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Volumn 10, Issue 25, 2004, Pages 3121-3130

An overview of the current and novel drugs for Alzheimer's disease with particular reference to anti-cholinesterase compounds

Author keywords

AchE; Alzheimer's disease; Cholinesterase inhibitors

Indexed keywords

ACETYLCHOLINE; ACETYLCHOLINESTERASE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; AP 2238; CHOLINERGIC RECEPTOR STIMULATING AGENT; CHOLINESTERASE INHIBITOR; DICLOFENAC; DONEPEZIL; FLUOXETINE; GALANTAMINE; HUPRINE; IBUPROFEN; IBUPROFEN DERIVATIVE; IBUPROFEN OCTYL PYRIDOSTIGMINE; LADOSTIGIL; METRIFONATE; MONOAMINE OXIDASE INHIBITOR; NEUROTRANSMITTER; NONSTEROID ANTIINFLAMMATORY AGENT; NOOTROPIC AGENT; PROTEIN ANTIBODY; PROTEIN INHIBITOR; RASAGILINE; RIVASTIGMINE; RS 1259; SEROTONIN TRANSPORTER; TACRINE; UNCLASSIFIED DRUG; ZANEPEZIL;

EID: 4544291755     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612043383359     Document Type: Review
Times cited : (79)

References (79)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001; 81 (2): 741-66.
    • (2001) Physiol. Rev. , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 0031821608 scopus 로고    scopus 로고
    • Pharmacological drug treatment of Alzheimer disease: The cholinergic hypothesis revisited
    • Ladner CJ, Lee JM. Pharmacological drug treatment of Alzheimer disease: the cholinergic hypothesis revisited. J Neuropathol Exp Neurol 1998; 57 (8): 719-31.
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , Issue.8 , pp. 719-731
    • Ladner, C.J.1    Lee, J.M.2
  • 3
    • 0030763602 scopus 로고    scopus 로고
    • From molecular structure to Alzheimer therapy
    • Giacobini E. From molecular structure to Alzheimer therapy. Jpn J Pharmacol 1997; 74 (3): 225-41.
    • (1997) Jpn. J. Pharmacol. , vol.74 , Issue.3 , pp. 225-241
    • Giacobini, E.1
  • 4
    • 0032078728 scopus 로고    scopus 로고
    • Invited review: Cholinesterase inhibitors for Alzheimer's disease therapy: From tacrine to future applications
    • Giacobini E. Invited review: Cholinesterase inhibitors for Alzheimer's disease therapy: from tacrine to future applications. Neurochem Int 1998; 32 (5-6): 413-9.
    • (1998) Neurochem. Int. , vol.32 , Issue.5-6 , pp. 413-419
    • Giacobini, E.1
  • 5
    • 0036855661 scopus 로고    scopus 로고
    • Deciphering the genesis and fate of amyloid beta-protein yields novel therapies for Alzheimer disease
    • Selkoe DJ. Deciphering the genesis and fate of amyloid beta-protein yields novel therapies for Alzheimer disease. J Clin Invest 2002; 110 (10): 1375-81.
    • (2002) J. Clin. Invest. , vol.110 , Issue.10 , pp. 1375-1381
    • Selkoe, D.J.1
  • 6
    • 0028031486 scopus 로고
    • Structural determinants of the Alzheimer's amyloid beta-peptide
    • Soto C, Branes MC, Alvarez J, Inestrosa NC. Structural determinants of the Alzheimer's amyloid beta-peptide. J Neurochem 1994; 63 (4): 1191-8.
    • (1994) J. Neurochem. , vol.63 , Issue.4 , pp. 1191-1198
    • Soto, C.1    Branes, M.C.2    Alvarez, J.3    Inestrosa, N.C.4
  • 7
    • 0037335663 scopus 로고    scopus 로고
    • Alzheimer vaccine: Amyloid-beta on trial
    • Robinson SR, Bishop GM, Munch G. Alzheimer vaccine: amyloid-beta on trial. Bioessays 2003; 25 (3): 283-8.
    • (2003) Bioessays , vol.25 , Issue.3 , pp. 283-288
    • Robinson, S.R.1    Bishop, G.M.2    Munch, G.3
  • 8
    • 0032080309 scopus 로고    scopus 로고
    • Stable complexes involving acetylcholinesterase and amyloid-beta peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
    • Alvarez A, Alarcon R, Opazo C, Campos EO, Munoz FJ, Calderon FH, et al. Stable complexes involving acetylcholinesterase and amyloid-beta peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J Neurosci 1998; 18 (9): 3213-23.
    • (1998) J. Neurosci. , vol.18 , Issue.9 , pp. 3213-3223
    • Alvarez, A.1    Alarcon, R.2    Opazo, C.3    Campos, E.O.4    Munoz, F.J.5    Calderon, F.H.6
  • 9
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa NC, Alvarez A, Perez CA, Moreno RD, Vicente M, Linker C, et al. Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 1996; 16 (4): 881-91.
    • (1996) Neuron , vol.16 , Issue.4 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6
  • 10
    • 0031587755 scopus 로고    scopus 로고
    • A monoclonal antibody against acetylcholinesterase inhibits the formation of amyloid fibrils induced by the enzyme
    • Reyes AE, Perez DR, Alvarez A, Garrido J, Gentry MK, Doctor BP, et al. A monoclonal antibody against acetylcholinesterase inhibits the formation of amyloid fibrils induced by the enzyme. Biochem Biophys Res Commun 1997; 232 (3): 652-5.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , Issue.3 , pp. 652-655
    • Reyes, A.E.1    Perez, D.R.2    Alvarez, A.3    Garrido, J.4    Gentry, M.K.5    Doctor, B.P.6
  • 11
    • 0031587286 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils
    • Alvarez A, Opazo C, Alarcon R, Garrido J, Inestrosa NC. Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils. J Mol Biol 1997; 272 (3): 348-61.
    • (1997) J. Mol. Biol. , vol.272 , Issue.3 , pp. 348-361
    • Alvarez, A.1    Opazo, C.2    Alarcon, R.3    Garrido, J.4    Inestrosa, N.C.5
  • 12
    • 0038618612 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes beta-amyloid plaques in cerebral cortex
    • Rees T, Hammond PI, Soreq H, Younkin S, Brimijoin S. Acetylcholinesterase promotes beta-amyloid plaques in cerebral cortex. Neurobiol Aging 2003; 24 (6): 777-87.
    • (2003) Neurobiol. Aging , vol.24 , Issue.6 , pp. 777-787
    • Rees, T.1    Hammond, P.I.2    Soreq, H.3    Younkin, S.4    Brimijoin, S.5
  • 13
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation
    • De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC. A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation. Biochemistry 2001; 40 (35): 10447-57.
    • (2001) Biochemistry , vol.40 , Issue.35 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 14
    • 0032584277 scopus 로고    scopus 로고
    • Liposome-catalyzed unfolding of acetylcholinesterase from Bungarus fasciatus
    • Shin I, Silman I, Bon C, Weiner L. Liposome-catalyzed unfolding of acetylcholinesterase from Bungarus fasciatus. Biochemistry 1998; 37 (13): 4310-6.
    • (1998) Biochemistry , vol.37 , Issue.13 , pp. 4310-4316
    • Shin, I.1    Silman, I.2    Bon, C.3    Weiner, L.4
  • 15
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase - New roles for an old actor
    • Soreq H, Seidman S. Acetylcholinesterase - new roles for an old actor. Nat Rev Neurosci 2001; 2 (4): 294-302.
    • (2001) Nat. Rev. Neurosci. , vol.2 , Issue.4 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 16
    • 0025161330 scopus 로고
    • Molecular cloning of mouse acetylcholinesterase: Tissue distribution of alternatively spliced mRNA species
    • Rachinsky TL, Camp S, Li Y, Ekstrom TJ, Newton M, Taylor P. Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species. Neuron 1990; 5 (3): 317-27.
    • (1990) Neuron , vol.5 , Issue.3 , pp. 317-327
    • Rachinsky, T.L.1    Camp, S.2    Li, Y.3    Ekstrom, T.J.4    Newton, M.5    Taylor, P.6
  • 17
    • 0037435051 scopus 로고    scopus 로고
    • Structure-activity relationships of acetylcholinesterase noncovalent inhibitors based on a polyamine backbone. 2. Role of the substituents on the phenyl ring and nitrogen atoms of caproctamine
    • Tumiatti V, Rosini M, Bartolini M, Cavalli A, Marucci G, Andrisano V, et al. Structure-activity relationships of acetylcholinesterase noncovalent inhibitors based on a polyamine backbone. 2. Role of the substituents on the phenyl ring and nitrogen atoms of caproctamine. J Med Chem 2003; 46 (6): 954-66.
    • (2003) J. Med. Chem. , vol.46 , Issue.6 , pp. 954-966
    • Tumiatti, V.1    Rosini, M.2    Bartolini, M.3    Cavalli, A.4    Marucci, G.5    Andrisano, V.6
  • 18
    • 0037413712 scopus 로고    scopus 로고
    • Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
    • Bourne Y, Taylor P, Radic Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 2003; 22 (1): 1-12.
    • (2003) EMBO J. , vol.22 , Issue.1 , pp. 1-12
    • Bourne, Y.1    Taylor, P.2    Radic, Z.3    Marchot, P.4
  • 19
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, et al. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 1991; 253 (5022): 872-9.
    • (1991) Science , vol.253 , Issue.5022 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6
  • 20
    • 0642309501 scopus 로고    scopus 로고
    • Acetylcholinesterase: A multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease
    • Greenblatt HM, Dvir H, Silman I, Sussman JL. Acetylcholinesterase: a multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease. J Mol Neurosci 2003; 20 (3): 369-83.
    • (2003) J. Mol. Neurosci. , vol.20 , Issue.3 , pp. 369-383
    • Greenblatt, H.M.1    Dvir, H.2    Silman, I.3    Sussman, J.L.4
  • 21
    • 0142039868 scopus 로고    scopus 로고
    • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
    • Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem 2003; 278 (42): 41141-7.
    • (2003) J. Biol. Chem. , vol.278 , Issue.42 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.C.4    Nachon, F.5
  • 22
    • 0141818332 scopus 로고    scopus 로고
    • Cholinergic function and Alzheimer's disease
    • Giacobini E. Cholinergic function and Alzheimer's disease. Int J Geriatr Psychiatry 2003; 18 (Suppl 1): S1-5.
    • (2003) Int. J. Geriatr. Psychiatry , vol.18 , Issue.SUPPL. 1
    • Giacobini, E.1
  • 23
    • 0026620028 scopus 로고
    • Tacrine restores cholinergic nicotinic receptors and glucose metabolism in Alzheimer patients as visualized by positron emission tomography
    • Nordberg A, Lilja A, Lundqvist H, Hartvig P, Amberla K, Viitanen M, et al. Tacrine restores cholinergic nicotinic receptors and glucose metabolism in Alzheimer patients as visualized by positron emission tomography. Neurobiol Aging 1992; 13 (6): 747-58.
    • (1992) Neurobiol. Aging , vol.13 , Issue.6 , pp. 747-758
    • Nordberg, A.1    Lilja, A.2    Lundqvist, H.3    Hartvig, P.4    Amberla, K.5    Viitanen, M.6
  • 24
    • 0029817834 scopus 로고    scopus 로고
    • Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's disease
    • Pang YP, Quiram P, Jelacic T, Hong F, Brimijoin S. Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's disease. J Biol Chem 1996; 271 (39): 23646-9.
    • (1996) J. Biol. Chem. , vol.271 , Issue.39 , pp. 23646-23649
    • Pang, Y.P.1    Quiram, P.2    Jelacic, T.3    Hong, F.4    Brimijoin, S.5
  • 25
    • 0034036419 scopus 로고    scopus 로고
    • SAR of 9-amino-1, 2, 3, 4-tetrahydroacridine-based acetylcholinesterase inhibitors: Synthesis, enzyme inhibitory activity, QSAR, and structure-based CoMFA of tacrine analogues
    • Recanatini M, Cavalli A, Belluti F, Piazzi L, Rampa A, Bisi A, et al. SAR of 9-amino-1, 2, 3, 4-tetrahydroacridine-based acetylcholinesterase inhibitors: synthesis, enzyme inhibitory activity, QSAR, and structure-based CoMFA of tacrine analogues. J Med Chem 2000; 43 (10): 2007-18.
    • (2000) J. Med. Chem. , vol.43 , Issue.10 , pp. 2007-2018
    • Recanatini, M.1    Cavalli, A.2    Belluti, F.3    Piazzi, L.4    Rampa, A.5    Bisi, A.6
  • 26
    • 0037413568 scopus 로고    scopus 로고
    • Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors
    • Savini L, Gaeta A, Fattorusso C, Catalanotti B, Campiani G, Chiasserini L, et al. Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors. J Med Chem 2003; 46 (1): 1-4.
    • (2003) J. Med. Chem. , vol.46 , Issue.1 , pp. 1-4
    • Savini, L.1    Gaeta, A.2    Fattorusso, C.3    Catalanotti, B.4    Campiani, G.5    Chiasserini, L.6
  • 27
    • 0029613811 scopus 로고
    • The pharmacotherapy of Alzheimer's disease based on the cholinergic hypothesis: An update
    • Weinstock M. The pharmacotherapy of Alzheimer's disease based on the cholinergic hypothesis: an update. Neurodegeneration 1995; 4 (4): 349-56.
    • (1995) Neurodegeneration , vol.4 , Issue.4 , pp. 349-356
    • Weinstock, M.1
  • 28
    • 0141818331 scopus 로고    scopus 로고
    • Have cholinergic therapies reached their clinical boundary in Alzheimer's disease?
    • Jones RW. Have cholinergic therapies reached their clinical boundary in Alzheimer's disease? Int J Geriatr Psychiatry 2003; 18 (Suppl 1): S7-S13.
    • (2003) Int. J. Geriatr. Psychiatry , vol.18 , Issue.SUPPL. 1
    • Jones, R.W.1
  • 29
    • 0033103478 scopus 로고    scopus 로고
    • Structure of acetylcholinesterase complexed with E2020 (Aricept): Implications for the design of new anti-Alzheimer drugs
    • Kryger G, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs. Structure Fold Des 1999; 7 (3): 297-307.
    • (1999) Structure Fold Des. , vol.7 , Issue.3 , pp. 297-307
    • Kryger, G.1    Silman, I.2    Sussman, J.L.3
  • 30
    • 0032754559 scopus 로고    scopus 로고
    • Effect of donepezil hydrochloride (E2020) on extracellular acetylcholine concentration in the cerebral cortex of rats
    • Kosasa T, Kuriya Y, Yamanishi Y. Effect of donepezil hydrochloride (E2020) on extracellular acetylcholine concentration in the cerebral cortex of rats. Jpn J Pharmacol 1999; 81 (2): 216-22.
    • (1999) Jpn. J. Pharmacol. , vol.81 , Issue.2 , pp. 216-222
    • Kosasa, T.1    Kuriya, Y.2    Yamanishi, Y.3
  • 31
    • 0038721593 scopus 로고    scopus 로고
    • A review of rivastigmine: A reversible cholinesterase inhibitor
    • Williams BR, Nazarians A, Gill MA. A review of rivastigmine: a reversible cholinesterase inhibitor. Clin Ther 2003; 25 (6): 1634-53.
    • (2003) Clin. Ther. , vol.25 , Issue.6 , pp. 1634-1653
    • Williams, B.R.1    Nazarians, A.2    Gill, M.A.3
  • 32
    • 0037133519 scopus 로고    scopus 로고
    • Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine
    • Bar-On P, Millard CB, Harel M, Dvir H, Enz A, Sussman JL, et al. Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine. Biochemistry 2002; 41 (11): 3555-64.
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3555-3564
    • Bar-On, P.1    Millard, C.B.2    Harel, M.3    Dvir, H.4    Enz, A.5    Sussman, J.L.6
  • 33
    • 0033893555 scopus 로고    scopus 로고
    • The two faces of Alzheimer's disease
    • van Gool WA, Eikelenboom P. The two faces of Alzheimer's disease. J Neurol 2000; 247 (7): 500-5.
    • (2000) J. Neurol. , vol.247 , Issue.7 , pp. 500-505
    • van Gool, W.A.1    Eikelenboom, P.2
  • 34
    • 12444257779 scopus 로고    scopus 로고
    • 3-(4-[[Benzyl(methyl)amino]methyl]phenyl)-6, 7-dimethoxy-2H-2-chromenone (AP2238) inhibits both acetylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation: A dual function lead for Alzheimer's disease therapy
    • Piazzi L, Rampa A, Bisi A, Gobbi S, Belluti F, Cavalli A, et al. 3-(4-[[Benzyl(methyl)amino]methyl]phenyl)-6, 7-dimethoxy-2H-2-chromenone (AP2238) inhibits both acetylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation: a dual function lead for Alzheimer's disease therapy. J Med Chem 2003; 46 (12): 2279-82.
    • (2003) J. Med. Chem. , vol.46 , Issue.12 , pp. 2279-2282
    • Piazzi, L.1    Rampa, A.2    Bisi, A.3    Gobbi, S.4    Belluti, F.5    Cavalli, A.6
  • 35
    • 0035855832 scopus 로고    scopus 로고
    • Coumarins derivatives as dual inhibitors of acetylcholinesterase and monoamine oxidase
    • Bruhlmann C, Ooms F, Carrupt PA, Testa B, Catto M, Leonetti F, et al. Coumarins derivatives as dual inhibitors of acetylcholinesterase and monoamine oxidase. J Med Chem 2001; 44 (19): 3195-8.
    • (2001) J. Med. Chem. , vol.44 , Issue.19 , pp. 3195-3198
    • Bruhlmann, C.1    Ooms, F.2    Carrupt, P.A.3    Testa, B.4    Catto, M.5    Leonetti, F.6
  • 36
    • 0035968202 scopus 로고    scopus 로고
    • Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites
    • De Ferrari GV, Mallender WD, Inestrosa NC, Rosenberry TL. Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites. J Biol Chem 2001; 276 (26): 23282-7.
    • (2001) J. Biol. Chem. , vol.276 , Issue.26 , pp. 23282-23287
    • De Ferrari, G.V.1    Mallender, W.D.2    Inestrosa, N.C.3    Rosenberry, T.L.4
  • 37
    • 0016852324 scopus 로고
    • Mechanism of inhibition in vitro of mammalian acetylcholinesterase and cholinesterase in solutions of O, O-dimethyl 2, 2, 2-trichloro-1-hydroxyethyl phosphonate (Trichlorphon)
    • Reiner E, Krauthacker B, Simeon V, Skrinjaric-Spoljar M. Mechanism of inhibition in vitro of mammalian acetylcholinesterase and cholinesterase in solutions of O, O-dimethyl 2, 2, 2-trichloro-1-hydroxyethyl phosphonate (Trichlorphon). Biochem Pharmacol 1975; 24 (6): 717-22.
    • (1975) Biochem. Pharmacol. , vol.24 , Issue.6 , pp. 717-722
    • Reiner, E.1    Krauthacker, B.2    Simeon, V.3    Skrinjaric-Spoljar, M.4
  • 38
    • 0033048440 scopus 로고    scopus 로고
    • Characterization of learning and memory behaviours and the effects of metrifonate in the C57BL strain of mice
    • Ikonen S, Schmidt BH, Riekkinen P, Jr. Characterization of learning and memory behaviours and the effects of metrifonate in the C57BL strain of mice. Eur J Pharmacol 1999; 372 (2): 117-26.
    • (1999) Eur. J. Pharmacol. , vol.372 , Issue.2 , pp. 117-126
    • Ikonen, S.1    Schmidt, B.H.2    Riekkinen Jr., P.3
  • 40
    • 0031842292 scopus 로고    scopus 로고
    • Metrifonate treatment of the cognitive deficits of Alzheimer's disease
    • Metrifonate Study Group
    • Cummings JL, Cyrus PA, Bieber F, Mas J, Orazem J, Gulanski B. Metrifonate treatment of the cognitive deficits of Alzheimer's disease. Metrifonate Study Group. Neurology 1998; 50 (5): 1214-21.
    • (1998) Neurology , vol.50 , Issue.5 , pp. 1214-1221
    • Cummings, J.L.1    Cyrus, P.A.2    Bieber, F.3    Mas, J.4    Orazem, J.5    Gulanski, B.6
  • 41
    • 0034045806 scopus 로고    scopus 로고
    • Metrifonate therapy in Alzheimer's disease: A pooled analysis of four randomized, double-blind, placebo-controlled trials
    • Farlow MR, Cyrus PA. Metrifonate therapy in Alzheimer's disease: a pooled analysis of four randomized, double-blind, placebo-controlled trials. Dement Geriatr Cogn Disord 2000; 11 (4): 202-11.
    • (2000) Dement Geriatr. Cogn. Disord. , vol.11 , Issue.4 , pp. 202-211
    • Farlow, M.R.1    Cyrus, P.A.2
  • 42
    • 0035049129 scopus 로고    scopus 로고
    • Effects of chronic metrifonate treatment on cholinergic enzymes and the blood-brain barrier
    • Rakonczay Z, Papp H. Effects of chronic metrifonate treatment on cholinergic enzymes and the blood-brain barrier. Neurochem Int 2001; 39 (1): 19-24.
    • (2001) Neurochem. Int. , vol.39 , Issue.1 , pp. 19-24
    • Rakonczay, Z.1    Papp, H.2
  • 43
    • 0036174969 scopus 로고    scopus 로고
    • The effects of long-term treatment with metrifonate, a cholinesterase inhibitor, on cholinergic activity, amyloid pathology, and cognitive function in APP and PS1 doubly transgenic mice
    • Liu L, Ikonen S, Heikkinen T, Tapiola T, van Groen T, Tanila H. The effects of long-term treatment with metrifonate, a cholinesterase inhibitor, on cholinergic activity, amyloid pathology, and cognitive function in APP and PS1 doubly transgenic mice. Exp Neurol 2002; 173 (2): 196-204.
    • (2002) Exp. Neurol. , vol.173 , Issue.2 , pp. 196-204
    • Liu, L.1    Ikonen, S.2    Heikkinen, T.3    Tapiola, T.4    van Groen, T.5    Tanila, H.6
  • 44
    • 18744366138 scopus 로고    scopus 로고
    • Design and synthesis of dual inhibitors of acetylcholinesterase and serotonin transporter targeting potential agents for Alzheimer's disease
    • Kogen H, Toda N, Tago K, Marumoto S, Takami K, Ori M, et al. Design and synthesis of dual inhibitors of acetylcholinesterase and serotonin transporter targeting potential agents for Alzheimer's disease. Org Lett 2002;4 (20): 3359-62.
    • (2002) Org. Lett. , vol.4 , Issue.20 , pp. 3359-3362
    • Kogen, H.1    Toda, N.2    Tago, K.3    Marumoto, S.4    Takami, K.5    Ori, M.6
  • 45
    • 0037401391 scopus 로고    scopus 로고
    • Design, synthesis and structure-activity relationships of dual inhibitors of acetylcholinesterase and serotonin transporter as potential agents for Alzheimer's disease
    • Toda N, Tago K, Marumoto S, Takami K, Ori M, Yamada N, et al. Design, synthesis and structure-activity relationships of dual inhibitors of acetylcholinesterase and serotonin transporter as potential agents for Alzheimer's disease. Bioorg Med Chem 2003; 11 (9): 1935-55.
    • (2003) Bioorg. Med. Chem. , vol.11 , Issue.9 , pp. 1935-1955
    • Toda, N.1    Tago, K.2    Marumoto, S.3    Takami, K.4    Ori, M.5    Yamada, N.6
  • 46
    • 12444279097 scopus 로고    scopus 로고
    • Pharmacological characterization of RS-1259, an orally active dual inhibitor of acetylcholinesterase and serotonin transporter, in rodents: Possible treatment of Alzheimer's disease
    • Abe Y, Aoyagi A, Hara T, Abe K, Yamazaki R, Kumagae Y, et al. Pharmacological characterization of RS-1259, an orally active dual inhibitor of acetylcholinesterase and serotonin transporter, in rodents: possible treatment of Alzheimer's disease. J Pharmacol Sci 2003; 93 (1): 95-105.
    • (2003) J. Pharmacol. Sci. , vol.93 , Issue.1 , pp. 95-105
    • Abe, Y.1    Aoyagi, A.2    Hara, T.3    Abe, K.4    Yamazaki, R.5    Kumagae, Y.6
  • 47
    • 0037153195 scopus 로고    scopus 로고
    • Novel dual inhibitors of AChE and MAO derived from hydroxy aminoindan and phenethylamine as potential treatment for Alzheimer's disease
    • Sterling J, Herzig Y, Goren T, 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 2002; 45 (24): 5260-79.
    • (2002) J. Med. Chem. , vol.45 , Issue.24 , pp. 5260-5279
    • Sterling, J.1    Herzig, Y.2    Goren, T.3    Finkelstein, N.4    Lerner, D.5    Goldenberg, W.6
  • 48
    • 0032999575 scopus 로고    scopus 로고
    • Neuroprotective effect of rasagiline, a selective monoamine oxidase-B inhibitor, against closed head injury in the mouse
    • Huang W, Chen Y, Shohami E, Weinstock M. Neuroprotective effect of rasagiline, a selective monoamine oxidase-B inhibitor, against closed head injury in the mouse. Eur J Pharmacol 1999;366 (2-3): 127-35.
    • (1999) Eur. J. Pharmacol. , vol.366 , Issue.2-3 , pp. 127-135
    • Huang, W.1    Chen, Y.2    Shohami, E.3    Weinstock, M.4
  • 49
    • 0033809197 scopus 로고    scopus 로고
    • Development of a novel neuroprotective drug (TV3326) for the treatment of Alzheimer's disease, with Cholinesterase and Monoamine Oxidase inhibitory activities
    • Weinstock M, Goren T, Youdim MB. Development of a novel neuroprotective drug (TV3326) for the treatment of Alzheimer's disease, with Cholinesterase and Monoamine Oxidase inhibitory activities. Drug Dev Res 2000; 50: 216-22.
    • (2000) Drug Dev. Res. , vol.50 , pp. 216-222
    • Weinstock, M.1    Goren, T.2    Youdim, M.B.3
  • 50
    • 0036777108 scopus 로고    scopus 로고
    • Involvement of MAP kinase in the regulation of annyloid precursor protein processing by novel cholinesterase inhibitors derived from rasagiline
    • Yogev-Falach M, Amit T, Bar-Am O, Weinstock M, Youdim MB. Involvement of MAP kinase in the regulation of annyloid precursor protein processing by novel cholinesterase inhibitors derived from rasagiline. FASEB J 2002; 16 (12): 1674-6.
    • (2002) FASEB J. , vol.16 , Issue.12 , pp. 1674-1676
    • Yogev-Falach, M.1    Amit, T.2    Bar-Am, O.3    Weinstock, M.4    Youdim, M.B.5
  • 51
    • 0038389436 scopus 로고    scopus 로고
    • Amyloid processing and signal transduction properties of antiparkinson-antialzheimer neuroprotective drugs rasagiline and TV3326
    • discussion 87-93
    • Youdim MB, Amit T, Bar-Am O, Weinstock M, Yogev-Falach M. Amyloid processing and signal transduction properties of antiparkinson-antialzheimer neuroprotective drugs rasagiline and TV3326. Ann NY Acad Sci 2003; 993: 378-86; discussion 87-93.
    • (2003) Ann. NY Acad. Sci. , vol.993 , pp. 378-386
    • Youdim, M.B.1    Amit, T.2    Bar-Am, O.3    Weinstock, M.4    Yogev-Falach, M.5
  • 52
    • 0038012567 scopus 로고    scopus 로고
    • A novel cholinesterase and brain-selective monoamine oxidase inhibitor for the treatment of dementia comorbid with depression and Parkinson's disease
    • Weinstock M, Gorodetsky E, Poltyrev T, Gross A, Sagi Y, Youdim M. A novel cholinesterase and brain-selective monoamine oxidase inhibitor for the treatment of dementia comorbid with depression and Parkinson's disease. Prog Neuropsychopharmacol Biol Psychiatry 2003; 27 (4): 555-61.
    • (2003) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.27 , Issue.4 , pp. 555-561
    • Weinstock, M.1    Gorodetsky, E.2    Poltyrev, T.3    Gross, A.4    Sagi, Y.5    Youdim, M.6
  • 54
    • 0034121289 scopus 로고    scopus 로고
    • Central selective acetylcholinesterase inhibitor with neurotrophic activity: Structure-activity relationships of TAK-147 and related compounds
    • Ishihara Y, Goto G, Miyamoto M. Central selective acetylcholinesterase inhibitor with neurotrophic activity: structure-activity relationships of TAK-147 and related compounds. Curr Med Chem 2000; 7 (3): 341-54.
    • (2000) Curr. Med. Chem. , vol.7 , Issue.3 , pp. 341-354
    • Ishihara, Y.1    Goto, G.2    Miyamoto, M.3
  • 55
    • 0030973899 scopus 로고    scopus 로고
    • Neurochemical effects of 3-[1-(phenylmethyl)-4-piperidinyl]-1-(2,3, 4, 5-tetrahydro-1H-1-b enzazepin-8-yl)-1-propanone fumarate (TAK-147), a novel acetylcholinesterase inhibitor, in rats
    • Hirai K, Kato K, Nakayama T, Hayako H, Ishihara Y, Goto G, et al. Neurochemical effects of 3-[1-(phenylmethyl)-4-piperidinyl]-1-(2,3, 4, 5-tetrahydro-1H-1-b enzazepin-8-yl)-1-propanone fumarate (TAK-147), a novel acetylcholinesterase inhibitor, in rats. J Pharmacol Exp Ther 1997; 280 (3): 1261-9.
    • (1997) J. Pharmacol. Exp. Ther. , vol.280 , Issue.3 , pp. 1261-1269
    • Hirai, K.1    Kato, K.2    Nakayama, T.3    Hayako, H.4    Ishihara, Y.5    Goto, G.6
  • 57
    • 85047691727 scopus 로고    scopus 로고
    • NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo
    • Eriksen JL, Sagi SA, Smith TE, Weggen S, Das P, McLendon DC, et al. NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo. J Clin Invest 2003; 112 (3): 440-9.
    • (2003) J. Clin. Invest. , vol.112 , Issue.3 , pp. 440-449
    • Eriksen, J.L.1    Sagi, S.A.2    Smith, T.E.3    Weggen, S.4    Das, P.5    McLendon, D.C.6
  • 59
    • 0141742312 scopus 로고    scopus 로고
    • Characterization of New Animal Models for the Study of Alzheimer's Disease
    • Faculty of Biological Sciences. Santiago: Pontifica Catholic University of Chile
    • Reyes AE. Characterization of New Animal Models for the Study of Alzheimer's Disease. Faculty of Biological Sciences. Santiago: Pontifica Catholic University of Chile, 2000.
    • (2000)
    • Reyes, A.E.1
  • 60
    • 0035479004 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease
    • Hock BJ Jr, Lamb BT. Transgenic mouse models of Alzheimer's disease. Trends Genet 2001; 17 (10): S7-12.
    • (2001) Trends Genet. , vol.17 , Issue.10
    • Hock Jr., B.J.1    Lamb, B.T.2
  • 61
    • 0030833055 scopus 로고    scopus 로고
    • Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins
    • Borchelt DR, Ratovitski T, van Lare J, Lee MK, Gonzales V, Jenkins NA, et al. Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 1997; 19 (4): 939-45.
    • (1997) Neuron , vol.19 , Issue.4 , pp. 939-945
    • Borchelt, D.R.1    Ratovitski, T.2    van Lare, J.3    Lee, M.K.4    Gonzales, V.5    Jenkins, N.A.6
  • 62
    • 0141642240 scopus 로고    scopus 로고
    • Acetylcholinesterase induces neuronal cell loss, astrocyte hypertrophy and behavioural deficits in mammalian hippocampus
    • Chacón MA, Reyes AE, Inestrosa NC. Acetylcholinesterase induces neuronal cell loss, astrocyte hypertrophy and behavioural deficits in mammalian hippocampus. J Neurochem 2003; 87 (1): 195-204.
    • (2003) J. Neurochem. , vol.87 , Issue.1 , pp. 195-204
    • Chacón, M.A.1    Reyes, A.E.2    Inestrosa, N.C.3
  • 63
    • 4544260597 scopus 로고    scopus 로고
    • Acetylcholinesterase-Aβ complexes are more toxic than Aβ fibrils in rat hippocampus: Effect on rat β-amyloid aggregation, laminin expression, reactive astrocytosis and neuronal cell loss
    • in press
    • Reyes A, Chacón M, Morgan C, Dinamarca M, Cerpa W, Inestrosa N. Acetylcholinesterase-Aβ complexes are more toxic than Aβ fibrils in rat hippocampus: Effect on rat β-amyloid aggregation, laminin expression, reactive astrocytosis and neuronal cell loss. Am J Pathol 2003; in press.
    • (2003) Am. J. Pathol.
    • Reyes, A.1    Chacón, M.2    Morgan, C.3    Dinamarca, M.4    Cerpa, W.5    Inestrosa, N.6
  • 64
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Abeta and synaptic dysfunction
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R, et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 2003; 39 (3): 409-21.
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6
  • 65
    • 0033230623 scopus 로고    scopus 로고
    • Neuroplasticity failure in Alzheimer's disease: Bridging the gap between plaques and tangles
    • Mesulam MM. Neuroplasticity failure in Alzheimer's disease: bridging the gap between plaques and tangles. Neuron 1999; 24 (3): 521-9.
    • (1999) Neuron , vol.24 , Issue.3 , pp. 521-529
    • Mesulam, M.M.1
  • 66
    • 0036828769 scopus 로고    scopus 로고
    • Alzheimer's disease: Treatments in discovery and development
    • Citron M. Alzheimer's disease: treatments in discovery and development. Nat Neurosci 2002; 5 Suppl: 1055-7.
    • (2002) Nat. Neurosci. , vol.5 , Issue.SUPPL. , pp. 1055-1057
    • Citron, M.1
  • 67
    • 0036441486 scopus 로고    scopus 로고
    • A cell biological perspective on Alzheimer's disease
    • Annaert W, De Strooper B. A cell biological perspective on Alzheimer's disease. Annu Rev Cell Dev Biol 2002; 18: 25-51.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 25-51
    • Annaert, W.1    De Strooper, B.2
  • 68
    • 0032839878 scopus 로고    scopus 로고
    • Plaque busters: Strategies to inhibit amyloid formation in Alzheimer's disease
    • Soto C. Plaque busters: strategies to inhibit amyloid formation in Alzheimer's disease. Mol Med Today 1999; 5 (8): 343-50.
    • (1999) Mol. Med. Today , vol.5 , Issue.8 , pp. 343-350
    • Soto, C.1
  • 69
    • 0035997225 scopus 로고    scopus 로고
    • Laminin affects polymerization, depolymerization and neurotoxicity of Abeta peptide
    • Morgan C, Bugueno MP, Garrido J, Inestrosa NC. Laminin affects polymerization, depolymerization and neurotoxicity of Abeta peptide. Peptides 2002; 23 (7): 1229-40.
    • (2002) Peptides , vol.23 , Issue.7 , pp. 1229-1240
    • Morgan, C.1    Bugueno, M.P.2    Garrido, J.3    Inestrosa, N.C.4
  • 70
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide
    • Permanne B, Adessi C, Saborio GP, Fraga S, Frossard MJ, Van Dorpe J, et al. Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide. FASEB J 2002; 16 (8): 860-2.
    • (2002) FASEB J. , vol.16 , Issue.8 , pp. 860-862
    • Permanne, B.1    Adessi, C.2    Saborio, G.P.3    Fraga, S.4    Frossard, M.J.5    Van Dorpe, J.6
  • 71
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F, Cannon C, Barbour R, Burke RL, Games D, Grajeda H, et al. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med 2000; 6 (8): 916-9.
    • (2000) Nat. Med. , vol.6 , Issue.8 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.L.4    Games, D.5    Grajeda, H.6
  • 72
    • 0000676441 scopus 로고    scopus 로고
    • Companies halt first Alzheimer vaccine trial
    • Steinberg D. Companies halt first Alzheimer vaccine trial. The Scientist. 2002; 16: 22-3.
    • (2002) The Scientist , vol.16 , pp. 22-23
    • Steinberg, D.1
  • 73
    • 0041886776 scopus 로고    scopus 로고
    • Increased T cell reactivity to amyloid beta protein in older humans and patients with Alzheimer disease
    • Monsonego A, Zota V, Karni A, Krieger JI, Bar-Or A, Bitan G, et al. Increased T cell reactivity to amyloid beta protein in older humans and patients with Alzheimer disease. J Clin Invest 2003; 112 (3): 415-22.
    • (2003) J. Clin. Invest. , vol.112 , Issue.3 , pp. 415-422
    • Monsonego, A.1    Zota, V.2    Karni, A.3    Krieger, J.I.4    Bar-Or, A.5    Bitan, G.6
  • 74
    • 0035160066 scopus 로고    scopus 로고
    • A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease
    • Refolo LM, Pappolla MA, LaFrancois J, Malester B, Schmidt SD, Thomas-Bryant T, et al. A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease. Neurobiol Dis 2001; 8 (5): 890-9.
    • (2001) Neurobiol. Dis. , vol.8 , Issue.5 , pp. 890-899
    • Refolo, L.M.1    Pappolla, M.A.2    LaFrancois, J.3    Malester, B.4    Schmidt, S.D.5    Thomas-Bryant, T.6
  • 75
    • 0037103378 scopus 로고    scopus 로고
    • Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1, 2-oxazines
    • Yu QS, Zhu X, Holloway HW, Whittaker NF, Brossi A, Greig NH. Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1, 2-oxazines. J Med Chem 2002; 45 (17): 3684-91.
    • (2002) J. Med. Chem. , vol.45 , Issue.17 , pp. 3684-3691
    • Yu, Q.S.1    Zhu, X.2    Holloway, H.W.3    Whittaker, N.F.4    Brossi, A.5    Greig, N.H.6
  • 76
    • 4544379681 scopus 로고    scopus 로고
    • Structural Bases of the Interaction between Acetylcholinesterase and the Amyloid β-Peptide
    • Faculty of Biological Sciences. Santiago: Pontifica Catholic University of Chile
    • De Ferrari GV. Structural Bases of the Interaction between Acetylcholinesterase and the Amyloid β-Peptide. Faculty of Biological Sciences. Santiago: Pontifica Catholic University of Chile, 2001; pp. 135.
    • (2001) , pp. 135
    • De Ferrari, G.V.1
  • 77
    • 0037239852 scopus 로고    scopus 로고
    • Emerging beta-amyloid therapies for the treatment of Alzheimer's disease
    • Conway KA, Baxter EW, Felsenstein KM, Reitz AB. Emerging beta-amyloid therapies for the treatment of Alzheimer's disease. Curr Pharm Design 2003; 9(6): 427-47.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.6 , pp. 427-447
    • Conway, K.A.1    Baxter, E.W.2    Felsenstein, K.M.3    Reitz, A.B.4
  • 78
    • 0036235070 scopus 로고    scopus 로고
    • Design and study of piracetam-like nootropics, controversial members of the problematic class of cognition-enhancing drugs
    • Gualtieri F, Manetti D, Romanelli MN, Ghelardini C. Design and study of piracetam-like nootropics, controversial members of the problematic class of cognition-enhancing drugs. Curr Pharm Design 2002; 8(2): 125-38.
    • (2002) Curr. Pharm. Design , vol.8 , Issue.2 , pp. 125-138
    • Gualtieri, F.1    Manetti, D.2    Romanelli, M.N.3    Ghelardini, C.4
  • 79
    • 0036431821 scopus 로고    scopus 로고
    • Amyloid forming proteases: Therapeutic targets for Alzheimer's disease
    • Schimmoller F, Higaki JN, Cordell B. Amyloid forming proteases: therapeutic targets for Alzheimer's disease. Curr Pharm Design 2002; 8(28): 2521-31.
    • (2002) Curr. Pharm. Design , vol.8 , Issue.28 , pp. 2521-2531
    • Schimmoller, F.1    Higaki, J.N.2    Cordell, B.3


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