메뉴 건너뛰기




Volumn 13, Issue 11-12, 2009, Pages 4329-4348

Neuronal death in Alzheimer's disease and therapeutic opportunities

Author keywords

Alzheimer's disease; Amyloid plaques; Neurodegeneration; Neuronal death; Neuroprotection; Neurotoxicity

Indexed keywords

ALZHEIMER DISEASE; ANIMAL; ARTICLE; CELL DEATH; HUMAN; NERVE CELL; PATHOLOGY;

EID: 77951150250     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2009.00889.x     Document Type: Article
Times cited : (95)

References (258)
  • 1
    • 84881788235 scopus 로고    scopus 로고
    • Alzheimer's disease - opportunities to address pharmaceutical gaps
    • Kaplan W, Laing R. In, editors, Geneva (Switzerland), World Health Organization, pp
    • Tana S. Alzheimer's disease - opportunities to address pharmaceutical gaps. Priority medicines for Europe and the world - A public health approach to innovation 2004, 3-6. Kaplan WLaing R. In, editors, Geneva (Switzerland), World Health Organization, pp
    • (2004) Priority medicines for Europe and the world - A public health approach to innovation , pp. 3-6
    • Tana, S.1
  • 2
    • 33845892752 scopus 로고    scopus 로고
    • Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database
    • Bertram L, McQueen M, Mullin K. Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database. Nat Genet. 2007, 39:17-23.
    • (2007) Nat Genet. , vol.39 , pp. 17-23
    • Bertram, L.1    McQueen, M.2    Mullin, K.3    et al4
  • 3
    • 33845286140 scopus 로고    scopus 로고
    • Convergence of genes implicated in Alzheimer's disease on the cerebral cholesterol shuttle: APP, cholesterol, lipoproteins, and atherosclerosis
    • Carter C. Convergence of genes implicated in Alzheimer's disease on the cerebral cholesterol shuttle: APP, cholesterol, lipoproteins, and atherosclerosis. Neurochem Int. 2007, 50:12-38.
    • (2007) Neurochem Int. , vol.50 , pp. 12-38
    • Carter, C.1
  • 4
    • 0035081475 scopus 로고    scopus 로고
    • Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein
    • Selkoe D. Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein. J Alzheimers Dis. 2001, 3:75-80.
    • (2001) J Alzheimers Dis. , vol.3 , pp. 75-80
    • Selkoe, D.1
  • 5
    • 0036922942 scopus 로고    scopus 로고
    • Risk factors for Alzheimer's disease: role of multiple antioxidants, non-steroidal anti-inflammatory and cholinergic agents alone or in combination in prevention and treatment
    • Prasad K, Cole W, Prasad K. Risk factors for Alzheimer's disease: role of multiple antioxidants, non-steroidal anti-inflammatory and cholinergic agents alone or in combination in prevention and treatment. J Am Coll Nutr. 2002, 21:506-22.
    • (2002) J Am Coll Nutr. , vol.21 , pp. 506-522
    • Prasad, K.1    Cole, W.2    Prasad, K.3
  • 6
    • 0028896679 scopus 로고
    • Nonsteroidal anti-inflammatory drugs in Alzheimer's disease
    • Rich J, Rasmusson D, Folstein M. Nonsteroidal anti-inflammatory drugs in Alzheimer's disease. Neurology. 1995, 45:51-5.
    • (1995) Neurology. , vol.45 , pp. 51-55
    • Rich, J.1    Rasmusson, D.2    Folstein, M.3    et al4
  • 8
    • 0032479929 scopus 로고    scopus 로고
    • Complement-dependent proinflammatory properties of the Alzheimer's disease beta-peptide
    • Bradt B, Kolb W, Cooper N. Complement-dependent proinflammatory properties of the Alzheimer's disease beta-peptide. J Exp Med. 1998, 188:431-8.
    • (1998) J Exp Med. , vol.188 , pp. 431-438
    • Bradt, B.1    Kolb, W.2    Cooper, N.3
  • 9
    • 0029160270 scopus 로고
    • Delayed onset of Alzheimer's disease with nonsteroidal anti-inflammatory and histamine H2 blocking drugs
    • Breitner J, Welsh K, Helms M. Delayed onset of Alzheimer's disease with nonsteroidal anti-inflammatory and histamine H2 blocking drugs. Neurobiol Aging. 1995, 16:523-30.
    • (1995) Neurobiol Aging. , vol.16 , pp. 523-530
    • Breitner, J.1    Welsh, K.2    Helms, M.3    et al4
  • 10
    • 0028289083 scopus 로고
    • Inverse association of anti-inflammatory treatments and Alzheimer's disease: initial results of a co-twin control study
    • Breitner J, Gau B, Welsh K. Inverse association of anti-inflammatory treatments and Alzheimer's disease: initial results of a co-twin control study. Neurology. 1994, 44:227-32.
    • (1994) Neurology. , vol.44 , pp. 227-232
    • Breitner, J.1    Gau, B.2    Welsh, K.3    et al4
  • 11
    • 0029021217 scopus 로고
    • Do nonsteroidal anti-inflammatory drugs decrease the risk for Alzheimer's disease? The Rotterdam Study
    • Andersen K, Launer L, Ott A. Do nonsteroidal anti-inflammatory drugs decrease the risk for Alzheimer's disease? The Rotterdam Study. Neurology. 1995, 45:1441-5.
    • (1995) Neurology. , vol.45 , pp. 1441-1445
    • Andersen, K.1    Launer, L.2    Ott, A.3    et al4
  • 13
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • McGeer P, Schulzer M, McGeer E. Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies. Neurology. 1996, 47:425-32.
    • (1996) Neurology. , vol.47 , pp. 425-432
    • McGeer, P.1    Schulzer, M.2    McGeer, E.3
  • 14
    • 0027268393 scopus 로고
    • Clinical trial of indomethacin in Alzheimer's disease
    • Rogers J, Kirby L, Hempelman S. Clinical trial of indomethacin in Alzheimer's disease. Neurology. 1993, 43:1609-11.
    • (1993) Neurology. , vol.43 , pp. 1609-1611
    • Rogers, J.1    Kirby, L.2    Hempelman, S.3    et al4
  • 15
    • 0027161306 scopus 로고
    • Human astrocyte production of tumour necrosis factor-alpha, interleukin-1 beta, and interleukin-6 following exposure to lipopolysaccharide endotoxin
    • Sharif S, Hariri R, Chang V. Human astrocyte production of tumour necrosis factor-alpha, interleukin-1 beta, and interleukin-6 following exposure to lipopolysaccharide endotoxin. Neurol Res. 1993, 15:109-12.
    • (1993) Neurol Res. , vol.15 , pp. 109-112
    • Sharif, S.1    Hariri, R.2    Chang, V.3    et al4
  • 16
    • 0028341702 scopus 로고
    • Elevated interleukin-6 secretion levels by mononuclear cells of Alzheimer's patients
    • Shalit F, Sredni B, Stern L. Elevated interleukin-6 secretion levels by mononuclear cells of Alzheimer's patients. Neurosci Lett. 1994, 174:130-2.
    • (1994) Neurosci Lett. , vol.174 , pp. 130-132
    • Shalit, F.1    Sredni, B.2    Stern, L.3    et al4
  • 17
    • 65949124441 scopus 로고    scopus 로고
    • Implication of complement system and its regulators in Alzheimer's disease
    • Kolev M, Ruseva M, Harris C. Implication of complement system and its regulators in Alzheimer's disease. Curr Neuropharmacol. 2009, 7:1-8.
    • (2009) Curr Neuropharmacol. , vol.7 , pp. 1-8
    • Kolev, M.1    Ruseva, M.2    Harris, C.3    et al4
  • 18
    • 0028523134 scopus 로고
    • Free radicals on the mind. Hydrogen peroxide mediates amyloid beta protein toxicity
    • Anderton B. Free radicals on the mind. Hydrogen peroxide mediates amyloid beta protein toxicity. Hum Exp Toxicol. 1994, 13:716-9.
    • (1994) Hum Exp Toxicol. , vol.13 , pp. 716-719
    • Anderton, B.1
  • 19
    • 0028385744 scopus 로고
    • Regional brain activity of free radical defense enzymes in autopsy samples from patients with Alzheimer's disease and from nondemented controls
    • Chen L, Richardson J, Caldwell J. Regional brain activity of free radical defense enzymes in autopsy samples from patients with Alzheimer's disease and from nondemented controls. Int J Neurosci. 1994, 75:83-90.
    • (1994) Int J Neurosci. , vol.75 , pp. 83-90
    • Chen, L.1    Richardson, J.2    Caldwell, J.3    et al4
  • 20
    • 0024394987 scopus 로고
    • Microglial cells around amyloid plaques in Alzheimers disease express leukocyte adhesion molecules of the LFA-1 family
    • Rozemuller J, Eikelenboom P, Pals S. Microglial cells around amyloid plaques in Alzheimers disease express leukocyte adhesion molecules of the LFA-1 family. Neurosci Lett. 1989, 101:288-92.
    • (1989) Neurosci Lett. , vol.101 , pp. 288-292
    • Rozemuller, J.1    Eikelenboom, P.2    Pals, S.3    et al4
  • 21
    • 0028239387 scopus 로고
    • Accumulation of intercellular adhesion molecule-1 in senile plaques in brain tissue of patients with Alzheimers disease
    • Verbeek M, Otteholler I, Westphal J. Accumulation of intercellular adhesion molecule-1 in senile plaques in brain tissue of patients with Alzheimers disease. Am J Pathol. 1994, 144:104-16.
    • (1994) Am J Pathol. , vol.144 , pp. 104-116
    • Verbeek, M.1    Otteholler, I.2    Westphal, J.3    et al4
  • 22
    • 0031670924 scopus 로고    scopus 로고
    • Prostaglandins as putative neurotoxins in Alzheimer's disease
    • Prasad K, Hovland A, La Rosa F. Prostaglandins as putative neurotoxins in Alzheimer's disease. Proc Soc Exp Biol Med. 1998, 219:120-5.
    • (1998) Proc Soc Exp Biol Med. , vol.219 , pp. 120-125
    • Prasad, K.1    Hovland, A.2    La Rosa, F.3    et al4
  • 23
    • 0034948192 scopus 로고    scopus 로고
    • Inflammatory repertoire of Alzheimer's disease and nondemented elderly microglia in vitro
    • Lue L, Rydel R, Brigham E. Inflammatory repertoire of Alzheimer's disease and nondemented elderly microglia in vitro. Glia. 2001, 35:72-9.
    • (2001) Glia. , vol.35 , pp. 72-79
    • Lue, L.1    Rydel, R.2    Brigham, E.3    et al4
  • 24
    • 0036277146 scopus 로고    scopus 로고
    • Amyloid-beta-induced chemokine production in primary human macrophages and astrocytes
    • Smits H, Rijsmus A, van Loon J. Amyloid-beta-induced chemokine production in primary human macrophages and astrocytes. J Neuroimmunol. 2002, 127:160-8.
    • (2002) J Neuroimmunol. , vol.127 , pp. 160-168
    • Smits, H.1    Rijsmus, A.2    van Loon, J.3    et al4
  • 25
    • 0036546148 scopus 로고    scopus 로고
    • Noradrenergic depletion potentiates beta -amyloid-induced cortical inflammation: implications for Alzheimer's disease
    • Heneka M, Galea E, Gavriluyk V. Noradrenergic depletion potentiates beta -amyloid-induced cortical inflammation: implications for Alzheimer's disease. J Neurosci. 2002, 22:2434-42.
    • (2002) J Neurosci. , vol.22 , pp. 2434-2442
    • Heneka, M.1    Galea, E.2    Gavriluyk, V.3    et al4
  • 26
    • 0026631036 scopus 로고
    • The seminal role of beta-amyloid in the pathogenesis of Alzheimer disease
    • Joachim C, Selkoe D. The seminal role of beta-amyloid in the pathogenesis of Alzheimer disease. Alzheimer Dis Assoc Disord. 1992, 6:7-34.
    • (1992) Alzheimer Dis Assoc Disord. , vol.6 , pp. 7-34
    • Joachim, C.1    Selkoe, D.2
  • 27
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe D. Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu Rev Cell Biol. 1994, 10:373-403.
    • (1994) Annu Rev Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.1
  • 28
    • 0025937121 scopus 로고
    • Brain ubiquitin is markedly elevated in Alzheimer disease
    • Wang G, Khatoon S, Iqbal K. Brain ubiquitin is markedly elevated in Alzheimer disease. Brain Res. 1991, 566:146-51.
    • (1991) Brain Res. , vol.566 , pp. 146-151
    • Wang, G.1    Khatoon, S.2    Iqbal, K.3    et al4
  • 29
    • 0028013249 scopus 로고
    • Alzheimer disease: correlation of cerebro-spinal fluid and brain ubiquitin levels
    • Kudo T, Iqbal K, Ravid R. Alzheimer disease: correlation of cerebro-spinal fluid and brain ubiquitin levels. Brain Res. 1994, 639:1-7.
    • (1994) Brain Res. , vol.639 , pp. 1-7
    • Kudo, T.1    Iqbal, K.2    Ravid, R.3    et al4
  • 31
    • 0034652238 scopus 로고    scopus 로고
    • Proteasome inhibition in neuronal cells induces a proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE(2)
    • Rockwell P, Yuan H, Magnusson R. Proteasome inhibition in neuronal cells induces a proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE(2). Arch Biochem Biophys. 2000, 374:325-33.
    • (2000) Arch Biochem Biophys. , vol.374 , pp. 325-333
    • Rockwell, P.1    Yuan, H.2    Magnusson, R.3    et al4
  • 32
    • 0031026231 scopus 로고    scopus 로고
    • Binding of amyloid beta protein to the 20 S proteasome
    • Gregori L, Hainfeld J, Simon M. Binding of amyloid beta protein to the 20 S proteasome. J Biol Chem. 1997, 272:58-62.
    • (1997) J Biol Chem. , vol.272 , pp. 58-62
    • Gregori, L.1    Hainfeld, J.2    Simon, M.3    et al4
  • 33
    • 0034620481 scopus 로고    scopus 로고
    • Anti-inflammatory drugs and Alzheimer-type pathology in aging
    • Mackenzie I. Anti-inflammatory drugs and Alzheimer-type pathology in aging. Neurology. 2000, 54:732-4.
    • (2000) Neurology. , vol.54 , pp. 732-734
    • Mackenzie, I.1
  • 34
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity
    • Weggen S, Eriksen J, Das P. A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity. Nature. 2001, 414:212-6.
    • (2001) Nature. , vol.414 , pp. 212-216
    • Weggen, S.1    Eriksen, J.2    Das, P.3    et al4
  • 35
    • 1542300853 scopus 로고    scopus 로고
    • Neurones treated with cyclo-oxygenase-1 inhibitors are resistant to amyloid-beta1-42
    • Bate C, Veerhuis R, Eikelenboom P. Neurones treated with cyclo-oxygenase-1 inhibitors are resistant to amyloid-beta1-42. Neuroreport. 2003, 14:2099-103.
    • (2003) Neuroreport. , vol.14 , pp. 2099-2103
    • Bate, C.1    Veerhuis, R.2    Eikelenboom, P.3    et al4
  • 36
    • 42649084052 scopus 로고    scopus 로고
    • The role of interleukin-1 in neuroinflammation and Alzheimer disease: an evolving perspective
    • DOI
    • Shaftel S, Griffin W, O'Banion M. The role of interleukin-1 in neuroinflammation and Alzheimer disease: an evolving perspective. J Neuroinflammation 10.1186/1742-2094-5-7, DOI
    • J Neuroinflammation
    • Shaftel, S.1    Griffin, W.2    O'Banion, M.3
  • 37
    • 34548191207 scopus 로고    scopus 로고
    • Studies on brain volume, Alzheimer-related proteins and cytokines in mice with chronic overexpression of IL-1 receptor antagonist
    • Oprica M, Hjorth E, Spulber S. Studies on brain volume, Alzheimer-related proteins and cytokines in mice with chronic overexpression of IL-1 receptor antagonist. J Cell Mol Med. 2007, 11:810-25.
    • (2007) J Cell Mol Med. , vol.11 , pp. 810-825
    • Oprica, M.1    Hjorth, E.2    Spulber, S.3    et al4
  • 38
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • Selkoe D, Schenk D. Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics. Annu Rev Pharmacol Toxicol. 2003, 43:545-84.
    • (2003) Annu Rev Pharmacol Toxicol. , vol.43 , pp. 545-584
    • Selkoe, D.1    Schenk, D.2
  • 39
    • 0027963235 scopus 로고
    • Posttranslational modifications of tau in paired helical filaments
    • Morishima M, Ihara Y. Posttranslational modifications of tau in paired helical filaments. Dementia. 1994, 5:282-8.
    • (1994) Dementia. , vol.5 , pp. 282-288
    • Morishima, M.1    Ihara, Y.2
  • 40
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury P. Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci. 2003, 26:267-98.
    • (2003) Annu Rev Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.2
  • 41
    • 0029031348 scopus 로고
    • Apoptotic cell death induced by beta-amyloid(1-42) peptide is cell type dependent
    • Gschwind M, Huber G. Apoptotic cell death induced by beta-amyloid(1-42) peptide is cell type dependent. J Neurochem. 1995, 65:292-300.
    • (1995) J Neurochem. , vol.65 , pp. 292-300
    • Gschwind, M.1    Huber, G.2
  • 42
    • 42149140619 scopus 로고    scopus 로고
    • Regulation of betaAPP and PrPc cleavage by alpha-secretase: mechanistic and therapeutic perspectives
    • Vincent B, Cisse M, Sunyach C. Regulation of betaAPP and PrPc cleavage by alpha-secretase: mechanistic and therapeutic perspectives. Curr Alzheimer Res. 2008, 5:202-11.
    • (2008) Curr Alzheimer Res. , vol.5 , pp. 202-211
    • Vincent, B.1    Cisse, M.2    Sunyach, C.3    et al4
  • 43
    • 18844378852 scopus 로고    scopus 로고
    • Presenilin function and gamma-secretase activity
    • Brunkan A, Goate A. Presenilin function and gamma-secretase activity. J Neurochem. 2005, 93:769-92.
    • (2005) J Neurochem. , vol.93 , pp. 769-792
    • Brunkan, A.1    Goate, A.2
  • 44
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe M, Xia W, Ostaszewski B. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature. 1999, 398:513-7.
    • (1999) Nature. , vol.398 , pp. 513-517
    • Wolfe, M.1    Xia, W.2    Ostaszewski, B.3    et al4
  • 45
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex
    • De Strooper B. Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex. Neuron. 2003, 38:9-12.
    • (2003) Neuron. , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 46
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation
    • Haass C. Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation. EMBO J. 2004, 23:483-8.
    • (2004) EMBO J. , vol.23 , pp. 483-488
    • Haass, C.1
  • 47
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo
    • Borchelt D, Thinakaran G, Eckman C. Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo. Neuron. 1996, 17:1005-13.
    • (1996) Neuron. , vol.17 , pp. 1005-1013
    • Borchelt, D.1    Thinakaran, G.2    Eckman, C.3    et al4
  • 48
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev E, Sherrington R, Rogaeva E. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature. 1995, 376:775-8.
    • (1995) Nature. , vol.376 , pp. 775-778
    • Rogaev, E.1    Sherrington, R.2    Rogaeva, E.3    et al4
  • 49
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D, Eckman C, Jensen M. Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat Med. 1996, 2:864-70.
    • (1996) Nat Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    et al4
  • 50
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper B, Saftig P, Craessaerts K. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature. 1998, 391:387-90.
    • (1998) Nature. , vol.391 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Craessaerts, K.3    et al4
  • 51
    • 21144447065 scopus 로고    scopus 로고
    • Dissociated phenotypes in presenilin transgenic mice define functionally distinct gamma-secretases
    • Mastrangelo P, Mathews P, Chishti M. Dissociated phenotypes in presenilin transgenic mice define functionally distinct gamma-secretases. Proc Natl Acad Sci USA. 2005, 102:8972-7.
    • (2005) Proc Natl Acad Sci USA. , vol.102 , pp. 8972-8977
    • Mastrangelo, P.1    Mathews, P.2    Chishti, M.3    et al4
  • 52
    • 23044524091 scopus 로고    scopus 로고
    • Neurons bearing presenilins: weapons for defense or suicide
    • Popescu B, Ankarcrona M. Neurons bearing presenilins: weapons for defense or suicide. J Cell Mol Med. 2000, 4:249-61.
    • (2000) J Cell Mol Med. , vol.4 , pp. 249-261
    • Popescu, B.1    Ankarcrona, M.2
  • 54
    • 1542377619 scopus 로고    scopus 로고
    • Toxicity of amyloid beta peptide: Tales of calcium, mitochondria, and oxidative stress
    • Canevari L, Abramov A, Duchen M. Toxicity of amyloid beta peptide: Tales of calcium, mitochondria, and oxidative stress. Neurochem Res. 2004, 29:637-50.
    • (2004) Neurochem Res. , vol.29 , pp. 637-650
    • Canevari, L.1    Abramov, A.2    Duchen, M.3
  • 55
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat Rev Neurosci. 2002, 3:862-72.
    • (2002) Nat Rev Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.1
  • 56
    • 0035478618 scopus 로고    scopus 로고
    • Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima Y, Gotoh Y, Zieg J. beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. J Neurosci. 2001, 21:7551-60.
    • (2001) J Neurosci. , vol.21 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    et al4
  • 57
    • 0034682414 scopus 로고    scopus 로고
    • Neurotoxicity induces cleavage of p35 to p25 by calpain
    • Lee M, Kwon Y, Li M. Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature. 2000, 405:360-4.
    • (2000) Nature. , vol.405 , pp. 360-364
    • Lee, M.1    Kwon, Y.2    Li, M.3    et al4
  • 58
    • 0035019371 scopus 로고    scopus 로고
    • CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with A beta-induced cortical neuron apoptosis
    • Bozyczko-Coyne D, O'Kane T, Wu Z. CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with A beta-induced cortical neuron apoptosis. J Neurochem. 2001, 77:849-63.
    • (2001) J Neurochem. , vol.77 , pp. 849-863
    • Bozyczko-Coyne, D.1    O'Kane, T.2    Wu, Z.3    et al4
  • 59
    • 0033635302 scopus 로고    scopus 로고
    • Effect of apolipoprotein E allele epsilon 4 on the initial phase of amyloid beta-protein accumulation in the human brain
    • Morishima-Kawashima M, Oshima N, Ogata H. Effect of apolipoprotein E allele epsilon 4 on the initial phase of amyloid beta-protein accumulation in the human brain. Am J Pathol. 2000, 157:2093-9.
    • (2000) Am J Pathol. , vol.157 , pp. 2093-2099
    • Morishima-Kawashima, M.1    Oshima, N.2    Ogata, H.3    et al4
  • 60
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of A beta(1-42) in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke L, Masliah E, Yu G. High-level neuronal expression of A beta(1-42) in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation. J Neurosci. 2000, 20:4050-8.
    • (2000) J Neurosci. , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.3    et al4
  • 61
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • Lue L, Kuo Y, Roher A. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Pathol. 1999, 155:853-62.
    • (1999) Am J Pathol. , vol.155 , pp. 853-862
    • Lue, L.1    Kuo, Y.2    Roher, A.3    et al4
  • 62
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis - Detection of a protofibrillar intermediate
    • Walsh D, Lomakin A, Benedek G. Amyloid beta-protein fibrillogenesis - Detection of a protofibrillar intermediate. J Biol Chem. 1997, 272:22364-72.
    • (1997) J Biol Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.1    Lomakin, A.2    Benedek, G.3    et al4
  • 63
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert M, Barlow A, Chromy B. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA. 1998, 95:6448-53.
    • (1998) Proc Natl Acad Sci USA. , vol.95 , pp. 6448-6453
    • Lambert, M.1    Barlow, A.2    Chromy, B.3    et al4
  • 64
    • 0037059598 scopus 로고    scopus 로고
    • Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
    • Wang H, Pasternak J, Kuo H. Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Res. 2002, 924:133-40.
    • (2002) Brain Res. , vol.924 , pp. 133-140
    • Wang, H.1    Pasternak, J.2    Kuo, H.3    et al4
  • 65
    • 0035993237 scopus 로고    scopus 로고
    • Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets
    • Klein W. Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem Int. 2002, 41:345-52.
    • (2002) Neurochem Int. , vol.41 , pp. 345-352
    • Klein, W.1
  • 66
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar G, Li S, Mehta T. Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med. 2008, 14:837-42.
    • (2008) Nat Med. , vol.14 , pp. 837-842
    • Shankar, G.1    Li, S.2    Mehta, T.3    et al4
  • 67
    • 58049203021 scopus 로고    scopus 로고
    • Is covalently crosslinked Abeta responsible for synaptotoxicity in Alzheimer's disease
    • Naylor R, Hill A, Barnham K. Is covalently crosslinked Abeta responsible for synaptotoxicity in Alzheimer's disease. Curr Alzheimer Res. 2008, 5:533-9.
    • (2008) Curr Alzheimer Res. , vol.5 , pp. 533-539
    • Naylor, R.1    Hill, A.2    Barnham, K.3
  • 68
    • 0034266604 scopus 로고    scopus 로고
    • Therapeutic inhibition of the complement system. Y2K update
    • Asghar S, Pasch M. Therapeutic inhibition of the complement system. Y2K update. Front Biosci 2000, 5:E63-81.
    • (2000) Front Biosci , vol.5
    • Asghar, S.1    Pasch, M.2
  • 69
    • 0021924975 scopus 로고
    • Local immunoglobulin synthesis and blood-brain barrier assessment in subacute sclerosing panencephalitis
    • Silva C, Rio M, Cruz C. Local immunoglobulin synthesis and blood-brain barrier assessment in subacute sclerosing panencephalitis. Eur Neurol. 1985, 24:128-33.
    • (1985) Eur Neurol. , vol.24 , pp. 128-133
    • Silva, C.1    Rio, M.2    Cruz, C.3
  • 70
    • 0029079605 scopus 로고
    • Complement biosynthesis in the central nervous system
    • Barnum S. Complement biosynthesis in the central nervous system. Crit Rev Oral Biol Med. 1995, 6:132-46.
    • (1995) Crit Rev Oral Biol Med. , vol.6 , pp. 132-146
    • Barnum, S.1
  • 72
    • 0029053689 scopus 로고
    • Complement expression in human brain - biosynthesis of terminal pathway components and regulators in human glial cells and cell lines
    • Gasque P, Fontaine M, Morgan B. Complement expression in human brain - biosynthesis of terminal pathway components and regulators in human glial cells and cell lines. J Immunol. 1995, 154:4726-33.
    • (1995) J Immunol. , vol.154 , pp. 4726-4733
    • Gasque, P.1    Fontaine, M.2    Morgan, B.3
  • 73
    • 0028068672 scopus 로고
    • The expression of CD59 in normal human nervos tissue
    • Vedeler C, Ulvestad E, Bjorge L. The expression of CD59 in normal human nervos tissue. Immunol. 1994, 82:542-7.
    • (1994) Immunol. , vol.82 , pp. 542-547
    • Vedeler, C.1    Ulvestad, E.2    Bjorge, L.3    et al4
  • 74
    • 0028137807 scopus 로고
    • Clusterin (SGP-2) - a multifunctional glycoprotein with regional expression in astrocytes and neurons of the adult rat brain
    • Pasinetti G, Johnson S, Oda T. Clusterin (SGP-2) - a multifunctional glycoprotein with regional expression in astrocytes and neurons of the adult rat brain. J Comp Neurol. 1994, 339:387-400.
    • (1994) J Comp Neurol. , vol.339 , pp. 387-400
    • Pasinetti, G.1    Johnson, S.2    Oda, T.3    et al4
  • 75
    • 0034667686 scopus 로고    scopus 로고
    • Deficiency of complement defense protein CD59 may contribute to neurodegeneration in Alzheimer's disease
    • Yang L, Li R, Meri S, Rogers J. Deficiency of complement defense protein CD59 may contribute to neurodegeneration in Alzheimer's disease. J Neurosci. 2000, 20:7505-9.
    • (2000) J Neurosci. , vol.20 , pp. 7505-7509
    • Yang, L.1    Li, R.2    Meri, S.3    Rogers, J.4    et al5
  • 76
    • 0033562337 scopus 로고    scopus 로고
    • Complement-derived anaphylatoxin C5a protects against glutamate-mediated neurotoxicity
    • Osaka H, Mukherjee P, Aisen P. Complement-derived anaphylatoxin C5a protects against glutamate-mediated neurotoxicity. J Cell Biochem. 1999, 73:303-11.
    • (1999) J Cell Biochem. , vol.73 , pp. 303-311
    • Osaka, H.1    Mukherjee, P.2    Aisen, P.3    et al4
  • 77
    • 0030250826 scopus 로고    scopus 로고
    • Inflammatory mechanisms in neurodegeneration and Alzheimer's disease: the role of the complement system
    • Pasinetti G. Inflammatory mechanisms in neurodegeneration and Alzheimer's disease: the role of the complement system. Neurobiol Aging. 1996, 17:707-16.
    • (1996) Neurobiol Aging. , vol.17 , pp. 707-716
    • Pasinetti, G.1
  • 78
    • 0036679142 scopus 로고    scopus 로고
    • Prominent neurodegeneration and increased plaque formation in complement-inhibited Alzheimer's mice
    • Wyss-Coray T, Yan F, Lin A. Prominent neurodegeneration and increased plaque formation in complement-inhibited Alzheimer's mice. Proc Natl Acad Sci USA. 2002, 99:10837-42.
    • (2002) Proc Natl Acad Sci USA. , vol.99 , pp. 10837-10842
    • Wyss-Coray, T.1    Yan, F.2    Lin, A.3    et al4
  • 79
    • 38049107388 scopus 로고    scopus 로고
    • Complement component C1q inhibits beta-amyloid- and serum amyloid P-induced neurotoxicity via caspase- and calpain-independent mechanisms
    • Pisalyaput K, Tenner A. Complement component C1q inhibits beta-amyloid- and serum amyloid P-induced neurotoxicity via caspase- and calpain-independent mechanisms. J Neurochem. 2008, 104:696-707.
    • (2008) J Neurochem. , vol.104 , pp. 696-707
    • Pisalyaput, K.1    Tenner, A.2
  • 80
    • 46749087854 scopus 로고    scopus 로고
    • Complement C3 deficiency leads to accelerated amyloid beta plaque deposition and neurodegeneration and modulation of the microglia/macrophage phenotype in amyloid precursor protein transgenic mice
    • Maier M, Peng Y, Jiang L. Complement C3 deficiency leads to accelerated amyloid beta plaque deposition and neurodegeneration and modulation of the microglia/macrophage phenotype in amyloid precursor protein transgenic mice. J Neurosci. 2008, 28:6333-41.
    • (2008) J Neurosci. , vol.28 , pp. 6333-6341
    • Maier, M.1    Peng, Y.2    Jiang, L.3    et al4
  • 81
    • 0029896853 scopus 로고    scopus 로고
    • Complement activation on human neuroblastoma cell lines in vitro: route of activation and expression of functional complement regulatory proteins
    • Gasque P, Thomas A, Fontaine M. Complement activation on human neuroblastoma cell lines in vitro: route of activation and expression of functional complement regulatory proteins. J Neuroimmunol. 1996, 66:29-40.
    • (1996) J Neuroimmunol. , vol.66 , pp. 29-40
    • Gasque, P.1    Thomas, A.2    Fontaine, M.3    et al4
  • 82
    • 0030967165 scopus 로고    scopus 로고
    • A controlled trial of selegiline, alpha-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study
    • Sano M, Ernesto C, Thomas R. A controlled trial of selegiline, alpha-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study. N Engl J Med. 1997, 336:1216-22.
    • (1997) N Engl J Med. , vol.336 , pp. 1216-1222
    • Sano, M.1    Ernesto, C.2    Thomas, R.3    et al4
  • 83
    • 0013249832 scopus 로고    scopus 로고
    • Coenzyme nicotinamide adenine dinucleotide: new therapeutic approach for improving dementia of the Alzheimer type
    • Birkmayer J. Coenzyme nicotinamide adenine dinucleotide: new therapeutic approach for improving dementia of the Alzheimer type. Ann Clin Lab Sci. 1996, 26:1-9.
    • (1996) Ann Clin Lab Sci. , vol.26 , pp. 1-9
    • Birkmayer, J.1
  • 84
    • 0034643895 scopus 로고    scopus 로고
    • Oxidative stress induces intracellular accumulation of amyloid beta-protein (A beta) in human neuroblastoma cells
    • Misonou H, Morishima-Kawashima M. Oxidative stress induces intracellular accumulation of amyloid beta-protein (A beta) in human neuroblastoma cells. Biochemistry. 2000, 39:6951-9.
    • (2000) Biochemistry. , vol.39 , pp. 6951-6959
    • Misonou, H.1    Morishima-Kawashima, M.2    et al3
  • 85
    • 0034663858 scopus 로고    scopus 로고
    • Accelerated accumulation of amyloid beta proteins on oxidatively damaged lipid membranes
    • Koppaka V, Axelsen P. Accelerated accumulation of amyloid beta proteins on oxidatively damaged lipid membranes. Biochemistry. 2000, 39:10011-6.
    • (2000) Biochemistry. , vol.39 , pp. 10011-10016
    • Koppaka, V.1    Axelsen, P.2
  • 86
    • 0028957882 scopus 로고
    • Amyloid peptides are toxic via a common oxidative mechanism
    • Schubert D, Behl C, Lesley R. Amyloid peptides are toxic via a common oxidative mechanism. Proc Natl Acad Sci USA. 1995, 92:1989-93.
    • (1995) Proc Natl Acad Sci USA. , vol.92 , pp. 1989-1993
    • Schubert, D.1    Behl, C.2    Lesley, R.3    et al4
  • 87
    • 0027129818 scopus 로고
    • Vitamin E protects nerve cells from amyloid beta protein toxicity
    • Behl C, Davis J, Cole G. Vitamin E protects nerve cells from amyloid beta protein toxicity. Biochem Biophys Res Commun. 1992, 186:944-50.
    • (1992) Biochem Biophys Res Commun. , vol.186 , pp. 944-950
    • Behl, C.1    Davis, J.2    Cole, G.3    et al4
  • 88
    • 0026547646 scopus 로고
    • Plasma concentrations of vitamin E and carotenoids in Alzheimers disease
    • Zaman Z, Roche S, Fielden P. Plasma concentrations of vitamin E and carotenoids in Alzheimers disease. Age Ageing. 1992, 21:91-4.
    • (1992) Age Ageing. , vol.21 , pp. 91-94
    • Zaman, Z.1    Roche, S.2    Fielden, P.3    et al4
  • 89
    • 0021064115 scopus 로고
    • Metabolic processes in Alzheimers disease adenine nucleotide content and production of (CO2)-C-14 from [U-C-14] glucose in vitro in human neocortex
    • Sims N, Bowen D, Neary D. Metabolic processes in Alzheimers disease adenine nucleotide content and production of (CO2)-C-14 from [U-C-14] glucose in vitro in human neocortex. J Neurochem. 1983, 41:1329-34.
    • (1983) J Neurochem. , vol.41 , pp. 1329-1334
    • Sims, N.1    Bowen, D.2    Neary, D.3    et al4
  • 90
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease - a potential molecular basis for neuronal degeneration
    • Saito K, Elce J, Hamos J. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease - a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci USA. 1993, 90:2628-32.
    • (1993) Proc Natl Acad Sci USA. , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.2    Hamos, J.3    et al4
  • 91
    • 0029159829 scopus 로고
    • Free radical formation in autopsy samples of Alzheimer and control cortex
    • Zhou Y, Richardson J, Mombourquette M. Free radical formation in autopsy samples of Alzheimer and control cortex. Neurosci Lett. 1995, 195:89-92.
    • (1995) Neurosci Lett. , vol.195 , pp. 89-92
    • Zhou, Y.1    Richardson, J.2    Mombourquette, M.3    et al4
  • 92
    • 0033834306 scopus 로고    scopus 로고
    • NNOS expression in reactive astrocytes correlates with increased cell death related DNA damage in the hippocampus and entorhinal cortex in Alzheimer's disease
    • Simic G, Lucassen P, Krsnik Z. nNOS expression in reactive astrocytes correlates with increased cell death related DNA damage in the hippocampus and entorhinal cortex in Alzheimer's disease. Exp Neurol. 2000, 165:12-26.
    • (2000) Exp Neurol. , vol.165 , pp. 12-26
    • Simic, G.1    Lucassen, P.2    Krsnik, Z.3    et al4
  • 94
    • 0034663662 scopus 로고    scopus 로고
    • Proteasome inhibition results in increased poly-ADP-ribosylation: Implications for neuron death
    • Keller J, Markesbery W. Proteasome inhibition results in increased poly-ADP-ribosylation: Implications for neuron death. J Neurosci Res. 2000, 61:436-42.
    • (2000) J Neurosci Res. , vol.61 , pp. 436-442
    • Keller, J.1    Markesbery, W.2
  • 95
    • 0000991680 scopus 로고    scopus 로고
    • Proteasome inhibitors induce cytochrome c-caspase-3-like protease-mediated apoptosis in cultured cortical neurons
    • Qiu J, Asai A, Chi S. Proteasome inhibitors induce cytochrome c-caspase-3-like protease-mediated apoptosis in cultured cortical neurons. J Neurosci. 2000, 20:259-65.
    • (2000) J Neurosci. , vol.20 , pp. 259-265
    • Qiu, J.1    Asai, A.2    Chi, S.3    et al4
  • 96
    • 0342393043 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells
    • Pasquini L, Moreno M, Adamo A. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells. J Neurosci Res. 2000, 59:601-11.
    • (2000) J Neurosci Res. , vol.59 , pp. 601-611
    • Pasquini, L.1    Moreno, M.2    Adamo, A.3    et al4
  • 97
    • 0033773607 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced apoptosis of glioma cells involves the processing of multiple caspases and cytochrome c release
    • Wagenknecht B, Hermisson M, Groscurth P. Proteasome inhibitor-induced apoptosis of glioma cells involves the processing of multiple caspases and cytochrome c release. J Neurochem. 2000, 75:2288-97.
    • (2000) J Neurochem. , vol.75 , pp. 2288-2297
    • Wagenknecht, B.1    Hermisson, M.2    Groscurth, P.3    et al4
  • 98
    • 0032536516 scopus 로고    scopus 로고
    • Central nervous system DNA fragmentation induced by the inhibition of nuclear factor kappa B
    • Taglialatela G, Kaufmann J, Trevino A. Central nervous system DNA fragmentation induced by the inhibition of nuclear factor kappa B. Neuroreport. 1998, 9:489-93.
    • (1998) Neuroreport. , vol.9 , pp. 489-493
    • Taglialatela, G.1    Kaufmann, J.2    Trevino, A.3    et al4
  • 99
    • 0033038942 scopus 로고    scopus 로고
    • Proteasome inhibitors induce mitochondria-independent apoptosis in human glioma cells
    • Kitagawa H, Tani E, Ikemoto H. Proteasome inhibitors induce mitochondria-independent apoptosis in human glioma cells. FEBS Lett. 1999, 443:181-6.
    • (1999) FEBS Lett. , vol.443 , pp. 181-186
    • Kitagawa, H.1    Tani, E.2    Ikemoto, H.3    et al4
  • 100
    • 0031022252 scopus 로고    scopus 로고
    • Proteasome contributes to the alpha-secretase pathway of amyloid precursor protein in human cells
    • Marambaud P, Chevallier N, Barelli H. Proteasome contributes to the alpha-secretase pathway of amyloid precursor protein in human cells. J Neurochem. 1997, 68:698-703.
    • (1997) J Neurochem. , vol.68 , pp. 698-703
    • Marambaud, P.1    Chevallier, N.2    Barelli, H.3    et al4
  • 101
    • 0034142022 scopus 로고    scopus 로고
    • A distinct ER/IC gamma-secretase competes with the proteasome for cleavage of APP
    • Skovronsky D, Pijak D, Doms R. A distinct ER/IC gamma-secretase competes with the proteasome for cleavage of APP. Biochemistry. 2000, 39:810-7.
    • (2000) Biochemistry. , vol.39 , pp. 810-817
    • Skovronsky, D.1    Pijak, D.2    Doms, R.3    et al4
  • 102
    • 0032925297 scopus 로고    scopus 로고
    • Dual roles of proteasome in the metabolism of presenilin 1
    • Honda T, Yasutake K, Nihonmatsu N. Dual roles of proteasome in the metabolism of presenilin 1. J Neurochem. 1999, 72:255-61.
    • (1999) J Neurochem. , vol.72 , pp. 255-261
    • Honda, T.1    Yasutake, K.2    Nihonmatsu, N.3    et al4
  • 103
    • 0034531674 scopus 로고    scopus 로고
    • Cytoplasmic presenilin aggregates in proteasome inhibitor-treated cells
    • Ingano L, Lentini K, Kovacs I. Cytoplasmic presenilin aggregates in proteasome inhibitor-treated cells. Mol Basis Dementia. 2000, 920:259-60.
    • (2000) Mol Basis Dementia. , vol.920 , pp. 259-260
    • Ingano, L.1    Lentini, K.2    Kovacs, I.3    et al4
  • 104
    • 0025760931 scopus 로고
    • Multicatalytic proteinase is present in Lewy bodies and neurofibrillary tangles in diffuse Lewy body disease brains
    • Kwak S, Masaki T, Ishiura S. Multicatalytic proteinase is present in Lewy bodies and neurofibrillary tangles in diffuse Lewy body disease brains. Neurosci Lett. 1991, 128:21-4.
    • (1991) Neurosci Lett. , vol.128 , pp. 21-24
    • Kwak, S.1    Masaki, T.2    Ishiura, S.3    et al4
  • 105
    • 0028297514 scopus 로고
    • Multicatalytic proteinsase is associated with characteristic oval structures in cortical Lewy bodies - an immunocytochemical study with light and electron microscopy
    • Masaki T, Ishiura S, Sugita H. Multicatalytic proteinsase is associated with characteristic oval structures in cortical Lewy bodies - an immunocytochemical study with light and electron microscopy. J Neurol Sci. 1994, 122:127-34.
    • (1994) J Neurol Sci. , vol.122 , pp. 127-134
    • Masaki, T.1    Ishiura, S.2    Sugita, H.3    et al4
  • 106
    • 0034651104 scopus 로고    scopus 로고
    • Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis
    • Canu N, Barbato C, Ciotti M. Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis. J Neurosci. 2000, 20:589-99.
    • (2000) J Neurosci. , vol.20 , pp. 589-599
    • Canu, N.1    Barbato, C.2    Ciotti, M.3    et al4
  • 107
    • 0033845065 scopus 로고    scopus 로고
    • Prevention of beta-amyloid neurotoxicity by blockade of the ubiquitin-proteasome proteolytic pathway
    • Favit A, Grimaldi M, Alkon D. Prevention of beta-amyloid neurotoxicity by blockade of the ubiquitin-proteasome proteolytic pathway. J Neurochem. 2000, 75:1258-63.
    • (2000) J Neurochem. , vol.75 , pp. 1258-1263
    • Favit, A.1    Grimaldi, M.2    Alkon, D.3
  • 108
    • 0032944799 scopus 로고    scopus 로고
    • Possible role of NF-kappa B and p53 in the glutamate-induced pro-apoptotic neuronal pathway
    • Grilli M, Memo M. Possible role of NF-kappa B and p53 in the glutamate-induced pro-apoptotic neuronal pathway. Cell Death Differ. 1999, 6:22-7.
    • (1999) Cell Death Differ. , vol.6 , pp. 22-27
    • Grilli, M.1    Memo, M.2
  • 109
    • 0033979815 scopus 로고    scopus 로고
    • Roles of nuclear factor kappa B in neuronal survival and plasticity
    • Mattson M, Culmsee C, Yu Z. Roles of nuclear factor kappa B in neuronal survival and plasticity. J Neurochem. 2000, 74:443-56.
    • (2000) J Neurochem. , vol.74 , pp. 443-456
    • Mattson, M.1    Culmsee, C.2    Yu, Z.3    et al4
  • 110
    • 0032568552 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits the generation of beta-amyloid in hippocampal neurons
    • Simons M, Keller P, De Strooper B. Cholesterol depletion inhibits the generation of beta-amyloid in hippocampal neurons. Proc Natl Acad Sci USA. 1998, 95:6460-4.
    • (1998) Proc Natl Acad Sci USA. , vol.95 , pp. 6460-6464
    • Simons, M.1    Keller, P.2    De Strooper, B.3    et al4
  • 111
    • 0033833354 scopus 로고    scopus 로고
    • Hypercholesterolemia accelerates the Alzheimer's amyloid pathology in a transgenic mouse model
    • Refolo L, Pappolla M, Malester B. Hypercholesterolemia accelerates the Alzheimer's amyloid pathology in a transgenic mouse model. Neurobiol Disease. 2000, 7:321-31.
    • (2000) Neurobiol Disease. , vol.7 , pp. 321-331
    • Refolo, L.1    Pappolla, M.2    Malester, B.3    et al4
  • 112
    • 0035160066 scopus 로고    scopus 로고
    • A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease
    • Refolo L, Pappolla M, LaFrancois J. A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease. Neurobiol Disease. 2001, 8:890-9.
    • (2001) Neurobiol Disease. , vol.8 , pp. 890-899
    • Refolo, L.1    Pappolla, M.2    LaFrancois, J.3    et al4
  • 113
    • 0028177562 scopus 로고
    • Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol
    • Sparks D, Scheff S, Hunsaker J. Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol. Exp Neurol. 1994, 126:88-94.
    • (1994) Exp Neurol. , vol.126 , pp. 88-94
    • Sparks, D.1    Scheff, S.2    Hunsaker, J.3    et al4
  • 114
    • 0029888944 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid immunoreactivity in the CNS
    • Sparks D. Intraneuronal beta-amyloid immunoreactivity in the CNS. Neurobiol Aging. 1996, 17:291-9.
    • (1996) Neurobiol Aging. , vol.17 , pp. 291-299
    • Sparks, D.1
  • 116
    • 33645826914 scopus 로고    scopus 로고
    • Relationship between Helicobacter pylori infection and Alzheimer disease
    • Kountouras J, Tsolaki M, Gavalas E. Relationship between Helicobacter pylori infection and Alzheimer disease. Neurology. 2006, 66:938-40.
    • (2006) Neurology. , vol.66 , pp. 938-940
    • Kountouras, J.1    Tsolaki, M.2    Gavalas, E.3    et al4
  • 117
    • 2542448088 scopus 로고    scopus 로고
    • Infiltration of the brain by pathogens causes Alzheimer's disease
    • Itzhaki R, Wozniak M, Appelt D. Infiltration of the brain by pathogens causes Alzheimer's disease. Neurobiol Aging. 2004, 25:619-27.
    • (2004) Neurobiol Aging. , vol.25 , pp. 619-627
    • Itzhaki, R.1    Wozniak, M.2    Appelt, D.3    et al4
  • 118
    • 33747384279 scopus 로고    scopus 로고
    • The essential lesion of Alzheimer disease: a surprise in retrospect
    • Ball M. The essential lesion of Alzheimer disease: a surprise in retrospect. J Alzheimers Dis. 2006, 9:29-33.
    • (2006) J Alzheimers Dis. , vol.9 , pp. 29-33
    • Ball, M.1
  • 119
    • 31644446108 scopus 로고    scopus 로고
    • Herpes simplex virus type 1, apolipoprotein E, and cholesterol: a dangerous liaison in Alzheimer's disease and other disorders
    • Itzhaki R, Wozniak M. Herpes simplex virus type 1, apolipoprotein E, and cholesterol: a dangerous liaison in Alzheimer's disease and other disorders. Prog Lipid Res. 2006, 45:73-90.
    • (2006) Prog Lipid Res. , vol.45 , pp. 73-90
    • Itzhaki, R.1    Wozniak, M.2
  • 120
    • 24144470801 scopus 로고    scopus 로고
    • Herpes simplex virus interferes with amyloid precursor protein processing
    • DOI
    • Shipley S, Parkin E, Itzhaki R. Herpes simplex virus interferes with amyloid precursor protein processing. BMC Microbiol 10.1186/1471-2180-5-48, DOI
    • BMC Microbiol
    • Shipley, S.1    Parkin, E.2    Itzhaki, R.3    et al4
  • 121
    • 2542424286 scopus 로고    scopus 로고
    • Fast anterograde transport of herpes simplex virus: role for the amyloid precursor protein of Alzheimer's disease
    • Satpute-Krishnan P, DeGiorgis J. Fast anterograde transport of herpes simplex virus: role for the amyloid precursor protein of Alzheimer's disease. Aging Cell. 2003, 2:305-18.
    • (2003) Aging Cell. , vol.2 , pp. 305-318
    • Satpute-Krishnan, P.1    DeGiorgis, J.2    et al3
  • 122
    • 36348931527 scopus 로고    scopus 로고
    • Herpes simplex virus infection causes cellular beta-amyloid accumulation and secretase upregulation
    • Wozniak M, Itzhaki R, Shipley S. Herpes simplex virus infection causes cellular beta-amyloid accumulation and secretase upregulation. Neurosci Lett. 2007, 429:95-100.
    • (2007) Neurosci Lett. , vol.429 , pp. 95-100
    • Wozniak, M.1    Itzhaki, R.2    Shipley, S.3    et al4
  • 123
    • 0021325636 scopus 로고
    • Alzheimer's disease: a study of epidemiological aspects
    • Heyman A, Wilkinson W, Stafford J. Alzheimer's disease: a study of epidemiological aspects. Ann Neurol. 1984, 15:335-41.
    • (1984) Ann Neurol. , vol.15 , pp. 335-341
    • Heyman, A.1    Wilkinson, W.2    Stafford, J.3    et al4
  • 124
    • 0021986226 scopus 로고
    • A case-control study of dementia of the Alzheimer type
    • French L, Schuman L, Mortimer J. A case-control study of dementia of the Alzheimer type. Am J Epidemiol. 1985, 121:414-21.
    • (1985) Am J Epidemiol. , vol.121 , pp. 414-421
    • French, L.1    Schuman, L.2    Mortimer, J.3    et al4
  • 125
    • 0025913996 scopus 로고
    • Head trauma as a risk factor for Alzheimer's disease: a collaborative re-analysis of case-control studies
    • EURODEM Risk Factors Research Group
    • Mortimer J, van Duijn C, Chandra V. Head trauma as a risk factor for Alzheimer's disease: a collaborative re-analysis of case-control studies. Int J Epidemiol 1991, 20:S28-35. EURODEM Risk Factors Research Group
    • (1991) Int J Epidemiol , vol.20
    • Mortimer, J.1    van Duijn, C.2    Chandra, V.3    et al4
  • 127
    • 0032910645 scopus 로고    scopus 로고
    • Prevalence and risks of dementia in the Japanese population: RERF's adult health study Hiroshima subjects. Radiation Effects Research Foundation
    • Yamada M, Sasaki H, Mimori Y. Prevalence and risks of dementia in the Japanese population: RERF's adult health study Hiroshima subjects. Radiation Effects Research Foundation. J Am Geriatr Soc. 1999, 47:189-95.
    • (1999) J Am Geriatr Soc. , vol.47 , pp. 189-195
    • Yamada, M.1    Sasaki, H.2    Mimori, Y.3    et al4
  • 128
    • 0025872497 scopus 로고
    • Latent herpes simplex virus type 1 in normal and Alzheimer's disease brains
    • Jamieson G, Maitland N, Wilcock G. Latent herpes simplex virus type 1 in normal and Alzheimer's disease brains. J Med Virol. 1991, 33:224-7.
    • (1991) J Med Virol. , vol.33 , pp. 224-227
    • Jamieson, G.1    Maitland, N.2    Wilcock, G.3    et al4
  • 129
    • 0029791629 scopus 로고    scopus 로고
    • Neurotropic viruses and Alzheimer disease. Interaction of herpes simplex type 1 virus and apolipoprotein E in the etiology of the disease
    • Lin W, Shang D, Itzhaki R. Neurotropic viruses and Alzheimer disease. Interaction of herpes simplex type 1 virus and apolipoprotein E in the etiology of the disease. Mol Chem Neuropathol. 1996, 28:135-41.
    • (1996) Mol Chem Neuropathol. , vol.28 , pp. 135-141
    • Lin, W.1    Shang, D.2    Itzhaki, R.3
  • 130
    • 0033523873 scopus 로고    scopus 로고
    • A prospective study of new infections with herpes simplex virus type 1 and type 2. Chiron HSV Vaccine Study Group
    • Langenberg A, Corey L, Ashley R. A prospective study of new infections with herpes simplex virus type 1 and type 2. Chiron HSV Vaccine Study Group. N Engl J Med. 1999, 341:1432-8.
    • (1999) N Engl J Med. , vol.341 , pp. 1432-1438
    • Langenberg, A.1    Corey, L.2    Ashley, R.3    et al4
  • 131
    • 7944226843 scopus 로고    scopus 로고
    • Statins lower the risk of developing Alzheimer's disease by limiting lipid raft endocytosis and decreasing the neuronal spread of Herpes simplex virus type 1
    • Hill J, Steiner I, Matthews K. Statins lower the risk of developing Alzheimer's disease by limiting lipid raft endocytosis and decreasing the neuronal spread of Herpes simplex virus type 1. Med Hypotheses. 2005, 64:53-8.
    • (2005) Med Hypotheses. , vol.64 , pp. 53-58
    • Hill, J.1    Steiner, I.2    Matthews, K.3    et al4
  • 132
    • 0030052279 scopus 로고    scopus 로고
    • Effect of interferon on protein translation during growth stages of 3T3 cells
    • Petryshyn R, Chen J, Danley L. Effect of interferon on protein translation during growth stages of 3T3 cells. Arch Biochem Biophys. 1996, 326:290-7.
    • (1996) Arch Biochem Biophys. , vol.326 , pp. 290-297
    • Petryshyn, R.1    Chen, J.2    Danley, L.3    et al4
  • 133
    • 3142622924 scopus 로고    scopus 로고
    • Complex regulation of the Csk homologous kinase (Chk) by IL-4 family cytokines and IFN-gamma in human peripheral blood monocytes
    • Hiremath M, Mikhael A, Taylor L. Complex regulation of the Csk homologous kinase (Chk) by IL-4 family cytokines and IFN-gamma in human peripheral blood monocytes. Mol Immunol. 2004, 41:901-10.
    • (2004) Mol Immunol. , vol.41 , pp. 901-910
    • Hiremath, M.1    Mikhael, A.2    Taylor, L.3    et al4
  • 134
    • 33644556126 scopus 로고    scopus 로고
    • P53 regulates cellular resistance to complement lysis through enhanced expression of CD59
    • Donev RM, Cole DS, Sivasankar B. p53 regulates cellular resistance to complement lysis through enhanced expression of CD59. Cancer Res. 2006, 66:2451-8.
    • (2006) Cancer Res. , vol.66 , pp. 2451-2458
    • Donev, R.M.1    Cole, D.S.2    Sivasankar, B.3    et al4
  • 135
    • 34347240373 scopus 로고    scopus 로고
    • A role for SC35 and hnRNPA1 in the determination of amyloid precursor protein isoforms
    • Donev R, Newall A, Thome J. A role for SC35 and hnRNPA1 in the determination of amyloid precursor protein isoforms. Mol Psychiatry. 2007, 12:681-90.
    • (2007) Mol Psychiatry. , vol.12 , pp. 681-690
    • Donev, R.1    Newall, A.2    Thome, J.3    et al4
  • 136
    • 33947512432 scopus 로고    scopus 로고
    • Interferon-gamma and tumor necrosis factor-alpha regulate amyloid-beta plaque deposition and beta-secretase expression in Swedish mutant APP transgenic mice
    • Yamamoto M, Kiyota T, Horiba M. Interferon-gamma and tumor necrosis factor-alpha regulate amyloid-beta plaque deposition and beta-secretase expression in Swedish mutant APP transgenic mice. Am J Pathol. 2007, 170:680-92.
    • (2007) Am J Pathol. , vol.170 , pp. 680-692
    • Yamamoto, M.1    Kiyota, T.2    Horiba, M.3    et al4
  • 137
    • 0028234467 scopus 로고
    • The herpes simplex virus regulatory protein ICP27 contributes to the decrease in cellular mRNA levels during infection
    • Hardwicke M, Sandri-Goldin R. The herpes simplex virus regulatory protein ICP27 contributes to the decrease in cellular mRNA levels during infection. J Virol. 1994, 68:4797-810.
    • (1994) J Virol. , vol.68 , pp. 4797-4810
    • Hardwicke, M.1    Sandri-Goldin, R.2
  • 138
    • 0035050518 scopus 로고    scopus 로고
    • Herpes simplex virus IE63 (ICP27) protein interacts with spliceosome-associated protein 145 and inhibits splicing prior to the first catalytic step
    • Bryant H, Wadd S, Lamond A. Herpes simplex virus IE63 (ICP27) protein interacts with spliceosome-associated protein 145 and inhibits splicing prior to the first catalytic step. J Virol. 2001, 75:4376-85.
    • (2001) J Virol. , vol.75 , pp. 4376-4385
    • Bryant, H.1    Wadd, S.2    Lamond, A.3    et al4
  • 139
    • 0036067973 scopus 로고    scopus 로고
    • Splicing inhibition at the level of spliceosome assembly in the presence of herpes simplex virus protein ICP27
    • Lindberg A, Kreivi J. Splicing inhibition at the level of spliceosome assembly in the presence of herpes simplex virus protein ICP27. Virology. 2002, 294:189-98.
    • (2002) Virology. , vol.294 , pp. 189-198
    • Lindberg, A.1    Kreivi, J.2
  • 140
    • 0037387122 scopus 로고    scopus 로고
    • ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by altering SR protein phosphorylation
    • Sciabica K, Dai Q, Sandri-Goldin R. ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by altering SR protein phosphorylation. EMBO J. 2003, 22:1608-19.
    • (2003) EMBO J. , vol.22 , pp. 1608-1619
    • Sciabica, K.1    Dai, Q.2    Sandri-Goldin, R.3
  • 141
  • 142
    • 15944366574 scopus 로고    scopus 로고
    • Cholesterol and amyloid beta fibrillogenesis
    • Yanagisawa K. Cholesterol and amyloid beta fibrillogenesis. Subcell Biochem. 2005, 38:179-202.
    • (2005) Subcell Biochem. , vol.38 , pp. 179-202
    • Yanagisawa, K.1
  • 143
    • 3042857903 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Cummings J. Alzheimer's disease. N Engl J Med. 2004, 351:56-67.
    • (2004) N Engl J Med. , vol.351 , pp. 56-67
    • Cummings, J.1
  • 144
    • 0032910197 scopus 로고    scopus 로고
    • The cholinergic hypothesis of Alzheimer's disease: a review of progress
    • Francis P, Palmer A, Snape M. The cholinergic hypothesis of Alzheimer's disease: a review of progress. J Neurol Neurosurg Psychiatry. 1999, 66:137-47.
    • (1999) J Neurol Neurosurg Psychiatry. , vol.66 , pp. 137-147
    • Francis, P.1    Palmer, A.2    Snape, M.3    et al4
  • 145
    • 0029838038 scopus 로고    scopus 로고
    • Neuropsychiatric aspects of Alzheimer's disease: the cholinergic hypothesis revisited
    • Cummings J, Kaufer D. Neuropsychiatric aspects of Alzheimer's disease: the cholinergic hypothesis revisited. Neurology. 1996, 47:876-83.
    • (1996) Neurology. , vol.47 , pp. 876-883
    • Cummings, J.1    Kaufer, D.2
  • 146
    • 84886631402 scopus 로고
    • Neurotransmitter enzyme abnormalities in senile dementia. Choline acetyltransferase and glutamic acid decarboxylase activities in necropsy brain tissue
    • Perry E, Gibson P, Blessed G. Neurotransmitter enzyme abnormalities in senile dementia. Choline acetyltransferase and glutamic acid decarboxylase activities in necropsy brain tissue. J Neurol Sci. 1977, 34:247-65.
    • (1977) J Neurol Sci. , vol.34 , pp. 247-265
    • Perry, E.1    Gibson, P.2    Blessed, G.3    et al4
  • 147
    • 0020397384 scopus 로고
    • Alzheimer's disease. Correlation of cortical choline acetyltransferase activity with the severity of dementia and histological abnormalities
    • Wilcock G, Esiri M, Bowen D. Alzheimer's disease. Correlation of cortical choline acetyltransferase activity with the severity of dementia and histological abnormalities. J Neurol Sci. 1982, 57:407-17.
    • (1982) J Neurol Sci. , vol.57 , pp. 407-417
    • Wilcock, G.1    Esiri, M.2    Bowen, D.3    et al4
  • 148
    • 0018078940 scopus 로고
    • Correlation of cholinergic abnormalities with senile plaques and mental test scores in senile dementia
    • Perry E, Tomlinson B, Blessed G. Correlation of cholinergic abnormalities with senile plaques and mental test scores in senile dementia. Br Med J. 1978, 2:1457-9.
    • (1978) Br Med J. , vol.2 , pp. 1457-1459
    • Perry, E.1    Tomlinson, B.2    Blessed, G.3    et al4
  • 149
    • 2942514710 scopus 로고    scopus 로고
    • Cholinesterase inhibitors used in the treatment of Alzheimer's disease: the relationship between pharmacological effects and clinical efficacy
    • Wilkinson D, Francis P, Schwam E. Cholinesterase inhibitors used in the treatment of Alzheimer's disease: the relationship between pharmacological effects and clinical efficacy. Drugs Aging. 2004, 21:453-78.
    • (2004) Drugs Aging. , vol.21 , pp. 453-478
    • Wilkinson, D.1    Francis, P.2    Schwam, E.3    et al4
  • 150
    • 0031013522 scopus 로고    scopus 로고
    • Removal of extracellular calcium after conditioning stimulation disrupts long-term potentiation in the CA1 region of rat hippocampal slices
    • Katsuki H, Izumi Y, Zorumski C. Removal of extracellular calcium after conditioning stimulation disrupts long-term potentiation in the CA1 region of rat hippocampal slices. Neuroscience. 1997, 76:1113-9.
    • (1997) Neuroscience. , vol.76 , pp. 1113-1119
    • Katsuki, H.1    Izumi, Y.2    Zorumski, C.3
  • 151
    • 15044338779 scopus 로고    scopus 로고
    • Failures and successes of NMDA receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults
    • Lipton S. Failures and successes of NMDA receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults. NeuroRx. 2004, 1:101-10.
    • (2004) NeuroRx. , vol.1 , pp. 101-110
    • Lipton, S.1
  • 152
    • 0037417238 scopus 로고    scopus 로고
    • Memantine in moderate-to-severe Alzheimer's disease
    • Reisberg B, Doody R, Stöffler A. Memantine in moderate-to-severe Alzheimer's disease. N Engl J Med. 2003, 348:1333-41.
    • (2003) N Engl J Med. , vol.348 , pp. 1333-1341
    • Reisberg, B.1    Doody, R.2    Stöffler, A.3    et al4
  • 153
    • 0032983786 scopus 로고    scopus 로고
    • Memantine in severe dementia: results of the 9M-Best Study (Benefit and efficacy in severely demented patients during treatment with memantine)
    • Winblad B, Poritis N. Memantine in severe dementia: results of the 9M-Best Study (Benefit and efficacy in severely demented patients during treatment with memantine). Int J Geriatr Psychiatry. 1999, 14:135-46.
    • (1999) Int J Geriatr Psychiatry. , vol.14 , pp. 135-146
    • Winblad, B.1    Poritis, N.2
  • 154
    • 17344388652 scopus 로고    scopus 로고
    • BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: implications for Alzheimer's disease therapeutics
    • Roberds S, Anderson J, Basi G. BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: implications for Alzheimer's disease therapeutics. Hum Mol Genet. 2001, 10:1317-24.
    • (2001) Hum Mol Genet. , vol.10 , pp. 1317-1324
    • Roberds, S.1    Anderson, J.2    Basi, G.3    et al4
  • 155
    • 1542349913 scopus 로고    scopus 로고
    • Beta-secretase activity increases with aging in human, monkey, and mouse brain
    • Fukumoto H, Rosene D, Moss M. Beta-secretase activity increases with aging in human, monkey, and mouse brain. Am J Pathol. 2004, 164:719-25.
    • (2004) Am J Pathol. , vol.164 , pp. 719-725
    • Fukumoto, H.1    Rosene, D.2    Moss, M.3    et al4
  • 156
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: current status and future prospects
    • Leung D, Abbenante G, Fairlie D. Protease inhibitors: current status and future prospects. J Med Chem. 2000, 43:305-41.
    • (2000) J Med Chem. , vol.43 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.3
  • 157
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor
    • Hong L, Koelsch G, Lin X. Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor. Science. 2000, 290:150-3.
    • (2000) Science. , vol.290 , pp. 150-153
    • Hong, L.1    Koelsch, G.2    Lin, X.3    et al4
  • 158
    • 33644878338 scopus 로고    scopus 로고
    • The novel beta-secretase inhibitor KMI-429 reduces amyloid beta peptide production in amyloid precursor protein transgenic and wild-type mice
    • Asai M, Hattori C, Iwata N. The novel beta-secretase inhibitor KMI-429 reduces amyloid beta peptide production in amyloid precursor protein transgenic and wild-type mice. J Neurochem. 2006, 96:533-40.
    • (2006) J Neurochem. , vol.96 , pp. 533-540
    • Asai, M.1    Hattori, C.2    Iwata, N.3    et al4
  • 159
    • 38749146862 scopus 로고    scopus 로고
    • Potent memapsin 2 (beta-secretase) inhibitors: design, synthesis, protein-ligand X-ray structure, and in vivo evaluation
    • Ghosh A, Kumaragurubaran N, Hong L. Potent memapsin 2 (beta-secretase) inhibitors: design, synthesis, protein-ligand X-ray structure, and in vivo evaluation. Bioorg Med Chem Lett. 2008, 18:1031-6.
    • (2008) Bioorg Med Chem Lett. , vol.18 , pp. 1031-1036
    • Ghosh, A.1    Kumaragurubaran, N.2    Hong, L.3    et al4
  • 161
    • 33846261909 scopus 로고    scopus 로고
    • Oral administration of a potent and selective non-peptidic BACE-1 inhibitor decreases beta-cleavage of amyloid precursor protein and amyloid-beta production in vivo
    • Hussain I, Hawkins J, Harrison D. Oral administration of a potent and selective non-peptidic BACE-1 inhibitor decreases beta-cleavage of amyloid precursor protein and amyloid-beta production in vivo. J Neurochem. 2007, 100:802-9.
    • (2007) J Neurochem. , vol.100 , pp. 802-809
    • Hussain, I.1    Hawkins, J.2    Harrison, D.3    et al4
  • 162
    • 17744401440 scopus 로고    scopus 로고
    • Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm
    • Wong P, Zheng H, Chen H. Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm. Nature. 1997, 387:288-92.
    • (1997) Nature. , vol.387 , pp. 288-292
    • Wong, P.1    Zheng, H.2    Chen, H.3    et al4
  • 163
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in presenilin-1-deficient mice
    • Shen J, Bronson R, Chen D. Skeletal and CNS defects in presenilin-1-deficient mice. Cell. 1997, 89:629-39.
    • (1997) Cell. , vol.89 , pp. 629-639
    • Shen, J.1    Bronson, R.2    Chen, D.3    et al4
  • 164
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration
    • Selkoe D, Kopan R. Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu Rev Neurosci. 2003, 26:565-97.
    • (2003) Annu Rev Neurosci. , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 165
    • 0242412482 scopus 로고    scopus 로고
    • Adipsin, a biomarker of gastrointestinal toxicity mediated by a functional gamma-secretase inhibitor
    • Searfoss G, Jordan W, Calligaro D. Adipsin, a biomarker of gastrointestinal toxicity mediated by a functional gamma-secretase inhibitor. J Biol Chem. 2003, 278:46107-16.
    • (2003) J Biol Chem. , vol.278 , pp. 46107-46116
    • Searfoss, G.1    Jordan, W.2    Calligaro, D.3    et al4
  • 166
    • 11144355129 scopus 로고    scopus 로고
    • Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits beta-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation
    • Wong G, Manfra D, Poulet F. Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits beta-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation. J Biol Chem. 2004, 279:12876-82.
    • (2004) J Biol Chem. , vol.279 , pp. 12876-12882
    • Wong, G.1    Manfra, D.2    Poulet, F.3    et al4
  • 167
    • 33645013015 scopus 로고    scopus 로고
    • Effects of a gamma-secretase inhibitor in a randomized study of patients with Alzheimer disease
    • Siemers E, Quinn J, Kaye J. Effects of a gamma-secretase inhibitor in a randomized study of patients with Alzheimer disease. Neurology. 2006, 66:602-4.
    • (2006) Neurology. , vol.66 , pp. 602-604
    • Siemers, E.1    Quinn, J.2    Kaye, J.3    et al4
  • 168
    • 19944430290 scopus 로고    scopus 로고
    • Dynamics of [beta]-amyloid reductions in brain, cerebrospinal fluid, and plasma of [beta]-amyloid precursor protein transgenic mice treated with a [gamma]-secretase inhibitor
    • Barten D, Guss V, Corsa J. Dynamics of [beta]-amyloid reductions in brain, cerebrospinal fluid, and plasma of [beta]-amyloid precursor protein transgenic mice treated with a [gamma]-secretase inhibitor. J Pharmacol Exp Ther. 2005, 312:635-43.
    • (2005) J Pharmacol Exp Ther. , vol.312 , pp. 635-643
    • Barten, D.1    Guss, V.2    Corsa, J.3    et al4
  • 169
    • 19944431428 scopus 로고    scopus 로고
    • Reductions in beta-amyloid concentrations in vivo by the gamma-secretase inhibitors BMS-289948 and BMS-299897
    • Anderson J, Holtz G, Baskin P. Reductions in beta-amyloid concentrations in vivo by the gamma-secretase inhibitors BMS-289948 and BMS-299897. Biochem Pharmacol. 2005, 69:689-98.
    • (2005) Biochem Pharmacol. , vol.69 , pp. 689-698
    • Anderson, J.1    Holtz, G.2    Baskin, P.3    et al4
  • 170
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: proteasome of the membrane
    • Kopan R, Ilagan M. Gamma-secretase: proteasome of the membrane. Nat Rev Mol Cell Biol. 2004, 5:499-504.
    • (2004) Nat Rev Mol Cell Biol. , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.2
  • 171
    • 46749097518 scopus 로고    scopus 로고
    • Inhibition and modulation of gamma-secretase for Alzheimer's disease
    • Wolfe M. Inhibition and modulation of gamma-secretase for Alzheimer's disease. Neurotherapeutics. 2008, 5:391-8.
    • (2008) Neurotherapeutics. , vol.5 , pp. 391-398
    • Wolfe, M.1
  • 172
    • 66349133387 scopus 로고    scopus 로고
    • Secretase inhibitors and modulators for Alzheimer's disease treatment
    • Tomita T. Secretase inhibitors and modulators for Alzheimer's disease treatment. Expert Rev Neurother. 2009, 9:661-79.
    • (2009) Expert Rev Neurother. , vol.9 , pp. 661-679
    • Tomita, T.1
  • 173
    • 0037031094 scopus 로고    scopus 로고
    • Heart Protection Study of antioxidant vitamin supplementation in 20,536 high-risk individuals: a randomised placebo-controlled trial
    • MRC/BHF
    • Heart Protection Study of antioxidant vitamin supplementation in 20,536 high-risk individuals: a randomised placebo-controlled trial. Lancet. 2002, 360:23-33. MRC/BHF
    • (2002) Lancet. , vol.360 , pp. 23-33
  • 174
    • 0037320324 scopus 로고    scopus 로고
    • Antioxidant vitamin intake and risk of Alzheimer disease
    • Luchsinger J, Tang M, Shea S. Antioxidant vitamin intake and risk of Alzheimer disease. Arch Neurol. 2003, 60:203-8.
    • (2003) Arch Neurol. , vol.60 , pp. 203-208
    • Luchsinger, J.1    Tang, M.2    Shea, S.3    et al4
  • 175
    • 2342608923 scopus 로고    scopus 로고
    • Midlife dietary intake of antioxidants and risk of late-life incident dementia: the Honolulu-Asia Aging Study
    • Laurin D, Masaki K, Foley D. Midlife dietary intake of antioxidants and risk of late-life incident dementia: the Honolulu-Asia Aging Study. Am J Epidemiol. 2004, 159:959-67.
    • (2004) Am J Epidemiol. , vol.159 , pp. 959-967
    • Laurin, D.1    Masaki, K.2    Foley, D.3    et al4
  • 176
    • 19944427642 scopus 로고    scopus 로고
    • Meta-analysis: high-dosage vitamin E supplementation may increase all-cause mortality
    • Miller Er, Pastor-Barriuso R, Dalal D. Meta-analysis: high-dosage vitamin E supplementation may increase all-cause mortality. Ann Intern Med. 2005, 142:37-46.
    • (2005) Ann Intern Med. , vol.142 , pp. 37-46
    • Miller, E.1    Pastor-Barriuso, R.2    Dalal, D.3
  • 177
    • 0033920019 scopus 로고    scopus 로고
    • The role of cholinergic agents in the management of behavioural disturbances in Alzheimer's disease
    • Cummings J. The role of cholinergic agents in the management of behavioural disturbances in Alzheimer's disease. Int J Neuropsychopharmacol. 2000, 3:21-9.
    • (2000) Int J Neuropsychopharmacol. , vol.3 , pp. 21-29
    • Cummings, J.1
  • 178
    • 0037151567 scopus 로고    scopus 로고
    • Ginkgo for memory enhancement: a randomized controlled trial
    • Solomon P, Adams F, Silver A. Ginkgo for memory enhancement: a randomized controlled trial. JAMA. 2002, 288:835-40.
    • (2002) JAMA. , vol.288 , pp. 835-840
    • Solomon, P.1    Adams, F.2    Silver, A.3    et al4
  • 179
    • 0038375640 scopus 로고    scopus 로고
    • Effect of non-steroidal anti-inflammatory drugs on risk of Alzheimer's disease: systematic review and meta-analysis of observational studies
    • Etminan M, Gill S, Samii A. Effect of non-steroidal anti-inflammatory drugs on risk of Alzheimer's disease: systematic review and meta-analysis of observational studies. BMJ 2003, 327:128.
    • (2003) BMJ , vol.327 , pp. 128
    • Etminan, M.1    Gill, S.2    Samii, A.3
  • 180
    • 0035936004 scopus 로고    scopus 로고
    • Nonsteroidal antiinflammatory drugs and the risk of Alzheimer's disease
    • in t' Veld B, Ruitenberg A, Hofman A. Nonsteroidal antiinflammatory drugs and the risk of Alzheimer's disease. N Engl J Med. 2001, 345:1515-21.
    • (2001) N Engl J Med. , vol.345 , pp. 1515-1521
    • in t' Veld, B.1    Ruitenberg, A.2    Hofman, A.3    et al4
  • 181
    • 0037167542 scopus 로고    scopus 로고
    • Reduced incidence of AD with NSAID but not H2 receptor antagonists: the Cache County Study
    • Zandi P, Anthony J, Hayden K. Reduced incidence of AD with NSAID but not H2 receptor antagonists: the Cache County Study. Neurology. 2002, 59:880-6.
    • (2002) Neurology. , vol.59 , pp. 880-886
    • Zandi, P.1    Anthony, J.2    Hayden, K.3    et al4
  • 182
    • 0031686954 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drug use and Alzheimer's disease: a case-control study in Rochester, Minnesota, 1980 through 1984
    • Beard C, Waring S, O'Brien P. Nonsteroidal anti-inflammatory drug use and Alzheimer's disease: a case-control study in Rochester, Minnesota, 1980 through 1984. Mayo Clin Proc. 1998, 73:951-5.
    • (1998) Mayo Clin Proc. , vol.73 , pp. 951-955
    • Beard, C.1    Waring, S.2    O'Brien, P.3    et al4
  • 183
    • 0037638809 scopus 로고    scopus 로고
    • Effects of rofecoxib or naproxen vs placebo on Alzheimer disease progression: a randomized controlled trial
    • Aisen P, Schafer K, Grundman M. Effects of rofecoxib or naproxen vs placebo on Alzheimer disease progression: a randomized controlled trial. JAMA. 2003, 289:2819-26.
    • (2003) JAMA. , vol.289 , pp. 2819-2826
    • Aisen, P.1    Schafer, K.2    Grundman, M.3    et al4
  • 184
    • 0035845325 scopus 로고    scopus 로고
    • Effect of hydroxychloroquine on progression of dementia in early Alzheimer's disease: an 18-month randomised, double-blind, placebo-controlled study
    • Van Gool W, Weinstein H, Scheltens P. Effect of hydroxychloroquine on progression of dementia in early Alzheimer's disease: an 18-month randomised, double-blind, placebo-controlled study. Lancet. 2001, 358:455-60.
    • (2001) Lancet. , vol.358 , pp. 455-460
    • Van Gool, W.1    Weinstein, H.2    Scheltens, P.3    et al4
  • 185
    • 0034576747 scopus 로고    scopus 로고
    • Anti-inflammatory therapy for Alzheimer's disease: implications of the prednisone trial
    • Aisen P. Anti-inflammatory therapy for Alzheimer's disease: implications of the prednisone trial. Acta Neurol Scand Suppl. 2000, 176:85-9.
    • (2000) Acta Neurol Scand Suppl. , vol.176 , pp. 85-89
    • Aisen, P.1
  • 186
    • 0037046179 scopus 로고    scopus 로고
    • Randomized pilot study of nimesulide treatment in Alzheimer's disease
    • Aisen P, Schmeidler J, Pasinetti G. Randomized pilot study of nimesulide treatment in Alzheimer's disease. Neurology. 2002, 58:1050-4.
    • (2002) Neurology. , vol.58 , pp. 1050-1054
    • Aisen, P.1    Schmeidler, J.2    Pasinetti, G.3
  • 187
    • 0033551547 scopus 로고    scopus 로고
    • A double-blind, placebo-controlled trial of diclofenac/misoprostol in Alzheimer's disease
    • Scharf S, Mander A, Ugoni A. A double-blind, placebo-controlled trial of diclofenac/misoprostol in Alzheimer's disease. Neurology. 1999, 53:197-201.
    • (1999) Neurology. , vol.53 , pp. 197-201
    • Scharf, S.1    Mander, A.2    Ugoni, A.3    et al4
  • 188
    • 0034017960 scopus 로고    scopus 로고
    • Vascular actions of estrogen and Alzheimer's disease
    • Thomas T, Rhodin J. Vascular actions of estrogen and Alzheimer's disease. Ann N Y Acad Sci. 2000, 903:501-9.
    • (2000) Ann N Y Acad Sci. , vol.903 , pp. 501-509
    • Thomas, T.1    Rhodin, J.2
  • 189
    • 0001447433 scopus 로고    scopus 로고
    • Vascular effects of estrogen and cholesterol-lowering therapies in hypercholesterolemic postmenopausal women
    • Koh K, Cardillo C, Bui M. Vascular effects of estrogen and cholesterol-lowering therapies in hypercholesterolemic postmenopausal women. Circulation. 1999, 99:354-60.
    • (1999) Circulation. , vol.99 , pp. 354-360
    • Koh, K.1    Cardillo, C.2    Bui, M.3    et al4
  • 190
    • 0014193642 scopus 로고
    • Effect of cobra venom-induced inhibition of complement activity on allograft and xenograft rejection reactions
    • Gewurz H, Clark D, Cooper M. Effect of cobra venom-induced inhibition of complement activity on allograft and xenograft rejection reactions. Transplantation. 1967, 5:1296-303.
    • (1967) Transplantation. , vol.5 , pp. 1296-1303
    • Gewurz, H.1    Clark, D.2    Cooper, M.3    et al4
  • 191
    • 0014295936 scopus 로고
    • [Decomplementization by a factor extracted from cobra venom. Effect on several immune reactions of the guinea pig and rat]
    • Maillard J, Zarco R. [Decomplementization by a factor extracted from cobra venom. Effect on several immune reactions of the guinea pig and rat]. Ann Inst Pasteur. 1968, 114:756-74.
    • (1968) Ann Inst Pasteur. , vol.114 , pp. 756-774
    • Maillard, J.1    Zarco, R.2
  • 192
    • 0014823471 scopus 로고
    • Depletion of plasma complement in vivo by a protein of cobra venom: its effect on various immunologic reactions
    • Cochrane C, Müller-Eberhard H, Aikin B. Depletion of plasma complement in vivo by a protein of cobra venom: its effect on various immunologic reactions. J Immunol. 1970, 105:55-69.
    • (1970) J Immunol. , vol.105 , pp. 55-69
    • Cochrane, C.1    Müller-Eberhard, H.2    Aikin, B.3
  • 193
    • 0014960268 scopus 로고
    • Studies on a hemolytic factor of cobra venom requiring a heat-labile serum factor
    • Phillips G. Studies on a hemolytic factor of cobra venom requiring a heat-labile serum factor. Biochim Biophys Acta. 1970, 201:364-74.
    • (1970) Biochim Biophys Acta. , vol.201 , pp. 364-374
    • Phillips, G.1
  • 194
    • 0015177025 scopus 로고
    • Isolation of the anticomplementary protein from cobra venom and its mode of action on C3
    • Müller-Eberhard H, Fjellström K. Isolation of the anticomplementary protein from cobra venom and its mode of action on C3. J Immunol. 1971, 107:1666-72.
    • (1971) J Immunol. , vol.107 , pp. 1666-1672
    • Müller-Eberhard, H.1    Fjellström, K.2
  • 195
    • 0015583906 scopus 로고
    • Formation and function of a complex of the C3 proactivator with a protein from cobra venom
    • Cooper N. Formation and function of a complex of the C3 proactivator with a protein from cobra venom. J Exp Med. 1973, 137:451-60.
    • (1973) J Exp Med. , vol.137 , pp. 451-460
    • Cooper, N.1
  • 196
    • 0017861957 scopus 로고
    • Modulation of the formation of the amplification convertase of complement, C3b, Bb, by native and commercial heparin
    • Weiler J, Yurt R, Fearon D. Modulation of the formation of the amplification convertase of complement, C3b, Bb, by native and commercial heparin. J Exp Med. 1978, 147:409-21.
    • (1978) J Exp Med. , vol.147 , pp. 409-421
    • Weiler, J.1    Yurt, R.2    Fearon, D.3    et al4
  • 197
    • 0016654167 scopus 로고
    • Studies on the inhibition of C56-induced lysis (reactive lysis). VI. Modulation of C56-induced lysis polyanions and polycations
    • Baker P, Lint T, McLeod B. Studies on the inhibition of C56-induced lysis (reactive lysis). VI. Modulation of C56-induced lysis polyanions and polycations. J Immunol. 1975, 114:554-8.
    • (1975) J Immunol. , vol.114 , pp. 554-558
    • Baker, P.1    Lint, T.2    McLeod, B.3    et al4
  • 198
    • 0017797008 scopus 로고
    • The reaction between the complement subcomponent C1q, IgG complexes and polyionic molecules
    • Hughes-Jones N, Gardner B. The reaction between the complement subcomponent C1q, IgG complexes and polyionic molecules. Immunology. 1978, 34:459-63.
    • (1978) Immunology. , vol.34 , pp. 459-463
    • Hughes-Jones, N.1    Gardner, B.2
  • 199
    • 0020656704 scopus 로고
    • The binding properties of human complement component C1q. Interaction with mucopolysaccharides
    • Almeda S, Rosenberg R, Bing D. The binding properties of human complement component C1q. Interaction with mucopolysaccharides. J Biol Chem. 1983, 258:785-91.
    • (1983) J Biol Chem. , vol.258 , pp. 785-791
    • Almeda, S.1    Rosenberg, R.2    Bing, D.3
  • 200
    • 0020991543 scopus 로고
    • Polyions regulate the alternative amplification pathway of complement
    • Weiler J. Polyions regulate the alternative amplification pathway of complement. Immunopharmacology. 1983, 6:245-55.
    • (1983) Immunopharmacology. , vol.6 , pp. 245-255
    • Weiler, J.1
  • 201
    • 0026529491 scopus 로고
    • Heparin and modified heparin inhibit complement activation in vivo
    • Weiler J, Edens R, Linhardt R. Heparin and modified heparin inhibit complement activation in vivo. J Immunol. 1992, 148:3210-5.
    • (1992) J Immunol. , vol.148 , pp. 3210-3215
    • Weiler, J.1    Edens, R.2    Linhardt, R.3    et al4
  • 202
    • 0028296813 scopus 로고
    • Heparin and derivatized heparin inhibit zymosan and cobra venom factor activation of complement in serum
    • Edens R, Linhardt R, Bell C. Heparin and derivatized heparin inhibit zymosan and cobra venom factor activation of complement in serum. Immunopharmacology. 1994, 27:145-53.
    • (1994) Immunopharmacology. , vol.27 , pp. 145-153
    • Edens, R.1    Linhardt, R.2    Bell, C.3    et al4
  • 203
    • 2442483898 scopus 로고    scopus 로고
    • Peripheral treatment with enoxaparin, a low molecular weight heparin, reduces plaques and beta-amyloid accumulation in a mouse model of Alzheimer's disease
    • Bergamaschini L, Rossi E, Storini C. Peripheral treatment with enoxaparin, a low molecular weight heparin, reduces plaques and beta-amyloid accumulation in a mouse model of Alzheimer's disease. J Neurosci. 2004, 24:4181-6.
    • (2004) J Neurosci. , vol.24 , pp. 4181-4186
    • Bergamaschini, L.1    Rossi, E.2    Storini, C.3    et al4
  • 204
    • 0021722808 scopus 로고
    • Pharmacological manipulation of complement system
    • Asghar S. Pharmacological manipulation of complement system. Pharmacol Rev. 1984, 36:223-44.
    • (1984) Pharmacol Rev. , vol.36 , pp. 223-244
    • Asghar, S.1
  • 205
    • 0019518823 scopus 로고
    • Inhibitory effect of K-76 monocarboxylic acid, an anticomplementary agent, on the C3b inactivator system
    • Hong K, Kinoshita T, Kitajima H. Inhibitory effect of K-76 monocarboxylic acid, an anticomplementary agent, on the C3b inactivator system. J Immunol. 1981, 127:104-8.
    • (1981) J Immunol. , vol.127 , pp. 104-108
    • Hong, K.1    Kinoshita, T.2    Kitajima, H.3    et al4
  • 206
    • 0021738389 scopus 로고
    • Effects of K-76 monocarboxylic acid, an anticomplementary agent, on various in vivo immunological reactions and on experimental glomerulonephritis
    • Miyazaki W, Izawa T, Nakano Y. Effects of K-76 monocarboxylic acid, an anticomplementary agent, on various in vivo immunological reactions and on experimental glomerulonephritis. Complement. 1984, 1:134-46.
    • (1984) Complement. , vol.1 , pp. 134-146
    • Miyazaki, W.1    Izawa, T.2    Nakano, Y.3    et al4
  • 207
    • 0023678913 scopus 로고
    • Rosmarinic acid: a new inhibitor of complement C3-convertase with anti-inflammatory activity
    • Englberger W, Hadding U, Etschenberg E. Rosmarinic acid: a new inhibitor of complement C3-convertase with anti-inflammatory activity. Int J Immunopharmacol. 1988, 10:729-37.
    • (1988) Int J Immunopharmacol. , vol.10 , pp. 729-737
    • Englberger, W.1    Hadding, U.2    Etschenberg, E.3    et al4
  • 208
    • 0032937081 scopus 로고    scopus 로고
    • Inhibition of complement by covalent attachment of rosmarinic acid to activated C3b
    • Sahu A, Rawal N, Pangburn M. Inhibition of complement by covalent attachment of rosmarinic acid to activated C3b. Biochem Pharmacol. 1999, 57:1439-46.
    • (1999) Biochem Pharmacol. , vol.57 , pp. 1439-1446
    • Sahu, A.1    Rawal, N.2    Pangburn, M.3
  • 209
    • 0029610154 scopus 로고
    • A component of the medicinal herb ephedra blocks activation in the classical and alternative pathways of complement
    • Ling M, Piddlesden S, Morgan B. A component of the medicinal herb ephedra blocks activation in the classical and alternative pathways of complement. Clin Exp Immunol. 1995, 102:582-8.
    • (1995) Clin Exp Immunol. , vol.102 , pp. 582-588
    • Ling, M.1    Piddlesden, S.2    Morgan, B.3
  • 210
    • 0019817468 scopus 로고
    • New synthetic inhibitors of C1r, C1 esterase, thrombin, plasmin, kallikrein and trypsin
    • Fujii S, Hitomi Y. New synthetic inhibitors of C1r, C1 esterase, thrombin, plasmin, kallikrein and trypsin. Biochim Biophys Acta. 1981, 661:342-5.
    • (1981) Biochim Biophys Acta. , vol.661 , pp. 342-345
    • Fujii, S.1    Hitomi, Y.2
  • 211
    • 0026088150 scopus 로고
    • FUT-175 as a potent inhibitor of C5/C3 convertase activity for production of C5a and C3a
    • Inagi R, Miyata T, Maeda K. FUT-175 as a potent inhibitor of C5/C3 convertase activity for production of C5a and C3a. Immunol Lett. 1991, 27:49-52.
    • (1991) Immunol Lett. , vol.27 , pp. 49-52
    • Inagi, R.1    Miyata, T.2    Maeda, K.3    et al4
  • 212
    • 0023262991 scopus 로고
    • Effects of FUT-175, a novel synthetic protease inhibitor, on the development of adjuvant arthritis in rats and some biological reactions dependent on complement activation
    • Ino Y, Sato T, Koshiyama Y. Effects of FUT-175, a novel synthetic protease inhibitor, on the development of adjuvant arthritis in rats and some biological reactions dependent on complement activation. Gen Pharmacol. 1987, 18:513-6.
    • (1987) Gen Pharmacol. , vol.18 , pp. 513-516
    • Ino, Y.1    Sato, T.2    Koshiyama, Y.3    et al4
  • 213
    • 0027521010 scopus 로고
    • Prolonging discordant xenograft survival with anticomplement reagents K76COOH and FUT175
    • Miyagawa S, Shirakura R, Matsumiya G. Prolonging discordant xenograft survival with anticomplement reagents K76COOH and FUT175. Transplantation. 1993, 55:709-13.
    • (1993) Transplantation. , vol.55 , pp. 709-713
    • Miyagawa, S.1    Shirakura, R.2    Matsumiya, G.3    et al4
  • 215
    • 0041563747 scopus 로고    scopus 로고
    • Complement therapeutics; history and current progress
    • Morgan B, Harris C. Complement therapeutics; history and current progress. Mol Immunol. 2003, 40:159-70.
    • (2003) Mol Immunol. , vol.40 , pp. 159-170
    • Morgan, B.1    Harris, C.2
  • 216
    • 0025354456 scopus 로고
    • Soluble human complement receptor type 1: in vivo inhibitor of complement suppressing post-ischemic myocardial inflammation and necrosis
    • Weisman H, Bartow T, Leppo M. Soluble human complement receptor type 1: in vivo inhibitor of complement suppressing post-ischemic myocardial inflammation and necrosis. Science. 1990, 249:146-51.
    • (1990) Science. , vol.249 , pp. 146-151
    • Weisman, H.1    Bartow, T.2    Leppo, M.3    et al4
  • 217
    • 34748814406 scopus 로고    scopus 로고
    • Beneficial effects of complement inhibition with soluble complement receptor 1 (TP10) during cardiac surgery: is there a gender difference
    • Lazar H, Keilani T, Fitzgerald C. Beneficial effects of complement inhibition with soluble complement receptor 1 (TP10) during cardiac surgery: is there a gender difference. Circulation 2007, 116:I83-8.
    • (2007) Circulation , vol.116
    • Lazar, H.1    Keilani, T.2    Fitzgerald, C.3    et al4
  • 218
    • 4644237694 scopus 로고    scopus 로고
    • Soluble human complement receptor 1 limits ischemic damage in cardiac surgery patients at high risk requiring cardiopulmonary bypass
    • Lazar H, Bokesch P, van Lenta F. Soluble human complement receptor 1 limits ischemic damage in cardiac surgery patients at high risk requiring cardiopulmonary bypass. Circulation 2004, 110:II274-9.
    • (2004) Circulation , vol.110
    • Lazar, H.1    Bokesch, P.2    van Lenta, F.3    et al4
  • 219
    • 0036381720 scopus 로고    scopus 로고
    • Coupling complement regulators to immunoglobulin domains generates effective anti-complement reagents with extended half-life in vivo
    • Harris C, Williams A, Linton S. Coupling complement regulators to immunoglobulin domains generates effective anti-complement reagents with extended half-life in vivo. Clin Exp Immunol. 2002, 129:198-207.
    • (2002) Clin Exp Immunol. , vol.129 , pp. 198-207
    • Harris, C.1    Williams, A.2    Linton, S.3    et al4
  • 220
    • 0034866117 scopus 로고    scopus 로고
    • Membrane-targeted complement inhibitors
    • Smith G, Smith R. Membrane-targeted complement inhibitors. Mol Immunol. 2001, 38:249-55.
    • (2001) Mol Immunol. , vol.38 , pp. 249-255
    • Smith, G.1    Smith, R.2
  • 221
    • 85047692710 scopus 로고    scopus 로고
    • Complement receptor 2-mediated targeting of complement inhibitors to sites of complement activation
    • Song H, He C, Knaak C. Complement receptor 2-mediated targeting of complement inhibitors to sites of complement activation. J Clin Invest. 2003, 111:1875-85.
    • (2003) J Clin Invest. , vol.111 , pp. 1875-1885
    • Song, H.1    He, C.2    Knaak, C.3    et al4
  • 222
    • 31044450701 scopus 로고    scopus 로고
    • Inhibition of complement activation by pexelizumab reduces death in patients undergoing combined aortic valve replacement and coronary artery bypass surgery
    • Carrier M, Ménasché P, Levy J. Inhibition of complement activation by pexelizumab reduces death in patients undergoing combined aortic valve replacement and coronary artery bypass surgery. J Thorac Cardiovasc Surg. 2006, 131:352-6.
    • (2006) J Thorac Cardiovasc Surg. , vol.131 , pp. 352-356
    • Carrier, M.1    Ménasché, P.2    Levy, J.3    et al4
  • 223
    • 41349089713 scopus 로고    scopus 로고
    • Multicenter phase 3 study of the complement inhibitor eculizumab for the treatment of patients with paroxysmal nocturnal hemoglobinuria
    • Brodsky R, Young N, Antonioli E. Multicenter phase 3 study of the complement inhibitor eculizumab for the treatment of patients with paroxysmal nocturnal hemoglobinuria. Blood. 2008, 111:1840-7.
    • (2008) Blood. , vol.111 , pp. 1840-1847
    • Brodsky, R.1    Young, N.2    Antonioli, E.3    et al4
  • 225
    • 33846507393 scopus 로고    scopus 로고
    • CD59, a complement regulatory protein, controls choroidal neovascularization in a mouse model of wet-type age-related macular degeneration
    • Bora N, Kaliappan S, Jha P. CD59, a complement regulatory protein, controls choroidal neovascularization in a mouse model of wet-type age-related macular degeneration. J Immunol. 2007, 178:1783-90.
    • (2007) J Immunol. , vol.178 , pp. 1783-1790
    • Bora, N.1    Kaliappan, S.2    Jha, P.3    et al4
  • 226
    • 0032940562 scopus 로고    scopus 로고
    • Targeting of functional antibody-CD59 fusion proteins to a cell surface
    • Zhang H, Yu J, Bajwa E. Targeting of functional antibody-CD59 fusion proteins to a cell surface. J Clin Invest. 1999, 103:55-61.
    • (1999) J Clin Invest. , vol.103 , pp. 55-61
    • Zhang, H.1    Yu, J.2    Bajwa, E.3    et al4
  • 227
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature. 1999, 400:173-7.
    • (1999) Nature. , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    et al4
  • 228
    • 0034700471 scopus 로고    scopus 로고
    • A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C, Pearson J, McLaurin J. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature. 2000, 408:979-82.
    • (2000) Nature. , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.3    et al4
  • 229
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease
    • DeMattos R, Bales K, Cummins D. Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA. 2001, 98:8850-5.
    • (2001) Proc Natl Acad Sci USA. , vol.98 , pp. 8850-8855
    • DeMattos, R.1    Bales, K.2    Cummins, D.3    et al4
  • 230
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model
    • Dodart J, Bales K, Gannon K. Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model. Nat Neurosci. 2002, 5:452-7.
    • (2002) Nat Neurosci. , vol.5 , pp. 452-457
    • Dodart, J.1    Bales, K.2    Gannon, K.3    et al4
  • 231
    • 13544268706 scopus 로고    scopus 로고
    • Immunological and anti-chaperone therapeutic approaches for Alzheimer disease
    • Wisniewski T, Frangione B. Immunological and anti-chaperone therapeutic approaches for Alzheimer disease. Brain Pathol. 2005, 15:72-7.
    • (2005) Brain Pathol. , vol.15 , pp. 72-77
    • Wisniewski, T.1    Frangione, B.2
  • 232
    • 11444267243 scopus 로고    scopus 로고
    • Evaluation of the safety and immunogenicity of synthetic Abeta42 (AN1792) in patients with AD
    • Bayer A, Bullock R, Jones R. Evaluation of the safety and immunogenicity of synthetic Abeta42 (AN1792) in patients with AD. Neurology. 2005, 64:94-101.
    • (2005) Neurology. , vol.64 , pp. 94-101
    • Bayer, A.1    Bullock, R.2    Jones, R.3    et al4
  • 233
    • 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. Progress in the active immunotherapeutic approach to Alzheimer's disease: clinical investigations into AN1792-associated meningoencephalitis. Neurodegener Dis. 2008, 5:194-6.
    • (2008) Neurodegener Dis. , vol.5 , pp. 194-196
    • Pride, M.1    Seubert, P.2    Grundman, M.3    et al4
  • 234
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo J, Gilman S, Dartigues J. Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology. 2003, 61:46-54.
    • (2003) Neurology. , vol.61 , pp. 46-54
    • Orgogozo, J.1    Gilman, S.2    Dartigues, J.3    et al4
  • 235
    • 41149149333 scopus 로고    scopus 로고
    • The role of the immune system in clearance of Abeta from the brain
    • Boche D, Nicoll J. The role of the immune system in clearance of Abeta from the brain. Brain Pathol. 2008, 18:267-78.
    • (2008) Brain Pathol. , vol.18 , pp. 267-278
    • Boche, D.1    Nicoll, J.2
  • 236
    • 58149129243 scopus 로고    scopus 로고
    • Consequence of Abeta immunization on the vasculature of human Alzheimer's disease brain
    • Boche D, Zotova E, Weller R. Consequence of Abeta immunization on the vasculature of human Alzheimer's disease brain. Brain. 2008, 131:3299-310.
    • (2008) Brain. , vol.131 , pp. 3299-3310
    • Boche, D.1    Zotova, E.2    Weller, R.3    et al4
  • 237
    • 34247113214 scopus 로고    scopus 로고
    • Absence of beta-amyloid deposits after immunization in Alzheimer disease with Lewy body dementia
    • Bombois S, Maurage C, Gompel M. Absence of beta-amyloid deposits after immunization in Alzheimer disease with Lewy body dementia. Arch Neurol. 2007, 64:583-7.
    • (2007) Arch Neurol. , vol.64 , pp. 583-587
    • Bombois, S.1    Maurage, C.2    Gompel, M.3    et al4
  • 238
    • 19944429065 scopus 로고    scopus 로고
    • Abeta vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
    • Masliah E, Hansen L, Adame A. Abeta vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease. Neurology. 2005, 64:129-31.
    • (2005) Neurology. , vol.64 , pp. 129-131
    • Masliah, E.1    Hansen, L.2    Adame, A.3    et al4
  • 240
    • 0036853548 scopus 로고    scopus 로고
    • Generation of antibodies specific for beta-amyloid by vaccination of patients with Alzheimer disease
    • Hock C, Konietzko U, Papassotiropoulos A. Generation of antibodies specific for beta-amyloid by vaccination of patients with Alzheimer disease. Nat Med. 2002, 8:1270-5.
    • (2002) Nat Med. , vol.8 , pp. 1270-1275
    • Hock, C.1    Konietzko, U.2    Papassotiropoulos, A.3    et al4
  • 241
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: a case report
    • Nicoll J, Wilkinson D, Holmes C. Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: a case report. Nat Med. 2003, 9:448-52.
    • (2003) Nat Med. , vol.9 , pp. 448-452
    • Nicoll, J.1    Wilkinson, D.2    Holmes, C.3    et al4
  • 242
    • 0035877075 scopus 로고    scopus 로고
    • Antibody-mediated phagocytosis of the amyloid beta-peptide in microglia is differentially modulated by C1q
    • Webster S, Galvan M, Ferran E. Antibody-mediated phagocytosis of the amyloid beta-peptide in microglia is differentially modulated by C1q. J Immunol. 2001, 166:7496-503.
    • (2001) J Immunol. , vol.166 , pp. 7496-7503
    • Webster, S.1    Galvan, M.2    Ferran, E.3    et al4
  • 243
    • 34347326512 scopus 로고    scopus 로고
    • Disease modifying approaches for Alzheimer's pathology
    • Sadowski M, Wisniewski T. Disease modifying approaches for Alzheimer's pathology. Curr Pharm Des. 2007, 13:1943-54.
    • (2007) Curr Pharm Des. , vol.13 , pp. 1943-1954
    • Sadowski, M.1    Wisniewski, T.2
  • 244
    • 20944448555 scopus 로고    scopus 로고
    • Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial
    • Gilman S, Koller M, Black R. Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial. Neurology. 2005, 64:1553-62.
    • (2005) Neurology. , vol.64 , pp. 1553-1562
    • Gilman, S.1    Koller, M.2    Black, R.3    et al4
  • 245
    • 47149112621 scopus 로고    scopus 로고
    • Long-term effects of Abeta42 immunisation in Alzheimer's disease: follow-up of a randomised, placebo-controlled phase I trial
    • Holmes C, Boche D, Wilkinson D. Long-term effects of Abeta42 immunisation in Alzheimer's disease: follow-up of a randomised, placebo-controlled phase I trial. Lancet. 2008, 372:216-23.
    • (2008) Lancet. , vol.372 , pp. 216-223
    • Holmes, C.1    Boche, D.2    Wilkinson, D.3    et al4
  • 246
    • 67649662393 scopus 로고    scopus 로고
    • AD vaccines: conclusions and future directions
    • Wisniewski T. AD vaccines: conclusions and future directions. CNS Neurol Disord Drug Targets. 2009, 8:160-6.
    • (2009) CNS Neurol Disord Drug Targets. , vol.8 , pp. 160-166
    • Wisniewski, T.1
  • 247
    • 34547215215 scopus 로고    scopus 로고
    • Immunotherapy against APP beta-secretase cleavage site improves cognitive function and reduces neuroinflammation in Tg2576 mice without a significant effect on brain abeta levels
    • Rakover I, Arbel M, Solomon B. Immunotherapy against APP beta-secretase cleavage site improves cognitive function and reduces neuroinflammation in Tg2576 mice without a significant effect on brain abeta levels. Neurodegener Dis. 2007, 4:392-402.
    • (2007) Neurodegener Dis. , vol.4 , pp. 392-402
    • Rakover, I.1    Arbel, M.2    Solomon, B.3
  • 248
    • 0031105062 scopus 로고    scopus 로고
    • Synthetic peptide-based activators of the proteasome
    • Wilk S, Chen W. Synthetic peptide-based activators of the proteasome. Mol Biol Rep. 1997, 24:119-24.
    • (1997) Mol Biol Rep. , vol.24 , pp. 119-124
    • Wilk, S.1    Chen, W.2
  • 249
    • 0033556709 scopus 로고    scopus 로고
    • Modulation of the PA28 alpha-20S proteasome interaction by a peptidyl alcohol
    • Wilk S, Chen W, Magnusson R. Modulation of the PA28 alpha-20S proteasome interaction by a peptidyl alcohol. Arch Biochem Biophys. 1999, 362:283-90.
    • (1999) Arch Biochem Biophys. , vol.362 , pp. 283-290
    • Wilk, S.1    Chen, W.2    Magnusson, R.3
  • 250
    • 0027368034 scopus 로고
    • Kinetic mechanism of activation by cardiolipin (diphosphatidylglycerol) of the rat liver multicatalytic proteinase
    • Demena I, Mahillo E, Arribas J. Kinetic mechanism of activation by cardiolipin (diphosphatidylglycerol) of the rat liver multicatalytic proteinase. Biochem J. 1993, 296:93-7.
    • (1993) Biochem J. , vol.296 , pp. 93-97
    • Demena, I.1    Mahillo, E.2    Arribas, J.3    et al4
  • 251
    • 0035853037 scopus 로고    scopus 로고
    • RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: A negative feedback circuit
    • Xie Y, Varshavsky A. RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: A negative feedback circuit. Proc Natl Acad Sci USA. 2001, 98:3056-61.
    • (2001) Proc Natl Acad Sci USA. , vol.98 , pp. 3056-3061
    • Xie, Y.1    Varshavsky, A.2
  • 252
    • 33646364811 scopus 로고    scopus 로고
    • Cerebrolysin decreases amyloid-beta production by regulating amyloid protein precursor maturation in a transgenic model of Alzheimer's disease
    • Rockenstein E, Torrance M, Mante M. Cerebrolysin decreases amyloid-beta production by regulating amyloid protein precursor maturation in a transgenic model of Alzheimer's disease. J Neurosci Res. 2006, 83:1252-61.
    • (2006) J Neurosci Res. , vol.83 , pp. 1252-1261
    • Rockenstein, E.1    Torrance, M.2    Mante, M.3    et al4
  • 253
    • 0036053138 scopus 로고    scopus 로고
    • Effects of Cerebrolysin on amyloid-beta deposition in a transgenic model of Alzheimer's disease
    • Rockenstein E, Mallory M, Mante M. Effects of Cerebrolysin on amyloid-beta deposition in a transgenic model of Alzheimer's disease. J Neural Transm Suppl. 2002, 62:327-36.
    • (2002) J Neural Transm Suppl. , vol.62 , pp. 327-336
    • Rockenstein, E.1    Mallory, M.2    Mante, M.3    et al4
  • 254
    • 0033911108 scopus 로고    scopus 로고
    • Sustained improvements in patients with dementia of Alzheimer's type (DAT) 6 months after termination of Cerebrolysin therapy
    • Rüther E, Ritter R, Apecechea M. Sustained improvements in patients with dementia of Alzheimer's type (DAT) 6 months after termination of Cerebrolysin therapy. J Neural Transm. 2000, 107:815-29.
    • (2000) J Neural Transm. , vol.107 , pp. 815-829
    • Rüther, E.1    Ritter, R.2    Apecechea, M.3    et al4
  • 255
    • 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
  • 256
    • 31144450053 scopus 로고    scopus 로고
    • Current pharmacotherapy for Alzheimer's disease
    • Lleó A, Greenberg S, Growdon J. Current pharmacotherapy for Alzheimer's disease. Annu Rev Med. 2006, 57:513-33.
    • (2006) Annu Rev Med. , vol.57 , pp. 513-533
    • Lleó, A.1    Greenberg, S.2    Growdon, J.3
  • 257
    • 27344454222 scopus 로고    scopus 로고
    • Drug design using the example of the complement system inhibitors' development
    • Bureeva S, Andia-Pravdivy J, Kaplun A. Drug design using the example of the complement system inhibitors' development. Drug Discov Today. 2005, 10:1535-42.
    • (2005) Drug Discov Today. , vol.10 , pp. 1535-1542
    • Bureeva, S.1    Andia-Pravdivy, J.2    Kaplun, A.3
  • 258
    • 0031919928 scopus 로고    scopus 로고
    • Therapeutic inhibition of the complement system
    • Makrides S. Therapeutic inhibition of the complement system. Pharmacol Rev. 1998, 50:59-87.
    • (1998) Pharmacol Rev. , vol.50 , pp. 59-87
    • Makrides, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.