurochem , vol.82 , pp. 913-923
    • Akao, Y.1    Maruyama, W.2    Shimizu, S.3
  • 100
    • 0038322479 scopus 로고    scopus 로고
    • cDNA gene expression profile homology of antioxidants and their antiapoptotic and proapoptotic activities in human neuroblastoma cells
    • Weinreb, O., Mandel, S., Youdim, M.B. cDNA gene expression profile homology of antioxidants and their antiapoptotic and proapoptotic activities in human neuroblastoma cells. FASEB J 2003, 17: 935-7.
    • (2003) FASEB J , vol.17 , pp. 935-937
    • Weinreb, O.1    Mandel, S.2    Youdim, M.B.3
  • 101
    • 0642303109 scopus 로고    scopus 로고
    • The importance of propargylamine moiety in the anti-Parkinson drug rasagiline and its derivatives in MAPK-dependent amyloid precursor protein processing
    • Yogev-Falach, M., Amit, T., Bar-Am, O., Youdim M.B. The importance of propargylamine moiety in the anti-Parkinson drug rasagiline and its derivatives in MAPK-dependent amyloid precursor protein processing. FASEB J 2003, 17: 2325-7.
    • (2003) FASEB J , vol.17 , pp. 2325-2327
    • Yogev-Falach, M.1    Amit, T.2    Bar-Am, O.3    Youdim, M.B.4
  • 102
    • 33544467024 scopus 로고    scopus 로고
    • The neuroprotective activity of rasagiline and its propargyl moiety is dependent on activation/gene expression of protein kinase C (PKC)
    • Bar Am, O., Amit, T., Weinreb, O., Yogev-Falach, M., Youdim, M.B.H. The neuroprotective activity of rasagiline and its propargyl moiety is dependent on activation/gene expression of protein kinase C (PKC). Neural Plasticity 2003, 10: 183.
    • (2003) Neural Plasticity , vol.10 , pp. 183
    • Bar Am, O.1    Amit, T.2    Weinreb, O.3    Yogev-Falach, M.4    Youdim, M.B.H.5
  • 103
    • 33544467409 scopus 로고    scopus 로고
    • Gene and protein expression profiles of neuroprotective and anti-apoptotic action of rasagiline in PC-12 cell cultures
    • Weinreb, O., Bar Am, O., Chilag-Tamar, O., Amit, T., Youdim, M.B.H. Gene and protein expression profiles of neuroprotective and anti-apoptotic action of rasagiline in PC-12 cell cultures. Neural Plasticity 2003, 10: 238.
    • (2003) Neural Plasticity , vol.10 , pp. 238
    • Weinreb, O.1    Bar Am, O.2    Chilag-Tamar, O.3    Amit, T.4    Youdim, M.B.H.5
  • 104
    • 0035062462 scopus 로고    scopus 로고
    • Immunophilin ligands can prevent progressive e dopaminergic degeneration in animal models of Parkinson's disease
    • Constantini, L.C., Cole, D., Chatuvedi, P., Isacson, P. Immunophilin ligands can prevent progressive e dopaminergic degeneration in animal models of Parkinson's disease. J Eur Neurosci 2001, 13: 1085-92.
    • (2001) J Eur Neurosci , vol.13 , pp. 1085-1092
    • Constantini, L.C.1    Cole, D.2    Chatuvedi, P.3    Isacson, P.4
  • 105
    • 0037189081 scopus 로고    scopus 로고
    • 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, M.B., 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: 105-8.
    • (2002) Neurosci Lett , vol.326 , pp. 105-108
    • Akao, Y.1    Maruyama, W.2    Yi, H.3    Shamoto-Nagai, M.4    Youdim, M.B.5    Naoi, M.6
  • 106
    • 0038155162 scopus 로고    scopus 로고
    • Attenuation of MPTP-induced dopaminergic neurotoxicity by TV3326, a cholinesterase-monoamine oxidase inhibitor
    • Sagi, Y., Weinstock, M., Youdim, M.B.H. Attenuation of MPTP-Induced Dopaminergic Neurotoxicity by TV3326, A cholinesterase-monoamine oxidase inhibitor. J Neurochem 2003, 2: 290-7.
    • (2003) J Neurochem , vol.2 , pp. 290-297
    • Sagi, Y.1    Weinstock, M.2    Youdim, M.B.H.3
  • 107
    • 0023764824 scopus 로고    scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka, Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 1998, 334: 661-5.
    • (1998) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 108
    • 0022154427 scopus 로고
    • Tumor-promoting phorbol diester mimics two distinct neuronotrophic factors
    • Montz, H.P., Davis, G.E., Skaper, S.D., Manthorpe, M., Varon, S. Tumor-promoting phorbol diester mimics two distinct neuronotrophic factors. Brain Res 1985, 355: 150-4.
    • (1985) Brain Res , vol.355 , pp. 150-154
    • Montz, H.P.1    Davis, G.E.2    Skaper, S.D.3    Manthorpe, M.4    Varon, S.5
  • 109
    • 0022553361 scopus 로고
    • Protein kinase Casa component of a nerve growth factor-sensitive phosphorylation system in PC12 cells
    • Hama, T., Huang, K.P., Guroff, G. Protein kinase Casa component of a nerve growth factor-sensitive phosphorylation system in PC12 cells. Proc Natl Acad Sci USA 1986, 83: 2353-7.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2353-2357
    • Hama, T.1    Huang, K.P.2    Guroff, G.3
  • 110
    • 0034041345 scopus 로고    scopus 로고
    • Pharmacological demonstration of the differential involvement of protein kinase C isoforms in short- and long-term memory formation and retrieval of one-trial avoidance in rats
    • Vianna, M.R., Barros, D.M., Silva, T. et al. Pharmacological demonstration of the differential involvement of protein kinase C isoforms in short- and long-term memory formation and retrieval of one-trial avoidance in rats. Psychopharmacology (Berl) 2000, 150: 77-84.
    • (2000) Psychopharmacology (Berl) , vol.150 , pp. 77-84
    • Vianna, M.R.1    Barros, D.M.2    Silva, T.3
  • 111
    • 0029240533 scopus 로고
    • Changes in protein kinases in brain aging and Alzheimer's disease. Implications for drug therapy
    • Jin, L.W., Saitoh, T. Changes in protein kinases in brain aging and Alzheimer's disease. Implications for drug therapy. Drugs Aging 1995, 6: 136-49.
    • (1995) Drugs Aging , vol.6 , pp. 136-149
    • Jin, L.W.1    Saitoh, T.2
  • 112
    • 0025833830 scopus 로고
    • Protein kinase C alteration is an early biochemical marker in Alzheimer's disease
    • Masliah, E., Cole, G.M., Hansen, L.A. et al. Protein kinase C alteration is an early biochemical marker in Alzheimer's disease. J Neurosci 1991, 11: 2759-67.
    • (1991) J Neurosci , vol.11 , pp. 2759-2767
    • Masliah, E.1    Cole, G.M.2    Hansen, L.A.3
  • 113
    • 0027265320 scopus 로고
    • Assessment of protein kinase C isozymes by two-site enzyme immunoassay in human brains and changes in Alzheimer's disease
    • Shimohama, S., Narita, M., Matsushima, H., Kimura, J., Kameyama, M., Hagiwara M., Hidaka, H., Taniguchi, T. Assessment of protein kinase C isozymes by two-site enzyme immunoassay in human brains and changes in Alzheimer's disease. Neurology 1993, 43: 1407-13.
    • (1993) Neurology , vol.43 , pp. 1407-1413
    • Shimohama, S.1    Narita, M.2    Matsushima, H.3    Kimura, J.4    Kameyama, M.5    Hagiwara, M.6    Hidaka, H.7    Taniguchi, T.8
  • 115
    • 0028916836 scopus 로고
    • Membrane alterations as causes of impaired signal transduction in Alzheimer's disease and aging
    • Roth, G.S., Joseph, J.A., Mason, R.P. Membrane alterations as causes of impaired signal transduction in Alzheimer's disease and aging. Trends Neurosci 1995, 18: 203-6.
    • (1995) Trends Neurosci , vol.18 , pp. 203-206
    • Roth, G.S.1    Joseph, J.A.2    Mason, R.P.3
  • 116
    • 0028339544 scopus 로고
    • Attenuated protein kinase C activity and translocation in Alzheimer's disease brain
    • Wang, H.Y., Pisano, M.R., Friedman, E. Attenuated protein kinase C activity and translocation in Alzheimer's disease brain. Neurobiol Aging 1994, 15: 293-8.
    • (1994) Neurobiol Aging , vol.15 , pp. 293-298
    • Wang, H.Y.1    Pisano, M.R.2    Friedman, E.3
  • 117
    • 0025296205 scopus 로고
    • Processing of Alzheimer beta/A4 amyloid precursor protein: Modulation by agents that regulate protein phosphorylation
    • Buxbaum, J.D., Gandy, S.E., Cicchetti, P. et al. Processing of Alzheimer beta/A4 amyloid precursor protein: Modulation by agents that regulate protein phosphorylation. Proc Natl Acad Sci USA 1990, 87: 6003-6.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6003-6006
    • Buxbaum, J.D.1    Gandy, S.E.2    Cicchetti, P.3
  • 118
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch, R.M., Slack, B.E., Wurtman, R.J., Growdon, J.H. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 1992, 258: 304-7.
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 119
    • 0027487188 scopus 로고
    • Regulation by phorbol esters of amyloid precursor protein release from Swiss 3T3 fibroblasts overexpressing protein kinase C alpha
    • Slack, B.E., Nitsch, R.M., Livneh, E. et al. Regulation by phorbol esters of amyloid precursor protein release from Swiss 3T3 fibroblasts overexpressing protein kinase C alpha. J Biol Chem 1993, 268: 21097-101.
    • (1993) J Biol Chem , vol.268 , pp. 21097-21101
    • Slack, B.E.1    Nitsch, R.M.2    Livneh, E.3
  • 120
    • 0029379605 scopus 로고
    • Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease
    • Checler, F. Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease. J Neurochem 1995, 65: 1431-44.
    • (1995) J Neurochem , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 121
    • 0030921730 scopus 로고    scopus 로고
    • Increased secretion of the amino-terminal fragment of amyloid precursor protein in brains of rats with a constitutive up-regulation of protein kinase C
    • Caputi, A., Barindelli, S., Pastorino, L. et al. Increased secretion of the amino-terminal fragment of amyloid precursor protein in brains of rats with a constitutive up-regulation of protein kinase C. J Neurochem 1997, 68: 2523-9.
    • (1997) J Neurochem , vol.68 , pp. 2523-2529
    • Caputi, A.1    Barindelli, S.2    Pastorino, L.3
  • 122
    • 0030722499 scopus 로고    scopus 로고
    • In vivo regulation of amyloid precursor protein secretion in rat neocortex by cholinergic activity
    • Rossner, S., Ueberham, U., Yu, J. et al. In vivo regulation of amyloid precursor protein secretion in rat neocortex by cholinergic activity. Eur J Neurosci 1997, 9: 2125-34.
    • (1997) Eur J Neurosci , vol.9 , pp. 2125-2134
    • Rossner, S.1    Ueberham, U.2    Yu, J.3
  • 123
    • 0032693398 scopus 로고    scopus 로고
    • Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation
    • Lin, L., Georgievska, B., Mattsson, A., Isacson, O. Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation. Proc Natl Acad Sci USA 1999, 96: 12108-13.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12108-12113
    • Lin, L.1    Georgievska, B.2    Mattsson, A.3    Isacson, O.4
  • 124
    • 0036777108 scopus 로고    scopus 로고
    • The involvement of mitogen-activated protein (MAP) kinase in the regulation of amyloid precursor protein processing by novel cholinesterase inhibitors derived from rasagiline
    • Yogev-Falach, M., Amit, T., Bar-Am, O., Weinstock, M., Youdim, M.B.H. The involvement of mitogen-activated protein (MAP) kinase in the regulation of amyloid precursor protein processing by novel cholinesterase inhibitors derived from rasagiline. FASEB J 2002, 16: 1674-6.
    • (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
  • 125
    • 2642529309 scopus 로고    scopus 로고
    • Regulation of protein kinase C by the anti-Parkinson drug, MAO-B inhibitor, rasagiline and its derivatives, in vivo
    • Bar Am, O., Yogev-Falach, M., Amit, T., Sagi, Y., Youdim, M.B. Regulation of protein kinase C by the anti-Parkinson drug, MAO-B inhibitor, rasagiline and its derivatives, in vivo. J Neurochem 2004b, 89: 1119-25.
    • (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.5
  • 126
    • 0032566717 scopus 로고    scopus 로고
    • A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis
    • Ruvolo, P.P., Deng, X., Carr, B.K., May, W.S. A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis. J Biol Chem 1998, 273: 25436-42.
    • (1998) J Biol Chem , vol.273 , pp. 25436-25442
    • Ruvolo, P.P.1    Deng, X.2    Carr, B.K.3    May, W.S.4
  • 127
    • 0035380994 scopus 로고    scopus 로고
    • Bcl-2 over-expression and activation of protein kinase C suppress the trail-induced apoptosis in Jurkat T cells
    • Quo, B.C., Xu, Y.H. Bcl-2 over-expression and activation of protein kinase C suppress the trail-induced apoptosis in Jurkat T cells. Cell Res 2001, 11: 101-6.
    • (2001) Cell Res , vol.11 , pp. 101-106
    • Quo, B.C.1    Xu, Y.H.2
  • 128
    • 6944242126 scopus 로고    scopus 로고
    • Neuroprotection via pro-survival protein kinase C isoforms associated with Bcl-2 family members
    • Weinreb, O., Bar-Am, O., Amit, T., Chillag-Talmor, O., Youdim, M.B. Neuroprotection via pro-survival protein kinase C isoforms associated with Bcl-2 family members. FASEB J 2004, 18: 1471-3.
    • (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.5
  • 129
    • 0027444597 scopus 로고
    • AVP-induced activation of MAP kinase in vascular smooth muscle cells is mediated through protein kinase C
    • Kribben, A., Wieder, E.D., Li, X. et al. AVP-induced activation of MAP kinase in vascular smooth muscle cells is mediated through protein kinase C. Am J Physiol 1993, 265: C939-45.
    • (1993) Am J Physiol , vol.265
    • Kribben, A.1    Wieder, E.D.2    Li, X.3
  • 130
    • 0035341268 scopus 로고    scopus 로고
    • How protein kinase C activation protects nerve cells from oxidative stress-induced cell death
    • Maher, P. How protein kinase C activation protects nerve cells from oxidative stress-induced cell death. J Neurosci 2001, 21: 2929-38.
    • (2001) J Neurosci , vol.21 , pp. 2929-2938
    • Maher, P.1
  • 131
    • 0033971901 scopus 로고    scopus 로고
    • Bcl-2 family: Life-or-death switch
    • Tsujimoto, Y., Shimizu, S. Bcl-2 family: life-or-death switch. FEBS Lett 2000, 466: 6-10.
    • (2000) FEBS Lett , vol.466 , pp. 6-10
    • Tsujimoto, Y.1    Shimizu, S.2
  • 132
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • Aderem, A. The MARCKS brothers: A family of protein kinase C substrates. Cell 1992, 71: 713-6.
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1
  • 133
    • 0027171638 scopus 로고
    • Protein kinase C phosphorylates Ser152, Ser156 and Ser163 but not Ser160 of MARCKS in rat brain
    • Heemskerk, F.M., Chen, H.C., Huang F.L. Protein kinase C phosphorylates Ser152, Ser156 and Ser163 but not Ser160 of MARCKS in rat brain. Biochem Biophys Res Commun 1993, 190: 236-41.
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 236-241
    • Heemskerk, F.M.1    Chen, H.C.2    Huang, F.L.3
  • 134
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrates
    • Blackshear, P.J. The MARCKS family of cellular protein kinase C substrates. J Biol Chem 1993, 268: 1501-4.
    • (1993) J Biol Chem , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 135
    • 0032479804 scopus 로고    scopus 로고
    • Distribution of the protein kinase C substrates MARCKS and MRP in the postnatal developing rat brain
    • McNamara, R.K., Lenox, R.H. Distribution of the protein kinase C substrates MARCKS and MRP in the postnatal developing rat brain. J Neurol 1998, 397: 337-56.
    • (1998) J Neurol , vol.397 , pp. 337-356
    • McNamara, R.K.1    Lenox, R.H.2
  • 136
    • 0032564337 scopus 로고    scopus 로고
    • Effect of reduced myristoylated alanine-rich C kinase substrate expression on hippocampal mossy fiber development and spatial learning in mutant mice: Transgenic rescue and interactions with gene background
    • McNamara, R.K., Stumpo, D.J., Morel, L.M. et al. Effect of reduced myristoylated alanine-rich C kinase substrate expression on hippocampal mossy fiber development and spatial learning in mutant mice: Transgenic rescue and interactions with gene background. Proc Natl Acad Sci USA 1998, 95: 14517-22.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14517-14522
    • McNamara, R.K.1    Stumpo, D.J.2    Morel, L.M.3
  • 137
    • 0027379653 scopus 로고
    • Hyperactivation of signal transduction systems in Alzheimer's disease
    • Saitoh, T., Horsburgh, K., Masliah, E. Hyperactivation of signal transduction systems in Alzheimer's disease. Ann NY Acad Sci 1993, 695: 34-41.
    • (1993) Ann NY Acad Sci , vol.695 , pp. 34-41
    • Saitoh, T.1    Horsburgh, K.2    Masliah, E.3
  • 138
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen, D. Localization of protein kinases by anchoring proteins: A theme in signal transduction. Science 1995, 268: 247-51.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 139
    • 0030813899 scopus 로고    scopus 로고
    • The role of anchoring protein RACK1 in PKC activation in the ageing rat brain
    • Battaini, F., Pascale, A., Paoletti, R., Govoni, S. The role of anchoring protein RACK1 in PKC activation in the ageing rat brain. Trends Neurosci 1997, 20: 410-5.
    • (1997) Trends Neurosci , vol.20 , pp. 410-415
    • Battaini, F.1    Pascale, A.2    Paoletti, R.3    Govoni, S.4
  • 140
    • 0032865258 scopus 로고    scopus 로고
    • Protein kinase C anchoring deficit in postmortem brains of Alzheimer's disease patients
    • Battaini, F., Pascale, A., Lucchi, L., Pasinetti, G.M., Govoni, S. Protein kinase C anchoring deficit in postmortem brains of Alzheimer's disease patients. Exp Neurol 1999, 159: 559-64.
    • (1999) Exp Neurol , vol.159 , pp. 559-564
    • Battaini, F.1    Pascale, A.2    Lucchi, L.3    Pasinetti, G.M.4    Govoni, S.5
  • 141
    • 0031985192 scopus 로고    scopus 로고
    • Peripheral markers in testing pathophysiological hypotheses and diagnosing Alzheimer's disease
    • Gasparini, L., Racchi, M., Binetti, G. et al. Peripheral markers in testing pathophysiological hypotheses and diagnosing Alzheimer's disease. FASEB J 1998, 12: 17-34.
    • (1998) FASEB J , vol.12 , pp. 17-34
    • Gasparini, L.1    Racchi, M.2    Binetti, G.3
  • 142
    • 0032960305 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein cleavage
    • Mills, J., Reiner, P.B. Regulation of amyloid precursor protein cleavage. J Neurochem 1999, 72: 443-60.
    • (1999) J Neurochem , vol.72 , pp. 443-460
    • Mills, J.1    Reiner, P.B.2
  • 143
    • 0032498135 scopus 로고    scopus 로고
    • Specific role for protein kinase C alpha in the constitutive and regulated secretion of amyloid precursor protein in human skin fibroblasts
    • Benussi, L., Govoni, S., Gasparini, L. et al. Specific role for protein kinase C alpha in the constitutive and regulated secretion of amyloid precursor protein in human skin fibroblasts. Neurosci Lett 1998, 240: 97-101.
    • (1998) Neurosci Lett , vol.240 , pp. 97-101
    • Benussi, L.1    Govoni, S.2    Gasparini, L.3
  • 144
    • 0028965767 scopus 로고
    • Conventional protein kinase C (PKC)-alpha and novel PKC epsilon, but not -delta, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts
    • Kinouchi T., Sorimachi H., Maruyama K. et al. Conventional protein kinase C (PKC)-alpha and novel PKC epsilon, but not -delta, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts. FEBS Lett 1995, 364: 203-6.
    • (1995) FEBS Lett , vol.364 , pp. 203-206
    • Kinouchi, T.1    Sorimachi, H.2    Maruyama, K.3
  • 145
    • 0035951755 scopus 로고    scopus 로고
    • Blockade of PKC epsilon activation attenuates phorbol ester-induced increase of alpha-secretase-derived secreted form of amyloid precursor protein
    • Yeon, S.W., Jung, M.W., Ha, M.J. et al. Blockade of PKC epsilon activation attenuates phorbol ester-induced increase of alpha-secretase-derived secreted form of amyloid precursor protein. Biochem Biophys Res Commun 2001, 280: 782-7.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 782-787
    • Yeon, S.W.1    Jung, M.W.2    Ha, M.J.3
  • 146
    • 0346848857 scopus 로고    scopus 로고
    • N-Propargyl-l (R)-aminoindan, rasagiline, increases glial cell line-derived neurotrophic factor (GDNF) in neuroblastoma SH-SY5Y cells through activation of NF-kappaB transcription factor
    • Maruyama, W., Nitta, A., Shamoto-Nagai, M. et al. N-Propargyl-l (R)-aminoindan, rasagiline, increases glial cell line-derived neurotrophic factor (GDNF) in neuroblastoma SH-SY5Y cells through activation of NF-kappaB 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
  • 147
    • 0032590061 scopus 로고    scopus 로고
    • Nuclear factor-KB/Rel proteins: A point of convergence of signaling pathway relevant in neuronal function and dysfunction
    • Grilli, M., Memo, M. Nuclear factor-KB/Rel proteins: A point of convergence of signaling pathway relevant in neuronal function and dysfunction. Biochem Pharmacol 1999, 57: 1-7.
    • (1999) Biochem Pharmacol , vol.57 , pp. 1-7
    • Grilli, M.1    Memo, M.2
  • 148
    • 0030983079 scopus 로고    scopus 로고
    • Transcription factor NF-κB is activated in primary neurons by amyloid beta peptides and in neurons surrounding early plaques from patients with Alzheimer disease
    • Kaltschmidt, B., Uherek, M., Volk, B., Baeuerle, P.A., Kaltschmidt, C. Transcription factor NF-κB is activated in primary neurons by amyloid beta peptides and in neurons surrounding early plaques from patients with Alzheimer disease. Proc Natl Acad Sci USA 1997, 94: 2642-7.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2642-2647
    • Kaltschmidt, B.1    Uherek, M.2    Volk, B.3    Baeuerle, P.A.4    Kaltschmidt, C.5
  • 149
    • 0030842085 scopus 로고    scopus 로고
    • Nuclear translocation of NF-κB is increased in dopaminergic neurons of patients with Parkinson disease
    • Hunot, S., Brugg, B., Ricard, D. et al. Nuclear translocation of NF-κB is increased in dopaminergic neurons of patients with Parkinson disease. Proc Natl Acad Sci USA 1997, 94: 7531-6.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7531-7536
    • Hunot, S.1    Brugg, B.2    Ricard, D.3
  • 150
    • 0031938280 scopus 로고    scopus 로고
    • Nuclear factor-κB contributes to excitotoxin-induced apoptosis in rat striatum
    • Qin, Z.H., Wang, Y., Nakai, M., Chase, T.N. Nuclear factor-κB contributes to excitotoxin-induced apoptosis in rat striatum. Mol Pharmacol 1998, 53: 33-42.
    • (1998) Mol Pharmacol , vol.53 , pp. 33-42
    • Qin, Z.H.1    Wang, Y.2    Nakai, M.3    Chase, T.N.4
  • 151
    • 0035983531 scopus 로고    scopus 로고
    • NFκ-B-mediated up-regulation of Bcl-Xs and Bax contributes to cytochrome c release in cyanide-induced apoptosis
    • Shou, Y., Li, N., Li, L., Borowitz, J.L., Isom, G.F. NFκ-B-mediated up-regulation of Bcl-Xs and Bax contributes to cytochrome c release in cyanide-induced apoptosis. J Neurochem 2002, 81: 842-8.
    • (2002) J Neurochem , vol.81 , pp. 842-848
    • Shou, Y.1    Li, N.2    Li, L.3    Borowitz, J.L.4    Isom, G.F.5
  • 152
    • 0030026613 scopus 로고    scopus 로고
    • Ceramide protects hippocampal neurons against excitotoxic and oxidative insults, and amyloid beta-peptide toxicity
    • Goodman, Y., Mattson, M.P. Ceramide protects hippocampal neurons against excitotoxic and oxidative insults, and amyloid beta-peptide toxicity. J Neurochem 1996, 66: 869-72.
    • (1996) J Neurochem , vol.66 , pp. 869-872
    • Goodman, Y.1    Mattson, M.P.2
  • 153
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin, M., Ben-Neriah, Y. Phosphorylation meets ubiquitination: The control of NF-κB activity. Ann Rev Immunol 2000, 18: 621-63.
    • (2000) Ann Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 154
    • 0034322370 scopus 로고    scopus 로고
    • Suppression of NF-κB activity by sulfasalazine is mediated by direct inhibition of IκB kinases alpha and beta
    • Weber, C.K., Liptay, S., Wirth, T., Adler, G., Schinid, R.M. Suppression of NF-κB activity by sulfasalazine is mediated by direct inhibition of IκB kinases alpha and beta. Gastroenterology 2000, 119: 1209-18.
    • (2000) Gastroenterology , vol.119 , pp. 1209-1218
    • Weber, C.K.1    Liptay, S.2    Wirth, T.3    Adler, G.4    Schinid, R.M.5
  • 156
    • 85047698430 scopus 로고    scopus 로고
    • Delayed delivery of AAV-GDNF prevents nigral neurodegeneration and promotes functional recovery in a rat model of Parkinson's disease
    • Wang, L., Muramatsu, S., Lu, Y. et al. Delayed delivery of AAV-GDNF prevents nigral neurodegeneration and promotes functional recovery in a rat model of Parkinson's disease. Gene Ther 2002, 9: 381-9.
    • (2002) Gene Ther , vol.9 , pp. 381-389
    • Wang, L.1    Muramatsu, S.2    Lu, Y.3
  • 157
    • 0037096359 scopus 로고    scopus 로고
    • Lentivirally delivered glial cell line-derived neurotrophic factor increases the number of striatal dopaminergic neurons in primate models of nigro-striatal degeneration
    • Palfi, S., Leventhal, L., Chu, Y. et al. Lentivirally delivered glial cell line-derived neurotrophic factor increases the number of striatal dopaminergic neurons in primate models of nigro-striatal degeneration. J Neurosci 2002, 22: 4942-54.
    • (2002) J Neurosci , vol.22 , pp. 4942-4954
    • Palfi, S.1    Leventhal, L.2    Chu, Y.3
  • 158
    • 0037435511 scopus 로고    scopus 로고
    • Randomized, double-blind trial of glial cell line-derived neurotrophic factor (GDNF) in PD
    • Nutt, J.G., Burchiel, K.J., Cornelia, C.L. et al. Randomized, double-blind trial of glial cell line-derived neurotrophic factor (GDNF) in PD. Neurology 2003, 14: 69-73.
    • (2003) Neurology , vol.14 , pp. 69-73
    • Nutt, J.G.1    Burchiel, K.J.2    Cornelia, C.L.3
  • 159
    • 0038249170 scopus 로고    scopus 로고
    • Direct brain infusion of glial cell line-derived neurotrophic factor in Parkinson disease
    • Gill, S.S., Patel, N.K., Hotton, G.R. et al. Direct brain infusion of glial cell line-derived neurotrophic factor in Parkinson disease. Nature Med 2003, 9: 589-95.
    • (2003) Nature Med , vol.9 , pp. 589-595
    • Gill, S.S.1    Patel, N.K.2    Hotton, G.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.