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Volumn 11, Issue 9, 2005, Pages

Alteration in spectral properties on ligand binding reveals flexibility in monoamine oxidase

Author keywords

Antidepressant; Circular dichroism; Flavin; Inhibitor; Monoamine oxidase A; Oxazolidinone; Oxidative stress; Pirlindole

Indexed keywords

ALANINE; AMINE OXIDASE (FLAVIN CONTAINING); AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; CYSTEINE; QUERCETIN; SEMIQUINONE; THIOL DERIVATIVE;

EID: 24944574725     PISSN: 12341010     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (10)

References (26)
  • 1
    • 0025116342 scopus 로고
    • Mechanism of the Neurotoxicity of Mptp - An update
    • Singer TP, Ramsay RR: Mechanism of the Neurotoxicity of Mptp - an Update. FEBS Lett, 1990; 274: 1-8
    • (1990) FEBS Lett , vol.274 , pp. 1-8
    • Singer, T.P.1    Ramsay, R.R.2
  • 2
    • 0031898408 scopus 로고    scopus 로고
    • Structural aspects of monoamine oxidase and its reversible inhibition
    • Wouters J: Structural aspects of monoamine oxidase and its reversible inhibition. Curr Med Chem, 1998; 5: 137-62
    • (1998) Curr Med Chem , vol.5 , pp. 137-162
    • Wouters, J.1
  • 3
    • 0034814085 scopus 로고    scopus 로고
    • Interactions of nitrogen-containing xenobiotics with monoamine oxidase (MAO) isozymes A and B: SAR studies on MAO substrates and inhibitors
    • Kalgutkar AS, Dalvie DK, Castagnoli N, Taylor TJ: Interactions of nitrogen-containing xenobiotics with monoamine oxidase (MAO) isozymes A and B: SAR studies on MAO substrates and inhibitors. Chem Res Toxicol, 2001; 14: 1139-62
    • (2001) Chem Res Toxicol , vol.14 , pp. 1139-1162
    • Kalgutkar, A.S.1    Dalvie, D.K.2    Castagnoli, N.3    Taylor, T.J.4
  • 5
    • 0038624568 scopus 로고    scopus 로고
    • Monoamine oxidases: To inhibit or not to inhibit
    • Ramsay RR, Gravestock MB: Monoamine oxidases: to inhibit or not to inhibit. Mini-Rev Med Chem, 2003; 3: 129-36
    • (2003) Mini-Rev Med Chem , vol.3 , pp. 129-136
    • Ramsay, R.R.1    Gravestock, M.B.2
  • 6
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    • Binda C, Newton-Vinson P, Hubalek F et al: Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol, 2002; 9: 22-26
    • (2002) Nat Struct Biol , vol.9 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubalek, F.3
  • 8
    • 1842474296 scopus 로고    scopus 로고
    • Structure of rat monoamine oxidase a and its specific recognitions for substrates and inhibitors
    • Ma JC, Yoshimura M, Yamashita E et al: Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors. J Mol Biol, 2004; 338: 103-14
    • (2004) J Mol Biol , vol.338 , pp. 103-114
    • Ma, J.C.1    Yoshimura, M.2    Yamashita, E.3
  • 9
    • 0025871857 scopus 로고
    • Kinetic Mechanism of Monoamine Oxidase-A
    • Ramsay RR: Kinetic Mechanism of Monoamine Oxidase-A. Biochemistry, 1991; 30: 4624-29
    • (1991) Biochemistry , vol.30 , pp. 4624-4629
    • Ramsay, R.R.1
  • 10
    • 1642587783 scopus 로고    scopus 로고
    • Conformational changes in monoamine oxidase A in response to ligand binding or reduction
    • Hynson RMG, Kelly SM, Price NC, Ramsay RR: Conformational changes in monoamine oxidase A in response to ligand binding or reduction. Biochim Biophys Acta-Gen Subj, 2004; 1672: 60-66
    • (2004) Biochim Biophys Acta-Gen Subj , vol.1672 , pp. 60-66
    • Hynson, R.M.G.1    Kelly, S.M.2    Price, N.C.3    Ramsay, R.R.4
  • 11
    • 0037121460 scopus 로고    scopus 로고
    • Inhibitors alter the spectrum and redox properties of monoamine oxidase A
    • Ramsay RR, Hunter DJB: Inhibitors alter the spectrum and redox properties of monoamine oxidase A. BBA-Proteins Proteomics, 2002; 1601: 178-84
    • (2002) BBA-Proteins Proteomics , vol.1601 , pp. 178-184
    • Ramsay, R.R.1    Hunter, D.J.B.2
  • 12
    • 0037716398 scopus 로고    scopus 로고
    • Monoamine oxidase a inhibitory potency and flavin perturbation are influenced by different aspects of pirlindole inhibitor structure
    • Hynson RMG, Wouters J, Ramsay RR: Monoamine oxidase A inhibitory potency and flavin perturbation are influenced by different aspects of pirlindole inhibitor structure. Biochem Pharmacol, 2003; 65: 1867-74
    • (2003) Biochem Pharmacol , vol.65 , pp. 1867-1874
    • Hynson, R.M.G.1    Wouters, J.2    Ramsay, R.R.3
  • 13
    • 0028806711 scopus 로고
    • A reversible monoamine-oxidase inhibitor toloxatone - Comparison of its physicochemical properties with those of other inhibitors including brofarimine, harmine, R40519 and moclobemide
    • Moureau F, Wouters J, Depas M et al: A Reversible Monoamine-Oxidase Inhibitor Toloxatone - Comparison of Its Physicochemical Properties with Those of Other Inhibitors Including Brofarimine, Harmine, R40519 and Moclobemide. Eur J Med Chem, 1995; 30: 823-38
    • (1995) Eur J Med Chem , vol.30 , pp. 823-838
    • Moureau, F.1    Wouters, J.2    Depas, M.3
  • 14
    • 0032486262 scopus 로고    scopus 로고
    • Monoamine oxidase contains a redox-active disulfide
    • Sablin SO, Ramsay RR: Monoamine oxidase contains a redox-active disulfide. J Biol Chem, 1998; 273: 14074-76
    • (1998) J Biol Chem , vol.273 , pp. 14074-14076
    • Sablin, S.O.1    Ramsay, R.R.2
  • 17
    • 0034059925 scopus 로고    scopus 로고
    • Imidazoline-binding domains on monoamine oxidase B and subpopulations of enzyme
    • Raddatz R, Savic SL, Bakthavachalam V et al: Imidazoline-binding domains on monoamine oxidase B and subpopulations of enzyme. J Pharmacol Exp Ther, 2000; 292: 1135-45
    • (2000) J Pharmacol Exp Ther , vol.292 , pp. 1135-1145
    • Raddatz, R.1    Savic, S.L.2    Bakthavachalam, V.3
  • 18
    • 0033785927 scopus 로고    scopus 로고
    • Analysis of the pharmacological and molecular heterogeneity of I-2-imidazoline-binding proteins using monoamine oxidase- deficient mouse models
    • Remaury A, Raddatz R, Ordener C et al: Analysis of the pharmacological and molecular heterogeneity of I-2-imidazoline-binding proteins using monoamine oxidase- deficient mouse models. Mol Pharmacol, 2000; 58: 1085-90
    • (2000) Mol Pharmacol , vol.58 , pp. 1085-1090
    • Remaury, A.1    Raddatz, R.2    Ordener, C.3
  • 20
    • 0022400583 scopus 로고
    • Purification and properties of mitochondrial monoamine-oxidase type-A from human-placenta
    • Weyler W, Salach JI: Purification and Properties of Mitochondrial Monoamine-Oxidase Type-a from Human-Placenta. J Biol Chem, 1985; 260: 3199-207
    • (1985) J Biol Chem , vol.260 , pp. 3199-3207
    • Weyler, W.1    Salach, J.I.2
  • 21
    • 24944517469 scopus 로고    scopus 로고
    • Thiol reactivities as probes of MAO a and MAO B structure and function
    • (Eds. Chapman SK, Perham RN and Scrutton NS), Rudolf Weber, Berlin
    • Hubalek F, Edmondson DE: Thiol reactivities as probes of MAO A and MAO B structure and function. In: Flavins and Flavoproteins 2002 (Eds. Chapman SK, Perham RN and Scrutton NS), Rudolf Weber, Berlin, 2002; 217-22
    • (2002) Flavins and Flavoproteins 2002 , pp. 217-222
    • Hubalek, F.1    Edmondson, D.E.2
  • 22
    • 0027245885 scopus 로고
    • Site-directed mutagenesis of monoamine oxidase-A and oxidase-B - Role of cysteines
    • Wu HF, Chen K, Shih JC: Site-Directed Mutagenesis of Monoamine Oxidase-a and Oxidase-B - Role of Cysteines. Mol Pharmacol, 1993; 43: 888-93
    • (1993) Mol Pharmacol , vol.43 , pp. 888-893
    • Wu, H.F.1    Chen, K.2    Shih, J.C.3
  • 23
    • 24944473508 scopus 로고    scopus 로고
    • Nuclear magnetic resonance and mass spectroscopic evidence for the flavin-1-phenylcyclopropylamine inactivator adduct of monoamine oxidase
    • Mitchell DJ, Silverman RB, Singer TP et al: Nuclear magnetic resonance and mass spectroscopic evidence for the flavin-1-phenylcyclopropylamine inactivator adduct of monoamine oxidase. Biochemistry, 2000; 39: 52
    • (2000) Biochemistry , vol.39 , pp. 52
    • Mitchell, D.J.1    Silverman, R.B.2    Singer, T.P.3
  • 24
    • 24944456335 scopus 로고    scopus 로고
    • Subtle differences between MAO a and its cysteine 374 mutant during mechanism-based inactivation by cyclopropylamines
    • (Ed. SK Chapman RNPaNSS), Rudolph Weber, Berlin
    • Vintem A-PB, Ramsay RR, Silverman RB: Subtle differences between MAO A and its cysteine 374 mutant during mechanism-based inactivation by cyclopropylamines. In: Flavins and Flavoproteins 2002 (Ed. SK Chapman RNPaNSS), Rudolph Weber, Berlin, 2002; 911-15
    • (2002) Flavins and Flavoproteins 2002 , pp. 911-915
    • Vintem, A.-P.B.1    Ramsay, R.R.2    Silverman, R.B.3
  • 25
    • 2442674057 scopus 로고    scopus 로고
    • Benzylamine exhibits insulin-like effects on glucose disposal, glucose transport, and fat cell lipolysis in rabbits and diabetic mice
    • Iglesias-Osma MC, Garcia-Barrado MJ, Visentin V et al: Benzylamine exhibits insulin-like effects on glucose disposal, glucose transport, and fat cell lipolysis in rabbits and diabetic mice. J Pharmacol Exp Ther, 2004; 309: 1020-28
    • (2004) J Pharmacol Exp Ther , vol.309 , pp. 1020-1028
    • Iglesias-Osma, M.C.1    Garcia-Barrado, M.J.2    Visentin, V.3
  • 26
    • 2342573633 scopus 로고    scopus 로고
    • Dopamine toxicity involves mitochondrial complex I inhibition: Implications to dopamine-related neuropsychiatric disorders
    • Ben-Shachar D, Zuk R, Gazawi H, Ljubuncic P: Dopamine toxicity involves mitochondrial complex I inhibition: implications to dopamine-related neuropsychiatric disorders. Biochem Pharmacol, 2004; 67: 1965-74
    • (2004) Biochem Pharmacol , vol.67 , pp. 1965-1974
    • Ben-Shachar, D.1    Zuk, R.2    Gazawi, H.3    Ljubuncic, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.