메뉴 건너뛰기




Volumn 100, Issue , 2011, Pages 43-64

Kinetic behavior and reversible inhibition of monoamine oxidases-enzymes that many want dead

Author keywords

Amine oxidation; Competitive inhibition; Half life; Mixed inhibition; Noncompetitive inhibition; Steady state kinetics; Tyramine; Uncompetitive inhibition

Indexed keywords

3 PHOSPHOSHIKIMATE 1 CARBOXYVINYLTRANSFERASE; ADRENALIN; AMINE OXIDASE (FLAVIN CONTAINING); AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; ANTIDEPRESSANT AGENT; BROFAROMINE; CLORGYLINE; DOPAMINE; ENZYME INHIBITOR; HARMALINE; LAZABEMIDE; MOCLOBEMIDE; MONOAMINE OXIDASE INHIBITOR; NORADRENALIN; PHENETHYLAMINE; RO 411049; SEROTONIN; TRYPTAMINE; TYRAMINE; UNCLASSIFIED DRUG;

EID: 80053485090     PISSN: 00747742     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386467-3.00003-0     Document Type: Chapter
Times cited : (15)

References (71)
  • 3
    • 0023654981 scopus 로고
    • Graphical and statistical analysis of hyperbolic tight-binding inhibition
    • Baici A. Graphical and statistical analysis of hyperbolic tight-binding inhibition. Biochem. J. 1987, 244:793-796.
    • (1987) Biochem. J. , vol.244 , pp. 793-796
    • Baici, A.1
  • 4
    • 43949123265 scopus 로고    scopus 로고
    • Structural and mechanistic studies of arylalkylhydrazine inhibition of human monoamine oxidases A and B
    • Binda C., Wang J., Li M., Hubalek F., Mattevi A., Edmondson D.E. Structural and mechanistic studies of arylalkylhydrazine inhibition of human monoamine oxidases A and B. Biochemistry 2008, 47:5616-5625.
    • (2008) Biochemistry , vol.47 , pp. 5616-5625
    • Binda, C.1    Wang, J.2    Li, M.3    Hubalek, F.4    Mattevi, A.5    Edmondson, D.E.6
  • 5
    • 0001137465 scopus 로고
    • Hypertensive crisis due to monoamine oxidase inhibitors
    • Blackwell B. Hypertensive crisis due to monoamine oxidase inhibitors. Lancet 1963, ii:849-851.
    • (1963) Lancet , vol.2 , pp. 849-851
    • Blackwell, B.1
  • 7
    • 0021095357 scopus 로고
    • Kinetics of inhibition of 5-enolpyruvylshikimate- 3-phosphate synthase by glyphosate
    • Boocock M.R., Coggins J.R. Kinetics of inhibition of 5-enolpyruvylshikimate- 3-phosphate synthase by glyphosate. FEBS Lett. 1983, 154:127-133.
    • (1983) FEBS Lett. , vol.154 , pp. 127-133
    • Boocock, M.R.1    Coggins, J.R.2
  • 8
    • 4243417574 scopus 로고
    • Some properties of amine oxidase activities in the rat intestine
    • Callingham B.A., Mazel P., Porter J.C. Some properties of amine oxidase activities in the rat intestine. Br. J. Pharmacol. 1985, 86:553.
    • (1985) Br. J. Pharmacol. , vol.86 , pp. 553
    • Callingham, B.A.1    Mazel, P.2    Porter, J.C.3
  • 9
    • 0023797315 scopus 로고
    • On tyramine, food beverages and the reversible MAO inhibitor moclobemide
    • Da Prada M., Zürcher G., Würthrich I., Haefely W.E. On tyramine, food beverages and the reversible MAO inhibitor moclobemide. J. Neural Transm. 1988, 26(Suppl.):33-56.
    • (1988) J. Neural Transm. , vol.26 , Issue.SUPPL. , pp. 33-56
    • Da Prada, M.1    Zürcher, G.2    Würthrich, I.3    Haefely, W.E.4
  • 10
    • 0347623862 scopus 로고
    • The effects of reversible and irreversible inhibitors of monoamine oxidase on tyramine deamination in dog intestine
    • Academic Press, London, K.F. Tipton, P. Dostert, M. Strolin Benedetti (Eds.)
    • Davis D.S., Tasuhara H., Boobis A.R., George C.F. The effects of reversible and irreversible inhibitors of monoamine oxidase on tyramine deamination in dog intestine. Monoamine Oxidase and Disease 1984, 443-448. Academic Press, London. K.F. Tipton, P. Dostert, M. Strolin Benedetti (Eds.).
    • (1984) Monoamine Oxidase and Disease , pp. 443-448
    • Davis, D.S.1    Tasuhara, H.2    Boobis, A.R.3    George, C.F.4
  • 11
    • 24644437716 scopus 로고    scopus 로고
    • Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B
    • De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., Mattevi A. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc. Natl. Acad. Sci. USA 2005, 102:12684-12689.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12684-12689
    • De Colibus, L.1    Li, M.2    Binda, C.3    Lustig, A.4    Edmondson, D.E.5    Mattevi, A.6
  • 12
    • 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, 29:811-815.
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 811-815
    • Della Corte, L.1    Tipton, K.F.2
  • 14
    • 0027300857 scopus 로고
    • Spectral and kinetic studies of imine product formation in the oxidation of p-(N,N-dimethylamino)- benzylamine analogues by monoamine oxidase B
    • Edmondson D.E., Bhattacharyya A.K., Walker M.C. Spectral and kinetic studies of imine product formation in the oxidation of p-(N,N-dimethylamino)- benzylamine analogues by monoamine oxidase B. Biochemistry 1993, 32:5196-5202.
    • (1993) Biochemistry , vol.32 , pp. 5196-5202
    • Edmondson, D.E.1    Bhattacharyya, A.K.2    Walker, M.C.3
  • 15
    • 0015021786 scopus 로고
    • 14 C]-pargyline: a tool for studying the synthesis of the enzyme
    • 14 C]-pargyline: a tool for studying the synthesis of the enzyme. Mol. Pharmacol. 1971, 7:219-228.
    • (1971) Mol. Pharmacol. , vol.7 , pp. 219-228
    • Erwin, V.G.1    Deitrich, R.A.2
  • 16
    • 0018764161 scopus 로고
    • Cumulative effects of irreversible MAO inhibitors in vivo
    • Felner A.E., Waldmeier P.C. Cumulative effects of irreversible MAO inhibitors in vivo. Biochem. Pharmacol. 1979, 28:995-1002.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 995-1002
    • Felner, A.E.1    Waldmeier, P.C.2
  • 17
    • 34249940141 scopus 로고    scopus 로고
    • Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: insights from molecular modeling studies
    • Fierro A., Osorio-Olivares M., Cassels B.K., Edmondson D.E., Sepúlveda-Boza S., Reyes-Parada M. Human and rat monoamine oxidase-A are differentially inhibited by (S)-4-alkylthioamphetamine derivatives: insights from molecular modeling studies. Bioorg. Med. Chem. 2007, 15:5198-5206.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 5198-5206
    • Fierro, A.1    Osorio-Olivares, M.2    Cassels, B.K.3    Edmondson, D.E.4    Sepúlveda-Boza, S.5    Reyes-Parada, M.6
  • 18
    • 0014407642 scopus 로고
    • Thyroidal biosynthesis of iodothyronines. II. General characteristics and purification of mitochondrial monoamine oxidase.
    • Fischer A.G., Schulz A.R., Oliner L. Thyroidal biosynthesis of iodothyronines. II. General characteristics and purification of mitochondrial monoamine oxidase. Biochim. Biophys. Acta 1968, 159:460-471.
    • (1968) Biochim. Biophys. Acta , vol.159 , pp. 460-471
    • Fischer, A.G.1    Schulz, A.R.2    Oliner, L.3
  • 20
    • 0000166289 scopus 로고
    • Treatment of Enzyme Kinetic Data. I. The effect of modifiers on the kinetic parameters of single substrate enzymes
    • Frieden C. Treatment of Enzyme Kinetic Data. I. The effect of modifiers on the kinetic parameters of single substrate enzymes. J. Biol. Chem. 1964, 239:3522-3531.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3522-3531
    • Frieden, C.1
  • 21
    • 0014944207 scopus 로고
    • Binding interactions between two ligands and a monomeric protein. Study on indole, protons and chymotrypsin
    • Garel J.R., Labouesse B. Binding interactions between two ligands and a monomeric protein. Study on indole, protons and chymotrypsin. J. Mol. Biol. 1970, 47:41-56.
    • (1970) J. Mol. Biol. , vol.47 , pp. 41-56
    • Garel, J.R.1    Labouesse, B.2
  • 22
    • 0019208983 scopus 로고
    • Species differences in the deamination of dopamine and other substrates for monoamine oxidase in brain
    • Garrick N.A., Murphy D.L. Species differences in the deamination of dopamine and other substrates for monoamine oxidase in brain. Psychopharmacology 1982, 72:27-33.
    • (1982) Psychopharmacology , vol.72 , pp. 27-33
    • Garrick, N.A.1    Murphy, D.L.2
  • 23
    • 0017755902 scopus 로고
    • Evidence for dopamine deamination by by both type A and type B monoamine oxidase in rat brain in vivo and for the degree of inhibition necessary for increased functional activity of dopamine and 5-hydroxytryptamine
    • Green A.R., Mitchell D., Todoff A., Youdim M.B.H. Evidence for dopamine deamination by by both type A and type B monoamine oxidase in rat brain in vivo and for the degree of inhibition necessary for increased functional activity of dopamine and 5-hydroxytryptamine. Br. J. Pharmacol. 1977, 60:343-3429.
    • (1977) Br. J. Pharmacol. , vol.60 , pp. 343-3429
    • Green, A.R.1    Mitchell, D.2    Todoff, A.3    Youdim, M.B.H.4
  • 24
    • 0023674662 scopus 로고
    • The involvement of intestinal monoamine oxidase in the transport and metabolism of tyramine
    • Hasan F., McCrodden J.M., Kennedy N.P., Tipton K.F. The involvement of intestinal monoamine oxidase in the transport and metabolism of tyramine. J. Neural Transm. 1988, 26(Suppl.):1-9.
    • (1988) J. Neural Transm. , vol.26 , Issue.SUPPL. , pp. 1-9
    • Hasan, F.1    McCrodden, J.M.2    Kennedy, N.P.3    Tipton, K.F.4
  • 26
    • 0015857036 scopus 로고
    • Steady-state enzyme kinetics with high-affinity substrates or inhibitors. A statistical treatment of dose-response curves.
    • Henderson P.J.F. Steady-state enzyme kinetics with high-affinity substrates or inhibitors. A statistical treatment of dose-response curves. Biochem. J. 1973, 135:101-107.
    • (1973) Biochem. J. , vol.135 , pp. 101-107
    • Henderson, P.J.F.1
  • 27
    • 0015711870 scopus 로고
    • The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase
    • Houslay M.D., Tipton K.F. The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase. Biochem. J. 1973, 135:735-750.
    • (1973) Biochem. J. , vol.135 , pp. 735-750
    • Houslay, M.D.1    Tipton, K.F.2
  • 28
    • 0016194258 scopus 로고
    • A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes
    • Houslay M.D., Tipton K.F. A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes. Biochem. J. 1974, 139:645-652.
    • (1974) Biochem. J. , vol.139 , pp. 645-652
    • Houslay, M.D.1    Tipton, K.F.2
  • 29
    • 0016476266 scopus 로고
    • Amine competition for oxidation by rat liver mitochondrial monoamine oxidase
    • Houslay M.D., Tipton K.F. Amine competition for oxidation by rat liver mitochondrial monoamine oxidase. Biochem. Pharmacol. 1975, 24:627-631.
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 627-631
    • Houslay, M.D.1    Tipton, K.F.2
  • 30
    • 0016613746 scopus 로고
    • Rat liver mitochondrial monoamine oxidase. A change in the reaction mechanism on solubilization.
    • Houslay M.D., Tipton K.F. Rat liver mitochondrial monoamine oxidase. A change in the reaction mechanism on solubilization. Biochem. J. 1975, 145:311-321.
    • (1975) Biochem. J. , vol.145 , pp. 311-321
    • Houslay, M.D.1    Tipton, K.F.2
  • 31
    • 0016229851 scopus 로고
    • Mixed substrate experiments with human brain monoamine oxidase
    • Houslay M.D., Garrett N.J., Tipton K.F. Mixed substrate experiments with human brain monoamine oxidase. Biochem. Pharmacol. 1974, 23:1937-1944.
    • (1974) Biochem. Pharmacol. , vol.23 , pp. 1937-1944
    • Houslay, M.D.1    Garrett, N.J.2    Tipton, K.F.3
  • 32
    • 0020473204 scopus 로고
    • Kinetic studies on the catalytic mechanism of liver monoamine oxidase
    • Husain M., Edmondson D.E., Singer T.P. Kinetic studies on the catalytic mechanism of liver monoamine oxidase. Biochemistry 1982, 21:595-600.
    • (1982) Biochemistry , vol.21 , pp. 595-600
    • Husain, M.1    Edmondson, D.E.2    Singer, T.P.3
  • 33
    • 0032696105 scopus 로고    scopus 로고
    • Species-dependent differences in monoamine oxidase A and B-catalyzed oxidation of various C4 substituted 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridinyl derivatives
    • Inoue H., Castagnoli K., Van Der Schyf C., Mabic S., Igarashi K., Castagnoli N. Species-dependent differences in monoamine oxidase A and B-catalyzed oxidation of various C4 substituted 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridinyl derivatives. J. Pharmacol. Exp. Ther. 1999, 291:856-864.
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , pp. 856-864
    • Inoue, H.1    Castagnoli, K.2    Van Der Schyf, C.3    Mabic, S.4    Igarashi, K.5    Castagnoli, N.6
  • 34
    • 0028928880 scopus 로고
    • Dramatic species differences in the susceptibility of monoamine oxidase B to a group of powerful inhibitors
    • Krueger M.J., Mazouz F., Ramsay R.R., Milcent R., Singer T.P. Dramatic species differences in the susceptibility of monoamine oxidase B to a group of powerful inhibitors. Biochem. Biophys. Res. Commun. 1995, 206:556-562.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 556-562
    • Krueger, M.J.1    Mazouz, F.2    Ramsay, R.R.3    Milcent, R.4    Singer, T.P.5
  • 35
    • 0142136016 scopus 로고    scopus 로고
    • Kinetics of catalyzed reactions-biological
    • John Wiley & Sons, New York, I.T. Horváth (Ed.)
    • McDonald A.G., Tipton K.F. Kinetics of catalyzed reactions-biological. Encyclopedia of Catalysis 2002, John Wiley & Sons, New York. http://www.mrw.interscience.wiley.com/enccat/, 10.1002/0471227617.eoc127. I.T. Horváth (Ed.).
    • (2002) Encyclopedia of Catalysis
    • McDonald, A.G.1    Tipton, K.F.2
  • 37
    • 0033550070 scopus 로고    scopus 로고
    • Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A
    • Miller J.R., Edmondson D.E. Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A. Biochemistry 1999, 38:13670-13683.
    • (1999) Biochemistry , vol.38 , pp. 13670-13683
    • Miller, J.R.1    Edmondson, D.E.2
  • 38
    • 0027725109 scopus 로고
    • Biochemistry and pharmacology of reversible inhibitors of MAO-A agents: focus on moclobemide
    • Nair N.P., Ahmed S.K., Kin N.M. Biochemistry and pharmacology of reversible inhibitors of MAO-A agents: focus on moclobemide. J. Psychiatry Neurosci. 1993, 18:214-225.
    • (1993) J. Psychiatry Neurosci. , vol.18 , pp. 214-225
    • Nair, N.P.1    Ahmed, S.K.2    Kin, N.M.3
  • 39
    • 0015270743 scopus 로고
    • Neuronal monoamine oxidase: specific enzyme types and their rates of formation
    • Neff N.H., Goridis C. Neuronal monoamine oxidase: specific enzyme types and their rates of formation. Adv. Biochem. Psychopharmacol. 1972, 5:307-323.
    • (1972) Adv. Biochem. Psychopharmacol. , vol.5 , pp. 307-323
    • Neff, N.H.1    Goridis, C.2
  • 40
    • 0018657038 scopus 로고
    • 3 H]Harmaline as a specific ligand of MAO A-II. Measurement of the turnover rates of MAO A during ontogenesis in the rat brain
    • 3 H]Harmaline as a specific ligand of MAO A-II. Measurement of the turnover rates of MAO A during ontogenesis in the rat brain. J. Neurochem. 1979, 32:1829-1936.
    • (1979) J. Neurochem. , vol.32 , pp. 1829-1936
    • Nelson, D.L.1    Herbet, A.2    Glowinski, J.3    Hamon, M.J.4
  • 41
    • 0029123373 scopus 로고
    • Species differences in the interactions of the anticonvulsant milacemide and some analogues with monoamine oxidase-B
    • O'Brien E.M., Dostert P., Tipton K.F. Species differences in the interactions of the anticonvulsant milacemide and some analogues with monoamine oxidase-B. Biochem. Pharmacol. 1995, 50:317-324.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 317-324
    • O'Brien, E.M.1    Dostert, P.2    Tipton, K.F.3
  • 42
    • 0015103108 scopus 로고
    • The effect of pH on the kinetic parameters and mechanism of beef liver monoamine oxidase
    • Oi S., Yasunobu K.T., Westley J. The effect of pH on the kinetic parameters and mechanism of beef liver monoamine oxidase. Arch. Biochem. Biophys. 1971, 145:557-564.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 557-564
    • Oi, S.1    Yasunobu, K.T.2    Westley, J.3
  • 43
    • 0019254011 scopus 로고
    • Some factors influencing the metabolism of benzylamine by type A and B monoamine oxidase in rat heart and liver
    • Parkinson D., Lyles G.A., Browne B.J., Callingham B.A. Some factors influencing the metabolism of benzylamine by type A and B monoamine oxidase in rat heart and liver. J. Pharm. Pharmacol. 1980, 32:844-850.
    • (1980) J. Pharm. Pharmacol. , vol.32 , pp. 844-850
    • Parkinson, D.1    Lyles, G.A.2    Browne, B.J.3    Callingham, B.A.4
  • 44
    • 0022262460 scopus 로고
    • Human brain monoamine oxidase type B: mechanism of deamination as probed by steady-state methods
    • Pearce L.B., Roth J.A. Human brain monoamine oxidase type B: mechanism of deamination as probed by steady-state methods. Biochemistry 1985, 24:1821-1826.
    • (1985) Biochemistry , vol.24 , pp. 1821-1826
    • Pearce, L.B.1    Roth, J.A.2
  • 45
    • 0015504866 scopus 로고
    • Dalziel rate behaviour in ternary-complex mechanisms for enzyme reactions involving two substrates
    • Pettersson G. Dalziel rate behaviour in ternary-complex mechanisms for enzyme reactions involving two substrates. Biochim. Biophys. Acta 1972, 276:1-11.
    • (1972) Biochim. Biophys. Acta , vol.276 , pp. 1-11
    • Pettersson, G.1
  • 47
    • 0025871857 scopus 로고
    • Kinetic mechanism of monoamine oxidase A
    • Ramsay R.R. Kinetic mechanism of monoamine oxidase A. Biochemistry 1991, 30:4624-4629.
    • (1991) Biochemistry , vol.30 , pp. 4624-4629
    • Ramsay, R.R.1
  • 48
    • 0024267587 scopus 로고
    • Interactions of tricyclic antidepressant drugs with human and rat monoamine oxidase type B
    • Reid A.A., Hill J.L., Murphy D.L. Interactions of tricyclic antidepressant drugs with human and rat monoamine oxidase type B. Naunyn-Schmied. Arch. Pharmacol. 1988, 388:678-683.
    • (1988) Naunyn-Schmied. Arch. Pharmacol. , vol.388 , pp. 678-683
    • Reid, A.A.1    Hill, J.L.2    Murphy, D.L.3
  • 49
    • 0345490838 scopus 로고    scopus 로고
    • Selegiline's neuroprotective capacity revisited
    • Riederer P., Lachenmayer L. Selegiline's neuroprotective capacity revisited. J. Neural Transm. 2003, 110:1273-1278.
    • (2003) J. Neural Transm. , vol.110 , pp. 1273-1278
    • Riederer, P.1    Lachenmayer, L.2
  • 50
    • 0026550390 scopus 로고
    • 3 H-Ro 19-6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain
    • 3 H-Ro 19-6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain. J. Neurosci. 1992, 12:1977-1999.
    • (1992) J. Neurosci. , vol.12 , pp. 1977-1999
    • Saura, J.1    Kettler, R.2    Da Prada, M.3    Richards, J.G.4
  • 51
  • 52
    • 0015177156 scopus 로고
    • A method for deriving kinetic constants for two enzymes acting on the same substrate
    • Spears G., Sneyd J.G., Loten E.G. A method for deriving kinetic constants for two enzymes acting on the same substrate. Biochem. J. 1971, 125:1149-1151.
    • (1971) Biochem. J. , vol.125 , pp. 1149-1151
    • Spears, G.1    Sneyd, J.G.2    Loten, E.G.3
  • 54
    • 0026633580 scopus 로고
    • Interactions of the neurotoxin MPTP and its demethylated derivative (PTP) with monoamine oxidase-B
    • Sullivan J.P., Tipton K.F. Interactions of the neurotoxin MPTP and its demethylated derivative (PTP) with monoamine oxidase-B. Neurochem. Res. 1992, 8:791-796.
    • (1992) Neurochem. Res. , vol.8 , pp. 791-796
    • Sullivan, J.P.1    Tipton, K.F.2
  • 55
    • 0028924136 scopus 로고
    • Kinetics of slow and tight-binding inhibitors
    • Szedlacsek S.E., Duggleby R.G. Kinetics of slow and tight-binding inhibitors. Methods Enzymol. 1995, 249:144-181.
    • (1995) Methods Enzymol. , vol.249 , pp. 144-181
    • Szedlacsek, S.E.1    Duggleby, R.G.2
  • 56
    • 0027534454 scopus 로고
    • Substrate-specific enhancement of the oxidative half-reaction of monoamine oxidase
    • Tan A.K., Ramsay R.R. Substrate-specific enhancement of the oxidative half-reaction of monoamine oxidase. Biochemistry 1993, 32:2137-2143.
    • (1993) Biochemistry , vol.32 , pp. 2137-2143
    • Tan, A.K.1    Ramsay, R.R.2
  • 57
    • 0003128364 scopus 로고
    • Mechanism-based inhibitors
    • Oxford University Press, Oxford, M. Sandler, H.J. Smith (Eds.)
    • Tipton K.F. Mechanism-based inhibitors. Design of Enzyme Inhibitors as Drugs 1989, 70-93. Oxford University Press, Oxford. M. Sandler, H.J. Smith (Eds.).
    • (1989) Design of Enzyme Inhibitors as Drugs , pp. 70-93
    • Tipton, K.F.1
  • 58
    • 0008176413 scopus 로고
    • Monoamine oxidase inhibitors as antidepressants
    • Taylor & Francis, London, K.F. Tipton, M.B.H. Youdim (Eds.)
    • Tipton K.F. Monoamine oxidase inhibitors as antidepressants. Biochemical and Pharmacological Aspects of Depression 1989, 1-24. Taylor & Francis, London. K.F. Tipton, M.B.H. Youdim (Eds.).
    • (1989) Biochemical and Pharmacological Aspects of Depression , pp. 1-24
    • Tipton, K.F.1
  • 59
    • 0001848949 scopus 로고    scopus 로고
    • Patterns of enzyme inhibition
    • Bios Scientific Publishers and Academic Press, Oxford, UK and San Diego, USA, P.C. Engel (Ed.)
    • Tipton K.F. Patterns of enzyme inhibition. EnzymologyLabFax 1996, 115-174. Bios Scientific Publishers and Academic Press, Oxford, UK and San Diego, USA. P.C. Engel (Ed.).
    • (1996) EnzymologyLabFax , pp. 115-174
    • Tipton, K.F.1
  • 60
    • 0031266402 scopus 로고    scopus 로고
    • Inhibitors of monoamine oxidase and the pressor response to dietary amines
    • Tipton K.F. Inhibitors of monoamine oxidase and the pressor response to dietary amines. Vopr. Med. Khim. 1997, 46:494-503.
    • (1997) Vopr. Med. Khim. , vol.46 , pp. 494-503
    • Tipton, K.F.1
  • 61
    • 84876760201 scopus 로고    scopus 로고
    • Enzymes: Irreversible Inhibition
    • John Wiley & Sons, Ltd, Chichester, [doi:10.1038/npg.els.0000601], A. Finazzi Agrò (Ed.)
    • Tipton K.F. Enzymes: Irreversible Inhibition. Encyclopedia of Life Sciences 2001, John Wiley & Sons, Ltd, Chichester, [doi:10.1038/npg.els.0000601]. http://www.els.net/WileyCDA/, 10.1038/npg.els.0000601. A. Finazzi Agrò (Ed.).
    • (2001) Encyclopedia of Life Sciences
    • Tipton, K.F.1
  • 62
    • 0343117269 scopus 로고
    • The kinetics of monoamine oxidase inhibitors in relation to their clinical behaviour
    • Academic Press, London, K.F. Tipton, P. Dostert, M. Strolin Benedetti (Eds.)
    • Tipton K.F., Fowler C.J. The kinetics of monoamine oxidase inhibitors in relation to their clinical behaviour. Monoamine Oxidase and Disease 1984, 27-40. Academic Press, London. K.F. Tipton, P. Dostert, M. Strolin Benedetti (Eds.).
    • (1984) Monoamine Oxidase and Disease , pp. 27-40
    • Tipton, K.F.1    Fowler, C.J.2
  • 63
    • 0027504297 scopus 로고
    • Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds
    • Tipton K.F., Singer T.P. Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds. J. Neurochem. 1993, 61:1191-1206.
    • (1993) J. Neurochem. , vol.61 , pp. 1191-1206
    • Tipton, K.F.1    Singer, T.P.2
  • 64
    • 0013600812 scopus 로고
    • Newer approaches to the study of monoamine oxidase inhibition
    • VSP BV, Utrecht, The Netherlands, H. Yashuhara, S.H. Parvez, K. Oguchi, M. Sandler, T. Nagatsu (Eds.)
    • Tipton K.F., Balsa D., Unzeta M. Newer approaches to the study of monoamine oxidase inhibition. Monoamine Oxidase: Basic and Clinical Aspects 1993, 1-13. VSP BV, Utrecht, The Netherlands. H. Yashuhara, S.H. Parvez, K. Oguchi, M. Sandler, T. Nagatsu (Eds.).
    • (1993) Monoamine Oxidase: Basic and Clinical Aspects , pp. 1-13
    • Tipton, K.F.1    Balsa, D.2    Unzeta, M.3
  • 65
    • 0021080932 scopus 로고
    • The monoamine oxidase inhibiting properties of CGP 11305A
    • Waldmeier P.C., Felner A.E., Tipton K.F. The monoamine oxidase inhibiting properties of CGP 11305A. Eur. J. Pharmacol. 1983, 94:73-83.
    • (1983) Eur. J. Pharmacol. , vol.94 , pp. 73-83
    • Waldmeier, P.C.1    Felner, A.E.2    Tipton, K.F.3
  • 66
    • 0029981211 scopus 로고    scopus 로고
    • Enzyme inhibition in open systems. Superiority of uncompetitive agents
    • Westley A.M., Westley J. Enzyme inhibition in open systems. Superiority of uncompetitive agents. J. Biol. Chem. 1996, 271:5347-5352.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5347-5352
    • Westley, A.M.1    Westley, J.2
  • 67
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams J.W., Morrison J.F. The kinetics of reversible tight-binding inhibition. Methods Enzymol. 1979, 63:437-467.
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 68
    • 0346154805 scopus 로고    scopus 로고
    • Clinical pharmacology of MAO inhibitors: safety and future
    • Yamada M., Yasuhara H. Clinical pharmacology of MAO inhibitors: safety and future. Neurotoxicology 2004, 25:215-221.
    • (2004) Neurotoxicology , vol.25 , pp. 215-221
    • Yamada, M.1    Yasuhara, H.2
  • 69
    • 0036162584 scopus 로고    scopus 로고
    • Rat striatal monoamine oxidase-B inhibition by l-deprenyl and rasagiline: its relationship to 2-phenylethylamine-induced stereotypy and Parkinson's disease
    • Youdim M.B.H., Tipton K.F. Rat striatal monoamine oxidase-B inhibition by l-deprenyl and rasagiline: its relationship to 2-phenylethylamine-induced stereotypy and Parkinson's disease. Parkinsonism Relat. Disord. 2002, 8:247-253.
    • (2002) Parkinsonism Relat. Disord. , vol.8 , pp. 247-253
    • Youdim, M.B.H.1    Tipton, K.F.2
  • 70
  • 71
    • 0024357953 scopus 로고
    • Deuterium isotope effect of phenelzine on the inhibition of rat liver mitochondrial monoamine oxidase activity
    • Yu P.H., Tipton K.F. Deuterium isotope effect of phenelzine on the inhibition of rat liver mitochondrial monoamine oxidase activity. Biochem. Pharmacol. 1989, 38:4245-4251.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 4245-4251
    • Yu, P.H.1    Tipton, K.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.