메뉴 건너뛰기




Volumn 125, Issue , 2017, Pages 853-864

Synthesis and evaluation of 7-substituted coumarin derivatives as multimodal monoamine oxidase-B and cholinesterase inhibitors for the treatment of Alzheimer's disease

Author keywords

Alzheimer's disease; Cholinesterase; Coumarin; Donepezil; MAO B; Molecular modeling

Indexed keywords

4 METHYL 2 OXO 7 [2 (BENZYLPIPERIDIN 1 YL)ETHOXY] 2H CHROMENE 3 CARBONITRILE; 7 (BENZYLOXY) 3 CHLORO 4 METHYL 2H CHROMEN 2 ONE; CHOLINESTERASE INHIBITOR; COUMARIN DERIVATIVE; DONEPEZIL; MONOAMINE OXIDASE INHIBITOR; UNCLASSIFIED DRUG; AMINE OXIDASE (FLAVIN CONTAINING); AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; BENZYL DERIVATIVE; PEPTIDE FRAGMENT; PIPERIDINE DERIVATIVE; PROTEIN BINDING;

EID: 84992028376     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2016.09.041     Document Type: Article
Times cited : (104)

References (63)
  • 1
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • [1] Goedert, M., Spillantini, M., A century of Alzheimer's disease. Science 314 (2006), 777–781.
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.2
  • 2
    • 85056603638 scopus 로고    scopus 로고
    • The dementias: diagnosis, treatment and Research
    • third ed.
    • [2] Cummings, J., The dementias: diagnosis, treatment and Research. third ed. Arch. Neurol., 61, 2004, 1623.
    • (2004) Arch. Neurol. , vol.61 , pp. 1623
    • Cummings, J.1
  • 3
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • [3] Grundke-Iqbal, I., Iqbal, K., Tung, Y., Quinlan, M., Wisniewski, H., Binder, L., Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. 83 (1986), 4913–4917.
    • (1986) Proc. Natl. Acad. Sci. , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.3    Quinlan, M.4    Wisniewski, H.5    Binder, L.6
  • 4
    • 33750883640 scopus 로고    scopus 로고
    • Targeting beta-amyloid pathogenesis through acetylcholinesterase inhibitors
    • [4] Castro, A., Martinez, A., Targeting beta-amyloid pathogenesis through acetylcholinesterase inhibitors. CPD 12 (2006), 4377–4387.
    • (2006) CPD , vol.12 , pp. 4377-4387
    • Castro, A.1    Martinez, A.2
  • 5
    • 67049134478 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer disease
    • [5] Gella, A., Durany, N., Oxidative stress in Alzheimer disease. Cell Adhesion Migr. 3 (2009), 88–93.
    • (2009) Cell Adhesion Migr. , vol.3 , pp. 88-93
    • Gella, A.1    Durany, N.2
  • 6
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • [6] Coyle, J., Puttfarcken, P., Oxidative stress, glutamate, and neurodegenerative disorders. Science 262 (1993), 689–695.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.1    Puttfarcken, P.2
  • 7
    • 0034806090 scopus 로고    scopus 로고
    • Acetylcholinesterase in Alzheimer's disease
    • [7] Talesa, V., Acetylcholinesterase in Alzheimer's disease. Mech. Ageing Dev. 122 (2001), 1961–1969.
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 1961-1969
    • Talesa, V.1
  • 8
    • 37649026816 scopus 로고    scopus 로고
    • Donepezil for dementia due to Alzheimer's disease
    • No. 1
    • [8] Birks, J., Harvey, R., Donepezil for dementia due to Alzheimer's disease. No. 1 Cochrane Database Syst. Rev., 2006, CD001190.
    • (2006) Cochrane Database Syst. Rev. , pp. CD001190
    • Birks, J.1    Harvey, R.2
  • 9
  • 11
    • 28044437122 scopus 로고    scopus 로고
    • Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer B-amyloid peptide in rodent
    • [11] Greig, N., Utsuki, T., Ingram, D., Wang, Y., Pepeu, G., Scali, C., et al. Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer B-amyloid peptide in rodent. Proc. Natl. Acad. Sci. 102 (2005), 17213–17218.
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 17213-17218
    • Greig, N.1    Utsuki, T.2    Ingram, D.3    Wang, Y.4    Pepeu, G.5    Scali, C.6
  • 12
    • 0141818332 scopus 로고    scopus 로고
    • Cholinergic function and Alzheimer's disease
    • [12] Giacobini, E., Cholinergic function and Alzheimer's disease. Int. J. Geriat Psychiatry 18 (2003), S1–S5.
    • (2003) Int. J. Geriat Psychiatry , vol.18 , pp. S1-S5
    • Giacobini, E.1
  • 13
    • 13544268496 scopus 로고    scopus 로고
    • Cholinergic–serotonergic imbalance contributes to cognitive and behavioral symptoms in Alzheimer's disease
    • [13] Garcia-Alloza, M., Gil-Bea, F., Diez-Ariza, M., Chen, C., Francis, P., Lasheras, B., et al. Cholinergic–serotonergic imbalance contributes to cognitive and behavioral symptoms in Alzheimer's disease. Neuropsychologia 43 (2005), 442–449.
    • (2005) Neuropsychologia , vol.43 , pp. 442-449
    • Garcia-Alloza, M.1    Gil-Bea, F.2    Diez-Ariza, M.3    Chen, C.4    Francis, P.5    Lasheras, B.6
  • 14
    • 53149107135 scopus 로고    scopus 로고
    • Cognitive dysfunction in neuropsychiatric disorders: selected serotonin receptor subtypes as therapeutic targets
    • [14] Terry, A., Buccafusco, J., Wilson, C., Cognitive dysfunction in neuropsychiatric disorders: selected serotonin receptor subtypes as therapeutic targets. Behav. Brain Res. 195 (2008), 30–38.
    • (2008) Behav. Brain Res. , vol.195 , pp. 30-38
    • Terry, A.1    Buccafusco, J.2    Wilson, C.3
  • 15
    • 0033805791 scopus 로고    scopus 로고
    • Alzheimer's disease: more than a ‘cholinergic disorder’ — evidence that cholinergic–monoaminergic interactions contribute to EEG slowing and dementia
    • [15] Dringenberg, H., Alzheimer's disease: more than a ‘cholinergic disorder’ — evidence that cholinergic–monoaminergic interactions contribute to EEG slowing and dementia. Behav. Brain Res. 115 (2000), 235–249.
    • (2000) Behav. Brain Res. , vol.115 , pp. 235-249
    • Dringenberg, H.1
  • 16
    • 0022496317 scopus 로고
    • Monoamine oxidase activity and monoamine metabolism in brains of Parkinsonian patients treated with l-deprenyl
    • [16] Riederer, P., Youdim, M., Monoamine oxidase activity and monoamine metabolism in brains of Parkinsonian patients treated with l-deprenyl. J. Neurochem. 46 (1986), 1359–1365.
    • (1986) J. Neurochem. , vol.46 , pp. 1359-1365
    • Riederer, P.1    Youdim, M.2
  • 17
    • 0035871771 scopus 로고    scopus 로고
    • Selective dopaminergic vulnerability: 3,4-dihydroxyphenylacetaldehyde targets mitochondria
    • [17] Kristal, S., Conway, D., Brown, M., Jain, C., Ulluci, A., Li, W., Burke, W., Selective dopaminergic vulnerability: 3,4-dihydroxyphenylacetaldehyde targets mitochondria. Free Radic. Biol. Med. 30 (2001), 924–931.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 924-931
    • Kristal, S.1    Conway, D.2    Brown, M.3    Jain, C.4    Ulluci, A.5    Li, W.6    Burke, W.7
  • 18
    • 0026505507 scopus 로고
    • Mitochondrial targeting signal of rat liver monoamine oxidase B is located at its carboxy terminus
    • [18] Mitoma, J., Ito, A., Mitochondrial targeting signal of rat liver monoamine oxidase B is located at its carboxy terminus. J. Biochem. 111 (1992), 20–24.
    • (1992) J. Biochem. , vol.111 , pp. 20-24
    • Mitoma, J.1    Ito, A.2
  • 19
    • 0014818521 scopus 로고
    • An appraisal of the use of monoamine oxidase as an enzyme marker for the outer membrane of rat liver mitochondria
    • [19] Greenawalt, J., An appraisal of the use of monoamine oxidase as an enzyme marker for the outer membrane of rat liver mitochondria. J. Cell Biol. 46 (1970), 173–179.
    • (1970) J. Cell Biol. , vol.46 , pp. 173-179
    • Greenawalt, J.1
  • 20
    • 0014314486 scopus 로고
    • Some observations upon a new inhibitor of monoamine oxidase in brain tissue
    • [20] Johnston, J., Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem. Pharmacol. 17 (1968), 1285–1297.
    • (1968) Biochem. Pharmacol. , vol.17 , pp. 1285-1297
    • Johnston, J.1
  • 21
    • 33645307953 scopus 로고    scopus 로고
    • The therapeutic potential of monoamine oxidase inhibitors
    • [21] Youdim, M., Edmondson, D., Tipton, K., The therapeutic potential of monoamine oxidase inhibitors. Nat. Rev. Neurosci. 7 (2006), 295–309.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 295-309
    • Youdim, M.1    Edmondson, D.2    Tipton, K.3
  • 23
    • 0024273128 scopus 로고
    • Platelet MAO-B activity and the psychopathology of Parkinson's disease, senile dementia and multi-infarct dementia
    • [23] Danielczyk, W., Streifler, M., Konradi, C., Riederer, P., Moll, G., Platelet MAO-B activity and the psychopathology of Parkinson's disease, senile dementia and multi-infarct dementia. Acta Psychiatr. Scand. 78 (1988), 730–736.
    • (1988) Acta Psychiatr. Scand. , vol.78 , pp. 730-736
    • Danielczyk, W.1    Streifler, M.2    Konradi, C.3    Riederer, P.4    Moll, G.5
  • 24
    • 84899577518 scopus 로고    scopus 로고
    • Monoamine oxidase inhibitors: promising therapeutic agents for Alzheimer's disease (Review)
    • [24] Cai, Z., Monoamine oxidase inhibitors: promising therapeutic agents for Alzheimer's disease (Review). Mol. Med. Rep., 5, 2014.
    • (2014) Mol. Med. Rep. , vol.5
    • Cai, Z.1
  • 25
    • 84884919003 scopus 로고    scopus 로고
    • Monoamine oxidase inhibitory activity of 3,5-biaryl-4,5-dihydro-1H-pyrazole-1-carboxylate derivatives
    • [25] Vishnu Nayak, B., Ciftci-Yabanoglu, S., Jadav, S., Jagrat, M., Sinha, B., Ucar, G., et al. Monoamine oxidase inhibitory activity of 3,5-biaryl-4,5-dihydro-1H-pyrazole-1-carboxylate derivatives. Eur. J. Med. Chem. 69 (2013), 762–767.
    • (2013) Eur. J. Med. Chem. , vol.69 , pp. 762-767
    • Vishnu Nayak, B.1    Ciftci-Yabanoglu, S.2    Jadav, S.3    Jagrat, M.4    Sinha, B.5    Ucar, G.6
  • 26
    • 0032999243 scopus 로고    scopus 로고
    • Selegiline in the treatment of Alzheimer's disease: a long-term randomized placebo-controlled trial. Czech and slovak senile dementia of alzheimer type study group
    • [26] Filip, B., Kolibas, E., Selegiline in the treatment of Alzheimer's disease: a long-term randomized placebo-controlled trial. Czech and slovak senile dementia of alzheimer type study group. J. Psychiatry Neurosci. 24 (1999), 234–243.
    • (1999) J. Psychiatry Neurosci. , vol.24 , pp. 234-243
    • Filip, B.1    Kolibas, E.2
  • 27
    • 84940885311 scopus 로고    scopus 로고
    • Multifunctional enzyme inhibition for neuroprotection: A focus on MAO, NOS and AChE inhibitors. In Drug Design and Discovery in Alzheimer's Disease
    • [27] Joubert, J., Petzer, J., Prins, L., Repsold, B., Malan, S., Multifunctional enzyme inhibition for neuroprotection: A focus on MAO, NOS and AChE inhibitors. In Drug Design and Discovery in Alzheimer's Disease. Bentham Books., 2014, 291–365.
    • (2014) Bentham Books. , pp. 291-365
    • Joubert, J.1    Petzer, J.2    Prins, L.3    Repsold, B.4    Malan, S.5
  • 29
    • 11144245220 scopus 로고    scopus 로고
    • Multi-functional drugs for various CNS targets in the treatment of neurodegenerative disorders
    • [29] Youdim, M., Buccafusco, J., Multi-functional drugs for various CNS targets in the treatment of neurodegenerative disorders. Trends Pharmacol. Sci. 26 (2005), 27–35.
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 27-35
    • Youdim, M.1    Buccafusco, J.2
  • 30
    • 0035855832 scopus 로고    scopus 로고
    • Coumarins derivatives as dual inhibitors of acetylcholinesterase and monoamine oxidase
    • [30] Brühlmann, C., Ooms, F., Carrupt, P., Testa, B., Catto, M., Leonetti, F., et al. Coumarins derivatives as dual inhibitors of acetylcholinesterase and monoamine oxidase. J. Med. Chem. 44 (2001), 3195–3198.
    • (2001) J. Med. Chem. , vol.44 , pp. 3195-3198
    • Brühlmann, C.1    Ooms, F.2    Carrupt, P.3    Testa, B.4    Catto, M.5    Leonetti, F.6
  • 31
    • 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
    • [31] Sterling, J., Herzig, Y., Goren, T., Finkelstein, N., Lerner, D., Goldenberg, W., 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. 45 (2002), 5260–5279.
    • (2002) J. Med. Chem. , vol.45 , pp. 5260-5279
    • Sterling, J.1    Herzig, Y.2    Goren, T.3    Finkelstein, N.4    Lerner, D.5    Goldenberg, W.6
  • 32
    • 80053462390 scopus 로고    scopus 로고
    • Targeting monoamine oxidases with multipotent ligands: an emerging strategy in the search of new drugs against neurodegenerative diseases
    • [32] Pisani, L., Catto, M., Leonetti, F., Nicolotti, O., Stefanachi, A., Campagna, F., et al. Targeting monoamine oxidases with multipotent ligands: an emerging strategy in the search of new drugs against neurodegenerative diseases. Curr. Med. Chem. 18 (2011), 4568–4587.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 4568-4587
    • Pisani, L.1    Catto, M.2    Leonetti, F.3    Nicolotti, O.4    Stefanachi, A.5    Campagna, F.6
  • 33
    • 84055217642 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and molecular modeling of donepezil and N -[(5-(benzyloxy)-1-methyl-1 H -indol-2-yl)methyl]- N -methylprop-2-yn-1-amine hybrids as new multipotent cholinesterase/monoamine oxidase inhibitors for the treatment of Alzheimer's disease
    • [33] Bolea, I., Juárez-Jiménez, J., de los Rı́os, C., Chioua, M., Pouplana, R., Luque, F., et al. Synthesis, biological evaluation, and molecular modeling of donepezil and N -[(5-(benzyloxy)-1-methyl-1 H -indol-2-yl)methyl]- N -methylprop-2-yn-1-amine hybrids as new multipotent cholinesterase/monoamine oxidase inhibitors for the treatment of Alzheimer's disease. J. Med. Chem. 54 (2011), 8251–8270.
    • (2011) J. Med. Chem. , vol.54 , pp. 8251-8270
    • Bolea, I.1    Juárez-Jiménez, J.2    de los Rı́os, C.3    Chioua, M.4    Pouplana, R.5    Luque, F.6
  • 34
    • 84860318738 scopus 로고    scopus 로고
    • Multipotent MAO and cholinesterase inhibitors for the treatment of Alzheimer's disease: synthesis, pharmacological analysis and molecular modeling of heterocyclic substituted alkyl and cycloalkyl propargyl amine
    • [34] Samadi, A., de los Ríos, C., Bolea, I., Chioua, M., Iriepa, I., Moraleda, I., et al. Multipotent MAO and cholinesterase inhibitors for the treatment of Alzheimer's disease: synthesis, pharmacological analysis and molecular modeling of heterocyclic substituted alkyl and cycloalkyl propargyl amine. Eur. J. Med. Chem. 52 (2012), 251–262.
    • (2012) Eur. J. Med. Chem. , vol.52 , pp. 251-262
    • Samadi, A.1    de los Ríos, C.2    Bolea, I.3    Chioua, M.4    Iriepa, I.5    Moraleda, I.6
  • 35
    • 84887881725 scopus 로고    scopus 로고
    • Dual inhibitors of monoamine oxidase and cholinesterase for the treatment of alzheimer disease
    • [35] Yanez, M., Vina, D., Dual inhibitors of monoamine oxidase and cholinesterase for the treatment of alzheimer disease. CTMC 13 (2013), 1692–1706.
    • (2013) CTMC , vol.13 , pp. 1692-1706
    • Yanez, M.1    Vina, D.2
  • 36
    • 84920175684 scopus 로고    scopus 로고
    • N -methyl- N -((1-methyl-5-(3-(1-(2-methylbenzyl)piperidin-4-yl)propoxy)-1 H -indol-2-yl)methyl)prop-2-yn-1-amine, a new cholinesterase and monoamine oxidase dual inhibitor
    • [36] Bautista-Aguilera, O., Samadi, A., Chioua, M., Nikolic, K., Filipic, S., Agbaba, D., et al. N -methyl- N -((1-methyl-5-(3-(1-(2-methylbenzyl)piperidin-4-yl)propoxy)-1 H -indol-2-yl)methyl)prop-2-yn-1-amine, a new cholinesterase and monoamine oxidase dual inhibitor. J. Med. Chem. 57 (2014), 10455–10463.
    • (2014) J. Med. Chem. , vol.57 , pp. 10455-10463
    • Bautista-Aguilera, O.1    Samadi, A.2    Chioua, M.3    Nikolic, K.4    Filipic, S.5    Agbaba, D.6
  • 37
    • 84900532421 scopus 로고    scopus 로고
    • Donepezil + propargylamine + 8-hydroxyquinoline hybrids as new multifunctional metal-chelators, ChE and MAO inhibitors for the potential treatment of Alzheimer's disease
    • [37] Wang, L., Esteban, G., Ojima, M., Bautista-Aguilera, O., Inokuchi, T., Moraleda, I., et al. Donepezil + propargylamine + 8-hydroxyquinoline hybrids as new multifunctional metal-chelators, ChE and MAO inhibitors for the potential treatment of Alzheimer's disease. Eur. J. Med. Chem. 80 (2014), 543–561.
    • (2014) Eur. J. Med. Chem. , vol.80 , pp. 543-561
    • Wang, L.1    Esteban, G.2    Ojima, M.3    Bautista-Aguilera, O.4    Inokuchi, T.5    Moraleda, I.6
  • 38
    • 84937680699 scopus 로고    scopus 로고
    • Structure-based design and optimization of multitarget-directed 2 H -Chromen-2-one derivatives as potent inhibitors of monoamine oxidase B and cholinesterases
    • [38] Farina, R., Pisani, L., Catto, M., Nicolotti, O., Gadaleta, D., Denora, N., et al. Structure-based design and optimization of multitarget-directed 2 H -Chromen-2-one derivatives as potent inhibitors of monoamine oxidase B and cholinesterases. J. Med. Chem. 58 (2015), 5561–5578.
    • (2015) J. Med. Chem. , vol.58 , pp. 5561-5578
    • Farina, R.1    Pisani, L.2    Catto, M.3    Nicolotti, O.4    Gadaleta, D.5    Denora, N.6
  • 39
    • 84960361124 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of novel donepezil–coumarin hybrids as multi-target agents for the treatment of Alzheimer's disease
    • [39] Xie, S., Lan, J., Wang, X., Wang, Z., Jiang, N., Li, F., et al. Design, synthesis and biological evaluation of novel donepezil–coumarin hybrids as multi-target agents for the treatment of Alzheimer's disease. Bioorg. Med. Chem. 24 (2016), 1528–1539.
    • (2016) Bioorg. Med. Chem. , vol.24 , pp. 1528-1539
    • Xie, S.1    Lan, J.2    Wang, X.3    Wang, Z.4    Jiang, N.5    Li, F.6
  • 40
    • 84876107554 scopus 로고    scopus 로고
    • A comprehensive review on synthesis and designing aspects of coumarin derivatives as monoamine oxidase inhibitors for depression and Alzheimer's disease
    • [40] Patil, P., Bari, S., Firke, S., Deshmukh, P., Donda, S., Patil, D., A comprehensive review on synthesis and designing aspects of coumarin derivatives as monoamine oxidase inhibitors for depression and Alzheimer's disease. Bioorg. Med. Chem. 21 (2013), 2434–2450.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 2434-2450
    • Patil, P.1    Bari, S.2    Firke, S.3    Deshmukh, P.4    Donda, S.5    Patil, D.6
  • 41
    • 0034649564 scopus 로고    scopus 로고
    • Inhibition of monoamine oxidases by functionalized coumarin derivatives: biological activities, QSARs, and 3D-QSARs
    • [41] Gnerre, C., Catto, M., Leonetti, F., Weber, P., Carrupt, P., Altomare, C., et al. Inhibition of monoamine oxidases by functionalized coumarin derivatives: biological activities, QSARs, and 3D-QSARs. J. Med. Chem. 43 (2000), 4747–4758.
    • (2000) J. Med. Chem. , vol.43 , pp. 4747-4758
    • Gnerre, C.1    Catto, M.2    Leonetti, F.3    Weber, P.4    Carrupt, P.5    Altomare, C.6
  • 42
    • 71049173711 scopus 로고    scopus 로고
    • Discovery of a novel class of potent coumarin monoamine oxidase B inhibitors: development and biopharmacological profiling of 7-[(3-Chlorobenzyl)oxy]-4-[(methylamino)methyl]-2H-chromen-2-one methanesulfonate (NW-1772) as a highly potent, selective, reversible, and orally active monoamine oxidase B inhibitor
    • [42] Pisani, L., Muncipinto, G., Miscioscia, T., Nicolotti, O., Leonetti, F., Catto, M., et al. Discovery of a novel class of potent coumarin monoamine oxidase B inhibitors: development and biopharmacological profiling of 7-[(3-Chlorobenzyl)oxy]-4-[(methylamino)methyl]-2H-chromen-2-one methanesulfonate (NW-1772) as a highly potent, selective, reversible, and orally active monoamine oxidase B inhibitor. J. Med. Chem. 52 (2009), 6685–6706.
    • (2009) J. Med. Chem. , vol.52 , pp. 6685-6706
    • Pisani, L.1    Muncipinto, G.2    Miscioscia, T.3    Nicolotti, O.4    Leonetti, F.5    Catto, M.6
  • 43
    • 36148955400 scopus 로고    scopus 로고
    • Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs
    • [43] Binda, C., Wang, J., Pisani, L., Caccia, C., Carotti, A., Salvati, P., et al. Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs. J. Med. Chem. 50 (2007), 5848–5852.
    • (2007) J. Med. Chem. , vol.50 , pp. 5848-5852
    • Binda, C.1    Wang, J.2    Pisani, L.3    Caccia, C.4    Carotti, A.5    Salvati, P.6
  • 44
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme
    • [44] Inestrosa, N., Alvarez, A., Pérez, C., Moreno, R., Vicente, M., Linker, C., et al. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16 (1996), 881–891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.1    Alvarez, A.2    Pérez, C.3    Moreno, R.4    Vicente, M.5    Linker, C.6
  • 45
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation
    • [45] De Ferrari, G., Canales, M., Shin, I., Weiner, L., Silman, I., Inestrosa, N., A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry 40 (2001), 10447–10457.
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.1    Canales, M.2    Shin, I.3    Weiner, L.4    Silman, I.5    Inestrosa, N.6
  • 46
    • 22144436584 scopus 로고    scopus 로고
    • Memory deficits correlating with acetylcholinesterase splice shift and amyloid burden in doubly transgenic mice
    • [46] Rees, T., Berson, A., Sklan, E., Younkin, L., Younkin, S., Brimijoin, S., et al. Memory deficits correlating with acetylcholinesterase splice shift and amyloid burden in doubly transgenic mice. CAR 2 (2005), 291–300.
    • (2005) CAR , vol.2 , pp. 291-300
    • Rees, T.1    Berson, A.2    Sklan, E.3    Younkin, L.4    Younkin, S.5    Brimijoin, S.6
  • 47
    • 77249136019 scopus 로고    scopus 로고
    • Amyloid-β-Acetylcholinesterase complexes potentiate neurodegenerative changes induced by the Aβ peptide. Implications for the pathogenesis of Alzheimer's disease
    • [47] Dinamarca, M., Sagal, J., Quintanilla, R., Godoy, J., Arrázola, M., Inestrosa, N., Amyloid-β-Acetylcholinesterase complexes potentiate neurodegenerative changes induced by the Aβ peptide. Implications for the pathogenesis of Alzheimer's disease. Mol. Neurodegener., 5, 2010, 4.
    • (2010) Mol. Neurodegener. , vol.5 , pp. 4
    • Dinamarca, M.1    Sagal, J.2    Quintanilla, R.3    Godoy, J.4    Arrázola, M.5    Inestrosa, N.6
  • 48
    • 25844509359 scopus 로고    scopus 로고
    • Human recombinant monoamine oxidase B as reliable and efficient enzyme source for inhibitor screening
    • [48] Novaroli, L., Reist, M., Favre, E., Carotti, A., Catto, M., Carrupt, P., Human recombinant monoamine oxidase B as reliable and efficient enzyme source for inhibitor screening. Bioorg. Med. Chem. 13 (2005), 6212–6217.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 6212-6217
    • Novaroli, L.1    Reist, M.2    Favre, E.3    Carotti, A.4    Catto, M.5    Carrupt, P.6
  • 49
    • 84982179413 scopus 로고    scopus 로고
    • [49] Tavari, M., Malan, S., Joubert, J., Design, synthesis, biological evaluation and docking studies of sulfonyl isatin derivatives as monoamine oxidase and caspase-3 inhibitors. Med. Chem. Commun., 2016, 10.1039/c6md00228e.
  • 50
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • [50] Ellman, G., Courtney, K., Andres, V., Featherstone, R., A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7 (1961), 88–95.
    • (1961) Biochem. Pharmacol. , vol.7 , pp. 88-95
    • Ellman, G.1    Courtney, K.2    Andres, V.3    Featherstone, R.4
  • 51
    • 84862159765 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of indanone derivatives as acetylcholinesterase inhibitors and metal-chelating agents
    • [51] Meng, F., Mao, F., Shan, W., Qin, F., Huang, L., Li, X., Design, synthesis, and evaluation of indanone derivatives as acetylcholinesterase inhibitors and metal-chelating agents. Bioorg. Med. Chem. Lett. 22 (2012), 4462–4466.
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 4462-4466
    • Meng, F.1    Mao, F.2    Shan, W.3    Qin, F.4    Huang, L.5    Li, X.6
  • 52
    • 0036016027 scopus 로고    scopus 로고
    • Research and development of donepezil hydrochloride, a new type of acetylcholinesterase inhibitor
    • [52] Sugimoto, H., Ogura, H., Arai, Y., Iimura, Y., Yamanishi, Y., Research and development of donepezil hydrochloride, a new type of acetylcholinesterase inhibitor. Jpn. J. Pharmacol. 89 (2002), 7–20.
    • (2002) Jpn. J. Pharmacol. , vol.89 , pp. 7-20
    • Sugimoto, H.1    Ogura, H.2    Arai, Y.3    Iimura, Y.4    Yamanishi, Y.5
  • 54
    • 0033103478 scopus 로고    scopus 로고
    • ®): implications for the design of new anti-Alzheimer drugs
    • [54] Kryger, G., Silman, I., Sussman, J., Structure of acetylcholinesterase complexed with E2020 (Aricept®): implications for the design of new anti-Alzheimer drugs. Structure 7 (1999), 297–307.
    • (1999) Structure , vol.7 , pp. 297-307
    • Kryger, G.1    Silman, I.2    Sussman, J.3
  • 55
    • 85032063650 scopus 로고    scopus 로고
    • [55] Molecular Operating Environment (MOE), Version 2015.10. http//www.chemcomp.com.
  • 56
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • [56] Arnold, K., Bordoli, L., Kopp, J., Schwede, T., The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22 (2005), 195–201.
    • (2005) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 58
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • [58] Trott Olson, A., AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31 (2009), 455–461.
    • (2009) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott Olson, A.1
  • 59
  • 60
    • 13844251864 scopus 로고    scopus 로고
    • Empirical evidence of neuroprotection by dual cholinesterase inhibition in Alzheimers disease
    • [60] Venneri, A., McGeown, W., Shanks, M., Empirical evidence of neuroprotection by dual cholinesterase inhibition in Alzheimers disease. NeuroReport 16 (2005), 107–110.
    • (2005) NeuroReport , vol.16 , pp. 107-110
    • Venneri, A.1    McGeown, W.2    Shanks, M.3
  • 61
    • 4043074138 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: new roles and therapeutic alternatives
    • [61] Giacobini, E., Cholinesterase inhibitors: new roles and therapeutic alternatives. Pharmacol. Res. 50 (2004), 433–440.
    • (2004) Pharmacol. Res. , vol.50 , pp. 433-440
    • Giacobini, E.1
  • 62
    • 0042693016 scopus 로고    scopus 로고
    • Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
    • [62] Binda, C., Li, M., Hubalek, F., Restelli, N., Edmondson, D., Mattevi, A., Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc. Natl. Acad. Sci. 100 (2003), 9750–9755.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 9750-9755
    • Binda, C.1    Li, M.2    Hubalek, F.3    Restelli, N.4    Edmondson, D.5    Mattevi, A.6
  • 63
    • 0347296066 scopus 로고    scopus 로고
    • Assessing the performance of OMEGA with respect to retrieving bioactive conformations
    • [63] Boström, J., Greenwood, J., Gottfries, J., Assessing the performance of OMEGA with respect to retrieving bioactive conformations. J. Mol. Graph. Model. 21 (2003), 449–462.
    • (2003) J. Mol. Graph. Model. , vol.21 , pp. 449-462
    • Boström, J.1    Greenwood, J.2    Gottfries, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.