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Volumn 3, Issue 1, 2008, Pages 65-81

Huprines for alzheimer's disease drug development

Author keywords

13 amidohuprine; Acetylcholinesterase inhibitor; Alzheimer's disease; Huprine; Huprine tacrine heterodimer; Neuroprotective agent; Prion protein antiaggregating agent

Indexed keywords

13 AMIDOHUPRINE DERIVATIVE; AMYLOID BETA PROTEIN; CHOLINESTERASE INHIBITOR; DONEPEZIL; GALANTAMINE; HETERODIMER; HUPERZINE A; HUPRINE DERIVATIVE; HUPRINE X; HUPRINE Y; MEMANTINE; NOOTROPIC AGENT; RIVASTIGMINE; TACRINE; UNCLASSIFIED DRUG;

EID: 38849116319     PISSN: 17460441     EISSN: None     Source Type: Journal    
DOI: 10.1517/17460441.3.1.65     Document Type: Review
Times cited : (20)

References (97)
  • 2
    • 33745893779 scopus 로고    scopus 로고
    • Alzheimer disease: Progress or profit?
    • Mount C, Dowton C. Alzheimer disease: progress or profit? Nat Med 2006;12:780-4
    • (2006) Nat Med , vol.12 , pp. 780-784
    • Mount, C.1    Dowton, C.2
  • 3
    • 31144450053 scopus 로고    scopus 로고
    • Current pharmacotherapy for Alzheimer's disease
    • Lleó A, Greenberg SM, Growdon JH. Current pharmacotherapy for Alzheimer's disease. Ann Rev Med 2006;57:513-33
    • (2006) Ann Rev Med , vol.57 , pp. 513-533
    • Lleó, A.1    Greenberg, S.M.2    Growdon, J.H.3
  • 4
    • 0017360731 scopus 로고
    • Necropsy evidence of central cholinergic deficits in senile dementia
    • Perry EK, Perry RH, Blessed G, Tomlinson BE. Necropsy evidence of central cholinergic deficits in senile dementia. Lancet 1977:189
    • (1977) Lancet , pp. 189
    • Perry, E.K.1    Perry, R.H.2    Blessed, G.3    Tomlinson, B.E.4
  • 5
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus RT, Dean RL III, Beer B, Lippa AS. The cholinergic hypothesis of geriatric memory dysfunction. Science 1982;217:408-17
    • (1982) Science , vol.217 , pp. 408-417
    • Bartus, R.T.1    Dean III, R.L.2    Beer, B.3    Lippa, A.S.4
  • 6
    • 0019410162 scopus 로고
    • Alzheimer disease: Evidence for selective loss of cholinergic neurons in the nucleus basalis
    • Whitehouse PJ, Price DL, Clark AW, et al. Alzheimer disease: evidence for selective loss of cholinergic neurons in the nucleus basalis. Ann Neurol 1981;10:122-6
    • (1981) Ann Neurol , vol.10 , pp. 122-126
    • Whitehouse, P.J.1    Price, D.L.2    Clark, A.W.3
  • 8
    • 34248326079 scopus 로고    scopus 로고
    • Castellani RJ, Zhu X, Lee H-G, et al. Neuropathology and treatment of Alzheimer disease: did we lose the forest for the trees? Expert Rev Neurother 2007;7:473-85
    • Castellani RJ, Zhu X, Lee H-G, et al. Neuropathology and treatment of Alzheimer disease: did we lose the forest for the trees? Expert Rev Neurother 2007;7:473-85
  • 10
    • 33645846948 scopus 로고    scopus 로고
    • A partial failure of membrane protein turnover may cause Alzheimer's disease: A new hypothesis
    • Sambamurti K, Suram A, Venugopal C, et al. A partial failure of membrane protein turnover may cause Alzheimer's disease: a new hypothesis. Curr Alzheimer Res 2006;81-91
    • (2006) Curr Alzheimer Res , pp. 81-91
    • Sambamurti, K.1    Suram, A.2    Venugopal, C.3
  • 11
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's diasese: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's diasese: progress and problems on the road to therapeutics. Science 2002;297:353-6
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 12
    • 33645829653 scopus 로고    scopus 로고
    • Hardy J. Has the amyloid cascade hypothesis for Alzheimer's disease been proved? Curr Alzheimer Res 2006;3:71-3
    • Hardy J. Has the amyloid cascade hypothesis for Alzheimer's disease been proved? Curr Alzheimer Res 2006;3:71-3
  • 13
    • 34247876141 scopus 로고    scopus 로고
    • Therapies for Alzheimer's disease
    • Melnikova I. Therapies for Alzheimer's disease. Nat Rev Drug Discov 2007;6:341-2
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 341-342
    • Melnikova, I.1
  • 14
    • 33644853531 scopus 로고    scopus 로고
    • Metabolism of amyloid β peptide and pathogenesis of Alzheimer's disease. Towards presymptomatic diagnosis, prevention and therapy
    • Saido TC, Iwata N. Metabolism of amyloid β peptide and pathogenesis of Alzheimer's disease. Towards presymptomatic diagnosis, prevention and therapy. Neurosci Res 2006;54:235-53
    • (2006) Neurosci Res , vol.54 , pp. 235-253
    • Saido, T.C.1    Iwata, N.2
  • 15
    • 33645728523 scopus 로고    scopus 로고
    • Neurodegenerative diseases: New concepts of pathogenesis and their therapeutic implications
    • Skovronsky DM, Lee VM-Y, Trojanowski JQ. Neurodegenerative diseases: new concepts of pathogenesis and their therapeutic implications. Ann Rev Pathol Mech Dis 2006;1:151-70
    • (2006) Ann Rev Pathol Mech Dis , vol.1 , pp. 151-170
    • Skovronsky, D.M.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 17
    • 15944423975 scopus 로고    scopus 로고
    • Acetylcholinergic neurotransmission and the β-amyloid cascade: Implications for Alzheimer's disease
    • Verhoeff NPLG. Acetylcholinergic neurotransmission and the β-amyloid cascade: implications for Alzheimer's disease. Expert Rev Neurother 2005;5:277-84
    • (2005) Expert Rev Neurother , vol.5 , pp. 277-284
    • Verhoeff, N.P.L.G.1
  • 18
    • 4544295150 scopus 로고    scopus 로고
    • Rationale for the development of cholinesterase inhibitors as anti-Alzheimer agents
    • Lahiri DK, Rogers JT, Greig NH, Sambamurti K. Rationale for the development of cholinesterase inhibitors as anti-Alzheimer agents. Curr Pharm Des 2004;10:3111-19
    • (2004) Curr Pharm Des , vol.10 , pp. 3111-3119
    • Lahiri, D.K.1    Rogers, J.T.2    Greig, N.H.3    Sambamurti, K.4
  • 19
    • 33748117752 scopus 로고    scopus 로고
    • Mechanisms behind the neuroprotective actions of cholinesterase inhibitors in Alzheimer disease
    • Nordberg A. Mechanisms behind the neuroprotective actions of cholinesterase inhibitors in Alzheimer disease. Alzheimer Dis Assoc Disord 2006;20(Suppl 1):S12-S18
    • (2006) Alzheimer Dis Assoc Disord , vol.20 , Issue.SUPPL. 1
    • Nordberg, A.1
  • 20
    • 4544291755 scopus 로고    scopus 로고
    • Overview of the current and novel drugs for Alzheimer's disease with particular reference to anti-cholinesterase compounds
    • Colombres M, Sagal JP, Inestrosa NC. Overview of the current and novel drugs for Alzheimer's disease with particular reference to anti-cholinesterase compounds. Curr Pharm Des 2004;10:3121-30
    • (2004) Curr Pharm Des , vol.10 , pp. 3121-3130
    • Colombres, M.1    Sagal, J.P.2    Inestrosa, N.C.3
  • 21
    • 33748094425 scopus 로고    scopus 로고
    • Preclinical evidence of neuroprotection by cholinesterase inhibitors
    • Akaike A. Preclinical evidence of neuroprotection by cholinesterase inhibitors. Alzheimer Dis Assoc Disord 2006;20(Suppl 1):S8-S11
    • (2006) Alzheimer Dis Assoc Disord , vol.20 , Issue.SUPPL. 1
    • Akaike, A.1
  • 22
    • 33748096585 scopus 로고    scopus 로고
    • What constitutes clinical evidence for neuroprotection in Alzheimer disease. Support for the cholinesterase inhibitors?
    • Mori E, Hashimoto M, Krishnan K, Doraiswamy PM. What constitutes clinical evidence for neuroprotection in Alzheimer disease. Support for the cholinesterase inhibitors? Alzheimer Dis Assoc Disord 2006;20(Suppl 1):S19-S26
    • (2006) Alzheimer Dis Assoc Disord , vol.20 , Issue.SUPPL. 1
    • Mori, E.1    Hashimoto, M.2    Krishnan, K.3    Doraiswamy, P.M.4
  • 24
    • 16844372347 scopus 로고    scopus 로고
    • Does donepezil treatment slow the progression of hippocampal atrophy in patients with Alzheimer's disease?
    • Hashimoto M, Kazui H, Matsumoto K, et al. Does donepezil treatment slow the progression of hippocampal atrophy in patients with Alzheimer's disease? Am J Psychiatry 2005;162:676-82
    • (2005) Am J Psychiatry , vol.162 , pp. 676-682
    • Hashimoto, M.1    Kazui, H.2    Matsumoto, K.3
  • 25
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, et al. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 1991;253:872-9
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3
  • 27
    • 0034092376 scopus 로고    scopus 로고
    • Synthesis of tacrine analogues and their structure-activity relationships
    • Proctor GR, Harvey AL. Synthesis of tacrine analogues and their structure-activity relationships. Curr Med Chem 2000;7:295-302
    • (2000) Curr Med Chem , vol.7 , pp. 295-302
    • Proctor, G.R.1    Harvey, A.L.2
  • 28
    • 0345034775 scopus 로고    scopus 로고
    • Chemistry, pharmacology and clinical efficacy of the Chinese nootropic agent huperzine A
    • Kozikowski AP, Tückmantel W. Chemistry, pharmacology and clinical efficacy of the Chinese nootropic agent huperzine A. Acc Chem Res 1999;32:641-50
    • (1999) Acc Chem Res , vol.32 , pp. 641-650
    • Kozikowski, A.P.1    Tückmantel, W.2
  • 29
    • 0032771261 scopus 로고    scopus 로고
    • Huperzine A: A novel acetylcholinesterase inhibitor
    • Tang XC, He XC, Bai DL. Huperzine A: a novel acetylcholinesterase inhibitor. Drugs Future 1999;24:647-63
    • (1999) Drugs Future , vol.24 , pp. 647-663
    • Tang, X.C.1    He, X.C.2    Bai, D.L.3
  • 30
    • 0026774930 scopus 로고
    • The synthesis and in vitro acetylcholinesterase and butyrylcholinesterase inhibitory activity of tacrine (Cognex) derivatives
    • Gregor VE, Emmerling MR, Lee C, Moore CJ. The synthesis and in vitro acetylcholinesterase and butyrylcholinesterase inhibitory activity of tacrine (Cognex) derivatives. Bioorg Med Chem Lett 1992;2:861-4
    • (1992) Bioorg Med Chem Lett , vol.2 , pp. 861-864
    • Gregor, V.E.1    Emmerling, M.R.2    Lee, C.3    Moore, C.J.4
  • 31
    • 0031015343 scopus 로고    scopus 로고
    • 3D structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A
    • Raves ML, Harel M, Pang Y-P, et al. 3D structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A. Nat Struct Biol 1997;4:57-63
    • (1997) Nat Struct Biol , vol.4 , pp. 57-63
    • Raves, M.L.1    Harel, M.2    Pang, Y.-P.3
  • 32
    • 0027368530 scopus 로고
    • Quaternary ligand binding to aromatic residues in the active-site gorge of acerylcholinesterase
    • Harel M, Schalk I, Ehret-Sabatier L, et al. Quaternary ligand binding to aromatic residues in the active-site gorge of acerylcholinesterase. Proc Natl Acad Sci USA 1993;90:9031-5
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9031-9035
    • Harel, M.1    Schalk, I.2    Ehret-Sabatier, L.3
  • 33
    • 0029817834 scopus 로고    scopus 로고
    • Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase
    • Pang Y-P, Quiram P, Jelacic T, et al. Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. J Biol Chem 1996;271:23646-9
    • (1996) J Biol Chem , vol.271 , pp. 23646-23649
    • Pang, Y.-P.1    Quiram, P.2    Jelacic, T.3
  • 34
    • 33748727771 scopus 로고    scopus 로고
    • Synthesis of alkylene linked bis-THA and alkylene linked benzyl-THA as highly potent and selective inhibitors and molecular probes of acetylcholinesterase
    • Pang Y-P, Hong F, Quiram P, et al. Synthesis of alkylene linked bis-THA and alkylene linked benzyl-THA as highly potent and selective inhibitors and molecular probes of acetylcholinesterase. J Chem Soc Perkin Trans I 1997;171-6
    • (1997) J Chem Soc Perkin Trans I , pp. 171-176
    • Pang, Y.-P.1    Hong, F.2    Quiram, P.3
  • 35
    • 0033044911 scopus 로고    scopus 로고
    • Evaluation of short-tether bis-THA AChE inhibitors. A further test of the dual binding site hypothesis
    • Carlier PR, Han YF, Chow ES-H, et al. Evaluation of short-tether bis-THA AChE inhibitors. A further test of the dual binding site hypothesis. Bioorg Med Chem 1999;7:351-7
    • (1999) Bioorg Med Chem , vol.7 , pp. 351-357
    • Carlier, P.R.1    Han, Y.F.2    Chow, E.S.-H.3
  • 36
    • 15844422678 scopus 로고    scopus 로고
    • The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase
    • Harel M, Quinn DM, Nair HK, et al. The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. J Am Chem Soc 1996;118:2340-6
    • (1996) J Am Chem Soc , vol.118 , pp. 2340-2346
    • Harel, M.1    Quinn, D.M.2    Nair, H.K.3
  • 37
    • 0035959984 scopus 로고    scopus 로고
    • A structure-based design approach to the development of novel, reversible AChE inhibitors
    • Doucet-Personeni C, Bentley PD, Fletcher RJ, et al. A structure-based design approach to the development of novel, reversible AChE inhibitors. J Med Chem 2001;44:3203-15
    • (2001) J Med Chem , vol.44 , pp. 3203-3215
    • Doucet-Personeni, C.1    Bentley, P.D.2    Fletcher, R.J.3
  • 38
    • 0037022789 scopus 로고    scopus 로고
    • 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 Å resolution: Kinetic and molecular dynamics correlates
    • Dvir H, Wong DM, Harel M, et al. 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 Å resolution: kinetic and molecular dynamics correlates. Biochemistry 2002;41:2970-81
    • (2002) Biochemistry , vol.41 , pp. 2970-2981
    • Dvir, H.1    Wong, D.M.2    Harel, M.3
  • 39
    • 0029945599 scopus 로고    scopus 로고
    • Camps P, El Achab R, Font-Bardia M, et al. Easy synthesis of 7-alkylbicyclo[3.3.1] non-6-en-3-ones by silical gel-promoted fragmentation of 3-alkyl-2-oxaadamant-1-yl mesylates. Tetrahedron 1996;52:5867-80
    • Camps P, El Achab R, Font-Bardia M, et al. Easy synthesis of 7-alkylbicyclo[3.3.1] non-6-en-3-ones by silical gel-promoted fragmentation of 3-alkyl-2-oxaadamant-1-yl mesylates. Tetrahedron 1996;52:5867-80
  • 40
    • 0032054003 scopus 로고    scopus 로고
    • Synthesis and evaluation of tacrine-huperzine A hybrids as acetylcholinesterase inhibitors of potential interest for the treatment of Alzheimer's disease
    • Badia A, Baños JE, Camps P, et al. Synthesis and evaluation of tacrine-huperzine A hybrids as acetylcholinesterase inhibitors of potential interest for the treatment of Alzheimer's disease. Bioorg Med Chem 1998;6:427-40
    • (1998) Bioorg Med Chem , vol.6 , pp. 427-440
    • Badia, A.1    Baños, J.E.2    Camps, P.3
  • 41
    • 0033538625 scopus 로고    scopus 로고
    • Synthesis of an 11-unsubstituted analogue of (±)-huperzine A
    • Camps P, Contreras J, Morral J, et al. Synthesis of an 11-unsubstituted analogue of (±)-huperzine A. Tetrahedron 1999;55:8481-96
    • (1999) Tetrahedron , vol.55 , pp. 8481-8496
    • Camps, P.1    Contreras, J.2    Morral, J.3
  • 42
    • 0034705526 scopus 로고    scopus 로고
    • New syntheses of rac-huperzine A and its rac-7-ethyl-derivative. Evaluation of several huperzine A analogues as acetylcholinesterase inhibitors
    • Camps P, Contreras J, El Achab R, et al. New syntheses of rac-huperzine A and its rac-7-ethyl-derivative. Evaluation of several huperzine A analogues as acetylcholinesterase inhibitors. Tetrahedron 2000;56:4541-53
    • (2000) Tetrahedron , vol.56 , pp. 4541-4553
    • Camps, P.1    Contreras, J.2    El Achab, R.3
  • 43
    • 0035411605 scopus 로고    scopus 로고
    • Tacrine-huperzine A hybrids (huprines): A new class of highly potent and selective acetylcholinesterase inhibitors of interest for the treatment of Alzheimer's disease
    • Camps P, Muñoz-Torrero D. Tacrine-huperzine A hybrids (huprines): a new class of highly potent and selective acetylcholinesterase inhibitors of interest for the treatment of Alzheimer's disease. Mini Rev Med Chem 2001;1:163-74
    • (2001) Mini Rev Med Chem , vol.1 , pp. 163-174
    • Camps, P.1    Muñoz-Torrero, D.2
  • 44
    • 0035924211 scopus 로고    scopus 로고
    • Synthesis, in vitro pharmacology, and molecular modeling of syn-huprines as acetylcholinesterase inhibitors
    • Camps P, Gómez E, Muñoz-Torrero D, et al. Synthesis, in vitro pharmacology, and molecular modeling of syn-huprines as acetylcholinesterase inhibitors. J Med Chem 2001;44:4733-6
    • (2001) J Med Chem , vol.44 , pp. 4733-4736
    • Camps, P.1    Gómez, E.2    Muñoz-Torrero, D.3
  • 45
    • 13044253491 scopus 로고    scopus 로고
    • Synthesis, in vitro pharmacology, and molecular modeling of very potent tacrine-huperzine A hybrids as acetylcholinesterase inhibitors of potential interest for the treatment of Alzheimer's disease
    • Camps P, El Achab R, Görbig DM, et al. Synthesis, in vitro pharmacology, and molecular modeling of very potent tacrine-huperzine A hybrids as acetylcholinesterase inhibitors of potential interest for the treatment of Alzheimer's disease. J Med Chem 1999;42:3227-42
    • (1999) J Med Chem , vol.42 , pp. 3227-3242
    • Camps, P.1    El Achab, R.2    Görbig, D.M.3
  • 46
    • 0016724999 scopus 로고
    • A hydrophobic binding site in acetylcholinesterase
    • Steinberg GM, Mednick ML, Maddox J, et al. A hydrophobic binding site in acetylcholinesterase. J Med Chem 1975;18:1056-61
    • (1975) J Med Chem , vol.18 , pp. 1056-1061
    • Steinberg, G.M.1    Mednick, M.L.2    Maddox, J.3
  • 47
    • 0034736034 scopus 로고    scopus 로고
    • New tacrine-huperzine A hybrids (huprines): Highly potent tight-binding acetylcholinesterase inhibitors of interest for the treatment of Alzheimer's disease
    • Camps P, El Achab R, Morral J, et al. New tacrine-huperzine A hybrids (huprines): highly potent tight-binding acetylcholinesterase inhibitors of interest for the treatment of Alzheimer's disease. J Med Chem 2000;43:4657-66
    • (2000) J Med Chem , vol.43 , pp. 4657-4666
    • Camps, P.1    El Achab, R.2    Morral, J.3
  • 48
    • 0035833105 scopus 로고    scopus 로고
    • Novel and potent tacrine-related hetero- and homobivalent ligands for acetylcholinesterase and butyrylcholinesterase
    • Savini L, Campiani G, Gaeta A, et al. Novel and potent tacrine-related hetero- and homobivalent ligands for acetylcholinesterase and butyrylcholinesterase. Bioorg Med Chem Lett 2001;11:1779-82
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 1779-1782
    • Savini, L.1    Campiani, G.2    Gaeta, A.3
  • 49
    • 0032513139 scopus 로고    scopus 로고
    • Enantioselective synthesis of tacrine-huperzine A hybrids. Preparative chiral MPLC separation of their racemic mixtures and absolute configuration assignments by X-ray diffraction analysis
    • Camps P, Contreras J, Font-Bardia M, et al. Enantioselective synthesis of tacrine-huperzine A hybrids. Preparative chiral MPLC separation of their racemic mixtures and absolute configuration assignments by X-ray diffraction analysis. Tetrahedron: Asymmetry 1998;9:835-49
    • (1998) Tetrahedron: Asymmetry , vol.9 , pp. 835-849
    • Camps, P.1    Contreras, J.2    Font-Bardia, M.3
  • 50
    • 0033966913 scopus 로고    scopus 로고
    • Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer's disease
    • Camps P, Cusack B, Mallender WD, et al. Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer's disease. Mol Pharmacol 2000;57:409-17
    • (2000) Mol Pharmacol , vol.57 , pp. 409-417
    • Camps, P.1    Cusack, B.2    Mallender, W.D.3
  • 51
    • 0037401596 scopus 로고    scopus 로고
    • Alcalá MM, Vivas NM, Hospital S, et al. Characterisation of the anticholinesterase activity of two new tacrine-huperzine A hybrids. Neuropharmacology 2003;44:749-55
    • Alcalá MM, Vivas NM, Hospital S, et al. Characterisation of the anticholinesterase activity of two new tacrine-huperzine A hybrids. Neuropharmacology 2003;44:749-55
  • 52
    • 30144437522 scopus 로고    scopus 로고
    • Progress in studies of huperzine A, a natural cholinesterase inhibitor from Chinese herbal medicine
    • Wang R, Yan H, Tang X-C. Progress in studies of huperzine A, a natural cholinesterase inhibitor from Chinese herbal medicine. Acta Pharmacol Sin 2006;27:1-26
    • (2006) Acta Pharmacol Sin , vol.27 , pp. 1-26
    • Wang, R.1    Yan, H.2    Tang, X.-C.3
  • 53
    • 0023755495 scopus 로고    scopus 로고
    • Perry EK, Smith CJ, Court JA, et al. Interaction of 9-amino- 1,2,3,4-tetrahydroaminoacridine (THA) with human cortical nicotinic and muscarinic receptor binding in vitro. Neurosci Lett 1988;91:211-16
    • Perry EK, Smith CJ, Court JA, et al. Interaction of 9-amino- 1,2,3,4-tetrahydroaminoacridine (THA) with human cortical nicotinic and muscarinic receptor binding in vitro. Neurosci Lett 1988;91:211-16
  • 54
    • 0032569990 scopus 로고    scopus 로고
    • The secretion of amyloid beta-peptides is inhibited in the tacrine-treated human neuroblastoma cells
    • Lahiri DK, Farlow MR, Sambamurti K. The secretion of amyloid beta-peptides is inhibited in the tacrine-treated human neuroblastoma cells. Mol Brain Res 1998;62:131-40
    • (1998) Mol Brain Res , vol.62 , pp. 131-140
    • Lahiri, D.K.1    Farlow, M.R.2    Sambamurti, K.3
  • 55
    • 0024460902 scopus 로고
    • Effect of huperzine A, a new cholinesterase inhibitor, on the central cholinergic system of the rat
    • Tang XC, De Sarno P, Sugaya K, Giacobini E. Effect of huperzine A, a new cholinesterase inhibitor, on the central cholinergic system of the rat. J Neurosci Res 1989;24:276-85
    • (1989) J Neurosci Res , vol.24 , pp. 276-285
    • Tang, X.C.1    De Sarno, P.2    Sugaya, K.3    Giacobini, E.4
  • 56
    • 1842713364 scopus 로고    scopus 로고
    • Huperzine A enhances the level of secretory amyloid precursor protein and protein kinase C-α in intracerebroventricular β-amyloid (1-40) infused rats and human embryonic kidney 293 Swedish mutant cells
    • Zhang HY, Yan H, Tang XC. Huperzine A enhances the level of secretory amyloid precursor protein and protein kinase C-α in intracerebroventricular β-amyloid (1-40) infused rats and human embryonic kidney 293 Swedish mutant cells. Neurosci Lett 2004;360:21-4
    • (2004) Neurosci Lett , vol.360 , pp. 21-24
    • Zhang, H.Y.1    Yan, H.2    Tang, X.C.3
  • 57
    • 0037036219 scopus 로고    scopus 로고
    • Interaction of a new potent anticholinesterasic compound (±)huprine X with muscarinic receptors in rat brain
    • Roman S, Vivas NM, Badia A, Clos MV. Interaction of a new potent anticholinesterasic compound (±)huprine X with muscarinic receptors in rat brain. Neurosci Lett 2002;325:103-6
    • (2002) Neurosci Lett , vol.325 , pp. 103-106
    • Roman, S.1    Vivas, N.M.2    Badia, A.3    Clos, M.V.4
  • 58
    • 17044404593 scopus 로고    scopus 로고
    • Effects of (±)-huprine Y and (±)-huprine Z, two new anticholinesterasic drugs, on muscarinic receptors
    • Alcaá MM, Maderuelo A, Vivas NM, et al. Effects of (±)-huprine Y and (±)-huprine Z, two new anticholinesterasic drugs, on muscarinic receptors. Neurosci Lett 2005; 379:106-9
    • (2005) Neurosci Lett , vol.379 , pp. 106-109
    • Alcaá, M.M.1    Maderuelo, A.2    Vivas, N.M.3
  • 59
    • 0030893633 scopus 로고    scopus 로고
    • Huperzine A, a potential therapeutic agent for dementia, reduces neuronal cell death caused by glutamate
    • Ved HS, Koenig ML, Dave JR, Doctor BP. Huperzine A, a potential therapeutic agent for dementia, reduces neuronal cell death caused by glutamate. Neuroreport 1997;8:963-8
    • (1997) Neuroreport , vol.8 , pp. 963-968
    • Ved, H.S.1    Koenig, M.L.2    Dave, J.R.3    Doctor, B.P.4
  • 61
    • 0037385750 scopus 로고    scopus 로고
    • Neuroprotective effects of (±)-huprine Y on in vitro and in vivo models of excitotoxicity damage
    • Canudas AM, Pubill D, Sureda FX, et al. Neuroprotective effects of (±)-huprine Y on in vitro and in vivo models of excitotoxicity damage. Exp Neurol 2003;180:123-30
    • (2003) Exp Neurol , vol.180 , pp. 123-130
    • Canudas, A.M.1    Pubill, D.2    Sureda, F.X.3
  • 62
    • 12844282302 scopus 로고    scopus 로고
    • Jordá EG, Verdaguer E, Jiménez A, et al. (±)-Huprine Y, (-)-huperzine A and tacrine do not show neuroprotective properties in an apoptotic model of neuronal cytoskeletal alteration. J Alzheimer Dis 2004;6:577-83
    • Jordá EG, Verdaguer E, Jiménez A, et al. (±)-Huprine Y, (-)-huperzine A and tacrine do not show neuroprotective properties in an apoptotic model of neuronal cytoskeletal alteration. J Alzheimer Dis 2004;6:577-83
  • 63
    • 0028818362 scopus 로고
    • Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides
    • Alvarez A, Bronfman F, Pérez CA, et al. Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides. Neurosci Lett 1995;201:49-52
    • (1995) Neurosci Lett , vol.201 , pp. 49-52
    • Alvarez, A.1    Bronfman, F.2    Pérez, C.A.3
  • 64
    • 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
    • Inestrosa NC, Alvarez A, Pérez CA, et al. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 1996;16:881-91
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Pérez, C.A.3
  • 65
    • 0032080309 scopus 로고    scopus 로고
    • Stable complexes involving acerylcholinesterase and amyloid-β-peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
    • Alvarez A, Alarcón R, Opazo C, et al. Stable complexes involving acerylcholinesterase and amyloid-β-peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J Neurosci 1998;18:3213-23
    • (1998) J Neurosci , vol.18 , pp. 3213-3223
    • Alvarez, A.1    Alarcón, R.2    Opazo, C.3
  • 66
    • 2442647903 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
    • Reyes AE, Chacón MA, Dinamarca MC, et al. 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 2004;164:2163-74
    • (2004) Am J Pathol , vol.164 , pp. 2163-2174
    • Reyes, A.E.1    Chacón, M.A.2    Dinamarca, M.C.3
  • 67
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation
    • De Ferrari GV, Canales MA, Shin I, et al. A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry 2001;40:10447-57
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3
  • 68
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993;90:10962-6
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3
  • 70
    • 0035708762 scopus 로고    scopus 로고
    • Spatial correlations between the vacuolation, prion protein deposits, and surviving neurons in the cerebral cortex in sporadic Creutzfeldt-Jakob disease
    • Armstrong RA, Lantos PL, Cairns NJ. Spatial correlations between the vacuolation, prion protein deposits, and surviving neurons in the cerebral cortex in sporadic Creutzfeldt-Jakob disease. Neuropathology 2001;21:266-71
    • (2001) Neuropathology , vol.21 , pp. 266-271
    • Armstrong, R.A.1    Lantos, P.L.2    Cairns, N.J.3
  • 71
    • 33744995785 scopus 로고    scopus 로고
    • Acetylcholinesterase triggers the aggregation of PrP 106-126
    • Pera M, Román S, Ratia M, et al. Acetylcholinesterase triggers the aggregation of PrP 106-126. Biochem Biophys Res Commun 2006;346:89-94
    • (2006) Biochem Biophys Res Commun , vol.346 , pp. 89-94
    • Pera, M.1    Román, S.2    Ratia, M.3
  • 72
    • 0037298750 scopus 로고    scopus 로고
    • β-Amyloid aggregation induction by human acetylcholinesterase: Inhibition studies
    • Bartolini M, Bertucci C, Cavrini V, Andrisano V. β-Amyloid aggregation induction by human acetylcholinesterase: inhibition studies. Biochem Pharmacol 2003;65:407-16.
    • (2003) Biochem Pharmacol , vol.65 , pp. 407-416
    • Bartolini, M.1    Bertucci, C.2    Cavrini, V.3    Andrisano, V.4
  • 73
    • 0141953955 scopus 로고    scopus 로고
    • Progress in clinical, pharmacological, chemical and structural biological studies of huperzine A: A drug of traditional Chinese medicine origin for the treatment of Alzheimer's disease
    • Jiang H, Luo X, Bai D. Progress in clinical, pharmacological, chemical and structural biological studies of huperzine A: a drug of traditional Chinese medicine origin for the treatment of Alzheimer's disease. Curr Med Chem 2003;10:2231-52
    • (2003) Curr Med Chem , vol.10 , pp. 2231-2252
    • Jiang, H.1    Luo, X.2    Bai, D.3
  • 74
    • 0026792979 scopus 로고
    • A controlled trial of tacrine in Alzheimer's patients
    • Farlow M, Gracon SI, Heshey LA, et al. A controlled trial of tacrine in Alzheimer's patients. JAMA 1992;268:2523-9
    • (1992) JAMA , vol.268 , pp. 2523-2529
    • Farlow, M.1    Gracon, S.I.2    Heshey, L.A.3
  • 75
    • 0027326685 scopus 로고
    • An investigation into the formation of stable, protein-reactive and cytotoxic metabolites from tacrine in vitro. Studies with human and rat liver microsomes
    • Madden S, Woolf TF, Pool WF, Park BK. An investigation into the formation of stable, protein-reactive and cytotoxic metabolites from tacrine in vitro. Studies with human and rat liver microsomes. Biochem Pharmacol 1993;46:13-20
    • (1993) Biochem Pharmacol , vol.46 , pp. 13-20
    • Madden, S.1    Woolf, T.F.2    Pool, W.F.3    Park, B.K.4
  • 76
    • 9944238750 scopus 로고    scopus 로고
    • Improving the decision-making process in structural modification of drug candidates: Reducing toxicity
    • Nassar A-EF, Kamel AM, Clarimont C. Improving the decision-making process in structural modification of drug candidates: reducing toxicity. Drug Discov Today 2004;9:1055-64
    • (2004) Drug Discov Today , vol.9 , pp. 1055-1064
    • Nassar, A.-E.F.1    Kamel, A.M.2    Clarimont, C.3
  • 77
    • 0037334851 scopus 로고    scopus 로고
    • Acute effects of huperzine A and tacrine on rat liver
    • Ma XC, Xin J, Wang HX, et al. Acute effects of huperzine A and tacrine on rat liver. Acta Pharmacol Sin 2003;24:247-50
    • (2003) Acta Pharmacol Sin , vol.24 , pp. 247-250
    • Ma, X.C.1    Xin, J.2    Wang, H.X.3
  • 78
    • 38849093150 scopus 로고    scopus 로고
    • Medichem SA. Nuevos compuestos aminopiridínicos policíclicos inhibidores de acetilcolinesterasa, procedimiento para su preparación y su utilización. ES2100129 (1995); Novel polycyclic aminopyridine compounds as acetylcholinesterase inhibitors, preparation process and use thereof. WO97/13754 (1997)
    • Medichem SA. Nuevos compuestos aminopiridínicos policíclicos inhibidores de acetilcolinesterasa, procedimiento para su preparación y su utilización. ES2100129 (1995); Novel polycyclic aminopyridine compounds as acetylcholinesterase inhibitors, preparation process and use thereof. WO97/13754 (1997)
  • 79
    • 0037015151 scopus 로고    scopus 로고
    • X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: Structural evidence for an active site rearrangement
    • Dvir H, Jiang HL, Wong DM, et al. X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement. Biochemistry 2002;41:10810-18
    • (2002) Biochemistry , vol.41 , pp. 10810-10818
    • Dvir, H.1    Jiang, H.L.2    Wong, D.M.3
  • 80
    • 0037720197 scopus 로고    scopus 로고
    • Synthesis of diastereomeric 13-amido-substituted huprines as potential high affinity acetylcholinesterase inhibitors
    • Camps P, Gómez E, Muñoz-Torrero D, et al. Synthesis of diastereomeric 13-amido-substituted huprines as potential high affinity acetylcholinesterase inhibitors. Tetrahedron 2003;59:4143-51
    • (2003) Tetrahedron , vol.59 , pp. 4143-4151
    • Camps, P.1    Gómez, E.2    Muñoz-Torrero, D.3
  • 81
    • 2542439663 scopus 로고    scopus 로고
    • Synthesis of 13-acylamino-huprines: Different behavior of diastereomeric 13-methanesulfonamido-huprines on PPA-mediated hydrolysis
    • Camps P, Gómez E, Muñoz-Torrero D. Synthesis of 13-acylamino-huprines: different behavior of diastereomeric 13-methanesulfonamido-huprines on PPA-mediated hydrolysis. Tetrahedron 2004;60:5423-31
    • (2004) Tetrahedron , vol.60 , pp. 5423-5431
    • Camps, P.1    Gómez, E.2    Muñoz-Torrero, D.3
  • 82
    • 84961981836 scopus 로고    scopus 로고
    • Binding of 13-amidohuprines to acetylcholinesterase: Exploring the ligand-induced conformational change of the Gly117-Gly118 peptide bond in the oxyanion hole
    • Camps P, Gómez E, Muñoz-Torrero D, et al. Binding of 13-amidohuprines to acetylcholinesterase: exploring the ligand-induced conformational change of the Gly117-Gly118 peptide bond in the oxyanion hole. J Med Chem 2006;49:6833-40
    • (2006) J Med Chem , vol.49 , pp. 6833-6840
    • Camps, P.1    Gómez, E.2    Muñoz-Torrero, D.3
  • 83
    • 84962422582 scopus 로고    scopus 로고
    • Origin of the catalytic power of acetylcholinesterase: Computer simulation studies
    • Fuxreiter M, Warshel A. Origin of the catalytic power of acetylcholinesterase: computer simulation studies. J Am Chem Soc 1998;120:183-94
    • (1998) J Am Chem Soc , vol.120 , pp. 183-194
    • Fuxreiter, M.1    Warshel, A.2
  • 84
    • 33644851841 scopus 로고    scopus 로고
    • Dimeric and hybrid anti-Alzheimer drug candidates
    • Muñoz-Torrero D, Camps P. Dimeric and hybrid anti-Alzheimer drug candidates. Curr Med Chem 2006;13:399-422
    • (2006) Curr Med Chem , vol.13 , pp. 399-422
    • Muñoz-Torrero, D.1    Camps, P.2
  • 85
    • 28544451677 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of dual binding site acetylcholinesterase inhibitors: New disease-modifying agents for Alzheimer's disease
    • Muñoz-Ruiz P, Rubio L, García-Palomero E, et al. Design, synthesis, and biological evaluation of dual binding site acetylcholinesterase inhibitors: new disease-modifying agents for Alzheimer's disease. J Med Chem 2005;48:7223-33
    • (2005) J Med Chem , vol.48 , pp. 7223-7233
    • Muñoz-Ruiz, P.1    Rubio, L.2    García-Palomero, E.3
  • 86
    • 12144257246 scopus 로고    scopus 로고
    • Propidium-based polyamine ligands as potent inhibitors of acetylcholinesterase and acetylcholinesterase-induced amyloid-β aggregation
    • Bolognesi ML, Andrisano V, Bartolini M, et al. Propidium-based polyamine ligands as potent inhibitors of acetylcholinesterase and acetylcholinesterase-induced amyloid-β aggregation. J Med Chem 2005;48:24-7
    • (2005) J Med Chem , vol.48 , pp. 24-27
    • Bolognesi, M.L.1    Andrisano, V.2    Bartolini, M.3
  • 87
    • 12344328416 scopus 로고    scopus 로고
    • Rational approach to discover multipotent anti-Alzheimer drugs
    • Rosini M, Andrisano V, Bartolini M, et al. Rational approach to discover multipotent anti-Alzheimer drugs. J Med Chem 2005;48:360-3
    • (2005) J Med Chem , vol.48 , pp. 360-363
    • Rosini, M.1    Andrisano, V.2    Bartolini, M.3
  • 88
    • 21244442338 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: Xanthostigmine derivatives blocking the acetylcholinesterase-induced β-amyloid aggregation
    • Belluti F, Rampa A, Piazzi L, et al. Cholinesterase inhibitors: xanthostigmine derivatives blocking the acetylcholinesterase-induced β-amyloid aggregation. J Med Chem 2005;48:4444-56
    • (2005) J Med Chem , vol.48 , pp. 4444-4456
    • Belluti, F.1    Rampa, A.2    Piazzi, L.3
  • 89
    • 34250872774 scopus 로고    scopus 로고
    • A small molecule targeting the multifactorial nature of Alzheimer's disease
    • Cavalli A, Bolognesi ML, Capsoni S, et al. A small molecule targeting the multifactorial nature of Alzheimer's disease. Angew Chem Int Ed 2007;46:3689-92
    • (2007) Angew Chem Int Ed , vol.46 , pp. 3689-3692
    • Cavalli, A.1    Bolognesi, M.L.2    Capsoni, S.3
  • 90
    • 34948904272 scopus 로고    scopus 로고
    • Novel class of quinone-bearing polyamines as multi-target-directed ligands to combat Alzheimer's disease
    • Bolognesi ML, Banzi R, Bartolini M, et al. Novel class of quinone-bearing polyamines as multi-target-directed ligands to combat Alzheimer's disease. J Med Chem 2007;50:4882-97
    • (2007) J Med Chem , vol.50 , pp. 4882-4897
    • Bolognesi, M.L.1    Banzi, R.2    Bartolini, M.3
  • 91
    • 34548133575 scopus 로고    scopus 로고
    • Extensive SAR and computational studies of 3-{4-[(benzylmethylamino)methyl] phenyl}-6,7-dimethoxy-2H-2-chromemone (AP2238) derivatives
    • Piazzi L, Cavalli A, Belluti F, et al. Extensive SAR and computational studies of 3-{4-[(benzylmethylamino)methyl] phenyl}-6,7-dimethoxy-2H-2-chromemone (AP2238) derivatives. J Med Chem 2007;50:4250-4
    • (2007) J Med Chem , vol.50 , pp. 4250-4254
    • Piazzi, L.1    Cavalli, A.2    Belluti, F.3
  • 92
    • 34548124528 scopus 로고    scopus 로고
    • 1-42 aggregation for Alzheimer's disease therapeutics
    • 1-42 aggregation for Alzheimer's disease therapeutics. Bioorg Med Chem 2007;15:6596-607
    • (2007) Bioorg Med Chem , vol.15 , pp. 6596-6607
    • Kwon, Y.E.1    Park, J.Y.2    No, K.T.3
  • 93
    • 0037161599 scopus 로고    scopus 로고
    • Homodimeric tacrine congeners as acetylcholinesterase inhibitors
    • Hu M-K, Wu L-J, Hsiao G, Yen MH. Homodimeric tacrine congeners as acetylcholinesterase inhibitors. J Med Chem 2002;45:2277-82
    • (2002) J Med Chem , vol.45 , pp. 2277-2282
    • Hu, M.-K.1    Wu, L.-J.2    Hsiao, G.3    Yen, M.H.4
  • 94
    • 31544477481 scopus 로고    scopus 로고
    • Novel tacrine-melatonin hybrids as dual-acting drugs for Alzheimer disease, with improved acetylcholinesterase inhibitory and antioxidant properties
    • Rodriguez-Franco MI, Fernández-Bachiller MI, Pérez C, et al. Novel tacrine-melatonin hybrids as dual-acting drugs for Alzheimer disease, with improved acetylcholinesterase inhibitory and antioxidant properties. J Med Chem 2006;49:459-62
    • (2006) J Med Chem , vol.49 , pp. 459-462
    • Rodriguez-Franco, M.I.1    Fernández-Bachiller, M.I.2    Pérez, C.3
  • 95
    • 15444378025 scopus 로고    scopus 로고
    • Synthesis and pharmacological evaluation of huprine-tacrine heterodimers: Subnanomolar dual binding site acetylcholinesterase inhibitors
    • Camps P, Formosa X, Muñoz-Torrero D, et al. Synthesis and pharmacological evaluation of huprine-tacrine heterodimers: subnanomolar dual binding site acetylcholinesterase inhibitors. J Med Chem 2005;48:1701-4
    • (2005) J Med Chem , vol.48 , pp. 1701-1704
    • Camps, P.1    Formosa, X.2    Muñoz-Torrero, D.3
  • 96
    • 30344485665 scopus 로고    scopus 로고
    • Targeting acetylcholinesterase and butyrylcholinesterase in dementia
    • Lane RM, Potkin SG, Enz A. Targeting acetylcholinesterase and butyrylcholinesterase in dementia. Int J Neuropsychopharmacol 2005;9:1-24
    • (2005) Int J Neuropsychopharmacol , vol.9 , pp. 1-24
    • Lane, R.M.1    Potkin, S.G.2    Enz, A.3
  • 97
    • 4043074138 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: New roles and therapeutic alternatives
    • Giacobini E. Cholinesterase inhibitors: new roles and therapeutic alternatives. Pharmacol Res 2004;50:433-40
    • (2004) Pharmacol Res , vol.50 , pp. 433-440
    • Giacobini, E.1


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