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Volumn 7, Issue 1, 2010, Pages 40-55

Towards disease-modifying treatment of Alzheimer's disease: Drugs targeting β-amyloid

Author keywords

secretase activators; amyloid; secretase inhibitors; secretase inhibitors; secretase modulators; Active immunotherapy; Alzheimer's disease; Passive immunotherapy

Indexed keywords

ALPHA SECRETASE; ALZHEIMER DISEASE VACCINE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; AZD 10; BAPINEUZUMAB; BEGACESTAT; BETA SECRETASE INHIBITOR; BMS 708163; BRYOSTATIN 1; CEVIMELINE; CTS 21166; DONEPEZIL; E 2012; EHT 0202; ELND 0005; ELND 005; GALANTAMINE; GAMMA SECRETASE INHIBITOR; HOMOTAURINE; MEMANTINE; MK 0752; MONOCLONAL ANTIBODY; N2 [2 (3,5 DIFLUOROPHENYL) 2 HYDROXYACETYL] N1 (6,7 DIHYDRO 5 METHYL 6 OXO 5H DIBENZ[B,D]AZEPIN 7 YL)ALANINAMIDE; PBT 2; PLACEBO; PROTEINASE; QS 21; RIVASTIGMINE; SEMAGACESTAT; TALSACLIDINE; TARENFLURBIL; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 77949768182     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720510790274400     Document Type: Review
Times cited : (107)

References (161)
  • 3
    • 34548591985 scopus 로고    scopus 로고
    • Alzheimer's Disease at mid century
    • Jucker M, Beyreuther K, Haas C. and Nitsch R, Eds, Springer-Verlag, Berlin Heidelberg
    • Terry RD. Alzheimer's Disease at mid century (1927-1977), in: Alzheimer: 100 Years and Beyond. (Jucker M, Beyreuther K, Haas C. and Nitsch R, Eds). Springer-Verlag, Berlin Heidelberg, 2006, pp. 58-61.
    • (2006) Alzheimer: 100 Years and Beyond , pp. 58-61
    • Terry, R.D.1
  • 4
    • 0035477333 scopus 로고    scopus 로고
    • The cell biology of Alzheimer's disease: Uncovering the secrets of secretases
    • Walter J, Kaether C, Steiner H, Haass C. The cell biology of Alzheimer's disease: uncovering the secrets of secretases. Curr Opin Neurobiol 11: 585-590 (2001).
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 585-590
    • Walter, J.1    Kaether, C.2    Steiner, H.3    Haass, C.4
  • 5
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J, Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci 12: 383-388 (1991).
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 8
    • 40449116728 scopus 로고    scopus 로고
    • Glutamatergic approaches to the treatment of cognitive and behavioural symptoms of Alzheimer's disease
    • Francis PT. Glutamatergic approaches to the treatment of cognitive and behavioural symptoms of Alzheimer's disease. Neurodegener Dis 5: 241-243 (2008).
    • (2008) Neurodegener Dis , vol.5 , pp. 241-243
    • Francis, P.T.1
  • 10
    • 33847711478 scopus 로고    scopus 로고
    • Disease-modifying therapies in Alzheimer's disease: How far have we come?
    • Hüll M, Berger M, Heneka M. Disease-modifying therapies in Alzheimer's disease: how far have we come? Drugs 66: 2075-2093 (2006).
    • (2006) Drugs , vol.66 , pp. 2075-2093
    • Hüll, M.1    Berger, M.2    Heneka, M.3
  • 11
    • 0035661483 scopus 로고    scopus 로고
    • A new therapeutic target in Alzheimer's disease treatment: Attention to butyrylcholinesterase
    • Greig NH, Utsuki T, Yu Q, Zhu X, Holloway HW, Perry T, et al. A new therapeutic target in Alzheimer's disease treatment: attention to butyrylcholinesterase. Curr Med Res Opin 17: 159-165 (2001).
    • (2001) Curr Med Res Opin , vol.17 , pp. 159-165
    • Greig, N.H.1    Utsuki, T.2    Yu, Q.3    Zhu, X.4    Holloway, H.W.5    Perry, T.6
  • 12
    • 41049111771 scopus 로고    scopus 로고
    • Effectiveness of cholinesterase inhibitors and memantine for treating dementia: Evidence review for a clinical practice guideline
    • Raina P, Santaguida P, Ismaila A, Patterson C, Cowan D, Levine M, et al. Effectiveness of cholinesterase inhibitors and memantine for treating dementia: evidence review for a clinical practice guideline. Ann Intern Med 148: 379-397 (2008).
    • (2008) Ann Intern Med , vol.148 , pp. 379-397
    • Raina, P.1    Santaguida, P.2    Ismaila, A.3    Patterson, C.4    Cowan, D.5    Levine, M.6
  • 13
    • 36849078870 scopus 로고    scopus 로고
    • Cholinesterase inhibitors in mild cognitive impairment: A systematic review of randomised trials
    • Raschetti R, Albanese E, Vanacore N, Maggini M. Cholinesterase inhibitors in mild cognitive impairment: a systematic review of randomised trials. PLoS Med 4: e338 (2007).
    • (2007) PLoS Med , vol.4
    • Raschetti, R.1    Albanese, E.2    Vanacore, N.3    Maggini, M.4
  • 14
    • 8844270149 scopus 로고    scopus 로고
    • The potential role of non-steroidal anti-inflammatory drugs in treating Alzheimer's disease
    • Imbimbo BP. The potential role of non-steroidal anti-inflammatory drugs in treating Alzheimer's disease. Expert Opin Investig Drugs 13: 1469-1481 (2004).
    • (2004) Expert Opin Investig Drugs , vol.13 , pp. 1469-1481
    • Imbimbo, B.P.1
  • 15
    • 33644499808 scopus 로고    scopus 로고
    • Estrogen-containing hormone therapy and Alzheimer's disease risk: Understanding discrepant inferences from observational and experimental research
    • Henderson VW. Estrogen-containing hormone therapy and Alzheimer's disease risk: understanding discrepant inferences from observational and experimental research. Neuroscience 138: 1031-1039 (2006).
    • (2006) Neuroscience , vol.138 , pp. 1031-1039
    • Henderson, V.W.1
  • 17
    • 18344363918 scopus 로고    scopus 로고
    • Relationship between dementia and nutrition-related factors and disorders: An overview
    • Salerno-Kennedy R, Cashman KD. Relationship between dementia and nutrition-related factors and disorders: an overview. Int J Vitam Nutr Res 75: 83-95 (2005).
    • (2005) Int J Vitam Nutr Res , vol.75 , pp. 83-95
    • Salerno-Kennedy, R.1    Cashman, K.D.2
  • 18
    • 34447261269 scopus 로고
    • Method and composition for treatment of central nervous systems disease states associated with abnormal amyloid protein
    • WO 91/16819
    • Kline EL, McMichael J. Method and composition for treatment of central nervous systems disease states associated with abnormal amyloid protein. WO 91/16819 (1991).
    • (1991)
    • Kline, E.L.1    McMichael, J.2
  • 19
    • 0030058382 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer β-amyloid peptide
    • Solomon B, Koppel R, Hanan E, Katzav T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer β-amyloid peptide. Proc Natl Acad Sci USA 93: 452-455 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 452-455
    • Solomon, B.1    Koppel, R.2    Hanan, E.3    Katzav, T.4
  • 20
    • 77649241980 scopus 로고    scopus 로고
    • Prevention and treatment of amyloidogenic disease
    • WO 99/27944
    • Schenk D. Prevention and treatment of amyloidogenic disease. WO 99/27944 (1998).
    • (1998)
    • Schenk, D.1
  • 21
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer-diseaselike pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W, Gordon G, Grajeda H, Guido T, et al. Immunization with amyloid-β attenuates Alzheimer-diseaselike pathology in the PDAPP mouse. Nature 400: 173-177 (1999).
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5    Guido, T.6
  • 22
    • 48949085739 scopus 로고    scopus 로고
    • Amyloid-β immunisation for Alzheimer's disease
    • Wisniewski T, Konietzko U. Amyloid-β immunisation for Alzheimer's disease. Lancet Neurol 7: 805-811 (2008).
    • (2008) Lancet Neurol , vol.7 , pp. 805-811
    • Wisniewski, T.1    Konietzko, U.2
  • 23
    • 33846537923 scopus 로고    scopus 로고
    • Amyloid-Based interventions in Alzheimer's disease
    • Kennedy GJ, Golde TE, Tariot PN, Cummings JL. Amyloid-Based interventions in Alzheimer's disease. CNS Spectr 12(12 suppl 1): 1-14 (2007).
    • (2007) CNS Spectr , vol.12 , Issue.12 SUPPL. 1 , pp. 1-14
    • Kennedy, G.J.1    Golde, T.E.2    Tariot, P.N.3    Cummings, J.L.4
  • 24
    • 0035106780 scopus 로고    scopus 로고
    • Imaging of amyloid-β deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy
    • Bacskai BJ, Kajdasz ST, Christie RH, Carter C, Games D, Seubert P, et al. Imaging of amyloid-β deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy. Nat Med 7: 369-372 (2001).
    • (2001) Nat Med , vol.7 , pp. 369-372
    • Bacskai, B.J.1    Kajdasz, S.T.2    Christie, R.H.3    Carter, C.4    Games, D.5    Seubert, P.6
  • 25
    • 0030058382 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer β-amyloid peptide
    • Solomon B, Koppel R, Hanan E, Katzav T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer β-amyloid peptide. Proc Natl Acad Sci USA 93: 452-455 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 452-455
    • Solomon, B.1    Koppel, R.2    Hanan, E.3    Katzav, T.4
  • 26
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid β-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 β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med 6: 916-919 (2000).
    • (2000) Nat Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.L.4    Games, D.5    Grajeda, H.6
  • 27
    • 0141457897 scopus 로고    scopus 로고
    • Amyloid-β immunization eff ectively reduces amyloid deposition in FcRγ-/- knock-out mice
    • Das P, Howard V, Loosbrock N, Dickson D, Murphy MP, Golde TE. Amyloid-β immunization eff ectively reduces amyloid deposition in FcRγ-/- knock-out mice. J Neurosci 23: 8532-8538 (2003).
    • (2003) J Neurosci , vol.23 , pp. 8532-8538
    • Das, P.1    Howard, V.2    Loosbrock, N.3    Dickson, D.4    Murphy, M.P.5    Golde, T.E.6
  • 28
    • 0034884382 scopus 로고    scopus 로고
    • Immunization with a non-toxic/non-fibrillar amyloid-β homologous peptide reduces Alzheimer's disease associated pathology in transgenic mice
    • Sigurdsson EM, Scholtzova H, Mehta P, Frangione B, Wisniewski T. Immunization with a non-toxic/non-fibrillar amyloid-β homologous peptide reduces Alzheimer's disease associated pathology in transgenic mice. Am J Pathol 159: 439-447 (2001).
    • (2001) Am J Pathol , vol.159 , pp. 439-447
    • Sigurdsson, E.M.1    Scholtzova, H.2    Mehta, P.3    Frangione, B.4    Wisniewski, T.5
  • 29
    • 3242694207 scopus 로고    scopus 로고
    • An attenuated immune response is sufficient to enhance cognition in an Alzheimer's disease mouse model immunized with amyloid-γ derivatives
    • Sigurdsson EM, Knudsen E, Asuni A, Fitzer-Attas C, Sage D, Quartermain D, et al. An attenuated immune response is sufficient to enhance cognition in an Alzheimer's disease mouse model immunized with amyloid-γ derivatives. J Neurosci 24: 6277-6282 (2004).
    • (2004) J Neurosci , vol.24 , pp. 6277-6282
    • Sigurdsson, E.M.1    Knudsen, E.2    Asuni, A.3    Fitzer-Attas, C.4    Sage, D.5    Quartermain, D.6
  • 30
    • 47949132196 scopus 로고    scopus 로고
    • Active and passive immunotherapy for neurodegenerative diseass
    • Brody DL, Holtzman DM. Active and passive immunotherapy for neurodegenerative diseass. Annu Rev Neurosci 31: 175-193 (2008).
    • (2008) Annu Rev Neurosci , vol.31 , pp. 175-193
    • Brody, D.L.1    Holtzman, D.M.2
  • 31
    • 13544268706 scopus 로고    scopus 로고
    • Immunological and anti-chaperone therapeutic approaches for Alzheimer's disease
    • Wisniewski T, Frangione B. Immunological and anti-chaperone therapeutic approaches for Alzheimer's disease. Brain Pathol 15: 72-77 (2005).
    • (2005) Brain Pathol , vol.15 , pp. 72-77
    • Wisniewski, T.1    Frangione, B.2
  • 32
    • 11444267243 scopus 로고    scopus 로고
    • Evaluation of the safety and immunogenicity of synthetic Aγ42 (AN1792) in patients with AD
    • Bayer AJ, Bullock R, Jones RW, Wilkinson D, Paterson KR, Jenkins L, et al. Evaluation of the safety and immunogenicity of synthetic Aγ42 (AN1792) in patients with AD. Neurology 64: 94-101 (2005).
    • (2005) Neurology , vol.64 , pp. 94-101
    • Bayer, A.J.1    Bullock, R.2    Jones, R.W.3    Wilkinson, D.4    Paterson, K.R.5    Jenkins, L.6
  • 33
    • 40449086748 scopus 로고    scopus 로고
    • Progress in the active immunotherapeutic approach to Alzheimer's disease: Clinical investigations into AN1792-associated meningoencephalitis
    • Pride M, Seubert P, Grundman M, Hagen M, Eldridge J, Black RS. Progress in the active immunotherapeutic approach to Alzheimer's disease: clinical investigations into AN1792-associated meningoencephalitis. Neurodegener Dis 5: 194-196 (2008).
    • (2008) Neurodegener Dis , vol.5 , pp. 194-196
    • Pride, M.1    Seubert, P.2    Grundman, M.3    Hagen, M.4    Eldridge, J.5    Black, R.S.6
  • 34
    • 34447625185 scopus 로고    scopus 로고
    • Practice point commentary on Clinical effects of Aγ immunization (AN1792) in patients with AD in an interupted trial
    • Wisniewski T. Practice point commentary on Clinical effects of Aγ immunization (AN1792) in patients with AD in an interupted trial. Nat Clin Prac Neurol 1: 84-85 (2005).
    • (2005) Nat Clin Prac Neurol , vol.1 , pp. 84-85
    • Wisniewski, T.1
  • 35
    • 2542443382 scopus 로고    scopus 로고
    • Lessons from the AN1792 Alzheimer vaccine: Lest we forget
    • Robinson SR, Bishop GM, Lee HG, Munch G. Lessons from the AN1792 Alzheimer vaccine: lest we forget. Neurobiol Aging 25: 609-615 (2004).
    • (2004) Neurobiol Aging , vol.25 , pp. 609-615
    • Robinson, S.R.1    Bishop, G.M.2    Lee, H.G.3    Munch, G.4
  • 37
    • 1042265187 scopus 로고    scopus 로고
    • Neuropathology and pathogenesis of encephalitis following amyloid-γ immunization in Alzheimer's disease
    • Ferrer I, Boada RM, Sanchez Guerra ML, Rey MJ, Costa-Jussa F. Neuropathology and pathogenesis of encephalitis following amyloid-γ immunization in Alzheimer's disease. Brain Pathol 14: 11-20 (2004).
    • (2004) Brain Pathol , vol.14 , pp. 11-20
    • Ferrer, I.1    Boada, R.M.2    Sanchez Guerra, M.L.3    Rey, M.J.4    Costa-Jussa, F.5
  • 38
    • 19944429065 scopus 로고    scopus 로고
    • Aβ vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
    • Masliah E, Hansen L, Adame A, Crews L, Bard F, Lee C, et al. Aβ vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease. Neurology 64: 129-131 (2005).
    • (2005) Neurology , vol.64 , pp. 129-131
    • Masliah, E.1    Hansen, L.2    Adame, A.3    Crews, L.4    Bard, F.5    Lee, C.6
  • 40
    • 20944448555 scopus 로고    scopus 로고
    • Clinical effects of Aβ immunization (AN1792) in patients with AD in an interupted trial
    • Gilman S, Koller M, Black RS, Jenkins L, Griffith SG, Fox NC, et al. Clinical effects of Aβ immunization (AN1792) in patients with AD in an interupted trial. Neurology 64:1553-1562 (2005).
    • (2005) Neurology , vol.64 , pp. 1553-1562
    • Gilman, S.1    Koller, M.2    Black, R.S.3    Jenkins, L.4    Griffith, S.G.5    Fox, N.C.6
  • 41
    • 47149112621 scopus 로고    scopus 로고
    • Long-term effects of Aβ42 immunisation in Alzheimer's disease: Follow-up of a randomised, placebo-controlled phase I trial
    • Holmes C, Boche D, Wilkinson D, Yadegarfar G, Hopkins V, Bayer A, et al. Long-term effects of Aβ42 immunisation in Alzheimer's disease: follow-up of a randomised, placebo-controlled phase I trial. Lancet 372: 216-223 (2008).
    • (2008) Lancet , vol.372 , pp. 216-223
    • Holmes, C.1    Boche, D.2    Wilkinson, D.3    Yadegarfar, G.4    Hopkins, V.5    Bayer, A.6
  • 42
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ42 fibrils
    • Götz J, Chen F, van Dorpe J, Nitsch RM. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ42 fibrils. Science 293: 1491-1495 (2001).
    • (2001) Science , vol.293 , pp. 1491-1495
    • Götz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 44
    • 4043167747 scopus 로고    scopus 로고
    • Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM. Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43: 321-332 (2004).
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 45
    • 33846451755 scopus 로고    scopus 로고
    • The novel γ secretase inhibitor N-[cis-4-[(4-chlorophenyl) sulfonyl]-4-(2,5-difluorophenyl)cyclohexyl]-1,1,1-trifluoromethanesulfonamide (MRK-560) reduces amyloid plaque depo-sition without evidence of notch-related pathology in the Tg2576 mouse
    • Best JD, Smith DW, Reilly MA, O'Donnell R, Lewis HD, Ellis S, et al. The novel γ secretase inhibitor N-[cis-4-[(4-chlorophenyl) sulfonyl]-4-(2,5-difluorophenyl)cyclohexyl]-1,1,1-trifluoromethanesulfonamide (MRK-560) reduces amyloid plaque depo-sition without evidence of notch-related pathology in the Tg2576 mouse. J Pharmacol Exp Ther 320: 552-558 (2007).
    • (2007) J Pharmacol Exp Ther , vol.320 , pp. 552-558
    • Best, J.D.1    Smith, D.W.2    Reilly, M.A.3    O'Donnell, R.4    Lewis, H.D.5    Ellis, S.6
  • 46
    • 36349011989 scopus 로고    scopus 로고
    • 1-(3′,4′-Dichloro-2-fluoro[1,1′- biphenyl]-4-yl)-cyclopropanecarboxylic acid (CHF5074), a novel γ-secretase modulator, reduces brain β-amyloid pathology in a transgenic mouse model of Alzheimer's disease without causing peripheral toxicity
    • Imbimbo BP, Del Giudice E, Colavito D, D'Arrigo A, Dalle Carbonare M, Villetti G, et al. 1-(3′,4′-Dichloro-2-fluoro[1,1′- biphenyl]-4-yl)-cyclopropanecarboxylic acid (CHF5074), a novel γ-secretase modulator, reduces brain β-amyloid pathology in a transgenic mouse model of Alzheimer's disease without causing peripheral toxicity. J Pharmacol Exp Ther 323: 822-830 (2007).
    • (2007) J Pharmacol Exp Ther , vol.323 , pp. 822-830
    • Imbimbo, B.P.1    Del Giudice, E.2    Colavito, D.3    D'Arrigo, A.4    Dalle Carbonare, M.5    Villetti, G.6
  • 47
    • 0034746897 scopus 로고    scopus 로고
    • Reduced effectiveness of Aβ1-42 immunization in APP transgenic mice with significant amyloid deposition
    • Das P, Murphy MP, Younkin LH, Younkin SG, Golde TE. Reduced effectiveness of Aβ1-42 immunization in APP transgenic mice with significant amyloid deposition. Neurobiol Aging 22: 721-727 (2001).
    • (2001) Neurobiol Aging , vol.22 , pp. 721-727
    • Das, P.1    Murphy, M.P.2    Younkin, L.H.3    Younkin, S.G.4    Golde, T.E.5
  • 48
    • 70049083865 scopus 로고    scopus 로고
    • 18-Month study of intravenous immunoglobulin for treatment of mild Alzheimer disease
    • Relkin NR, Szabo P, Adamiak B, Burgut T, Monthe C, Lent RW, et al. 18-Month study of intravenous immunoglobulin for treatment of mild Alzheimer disease. Neurobiol Aging; 30(11): 1728-36 (2009).
    • (2009) Neurobiol Aging , vol.30 , Issue.11 , pp. 1728-1736
    • Relkin, N.R.1    Szabo, P.2    Adamiak, B.3    Burgut, T.4    Monthe, C.5    Lent, R.W.6
  • 49
    • 0036137241 scopus 로고    scopus 로고
    • ProPred: Prediction of HLA-DR binding sites
    • Singh H, Raghava GP. ProPred: prediction of HLA-DR binding sites. Bioinformatics 17: 1236-1237 (2001).
    • (2001) Bioinformatics , vol.17 , pp. 1236-1237
    • Singh, H.1    Raghava, G.P.2
  • 50
    • 0037606124 scopus 로고    scopus 로고
    • ProPred1: Prediction of promiscuous MHC class-I binding sites
    • Singh H, Raghava GP. ProPred1: prediction of promiscuous MHC class-I binding sites. Bioinformatics 19: 1009-1014 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 1009-1014
    • Singh, H.1    Raghava, G.P.2
  • 51
    • 0035689690 scopus 로고    scopus 로고
    • Nasal vaccination with β-amyloid peptide for the treatment of Alzheimer's disease
    • Lemere CA, Maron R, Selkoe DJ, Weiner HL. Nasal vaccination with β-amyloid peptide for the treatment of Alzheimer's disease. DNA Cell Biol 20: 705-711 (2001).
    • (2001) DNA Cell Biol , vol.20 , pp. 705-711
    • Lemere, C.A.1    Maron, R.2    Selkoe, D.J.3    Weiner, H.L.4
  • 52
    • 10744225891 scopus 로고    scopus 로고
    • A novel recombinant adeno-associated virus vaccine reduces behavioral impairment and β-amyloid plaques in a mouse model of Alzheimer's disease
    • Zhang J, Wu X, Qin C, Qi J, Ma S, Zhang H, et al. A novel recombinant adeno-associated virus vaccine reduces behavioral impairment and β-amyloid plaques in a mouse model of Alzheimer's disease. Neurobiol Dis 14: 365-379 (2003).
    • (2003) Neurobiol Dis , vol.14 , pp. 365-379
    • Zhang, J.1    Wu, X.2    Qin, C.3    Qi, J.4    Ma, S.5    Zhang, H.6
  • 53
    • 0033801852 scopus 로고    scopus 로고
    • Nasal administration of amyloid-β peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease
    • Weiner HL, Lemere CA, Maron R, Spooner ET, Grenfell TJ, Mori C, et al. Nasal administration of amyloid-β peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease. Ann Neurol 48: 567-579 (2000).
    • (2000) Ann Neurol , vol.48 , pp. 567-579
    • Weiner, H.L.1    Lemere, C.A.2    Maron, R.3    Spooner, E.T.4    Grenfell, T.J.5    Mori, C.6
  • 55
    • 34548409654 scopus 로고    scopus 로고
    • Toll-like receptors in the brain and their potential roles in neuropathology
    • Crack PJ, Bray PJ. Toll-like receptors in the brain and their potential roles in neuropathology. Immunol Cell Biol 85: 476-480 (2007).
    • (2007) Immunol Cell Biol , vol.85 , pp. 476-480
    • Crack, P.J.1    Bray, P.J.2
  • 56
    • 43049180959 scopus 로고    scopus 로고
    • CpG oligodeoxynucleotide-enhanced humoral immune response and production of antibodies to prion protein PrPSc in mice immunized with 139A scrapie-associated fi brils
    • Spinner DS, Kascsak RB, Lafauci G, Meeker HC, Ye X, Flory MJ, et al. CpG oligodeoxynucleotide-enhanced humoral immune response and production of antibodies to prion protein PrPSc in mice immunized with 139A scrapie-associated fi brils. J Leukoc Biol 14: 36-43 (2007).
    • (2007) J Leukoc Biol , vol.14 , pp. 36-43
    • Spinner, D.S.1    Kascsak, R.B.2    Lafauci, G.3    Meeker, H.C.4    Ye, X.5    Flory, M.J.6
  • 57
    • 2142706520 scopus 로고    scopus 로고
    • Breaking immune tolerance to the prion protein us ing prion protein peptides plus oligodeoxynucleotide-CpG in mice
    • Rosset MB, Ballerini C, Gregoire S, Metharom P, Carnaud C, Aucouturier P. Breaking immune tolerance to the prion protein us ing prion protein peptides plus oligodeoxynucleotide-CpG in mice. J Immunol 172: 5168-5174 (2004).
    • (2004) J Immunol , vol.172 , pp. 5168-5174
    • Rosset, M.B.1    Ballerini, C.2    Gregoire, S.3    Metharom, P.4    Carnaud, C.5    Aucouturier, P.6
  • 58
    • 77949759387 scopus 로고    scopus 로고
    • clinical trial of bapineuzumab for Alzheimer's disease. Available from:, accessed: November 30, 2008
    • Wyeth E. Wyeth announce encouraging top-line results from phase 2 clinical trial of bapineuzumab for Alzheimer's disease. Available from: http://wyeth.com/news?nav=display&navTo=/wyeth-html/home/news/pressreleases/ 2008/1213683456273.html [accessed: November 30, 2008].
    • Wyeth announce encouraging top-line results from phase , vol.2
    • Wyeth, E.1
  • 59
    • 64549152492 scopus 로고    scopus 로고
    • Long-term follow-up of patients immunized with AN1792: Reduced functional decline in antibody responders
    • Vellas B, Black R, Thal LJ, Fox NC, Daniels M, McLennan G, et al. Long-term follow-up of patients immunized with AN1792: reduced functional decline in antibody responders. Curr Alzheimer Res 6: 144-151 (2009).
    • (2009) Curr Alzheimer Res , vol.6 , pp. 144-151
    • Vellas, B.1    Black, R.2    Thal, L.J.3    Fox, N.C.4    Daniels, M.5    McLennan, G.6
  • 60
    • 0037010308 scopus 로고    scopus 로고
    • Amyloid-β: A vascular sealant that protects against hemorrhage?
    • Atwood CS, Bishop GM, Perry G, Smith MA. Amyloid-β: a vascular sealant that protects against hemorrhage? J Neurosci Res 70: 356 (2002)
    • (2002) J Neurosci Res , vol.70 , pp. 356
    • Atwood, C.S.1    Bishop, G.M.2    Perry, G.3    Smith, M.A.4
  • 63
    • 19944431509 scopus 로고    scopus 로고
    • Exacerbation of cerebral amyloid angiopathyassociated microhemorrhages in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyoid-β
    • Racke MM, Boone LI, Hepburn DL, Parsadainian M, Bryan MT, Ness DK, et al. Exacerbation of cerebral amyloid angiopathyassociated microhemorrhages in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyoid-β. J Neurosci 25: 629-636 (2005).
    • (2005) J Neurosci , vol.25 , pp. 629-636
    • Racke, M.M.1    Boone, L.I.2    Hepburn, D.L.3    Parsadainian, M.4    Bryan, M.T.5    Ness, D.K.6
  • 64
    • 33845904135 scopus 로고    scopus 로고
    • Amyloid-β vaccination, but not nitro-nonsteroidal anti-inflammatory drug treatment, increases vascular amyloid and microhemorrhage while both reduce parenchymal amyloid
    • Wilcock DM, Jantzen PT, Li Q, Morgan D, Gordon MN. Amyloid-β vaccination, but not nitro-nonsteroidal anti-inflammatory drug treatment, increases vascular amyloid and microhemorrhage while both reduce parenchymal amyloid. Neuroscience 144: 950-960 (2007).
    • (2007) Neuroscience , vol.144 , pp. 950-960
    • Wilcock, D.M.1    Jantzen, P.T.2    Li, Q.3    Morgan, D.4    Gordon, M.N.5
  • 65
    • 33748767945 scopus 로고    scopus 로고
    • Amyloid-β peptide remnants in AN-1792-immunized Alzheimer's disease patients: A biochemical analysis
    • Patton RL, Kalback WM, Esh CL, Kokjohn TA, Van Vickle GD, Luehrs DC, et al. Amyloid-β peptide remnants in AN-1792-immunized Alzheimer's disease patients: a biochemical analysis. Am J Pathol 169: 1048-1063 (2006).
    • (2006) Am J Pathol , vol.169 , pp. 1048-1063
    • Patton, R.L.1    Kalback, W.M.2    Esh, C.L.3    Kokjohn, T.A.4    Van Vickle, G.D.5    Luehrs, D.C.6
  • 66
    • 42149140619 scopus 로고    scopus 로고
    • Regulation of βAPP and PrPc cleavage by α-secretase: Mechanistic and therapeutic perspectives
    • Vincent B, Cisse MA, Sunyach C, Guillot-Sestier MV, Checler F. Regulation of βAPP and PrPc cleavage by α-secretase: mechanistic and therapeutic perspectives. Curr Alzheimer Res 5: 202-211 (2008).
    • (2008) Curr Alzheimer Res , vol.5 , pp. 202-211
    • Vincent, B.1    Cisse, M.A.2    Sunyach, C.3    Guillot-Sestier, M.V.4    Checler, F.5
  • 68
    • 70349109799 scopus 로고    scopus 로고
    • β-Amyloid Therapeutic Strategies for Alzheimer's Disease
    • Abraham DJ, Ed, 6th Edition, John Wiley & Sons Inc, Hoboken, pp
    • Imbimbo BP, Speroni F. β-Amyloid Therapeutic Strategies for Alzheimer's Disease. (Abraham DJ, Ed). Burger's Medicinal Chemistry and Drug Discovery. 6th Edition, John Wiley & Sons Inc, Hoboken, pp. 1-115 (2005).
    • (2005) Burger's Medicinal Chemistry and Drug Discovery , pp. 1-115
    • Imbimbo, B.P.1    Speroni, F.2
  • 69
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • Postina R, Schroeder A, Dewachter I, Bohl J, Schmitt U, Kojro E, et al. A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J Clin Invest 113: 1456-1464 (2004).
    • (2004) J Clin Invest , vol.113 , pp. 1456-1464
    • Postina, R.1    Schroeder, A.2    Dewachter, I.3    Bohl, J.4    Schmitt, U.5    Kojro, E.6
  • 70
    • 0035089318 scopus 로고    scopus 로고
    • Constitutive α-secretase cleavage of the β-amyloid precursor protein in the furin-deficient LoVo cell line: Involvement of the pro-hormone convertase 7 and the disintegrin ADAM10
    • Lopez-Perez E, Zhang Y, Frank SLJ, Creemers J, Seidah N, Checler F. Constitutive α-secretase cleavage of the β-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase 7 and the disintegrin ADAM10. J Neurochem 76: 1532-1539 (2001).
    • (2001) J Neurochem , vol.76 , pp. 1532-1539
    • Lopez-Perez, E.1    Zhang, Y.2    Frank, S.L.J.3    Creemers, J.4    Seidah, N.5    Checler, F.6
  • 71
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
    • Kojro E, Gimpl G, Lammich S, Marz W, Fahrenholz F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10. Proc Natl Acad Sci USA 98: 5815-5820 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 72
    • 4143063543 scopus 로고    scopus 로고
    • Atorvastatin-induced activation of Alzheimer's secretase is resistant to standard inhibitors of protein phosphorylation-regulated ectodomain shedding
    • Parvathy S, Ehrlich M, Pedrini S, Diaz N, Refolo L, Buxbaum JD, et al. Atorvastatin-induced activation of Alzheimer's secretase is resistant to standard inhibitors of protein phosphorylation-regulated ectodomain shedding. J Neurochem 90: 1005-1010 (2004).
    • (2004) J Neurochem , vol.90 , pp. 1005-1010
    • Parvathy, S.1    Ehrlich, M.2    Pedrini, S.3    Diaz, N.4    Refolo, L.5    Buxbaum, J.D.6
  • 74
    • 7444229915 scopus 로고    scopus 로고
    • Rosuvastatin reduces caspase-3 activity and up-regulates α-secretase in human neuroblastoma SH-SY5Y cells exposed to A
    • Famer D, Crisby M. Rosuvastatin reduces caspase-3 activity and up-regulates α-secretase in human neuroblastoma SH-SY5Y cells exposed to A. Neurosci Lett 371: 209-214 (2004).
    • (2004) Neurosci Lett , vol.371 , pp. 209-214
    • Famer, D.1    Crisby, M.2
  • 75
    • 77649250851 scopus 로고    scopus 로고
    • The effect of simvastatin treatment on the processing of the amyloid precursor protein in patients with Alzheimer's disease
    • abstract P4-386
    • Hoglund K, Thelen KM, Syversen S, Sjogren M, von Bergmann K, Wallin A, et al. The effect of simvastatin treatment on the processing of the amyloid precursor protein in patients with Alzheimer's disease. Neurobiol Aging 25: S584 (abstract P4-386) (2004).
    • (2004) Neurobiol Aging , vol.25
    • Hoglund, K.1    Thelen, K.M.2    Syversen, S.3    Sjogren, M.4    von Bergmann, K.5    Wallin, A.6
  • 76
    • 0037472674 scopus 로고    scopus 로고
    • New amide-bearing benzolactam-based protein kinase C modulators induce enhanced secretion of the amyloid precursor protein metabolite sAPPα
    • Kozikowski AP, Nowak I, Petukhov PA, Etcheberrigaray R, Mohamed A, Tan M, et al. New amide-bearing benzolactam-based protein kinase C modulators induce enhanced secretion of the amyloid precursor protein metabolite sAPPα. J Med Chem 46: 364-373 (2003).
    • (2003) J Med Chem , vol.46 , pp. 364-373
    • Kozikowski, A.P.1    Nowak, I.2    Petukhov, P.A.3    Etcheberrigaray, R.4    Mohamed, A.5    Tan, M.6
  • 79
    • 0034528415 scopus 로고    scopus 로고
    • Treatment with the selective muscarinic agonist talsaclidine decreases cerebrospinal fluid levels of total amyloid β-peptide in patients with Alzheimer's disease
    • Hock C, Maddalena A, Heuser I, Naber D, Oertel W, von der Kammer H, et al. Treatment with the selective muscarinic agonist talsaclidine decreases cerebrospinal fluid levels of total amyloid β-peptide in patients with Alzheimer's disease. Ann NY Acad Sci 920: 285-291 (2000).
    • (2000) Ann NY Acad Sci , vol.920 , pp. 285-291
    • Hock, C.1    Maddalena, A.2    Heuser, I.3    Naber, D.4    Oertel, W.5    von der Kammer, H.6
  • 80
    • 12444313989 scopus 로고    scopus 로고
    • Treatment with the selective muscarinic m1 agonist talsaclidine decreases cerebrospinal fluid levels of Aβ42 in patients with Alzheimer's disease
    • Hock C, Maddalena A, Raschig A, Müller-Spahn F, Eschweiler G, Hager K, et al. Treatment with the selective muscarinic m1 agonist talsaclidine decreases cerebrospinal fluid levels of Aβ42 in patients with Alzheimer's disease. Amyloid 10: 1-6 (2003).
    • (2003) Amyloid , vol.10 , pp. 1-6
    • Hock, C.1    Maddalena, A.2    Raschig, A.3    Müller-Spahn, F.4    Eschweiler, G.5    Hager, K.6
  • 81
    • 0033663907 scopus 로고    scopus 로고
    • The selective muscarinic M1 agonist AF102B decreases levels of total Aβ in cerebrospinal fluid of patients with Alzheimer's disease
    • Nitsch RM, Deng M, Tennis M, Schoenfeld D, Growdon JH. The selective muscarinic M1 agonist AF102B decreases levels of total Aβ in cerebrospinal fluid of patients with Alzheimer's disease. Ann Neurol 48: 913-918 (2000).
    • (2000) Ann Neurol , vol.48 , pp. 913-918
    • Nitsch, R.M.1    Deng, M.2    Tennis, M.3    Schoenfeld, D.4    Growdon, J.H.5
  • 82
    • 33344458827 scopus 로고    scopus 로고
    • M1 receptors play a central role in modulating AD like pathology in transgenic mice
    • Caccamo A, Oddo S, Billings LM, Green KN, Martinez-Coria H, Fisher A, et al. M1 receptors play a central role in modulating AD like pathology in transgenic mice. Neuron 49: 671-682 (2006).
    • (2006) Neuron , vol.49 , pp. 671-682
    • Caccamo, A.1    Oddo, S.2    Billings, L.M.3    Green, K.N.4    Martinez-Coria, H.5    Fisher, A.6
  • 83
    • 33745209915 scopus 로고    scopus 로고
    • ADAM10 activation is required for green tea (-)-epigallocatechin-3-gallate- induced α-secretase cleavage of amyloid precursor protein
    • Obregon DF, Rezai-Zadeh K, Bai Y, Sun N, Hou H, Ehrhart J, et al. ADAM10 activation is required for green tea (-)-epigallocatechin-3-gallate- induced α-secretase cleavage of amyloid precursor protein. J Biol Chem 281: 16419-16427 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 16419-16427
    • Obregon, D.F.1    Rezai-Zadeh, K.2    Bai, Y.3    Sun, N.4    Hou, H.5    Ehrhart, J.6
  • 84
    • 33847171931 scopus 로고    scopus 로고
    • Synapse-associated protein-97 mediates α-secretase ADAM10 trafficking and promotes its activity
    • Marcello E, Gardoni F, Mauceri D, Romorini S, Jeromin A, Epis R, et al. Synapse-associated protein-97 mediates α-secretase ADAM10 trafficking and promotes its activity. J Neurosci 14: 1682-1691 (2007).
    • (2007) J Neurosci , vol.14 , pp. 1682-1691
    • Marcello, E.1    Gardoni, F.2    Mauceri, D.3    Romorini, S.4    Jeromin, A.5    Epis, R.6
  • 85
    • 84992732653 scopus 로고    scopus 로고
    • EHT 0202: A neuroprotective and procognitive α-secretase stimulator targeted towards Alzheimer's disease therapy
    • Abstract P1019
    • Desire L, Drouin D, Sol O, Lambeng N, Schweighoffer F. EHT 0202: a neuroprotective and procognitive α-secretase stimulator targeted towards Alzheimer's disease therapy. Eur J Neurol 15: (Suppl. 3): 1104 (Abstract P1019) (2008).
    • (2008) Eur J Neurol , vol.15 , Issue.SUPPL. 3 , pp. 1104
    • Desire, L.1    Drouin, D.2    Sol, O.3    Lambeng, N.4    Schweighoffer, F.5
  • 86
    • 0033595706 scopus 로고    scopus 로고
    • α-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, Denis P, et al. α-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286: 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5    Denis, P.6
  • 87
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the α-secretase site of β-amyloid precursor protein
    • Lin X, Koelsch G, Wu S, Downs D, Dashti A, Tang J. Human aspartic protease memapsin 2 cleaves the α-secretase site of β-amyloid precursor protein. Proc Natl Acad Sci USA 97: 1456-1460 (2000).
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1456-1460
    • Lin, X.1    Koelsch, G.2    Wu, S.3    Downs, D.4    Dashti, A.5    Tang, J.6
  • 88
    • 17344388652 scopus 로고    scopus 로고
    • BACE knockout mice are healthy despite lacking the primary β-secretase activity in brain:implications for Alzheimer's disease therapeutics
    • Roberds SL, Anderson J, Basi G, Bienkowski MJ, Branstetter DG, Chen KS, et al. BACE knockout mice are healthy despite lacking the primary β-secretase activity in brain:implications for Alzheimer's disease therapeutics. Hum Mol Genet 10: 1317-1324 (2001).
    • (2001) Hum Mol Genet , vol.10 , pp. 1317-1324
    • Roberds, S.L.1    Anderson, J.2    Basi, G.3    Bienkowski, M.J.4    Branstetter, D.G.5    Chen, K.S.6
  • 89
    • 43149100823 scopus 로고    scopus 로고
    • Inhibitors of cathepsin B improve memory and reduce β-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, β-secretase site of the amyloid precursor protein
    • Hook VY, Kindy M, Hook G. Inhibitors of cathepsin B improve memory and reduce β-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, β-secretase site of the amyloid precursor protein. J Biol Chem 283: 7745-7753 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 7745-7753
    • Hook, V.Y.1    Kindy, M.2    Hook, G.3
  • 90
    • 0037085353 scopus 로고    scopus 로고
    • Substrate and inhibitor profile of BACE (β-secretase) and comparison with other mammalian aspartic proteases
    • Gruninger-Leitch F, Schlatter D, Kung E, Nelbock P, Dobeli H. Substrate and inhibitor profile of BACE (β-secretase) and comparison with other mammalian aspartic proteases. J Biol Chem 277: 4687-4693 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 4687-4693
    • Gruninger-Leitch, F.1    Schlatter, D.2    Kung, E.3    Nelbock, P.4    Dobeli, H.5
  • 93
    • 0035974650 scopus 로고    scopus 로고
    • Structure-based design: Potent inhibitors of human brain memapsin 2 (β-secretase)
    • Ghosh AK, Bilcer G, Harwood C, Kawahama R, Shin D, Hussain KA, et al. Structure-based design: potent inhibitors of human brain memapsin 2 (β-secretase). J Med Chem 44: 2865-2868 (2001).
    • (2001) J Med Chem , vol.44 , pp. 2865-2868
    • Ghosh, A.K.1    Bilcer, G.2    Harwood, C.3    Kawahama, R.4    Shin, D.5    Hussain, K.A.6
  • 94
    • 33644878338 scopus 로고    scopus 로고
    • The novel β-secretase inhibitor KMI-429 reduces amyloid β peptide production in amyloid precursor protein transgenic and wildtype mice
    • Asai M, Hattori C, Iwata N, Saido TC, Sasagawa N, Szabó B, et al. The novel β-secretase inhibitor KMI-429 reduces amyloid β peptide production in amyloid precursor protein transgenic and wildtype mice. Neurochem 96: 533-540 (2006).
    • (2006) Neurochem , vol.96 , pp. 533-540
    • Asai, M.1    Hattori, C.2    Iwata, N.3    Saido, T.C.4    Sasagawa, N.5    Szabó, B.6
  • 95
    • 1542374176 scopus 로고    scopus 로고
    • A β-secretase (BACE1) inhibitor hispidin from the mycelial cultures of Phellinus linteus
    • Park ICH, Jeon SY, Lee HJ, Kim SI, Song KS. A β-secretase (BACE1) inhibitor hispidin from the mycelial cultures of Phellinus linteus. Planta Med 70: 143-146 (2004).
    • (2004) Planta Med , vol.70 , pp. 143-146
    • Park, I.C.H.1    Jeon, S.Y.2    Lee, H.J.3    Kim, S.I.4    Song, K.S.5
  • 96
    • 0242285619 scopus 로고    scopus 로고
    • Green tea catechins as a BACE1 (β-secretase) inhibitor
    • Jeon SY, Bae K, Seong YH, Song KS. Green tea catechins as a BACE1 (β-secretase) inhibitor. Bioorg Med Chem Lett 13: 3905-3908 (2003).
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 3905-3908
    • Jeon, S.Y.1    Bae, K.2    Seong, Y.H.3    Song, K.S.4
  • 97
    • 9644254194 scopus 로고    scopus 로고
    • Structure-based design of cycloamideurethane-derived novel inhibitors of human brain memapsin 2 (β-secretase)
    • Ghosh AK, Devasamudram T, Hong L, DeZutter C, Xu X, Weerasena V, et al. Structure-based design of cycloamideurethane-derived novel inhibitors of human brain memapsin 2 (β-secretase). Bioorg Med Chem Lett 15: 15-20 (2005).
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 15-20
    • Ghosh, A.K.1    Devasamudram, T.2    Hong, L.3    DeZutter, C.4    Xu, X.5    Weerasena, V.6
  • 98
    • 11844297294 scopus 로고    scopus 로고
    • Structural locations and functional roles of new subsites S(5), S(6), and S(7) in memapsin 2 (β-secretase)
    • Turner RT 3rd, Hong L, Koelsch G, Ghosh AK, Tang J. Structural locations and functional roles of new subsites S(5), S(6), and S(7) in memapsin 2 (β-secretase). Biochemistry 44: 105-112 (2005).
    • (2005) Biochemistry , vol.44 , pp. 105-112
    • Turner 3rd, R.T.1    Hong, L.2    Koelsch, G.3    Ghosh, A.K.4    Tang, J.5
  • 99
    • 3042658599 scopus 로고    scopus 로고
    • In vivo inhibition of Aβ production by memapsin 2 (β-secretase) inhibitors
    • Chang WP, Koelsch G, Wong S, Downs D, Da H, Weerasena V, et al. In vivo inhibition of Aβ production by memapsin 2 (β-secretase) inhibitors. J Neurochem 89: 1409-1416 (2004).
    • (2004) J Neurochem , vol.89 , pp. 1409-1416
    • Chang, W.P.1    Koelsch, G.2    Wong, S.3    Downs, D.4    Da, H.5    Weerasena, V.6
  • 100
    • 35248882587 scopus 로고    scopus 로고
    • Amyloid-β reduction by memapsin 2 (β-secretase) immunization
    • Chang WP, Downs D, Huang XP, Da H, Fung KM, Tang J. Amyloid-β reduction by memapsin 2 (β-secretase) immunization. FASEB J 21: 3184-3196 (2007).
    • (2007) FASEB J , vol.21 , pp. 3184-3196
    • Chang, W.P.1    Downs, D.2    Huang, X.P.3    Da, H.4    Fung, K.M.5    Tang, J.6
  • 101
    • 34247112490 scopus 로고    scopus 로고
    • Apolipoprotein receptor 2 and X11 α/β mediate apolipoprotein E-induced endocytosis of amyloid-β precursor protein and β-secretase, leading to amyloid-β production
    • He X, Cooley K, Chung CH, Dashti N, Tang J. Apolipoprotein receptor 2 and X11 α/β mediate apolipoprotein E-induced endocytosis of amyloid-β precursor protein and β-secretase, leading to amyloid-β production. J Neurosci 27: 4052- 4060 (2007).
    • (2007) J Neurosci , vol.27 , pp. 4052-4060
    • He, X.1    Cooley, K.2    Chung, C.H.3    Dashti, N.4    Tang, J.5
  • 102
    • 38749146862 scopus 로고    scopus 로고
    • Potent memapsin 2 (β-secretase) inhibitors: Design, synthesis, protein-ligand X-ray structure, and in vivo evaluation
    • Ghosh AK, Kumaragurubaran N, Hong L, Kulkarni S, Xu X, Miller HB, et al. Potent memapsin 2 (β-secretase) inhibitors: design, synthesis, protein-ligand X-ray structure, and in vivo evaluation. Bioorg Med Chem Lett 18: 1031-1036 (2008).
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 1031-1036
    • Ghosh, A.K.1    Kumaragurubaran, N.2    Hong, L.3    Kulkarni, S.4    Xu, X.5    Miller, H.B.6
  • 103
    • 77949767923 scopus 로고    scopus 로고
    • CoMentis Announces Proof-of-Activity-Data from its Phase I Study of Disease-Modifying Alzheimer's Disease Therapy CoMentis News Room. Available from URL: www.athenagen.com/index.php?/athenagen/press-releases/48 [Accessed 30 November 2008].
    • CoMentis Announces Proof-of-Activity-Data from its Phase I Study of Disease-Modifying Alzheimer's Disease Therapy CoMentis News Room. Available from URL: www.athenagen.com/index.php?/athenagen/press-releases/48 [Accessed 30 November 2008].
  • 104
    • 77949720072 scopus 로고    scopus 로고
    • CoMentis receives FDA clearance to begin human clinical trials for its disease-modifying Alzheimer's therapy. CoMentis News Room. Available from URL: www.athenagen.com/index.php?/athenagen/press-releases/45 [Accessed 30 November 2008].
    • CoMentis receives FDA clearance to begin human clinical trials for its disease-modifying Alzheimer's therapy. CoMentis News Room. Available from URL: www.athenagen.com/index.php?/athenagen/press-releases/45 [Accessed 30 November 2008].
  • 105
    • 0035736326 scopus 로고    scopus 로고
    • Endogenous β-amyloid production in presenilin deficient embryonic mouse fibroblasts
    • Armogida M, Petit A, Vincent B, Scarzello S, Alves da Costa C, et al. Endogenous β-amyloid production in presenilin deficient embryonic mouse fibroblasts. Nature Cell Biol 3: 1030-1033 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 1030-1033
    • Armogida, M.1    Petit, A.2    Vincent, B.3    Scarzello, S.4    Alves da Costa, C.5
  • 107
    • 40349111175 scopus 로고    scopus 로고
    • Therapeutic potential of γ-secretase inhibitors and modulators
    • Imbimbo BP. Therapeutic potential of γ-secretase inhibitors and modulators. Curr Top Med Chem 8: 54-61 (2008).
    • (2008) Curr Top Med Chem , vol.8 , pp. 54-61
    • Imbimbo, B.P.1
  • 108
    • 62249157012 scopus 로고    scopus 로고
    • Imbimbo BP. Alzheimer's Disease: γ-Secretase Inhibitors. Drug Discov Today Ther Strateg 5(3): 169-75 2008 (in press).
    • Imbimbo BP. Alzheimer's Disease: γ-Secretase Inhibitors. Drug Discov Today Ther Strateg 5(3): 169-75 2008 (in press).
  • 109
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in presenilin-1-deficient mice
    • Shen J, Bronson RT, Chen DF, Xia W, Selkoe DJ. Skeletal and CNS defects in presenilin-1-deficient mice. Cell 89: 629-639 (1997).
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1    Bronson, R.T.2    Chen, D.F.3    Xia, W.4    Selkoe, D.J.5
  • 110
    • 0038746673 scopus 로고    scopus 로고
    • Catalytic site-directed γ-secretase complex inhibitors do not discriminate pharmacologically between Notch S3 and β-APP cleavages
    • Lewis HD, Perez Revuelta BI, Nadin A, Neduvelil JG, Harrison T, Pollack SJ, et al. Catalytic site-directed γ-secretase complex inhibitors do not discriminate pharmacologically between Notch S3 and β-APP cleavages. Biochemistry 42: 7580-7586 (2003).
    • (2003) Biochemistry , vol.42 , pp. 7580-7586
    • Lewis, H.D.1    Perez Revuelta, B.I.2    Nadin, A.3    Neduvelil, J.G.4    Harrison, T.5    Pollack, S.J.6
  • 113
    • 40349088899 scopus 로고    scopus 로고
    • The Notch pathway: Hair graying and pigment cell homeostasis
    • Schouwey K, Beermann F. The Notch pathway: hair graying and pigment cell homeostasis. Histol Histopathol 23: 609-619 (2008).
    • (2008) Histol Histopathol , vol.23 , pp. 609-619
    • Schouwey, K.1    Beermann, F.2
  • 116
    • 33847719509 scopus 로고    scopus 로고
    • The γ secretase inhibitor MK-0752 acutely and significantly reduces CSF Aβ40 concentrations in humans
    • Abstract O4-03-02
    • Rosen LB, Stone JA, Plump A, Yuan J, Harrison T, Flynn M, et al. The γ secretase inhibitor MK-0752 acutely and significantly reduces CSF Aβ40 concentrations in humans. Alzheimers Dement 2 (Suppl. 1): S79 (Abstract O4-03-02) (2006).
    • (2006) Alzheimers Dement , vol.2 , Issue.SUPPL. 1
    • Rosen, L.B.1    Stone, J.A.2    Plump, A.3    Yuan, J.4    Harrison, T.5    Flynn, M.6
  • 117
    • 62249195668 scopus 로고    scopus 로고
    • BMS-708163, a potent and selective γ-secretase inhibitor, decreases CSF Aβ at safe and tolerable doses in animals and humans
    • 26-31 July, Chicago, IL, USA Abstract HT-01-05
    • Albright CF, Dockens R, Olson RE, Meredith J, Slemmon R, Lentz K, et al. BMS-708163, a potent and selective γ-secretase inhibitor, decreases CSF Aβ at safe and tolerable doses in animals and humans. International Conference on Alzheimer's Disease, 26-31 July, Chicago, IL, USA (Abstract HT-01-05) (2008).
    • (2008) International Conference on Alzheimer's Disease
    • Albright, C.F.1    Dockens, R.2    Olson, R.E.3    Meredith, J.4    Slemmon, R.5    Lentz, K.6
  • 118
    • 77949700366 scopus 로고    scopus 로고
    • Wood KM, Lanz TA, Coffman KJ, Becker SL, van Deusen J, Nolan CE, et al. Efficacy of the novel γ-secretase inhibitor, Pf-3084014, in reducing Aβ in brain, CSF, and plasma in guinea pigs and Tg2576 mice. Alzheimers Dement (4 Suppl. 2): T482 (Abstract P2-375) (2008).
    • Wood KM, Lanz TA, Coffman KJ, Becker SL, van Deusen J, Nolan CE, et al. Efficacy of the novel γ-secretase inhibitor, Pf-3084014, in reducing Aβ in brain, CSF, and plasma in guinea pigs and Tg2576 mice. Alzheimers Dement (4 Suppl. 2): T482 (Abstract P2-375) (2008).
  • 119
    • 62249142932 scopus 로고    scopus 로고
    • GSI-953, a potent and selective γ-secretase inhibitor-modulation of β amyloid peptides and plasma and cerebrospinal fluid pharmacokinetic/ pharmacodynamic relationships in humans
    • Abstract P4-366
    • Frick G, Raje S, Wan H, Forlow SB, Balliet C, Pastore A, et al. GSI-953, a potent and selective γ-secretase inhibitor-modulation of β amyloid peptides and plasma and cerebrospinal fluid pharmacokinetic/ pharmacodynamic relationships in humans. Alzheimers Dement 4 (Suppl. 2): T781 (Abstract P4-366) (2008).
    • (2008) Alzheimers Dement , vol.4 , Issue.SUPPL. 2
    • Frick, G.1    Raje, S.2    Wan, H.3    Forlow, S.B.4    Balliet, C.5    Pastore, A.6
  • 120
    • 21544432780 scopus 로고    scopus 로고
    • Reduced β-amyloid burden, increased C-99 concentrations and evaluation of neuropathology in the brains of PDAPP mice given LY450139 dihydrate daily by gavage for 5 months
    • Ness DK, Boggs LN, Hepburn DL, Gitter B, Long GG, May PC, et al. Reduced β-amyloid burden, increased C-99 concentrations and evaluation of neuropathology in the brains of PDAPP mice given LY450139 dihydrate daily by gavage for 5 months. Neurobiol Aging 25 (Suppl. 2): 238 (2004).
    • (2004) Neurobiol Aging , vol.25 , Issue.SUPPL. 2 , pp. 238
    • Ness, D.K.1    Boggs, L.N.2    Hepburn, D.L.3    Gitter, B.4    Long, G.G.5    May, P.C.6
  • 121
    • 21544458621 scopus 로고    scopus 로고
    • Safety, tolerability, and changes in amyloid β concentrations after administration of a γ-secretase inhibitor in volunteers
    • Siemers E, Skinner M, Dean RA, Gonzales C, Satterwhite J, Farlow M, et al. Safety, tolerability, and changes in amyloid β concentrations after administration of a γ-secretase inhibitor in volunteers. Clin Neuropharmacol 28: 126-132 (2005).
    • (2005) Clin Neuropharmacol , vol.28 , pp. 126-132
    • Siemers, E.1    Skinner, M.2    Dean, R.A.3    Gonzales, C.4    Satterwhite, J.5    Farlow, M.6
  • 122
    • 37349072443 scopus 로고    scopus 로고
    • Safety, tolerability, and effects on plasma and cerebrospinal fluid amyloid-β after inhibition of γ-secretase
    • Siemers ER, Dean RA, Friedrich S, Ferguson-Sells L, Gonzales C, Farlow MR, et al. Safety, tolerability, and effects on plasma and cerebrospinal fluid amyloid-β after inhibition of γ-secretase. Clin Neuropharmacol 30: 317-325 (2007).
    • (2007) Clin Neuropharmacol , vol.30 , pp. 317-325
    • Siemers, E.R.1    Dean, R.A.2    Friedrich, S.3    Ferguson-Sells, L.4    Gonzales, C.5    Farlow, M.R.6
  • 123
    • 33645013015 scopus 로고    scopus 로고
    • Effects of a γ-secretase inhibitor in a randomized study of patients with Alzheimer disease
    • Siemers ER, Quinn JF, Kaye J, Farlow MR, Porsteinsson A, Tariot P, et al. Effects of a γ-secretase inhibitor in a randomized study of patients with Alzheimer disease. Neurology 66: 602-604 (2006).
    • (2006) Neurology , vol.66 , pp. 602-604
    • Siemers, E.R.1    Quinn, J.F.2    Kaye, J.3    Farlow, M.R.4    Porsteinsson, A.5    Tariot, P.6
  • 124
    • 49449101906 scopus 로고    scopus 로고
    • Phase 2 safety trial targeting amyloid β production with a γ-secretase inhibitor in Alzheimer disease
    • Fleisher AS, Raman R, Siemers ER, Becerra L, Clark CM, Dean RA, et al. Phase 2 safety trial targeting amyloid β production with a γ-secretase inhibitor in Alzheimer disease. Arch Neurol 65: 1031-1038 (2008).
    • (2008) Arch Neurol , vol.65 , pp. 1031-1038
    • Fleisher, A.S.1    Raman, R.2    Siemers, E.R.3    Becerra, L.4    Clark, C.M.5    Dean, R.A.6
  • 126
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
    • Weggen S, Eriksen JL, Das P, Sagi SA, Wang R, Pietrzik CU, et al. A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity. Nature 414: 212-216 (2001).
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1    Eriksen, J.L.2    Das, P.3    Sagi, S.A.4    Wang, R.5    Pietrzik, C.U.6
  • 127
    • 46749097518 scopus 로고    scopus 로고
    • Inhibition and modulation of γ-secretase for Alzheimer's disease
    • Wolfe MS. Inhibition and modulation of γ-secretase for Alzheimer's disease. Neurotherapeutics 5: 391-398 (2008).
    • (2008) Neurotherapeutics , vol.5 , pp. 391-398
    • Wolfe, M.S.1
  • 129
    • 85047691727 scopus 로고    scopus 로고
    • NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ 42 in vivo
    • Eriksen JL, Sagi SA, Smith TE, Weggen S, Das P, McLendon DC, et al. NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ 42 in vivo. J Clin Invest 112: 440-449 (2003).
    • (2003) J Clin Invest , vol.112 , 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
  • 130
    • 34547884277 scopus 로고    scopus 로고
    • Chronic administration of R-flurbiprofen attenuates learning impairments in transgenic amyloid precursor protein mice
    • Kukar T, Prescott S, Eriksen JL, Holloway V, Murphy MP, Koo EH, et al. Chronic administration of R-flurbiprofen attenuates learning impairments in transgenic amyloid precursor protein mice. BMC Neurosci 8: 54 (2007).
    • (2007) BMC Neurosci , vol.8 , pp. 54
    • Kukar, T.1    Prescott, S.2    Eriksen, J.L.3    Holloway, V.4    Murphy, M.P.5    Koo, E.H.6
  • 131
    • 37349104196 scopus 로고    scopus 로고
    • Safety, tolerability, pharmacokinetics and Aβ levels after short-term administration of R-flurbiprofen in healthy elderly individuals
    • Galasko DR, Graff-Radford N, May S, Hendrix S, Cottrell BA, Sagi SA, et al. Safety, tolerability, pharmacokinetics and Aβ levels after short-term administration of R-flurbiprofen in healthy elderly individuals. Alzheimer Dis Assoc Disord 21: 292-299 (2007).
    • (2007) Alzheimer Dis Assoc Disord , vol.21 , pp. 292-299
    • Galasko, D.R.1    Graff-Radford, N.2    May, S.3    Hendrix, S.4    Cottrell, B.A.5    Sagi, S.A.6
  • 132
    • 43249122280 scopus 로고    scopus 로고
    • Tarenflurbil Phase II Study investigators. Efficacy and safety of tarenflurbil in mild to moderate Alzheimer's disease; a randomised phase II trial
    • Wilcock GK, Black SE, Hendrix SB, Zavitz KH, Swabb EA, Laughlin MA. Tarenflurbil Phase II Study investigators. Efficacy and safety of tarenflurbil in mild to moderate Alzheimer's disease; a randomised phase II trial. Lancet Neurol 7: 483-493 (2008).
    • (2008) Lancet Neurol , vol.7 , pp. 483-493
    • Wilcock, G.K.1    Black, S.E.2    Hendrix, S.B.3    Zavitz, K.H.4    Swabb, E.A.5    Laughlin, M.A.6
  • 133
    • 77949687744 scopus 로고    scopus 로고
    • Available from URL:, Accessed 30 November 2008
    • Available from URL: http://www.alzforum.org [Accessed 30 November 2008].
  • 134
    • 77949765522 scopus 로고    scopus 로고
    • Why did Flurizan fail?
    • In press
    • Imbimbo BP. Why did Flurizan fail? J Alzheimers Dis (2009) (In press).
    • (2009) J Alzheimers Dis
    • Imbimbo, B.P.1
  • 135
    • 11844299025 scopus 로고    scopus 로고
    • Lack of specific amyloid-β1-42 suppression by nonsteroidal anti-inflammatory drugs in young, plaque-free Tg2576 mice and in guinea pig neuronal cultures
    • Lanz TA, Fici GJ, Merchant KM. Lack of specific amyloid-β1-42 suppression by nonsteroidal anti-inflammatory drugs in young, plaque-free Tg2576 mice and in guinea pig neuronal cultures. J Pharmacol Exp Ther 312: 399-406 (2005).
    • (2005) J Pharmacol Exp Ther , vol.312 , pp. 399-406
    • Lanz, T.A.1    Fici, G.J.2    Merchant, K.M.3
  • 136
    • 0034620538 scopus 로고    scopus 로고
    • A randomized controlled trial of prednisone in Alzheimer's disease. Alzheimer's Disease Cooperative Study
    • Aisen PS, Davis KL, Berg JD, Schafer K, Campbell K, Thomas RG, et al. A randomized controlled trial of prednisone in Alzheimer's disease. Alzheimer's Disease Cooperative Study. Neurology 54: 588-593 (2000).
    • (2000) Neurology , vol.54 , pp. 588-593
    • Aisen, P.S.1    Davis, K.L.2    Berg, J.D.3    Schafer, K.4    Campbell, K.5    Thomas, R.G.6
  • 137
    • 21144447586 scopus 로고    scopus 로고
    • A randomized, double-blind, study of rofecoxib in patients with mild cognitive impairment
    • Thal LJ, Ferris SH, Kirby L, Block GA, Lines CR, Yuen E, et al. A randomized, double-blind, study of rofecoxib in patients with mild cognitive impairment. Neuropsychopharmacology 30: 1204-1215 (2005).
    • (2005) Neuropsychopharmacology , vol.30 , pp. 1204-1215
    • Thal, L.J.1    Ferris, S.H.2    Kirby, L.3    Block, G.A.4    Lines, C.R.5    Yuen, E.6
  • 138
    • 34249058674 scopus 로고    scopus 로고
    • Naproxen and celecoxib do not prevent AD in early results from a randomized controlled trial
    • ADAPT Research Group
    • ADAPT Research Group, Lyketsos CG, Breitner JC, Green RC, Martin BK, Meinert C, et al. Naproxen and celecoxib do not prevent AD in early results from a randomized controlled trial. Neurology 68: 1800-1808 (2007).
    • (2007) Neurology , vol.68 , pp. 1800-1808
    • Lyketsos, C.G.1    Breitner, J.C.2    Green, R.C.3    Martin, B.K.4    Meinert, C.5
  • 139
    • 27744600566 scopus 로고    scopus 로고
    • Modulators of γ-secretase activity that lower Aβ42 levels without affecting Notch proteolytic processing
    • Sorrento, Italy, March 9-13. Abstract Book. p
    • Wagner S, Kounnas M, Tyree C, Cheng S, Danks A, Ackermann L, et al. Modulators of γ-secretase activity that lower Aβ42 levels without affecting Notch proteolytic processing. 7th International Conference AD/PD, Sorrento, Italy, March 9-13. Abstract Book. p. 11 (2005).
    • (2005) 7th International Conference AD/PD , pp. 11
    • Wagner, S.1    Kounnas, M.2    Tyree, C.3    Cheng, S.4    Danks, A.5    Ackermann, L.6
  • 140
    • 77949670209 scopus 로고    scopus 로고
    • Beher D, Bettati M, Checksfield GD, Churcher I, Doughty VA, Oakley PJ, et al. Treatment of Alzheimer's disease and related conditions. WO 2005/013985 A1, (2005).
    • Beher D, Bettati M, Checksfield GD, Churcher I, Doughty VA, Oakley PJ, et al. Treatment of Alzheimer's disease and related conditions. WO 2005/013985 A1, (2005).
  • 141
    • 77949738848 scopus 로고    scopus 로고
    • Kimura T, Kawano K, Doi E, Kitazawa N, Shin K, Miyagawa T, et al. Ciannamide compound. US 2006/0004013 A1, (2006).
    • Kimura T, Kawano K, Doi E, Kitazawa N, Shin K, Miyagawa T, et al. Ciannamide compound. US 2006/0004013 A1, (2006).
  • 143
    • 33847133125 scopus 로고    scopus 로고
    • Targeting soluble Aβ peptide with tramiprosate for the treatment of brain amyloidosis
    • Gervais F, Paquette J, Morissette C, Krzywkowski P, Yu M, Azzi M, et al. Targeting soluble Aβ peptide with tramiprosate for the treatment of brain amyloidosis. Neurobiol Aging 28: 537-547 (2007).
    • (2007) Neurobiol Aging , vol.28 , pp. 537-547
    • Gervais, F.1    Paquette, J.2    Morissette, C.3    Krzywkowski, P.4    Yu, M.5    Azzi, M.6
  • 144
    • 33845388059 scopus 로고    scopus 로고
    • A Phase II study targeting amyloid-β with 3APS in mild-tomoderate Alzheimer disease
    • Aisen PS, Gauthier S, Vellas B, Briand R, Saumier D, Laurin J, et al. A Phase II study targeting amyloid-β with 3APS in mild-tomoderate Alzheimer disease. Neurology 67: 1757-1763 (2006).
    • (2006) Neurology , vol.67 , pp. 1757-1763
    • Aisen, P.S.1    Gauthier, S.2    Vellas, B.3    Briand, R.4    Saumier, D.5    Laurin, J.6
  • 145
    • 77949681897 scopus 로고    scopus 로고
    • Available from URL:, Accessed 30 November 2008
    • Available from URL: http://www.alzforum.org/new/detail. asp?id=1647 [Accessed 30 November 2008].
  • 146
    • 54249103057 scopus 로고    scopus 로고
    • Drug development based on the metals hypothesis of Alzheimer's disease
    • Bush AI. Drug development based on the metals hypothesis of Alzheimer's disease. J Alzheimers Dis 15: 223-240 (2008).
    • (2008) J Alzheimers Dis , vol.15 , pp. 223-240
    • Bush, A.I.1
  • 147
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copperzinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, Gray DN, Jones WD, McLean CA, et al. Treatment with a copperzinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30: 665-676 (2001).
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3    Gray, D.N.4    Jones, W.D.5    McLean, C.A.6
  • 148
    • 10744224267 scopus 로고    scopus 로고
    • Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer disease: A pilot phase 2 clinical trial
    • Ritchie CW, Bush AI, Mackinnon A, Macfarlane S, Mastwyk M, MacGregor L, et al. Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer disease: a pilot phase 2 clinical trial. Arch Neurol 60: 1685-1691 (2003).
    • (2003) Arch Neurol , vol.60 , pp. 1685-1691
    • Ritchie, C.W.1    Bush, A.I.2    Mackinnon, A.3    Macfarlane, S.4    Mastwyk, M.5    MacGregor, L.6
  • 149
    • 48949098573 scopus 로고    scopus 로고
    • Safety, efficacy, and biomarker findings of PBT2 in targeting Aβ as a modifying therapy for Alzheimer's disease: A phase IIa, double-blind, randomised, placebo-controlled trial
    • Lannfelt L, Blennow K, Zetterberg H, Batsman S, Ames D, Harrison J, et al. Safety, efficacy, and biomarker findings of PBT2 in targeting Aβ as a modifying therapy for Alzheimer's disease: a phase IIa, double-blind, randomised, placebo-controlled trial. Lancet Neurol 8: 779-786 (2008).
    • (2008) Lancet Neurol , vol.8 , pp. 779-786
    • Lannfelt, L.1    Blennow, K.2    Zetterberg, H.3    Batsman, S.4    Ames, D.5    Harrison, J.6
  • 150
    • 46149107512 scopus 로고    scopus 로고
    • Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aβ
    • Adlard PA, Cherny RA, Finkelstein DI, Gautier E, Robb E, Cortes M, et al. Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Aβ. Neuron 59: 43-55 (2008).
    • (2008) Neuron , vol.59 , pp. 43-55
    • Adlard, P.A.1    Cherny, R.A.2    Finkelstein, D.I.3    Gautier, E.4    Robb, E.5    Cortes, M.6
  • 151
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid β peptide and inhibit aβ-induced toxicity
    • McLaurin J, Golomb R, Jurewicz A, Antel JP, Fraser PE. Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid β peptide and inhibit aβ-induced toxicity. J Biol Chem 275: 18495-18502 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 152
    • 33745922350 scopus 로고    scopus 로고
    • Cyclohexanehexol inhibitors of Aβ aggregation prevent and reverse Alzheimer phenotype in a mouse model
    • McLaurin J, Kierstead ME, Brown ME, Hawkes CA, Lambermon MH, Phinney AL, et al. Cyclohexanehexol inhibitors of Aβ aggregation prevent and reverse Alzheimer phenotype in a mouse model. Nat Med 12: 801-808 (2006).
    • (2006) Nat Med , vol.12 , pp. 801-808
    • McLaurin, J.1    Kierstead, M.E.2    Brown, M.E.3    Hawkes, C.A.4    Lambermon, M.H.5    Phinney, A.L.6
  • 153
    • 84889246801 scopus 로고    scopus 로고
    • National Institute on Aging, online, Available from URL:, Accessed 30 November 2008
    • National Institute on Aging. ELND005 in Patients With Mild to Moderate Alzheimer's Disease [online]. Available from URL: http://www.clinicaltrials.gov [Accessed 30 November 2008].
    • ELND005 in Patients With Mild to Moderate Alzheimer's Disease
  • 154
    • 33846054061 scopus 로고    scopus 로고
    • Disrupting β-amyloid aggregation for Alzheimer disease treatment
    • Estrada LD, Soto C. Disrupting β-amyloid aggregation for Alzheimer disease treatment. Curr Top Med Chem 7: 115-126 (2007).
    • (2007) Curr Top Med Chem , vol.7 , pp. 115-126
    • Estrada, L.D.1    Soto, C.2
  • 155
    • 38049056730 scopus 로고    scopus 로고
    • Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice
    • Martins IC, Kuperstein I, Wilkinson H, Maes E, Vanbrabant M, Jonckheere W, et al. Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J 27: 224-233 (2008).
    • (2008) EMBO J , vol.27 , pp. 224-233
    • Martins, I.C.1    Kuperstein, I.2    Wilkinson, H.3    Maes, E.4    Vanbrabant, M.5    Jonckheere, W.6
  • 156
    • 0011162190 scopus 로고
    • Selective loss of central cholinergic neurons in Alzheimer's disease
    • Davies P, Maloney AJ. Selective loss of central cholinergic neurons in Alzheimer's disease. Lancet 2: 1403 (1976).
    • (1976) Lancet , vol.2 , pp. 1403
    • Davies, P.1    Maloney, A.J.2
  • 158
    • 10244259208 scopus 로고    scopus 로고
    • The efficacy and safety of donepezil in patients with Alzheimer's disease: Results of a US multicentre, randomized, double-blind, placebo-controlled trial. The Donepezil Study Group
    • Rogers SL, Friedhoff LT. The efficacy and safety of donepezil in patients with Alzheimer's disease: results of a US multicentre, randomized, double-blind, placebo-controlled trial. The Donepezil Study Group. Dementia 7: 293-303 (1996).
    • (1996) Dementia , vol.7 , pp. 293-303
    • Rogers, S.L.1    Friedhoff, L.T.2


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