메뉴 건너뛰기




Volumn 22, Issue 8, 2012, Pages 871-886

Acetylcholinesterase inhibitors: A patent review (2008 present)

Author keywords

Alzheimer's disease; Carbofuran; Donepezil; Galantamine; Huperzine; Myasthenia gravis; Nerve agents; Pyridostigmine; Rivastigmine; Tacrine

Indexed keywords

ACETYLCHOLINESTERASE; ADONEP; CARBAMIC ACID DERIVATIVE; CARBOFURAN; CHOLINESTERASE INHIBITOR; DESMEDIPHAM; DIMETHOATE; DONEPEZIL; EVERTAS; FENOXYCARB; FOSETYL ALUMINUM; GALANTAMINE; HUPERZINE A; HUPERZINE B; METHIOCARB; METRIFONATE; ORGANOPHOSPHATE INSECTICIDE; PHENMEDIPHAM; PIRIMICARB; PROPAMOCARB; RISTIDIC; RIVASTIGMINE; SARIN; SOMAN; TABUN; TACRINE; UNCLASSIFIED DRUG; VASTIGMEX; YASNAL; ZT 1;

EID: 84864213744     PISSN: 13543776     EISSN: 17447674     Source Type: Journal    
DOI: 10.1517/13543776.2012.701620     Document Type: Review
Times cited : (138)

References (114)
  • 1
    • 79955729234 scopus 로고    scopus 로고
    • Localisation of pre- and postsynaptic cholinergic markers in the human brain
    • Wevers A. Localisation of pre- and postsynaptic cholinergic markers in the human brain. Behav Brain Res 2011;221:341-55
    • (2011) Behav. Brain. Res. , vol.221 , pp. 341-355
    • Wevers, A.1
  • 2
    • 33947684265 scopus 로고    scopus 로고
    • Human serum cholinesterase from liver pathological samples exhibit highly elevated aryl acylamidase activity
    • DOI 10.1016/j.cca.2007.02.001, PII S0009898107000617
    • Boopathy R, Rajesh RV, Darvesh S, Layer PG. Human serum cholinesterase from liver pathological samples exhibit highly elevated aryl acylamidase activity. Clin Chim Acta 2007;380:151-6 (Pubitemid 46498047)
    • (2007) Clinica Chimica Acta , vol.380 , Issue.1-2 , pp. 151-156
    • Boopathy, R.1    Rajesh, R.V.2    Darvesh, S.3    Layer, P.G.4
  • 4
    • 0033654537 scopus 로고    scopus 로고
    • Blood cholinesterases as human biomarkers of organophosphorus pesticide exposure
    • Nigg HN, Knaak JB. Blood cholinesterases as human biomarkers of organophosphorus pesticide exposure. Rev Environ Contam Toxicol 2000;163:29-111
    • (2000) Rev. Environ Contam Toxicol , vol.163 , pp. 29-111
    • Nigg, H.N.1    Knaak, J.B.2
  • 5
    • 10444252700 scopus 로고
    • Uber humorale ubertragbarkeit der Hernervenwirkung
    • Loewi O. Uber humorale ubertragbarkeit der Hernervenwirkung. I Mitt Pflugers Arch 1921;189:239-42
    • (1921) I. Mitt. Pflugers. Arch. , vol.189 , pp. 239-242
    • Loewi, O.1
  • 6
    • 78650475178 scopus 로고    scopus 로고
    • Cholinergic central system, Alzheimer's disease, and anesthetics liaison a vicious circle
    • Schifilliti D, Santamaria LB, Rosa G, et al. Cholinergic central system, Alzheimer's disease, and anesthetics liaison: A vicious circle? J Alzheimers Dis 2010;3:35-41
    • (2010) J. Alzheimers Dis. , vol.3 , pp. 35-41
    • Schifilliti, D.1    Santamaria, L.B.2    Rosa, G.3
  • 7
    • 79955713813 scopus 로고    scopus 로고
    • Cholinergic systems mediate action from movement to higher consciousness
    • Woolf NJ, Butcher LL. Cholinergic systems mediate action from movement to higher consciousness. Behav Brain Res 2011;221:488-98
    • (2011) Behav. Brain. Res. , vol.221 , pp. 488-498
    • Woolf, N.J.1    Butcher, L.L.2
  • 8
    • 49449094458 scopus 로고    scopus 로고
    • Acetylcholine beyond neurons: The non-neuronal cholinergic system in humans
    • Wessler I, Kirkpatrick CJ. Acetylcholine beyond neurons: The non-neuronal cholinergic system in humans. Br J Pharmacol 2008;154:1558-71
    • (2008) Br. J. Pharmacol , vol.154 , pp. 1558-1571
    • Wessler, I.1    Kirkpatrick, C.J.2
  • 9
    • 0037375478 scopus 로고    scopus 로고
    • Cytosolic choline acetyltransferase binds specifically to cholinergic plasma membrane of rat brain synaptosomes to generate membrane-bound enzyme
    • DOI 10.1023/A:1022825407631
    • Gabrielle P, Jeana M, Lorenza EC. Cytosolic choline acetyltransferase binds specifically to cholinergic plasma membrane of rat brain synaptosomes to generate membrane-bound enzyme. Neurochem Res 2003;28:543-9 (Pubitemid 36314845)
    • (2003) Neurochemical Research , vol.28 , Issue.3-4 , pp. 543-549
    • Gabrielle, P.1    Jeana, M.2    Lorenza, E.-C.3
  • 10
    • 0029122830 scopus 로고
    • Synaptic like microvesicles: Do they participate in regulated exocytosis
    • Llona I. Synaptic like microvesicles: do they participate in regulated exocytosis? Neurochem Int 1995;27:219-26
    • (1995) Neurochem Int. , vol.27 , pp. 219-226
    • Llona, I.1
  • 13
    • 33747188659 scopus 로고    scopus 로고
    • Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting
    • Singh BR. Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting. Neurotox Res 2006;9:73-92
    • (2006) Neurotox Res. , vol.9 , pp. 73-92
    • Singh, B.R.1
  • 14
    • 68349146499 scopus 로고    scopus 로고
    • A review of experimental techniques used for the heterologous expression of nicotinic acetylcholine receptors
    • Millar NS. A review of experimental techniques used for the heterologous expression of nicotinic acetylcholine receptors. Biochem Pharmacol 2009;78:766-76
    • (2009) Biochem Pharmacol , vol.78 , pp. 766-776
    • Millar, N.S.1
  • 15
    • 58249113980 scopus 로고    scopus 로고
    • Mammalian nicotinic acetylcholine receptors: From structure to function
    • Albuquerque EX, Pereira EF, Alkondon M, Rogers SW. Mammalian nicotinic acetylcholine receptors: from structure to function. Physiol Rev 2009;89:73-120
    • (2009) Physiol Rev. , vol.89 , pp. 73-120
    • Albuquerque, E.X.1    Pereira, E.F.2    Alkondon, M.3    Rogers, S.W.4
  • 16
    • 84857663983 scopus 로고    scopus 로고
    • Alpha7 nicotinic acetylcholine receptor is a target in pharmacology and toxicology
    • Pohanka M. Alpha7 nicotinic acetylcholine receptor is a target in pharmacology and toxicology. Int J Mol Sci 2012;13:2219-38
    • (2012) Int. J. Mol. Sci. , Issue.13 , pp. 2219-2238
    • Pohanka, M.1
  • 17
    • 79851491493 scopus 로고    scopus 로고
    • Macrophage-assisted inflammation and pharmacological regulation of the cholinergic anti-inflammatory pathway
    • Pohanka M, Snopkova S, Havlickova K, et al. Macrophage-assisted inflammation and pharmacological regulation of the cholinergic anti-inflammatory pathway. Curr Med Chem 2011;18:539-51
    • (2011) Curr. Med. Chem. , vol.18 , pp. 539-551
    • Pohanka, M.1    Snopkova, S.2    Havlickova, K.3
  • 18
    • 0026722913 scopus 로고
    • Reconstitution of agonist-stimulated phoshpatidylinostiol 4,5-bisphosphate hydrolysis using purified m1 muscarinic receptor, Gq/11 and phospholipase C-beta1
    • Berstein G, Blank JL, Smrcka AV, et al. Reconstitution of agonist-stimulated phoshpatidylinostiol 4,5-bisphosphate hydrolysis using purified m1 muscarinic receptor, Gq/11 and phospholipase C-beta1. J Biol Chem 1992;267:8081-8
    • (1992) J. Biol. Chem. , vol.267 , pp. 8081-8088
    • Berstein, G.1    Blank, J.L.2    Smrcka, A.V.3
  • 19
    • 75749117137 scopus 로고    scopus 로고
    • Kinetics of M1 muscarinic receptor and G protein signaling to phospholipase C in living cells
    • Falkenburger BH, Jensen JB, Hille B. Kinetics of M1 muscarinic receptor and G protein signaling to phospholipase C in living cells. J Gen Physiol 2010;135:81-97
    • (2010) J. Gen. Physiol. , vol.135 , pp. 81-97
    • Falkenburger, B.H.1    Jensen, J.B.2    Hille, B.3
  • 20
    • 0026086012 scopus 로고
    • Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells
    • Parker EM, Kameyama K, Higashijima T, Ross EM. Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells. J Biol Chem 1991;266:519-27 (Pubitemid 21906154)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.1 , pp. 519-527
    • Parker, E.M.1    Kameyama, K.2    Higashijima, T.3    Ross, E.M.4
  • 21
    • 33846981174 scopus 로고    scopus 로고
    • Excessive hippocampal acetylcholine levels in acetylcholinesterase- deficient mice are moderated by butyrylcholinesterase activity
    • Hartmann J, Kiewert C, Duysen EG, et al. Excessive hippocampal acetylcholine levels in acetylcholinesterase-deficient mice are moderated by butyrylcholinesterase activity. J Neurochem 2007;100:1421-9
    • (2007) J. Neurochem , vol.100 , pp. 1421-1429
    • Hartmann, J.1    Kiewert, C.2    Duysen, E.G.3
  • 22
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
    • Cygler M, Schrag JD, Sussman JL, et al. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related enzymes. Protein Sci 1993;2:366-82 (Pubitemid 23071285)
    • (1993) Protein Science , vol.2 , Issue.3 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 23
    • 50649087289 scopus 로고    scopus 로고
    • Acetylcholinesterase: How is structure related to function
    • Silman I, Sussman JL. Acetylcholinesterase: how is structure related to function? Chem Biol Interact 2008;175:3-10
    • (2008) Chem. Biol. Interact , vol.175 , pp. 3-10
    • Silman, I.1    Sussman, J.L.2
  • 24
    • 77249107098 scopus 로고    scopus 로고
    • Probing Torpedo californica acetylcholinesterase catalytic gorge with two novel bis-functional galanthamine derivatives
    • Bartolucci C, Haller LA, Jardis U, et al. Probing Torpedo californica acetylcholinesterase catalytic gorge with two novel bis-functional galanthamine derivatives. J Med Chem 2010;53:745-51
    • (2010) J. Med. Chem. , vol.53 , pp. 745-751
    • Bartolucci, C.1    Haller, L.A.2    Jardis, U.3
  • 26
    • 51649083818 scopus 로고    scopus 로고
    • Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics
    • Xu T, Colletier JP, Weik M, et al. Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics. Biophys J 2008;95:2500-11
    • (2008) Biophys J. , vol.95 , pp. 2500-11
    • Xu, T.1    Colletier, J.P.2    Weik, M.3
  • 28
    • 0033583819 scopus 로고    scopus 로고
    • The adhesion function on acetylcholinesterase is located at the peripheral anionic site
    • DOI 10.1006/bbrc.1999.0705
    • Johnson G, Moore SW. The adhesion function on acetylcholinesterase is located at the peripheral anionic site. Biochem Biophys Res Commun 1999;258:758-62 (Pubitemid 29290343)
    • (1999) Biochemical and Biophysical Research Communications , vol.258 , Issue.3 , pp. 758-762
    • Johnson, G.1    Moore, S.W.2
  • 29
    • 0025636509 scopus 로고
    • Are soluble and membrane-bound rat brain acetylcholinesterase different
    • Andres C, elMourabit M, Stutz C, et al. Are soluble and membrane-bound rat brain acetylcholinesterase different? Neurochem Res 1990;15:1065-72
    • (1990) Neurochem Res. , vol.15 , pp. 1065-1072
    • Andres, C.1    Lmourabit, M.2    Stutz, C.3
  • 30
    • 0033038088 scopus 로고    scopus 로고
    • The polymorphism of acetylcholinesterase: Post-translational processing, quaternary associations and localization
    • DOI 10.1016/S0009-2797(99)00011-3, PII S0009279799000113
    • Massoulie J, Anselment A, Bon S, et al. The polymorphism of acetylcholinesterase: Post-translational processing, quaternary associations and localization. Chem Biol Interact 1999;119:29-42 (Pubitemid 29278536)
    • (1999) Chemico-Biological Interactions , vol.119-120 , pp. 29-42
    • Massoulie, J.1    Anselmet, A.2    Bon, S.3    Krejci, E.4    Legay, C.5    Morel, N.6    Simon, S.7
  • 31
    • 0027228514 scopus 로고
    • Subunit association and glycosylation of acetylcholinesterase from monkey brain
    • Liao J, Norgaard-Pedersen B, Brodbeck U. Subunit association and glycosylation of acetylcholinesterase from monkey brain. J Neurochem 1993;61:1127-34 (Pubitemid 23241254)
    • (1993) Journal of Neurochemistry , vol.61 , Issue.3 , pp. 1127-1134
    • Liao, J.1    Norgaard-Pedersen, B.2    Brodbeck, U.3
  • 34
    • 10044275708 scopus 로고    scopus 로고
    • Organophosphates/nerve agents poisoning: Mechanism of action, diagnosis, prophylaxis, and treatment
    • Bajgar J. Organophosphates/nerve agents poisoning: mechanism of action, diagnosis, prophylaxis, and treatment. Adv Clin Chem 2004;38:151-216
    • (2004) Adv. Clin. Chem. , vol.38 , pp. 151-216
    • Bajgar, J.1
  • 35
    • 79960594305 scopus 로고    scopus 로고
    • Organophosphate poisoning in a 12-day-old infant: Case report
    • O'Reilly DA, Heikens GT. Organophosphate poisoning in a 12-day-old infant: Case report. Ann Trop Paediatr 2011;31:263-7
    • (2011) Ann. Trop. Paediatr. , vol.31 , pp. 263-267
    • O'Reilly, D.A.1    Heikens, G.T.2
  • 36
    • 80051813965 scopus 로고    scopus 로고
    • Atropine maintenance dosage in Acetylcholinesterase inhibitors: A patent review 2008 - Present
    • Thiermann H, Steinritz D, Worek F, et al. Atropine maintenance dosage in Acetylcholinesterase inhibitors: A patent review (2008 - present) Expert Opin. Ther. Patents (2012) 22(8) 883 patients with severe organophosphate pesticide poisoning. Toxicol Lett 2011;206:77-83
    • (2012) Expert Opin. Ther. Patents. , vol.22 , Issue.8 , pp. 77-83
    • Thiermann, H.1    Steinritz, D.2    Worek, F.3
  • 37
    • 80053260978 scopus 로고    scopus 로고
    • Metrifonate alters antioxidant levels and caspase activity in cerebral cortex of Wistar rats
    • Pohanka M, Novotny L, Pikula J. Metrifonate alters antioxidant levels and caspase activity in cerebral cortex of Wistar rats. Toxicol Mech Methods 2011;21:585-90
    • (2011) Toxicol Mech. Methods. , vol.21 , pp. 585-590
    • Pohanka, M.1    Novotny, L.2    Pikula, J.3
  • 39
    • 77955551992 scopus 로고    scopus 로고
    • Aging mechanism of butyrylcholinesterase inhibited by an N-methyl analogue of tabun: Implications of the trigonal-bipyramidal transition state rearrangement for the phosphorylation or reactivation of cholinesterases
    • Nachon F, Carletti E, Worek F, Masson P. Aging mechanism of butyrylcholinesterase inhibited by an N-methyl analogue of tabun: Implications of the trigonal-bipyramidal transition state rearrangement for the phosphorylation or reactivation of cholinesterases. Chem Biol Interact 2010;187:44-8
    • (2010) Chem. Biol. Interact. , vol.187 , pp. 44-48
    • Nachon, F.1    Carletti, E.2    Worek, F.3    Masson, P.4
  • 40
    • 84855170541 scopus 로고    scopus 로고
    • The developmental neurotoxicity of organophosphorus insecticides insecticides: A direct role for the oxon metabolites
    • Flaskos J. The developmental neurotoxicity of organophosphorus insecticides insecticides: A direct role for the oxon metabolites. Toxicol Lett 2012;209:86-93
    • (2012) Toxicol Lett. , Issue.209 , pp. 86-93
    • Flaskos, J.1
  • 41
    • 0036830397 scopus 로고    scopus 로고
    • Activated transformations of organophosphorus insecticides in the case of non-AChE inhibitory oxons
    • DOI 10.1002/ps.546
    • Kasagami T, Miyamoto T, Yamamoto I. Activated transformations of organophosphorus insecticides in the case of non-AChE inhibitory oxons. Pest Manag Sci 2002;58:1107-17 (Pubitemid 35252446)
    • (2002) Pest Management Science , vol.58 , Issue.11 , pp. 1107-1117
    • Kasagami, T.1    Miyamoto, T.2    Yamamoto, I.3
  • 42
    • 83455213369 scopus 로고    scopus 로고
    • Environmental aspects of organophosphorus and carbamate pesticides approved for use in the Czech Republic
    • Vlcek V, Pohanka M. Environmental aspects of organophosphorus and carbamate pesticides approved for use in the Czech Republic. Chem Listy 2011;105:908-12
    • (2011) Chem. Listy. , vol.105 , pp. 908-912
    • Vlcek, V.1    Pohanka, M.2
  • 44
    • 35848970751 scopus 로고    scopus 로고
    • Carbofuran-induced oxidative stress in mammalian brain
    • DOI 10.1007/s12033-007-0046-9
    • Rai DK, Sharma B. Carbofuran-induced oxidative stress in mammalian brain. Mol Biotechnol 2007;37:66-71 (Pubitemid 350135908)
    • (2007) Molecular Biotechnology , vol.37 , Issue.1 , pp. 66-71
    • Rai, D.K.1    Sharma, B.2
  • 48
    • 80053160297 scopus 로고    scopus 로고
    • Alzheimer's disease and related neurodegenerative disorders: Implication and counteracting of melatonin
    • Pohanka M. Alzheimer's disease and related neurodegenerative disorders: Implication and counteracting of melatonin. J Appl Biomed 2011;9:185-96
    • (2011) J. Appl. Biomed. , vol.9 , pp. 185-196
    • Pohanka, M.1
  • 49
    • 78149463046 scopus 로고    scopus 로고
    • Modulators of cytoskeletal reorganization in CA1 hippocampal neurons show increased expression in patients at mid-stage Alzheimer's disease
    • Kao PF, Davis DA, Banigan MG, et al. Modulators of cytoskeletal reorganization in CA1 hippocampal neurons show increased expression in patients at mid-stage Alzheimer's disease. PLoS ONE 2010;5:e13337
    • (2010) PLoS ONE , vol.5
    • Kao, P.F.1    Davis, D.A.2    Banigan, M.G.3
  • 51
    • 84860226091 scopus 로고    scopus 로고
    • Acitretin, an enhancer of alpha-secretase expression, crosses the blood-brain barrier and is not eliminated by p-glycoprotein
    • Holthoewer D, Endres K, Schuck F, et al. Acitretin, an enhancer of alpha-secretase expression, crosses the blood-brain barrier and is not eliminated by p-glycoprotein. Neurodegener Dis 2012;10:224-8
    • (2012) Neurodegener Dis. , Issue.10 , pp. 224-228
    • Holthoewer, D.1    Endres, K.2    Schuck, F.3
  • 52
    • 84862300133 scopus 로고    scopus 로고
    • Generation of Alzheimer disease-associated Abeta42/43 by gamma-secretase can directly be inhibited by modulation of membrane thickness
    • In press
    • Winkler E, Kamp F, Scheuring J, et al. Generation of Alzheimer disease-associated Abeta42/43 by gamma-secretase can directly be inhibited by modulation of membrane thickness. J Biol Chem 2012;In press
    • J Biol Chem 2012
    • Winkler, E.1    Kamp, F.2    Scheuring, J.3
  • 53
    • 80155190091 scopus 로고    scopus 로고
    • Which memory system is impaired first in Alzheimer's disease
    • Didic M, Barbeau EJ, Felician O, et al. Which memory system is impaired first in Alzheimer's disease. J Alzheimers Dis 2011;27:11-22
    • (2011) J. Alzheimers Dis. , vol.27 , pp. 11-22
    • Didic M Barbeau, E.J.1    Felician, O.2
  • 54
    • 0042508791 scopus 로고    scopus 로고
    • Neuropathologic changes in Alzheimer's disease
    • Wenk GL. Neuropathologic changes in Alzheimer's disease. J Clin Psychiatry 2003;64(Suppl 9):7-10
    • (2003) J. Clin. Psychiatry. , vol.64 , Issue.SUPPL. 9 , pp. 7-10
    • Wenk, G.L.1
  • 55
    • 2942514710 scopus 로고    scopus 로고
    • Cholinesterase inhibitors used in the treatment of Alzheimer's disease: The relationship between pharmacological effects and clinical efficacy
    • DOI 10.2165/00002512-200421070-00004
    • Wilkinson DG, Francis PT, Schwam E, Payne-Parrish J. Cholinesterase inhibitors used in the treatment of Alzheimer's disease: The relationship between pharmacological effects and clinical efficacy. Drugs Aging 2004;21:453-78 (Pubitemid 38736890)
    • (2004) Drugs and Aging , vol.21 , Issue.7 , pp. 453-478
    • Wilkinson, D.G.1    Francis, P.T.2    Schwam, E.3    Payne-Parrish, J.4
  • 56
    • 80052028010 scopus 로고    scopus 로고
    • Targeting the nicotinic alpha7 acetylcholine receptor to enhance cognition in disease
    • Wallace TL, Porter RH. Targeting the nicotinic alpha7 acetylcholine receptor to enhance cognition in disease. Biochem Pharmacol 2011;82:891-903
    • (2011) Biochem Pharmacol , vol.82 , pp. 891-903
    • Wallace, T.L.1    Porter, R.H.2
  • 58
    • 77953625660 scopus 로고    scopus 로고
    • Memantine ER a one-daily formulation for the treatment of Alzheimer's disease
    • Bassil N, Thaipisuttikul P, Grossberg GT. Memantine ER, a one-daily formulation for the treatment of Alzheimer's disease. Expert Opin Pharmacother 2010;11:1765-71
    • (2010) Expert. Opin. Pharmacother , vol.11 , pp. 1765-1771
    • Bassil, N.1    Thaipisuttikul, P.2    Grossberg, G.T.3
  • 60
    • 0030879494 scopus 로고    scopus 로고
    • Donepezil (E2020): A new acetylcholinesterase inhibitor. Review of its pharmacology, pharmacokinetics, and utility in the treatment of Alzheimer's disease
    • DOI 10.1517/13543784.6.10.1527
    • Heydorn WE. Donepezil (E2020): A new acetylcholinesterase inhibitor. Review of its pharmacology, pharmacokinetics, and utility in the treatment of Alzheimer's disease. Expert Opin Investig Drugs 1997;6:1527-35 (Pubitemid 27432489)
    • (1997) Expert Opinion on Investigational Drugs , vol.6 , Issue.10 , pp. 1527-1535
    • Heydorn, W.E.1
  • 62
    • 77951560923 scopus 로고    scopus 로고
    • A review of clinical pharmacokinetics and pharmacodynamics of galantamine, a reversible acetylcholinesterase inhibitor for the treatment of Alzheimer's disease, in healthy subjects and patients
    • Huang F, Fu Y. A review of clinical pharmacokinetics and pharmacodynamics of galantamine, a reversible acetylcholinesterase inhibitor for the treatment of Alzheimer's disease, in healthy subjects and patients. Curr Clin Pharmacol 2010;5:115-24
    • (2010) Curr. Clin. Pharmacol , vol.5 , pp. 115-124
    • Huang, F.1    Fu, Y.2
  • 63
    • 0035254937 scopus 로고    scopus 로고
    • Three-dimensional structure of a complex of galanthamine (Nivalin®) with acetylcholinesterase from Torpedo californica: Implications for the design of new anti-Alzheimer drugs
    • DOI 10.1002/1097-0134(20010201)42:2<182::AID-PROT50>3.0.CO;2-1
    • Bartolucci C, Perola E, Pilger C, et al. Three dimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: Implications for the design of new anti-Alzheimer drugs. Proteins 2001;42:182-91 (Pubitemid 32047326)
    • (2001) Proteins: Structure, Function and Genetics , vol.42 , Issue.2 , pp. 182-191
    • Bartolucci, C.1    Perola, E.2    Pilger, C.3    Fels, G.4    Lamba, D.5
  • 64
    • 33845712062 scopus 로고    scopus 로고
    • Galantamine enhances dopaminergic neurotransmission in vivo via allosteric potentiation of nicotinic acetylcholine receptors
    • DOI 10.1038/sj.npp.1301087, PII 1301087
    • Schilstrom B, Ivanov VB, Wiker C, Svensson TH. Galantamine enhances dopaminergic neurotransmission in vivo via allosteric potentiation of nicotinic acetylcholine receptors. Neuropsychopharmacology 2007;32:43-53 (Pubitemid 44967783)
    • (2007) Neuropsychopharmacology , vol.32 , Issue.1 , pp. 43-53
    • Schilstrom, B.1    Ivanov, V.B.2    Wiker, C.3    Svensson, T.H.4
  • 65
    • 70349319533 scopus 로고    scopus 로고
    • Effects of rivastigmine and donepezil on brain acetylcholine levels in acetylcholinesterase-deficient mice
    • Naik RS, Hartmann J, Kiewert C, et al. Effects of rivastigmine and donepezil on brain acetylcholine levels in acetylcholinesterase-deficient mice. J Pharm Pharm Sci 2009;12:79-85
    • (2009) J. Pharm. Pharm. Sci. , vol.12 , pp. 79-85
    • Naik, R.S.1    Hartmann, J.2    Kiewert, C.3
  • 66
    • 80855132396 scopus 로고    scopus 로고
    • Rivastigmine transdermal patch and capsule in Alzheimer's disease: Influence of disease stage on response to therapy
    • Farlow MR, Grossberg GT, Meng X, et al. Rivastigmine transdermal patch and capsule in Alzheimer's disease: Influence of disease stage on response to therapy. Int J Gariatric Psychiatry 2011;26:1236-43
    • (2011) Int. J. Gariatric Psychiatry , vol.26 , pp. 1236-1243
    • Farlow, M.R.1    Grossberg, G.T.2    Meng, X.3
  • 67
    • 34249902022 scopus 로고    scopus 로고
    • Rivastigmine in the treatment of patients with Alzheimer's disease
    • DOI 10.2147/nedt.2007.3.2.211
    • Muller T. Rivastigmine in the treatment of patients with Alzheimer's disease. Neuropsychiatr Dis Treat 2007;3:211-18 (Pubitemid 46864060)
    • (2007) Neuropsychiatric Disease and Treatment , vol.3 , Issue.2 , pp. 211-218
    • Muller, T.1
  • 68
    • 67349281227 scopus 로고    scopus 로고
    • Huperzine A protects isolated rat brain mitochondria against beta-amyloid peptide
    • Gao X, Zheng CY, Yang L, et al. Huperzine A protects isolated rat brain mitochondria against beta-amyloid peptide. Free Radic Biol Med 2009;46:1454-62
    • (2009) Free. Radic. Biol. Med. , vol.46 , pp. 1454-1462
    • Gao, X.1    Zheng, C.Y.2    Yang, L.3
  • 69
    • 0342409367 scopus 로고    scopus 로고
    • Huperzine B a novel acetylcholinesterase inhibitor, attenuates hydrogen peroxide induced injury in PC12 cells
    • Zhang HY, Tang XC. Huperzine B, a novel acetylcholinesterase inhibitor, attenuates hydrogen peroxide induced injury in PC12 cells. Neurosci Lett 2000;292:41-4
    • (2000) Neurosci Lett. , vol.292 , pp. 41-44
    • Zhang, H.Y.1    Tang, X.C.2
  • 70
    • 50649113266 scopus 로고    scopus 로고
    • Huperzine A treatment protects against N-methyl-D-aspartate-induced seizure/status epilepticus in rats
    • Coleman BR, Ratcliffe RH, Oguntayo SA, et al. [+]-Huperzine A treatment protects against N-methyl-D-aspartate-induced seizure/status epilepticus in rats. Chem Biol Interact 2008;175:387-95
    • (2008) Chem. Biol. Interact. , vol.175 , pp. 387-395
    • Coleman, B.R.1    Ratcliffe, R.H.2    Oguntayo, S.A.3
  • 71
    • 67349262023 scopus 로고    scopus 로고
    • Efficacy and safety of natural acetylcholinesterase inhibitor huperzine A in the treatment of Alzheimer's disease: An updated meta-analysis
    • Wang BS, Wang H, Wei ZH, et al. Efficacy and safety of natural acetylcholinesterase inhibitor huperzine A in the treatment of Alzheimer's disease: An updated meta-analysis. J Neural Transm 2009;116:457-65
    • (2009) J. Neural. Transm. , vol.116 , pp. 457-465
    • Wang, B.S.1    Wang, H.2    Wei, Z.H.3
  • 72
    • 79960600801 scopus 로고    scopus 로고
    • Huperzine a as potential treatment of Alzheimer's disease: An assessment on chemistry, pharmacology, and clinical studies
    • Ha GT, Wong RK, Zhang Y. Huperzine a as potential treatment of Alzheimer's disease: An assessment on chemistry, pharmacology, and clinical studies. Chem Biodivers 2011;8:1189-204
    • (2011) Chem. Biodivers. , vol.8 , pp. 1189-1204
    • Ha, G.T.1    Wong, R.K.2    Zhang, Y.3
  • 73
    • 84857400037 scopus 로고    scopus 로고
    • Huperzine induces alteration in oxidative balance and antioxidant in a guinea pig model
    • Pohanka M, Hrabinova M, Zemek F, et al. Huperzine induces alteration in oxidative balance and antioxidant in a guinea pig model. Neuro Endocrinol Lett 2011;32(Suppl 1):95-100
    • (2011) Neuro. Endocrinol Lett. , vol.32 , Issue.SUPPL. 1 , pp. 95-100
    • Pohanka, M.1    Hrabinova, M.2    Zemek, F.3
  • 74
    • 84856869571 scopus 로고    scopus 로고
    • Toxicological scoring of Alzheimer's disease drug huperzine in a guinea pig model
    • Pohanka M, Zemek F, Bandouchova H, Pikula J. Toxicological scoring of Alzheimer's disease drug huperzine in a guinea pig model. Toxicol Mech Methods 2012;22:231-5
    • (2012) Toxicol. Mech. Methods. , Issue.22 , pp. 231-235
    • Pohanka, M.1    Zemek, F.2    Bandouchova, H.3    Pikula, J.4
  • 76
    • 12244291292 scopus 로고    scopus 로고
    • Identification of cytochrome P450 1A2 as enzyme involved in the microsomal metabolism of Huperzine A
    • DOI 10.1016/S0014-2999(03)01290-1
    • Ma X, Wang H, Xin J, et al. Identification of cytochrome P450 1A2 as enzyme involved in the microsomal metabolism of huperzine A. Eur J Pharmacol 2003;461:89-92 (Pubitemid 36174026)
    • (2003) European Journal of Pharmacology , vol.461 , Issue.2-3 , pp. 89-92
    • Ma, X.1    Wang, H.2    Xin, J.3    Zhang, T.4    Tu, Z.5
  • 77
    • 34447578839 scopus 로고    scopus 로고
    • Huperzine A from Huperzia species-An ethnopharmacolgical review
    • DOI 10.1016/j.jep.2007.05.030, PII S0378874107002784
    • Ma X, Tan C, Zhu D, et al. Huperzine A from Huperzia species - an ethnopharmacological review. J Ethnopharmacol 2007;113:15-34 (Pubitemid 47077860)
    • (2007) Journal of Ethnopharmacology , vol.113 , Issue.1 , pp. 15-34
    • Ma, X.1    Tan, C.2    Zhu, D.3    Gang, D.R.4    Xiao, P.5
  • 78
    • 57849085355 scopus 로고    scopus 로고
    • Seasonal phenology and management of Tomarus subtropicus (Coleoptera: Scarabaedae) in St
    • Kostromytska OS, Buss EA. Seasonal phenology and management of Tomarus subtropicus (Coleoptera: Scarabaedae) in St. Augustinegrass J Econ Entomol 2008;101:1847-55
    • (2008) Augustinegrass J. Econ. Entomol , vol.101 , pp. 1847-1855
    • Kostromytska, O.S.1    Buss, E.A.2
  • 79
    • 80053260978 scopus 로고    scopus 로고
    • Metrifonate alters antioxidant levels and caspase activity in cerebral cortex of Wistar rats
    • Pohanka M, Novotny L, Pikula J. Metrifonate alters antioxidant levels and caspase activity in cerebral cortex of Wistar rats. Toxicol Mech Methods 2011;21:585-90
    • (2011) Toxicol Mech. Methods. , vol.21 , pp. 585-590
    • Pohanka, M.1    Novotny, L.2    Pikula, J.3
  • 80
    • 0032856188 scopus 로고    scopus 로고
    • The effect of food and time of administration on the pharmacokinetic and pharmacodynamic profile of metrifonate
    • Heining R, Sachse R. The effect of food and time of administration on the pharmacokinetic and pharmacodynamic profile of metrifonate. Int J Clin Pharmacol Ther 1999;37:456-64 (Pubitemid 29423983)
    • (1999) International Journal of Clinical Pharmacology and Therapeutics , vol.37 , Issue.9 , pp. 456-464
    • Heinig, R.1    Sachse, R.2
  • 81
    • 0034090742 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled, multicenter study to evaluate the safety and tolerability of metrifonate in patients with probable Alzheimer disease
    • DOI 10.1097/00002093-200001000-00005
    • Blass JP, Cyrus PA, Bieber F, Gulanski B. Randomized, double-blind, placebo controlled, multicenter study to evaluate the safety and tolerability of metrifonate in patients with probable Alzheimer disease. The metrifonate study group. Alzheimer Dis Assoc Disord 2000;14:39-45 (Pubitemid 30142730)
    • (2000) Alzheimer Disease and Associated Disorders , vol.14 , Issue.1 , pp. 39-45
    • Blass, J.P.1    Cyrus, P.A.2    Bieber, F.3    Gulanski, B.4
  • 83
    • 33845984024 scopus 로고    scopus 로고
    • Re-evaluation of tacrine hepatotoxicity using gel entrapped hepatocytes
    • Meng Q, Ru J, Zhang G, et al. Re-evaluation of tacrine hepatotoxicity using gel entrapped hepatocytes. Toxicol Lett 2006;168:140-7
    • (2006) Toxicol. Lett. , vol.168 , pp. 140-147
    • Meng, Q.1    Ru, J.2    Zhang, G.3
  • 84
    • 77951447009 scopus 로고    scopus 로고
    • Structure, function, regulation and polymorphism and the clinical significance of human cytochrome P450 1A2
    • Zhou SF, Wang B, Yang LP, Liu JP. Structure, function, regulation and polymorphism and the clinical significance of human cytochrome P450 1A2. Drug Metab Rev 2010;42:268-354
    • (2010) Drug. Metab. Rev. , vol.42 , pp. 268-354
    • Zhou, S.F.1    Wang, B.2    Yang, L.P.3    Liu, J.P.4
  • 85
    • 84856212958 scopus 로고    scopus 로고
    • 3D-pharmacophore model based virtual screening to identify dual-binding site and selective acetylcholinesterase inhibitors
    • Gupta S, Mohan CG. 3D-pharmacophore model based virtual screening to identify dual-binding site and selective acetylcholinesterase inhibitors. Med Chem Res 2011;20:1422-30
    • (2011) Med. Chem. Res. , vol.20 , pp. 1422-1430
    • Gupta, S.1    Mohan, C.G.2
  • 86
    • 37549022563 scopus 로고    scopus 로고
    • Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology
    • Berson A, Knobloch M, Hanan M, et al. Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology. Brain 2008;131:109-19
    • (2008) Brain , vol.131 , pp. 109-119
    • Berson, A.1    Knobloch, M.2    Hanan, M.3
  • 87
    • 62249171200 scopus 로고    scopus 로고
    • Different cholinesterase inhibitor effects on CSF cholinesterases in Alzheimer patients
    • Nordberg A, Darreh-Shori T, Peskind E, et al. Different cholinesterase inhibitor effects on CSF cholinesterases in Alzheimer patients. Curr Alzheimer Res 2009;6:4-14
    • (2009) Curr. Alzheimer Res. , vol.6 , pp. 4-14
    • Nordberg, A.1    Darreh-Shori, T.2    Peskind, E.3
  • 88
    • 77649234636 scopus 로고    scopus 로고
    • Effects of cholinesterase inhibitors on the activities and protein levels of cholinesterases in the cerebrospinal fluid of patients with Alzeheimer's disease: A review of recent clinical studies
    • Darreh-Shori T, Soininen H. Effects of cholinesterase inhibitors on the activities and protein levels of cholinesterases in the cerebrospinal fluid of patients with Alzeheimer's disease: A review of recent clinical studies. Curr Alzheimer Res 2010;7:67-73
    • (2010) Curr. Alzheimer Res. , vol.7 , pp. 67-73
    • Darreh-Shori, T.1    Soininen, H.2
  • 89
    • 84862825057 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of isaindigotone derivatives as dual inhibitors for acetylcholinesterase and amyloid beta aggregation
    • Yan JW, Li YP, Ye WJ, et al. Design, synthesis and evaluation of isaindigotone derivatives as dual inhibitors for acetylcholinesterase and amyloid beta aggregation. Bioorg Med Chem 2012;20:2527-34
    • (2012) Bioorg. Med. Chem. , Issue.20 , pp. 2527-2534
    • Yan, J.W.1    Li, Y.P.2    Ye, W.J.3
  • 90
    • 78651472058 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of novel tacrine-multialkoxybenzene hybrids as dual inhibitors for cholinesterases and amyloid beta aggregation
    • Luo W, Li YP, He Y, et al. Design, synthesis and evaluation of novel tacrine-multialkoxybenzene hybrids as dual inhibitors for cholinesterases and amyloid beta aggregation. Bioorg Med Chem 2011;19:763-70
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 763-770
    • Luo, W.1    Li, Y.P.2    He, Y.3
  • 91
    • 84655164943 scopus 로고    scopus 로고
    • Ache inhibitor: A regio- and stereo-selective 13-dipolar cycloaddition for the synthesis of novel substituted 56-dimethoxy spiro[ 5.3 ']-oxindolespiro-[ 6.3 "]-2,3-dihydro-1H-inden-1 "-one-7-(substituted aryl)-tetrahydro-1Hpyrrolo[1,2-c][1,3]thiazole
    • Ali MA, Ismail R, Choon TS, et al. AChE inhibitor: A regio- and stereo-selective 1,3-dipolar cycloaddition for the synthesis of novel substituted 5,6-dimethoxy spiro[5.3 ']-oxindolespiro-[6.3 "]-2,3-dihydro- 1H-inden-1 "-one-7-(substituted aryl)-tetrahydro-1Hpyrrolo[1,2-c][1,3] thiazole. Bioorg Med Chem Lett 2012;22:508-11
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 508-511
    • Ali, M.A.1    Ismail, R.2    Choon, T.S.3
  • 92
    • 84858241256 scopus 로고    scopus 로고
    • The first dual ChE/FAAH inhibitors: New perspectives for Alzheimer's disease
    • Ramba A, Bartolini M, Bisi A, et al. The first dual ChE/FAAH inhibitors: new perspectives for Alzheimer's disease? ACS Med Chem Lett 2012;3:182-6
    • (2012) ACS. Med. Chem. Lett. , Issue.3 , pp. 182-186
    • Ramba, A.1    Bartolini, M.2    Bisi, A.3
  • 93
    • 84856914519 scopus 로고    scopus 로고
    • New tacrine-4-oxo-4Hchromene hybrids as multifunctional agents for the treatment of Alzheimer's disease, with cholinergic, antioxidant, and beta-amyloid reducing properties
    • Fernandez-Bachiller MI, Perez C, Monjas L, et al. New tacrine-4-oxo-4Hchromene hybrids as multifunctional agents for the treatment of Alzheimer's disease, with cholinergic, antioxidant, and beta-amyloid reducing properties. J Med Chem 2012;55:1303-17
    • (2012) J. Med. Chem. , Issue.55 , pp. 1303-1317
    • Fernandez-Bachiller, M.I.1    Perez, C.2    Monjas, L.3
  • 94
    • 67651114110 scopus 로고    scopus 로고
    • Tacrine-melatonin hybrids as multifunctional agents for Alzheimer's disease, with cholinergic, anti-oxidant, and neuroprotective properties
    • Fernandez-Bachiller MI, Perez C, Campillo NE, et al. Tacrine-melatonin hybrids as multifunctional agents for Alzheimer's disease, with cholinergic, anti-oxidant, and neuroprotective properties. ChemMedChem 2009;4:828-41
    • (2009) Chem. Med. Chem. , vol.4 , pp. 828-841
    • Fernandez-Bachiller, M.I.1    Perez, C.2    Campillo, N.E.3
  • 98
    • 84872209887 scopus 로고    scopus 로고
    • Acetylcholinesterase dual inhibitors. US20050148621A1 2005 Acetylcholinesterase inhibitors: A patent review 2008 - Present
    • Gil AM, Diaz ID, Arrieta LR, et al. Acetylcholinesterase dual inhibitors. US20050148621A1; 2005 Acetylcholinesterase inhibitors: A patent review (2008 - present) Expert Opin. Ther. Patents (2012) 22(8)
    • (2012) Expert. Opin. Ther. Patents , vol.22 , pp. 8
    • Gil, A.M.1    Diaz, I.D.2    Arrieta, L.R.3
  • 102
    • 3042561627 scopus 로고    scopus 로고
    • 6 receptor antagonists reverse delay-dependent deficits in novel object discrimination by enhancing consolidation - An effect sensitive to NMDA receptor antagonism
    • DOI 10.1016/j.neuropharm.2004.03.012, PII S0028390804000863
    • King MV, Sleight AJ, Woolley ML, et al.. 5-HT6 receptor antagonists reverse delay-dependent deficits in novel object discrimination by enhancing consolidation - an effect sensitive to NMDA receptor antagonism. Neuropharmacology 2004;47:195-204 (Pubitemid 38824643)
    • (2004) Neuropharmacology , vol.47 , Issue.2 , pp. 195-204
    • King, M.V.1    Sleight, A.J.2    Woolley, M.L.3    Topham, I.A.4    Marsden, C.A.5    Fone, K.C.F.6
  • 104
    • 34249705331 scopus 로고    scopus 로고
    • Therapeutic options in autoimmune myasthenia gravis
    • DOI 10.1016/j.autrev.2007.01.001, PII S1568997207000122, The predictive value of autoantibodies: analytical, diagnostic and counselling aspects
    • Garcia-Carrasco M, Escarcega RO, Fuentes-Alexandro S, et al. Therapeutic options in autoimmune myasthenia gravis. Autoimmun Rev 2007;6:373-8 (Pubitemid 46824097)
    • (2007) Autoimmunity Reviews , vol.6 , Issue.6 , pp. 373-378
    • Garcia-Carrasco, M.1    Escarcega, R.O.2    Fuentes-Alexandro, S.3    Riebeling, C.4    Cervera, R.5
  • 105
    • 34547895887 scopus 로고    scopus 로고
    • Treatment of human myasthenia gravis with oral antisense suppression of acetylcholinesterase
    • DOI 10.1212/01.wnl.0000267884.39468.7a, PII 0000611420070814000013
    • Argov Z, McKee D, Agus S, et al. Treatment of human myasthenia gravis with oral antisense suppression of acetylcholinesterase. Neurology 2007;69:699-700 (Pubitemid 47256014)
    • (2007) Neurology , vol.69 , Issue.7 , pp. 699-700
    • Argov, Z.1    McKee, D.2    Agus, S.3    Brawer, S.4    Shlomowitz, N.5    Yoseph, O.B.6    Soreq, H.7    Sussman, J.D.8
  • 107
    • 34547890688 scopus 로고    scopus 로고
    • Restoring balance at the neuromuscular junction
    • Kaminsky HJ. Restoring balance at the neuromuscular junction. Neurology 2007;69:629-30
    • (2007) Neurology , vol.69 , pp. 629-630
    • Kaminsky, H.J.1
  • 109
    • 33745700892 scopus 로고    scopus 로고
    • Cholinergic neuromuscular hyperactivity in patients with myasthenia gravis seropositive for MuSK antibody
    • Punga AR, Flink R, Askmark H, Stalberg EV. Cholinergic neuromuscular hyperactivity in patients with myasthenia gravis seropositive for MuSK antibody. Muscle Nerve 2006;34:111-15
    • (2006) Muscle. Nerve. , vol.34 , pp. 111-115
    • Punga, A.R.1    Flink, R.2    Askmark, H.3    Stalberg, E.V.4
  • 110
    • 80052441353 scopus 로고    scopus 로고
    • Treatment of myasthenia gravis: Focus on pyridostigmine
    • Maggi L, Mantegazza R. Treatment of myasthenia gravis: focus on pyridostigmine. Clin Drug Investig 2011;31:691-701
    • (2011) Clin. Drug. Investig. , vol.31 , pp. 691-701
    • Maggi, L.1    Mantegazza, R.2
  • 111
    • 67049165109 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors in MG: To be or not to be
    • Punga AR, Stalberg E. Acetylcholinesterase inhibitors in MG: To be or not to be? Muscle Nerve 2009;39:724-8
    • (2009) Muscle Nerve. , vol.39 , pp. 724-728
    • Punga, A.R.1    Stalberg, E.2
  • 113
    • 0037308205 scopus 로고    scopus 로고
    • The role of readthrough acetylcholinesterase in the pathophysiology of myasthenia gravis
    • DOI 10.1096/fj.02-0609com
    • Brenner T, Hamra-Amitay Y, Evron T, et al. The role of readthrough acetylcholinesterase in the pathophysiology of myasthenia gravis. FASEB J 2003;17:214-22 (Pubitemid 36164391)
    • (2003) FASEB Journal , vol.17 , Issue.2 , pp. 214-222
    • Brenner, T.1    Hamra-Amitay, Y.2    Evron, T.3    Boneva, N.4    Seidman, S.5    Soreq, H.6
  • 114
    • 0028843893 scopus 로고
    • Genetic predisposition to adverse consequences of anti-cholinesterases in 'atypical' BCHE carriers
    • Loewenstein-Lichtenstein Y, Scharz M, Glick D, et al. Genetic predisposition to adverse consequences of anti-cholinesterases in 'atypical' BCHE carriers. Nat Med 1995;1:1082-5
    • (1995) Nat. Med. , vol.1 , pp. 1082-1085
    • Loewenstein-Lichtenstein, Y.1    Scharz, M.2    Glick, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.