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Volumn 47, Issue 26, 2004, Pages 6490-6498

Structure-activity relationships of acetylcholinesterase noncovalent inhibitors based on a polyamine backbone. 3. Effect of replacing the inner polymethylene chain with cyclic moieties

Author keywords

[No Author keywords available]

Indexed keywords

ANILINE DERIVATIVE; CAPROCTAMINE; CHOLINESTERASE INHIBITOR; DONEPEZIL; LIGAND; MUSCARINIC M2 RECEPTOR ANTAGONIST; PHYSOSTIGMINE; PIPERIDINE DERIVATIVE; POLYAMINE DERIVATIVE; TACRINE; UNCLASSIFIED DRUG;

EID: 10644228563     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0494366     Document Type: Article
Times cited : (36)

References (30)
  • 1
    • 0037216854 scopus 로고    scopus 로고
    • Medicinal chemistry approaches for the treatment and prevention of Alzheimer's disease
    • Bachurin, S. O. Medicinal chemistry approaches for the treatment and prevention of Alzheimer's disease. Med. Res. Rev. 2003, 23, 48-88.
    • (2003) Med. Res. Rev. , vol.23 , pp. 48-88
    • Bachurin, S.O.1
  • 2
    • 0030772890 scopus 로고    scopus 로고
    • Cholinergic activity and amyloid precursor protein metabolism
    • Roberson, M. R.; Harrell, L. E. Cholinergic activity and amyloid precursor protein metabolism. Brain Res. Rev. 1997, 25, 50-69.
    • (1997) Brain Res. Rev. , vol.25 , pp. 50-69
    • Roberson, M.R.1    Harrell, L.E.2
  • 3
    • 0141483376 scopus 로고    scopus 로고
    • Current treatment for Alzheimer disease and future prospects
    • Tariot, P. N.; Federoff, H. J. Current treatment for Alzheimer disease and future prospects. Alzheimer Dis. Assoc. Disord. 2003, 17 (Suppl. 4), S105-113.
    • (2003) Alzheimer Dis. Assoc. Disord. , vol.17 , Issue.4 SUPPL.
    • Tariot, P.N.1    Federoff, H.J.2
  • 4
    • 0042020173 scopus 로고    scopus 로고
    • Treatment of Alzheimer's disease: Current status and new perspectives
    • Scarpini, E.; Scheltens, P.; Feldman, H. Treatment of Alzheimer's disease: current status and new perspectives. Lancet Neurol. 2003, 2, 539-547.
    • (2003) Lancet Neurol. , vol.2 , pp. 539-547
    • Scarpini, E.1    Scheltens, P.2    Feldman, H.3
  • 5
    • 0030767243 scopus 로고    scopus 로고
    • The cholinergic system in Alzheimer's disease
    • Kasa, P.; Rakonczay, Z.; Gulya, K. The cholinergic system in Alzheimer's disease. Prog. Neurobiol. 1997, 52, 511-535.
    • (1997) Prog. Neurobiol. , vol.52 , pp. 511-535
    • Kasa, P.1    Rakonczay, Z.2    Gulya, K.3
  • 6
    • 0029147991 scopus 로고
    • The medicinal chemistry of Alzheimer's and Alzheimer-like diseases with emphasis on the cholinergic hypothesis
    • Gualtieri, F.; Dei, S.; Manetti, D.; Romanelli, M. N.; Scapecchi, S.; Teodori, E. The medicinal chemistry of Alzheimer's and Alzheimer-like diseases with emphasis on the cholinergic hypothesis. Farmaco 1995, 50, 489-503.
    • (1995) Farmaco , vol.50 , pp. 489-503
    • Gualtieri, F.1    Dei, S.2    Manetti, D.3    Romanelli, M.N.4    Scapecchi, S.5    Teodori, E.6
  • 8
    • 0029897490 scopus 로고    scopus 로고
    • Non-classical actions of cholinesterases: Role in cellular differentiation, tumorigenesis and Alzheimer's disease
    • Small, D. H.; Michaelson, S.; Sberna, G. Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease. Neurochem. Int. 1996, 28, 453-483.
    • (1996) Neurochem. Int. , vol.28 , pp. 453-483
    • Small, D.H.1    Michaelson, S.2    Sberna, G.3
  • 9
    • 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, 294-302.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 10
    • 0347479362 scopus 로고    scopus 로고
    • Acetylcholinesterase induces the expression of the β-amyloid precursor protein in glia and activates glial cells in culture
    • von Bernhardi, R.; Ramirez, G.; De Ferrari, G. V.; Inestrosa, N. C. Acetylcholinesterase induces the expression of the β-amyloid precursor protein in glia and activates glial cells in culture. Neurobiol. Dis. 2003, 14, 447-457.
    • (2003) Neurobiol. Dis. , vol.14 , pp. 447-457
    • Von Bernhardi, R.1    Ramirez, G.2    De Ferrari, G.V.3    Inestrosa, N.C.4
  • 11
    • 0038618612 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes beta-amyloid plaques in cerebral cortex
    • Rees, T.; Hammond, P. I.; Soreq, H.; Younkin, S.; Brimijoin, S. Acetylcholinesterase promotes beta-amyloid plaques in cerebral cortex. Neurobiol. Aging 2003, 24, 777-787.
    • (2003) Neurobiol. Aging , vol.24 , pp. 777-787
    • Rees, T.1    Hammond, P.I.2    Soreq, H.3    Younkin, S.4    Brimijoin, S.5
  • 12
    • 0032080309 scopus 로고    scopus 로고
    • Stable complexes involving acetylcholinesterase and amyloid-β peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
    • Alvarez, A.; Alarcon, R.; Opazo, C.; Campos, E. O.; Munoz, F. J.; Calderon, F. H.; Dajas, F.; Gentry, M. K.; Doctor, B. P.; De Mello, F. G.; Inestrosa, N. C. Stable complexes involving acetylcholinesterase and amyloid-β peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J. Neurosci. Res. 1998, 18, 3213-3223.
    • (1998) J. Neurosci. Res. , vol.18 , pp. 3213-3223
    • Alvarez, A.1    Alarcon, R.2    Opazo, C.3    Campos, E.O.4    Munoz, F.J.5    Calderon, F.H.6    Dajas, F.7    Gentry, M.K.8    Doctor, B.P.9    De Mello, F.G.10    Inestrosa, N.C.11
  • 13
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation
    • De Ferrari, G. V.; Canales, M. A.; Shin, I.; Weiner, L. M.; Silman, I.; Inestrosa, N. C. A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry 2001, 40, 10447-10457.
    • (2001) Biochemistry , vol.40 , 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
    • 0024352019 scopus 로고
    • Comparison of butyrylcholinesterase and acetylcholinesterase
    • Chatonnet, A.; Lockridge, O. Comparison of butyrylcholinesterase and acetylcholinesterase. Biochem. J. 1989, 260, 625-634.
    • (1989) Biochem. J. , vol.260 , pp. 625-634
    • Chatonnet, A.1    Lockridge, O.2
  • 15
    • 0027514286 scopus 로고
    • Colocalization of cholinesterases with beta amyloid protein in aged and Alzheimer's brains
    • Moran, M. A.; Mufson, E. J.; Gomez-Ramos, P. Colocalization of cholinesterases with beta amyloid protein in aged and Alzheimer's brains. Acta Neuropathol. 1993, 85, 362-369.
    • (1993) Acta Neuropathol. , vol.85 , pp. 362-369
    • Moran, M.A.1    Mufson, E.J.2    Gomez-Ramos, P.3
  • 16
    • 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, N. C.; Alvarez, A.; Perez, C. A.; Moreno, R. D.; Vicente, M.; Linker, C.; Casanueva, O. I.; Soto, C.; Garrido, J. Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 1996, 16, 881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 17
    • 0027515387 scopus 로고
    • Structure and functions of acetylcholinesterase and butyrylcholinesterase
    • Massoulie, J.; Sussman, J.; Bon, S.; Silman, I. Structure and functions of acetylcholinesterase and butyrylcholinesterase. Prog. Brain Res. 1993, 98, 139-146.
    • (1993) Prog. Brain Res. , vol.98 , pp. 139-146
    • Massoulie, J.1    Sussman, J.2    Bon, S.3    Silman, I.4
  • 21
    • 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.; Angeli, P.; Banzi, R.; Minarini, A.; Recanatini, M.; Melchiorre, C. 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, 954-966.
    • (2003) J. Med. Chem. , vol.46 , pp. 954-966
    • Tumiatti, V.1    Rosini, M.2    Bartolini, M.3    Cavalli, A.4    Marucci, G.5    Andrisano, V.6    Angeli, P.7    Banzi, R.8    Minarini, A.9    Recanatini, M.10    Melchiorre, C.11
  • 23
    • 0027945826 scopus 로고
    • Design, synthesis, and biological activity of methoctramine-related tetraamines bearing an 11-acetyl-5,11-dihydro-6H-pyrido[2,3-b][1,4] benzodiazepin-6-one moiety: Structural requirements for optimum occupancy of muscarinic receptor subtypes as revealed by symmetrical and unsymmetrical polyamines
    • Minarini, A.; Bolognesi, M. L.; Budriesi, R.; Canossa, M.; Chiarini, A.; Spampinato, S.; Melchiorre, C. Design, synthesis, and biological activity of methoctramine-related tetraamines bearing an 11-acetyl-5,11-dihydro-6H-pyrido[2, 3-b][1,4]benzodiazepin-6-one moiety: structural requirements for optimum occupancy of muscarinic receptor subtypes as revealed by symmetrical and unsymmetrical polyamines. J. Med. Chem. 1994, 37, 3363-3372.
    • (1994) J. Med. Chem. , vol.37 , pp. 3363-3372
    • Minarini, A.1    Bolognesi, M.L.2    Budriesi, R.3    Canossa, M.4    Chiarini, A.5    Spampinato, S.6    Melchiorre, C.7
  • 24
    • 73649209211 scopus 로고
    • Cumulative dose-response curves. II. Technique for the making of dose-response curves in isolated organs and the evaluation of drug parameters
    • Van Rossum, J. M. Cumulative dose-response curves. II. Technique for the making of dose-response curves in isolated organs and the evaluation of drug parameters. Arch. Int. Pharmacodyn. Ther. 1963, 143, 299-330.
    • (1963) Arch. Int. Pharmacodyn. Ther. , vol.143 , pp. 299-330
    • Van Rossum, J.M.1
  • 25
    • 0033043305 scopus 로고    scopus 로고
    • A comparative study in rats of the in vitro and in vivo pharmacology of the acetylcholinesterase inhibitors tacrine, donepezil and NXX-066
    • Snape, M. F.; Misra, A.; Murray, T. K.; De Souza, R. J.; Williams, J. L.; Cross, A. J.; Green, A. R. A comparative study in rats of the in vitro and in vivo pharmacology of the acetylcholinesterase inhibitors tacrine, donepezil and NXX-066. Neuropharmacology 1999, 38, 181-193.
    • (1999) Neuropharmacology , vol.38 , pp. 181-193
    • Snape, M.F.1    Misra, A.2    Murray, T.K.3    De Souza, R.J.4    Williams, J.L.5    Cross, A.J.6    Green, A.R.7
  • 26
    • 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 β-amyloid aggregation: A dual function lead for Alzheimer's disease therapy
    • Piazzi, L.; Rampa, A.; Bisi, A.; Gobbi, S.; Belluti, F.; Cavalli, A.; Bartolini, M.; Andrisano, V.; Valenti, P.; Recanatini, M. 3-(4-[[Benzyl(methyl) amino]methyl]phenyl)-6,7-dimethoxy-2H-2-chromenone (AP2238) inhibits both acetylcholinesterase and acetylcholinesterase-induced β-amyloid aggregation: a dual function lead for Alzheimer's disease therapy. J. Med. Chem. 2003, 46, 2279-2282.
    • (2003) J. Med. Chem. , vol.46 , pp. 2279-2282
    • Piazzi, L.1    Rampa, A.2    Bisi, A.3    Gobbi, S.4    Belluti, F.5    Cavalli, A.6    Bartolini, M.7    Andrisano, V.8    Valenti, P.9    Recanatini, M.10
  • 27
    • 0030276257 scopus 로고    scopus 로고
    • Acetylcholinesterase is a senile plaque component that promotes assembly of amyloid β-peptide into Alzheimer's filaments
    • Inestrosa, N. C.; Alvarez, A.; Calderon, F. Acetylcholinesterase is a senile plaque component that promotes assembly of amyloid β-peptide into Alzheimer's filaments. Mol. Psychiatry 1996, 1, 359-361.
    • (1996) Mol. Psychiatry , vol.1 , pp. 359-361
    • Inestrosa, N.C.1    Alvarez, A.2    Calderon, F.3
  • 28
    • 0037298750 scopus 로고    scopus 로고
    • β-Amyloid aggregation induced by human acetylcholinesterase: Inhibition studies
    • Bartolini, M.; Bertucci, C.; Cavrini, V.; Andrisano, V. β-Amyloid aggregation induced by human acetylcholinesterase: inhibition studies. Biochem. Pharmacol. 2003, 65, 407-416.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 407-416
    • Bartolini, M.1    Bertucci, C.2    Cavrini, V.3    Andrisano, V.4
  • 29
    • 0035727527 scopus 로고    scopus 로고
    • Selective inhibitors of butyrylcholinesterase: A valid alternative for therapy of Alzheimer's disease?
    • Giacobini, E. Selective inhibitors of butyrylcholinesterase: a valid alternative for therapy of Alzheimer's disease? Drugs Aging 2001, 18, 891-898.
    • (2001) Drugs Aging , vol.18 , pp. 891-898
    • Giacobini, E.1


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