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Volumn 14, Issue 11, 2005, Pages 1385-1409

Protease inhibitors as potential disease-modifying therapeutics for Alzheimer's disease

Author keywords

secretase; secretase; A ; Alzheimer's disease; Aspartyl protease; BACE; NSAID

Indexed keywords

ALDEHYDE DERIVATIVE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; ASPARTIC PROTEINASE; BENZODIAZEPINE DERIVATIVE; BETA SECRETASE; BETA SECRETASE INHIBITOR; BMS 299897; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; DIPEPTIDE DERIVATIVE; FLURBIPROFEN; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; GMS 299897; HEPARAN SULFATE; IBUPROFEN; INDOMETACIN; LEVO FLURBIPROFEN; LOW MOLECULAR WEIGHT HEPARIN; LY 411575; LY 450139; MW 167; MW 936; NONSTEROID ANTIINFLAMMATORY AGENT; NOTCH RECEPTOR; PROTEINASE INHIBITOR; SULFONE DERIVATIVE; SULINDAC SULFIDE; THIAZOLE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 27744480831     PISSN: 13543784     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543784.14.11.1385     Document Type: Review
Times cited : (59)

References (263)
  • 1
    • 0033853008 scopus 로고    scopus 로고
    • Prevalence of AD among whites: A summary by levels of severity
    • HY LX, KELLER DM: Prevalence of AD among whites: a summary by levels of severity. Neurology (2000) 55(2):198-204.
    • (2000) Neurology , vol.55 , Issue.2 , pp. 198-204
    • Hy, L.X.1    Keller, D.M.2
  • 2
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer's disease: Identification as the microtubule-associated protein tau
    • GOEDERT M, WISCHIK CM, CROWTHER RA, WALKER JE, KLUG A: Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer's disease: identification as the microtubule-associated protein tau. Proc. Natl. Acad. Sci. USA (1988) 85(11):4051-4055.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , Issue.11 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 3
    • 0026231697 scopus 로고
    • Neurofibrillary tangles and β-amyloid deposits in Alzheimer's disease
    • GOEDERT M, SISODIA SS, PRICE DL: Neurofibrillary tangles and β-amyloid deposits in Alzheimer's disease. Curr. Opin. Neurobiol. (1991) 1(3):441-447.
    • (1991) Curr. Opin. Neurobiol. , vol.1 , Issue.3 , pp. 441-447
    • Goedert, M.1    Sisodia, S.S.2    Price, D.L.3
  • 4
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • GLENNER GG, WONG CW: Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. (1984) 120(3):885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer's disease and Down's syndrome
    • MASTERS CL, SIMMS G, WEINMAN NA et al.: Amyloid plaque core protein in Alzheimer's disease and Down's syndrome. Proc. Natl. Acad. Sci. USA (1985) 82(12):4245-4249.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , Issue.12 , pp. 4245-4249
    • Masters, C.L.1    Simms, G.2    Weinman, N.A.3
  • 6
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • KANG J, LEMAIRE HG, UNTERBECK A et al.: The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature (1987) 325(6106):733-736.
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 7
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • HAASS C, SCHLOSSMACHER MG, HUNG AY et al.: Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature (1992) 359(6393):322-325.
    • (1992) Nature , vol.359 , Issue.6393 , pp. 322-325
    • Haass, C.1    Schlossmacher, M.G.2    Hung, A.Y.3
  • 8
    • 0032560487 scopus 로고    scopus 로고
    • Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
    • SPILLANTINI MG, MURRELL JR, GOEDERT M et al.: Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc. Natl. Acad. Sci. USA (1998) 95(13):7737-7741.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.13 , pp. 7737-7741
    • Spillantini, M.G.1    Murrell, J.R.2    Goedert, M.3
  • 9
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • HUTTON M, LENDON CL, RIZZU P et al.: Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature (1998) 393(6686):702-705.
    • (1998) Nature , vol.393 , Issue.6686 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 10
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • ODDO S, CACCAMO A, SHEPHERD JD et al.: Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Aβ and synaptic dysfunction. Neuron (2003) 39(3):409-421.
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3
  • 11
    • 4043167747 scopus 로고    scopus 로고
    • Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • ODDO S, BILLINGS L, KESSLAK JP. CRIBBS DH, LAFERLA FM: Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron (2004) 43(3):321-332.
    • (2004) Neuron , vol.43 , Issue.3 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    Laferla, F.M.5
  • 12
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • HARDY JA, HIGGINS GA: Alzheimer's disease: the amyloid cascade hypothesis. Science (1992) 256(5054):184-185.
    • (1992) Science , vol.256 , Issue.5054 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 13
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of β-amyloid
    • MULLAN M, CRAWFORD F, AXELMAN K et al.: A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of β-amyloid. Nat. Genet. (1992) 1(5):345-347.
    • (1992) Nat. Genet. , vol.1 , Issue.5 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 14
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • GOATE A, CHARTIER-HARLIN MC, MULLAN M et al.: Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature (1991) 349(6311):704-706.
    • (1991) Nature , vol.349 , Issue.6311 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 15
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • MURRELL J, FARLOW M, GHETTI B, BENSON MD: A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science (1991) 254(5028):97-99.
    • (1991) Science , vol.254 , Issue.5028 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.D.4
  • 16
    • 0025754007 scopus 로고
    • Mis-sense mutation Val-Ile in exon 17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease
    • NARUSE S, IGARASHI S, KOBAYASHI H et al.: Mis-sense mutation Val-Ile in exon 17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease. Lancet (1991) 337(8747):978-979.
    • (1991) Lancet , vol.337 , Issue.8747 , pp. 978-979
    • Naruse, S.1    Igarashi, S.2    Kobayashi, H.3
  • 17
    • 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 EI, SHERRINGTON R, ROGAEVA EA et al.: 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(6543):775-778.
    • (1995) Nature , vol.376 , Issue.6543 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3
  • 18
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • SHERRINGTON R, ROGAEV EI, LIANG Y et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature (1995) 375(6534):754-760.
    • (1995) Nature , vol.375 , Issue.6534 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 19
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • LEVY-LAHAD E, WASCO W, POORKAJ P et al.: Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science (1995) 269(5226):973-977.
    • (1995) Science , vol.269 , Issue.5226 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 20
    • 0029150716 scopus 로고
    • A familial Alzheimer's disease locus on chromosome 1
    • LEVY-LAHAD E, WIJSMAN EM, NEMENS E et al.: A familial Alzheimer's disease locus on chromosome 1. Science (1995) 269(5226):970-973.
    • (1995) Science , vol.269 , Issue.5226 , pp. 970-973
    • Levy-Lahad, E.1    Wijsman, E.M.2    Nemens, E.3
  • 21
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • HARDY J: Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. (1997) 20(4):154-159.
    • (1997) Trends Neurosci. , vol.20 , Issue.4 , pp. 154-159
    • Hardy, J.1
  • 22
    • 0031003233 scopus 로고    scopus 로고
    • The Alzheimer family of diseases: Many etiologies, one pathogenesis?
    • HARDY J: The Alzheimer family of diseases: many etiologies, one pathogenesis? Proc. Natl. Acad. Sci. USA (1997) 94(6):2095-2097.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.6 , pp. 2095-2097
    • Hardy, J.1
  • 23
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • LAMBERT MP, BARLOW AK, CHROMY BA et al.: Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA (1998) 95(11):6448-6453.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.11 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 24
    • 0035993237 scopus 로고    scopus 로고
    • Aβ toxicity in Alzheimer's disease: Globular oligomers (ADDLs) as new vaccine and drug targets
    • KLEIN WL: Aβ toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem. Int. (2002) 41(5):345-352.
    • (2002) Neurochem. Int. , vol.41 , Issue.5 , pp. 345-352
    • Klein, W.L.1
  • 25
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric A β ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • GONG Y, CHANG L, VIOLA KL et al.: Alzheimer's disease-affected brain: presence of oligomeric A β ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. USA (2003) 100(18):10417-10422.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.18 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3
  • 26
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • TANZI RE, BERTRAM L: Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell (2005) 120(4):545-555.
    • (2005) Cell , vol.120 , Issue.4 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 27
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • LEISSRING MA, FARRIS W, CHANG AY et al.: Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron (2003) 40(6):1087-1093.
    • (2003) Neuron , vol.40 , Issue.6 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3
  • 28
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
    • IWATA N, TSUBUKI S, TAKAKI Y et al.: Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat. Med. (2000) 6(2):143-150.
    • (2000) Nat. Med. , vol.6 , Issue.2 , pp. 143-150
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3
  • 29
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-Aβ antibody alters CNS and plasma A β clearance and decreases brain A β burden in a mouse model of Alzheimer's disease
    • DEMATTOS RB, BALES KR, CUMMINS DJ et al.: Peripheral anti-Aβ antibody alters CNS and plasma A β clearance and decreases brain A β burden in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA (2001) 98(15):8850-8855.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.15 , pp. 8850-8855
    • Demattos, R.B.1    Bales, K.R.2    Cummins, D.J.3
  • 30
    • 0026745610 scopus 로고
    • Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
    • CITRON M, OLTERSDORF T, HAASS C et al.: Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production. Nature (1992) 360(6405):672-674.
    • (1992) Nature , vol.360 , Issue.6405 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3
  • 31
    • 0024093904 scopus 로고
    • Expression of the Alzheimer amyloid precursor gene transcripts in the human brain
    • NEVE RL, FINCH EA, DAWES LR: Expression of the Alzheimer amyloid precursor gene transcripts in the human brain. Neuron (1988) 1(8):669-677.
    • (1988) Neuron , vol.1 , Issue.8 , pp. 669-677
    • Neve, R.L.1    Finch, E.A.2    Dawes, L.R.3
  • 32
    • 0024432039 scopus 로고
    • Expression and cellular localization of amyloid β-protein precursor transcripts in normal human brain and in Alzheimer's disease
    • SPILLANTINI MG, HUNT SP, ULRICH J, GOEDERT M: Expression and cellular localization of amyloid β-protein precursor transcripts in normal human brain and in Alzheimer's disease. Brain Res. Mol. Brain Res. (1989) 6(2-3):143-150.
    • (1989) Brain Res. Mol. Brain Res. , vol.6 , Issue.2-3 , pp. 143-150
    • Spillantini, M.G.1    Hunt, S.P.2    Ulrich, J.3    Goedert, M.4
  • 33
    • 5144224126 scopus 로고    scopus 로고
    • Coordinated and widespread expression of γ-secretase in vivo: Evidence for size and molecular heterogeneity
    • HEBERT SS, SERNEELS L, DEJAEGERE T et al.: Coordinated and widespread expression of γ-secretase in vivo: evidence for size and molecular heterogeneity. Neurobiol. Dis. (2004) 17(2):260-272.
    • (2004) Neurobiol. Dis. , vol.17 , Issue.2 , pp. 260-272
    • Hebert, S.S.1    Serneels, L.2    Dejaegere, T.3
  • 34
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • VASSAR R, BENNETT BD, BABU-KHAN S et al.: β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science (1999) 286(5440):735-741.
    • (1999) Science , vol.286 , Issue.5440 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3
  • 35
    • 0027186334 scopus 로고
    • The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex
    • GHISO J, MATSUBARA E, KOUDINOV A et al.: The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex. Biochem. J. (1993) 293(Part 1):27-30.
    • (1993) Biochem. J. , vol.293 , Issue.PART 1 , pp. 27-30
    • Ghiso, J.1    Matsubara, E.2    Koudinov, A.3
  • 36
    • 9144224765 scopus 로고    scopus 로고
    • ApoE and clusterin cooperatively suppress Aβ levels and deposition. Evidence that ApoE regulates extracellular Aβ metabolism in vivo
    • DEMATTOS RB, CIRRITO JR, PARSADANIAN M et al.: ApoE and clusterin cooperatively suppress Aβ levels and deposition. Evidence that ApoE regulates extracellular Aβ metabolism in vivo. Neuron (2004) 41(2):193-202.
    • (2004) Neuron , vol.41 , Issue.2 , pp. 193-202
    • Demattos, R.B.1    Cirrito, J.R.2    Parsadanian, M.3
  • 37
    • 0014481056 scopus 로고
    • Junctions between intimately apposed cell membranes in the vertebrate brain
    • BRIGHTMAN MW, REESE TS: Junctions between intimately apposed cell membranes in the vertebrate brain. J. Cell Biol. (1969) 40(3):648-677.
    • (1969) J. Cell Biol. , vol.40 , Issue.3 , pp. 648-677
    • Brightman, M.W.1    Reese, T.S.2
  • 38
    • 18144450676 scopus 로고
    • Blood-brain interfaces in vertebrates: A comparative approach
    • CSERR HF, BUNDGAARD M: Blood-brain interfaces in vertebrates: a comparative approach. Am. J. Physiol. (1984) 246(3 Part 2):R277-R288.
    • (1984) Am. J. Physiol. , vol.246 , Issue.3 PART 2
    • Cserr, H.F.1    Bundgaard, M.2
  • 39
    • 13544268809 scopus 로고    scopus 로고
    • Neurovascular mechanisms of Alzheimer's neurodegeneration
    • ZLOKOVIC BV: Neurovascular mechanisms of Alzheimer's neurodegeneration. Trends Neurosci. (2005) 28(4):202-208.
    • (2005) Trends Neurosci. , vol.28 , Issue.4 , pp. 202-208
    • Zlokovic, B.V.1
  • 40
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid β-peptide interaction mediates differential brain efflux of Aβ isoforms
    • DEANE R, WU Z, SAGARE A et al.: LRP/amyloid β-peptide interaction mediates differential brain efflux of Aβ isoforms. Neuron (2004) 43(3):333-344.
    • (2004) Neuron , vol.43 , Issue.3 , pp. 333-344
    • Deane, R.1    Wu, Z.2    Sagare, A.3
  • 41
    • 0037703255 scopus 로고    scopus 로고
    • RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
    • DEANE R, DU YS, SUBMAMARYAN RK et al.: RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain. Nat. Med. (2003) 9(7):907-913.
    • (2003) Nat. Med. , vol.9 , Issue.7 , pp. 907-913
    • Deane, R.1    Du, Y.S.2    Submamaryan, R.K.3
  • 42
    • 0029920929 scopus 로고    scopus 로고
    • Glycoprotein 330/megalin: Probable role in receptor-mediated transport of apolipoprotein J alone and in a complex with Alzheimer's disease amyloid β at the blood-brain and blood-cerebrospinal fluid barriers
    • ZLOKOVIC BV, MARTEL CL, MATSUBARA E et al.: Glycoprotein 330/megalin: probable role in receptor-mediated transport of apolipoprotein J alone and in a complex with Alzheimer's disease amyloid β at the blood-brain and blood-cerebrospinal fluid barriers. Proc. Natl. Acad. Sci. USA (1996) 93(9):4229-4234.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.9 , pp. 4229-4234
    • Zlokovic, B.V.1    Martel, C.L.2    Matsubara, E.3
  • 43
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
    • GAMES D, ADAMS D, ALESSANDRINI R et al.: Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature (1995) 373(6514):523-527.
    • (1995) Nature , vol.373 , Issue.6514 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 44
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • HSIAO K, CHAPMAN P, NILSEN S et al.: Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science (1996) 274(5284):99-102.
    • (1996) Science , vol.274 , Issue.5284 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 45
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid (β) protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • KAWARABAYASHI T, YOUNKIN LH, SAIDO TC et al.: Age-dependent changes in brain, CSF, and plasma amyloid (β) protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J. Neurosci. (2001) 21(2):372-381.
    • (2001) J. Neurosci. , vol.21 , Issue.2 , pp. 372-381
    • Kawarabayashi, T.1    Younkin, L.H.2    Saido, T.C.3
  • 46
    • 0032032493 scopus 로고    scopus 로고
    • Turnover of amyloid β-protein in mouse brain and acute reduction of its level by phorbol ester
    • SAVAGE MJ, TRUSKO SP, HOWLAND DS et al.: Turnover of amyloid β-protein in mouse brain and acute reduction of its level by phorbol ester. J. Neurosci. (1998) 18(5):1743-1752.
    • (1998) J. Neurosci. , vol.18 , Issue.5 , pp. 1743-1752
    • Savage, M.J.1    Trusko, S.P.2    Howland, D.S.3
  • 47
    • 19944430290 scopus 로고    scopus 로고
    • Dynamics of β-amyloid reductions in brain, cerebrospinal fluid, and plasma of β-amyloid precursor protein transgenic mice treated with a γ-secretase inhibitor
    • BARTEN DM, GUSS VL, CORSA JA et al.: Dynamics of β-amyloid reductions in brain, cerebrospinal fluid, and plasma of β-amyloid precursor protein transgenic mice treated with a γ-secretase inhibitor. J. Pharmacol. Exp. Ther. (2005) 312(2):635-643.
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , Issue.2 , pp. 635-643
    • Barten, D.M.1    Guss, V.L.2    Corsa, J.A.3
  • 48
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • HOLCOMB L, GORDON MN, McGOWAN E et al.: Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat. Med. (1998) 4(1):97-100.
    • (1998) Nat. Med. , vol.4 , Issue.1 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3
  • 49
    • 0031020909 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and A β42 deposition in a transgenic mouse model of Alzheimer's disease
    • JOHNSON-WOOD K, LEE M, MOTTER R et al.: Amyloid precursor protein processing and A β42 deposition in a transgenic mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA (1997) 94(4):1550-1555.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.4 , pp. 1550-1555
    • Johnson-Wood, K.1    Lee, M.2    Motter, R.3
  • 50
    • 0141529993 scopus 로고    scopus 로고
    • In vivo assessment of brain interstitial fluid with microdialysis reveals plaque-associated changes in amyloid-β metabolism and half-life
    • CIRRITO JR, MAY PC, O'DELL MA et al.: In vivo assessment of brain interstitial fluid with microdialysis reveals plaque-associated changes in amyloid-β metabolism and half-life. J. Neurosci. (2003) 23(26):8844-8853.
    • (2003) J. Neurosci. , vol.23 , Issue.26 , pp. 8844-8853
    • Cirrito, J.R.1    May, P.C.2    O'Dell, M.A.3
  • 51
    • 0027242091 scopus 로고
    • Introduction and expression of the 400 kilobase amyloid precursor protein gene in transgenic mice
    • LAMB BT, SISODIA SS, LAWLER AM et al.: Introduction and expression of the 400 kilobase amyloid precursor protein gene in transgenic mice. Nat. Genet. (1993) 5(1):22-30.
    • (1993) Nat. Genet. , vol.5 , Issue.1 , pp. 22-30
    • Lamb, B.T.1    Sisodia, S.S.2    Lawler, A.M.3
  • 52
    • 19944431428 scopus 로고    scopus 로고
    • Reductions in β-amyloid concentrations in vivo by the γ-secretase inhibitors BMS-289948 and BMS-299897
    • ANDERSON JJ, HOLTZ G, BASKIN PP et al.: Reductions in β-amyloid concentrations in vivo by the γ-secretase inhibitors BMS-289948 and BMS-299897. Biochem. Pharmacol. (2005) 69(4):689-698.
    • (2005) Biochem. Pharmacol. , vol.69 , Issue.4 , pp. 689-698
    • Anderson, J.J.1    Holtz, G.2    Baskin, P.P.3
  • 53
    • 20944432999 scopus 로고    scopus 로고
    • Quantitative measurement of changes in amyloid-β(40) in the rat brain and cerebrospinal fluid following treatment with the γ-secretase inhibitor LY-411575 [N2- [(2S)-2-(3,5-difluorophenyl)-2- hydroxyethanoyl]-N1-[(7S)-5-methyl-6- oxo-6,7-dihydro-5H-dibenzo[b,d]azepin-7-yl]-L-alaninamide]
    • BEST JD, JAY MT, OTU F et al.: Quantitative measurement of changes in amyloid-β(40) in the rat brain and cerebrospinal fluid following treatment with the γ-secretase inhibitor LY-411575 [N2- [(2S)-2-(3,5-difluorophenyl)-2- hydroxyethanoyl]-N1-[(7S)-5-methyl-6- oxo-6,7-dihydro-5H-dibenzo[b,d]azepin-7-yl]-L-alaninamide]. J. Pharmacol. Exp. Ther. (2005) 313(2):902-908.
    • (2005) J. Pharmacol. Exp. Ther. , vol.313 , Issue.2 , pp. 902-908
    • Best, J.D.1    Jay, M.T.2    Otu, F.3
  • 54
    • 18044392754 scopus 로고    scopus 로고
    • Determination of guinea-pig cortical γ-secretase activity ex vivo following the systemic administration of a γ-secretase inhibitor
    • GRIMWOOD S, HOGG J, JAY MT et al.: Determination of guinea-pig cortical γ-secretase activity ex vivo following the systemic administration of a γ-secretase inhibitor. Neuropharmacology (2005) 48(7):1002-1011.
    • (2005) Neuropharmacology , vol.48 , Issue.7 , pp. 1002-1011
    • Grimwood, S.1    Hogg, J.2    Jay, M.T.3
  • 55
    • 1642296212 scopus 로고    scopus 로고
    • Studies of Aβ pharmacodynamics in the brain, CSF and plasma in young (plaque-free) Tg2576 mice using the γ-secretase inhibitor, LY-411575
    • LANZ TA, HOSLEY JD, ADAMS WJ, MERCHANT KM: Studies of Aβ pharmacodynamics in the brain, CSF and plasma in young (plaque-free) Tg2576 mice using the γ-secretase inhibitor, LY-411575. J. Pharmacol. Exp. Ther. (2004) 309(1):49-55.
    • (2004) J. Pharmacol. Exp. Ther. , vol.309 , Issue.1 , pp. 49-55
    • Lanz, T.A.1    Hosley, J.D.2    Adams, W.J.3    Merchant, K.M.4
  • 56
    • 0032857103 scopus 로고    scopus 로고
    • Cerebrospinal fluid tau and Aβ42 as predictors of development of Alzheimer's disease in patients with mild cognitive impairment
    • ANDREASEN N, MINTHON L, VANMECHELEN E et al.: Cerebrospinal fluid tau and Aβ42 as predictors of development of Alzheimer's disease in patients with mild cognitive impairment. Neurosci. Lett. (1999) 273(1):5-8.
    • (1999) Neurosci. Lett. , vol.273 , Issue.1 , pp. 5-8
    • Andreasen, N.1    Minthon, L.2    Vanmechelen, E.3
  • 57
    • 0033061647 scopus 로고    scopus 로고
    • Cerebrospinal fluid β-amyloid(1-42) in Alzheimer's disease: Differences between early- and late-onset Alzheimer's disease and stability during the course of disease
    • ANDREASEN N, HESSE C, DAVIDSSON P et al.: Cerebrospinal fluid β-amyloid(1-42) in Alzheimer's disease: differences between early- and late-onset Alzheimer's disease and stability during the course of disease. Arch. Neurol. (1999) 56(6):673-680.
    • (1999) Arch. Neurol. , vol.56 , Issue.6 , pp. 673-680
    • Andreasen, N.1    Hesse, C.2    Davidsson, P.3
  • 58
    • 17044430985 scopus 로고    scopus 로고
    • CSF biomarkers for mild cognitive impairment and early Alzheimer's disease
    • ANDREASEN N, BLENNOW K: CSF biomarkers for mild cognitive impairment and early Alzheimer's disease. Clin. Neurol. Neurosurg. (2005) 107(3):165-173.
    • (2005) Clin. Neurol. Neurosurg. , vol.107 , Issue.3 , pp. 165-173
    • Andreasen, N.1    Blennow, K.2
  • 59
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • WOLFE MS, XIA W, OSTASZEWSKI BL et al.: Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature (1999) 398(6727):513-517.
    • (1999) Nature , vol.398 , Issue.6727 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3
  • 60
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • WEIHOFEN A, BINNS K, LEMBERG MK, ASHMAN K, MARTOGLIO B: Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science (2002) 296(5576):2215-2218.
    • (2002) Science , vol.296 , Issue.5576 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 61
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • RAWSON RB, ZELENSKI NG, NIJHAWAN D et al.: Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs. Mol. Cell (1997) 1(1):47-57.
    • (1997) Mol. Cell , vol.1 , Issue.1 , pp. 47-57
    • Rawson, R.B.1    Zelenski, N.G.2    Nijhawan, D.3
  • 62
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila rhomboid-1 defines a family of putative intramembrane scrine proteases
    • URBAN S, LEE JR, FREEMAN M: Drosophila rhomboid-1 defines a family of putative intramembrane scrine proteases. Cell (2001) 107(2):173-182.
    • (2001) Cell , vol.107 , Issue.2 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 63
    • 18644367748 scopus 로고    scopus 로고
    • Presenilins mediate a dual intramembranous γ-secretase cleavage of Notch-1
    • OKOCHI M, STEINER H, FUKUMORI A et al.: Presenilins mediate a dual intramembranous γ-secretase cleavage of Notch-1. EMBO J. (2002) 21(20):5408-5416.
    • (2002) EMBO J. , vol.21 , Issue.20 , pp. 5408-5416
    • Okochi, M.1    Steiner, H.2    Fukumori, A.3
  • 64
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • SASTRE M, STEINER H, FUCHS K et al.: Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep. (2001) 2:835-841.
    • (2001) EMBO Rep. , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3
  • 65
    • 0037176727 scopus 로고    scopus 로고
    • A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • WEIDEMANN A, EGGERT S, REINHARD FB et al.: A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry (2002) 41(8):2825-2835.
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3
  • 66
    • 6344265522 scopus 로고    scopus 로고
    • Truncated carboxyl-terminal fragments of β-amyloid precursor protein are processed to amyloid β-proteins 40 and 42
    • FUNAMOTO S, MORISHIMA-KAWASHIMA M, TANIMURA Y et al.: Truncated carboxyl-terminal fragments of β-amyloid precursor protein are processed to amyloid β-proteins 40 and 42. Biochemistry (2004) 43(42):13532-13540.
    • (2004) Biochemistry , vol.43 , Issue.42 , pp. 13532-13540
    • Funamoto, S.1    Morishima-Kawashima, M.2    Tanimura, Y.3
  • 67
    • 19944430034 scopus 로고    scopus 로고
    • Longer forms of amyloid β protein: Implications for the mechanism of intramembrane cleavage by γ-secretase
    • QI-TAKAHARA Y, MORISHIMA-KAWASHIMA M, TANIMURA Y et al.: Longer forms of amyloid β protein: implications for the mechanism of intramembrane cleavage by γ-secretase. J. Neurosci. (2005) 25(2):436-445.
    • (2005) J. Neurosci. , vol.25 , Issue.2 , pp. 436-445
    • Qi-Takahara, Y.1    Morishima-Kawashima, M.2    Tanimura, Y.3
  • 68
    • 0026045172 scopus 로고
    • Secretion of the β/A4 amyloid precursor protein. Identification of a cleavage site in cultured mammalian cells
    • WANG R, MESCHIA JF, COTTER RJ, SISODIA SS: Secretion of the β/A4 amyloid precursor protein. Identification of a cleavage site in cultured mammalian cells. J. Biol. Chem. (1991) 266(25):16960-16964.
    • (1991) J. Biol. Chem. , vol.266 , Issue.25 , pp. 16960-16964
    • Wang, R.1    Meschia, J.F.2    Cotter, R.J.3    Sisodia, S.S.4
  • 69
    • 0036322138 scopus 로고    scopus 로고
    • Generation of C-terminally truncated amyloid-β peptides is dependent on γ-secretase activity
    • BEHER D, WRIGLEY JD, OWENS AP, SHEARMAN MS: Generation of C-terminally truncated amyloid-β peptides is dependent on γ-secretase activity. J. Neurochem. (2002) 82(3):563-575.
    • (2002) J. Neurochem. , vol.82 , Issue.3 , pp. 563-575
    • Beher, D.1    Wrigley, J.D.2    Owens, A.P.3    Shearman, M.S.4
  • 70
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch
    • GU Y, MISONOU H, SATO T et al.: Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch. J. Biol. Chem. (2001) 276(38):35235-35238.
    • (2001) J. Biol. Chem. , vol.276 , Issue.38 , pp. 35235-35238
    • Gu, Y.1    Misonou, H.2    Sato, T.3
  • 71
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease
    • WOLFE MS, XIA W, MOORE CL et al.: Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease. Biochemistry (1999) 38(15):4720-4727.
    • (1999) Biochemistry , vol.38 , Issue.15 , pp. 4720-4727
    • Wolfe, M.S.1    Xia, W.2    Moore, C.L.3
  • 72
    • 0034254585 scopus 로고    scopus 로고
    • L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity
    • SHEARMAN MS, BEHER D, CLARKE EE et al.: L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity. Biochemistry (2000) 39(30):8698-8704.
    • (2000) Biochemistry , vol.39 , Issue.30 , pp. 8698-8704
    • Shearman, M.S.1    Beher, D.2    Clarke, E.E.3
  • 73
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • DE STROOPER B, SAFTIG P, CRAESSAERTS K et al.: Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature (1998) 391(6665):387-390.
    • (1998) Nature , vol.391 , Issue.6665 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Craessaerts, K.3
  • 74
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated γ-secretatase inhibitors directed to the active site covalently label presenilin 1
    • LI YM, XU M, LAI MT et al.: Photoactivated γ-secretatase inhibitors directed to the active site covalently label presenilin 1. Nature (2000) 405:689-694.
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1    Xu, M.2    Lai, M.T.3
  • 75
    • 0033780472 scopus 로고    scopus 로고
    • Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
    • ESLER WP, KIMBERLY WT, OSTASZEWSKI BL et al.: Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1. Nat. Cell Biol. (2000) 2:428-434.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 428-434
    • Esler, W.P.1    Kimberly, W.T.2    Ostaszewski, B.L.3
  • 76
    • 0034602419 scopus 로고    scopus 로고
    • Presenilin-1 and 2 are molecular targets for γ secretase inhibitors
    • SEIFFERT D, BRADLEY JD, ROMINGER CM et al.: Presenilin-1 and 2 are molecular targets for γ secretase inhibitors. J. Biol. Chem. (2000) 275:34086-34091.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34086-34091
    • Seiffert, D.1    Bradley, J.D.2    Rominger, C.M.3
  • 77
    • 4544229745 scopus 로고    scopus 로고
    • Conserved residues within the putative active site of γ-secretase differentially influence enzyme activity and inhibitor binding
    • WRIGLEY JD, NUNN EJ, NYABI O et al.: Conserved residues within the putative active site of γ-secretase differentially influence enzyme activity and inhibitor binding. J. Neurochem. (2004) 90(6):1312-1320.
    • (2004) J. Neurochem. , vol.90 , Issue.6 , pp. 1312-1320
    • Wrigley, J.D.1    Nunn, E.J.2    Nyabi, O.3
  • 78
    • 0032211774 scopus 로고    scopus 로고
    • Mechanism of activation of the gastric aspartic proteinases: Pepsinogen, progastricsin and prochymosin
    • RICHTER C, TANAKA T, YADA RY: Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosin. Biochem. J. (1998) 335(Part 3):481-490.
    • (1998) Biochem. J. , vol.335 , Issue.PART 3 , pp. 481-490
    • Richter, C.1    Tanaka, T.2    Yada, R.Y.3
  • 79
    • 2442657939 scopus 로고    scopus 로고
    • Mechanism of γ-secretase cleavage activation: Is γ-secretase regulated through autoinhibition involving the presenilin-1 exon 9 loop?
    • KNAPPENBERGER KS, TIAN G, YE X et al.: Mechanism of γ-secretase cleavage activation: is γ-secretase regulated through autoinhibition involving the presenilin-1 exon 9 loop? Biochemistry (2004) 43(20):6208-6218.
    • (2004) Biochemistry , vol.43 , Issue.20 , pp. 6208-6218
    • Knappenberger, K.S.1    Tian, G.2    Ye, X.3
  • 80
    • 0035977071 scopus 로고    scopus 로고
    • Pharmacological knock-down of the presenilin 1 heterodimer by a novel γ-secretase inhibitor: Implications for presenilin biology
    • BEHER D, WRIGLEY JD, NADIN A et al.: Pharmacological knock-down of the presenilin 1 heterodimer by a novel γ-secretase inhibitor: implications for presenilin biology. J. Biol. Chem. (2001) 276(48):45394-45402.
    • (2001) J. Biol. Chem. , vol.276 , Issue.48 , pp. 45394-45402
    • Beher, D.1    Wrigley, J.D.2    Nadin, A.3
  • 81
    • 0035923750 scopus 로고    scopus 로고
    • Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins
    • ANNAERT WG, ESSELENS C, BAERT V et al.: Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins. Neuron (2001) 32(4):579-589.
    • (2001) Neuron , vol.32 , Issue.4 , pp. 579-589
    • Annaert, W.G.1    Esselens, C.2    Baert, V.3
  • 82
    • 0037022644 scopus 로고    scopus 로고
    • Activity-dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a γ substrate
    • ESLER WP, KIMBERLY WT, OSTASZEWSKI BL et al.: Activity-dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a γ substrate. Proc. Natl. Acad. Sci. USA (2002) 99(5):2720-2725.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.5 , pp. 2720-2725
    • Esler, W.P.1    Kimberly, W.T.2    Ostaszewski, B.L.3
  • 83
    • 0037200036 scopus 로고    scopus 로고
    • Linear non-competitive inhibition of solubilized human γ-secretase by pepstatin A methylester, L-685458, sulfonamides and benzodiazepines
    • TIAN G, SOBOTKA-BRINER CD, ZYSK J et al.: Linear non-competitive inhibition of solubilized human γ-secretase by pepstatin A methylester, L-685458, sulfonamides and benzodiazepines. J. Biol. Chem. (2002) 277:31499-31505.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31499-31505
    • Tian, G.1    Sobotka-Briner, C.D.2    Zysk, J.3
  • 84
    • 0038503396 scopus 로고    scopus 로고
    • In vitro characterization of the presenilin-dependent γ-secretase complex using a novel affinity ligand
    • BEHER D, FRICKER M, NADIN A et al.: In vitro characterization of the presenilin-dependent γ-secretase complex using a novel affinity ligand. Biochemistry (2003) 42(27):8133-8142.
    • (2003) Biochemistry , vol.42 , Issue.27 , pp. 8133-8142
    • Beher, D.1    Fricker, M.2    Nadin, A.3
  • 85
    • 23744491374 scopus 로고    scopus 로고
    • Nicastrin functions as a γ-secretase-substrate receptor
    • SHAH S, LEE SF, TABUCHI K et al.: Nicastrin functions as a γ-secretase-substrate receptor. Cell (2005) 122(3):435-447.
    • (2005) Cell , vol.122 , Issue.3 , pp. 435-447
    • Shah, S.1    Lee, S.F.2    Tabuchi, K.3
  • 86
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • YU G, NISHIMURA M, ARAWAKA S et al.: Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature (2000) 407(6300):48-54.
    • (2000) Nature , vol.407 , Issue.6300 , pp. 48-54
    • Yu, G.1    Nishimura, M.2    Arawaka, S.3
  • 87
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
    • GOUTTE C, TSUNOZAKI M, HALE VA, PRIESS JR: APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc. Natl. Acad. Sci. USA (2002) 99(2):775-779.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.2 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 88
    • 18444417998 scopus 로고    scopus 로고
    • Aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation
    • FRANCIS R, McGRATH G, ZHANG J et al.: Aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell (2002) 3(1):85-97.
    • (2002) Dev. Cell , vol.3 , Issue.1 , pp. 85-97
    • Francis, R.1    McGrath, G.2    Zhang, J.3
  • 89
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of γ-secretase activity
    • EDBAUER D, WINKLER E, REGULA JT et al.: Reconstitution of γ-secretase activity. Nat. Cell Biol. (2003) 5(5):486-488.
    • (2003) Nat. Cell Biol. , vol.5 , Issue.5 , pp. 486-488
    • Edbauer, D.1    Winkler, E.2    Regula, J.T.3
  • 90
    • 0037468759 scopus 로고    scopus 로고
    • The role of presenilin cofactors in the γ-secretase complex
    • TAKASUGI N, TOMITA T, HAYASHI I et al.: The role of presenilin cofactors in the γ-secretase complex. Nature (2003) 422(6930):438-441.
    • (2003) Nature , vol.422 , Issue.6930 , pp. 438-441
    • Takasugi, N.1    Tomita, T.2    Hayashi, I.3
  • 91
    • 36048985389 scopus 로고    scopus 로고
    • γ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1, and pen-2
    • KIMBERLY WT, LAVOIE MJ, OSTASZEWSKI BL et al.: γ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1, and pen-2. Proc. Natl. Acad. Sci. USA (2003) 42(22):6664-6673
    • (2003) Proc. Natl. Acad. Sci. USA , vol.42 , Issue.22 , pp. 6664-6673
    • Kimberly, W.T.1    Lavoie, M.J.2    Ostaszewski, B.L.3
  • 92
    • 16844367458 scopus 로고    scopus 로고
    • Functional overexpression of γ-secretase reveals protease-independent trafficking functions and a critical role of lipids for protease activity
    • WRIGLEY JD, SCHUROV I, NUNN EJ et al.: Functional overexpression of γ-secretase reveals protease-independent trafficking functions and a critical role of lipids for protease activity. J. Biol. Chem. (2005) 280(13):12523-12535.
    • (2005) J. Biol. Chem. , vol.280 , Issue.13 , pp. 12523-12535
    • Wrigley, J.D.1    Schurov, I.2    Nunn, E.J.3
  • 93
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • HAASS C: Take five-BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation. EMBO J. (2004) 23(3):483-488.
    • (2004) EMBO J. , vol.23 , Issue.3 , pp. 483-488
    • Haass, C.1
  • 94
    • 0038360879 scopus 로고    scopus 로고
    • Different cofactor activities in γ-secretase assembly: Evidence for a nicastrin-Aph-1 subcomplex
    • HU Y, FORTINI ME: Different cofactor activities in γ-secretase assembly: evidence for a nicastrin-Aph-1 subcomplex. J. Cell Biol. (2003) 161(4):685-690.
    • (2003) J. Cell Biol. , vol.161 , Issue.4 , pp. 685-690
    • Hu, Y.1    Fortini, M.E.2
  • 95
    • 0141733241 scopus 로고    scopus 로고
    • Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin
    • LAVOIE MJ, FRAERING PC, OSTASZEWSKI BL et al.: Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin. J. Biol. Chem. (2003) 278(39):37213-37222.
    • (2003) J. Biol. Chem. , vol.278 , Issue.39 , pp. 37213-37222
    • Lavoie, M.J.1    Fraering, P.C.2    Ostaszewski, B.L.3
  • 96
    • 11244272819 scopus 로고    scopus 로고
    • The presenilin C-terminus is required for ER-retention, nicastrin-binding and γ-secretase activity
    • KAETHER C, CAPELL A, EDBAUER D et al.: The presenilin C-terminus is required for ER-retention, nicastrin-binding and γ-secretase activity. EMBO J. (2004) 23(24):4738-4748.
    • (2004) EMBO J. , vol.23 , Issue.24 , pp. 4738-4748
    • Kaether, C.1    Capell, A.2    Edbauer, D.3
  • 97
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex
    • DE STROOPER B: Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex. Neuron (2003) 38(1):9-12.
    • (2003) Neuron , vol.38 , Issue.1 , pp. 9-12
    • De Strooper, B.1
  • 98
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct γ-secretase complexes with different APH-1 variants
    • SHIROTANI K, EDBAUER D, PROKOP S, HAASS C, STEINER H: Identification of distinct γ-secretase complexes with different APH-1 variants. J. Biol. Chem. (2004) 279(40):41340-41345.
    • (2004) J. Biol. Chem. , vol.279 , Issue.40 , pp. 41340-41345
    • Shirotani, K.1    Edbauer, D.2    Prokop, S.3    Haass, C.4    Steiner, H.5
  • 99
    • 0037590902 scopus 로고    scopus 로고
    • Presenilin-1 and presenilin-2 exhibit distinct yet overlapping γ-secretase activities
    • LAI MT, CHEN E, CROUTHAMEL MC et al.: Presenilin-1 and presenilin-2 exhibit distinct yet overlapping γ-secretase activities. J. Biol. Chem. (2003) 278(25):22475-22481
    • (2003) J. Biol. Chem. , vol.278 , Issue.25 , pp. 22475-22481
    • Lai, M.T.1    Chen, E.2    Crouthamel, M.C.3
  • 100
    • 12144250683 scopus 로고    scopus 로고
    • APH-1a is the principal mammalian APH-1 isoform present in γ-secretase complexes during embryonic development
    • MA G, LI T, PRICE DL, WONG PC: APH-1a is the principal mammalian APH-1 isoform present in γ-secretase complexes during embryonic development. J. Neurosci. (2005) 25(1):192-198.
    • (2005) J. Neurosci. , vol.25 , Issue.1 , pp. 192-198
    • Ma, G.1    Li, T.2    Price, D.L.3    Wong, P.C.4
  • 101
    • 13444268952 scopus 로고    scopus 로고
    • Differential contribution of the three Aph1 genes to γ-secretase activity in vivo
    • SERNEELS L, DEJAEGERE T, CRAESSAERTS K et al.: Differential contribution of the three Aph1 genes to γ-secretase activity in vivo. Proc. Natl. Acad. Sci. USA (2005) 102(5):1719-1724.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.5 , pp. 1719-1724
    • Serneels, L.1    Dejaegere, T.2    Craessaerts, K.3
  • 102
    • 21144447065 scopus 로고    scopus 로고
    • Dissociated phenotypes in presenilin transgenic mice define functionally distinct γ-secretases
    • MASTRANGELO P, MATHEWS PM, CHISHTI MA et al.: Dissociated phenotypes in presenilin transgenic mice define functionally distinct γ-secretases. Proc. Natl. Acad. Sci. USA (2005) 102(25):8972-8977.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.25 , pp. 8972-8977
    • Mastrangelo, P.1    Mathews, P.M.2    Chishti, M.A.3
  • 103
    • 0032981558 scopus 로고    scopus 로고
    • Mechanism of the cleavage specificity of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein
    • LICHTENTHALER SF, WANG R, GRIMM H et al.: Mechanism of the cleavage specificity of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. Proc. Natl. Acad. Sci. USA (1999) 96(6):3053-3058.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.6 , pp. 3053-3058
    • Lichtenthaler, S.F.1    Wang, R.2    Grimm, H.3
  • 104
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor
    • BUXBAUM JD, LIU KN, LUO Y et al.: Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. (1998) 273(43):27765-27767.
    • (1998) J. Biol. Chem. , vol.273 , Issue.43 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3
  • 105
    • 12544258201 scopus 로고    scopus 로고
    • Secretase inhibitors for Alzheimer's disease: Challenges of a promiscuous protease
    • POLLACK SJ, LEWIS H: Secretase inhibitors for Alzheimer's disease: challenges of a promiscuous protease. Curr. Opin. Investig. Drugs (2005) 6(1):35-47.
    • (2005) Curr. Opin. Investig. Drugs , vol.6 , Issue.1 , pp. 35-47
    • Pollack, S.J.1    Lewis, H.2
  • 106
    • 0037114010 scopus 로고    scopus 로고
    • Processing of β-amyloid precursor-like protein-1 and -2 by γ-secretase regulates transcription
    • SCHEINFELD MH, GHERSI E, LAKY K, FOWLKES BJ, D'ADAMIO L: Processing of β-amyloid precursor-like protein-1 and -2 by γ-secretase regulates transcription. J. Biol. Chem. (2002) 277(46):44195-44201.
    • (2002) J. Biol. Chem. , vol.277 , Issue.46 , pp. 44195-44201
    • Scheinfeld, M.H.1    Ghersi, E.2    Laky, K.3    Fowlkes, B.J.4    D'Adamio, L.5
  • 107
    • 2442592973 scopus 로고    scopus 로고
    • The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves α-, β-, γ-, and E-like cleavages. Modulation of APLP-1 processing by N-glycosylation
    • EGGERT S, PALIGA K, SOBA P et al.: The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves α-, β-, γ-, and E-like cleavages. Modulation of APLP-1 processing by N-glycosylation. J. Biol. Chem. (2004) 279(18):18146-18156.
    • (2004) J. Biol. Chem. , vol.279 , Issue.18 , pp. 18146-18156
    • Eggert, S.1    Paliga, K.2    Soba, P.3
  • 108
    • 0035824391 scopus 로고    scopus 로고
    • γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • NI CY, MURPHY MP, GOLDE TE, CARPENTER G: γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science (2001) 294(5549):2179-2181.
    • (2001) Science , vol.294 , Issue.5549 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 109
    • 0037155219 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase-like intramembrane cleavage of ErbB4
    • LEE HJ, JUNG KM, HUANG YZ et al.: Presenilin-dependent γ-secretase-like intramembrane cleavage of ErbB4. J. Biol. Chem. (2002) 277(8):6318-6323.
    • (2002) J. Biol. Chem. , vol.277 , Issue.8 , pp. 6318-6323
    • Lee, H.J.1    Jung, K.M.2    Huang, Y.Z.3
  • 110
    • 17644421407 scopus 로고    scopus 로고
    • Shedding and γ-secretase-mediated intramembrane proteolysis of the mucin-type molecule CD43
    • ANDERSSON CX, FERNANDEZ-RODRIGUEZ J, LAOS S et al.: Shedding and γ-secretase-mediated intramembrane proteolysis of the mucin-type molecule CD43. Biochem. J. (2005) 387(Part 2):377-384.
    • (2005) Biochem. J. , vol.387 , Issue.PART 2 , pp. 377-384
    • Andersson, C.X.1    Fernandez-Rodriguez, J.2    Laos, S.3
  • 111
    • 0347785491 scopus 로고    scopus 로고
    • Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Aβ-like peptide
    • LAMMICH S, OKOCHI M, TAKEDA M et al.: Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Aβ-like peptide. J. Biol. Chem. (2002) 277(47):44754-44759.
    • (2002) J. Biol. Chem. , vol.277 , Issue.47 , pp. 44754-44759
    • Lammich, S.1    Okochi, M.2    Takeda, M.3
  • 112
    • 1542677095 scopus 로고    scopus 로고
    • Syndecan 3 intramembrane proteolysis is presenilin/γ-secretase-dependent and modulates cytosolic signaling
    • SCHULZ JG, ANNAERT W, VANDEKERCKHOVE J et al.: Syndecan 3 intramembrane proteolysis is presenilin/γ-secretase-dependent and modulates cytosolic signaling. J. Biol. Chem. (2003) 278(49):48651-48657.
    • (2003) J. Biol. Chem. , vol.278 , Issue.49 , pp. 48651-48657
    • Schulz, J.G.1    Annaert, W.2    Vandekerckhove, J.3
  • 113
    • 0037146553 scopus 로고    scopus 로고
    • Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin /γ-secretase-like cleavage
    • KIM DY, INGANO LA, KOVACS DM: Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/γ-secretase-like cleavage. J. Biol. Chem. (2002) 277(51):49976-49981.
    • (2002) J. Biol. Chem. , vol.277 , Issue.51 , pp. 49976-49981
    • Kim, D.Y.1    Ingano, L.A.2    Kovacs, D.M.3
  • 114
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/E-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • MARAMBAUD P, WEN PH, DUTT A et al.: A CBP binding transcriptional repressor produced by the PS1/E-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell (2003) 114(5):635-645.
    • (2003) Cell , vol.114 , Issue.5 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3
  • 115
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • MARAMBAUD P, SHIOI J, SERBAN G et al.: A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. (2002) 21(8):1948-1956.
    • (2002) EMBO J. , vol.21 , Issue.8 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3
  • 116
    • 0043235625 scopus 로고    scopus 로고
    • Presenilin-dependent 'γ-secretase' processing of deleted in colorectal cancer (DCC)
    • TANIGUCHI Y, KIM SH, SISODIA SS: Presenilin-dependent 'γ-secretase' processing of deleted in colorectal cancer (DCC). J. Biol. Chem. (2003) 278(33):30425-30428.
    • (2003) J. Biol. Chem. , vol.278 , Issue.33 , pp. 30425-30428
    • Taniguchi, Y.1    Kim, S.H.2    Sisodia, S.S.3
  • 117
    • 0142242199 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor
    • JUNG KM, TAN S, LANDMAN N et al.: Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor. J. Biol. Chem. (2003) 278(43):42161-42169.
    • (2003) J. Biol. Chem. , vol.278 , Issue.43 , pp. 42161-42169
    • Jung, K.M.1    Tan, S.2    Landman, N.3
  • 118
    • 4944225803 scopus 로고    scopus 로고
    • Release of a membrane-bound death domain by γ-secretase processing of the p75NTR homolog NRADD
    • GOWRISHANKAR K, ZEIDLER MG, VINCENZ C: Release of a membrane-bound death domain by γ-secretase processing of the p75NTR homolog NRADD. J. Cell Sci. (2004) 117(Part 18):4099-4111.
    • (2004) J. Cell Sci. , vol.117 , Issue.PART 18 , pp. 4099-4111
    • Gowrishankar, K.1    Zeidler, M.G.2    Vincenz, C.3
  • 119
    • 18144427413 scopus 로고    scopus 로고
    • γ-Protocadherins, presenilin-mediated release of C-terminal fragment promotes locus expression
    • HAMBSCH B, GRINEVICH V, SEEBURG PH, SCHWARZ MK: γ-Protocadherins, presenilin-mediated release of C-terminal fragment promotes locus expression. J. Biol. Chem. (2005) 280(16):15888-15897.
    • (2005) J. Biol. Chem. , vol.280 , Issue.16 , pp. 15888-15897
    • Hambsch, B.1    Grinevich, V.2    Seeburg, P.H.3    Schwarz, M.K.4
  • 120
    • 15744388308 scopus 로고    scopus 로고
    • Presenilin-dependent processing and nuclear function of γ-protocadherins
    • HAAS IG, FRANK M, VERON N, KEMLER R: Presenilin-dependent processing and nuclear function of γ-protocadherins. J. Biol. Chem. (2005) 280(10):9313-9319.
    • (2005) J. Biol. Chem. , vol.280 , Issue.10 , pp. 9313-9319
    • Haas, I.G.1    Frank, M.2    Veron, N.3    Kemler, R.4
  • 121
    • 20744458852 scopus 로고    scopus 로고
    • Presenilin/γ-secretase-mediated cleavage of the voltage-gated sodium channel β2-subunit regulates cell adhesion and migration
    • KIM DY, INGANO LA, CAREY BW, PETTINGELL WH, KOVACS DM: Presenilin/γ-secretase-mediated cleavage of the voltage-gated sodium channel β2-subunit regulates cell adhesion and migration. J. Biol. Chem. (2005) 280(24):23251-23261.
    • (2005) J. Biol. Chem. , vol.280 , Issue.24 , pp. 23251-23261
    • Kim, D.Y.1    Ingano, L.A.2    Carey, B.W.3    Pettingell, W.H.4    Kovacs, D.M.5
  • 122
    • 20744454142 scopus 로고    scopus 로고
    • β Subunits of voltage-gated sodium channels are novel substrates of β-site amyloid precursor protein-cleaving enzyme (BACE1) and γ-secretase
    • WONG HK, SAKURAI T, OYAMA F et al.: β Subunits of voltage-gated sodium channels are novel substrates of β-site amyloid precursor protein-cleaving enzyme (BACE1) and γ-secretase. J. Biol. Chem. (2005) 280(24):23009-23017.
    • (2005) J. Biol. Chem. , vol.280 , Issue.24 , pp. 23009-23017
    • Wong, H.K.1    Sakurai, T.2    Oyama, F.3
  • 123
    • 21444457762 scopus 로고    scopus 로고
    • Growth hormone receptor is a target for presenilin-dependent γ-secretase cleavage
    • COWAN JW, WANG Y, GUAN R et al.: Growth hormone receptor is a target for presenilin-dependent γ-secretase cleavage. J. Biol. Chem. (2005) 280(19):19331-19342.
    • (2005) J. Biol. Chem. , vol.280 , Issue.19 , pp. 19331-19342
    • Cowan, J.W.1    Wang, Y.2    Guan, R.3
  • 124
    • 0037166319 scopus 로고    scopus 로고
    • Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain
    • MAY P, REDDY YK, HERZ J: Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain. J. Biol. Chem. (2002) 277(21):18736-18743.
    • (2002) J. Biol. Chem. , vol.277 , Issue.21 , pp. 18736-18743
    • May, P.1    Reddy, Y.K.2    Herz, J.3
  • 125
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
    • DE STROOPER B, ANNAERT W, CUPERS P et al.: A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature (1999) 398(6727):518-522.
    • (1999) Nature , vol.398 , Issue.6727 , pp. 518-522
    • De Strooper, B.1    Annaert, W.2    Cupers, P.3
  • 126
    • 0038610845 scopus 로고    scopus 로고
    • The Notch ligand E1 is sequentially cleaved by an ADAM protease and γ-secretase
    • SIX E, NDIAYE D, LAABI Y et al.: The Notch ligand E1 is sequentially cleaved by an ADAM protease and γ-secretase. Proc. Natl. Acad. Sci. USA (2003) 100(13):7638-7643.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.13 , pp. 7638-7643
    • Six, E.1    Ndiaye, D.2    Laabi, Y.3
  • 127
    • 0141817915 scopus 로고    scopus 로고
    • The Notch ligands, Jagged and E, are sequentially processed by α-secretase and presenilin/γ-secretase and release signaling fragments
    • LAVOIE MJ, SELKOE DJ: The Notch ligands, Jagged and E, are sequentially processed by α-secretase and presenilin /γ-secretase and release signaling fragments. J. Biol. Chem. (2003) 278(36):34427-34437.
    • (2003) J. Biol. Chem. , vol.278 , Issue.36 , pp. 34427-34437
    • Lavoie, M.J.1    Selkoe, D.J.2
  • 128
    • 0030003538 scopus 로고    scopus 로고
    • Signal transduction by activated mNotch: Importance of proteolytic processing and its regulation by the extracellular domain
    • KOPAN R, SCHROETER EH, WEINTRAUB H, NYE JS: Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain. Proc. Natl. Acad. Sci. USA (1996) 93(4):1683-1688.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.4 , pp. 1683-1688
    • Kopan, R.1    Schroeter, E.H.2    Weintraub, H.3    Nye, J.S.4
  • 129
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • SCHROETER EH, KISSLINGER JA, KOPAN R: Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature (1998) 393(6683):382-386.
    • (1998) Nature , vol.393 , Issue.6683 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 130
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1
    • MUMM JS, SCHROETER EH, SAXENA MT et al.: A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1. Mol. Cell (2000) 5(2):197-206.
    • (2000) Mol. Cell , vol.5 , Issue.2 , pp. 197-206
    • Mumm, J.S.1    Schroeter, E.H.2    Saxena, M.T.3
  • 131
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • BROU C, LOGEAT F, GUPTA N et al.: A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol. Cell (2000) 5(2):207-216.
    • (2000) Mol. Cell , vol.5 , Issue.2 , pp. 207-216
    • Brou, C.1    Logeat, F.2    Gupta, N.3
  • 133
    • 0031001247 scopus 로고    scopus 로고
    • Notch activity influences the αβ versus γδ T cell lineage decision
    • WASHBURN T, SCHWEIGHOFFER E, GRIDLEY T et al.: Notch activity influences the αβ versus γδ T cell lineage decision. Cell (1997) 88(6):833-843.
    • (1997) Cell , vol.88 , Issue.6 , pp. 833-843
    • Washburn, T.1    Schweighoffer, E.2    Gridley, T.3
  • 134
    • 20544447734 scopus 로고    scopus 로고
    • Notch signals control the fate of immature progenitor cells in the intestine
    • FRE S, HUYGHE M, MOURIKIS P et al.: Notch signals control the fate of immature progenitor cells in the intestine. Nature (2005) 435(7044):964-968.
    • (2005) Nature , vol.435 , Issue.7044 , pp. 964-968
    • Fre, S.1    Huyghe, M.2    Mourikis, P.3
  • 135
    • 0038410044 scopus 로고    scopus 로고
    • γ-Secretase inhibitors-from molecular probes to new therapeutics?
    • HARRISON T, BEHER D: γ-Secretase inhibitors-from molecular probes to new therapeutics? Prog. Med. Chem. (2003) 41:99-127.
    • (2003) Prog. Med. Chem. , vol.41 , pp. 99-127
    • Harrison, T.1    Beher, D.2
  • 136
    • 4944262700 scopus 로고    scopus 로고
    • γ-Secretase as a target for drug intervention in Alzheimer's disease
    • HARRISON T, CHURCHER I, BEHER D: γ-Secretase as a target for drug intervention in Alzheimer's disease. Curr. Opin. Drug Discov. Devel. (2004) 7(5):709-719.
    • (2004) Curr. Opin. Drug Discov. Devel. , vol.7 , Issue.5 , pp. 709-719
    • Harrison, T.1    Churcher, I.2    Beher, D.3
  • 137
    • 0028987849 scopus 로고
    • Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
    • HIGAKI J, QUON D, ZHONG Z, CORDELL B: Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism. Neuron (1995) 14(3):651-659.
    • (1995) Neuron , vol.14 , Issue.3 , pp. 651-659
    • Higaki, J.1    Quon, D.2    Zhong, Z.3    Cordell, B.4
  • 138
    • 0031915681 scopus 로고    scopus 로고
    • A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity
    • WOLFE MS, CITRON M, DIEHL TS et al.: A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity. J. Med. Chem. (1998) 41(1):6-9.
    • (1998) J. Med. Chem. , vol.41 , Issue.1 , pp. 6-9
    • Wolfe, M.S.1    Citron, M.2    Diehl, T.S.3
  • 139
    • 20944443757 scopus 로고    scopus 로고
    • Aryl sulfones: A new class of γ-secretase inhibitors
    • TEALL M, OAKLEY P, HARRISON T et al.: Aryl sulfones: a new class of γ-secretase inhibitors. Bioorg. Med. Chem. Lett. (2005) 15(10):2685-2688.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , Issue.10 , pp. 2685-2688
    • Teall, M.1    Oakley, P.2    Harrison, T.3
  • 140
    • 12444343107 scopus 로고    scopus 로고
    • Design and synthesis of highly potent benzodiazepine γ-secretase inhibitors: Preparation of (2S,3R)-3-(3,4-difluorophenyl)-2-(4-fluorophenyl) -4-hydroxy-N-((3S)-1-methyl-2-oxo-5-phenyl-2, 3-dihydro-1H-benzo[e][1,4]-diazepin-3-yl)butyramide by use of an asymmetric Ireland-Claisen rearrangement
    • CHURCHER I, WILLIAMS S, KERRAD S et al.: Design and synthesis of highly potent benzodiazepine γ-secretase inhibitors: preparation of (2S,3R)-3-(3,4-difluorophenyl)-2-(4-fluorophenyl) -4-hydroxy-N-((3S)-1-methyl-2-oxo-5-phenyl-2, 3-dihydro-1H-benzo[e][1,4]-diazepin-3-yl)butyramide by use of an asymmetric Ireland-Claisen rearrangement. J. Med. Chem. (2003) 46(12):2275-2278.
    • (2003) J. Med. Chem. , vol.46 , Issue.12 , pp. 2275-2278
    • Churcher, I.1    Williams, S.2    Kerrad, S.3
  • 141
    • 21544432780 scopus 로고    scopus 로고
    • Reduced β-amyloid burden, increased C-99 concentrations and evaluation of neuropathology in the brains of PDAPP mice given LY450139 dihydrate daily by gavage for 5 months
    • NESS D, BOGGS LN, HEPBURN D et al.: Reduced β-amyloid burden, increased C-99 concentrations and evaluation of neuropathology in the brains of PDAPP mice given LY450139 dihydrate daily by gavage for 5 months. Neurobiol. Aging (2004) 25(Suppl. 2):S238.
    • (2004) Neurobiol. Aging , vol.25 , Issue.SUPPL. 2
    • Ness, D.1    Boggs, L.N.2    Hepburn, D.3
  • 142
    • 0035163347 scopus 로고    scopus 로고
    • Functional γ-secretase inhibitors reduce β-amyloid peptide levels in brain
    • DOVEY HF, JOHN V, ANDERSON JP et al.: Functional γ-secretase inhibitors reduce β-amyloid peptide levels in brain. J. Neurochem. (2001) 76(1):173-181.
    • (2001) J. Neurochem. , vol.76 , Issue.1 , pp. 173-181
    • Dovey, H.F.1    John, V.2    Anderson, J.P.3
  • 143
    • 0038476561 scopus 로고    scopus 로고
    • The γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-L -alanyll-S-phenylglycine t-butyl ester reduces Aβ levels in vivo in plasma and cerebrospinal fluid in young (plaque-free) and aged (plaque-bearing) Tg2576 mice
    • LANZ TA, HIMES CS, PALLANTE G et al.: The γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-L -alanyll-S-phenylglycine t-butyl ester reduces Aβ levels in vivo in plasma and cerebrospinal fluid in young (plaque-free) and aged (plaque-bearing) Tg2576 mice. J. Pharmacol. Exp. Ther. (2003) 305(3):864-871.
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , Issue.3 , pp. 864-871
    • Lanz, T.A.1    Himes, C.S.2    Pallante, G.3
  • 144
    • 0038746673 scopus 로고    scopus 로고
    • Catalytic site-directed γ-secretase complex inhibitors do not discriminate pharmacologically between Notch S3 and β-APP cleavages
    • LEWIS HD, PEREZ REVUELTA BI, NADIN A et al.: Catalytic site-directed γ-secretase complex inhibitors do not discriminate pharmacologically between Notch S3 and β-APP cleavages. Biochemistry (2003) 42(24):7580-7586.
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7580-7586
    • Lewis, H.D.1    Perez Revuelta, B.I.2    Nadin, A.3
  • 145
    • 11144355129 scopus 로고    scopus 로고
    • Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits Aβ production and alters lymphopoiesis and intestinal cell differentiation
    • WONG GT, MANFRA D, POULET FM et al.: Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits Aβ production and alters lymphopoiesis and intestinal cell differentiation. J. Biol. Chem. (2004) 279(13):12876-12882.
    • (2004) J. Biol. Chem. , vol.279 , Issue.13 , pp. 12876-12882
    • Wong, G.T.1    Manfra, D.2    Poulet, F.M.3
  • 146
    • 0242412482 scopus 로고    scopus 로고
    • Adipsin, a biomarker of gastrointestinal toxicity mediated by a functional γ-secretase inhibitor
    • SEARFOSS GH, JORDAN WH, CALLIGARO DO et al.: Adipsin, a biomarker of gastrointestinal toxicity mediated by a functional γ-secretase inhibitor. J. Biol. Chem. (2003) 278(46):46107-46116.
    • (2003) J. Biol. Chem. , vol.278 , Issue.46 , pp. 46107-46116
    • Searfoss, G.H.1    Jordan, W.H.2    Calligaro, D.O.3
  • 147
    • 21544458621 scopus 로고    scopus 로고
    • Safety, Tolerability, and Changes in Amyloid β Concentrations After Administration of a γ-Secretase Inhibitor in Volunteers
    • SIEMERS E, SKINNER M, DEAN RA et al.: Safety, Tolerability, and Changes in Amyloid β Concentrations After Administration of a γ-Secretase Inhibitor in Volunteers. Clin. Neuropharmacol. (2005) 28(3):126-132.
    • (2005) Clin. Neuropharmacol. , vol.28 , Issue.3 , pp. 126-132
    • Siemers, E.1    Skinner, M.2    Dean, R.A.3
  • 148
    • 17744401440 scopus 로고    scopus 로고
    • Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm
    • WONG PC, ZHENG H, CHEN H et al.: Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm. Nature (1997) 387(6630):288-292.
    • (1997) Nature , vol.387 , Issue.6630 , pp. 288-292
    • Wong, P.C.1    Zheng, H.2    Chen, H.3
  • 149
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in presenilin-1-deficient mice
    • SHEN J, BRONSON RT, CHEN DF et al.: Skeletal and CNS defects in presenilin-1-deficient mice. Cell (1997) 89(4):629-639.
    • (1997) Cell , vol.89 , Issue.4 , pp. 629-639
    • Shen, J.1    Bronson, R.T.2    Chen, D.F.3
  • 150
    • 0036023971 scopus 로고    scopus 로고
    • A γ-secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish
    • GELING A, STEINER H, WILLEM M, BALLY-CUIF L, HAASS C: A γ-secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish. EMBO Rep. (2002) 3(7):688-694.
    • (2002) EMBO Rep. , vol.3 , Issue.7 , pp. 688-694
    • Geling, A.1    Steiner, H.2    Willem, M.3    Bally-Cuif, L.4    Haass, C.5
  • 151
    • 0037271081 scopus 로고    scopus 로고
    • γ-Secretase/presenilin inhibitors for Alzheimer's disease phenocopy Notch mutations in Drosophila
    • MICCHELLI CA, ESLER WP, KIMBERLY WT et al.: γ-Secretase/presenilin inhibitors for Alzheimer's disease phenocopy Notch mutations in Drosophila. FASEB J. (2003) 17(1):79-81.
    • (2003) FASEB J. , vol.17 , Issue.1 , pp. 79-81
    • Micchelli, C.A.1    Esler, W.P.2    Kimberly, W.T.3
  • 152
  • 153
    • 1542317449 scopus 로고    scopus 로고
    • Notch regulation of lymphocyte development and function
    • RADTKE F, WILSON A, MANCINI SJ, MacDONALD HR: Notch regulation of lymphocyte development and function. Nat. Immunol. (2004) 5(3):247-253.
    • (2004) Nat. Immunol. , vol.5 , Issue.3 , pp. 247-253
    • Radtke, F.1    Wilson, A.2    Mancini, S.J.3    Macdonald, H.R.4
  • 154
    • 0035979234 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase activity modulates thymocyte development
    • DOERFLER P, SHEARMAN MS, PERLMUTTER RM: Presenilin-dependent γ-secretase activity modulates thymocyte development. Proc. Natl. Acad. Sci. USA (2001) 98(16):9312-9317.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.16 , pp. 9312-9317
    • Doerfler, P.1    Shearman, M.S.2    Perlmutter, R.M.3
  • 155
    • 0035912829 scopus 로고    scopus 로고
    • γ-secretase inhibitors repress thymocyte development
    • HADLAND BK, MANLEY NR, SU D et al.: γ-secretase inhibitors repress thymocyte development. Proc. Natl. Acad. Sci. USA (2001) 98(13):7487-7491.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.13 , pp. 7487-7491
    • Hadland, B.K.1    Manley, N.R.2    Su, D.3
  • 156
    • 8444247084 scopus 로고    scopus 로고
    • Modulation of notch processing by γ-secretase inhibitors causes intestinal goblet cell metaplasia and induction of genes known to specify gut secretory lineage differentiation
    • MILANO J, McKAY J, DAGENAIS C et al.: Modulation of notch processing by γ-secretase inhibitors causes intestinal goblet cell metaplasia and induction of genes known to specify gut secretory lineage differentiation. Toxicol. Sci. (2004) 82(1):341-358.
    • (2004) Toxicol. Sci. , vol.82 , Issue.1 , pp. 341-358
    • Milano, J.1    Mckay, J.2    Dagenais, C.3
  • 157
    • 0038742790 scopus 로고    scopus 로고
    • Notch2 is preferentially expressed in mature B cells and indispensable for marginal zone B lineage development
    • SAITO T, CHIBA S, ICHIKAWA M et al.: Notch2 is preferentially expressed in mature B cells and indispensable for marginal zone B lineage development. Immunity (2003) 18(5):675-685.
    • (2003) Immunity , vol.18 , Issue.5 , pp. 675-685
    • Saito, T.1    Chiba, S.2    Ichikawa, M.3
  • 158
    • 0037332254 scopus 로고    scopus 로고
    • Regulation of marginal zone B cell development by MINT, a suppressor of Notch/RBP-J signaling pathway
    • KURODA K, HAN H, TANI S et al.: Regulation of marginal zone B cell development by MINT, a suppressor of Notch/RBP-J signaling pathway. Immunity (2003) 18(2):301-312.
    • (2003) Immunity , vol.18 , Issue.2 , pp. 301-312
    • Kuroda, K.1    Han, H.2    Tani, S.3
  • 159
    • 0036094254 scopus 로고    scopus 로고
    • Notch-RBP-J signaling is involved in cell fate determination of marginal zone B cells
    • TANIGAKI K, HAN H, YAMAMOTO N et al.: Notch-RBP-J signaling is involved in cell fate determination of marginal zone B cells. Nat. Immunol. (2002) 3(5):443-450.
    • (2002) Nat. Immunol. , vol.3 , Issue.5 , pp. 443-450
    • Tanigaki, K.1    Han, H.2    Yamamoto, N.3
  • 160
    • 18544404101 scopus 로고    scopus 로고
    • Control of endodermal endocrine development by Hes-1
    • JENSEN J, PEDERSEN EE, GALANTE P et al.: Control of endodermal endocrine development by Hes-1. Nat. Genet. (2000) 24(1):36-44.
    • (2000) Nat. Genet. , vol.24 , Issue.1 , pp. 36-44
    • Jensen, J.1    Pedersen, E.E.2    Galante, P.3
  • 161
    • 20544460148 scopus 로고    scopus 로고
    • Notch/γ-secretase inhibition turns proliferative cells in intestinal crypts and adenomas into goblet cells
    • VAN ES JH, VAN GIJN ME, RICCIO O et al.: Notch/γ-secretase inhibition turns proliferative cells in intestinal crypts and adenomas into goblet cells. Nature (2005) 435(7044):959-963.
    • (2005) Nature , vol.435 , Issue.7044 , pp. 959-963
    • Van Es, J.H.1    Van Gijn, M.E.2    Riccio, O.3
  • 162
    • 0025856717 scopus 로고
    • TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms
    • ELLISEN LW, BIRD J, WEST DC et al.: TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms. Cell (1991) 66(4):649-661.
    • (1991) Cell , vol.66 , Issue.4 , pp. 649-661
    • Ellisen, L.W.1    Bird, J.2    West, D.C.3
  • 163
    • 5044225888 scopus 로고    scopus 로고
    • Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia
    • WENG AP, FERRANDO AA, LEE W et al.: Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia. Science (2004) 306(5694):269-271.
    • (2004) Science , vol.306 , Issue.5694 , pp. 269-271
    • Weng, A.P.1    Ferrando, A.A.2    Lee, W.3
  • 164
    • 0030054646 scopus 로고    scopus 로고
    • Notch4/int-3, a mammary proto-oncogene, is an endothelial cell-specific mammalian Notch gene
    • UYTTENDAELE H, MARAZZI G, WU G et al.: Notch4/int-3, a mammary proto-oncogene, is an endothelial cell-specific mammalian Notch gene. Development (1996) 122(7):2251-2259.
    • (1996) Development , vol.122 , Issue.7 , pp. 2251-2259
    • Uyttendaele, H.1    Marazzi, G.2    Wu, G.3
  • 165
    • 3142702839 scopus 로고    scopus 로고
    • Notch oncoproteins depend on γ-secretase/presenilin activity for processing and function
    • DAS I, CRAIG C, FUNAHASHI Y et al.: Notch oncoproteins depend on γ-secretase/presenilin activity for processing and function. J. Biol. Chem. (2004) 279(29):30771-30780.
    • (2004) J. Biol. Chem. , vol.279 , Issue.29 , pp. 30771-30780
    • Das, I.1    Craig, C.2    Funahashi, Y.3
  • 166
    • 7244250027 scopus 로고    scopus 로고
    • Loss of negative regulation by Numb over Notch is relevant to human breast carcinogenesis
    • PECE S, SERRESI M, SANTOLINI E et al.: Loss of negative regulation by Numb over Notch is relevant to human breast carcinogenesis. J. Cell Biol. (2004) 167(2):215-221.
    • (2004) J. Cell Biol. , vol.167 , Issue.2 , pp. 215-221
    • Pece, S.1    Serresi, M.2    Santolini, E.3
  • 167
    • 0030199973 scopus 로고    scopus 로고
    • Control of daughter cell fates during asymmetric division: Interaction of Numb and Notch
    • GUO M, JAN LY, JAN YN: Control of daughter cell fates during asymmetric division: interaction of Numb and Notch. Neuron (1996) 17(1):27-41.
    • (1996) Neuron , vol.17 , Issue.1 , pp. 27-41
    • Guo, M.1    Jan, L.Y.2    Jan, Y.N.3
  • 168
    • 0027947609 scopus 로고
    • Asymmetric distribution of numb protein during division of the sensory organ precursor cell confers distinct fates to daughter cells
    • RHYU MS, JAN LY, JAN YN: Asymmetric distribution of numb
    • (1994) Cell , vol.76 , Issue.3 , pp. 477-491
    • Rhyu, M.S.1    Jan, L.Y.2    Jan, Y.N.3
  • 169
    • 18844386841 scopus 로고    scopus 로고
    • Inhibition of angiogenesis and tumor growth by β and γ-secretase inhibitors
    • PARIS D, QUADROS A, PATEL N et al.: Inhibition of angiogenesis and tumor growth by β and γ-secretase inhibitors. Eur. J. Pharmacol. (2005) 514(1):1-15.
    • (2005) Eur. J. Pharmacol. , vol.514 , Issue.1 , pp. 1-15
    • Paris, D.1    Quadros, A.2    Patel, N.3
  • 170
    • 27144512725 scopus 로고    scopus 로고
    • γ-Secretase inhibitor blocks Notch activation and induces apoptosis in Kaposi's sarcoma tumor cells
    • CURRY CL, REED LL, GOLDE TE et al.: γ-Secretase inhibitor blocks Notch activation and induces apoptosis in Kaposi's sarcoma tumor cells. Oncogene (2005) 24(42):6333-6344.
    • (2005) Oncogene , vol.24 , Issue.42 , pp. 6333-6344
    • Curry, C.L.1    Reed, L.L.2    Golde, T.E.3
  • 171
    • 0036734148 scopus 로고    scopus 로고
    • Activation of Notch-1 signaling maintains the neoplastic phenotype in human Ras-transformed cells
    • WEIJZEN S, RIZZO P, BRAID M et al.: Activation of Notch-1 signaling maintains the neoplastic phenotype in human Ras-transformed cells. Nat. Med. (2002) 8(9):979-986.
    • (2002) Nat. Med. , vol.8 , Issue.9 , pp. 979-986
    • Weijzen, S.1    Rizzo, P.2    Braid, M.3
  • 172
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
    • WEGGEN S, ERIKSEN JL, DAS P et al.: A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity. Nature (2001) 414(6860):212-216.
    • (2001) Nature , vol.414 , Issue.6860 , pp. 212-216
    • Weggen, S.1    Eriksen, J.L.2    Das, P.3
  • 173
    • 0030897133 scopus 로고    scopus 로고
    • Risk of Alzheimer's disease and duration of NSAID use
    • STEWART WF, KAWAS C, CORRADA M, METTER EJ: Risk of Alzheimer's disease and duration of NSAID use. Neurology (1997) 48(3):626-632.
    • (1997) Neurology , vol.48 , Issue.3 , pp. 626-632
    • Stewart, W.F.1    Kawas, C.2    Corrada, M.3    Metter, E.J.4
  • 174
    • 85047691727 scopus 로고    scopus 로고
    • NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ 42 in vivo
    • ERIKSEN JL, SAGI SA, SMITH TE et al.: NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ 42 in vivo. J. Clin. Invest. (2003) 112(3):440-449.
    • (2003) J. Clin. Invest. , vol.112 , Issue.3 , pp. 440-449
    • Eriksen, J.L.1    Sagi, S.A.2    Smith, T.E.3
  • 175
    • 0034618705 scopus 로고    scopus 로고
    • Difluoro ketone peptidomimetics suggest a large S1 pocket for Alzheimer's γ-secretase: Implications for inhibitor design
    • MOORE CL, LEATHERWOOD DD, DIEHL TS, SELKOE DJ, WOLFE MS: Difluoro ketone peptidomimetics suggest a large S1 pocket for Alzheimer's γ-secretase: implications for inhibitor design. J. Med. Chem. (2000) 43(18):3434-3442.
    • (2000) J. Med. Chem. , vol.43 , Issue.18 , pp. 3434-3442
    • Moore, C.L.1    Leatherwood, D.D.2    Diehl, T.S.3    Selkoe, D.J.4    Wolfe, M.S.5
  • 176
    • 0041876229 scopus 로고    scopus 로고
    • Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid β 42 production by direct modulation of γ-secretase activity
    • WEGGEN S, ERIKSEN JL, SAGI SA et al.: Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid β 42 production by direct modulation of γ-secretase activity. J. Biol. Chem. (2003) 278(34):31831-31837.
    • (2003) J. Biol. Chem. , vol.278 , Issue.34 , pp. 31831-31837
    • Weggen, S.1    Eriksen, J.L.2    Sagi, S.A.3
  • 177
    • 0042878457 scopus 로고    scopus 로고
    • The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of κB kinase, and NF κB, do not reduce amyloid β 42 production
    • SAGI SA, WEGGEN S, ERIKSEN J, GOLDE TE, KOO EH: The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of κB kinase, and NF κB, do not reduce amyloid β 42 production. J. Biol. Chem. (2003) 278(34):31825-31830.
    • (2003) J. Biol. Chem. , vol.278 , Issue.34 , pp. 31825-31830
    • Sagi, S.A.1    Weggen, S.2    Eriksen, J.3    Golde, T.E.4    Koo, E.H.5
  • 178
    • 0242414463 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs can lower amyloidogenic Aβ42 by inhibiting Rho
    • ZHOU Y, SU Y, LI B et al.: Nonsteroidal anti-inflammatory drugs can lower amyloidogenic Aβ42 by inhibiting Rho. Science (2003) 302(5648):1215-1217.
    • (2003) Science , vol.302 , Issue.5648 , pp. 1215-1217
    • Zhou, Y.1    Su, Y.2    Li, B.3
  • 179
    • 21044458540 scopus 로고    scopus 로고
    • Diverse compounds mimic Alzheimer's disease-causing mutations by augmenting Aβ42 production
    • KUKAR T, MURPHY MP, ERIKSEN JL et al.: Diverse compounds mimic Alzheimer's disease-causing mutations by augmenting Aβ42 production. Nat. Med. (2005) 11(5):545-550.
    • (2005) Nat. Med. , vol.11 , Issue.5 , pp. 545-550
    • Kukar, T.1    Murphy, M.P.2    Eriksen, J.L.3
  • 180
    • 0038719688 scopus 로고    scopus 로고
    • Sulindac sulfide is a noncompetitive γ-secretase inhibitor that preferentially reduces Aβ 42 generation
    • TAKAHASHI Y, HAYASHI I, TOMINARI Y et al.: Sulindac sulfide is a noncompetitive γ-secretase inhibitor that preferentially reduces Aβ 42 generation. J. Biol. Chem. (2003) 278(20):18664-18670.
    • (2003) J. Biol. Chem. , vol.278 , Issue.20 , pp. 18664-18670
    • Takahashi, Y.1    Hayashi, I.2    Tominari, Y.3
  • 181
    • 6344233805 scopus 로고    scopus 로고
    • Selected non-steroidal anti-inflammatory drugs and their derivatives target γ-secretase at a novel site. Evidence for an allosteric mechanism
    • BEHER D, CLARKE EE, WRIGLEY JD et al.: Selected non-steroidal anti-inflammatory drugs and their derivatives target γ-secretase at a novel site. Evidence for an allosteric mechanism. J. Biol. Chem. (2004) 279(42):43419-43426.
    • (2004) J. Biol. Chem. , vol.279 , Issue.42 , pp. 43419-43426
    • Beher, D.1    Clarke, E.E.2    Wrigley, J.D.3
  • 182
    • 3342993335 scopus 로고    scopus 로고
    • Purification and characterization of the human γ-secretase complex
    • FRAERING PC, YE W, STRUB JM et al.: Purification and characterization of the human γ-secretase complex. Biochemistry (2004) 43(30):9774-9789.
    • (2004) Biochemistry , vol.43 , Issue.30 , pp. 9774-9789
    • Fraering, P.C.1    Ye, W.2    Strub, J.M.3
  • 183
    • 7044254509 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs lower Aβ42 and change presenilin 1 conformation
    • LLEO A, BEREZOVSKA O, HERL L et al.: Nonsteroidal anti-inflammatory drugs lower Aβ42 and change presenilin 1 conformation. Nat. Med. (2004) 10(10):1065-1066.
    • (2004) Nat. Med. , vol.10 , Issue.10 , pp. 1065-1066
    • Lleo, A.1    Berezovska, O.2    Herl, L.3
  • 184
    • 27744600566 scopus 로고    scopus 로고
    • Modulators of γ-secretase activity that lower Aβ-42 levels without affecting Notch proteolytic processing
    • Sorrento, Italy
    • WAGNER SL, KOUNNAS MZ, TYREE CM et al.: Modulators of γ-secretase activity that lower Aβ-42 levels without affecting Notch proteolytic processing. 7th International Conference AD /PD, Sorrento, Italy (2005):11.
    • (2005) 7th International Conference AD/PD , pp. 11
    • Wagner, S.L.1    Kounnas, M.Z.2    Tyree, C.M.3
  • 185
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein β-secretase from human brain
    • SINHA S, ANDERSON JP, BARBOUR R et al.: Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature (1999) 402(6761):537-540.
    • (1999) Nature , vol.402 , Issue.6761 , pp. 537-540
    • Sinha, S.1    Anderson, J.P.2    Barbour, R.3
  • 186
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp 2) as β-secretase
    • HUSSAIN I, POWELL D, HOWLETT DR et al.: Identification of a novel aspartic protease (Asp 2) as β-secretase. Mol. Cell Neurosci. (1999) 14(6):419-427.
    • (1999) Mol. Cell Neurosci. , vol.14 , Issue.6 , pp. 419-427
    • Hussain, I.1    Powell, D.2    Howlett, D.R.3
  • 187
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein
    • LIN X, KOELSCH G, WU S et al.: Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein. Proc. Natl. Acad. Sci. USA (2000) 97(4):1456-1460.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.4 , pp. 1456-1460
    • Lin, X.1    Koelsch, G.2    Wu, S.3
  • 188
    • 0001050325 scopus 로고    scopus 로고
    • BACE maps to chromosome 11 and a BACE homolog, BACE2, reside in the obligate Down's syndrome region of chromosome 21
    • SAUNDERS AJ, KIM T-W, TANZI RE: BACE maps to chromosome 11 and a BACE homolog, BACE2, reside in the obligate Down's syndrome region of chromosome 21. Science (1998) 286:1255a.
    • (1998) Science , vol.286
    • Saunders, A.J.1    Kim, T.-W.2    Tanzi, R.E.3
  • 189
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
    • YAN R, BIENKOWSKI MJ, SHUCK ME et al.: Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity. Nature (1999) 402(6761):533-537.
    • (1999) Nature , vol.402 , Issue.6761 , pp. 533-537
    • Yan, R.1    Bienkowski, M.J.2    Shuck, M.E.3
  • 190
    • 0034662929 scopus 로고    scopus 로고
    • BACE2, a β-secretase homolog, cleaves at the β site and within the amyloid-β region of the amyloid-β precursor protein
    • FARZAN M, SCHNITZLER CE, VASILIEVA N, LEUNG D, CHOE H: BACE2, a β-secretase homolog, cleaves at the β site and within the amyloid-β region of the amyloid-β precursor protein. Proc. Natl. Acad. Sci. USA (2000) 97(17):9712-9717.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.17 , pp. 9712-9717
    • Farzan, M.1    Schnitzler, C.E.2    Vasilieva, N.3    Leung, D.4    Choe, H.5
  • 192
    • 0842309491 scopus 로고    scopus 로고
    • b-Secretase inhibition for the treatment of Alzheimer's disease - Promise and challenge
    • CITRON M: b-Secretase inhibition for the treatment of Alzheimer's disease - promise and challenge. Trends Pharmacol. Sci. (2004) 25(2):92-97.
    • (2004) Trends Pharmacol. Sci. , vol.25 , Issue.2 , pp. 92-97
    • Citron, M.1
  • 193
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor β-secretase in Alzheimer's disease
    • HOLSINGER R, McLEAN C, BEYREUTHER K, MASTERS C, EVIN G: Increased expression of the amyloid precursor β-secretase in Alzheimer's disease. Ann. Neurol. (2002) 51(6):783-786.
    • (2002) Ann. Neurol. , vol.51 , Issue.6 , pp. 783-786
    • Holsinger, R.1    McLean, C.2    Beyreuther, K.3    Masters, C.4    Evin, G.5
  • 194
    • 1542349913 scopus 로고    scopus 로고
    • b-secretase activity increases with aging in human, monkey, and mouse brain
    • FUKUMOTO H, ROSENE DL, MOSS MB et al.: b-secretase activity increases with aging in human, monkey, and mouse brain. Am. J. Pathol. (2004) 164(2):719-725.
    • (2004) Am. J. Pathol. , vol.164 , Issue.2 , pp. 719-725
    • Fukumoto, H.1    Rosene, D.L.2    Moss, M.B.3
  • 195
    • 12144286502 scopus 로고    scopus 로고
    • Amyloid β peptide load is correlated with increased b-secretase activity in sporadic Alzheimer's disease patients
    • LI R, LINDHOLM K, YANG L-B et al.: Amyloid β peptide load is correlated with increased b-secretase activity in sporadic Alzheimer's disease patients. Proc. Natl. Acad. Sci. USA (2004) 101(10):3632-3637.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.10 , pp. 3632-3637
    • Li, R.1    Lindholm, K.2    Yang, L.-B.3
  • 197
    • 0037236622 scopus 로고    scopus 로고
    • Elevated β-secretase expression and enzymatic activity detected in sporadic Alzheimer's disease
    • YANG L, LINDHOLM K, YAN R et al.: Elevated β-secretase expression and enzymatic activity detected in sporadic Alzheimer's disease. Nat. Med. (2003) 9(1):3-4.
    • (2003) Nat. Med. , vol.9 , Issue.1 , pp. 3-4
    • Yang, L.1    Lindholm, K.2    Yan, R.3
  • 198
    • 2542604678 scopus 로고    scopus 로고
    • Increased β-Secretase activity in cerebrospinal fluid of Alzheimer's disease subjects
    • HOLSINGER R, McLEAN C, COLLINS S, MASTERS C, EVIN G: Increased β-Secretase activity in cerebrospinal fluid of Alzheimer's disease subjects. Ann. Neurol. (2004) 55(6):898-899.
    • (2004) Ann. Neurol. , vol.55 , Issue.6 , pp. 898-899
    • Holsinger, R.1    McLean, C.2    Collins, S.3    Masters, C.4    Evin, G.5
  • 199
    • 19944433845 scopus 로고    scopus 로고
    • β-Site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways
    • TAMAGNO E, PAROLA M, BARDINI P et al.: β-Site APP cleaving enzyme up-regulation induced by 4-hydroxynonenal is mediated by stress-activated protein kinases pathways. J. Neurochem. (2005) 92(3):628-636.
    • (2005) J. Neurochem. , vol.92 , Issue.3 , pp. 628-636
    • Tamagno, E.1    Parola, M.2    Bardini, P.3
  • 200
    • 17144427706 scopus 로고    scopus 로고
    • Neuronal and nonneuronal quantitative BACE immunocytochemical expression in the entorhinohippocampal and frontal regions in Alzheimer's disease
    • LEUBA G, WERNLI G, VERNEY A et al.: Neuronal and nonneuronal quantitative BACE immunocytochemical expression in the entorhinohippocampal and frontal regions in Alzheimer's disease. Dement. Geriatr. Cogn. Disord. (2005) 19(4):171-183.
    • (2005) Dement. Geriatr. Cogn. Disord. , vol.19 , Issue.4 , pp. 171-183
    • Leuba, G.1    Wernli, G.2    Verney, A.3
  • 201
    • 13244264935 scopus 로고    scopus 로고
    • Alzheimer's disease β-secretase BACE1 is not a neuron-specific enzyme
    • ROSSNER S, LANGE DOHNA C, ZEITSCHEL U, PEREZ POLO JR: Alzheimer's disease β-secretase BACE1 is not a neuron-specific enzyme. J. Neurochem. (2005) 92(2):226-234.
    • (2005) J. Neurochem. , vol.92 , Issue.2 , pp. 226-234
    • Rossner, S.1    Lange Dohna, C.2    Zeitschel, U.3    Perez Polo, J.R.4
  • 202
    • 0035112647 scopus 로고    scopus 로고
    • BACE1 is the major β-secretase for generation of Aβ peptides by neurons
    • CAI H, WANG Y, McCARTHY D et al.: BACE1 is the major β-secretase for generation of Aβ peptides by neurons. Nat. Neurosci. (2001) 4(3):233-234.
    • (2001) Nat. Neurosci. , vol.4 , Issue.3 , pp. 233-234
    • Cai, H.1    Wang, Y.2    McCarthy, D.3
  • 203
    • 0035116273 scopus 로고    scopus 로고
    • Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation
    • LUO Y, BOLON B, KAHN S et al.: Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation. Nat. Neurosci. (2001) 4(3):231-232.
    • (2001) Nat. Neurosci. , vol.4 , Issue.3 , pp. 231-232
    • Luo, Y.1    Bolon, B.2    Kahn, S.3
  • 204
    • 10744231282 scopus 로고    scopus 로고
    • BACE1 (β-secretase) transgenic and knockout mice: Identification of neurochemical deficits and behavioral changes
    • HARRISON SM, HARPER AJ, HAWKINS J et al.: BACE1 (β-secretase) transgenic and knockout mice: identification of neurochemical deficits and behavioral changes. Mol. Cell. Neurosci. (2003) 24(3):646-655.
    • (2003) Mol. Cell. Neurosci. , vol.24 , Issue.3 , pp. 646-655
    • Harrison, S.M.1    Harper, A.J.2    Hawkins, J.3
  • 205
    • 0346055155 scopus 로고    scopus 로고
    • BACE1 Deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer's disease
    • OHNO M, SAMETSKY E, YOUNKIN L et al.: BACE1 Deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer's disease. Neuron (2004) 41(1):27-33.
    • (2004) Neuron , vol.41 , Issue.1 , pp. 27-33
    • Ohno, M.1    Sametsky, E.2    Younkin, L.3
  • 206
    • 0344672942 scopus 로고    scopus 로고
    • APP processing and synaptic function
    • KAMENETZ F, TOMITA T, HSIEH H et al.: APP processing and synaptic function. Neuron (2003) 37(6):925-937.
    • (2003) Neuron , vol.37 , Issue.6 , pp. 925-937
    • Kamenetz, F.1    Tomita, T.2    Hsieh, H.3
  • 207
    • 24744449320 scopus 로고    scopus 로고
    • Phenotypical and biochemical analysis of BACE1 and BACE2 deficient mice
    • DOMINGUEZ D, TOURNOY J, HARTMANN D et al.: Phenotypical and biochemical analysis of BACE1 and BACE2 deficient mice. J. Biol. Chem. (2005) 280(35):30797-30806.
    • (2005) J. Biol. Chem. , vol.280 , Issue.35 , pp. 30797-30806
    • Dominguez, D.1    Tournoy, J.2    Hartmann, D.3
  • 208
    • 10844278034 scopus 로고    scopus 로고
    • Altered amyloid-β metabolism and deposition in genomic-based β-secretase transgenic mice
    • CHIOCCO MJ, KULNANE LS, YOUNKIN L et al.: Altered amyloid-β metabolism and deposition in genomic-based β-secretase transgenic mice. J. Biol. Chem. (2004) 279(50):52535-52542.
    • (2004) J. Biol. Chem. , vol.279 , Issue.50 , pp. 52535-52542
    • Chiocco, M.J.1    Kulnane, L.S.2    Younkin, L.3
  • 209
    • 1542313772 scopus 로고    scopus 로고
    • Transgenic BACE expression in mouse neurons accelerates amyloid plaque pathology
    • MOHAJERI MH, SAINI KD, NITSCH RM: Transgenic BACE expression in mouse neurons accelerates amyloid plaque pathology. J. Neural. Trans. (2004) 111(3):413-425.
    • (2004) J. Neural. Trans. , vol.111 , Issue.3 , pp. 413-425
    • Mohajeri, M.H.1    Saini, K.D.2    Nitsch, R.M.3
  • 210
    • 0036315584 scopus 로고    scopus 로고
    • Expression of human β-secretase in the mouse brain increases the steady-state level of β-amyloid
    • BODENDORF U, DANNER S, FISCHER F et al.: Expression of human β-secretase in the mouse brain increases the steady-state level of β-amyloid. J. Neurochem. (2002) 80(5):799-806.
    • (2002) J. Neurochem. , vol.80 , Issue.5 , pp. 799-806
    • Bodendorf, U.1    Danner, S.2    Fischer, F.3
  • 211
    • 0034647752 scopus 로고    scopus 로고
    • Characterization of Alzheimer's β-secretase protein BACE. A pepsin family member with unusual properties
    • HANIU M, DENIS P, YOUNG Y et al.: Characterization of Alzheimer's β-secretase protein BACE. A pepsin family member with unusual properties. J. Biol. Chem. (2000) 275(28):21099-21106.
    • (2000) J. Biol. Chem. , vol.275 , Issue.28 , pp. 21099-21106
    • Haniu, M.1    Denis, P.2    Young, Y.3
  • 212
    • 0034529080 scopus 로고    scopus 로고
    • A furin-like convertase mediates propeptide cleavage of BACE, the Alzheimer's β-secretase
    • BENNETT BD, DENIS P, HANIU M et al.: A furin-like convertase mediates propeptide cleavage of BACE, the Alzheimer's β-secretase. J. Biol. Chem. (2000) 275(48):37712-37717.
    • (2000) J. Biol. Chem. , vol.275 , Issue.48 , pp. 37712-37717
    • Bennett, B.D.1    Denis, P.2    Haniu, M.3
  • 213
    • 0035971166 scopus 로고    scopus 로고
    • The pro domain of β-secretase does not confer strict zymogen-like properties but does assist proper folding of the protease domain
    • SHI XP, CHEN E, YIN KC et al.: The pro domain of β-secretase does not confer strict zymogen-like properties but does assist proper folding of the protease domain. J. Biol. Chem. (2001) 276(13):10366-10373.
    • (2001) J. Biol. Chem. , vol.276 , Issue.13 , pp. 10366-10373
    • Shi, X.P.1    Chen, E.2    Yin, K.C.3
  • 214
    • 0035815635 scopus 로고    scopus 로고
    • Post-translational processing of β-secretase (β-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activityand amyloid-β production
    • BENJANNET S, ELAGOZ A, WICKHAM L et al.: Post-translational processing of β-secretase (β-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activityand amyloid-β production. J. Biol. Chem. (2001) 276(14):10879-10887.
    • (2001) J. Biol. Chem. , vol.276 , Issue.14 , pp. 10879-10887
    • Benjannet, S.1    Elagoz, A.2    Wickham, L.3
  • 215
    • 4444283663 scopus 로고    scopus 로고
    • Internalization of exogenously added memapsin 2 (β-secretase) ectodomain by cells Is mediated by amyloid precursor protein
    • HUANG X-P, CHANG W-P, KOELSCH G et al.: Internalization of exogenously added memapsin 2 (β-secretase) ectodomain by cells Is mediated by amyloid precursor protein. J. Biol. Chem. (2004) 279(36):37886-37894.
    • (2004) J. Biol. Chem. , vol.279 , Issue.36 , pp. 37886-37894
    • Huang, X.-P.1    Chang, W.-P.2    Koelsch, G.3
  • 216
    • 0037931840 scopus 로고    scopus 로고
    • Endoproteolysis of β-secretase (β-site amyloid precursor protein-cleaving enzyme) within its catalytic domain
    • HUSE JT, BYANT D, YANG Y et al.: Endoproteolysis of β-secretase (β-site amyloid precursor protein-cleaving enzyme) within its catalytic domain. J. Biol. Chem. (2003) 278(19):17141-17149.
    • (2003) J. Biol. Chem. , vol.278 , Issue.19 , pp. 17141-17149
    • Huse, J.T.1    Byant, D.2    Yang, Y.3
  • 217
    • 7444264029 scopus 로고    scopus 로고
    • The metabolism of β-amyloid converting enzyme and β-amyloid precursor protein processing
    • BENJANNET S, CROMLISH J, DIALLO K, CHRETIEN M, SEIDAH N: The metabolism of β-amyloid converting enzyme and β-amyloid precursor protein processing. Biochem. Biophys. Res. Commun. (2004) 325(1):235-242.
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , Issue.1 , pp. 235-242
    • Benjannet, S.1    Cromlish, J.2    Diallo, K.3    Chretien, M.4    Seidah, N.5
  • 218
    • 1042265051 scopus 로고    scopus 로고
    • Platelet APP, ADAM 10 and BACE alterations in the early stages of Alzheimer's disease
    • COLCIAGHI F, MARCELLO E, BORRONI B et al.: Platelet APP, ADAM 10 and BACE alterations in the early stages of Alzheimer's disease. Neurology (2004) 62(3):498-501.
    • (2004) Neurology , vol.62 , Issue.3 , pp. 498-501
    • Colciaghi, F.1    Marcello, E.2    Borroni, B.3
  • 219
    • 0037085353 scopus 로고    scopus 로고
    • Substrate and inhibitor profile of BACE (β-secretase) and comparison with other mammalian aspartic proteases
    • GRUNINGER-LEITCH F, SCHLATTER D, KUNG E, NELBOCK P, DOBELI H: Substrate and inhibitor profile of BACE (β-secretase) and comparison with other mammalian aspartic proteases. J. Biol. Chem. (2002) 277(7):4687-4693.
    • (2002) J. Biol. Chem. , vol.277 , Issue.7 , pp. 4687-4693
    • Gruninger-Leitch, F.1    Schlatter, D.2    Kung, E.3    Nelbock, P.4    Dobeli, H.5
  • 220
    • 0037343153 scopus 로고    scopus 로고
    • Employing a superior BACE1 cleavage sequence to probe cellular APP processing
    • TOMASSELLI AG, QAHWASH I, EMMONS TL et al.: Employing a superior BACE1 cleavage sequence to probe cellular APP processing. J. Neurochem. (2003) 84(5):1006-1017.
    • (2003) J. Neurochem. , vol.84 , Issue.5 , pp. 1006-1017
    • Tomasselli, A.G.1    Qahwash, I.2    Emmons, T.L.3
  • 221
    • 20944431925 scopus 로고    scopus 로고
    • Novel mutations introduced at the β-site of amyloid β protein precursor enhance the production of amyloid β peptide by BACE1 in vitro and in cells
    • SHI X, TUGUSHEVA K, BRUCE J et al.: Novel mutations introduced at the β-site of amyloid β protein precursor enhance the production of amyloid β peptide by BACE1 in vitro and in cells. J. Alzheimers. Dis. (2005) 7(2):139-48.
    • (2005) J. Alzheimers Dis. , vol.7 , Issue.2 , pp. 139-148
    • Shi, X.1    Tugusheva, K.2    Bruce, J.3
  • 222
    • 0038136955 scopus 로고    scopus 로고
    • Kinetic studies on β-site amyloid precursor protein-cleaving enzyme (BACE). Confirmation of an iso mechanism
    • TOULOKHONOVA L, METZLER WJ, WITMER MR, COPELAND RA, MARCINKEVICIENE J: Kinetic studies on β-site amyloid precursor protein-cleaving enzyme (BACE). Confirmation of an iso mechanism. J. Biol. Chem. (2003) 278(7):4582-4589.
    • (2003) J. Biol. Chem. , vol.278 , Issue.7 , pp. 4582-4589
    • Toulokhonova, L.1    Metzler, W.J.2    Witmer, M.R.3    Copeland, R.A.4    Marcinkeviciene, J.5
  • 223
    • 0034778987 scopus 로고    scopus 로고
    • Follow the protons: A low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases
    • NORTHROP DB: Follow the protons: a low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases. Acc. Chem. Res. (2001) 34(10):790-797.
    • (2001) Acc. Chem. Res. , vol.34 , Issue.10 , pp. 790-797
    • Northrop, D.B.1
  • 224
    • 4644364822 scopus 로고    scopus 로고
    • Apo and Inhibitor Complex Structures of BACE (β-secretase)
    • PATEL S, VUILLARD L, CLEASBY A, MURRAY CW, YON J: Apo and Inhibitor Complex Structures of BACE (β-secretase). J. Mol. Biol. (2004) 343(2):407-416.
    • (2004) J. Mol. Biol. , vol.343 , Issue.2 , pp. 407-416
    • Patel, S.1    Vuillard, L.2    Cleasby, A.3    Murray, C.W.4    Yon, J.5
  • 225
    • 15444379155 scopus 로고    scopus 로고
    • Structural features of human memapsin 2 (β-secretase) and their biological and pathological implications
    • HONG L, HE X, HUANG X, CHANG W, TANG J: Structural features of human memapsin 2 (β-secretase) and their biological and pathological implications. Acta Biochim. Biophys. Sin. (2004) 36(12):787-792.
    • (2004) Acta Biochim. Biophys. Sin. , vol.36 , Issue.12 , pp. 787-792
    • Hong, L.1    He, X.2    Huang, X.3    Chang, W.4    Tang, J.5
  • 226
    • 0037442871 scopus 로고    scopus 로고
    • Comparative studies of active site-ligand interactions among various recombinant constructs of human β-amyloid precursor protein cleaving enzyme
    • KOPCHO LM, MA J, MARCINKEVICIENE J et al.: Comparative studies of active site-ligand interactions among various recombinant constructs of human β-amyloid precursor protein cleaving enzyme. Arch. Biochem. Biophys. (2003) 410(2):307-316.
    • (2003) Arch. Biochem. Biophys. , vol.410 , Issue.2 , pp. 307-316
    • Kopcho, L.M.1    Ma, J.2    Marcinkeviciene, J.3
  • 227
    • 34248353880 scopus 로고    scopus 로고
    • Pro-domain removal in ASP-2 and the cleavage of the amyloid precursor are influenced by pH
    • SIDERA C, LIU C, AUSTEN B: Pro-domain removal in ASP-2 and the cleavage of the amyloid precursor are influenced by pH. BMC Biochemistry (2002) 3(1):25.
    • (2002) BMC Biochemistry , vol.3 , Issue.1 , pp. 25
    • Sidera, C.1    Liu, C.2    Austen, B.3
  • 228
    • 4544271980 scopus 로고    scopus 로고
    • Human BACE Forms Dimers and Colocalizes with APP
    • SCHMECHEL A, STRAUSS M, SCHLICKSUPP A et al.: Human BACE Forms Dimers and Colocalizes with APP. J. Biol. Chem. (2004) 279(38):39710-39717.
    • (2004) J. Biol. Chem. , vol.279 , Issue.38 , pp. 39710-39717
    • Schmechel, A.1    Strauss, M.2    Schlicksupp, A.3
  • 229
    • 11144242097 scopus 로고    scopus 로고
    • Dimerization of β-site β-amyloid precursor protein-cleaving enzyme
    • WESTMEYER GG, WILLEM M, LICHTENTHALER SF et al.: Dimerization of β-site β-amyloid precursor protein-cleaving enzyme. J. Biol. Chem. (2004) 279(51):53205-53212.
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 53205-53212
    • Westmeyer, G.G.1    Willem, M.2    Lichtenthaler, S.F.3
  • 230
    • 0642371716 scopus 로고    scopus 로고
    • β-Secretase processing of the Alzheimer's amyloid protein precursor (APP)
    • MARLOW L, CAIN M, PAPPOLLA MA, SAMBAMURTI K: β-Secretase processing of the Alzheimer's amyloid protein precursor (APP). J. Mol. Neurosci. (2003) 20(3):233-239.
    • (2003) J. Mol. Neurosci. , vol.20 , Issue.3 , pp. 233-239
    • Marlow, L.1    Cain, M.2    Pappolla, M.A.3    Sambamurti, K.4
  • 232
    • 5744225747 scopus 로고    scopus 로고
    • Secretases as therapeutic targets in Alzheimer's disease: Patents 2000-2004
    • LARNER AJ: Secretases as therapeutic targets in Alzheimer's disease: patents 2000-2004. Expert Opin. Ther. Patents (2004) 14(10):1403-1420.
    • (2004) Expert Opin. Ther. Patents , vol.14 , Issue.10 , pp. 1403-1420
    • Larner, A.J.1
  • 233
    • 16544383036 scopus 로고    scopus 로고
    • The Potential for BACE1 inhibitors in the treatment of Alzheimer's disease
    • HUSSAIN I: The Potential for BACE1 inhibitors in the treatment of Alzheimer's disease. IDrugs (2004) 7(7):653-658.
    • (2004) IDrugs , vol.7 , Issue.7 , pp. 653-658
    • Hussain, I.1
  • 234
    • 3042658599 scopus 로고    scopus 로고
    • In vivo inhibition of Ab production by memapsin 2 (b-secretase) inhibitors
    • CHANG W-P, KOELSCH G, WONG S et al.: In vivo inhibition of Ab production by memapsin 2 (b-secretase) inhibitors. J. Neurochem. (2004) 89(6):1409-1416.
    • (2004) J. Neurochem. , vol.89 , Issue.6 , pp. 1409-1416
    • Chang, W.-P.1    Koelsch, G.2    Wong, S.3
  • 235
    • 18644377487 scopus 로고    scopus 로고
    • Structure-based design of cycloamide-urethane-derived novel inhibitors of human brain memapsin 2 (β-secretase)
    • GHOSH AK, DEVASAMUDRAM T, HONG L et al.: Structure-based design of cycloamide-urethane-derived novel inhibitors of human brain memapsin 2 (β-secretase). Bioorg. Med. Chem. Lett. (2005) 15(1):3576-3585.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , Issue.1 , pp. 3576-3585
    • Ghosh, A.K.1    Devasamudram, T.2    Hong, L.3
  • 236
    • 11844297294 scopus 로고    scopus 로고
    • Structural locations and functional roles of new subsites S-5, S-6, and S-7 in memapsin 2 (P-secretase)
    • TURNER RT, HONG L, KOELSCH G, CHOSH AK, TANG J: Structural locations and functional roles of new subsites S-5, S-6, and S-7 in memapsin 2 (P-secretase). Biochemistry (2005) 44(1):105-112
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 105-112
    • Turner, R.T.1    Hong, L.2    Koelsch, G.3    Chosh, A.K.4    Tang, J.5
  • 237
    • 0036714840 scopus 로고    scopus 로고
    • Crystal structure of memapsin 2 (β-secretase) in complex with an inhibitor OM00-3
    • HONG L, TURNER RT, KOELSCH G et al.: Crystal structure of memapsin 2 (β-secretase) in complex with an inhibitor OM00-3. Biochemistry (2002) 41(36):10963-10967.
    • (2002) Biochemistry , vol.41 , Issue.36 , pp. 10963-10967
    • Hong, L.1    Turner, R.T.2    Koelsch, G.3
  • 238
    • 15244340778 scopus 로고    scopus 로고
    • Inhibition of BACE-1 by hydroxyethylsulfide, hydroxyethylamine and hydroxyethylurea isosteric replacements
    • RIZZI L, ROMEO S: Inhibition of BACE-1 by hydroxyethylsulfide, hydroxyethylamine and hydroxyethylurea isosteric replacements. Lett. Drug Design Discov. (2005) 2(2):109-112.
    • (2005) Lett. Drug Design Discov. , vol.2 , Issue.2 , pp. 109-112
    • Rizzi, L.1    Romeo, S.2
  • 239
    • 2942615456 scopus 로고    scopus 로고
    • Synthesis and SAR of bis-statine based peptides as BACE1 inhibitors
    • HU B, FAN KY, BRIDGES K et al.: Synthesis and SAR of bis-statine based peptides as BACE1 inhibitors. Bioorg. Med. Chem. Lett. (2004) 14(13):3457-3460.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , Issue.13 , pp. 3457-3460
    • Hu, B.1    Fan, K.Y.2    Bridges, K.3
  • 240
    • 9644266667 scopus 로고    scopus 로고
    • Design and synthesis of highly active Alzheimer's (β)-secretase (BACE1) inhibitors, KMI-420 and KMI-429, with enhanced chemical stability
    • KIMURA T, SHUTO D, HAMADA Y et al.: Design and synthesis of highly active Alzheimer's (β)-secretase (BACE1) inhibitors, KMI-420 and KMI-429, with enhanced chemical stability. Bioorg. Med. Chem. Lett. (2005) 15(1):211-215.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , Issue.1 , pp. 211-215
    • Kimura, T.1    Shuto, D.2    Hamada, Y.3
  • 241
    • 9744221865 scopus 로고    scopus 로고
    • Identification of a small molecule nonpeptide active site (β)-secretase inhibitor that displays a nontraditional binding mode for aspartyl proteases
    • COBURN CA, STACHEL SJ, LI YM et al.: Identification of a small molecule nonpeptide active site (β)-secretase inhibitor that displays a nontraditional binding mode for aspartyl proteases. J. Med. Chem. (2004) 47(25): 6117-6119.
    • (2004) J. Med. Chem. , vol.47 , Issue.25 , pp. 6117-6119
    • Coburn, C.A.1    Stachel, S.J.2    Li, Y.M.3
  • 242
    • 10644249886 scopus 로고    scopus 로고
    • Structure-based design of potent and selective cell-permeable inhibitors of human (β)-secretase (BACE-1)
    • STACHEL SJ, COBURN CA, STEELE TG et al.: Structure-based design of potent and selective cell-permeable inhibitors of human (β)-secretase (BACE-1). J. Med. Chem. (2004) 47(26):6447-6450
    • (2004) J. Med. Chem. , vol.47 , Issue.26 , pp. 6447-6450
    • Stachel, S.J.1    Coburn, C.A.2    Steele, T.G.3
  • 243
    • 0142059961 scopus 로고    scopus 로고
    • Heparan sulfate regulates amyloid precursor protein processing by BACE1, the Alzheimer's b-secretase
    • SCHOLEFIELD Z, YATES EA, WAYNE G et al.: Heparan sulfate regulates amyloid precursor protein processing by BACE1, the Alzheimer's b-secretase. J. Cell Biol. (2003) 163(1):97-107.
    • (2003) J. Cell Biol. , vol.163 , Issue.1 , pp. 97-107
    • Scholefield, Z.1    Yates, E.A.2    Wayne, G.3
  • 244
    • 0037076799 scopus 로고    scopus 로고
    • Platelet phagocytosis and processing of b-amyloid precursor protein as a mechanism of macrophage activation in atherosclerosis
    • DE MEYER GRY, DE CLEEN DMM, COOPER S et al.: Platelet phagocytosis and processing of b-amyloid precursor protein as a mechanism of macrophage activation in atherosclerosis. Circ. Res. (2002) 90(11):1197-1204.
    • (2002) Circ. Res. , vol.90 , Issue.11 , pp. 1197-1204
    • De Meyer, G.R.Y.1    De Cleen, D.M.M.2    Cooper, S.3
  • 245
    • 0037332094 scopus 로고    scopus 로고
    • BACE1 and BACE2 in pathologic and normal human muscle
    • VATTEMI G, ENGEL WK, McFERRIN J et al.: BACE1 and BACE2 in pathologic and normal human muscle. Exp. Neurol. (2003) 179(2):150-158.
    • (2003) Exp. Neurol. , vol.179 , Issue.2 , pp. 150-158
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3
  • 246
    • 11144355408 scopus 로고    scopus 로고
    • BACE (β-secretase) modulates the processing of APLP2 in vivo
    • PASTORINO L, IKIN AF, LAMPRIANOU S et al.: BACE (β-secretase) modulates the processing of APLP2 in vivo. Mol. Cell. Neurosci. (2004) 25(4):642-649.
    • (2004) Mol. Cell. Neurosci. , vol.25 , Issue.4 , pp. 642-649
    • Pastorino, L.1    Ikin, A.F.2    Lamprianou, S.3
  • 247
    • 1642345964 scopus 로고    scopus 로고
    • Cleavage of amyloid-β precursor protein and amyloid-β precursor-like protein by BACE 1
    • LI Q, SUEDHOF TC: Cleavage of amyloid-β precursor protein and amyloid-β precursor-like protein by BACE 1. J. Biol. Chem. (2004) 279(11):10542-10550.
    • (2004) J. Biol. Chem. , vol.279 , Issue.11 , pp. 10542-10550
    • Li, Q.1    Suedhof, T.C.2
  • 248
    • 24044497252 scopus 로고    scopus 로고
    • The LDL-receptor related protein (LRP) is a novel β-secretase (BACE 1) substrate
    • VON ARNIM CAF, KINOSHITA A, PELTAN ID et al.: The LDL-receptor related protein (LRP) is a novel β-secretase (BACE 1) substrate. J. Biol. Chem. (2005) 280(18):17777-17785
    • (2005) J. Biol. Chem. , vol.280 , Issue.18 , pp. 17777-17785
    • Von Arnim, C.A.F.1    Kinoshita, A.2    Peltan, I.D.3
  • 249
    • 21244506747 scopus 로고    scopus 로고
    • Sequences from the LRP cytoplasmic domain enhances amyloid β-protein production via the β-secretase pathway without altering APP/LRP nuclear signaling
    • YOON I-S, PIETRZIK CU, KANG DE, KOO EH: Sequences from the LRP cytoplasmic domain enhances amyloid β-protein production via the β-secretase pathway without altering APP/LRP nuclear signaling. J. Biol. Chem. (2005) 280(20):20140-20147
    • (2005) J. Biol. Chem. , vol.280 , Issue.20 , pp. 20140-20147
    • Yoon, I.-S.1    Pietrzik, C.U.2    Kang, D.E.3    Koo, E.H.4
  • 250
    • 0842325530 scopus 로고    scopus 로고
    • The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1
    • LICHTENTHALER S, DOMINGUEZ D, WESTMEYER G et al.: The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1. J. Biol. Chem. (2003) 278(49):48713-48719.
    • (2003) J. Biol. Chem. , vol.278 , Issue.49 , pp. 48713-48719
    • Lichtenthaler, S.1    Dominguez, D.2    Westmeyer, G.3
  • 251
    • 0035923502 scopus 로고    scopus 로고
    • Alzheimer's β-secretase, β-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase
    • KITAZUME S, TACHIDA Y, OKA R et al.: Alzheimer's β-secretase, β-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase. Proc. Natl. Acad. Sci. USA (2001) 98(24):13554-13559.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.24 , pp. 13554-13559
    • Kitazume, S.1    Tachida, Y.2    Oka, R.3
  • 252
    • 0037675876 scopus 로고    scopus 로고
    • Characterization of α2,6sialyltransferase cleavage by Alzheimer's β-secretase (BACE1)
    • KITAZUME S, TACHIDA Y, OKA R et al.: Characterization of α2,6sialyltransferase cleavage by Alzheimer's β-secretase (BACE1). J. Biol. Chem. (2003) 278(17):14865-14871.
    • (2003) J. Biol. Chem. , vol.278 , Issue.17 , pp. 14865-14871
    • Kitazume, S.1    Tachida, Y.2    Oka, R.3
  • 253
    • 20044374165 scopus 로고    scopus 로고
    • In vivo cleavage of α 2,6-sialyltransferase by Alzheimer β-secretase
    • KITAZUME S, NAKAGAWA K, OKA R et al.: In vivo cleavage of α 2,6-sialyltransferase by Alzheimer β-secretase. J. Biol. Chem. (2005) 280(9):8589-8595.
    • (2005) J. Biol. Chem. , vol.280 , Issue.9 , pp. 8589-8595
    • Kitazume, S.1    Nakagawa, K.2    Oka, R.3
  • 254
    • 0037930851 scopus 로고    scopus 로고
    • Targeting presenilin-type aspartic protease signal peptide peptidase with γ-secretase inhibitors
    • WEIHOFEN A, LEMBERG MK, FRIEDMANN E et al.: Targeting presenilin-type aspartic protease signal peptide peptidase with γ-secretase inhibitors. J. Biol. Chem. (2003) 278(19):16528-16533.
    • (2003) J. Biol. Chem. , vol.278 , Issue.19 , pp. 16528-16533
    • Weihofen, A.1    Lemberg, M.K.2    Friedmann, E.3
  • 255
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • LAMMICH S, KOJRO E, POSTINA R et al.: Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl. Acad. Sci. USA (1999) 96(7):3922-3927.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.7 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3
  • 256
    • 8544240891 scopus 로고    scopus 로고
    • Systemic catabolism of Alzheimer's Aβ40 and Aβ42
    • GHISO J, SHAYO, M, CALERO M et al.: Systemic catabolism of Alzheimer's Aβ40 and Aβ42. J. Biol. Chem. (2004) 279(44):45897-45908.
    • (2004) J. Biol. Chem. , vol.279 , Issue.44 , pp. 45897-45908
    • Ghiso, J.1    Shayo, M.2    Calero, M.3
  • 257
    • 0030293854 scopus 로고    scopus 로고
    • Protein topology of presenilin 1
    • DOAN A, THINAKARAN G, BORCHELT DR et al.: Protein topology of presenilin 1. Neuron (1996) 17(5):1023-1030.
    • (1996) Neuron , vol.17 , Issue.5 , pp. 1023-1030
    • Doan, A.1    Thinakaran, G.2    Borchelt, D.R.3
  • 258
    • 0942298101 scopus 로고    scopus 로고
    • Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a component of the γ-secretase complex
    • FORTNA RR, CRYSTAL AS, MORAIS VA et al.: Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a component of the γ-secretase complex. J. Biol. Chem. (2004) 279(5):3685-3693.
    • (2004) J. Biol. Chem. , vol.279 , Issue.5 , pp. 3685-3693
    • Fortna, R.R.1    Crystal, A.S.2    Morais, V.A.3
  • 259
    • 0037490200 scopus 로고    scopus 로고
    • Membrane topology of γ-secretase component PEN-2
    • CRYSTAL AS, MORAIS VA, PIERSON TC et al.: Membrane topology of γ-secretase component PEN-2. J. Biol. Chem. (2003) 278(22):20117-20123.
    • (2003) J. Biol. Chem. , vol.278 , Issue.22 , pp. 20117-20123
    • Crystal, A.S.1    Morais, V.A.2    Pierson, T.C.3
  • 260
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • THINAKARAN G, BORCHELT DR, LEE MK et al.: Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron (1996) 17(1):181-190.
    • (1996) Neuron , vol.17 , Issue.1 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3
  • 261
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • DUNN BM: Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. (2002) 102(12):4431-4458.
    • (2002) Chem. Rev. , vol.102 , Issue.12 , pp. 4431-4458
    • Dunn, B.M.1
  • 262
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize β strands in their active sites
    • TYNDALL JD, NALL T, FAIRLIE DP: Proteases universally recognize β strands in their active sites. Chem. Rev. (2005) 105(3):973-999.
    • (2005) Chem. Rev. , vol.105 , Issue.3 , pp. 973-999
    • Tyndall, J.D.1    Nall, T.2    Fairlie, D.P.3
  • 263
    • 0033950453 scopus 로고    scopus 로고
    • The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix
    • LI M, PHYLIP LH, LEES WE et al.: The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. Nat. Struct. Biol. (2000) 7(12):113-117.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.12 , pp. 113-117
    • Li, M.1    Phylip, L.H.2    Lees, W.E.3


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