메뉴 건너뛰기




Volumn 14, Issue 10, 2004, Pages 1403-1420

Secretases as therapeutic targets in Alzheimer's disease: Patents 2000 - 2004

Author keywords

secretase; secretase; secretase; Alzheimer's disease; Amyloid peptide; Inhibitor

Indexed keywords

ALDEHYDE DERIVATIVE; ALIPHATIC AMINE; ALPHA SECRETASE; ALPHA SECRETASE INHIBITOR; AMYLOID PRECURSOR PROTEIN; AROMATIC COMPOUND; BENZAMIDE DERIVATIVE; BETA SECRETASE; BETA SECRETASE INHIBITOR; BMS 299897; ETHYLENE DERIVATIVE; FUSED HETEROCYCLIC RINGS; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; GLUTARIC ACID DERIVATIVE; HYDRAZINE DERIVATIVE; LACTAM DERIVATIVE; LETEPRINIM; LY 450139; MACROCYCLIC COMPOUND; MIFEPRISTONE; NOOTROPIC AGENT; PIPERAZINE DERIVATIVE; PIPERIDINE DERIVATIVE; QUINALDINE DERIVATIVE; S ADENOSYLMETHIONINE; STATINE DERIVATIVE; SUCCINIC ACID DERIVATIVE; TALSACLIDINE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 5744225747     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.14.10.1403     Document Type: Review
Times cited : (20)

References (84)
  • 1
    • 0030930122 scopus 로고    scopus 로고
    • Alzheimer's disease: Towards therapeutic manipulation of the amyloid precursor protein and amyloid β-peptides
    • LARNER AJ, ROSSOR MN: Alzheimer's disease: towards therapeutic manipulation of the amyloid precursor protein and amyloid β-peptides. Expert Opin. Ther. Patents (1997) 7 10):1115-1127.
    • (1997) Expert Opin. Ther. Patents , vol.7 , Issue.10 , pp. 1115-1127
    • Larner, A.J.1    Rossor, M.N.2
  • 2
    • 0036481246 scopus 로고    scopus 로고
    • Alzheimer's disease: Targets for drug development
    • LARNER AJ: Alzheimer's disease: targets for drug development. Mini Rev. Med. Chem. (2002) 2:1-9.
    • (2002) Mini Rev. Med. Chem. , vol.2 , pp. 1-9
    • Larner, A.J.1
  • 3
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • HARDY J, ALLSOP D: Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. (1991) 12:383-388.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 4
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • ARRIAGADA PV, GROWDON JH, HEDLEY-WHITE ET, HYMAN BT: Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology (1992) 42:631-639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-White, E.T.3    Hyman, B.T.4
  • 5
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLEAN CA, CHERNY RA, FRASER FW et al.: Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. (1999) 46:860-866.
    • (1999) Ann. Neurol. , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3
  • 6
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • LUE LF, KUO YM, ROHER AE et al.: Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. (1999) 155:853-862.
    • (1999) Am. J. Pathol. , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3
  • 7
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline
    • NÄSLUND J, HAROUTUNIAN V, MOHS R et al.: Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA (2000) 283:1571-1577.
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Näslund, J.1    Haroutunian, V.2    Mohs, R.3
  • 8
    • 0026721943 scopus 로고
    • β-Amyloid precursor protein cleavage by a membrane-bound protease
    • SISODIA SS: β-Amyloid precursor protein cleavage by a membrane-bound protease. Proc. Natl. Acad. Sci. USA (1992) 89 6075-6079.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 9
    • 0034107524 scopus 로고    scopus 로고
    • A second cytotoxic proteolytic peptide derived from amyloid β-protein precursor
    • LU DC, RABIZADEH S, CHANDRA S et al.: A second cytotoxic proteolytic peptide derived from amyloid β-protein precursor. Nat. Med. (2000) 6:397-404.
    • (2000) Nat. Med. , vol.6 , pp. 397-404
    • Lu, D.C.1    Rabizadeh, S.2    Chandra, S.3
  • 10
    • 0029360529 scopus 로고
    • Hypothesis: Physiological and pathological interrelationships of amyloid β-peptide and the amyloid precursor protein
    • LARNER AJ: Hypothesis: physiological and pathological interrelationships of amyloid β-peptide and the amyloid precursor protein. Bioessays (1995) 17:819-824.
    • (1995) Bioessays , vol.7 , pp. 819-824
    • Larner, A.J.1
  • 11
    • 0033944538 scopus 로고    scopus 로고
    • Amyloid β interacts with the amyloid precursor protein: A potential toxic mechanism in Alzheimer's disease
    • LORENZO A, YUAN M, ZHANG Z et al.: Amyloid β interacts with the amyloid precursor protein: a potential toxic mechanism in Alzheimer's disease. Nat. Neurosci. (2000) 3:460-464.
    • (2000) Nat. Neurosci. , vol.3 , pp. 460-464
    • Lorenzo, A.1    Yuan, M.2    Zhang, Z.3
  • 12
    • 0345602771 scopus 로고    scopus 로고
    • Amyloid β-protein toxicity mediated by the formation of amyloid-β protein precursor complexes
    • LU DC, SHAKED GM, MASLIAH E, BREDESEN DE, KOO EH: Amyloid β-protein toxicity mediated by the formation of amyloid-β protein precursor complexes. Ann. Neurol. (2003) 54:781-789.
    • (2003) Ann. Neurol. , vol.54 , pp. 781-789
    • Lu, D.C.1    Shaked, G.M.2    Masliah, E.3    Bredesen, D.E.4    Koo, E.H.5
  • 13
    • 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) 373:523-527.
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 14
    • 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) 274:99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 15
    • 0041357787 scopus 로고    scopus 로고
    • The secretases of Alzheimer's disease
    • WOLFE MS: The secretases of Alzheimer's disease. Curr. Top. Dev. Biol. (2003) 54:233-261.
    • (2003) Curr. Top. Dev. Biol. , vol.54 , pp. 233-261
    • Wolfe, M.S.1
  • 16
    • 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) 286:735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3
  • 17
    • 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) 402:537-540.
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1    Anderson, J.P.2    Barbour, R.3
  • 18
    • 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) 402:533-537.
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1    Bienkowski, M.J.2    Shuck, M.E.3
  • 19
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp2) as β-secretase
    • HUSSAIN I, POWELL D, HOWLETT DR et al.: Identification of a novel aspartic protease (Asp2) as β-secretase. Mol. Cell. Neurosci. (1999) 14:419-427.
    • (1999) Mol. Cell. Neurosci. , vol.14 , pp. 419-427
    • Hussain, I.1    Powell, D.2    Howlett, D.R.3
  • 20
    • 0034192158 scopus 로고    scopus 로고
    • β-Secretase revealed: Starting gate for race to novel therapies for Alzheimer's disease
    • SKOVRONSKY DM, LEE VM-Y: β-Secretase revealed: starting gate for race to novel therapies for Alzheimer's disease. Trends Pharmacol. Sci. (2000) 21:161-163.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 161-163
    • Skovronsky, D.M.1    Lee, V.M.-Y.2
  • 21
    • 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) 4:233-234.
    • (2001) Nat. Neurosci. , vol.4 , pp. 233-234
    • Cai, H.1    Wang, Y.2    Mccarthy, D.3
  • 22
    • 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) 97:9712-9717.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9712-9717
    • Farzan, M.1    Schnitzler, C.E.2    Vasilieva, N.3    Leung, D.4    Choe, H.5
  • 23
    • 0033819772 scopus 로고    scopus 로고
    • A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein β-secretase
    • SOLANS A, ESTIVILL X, DE LA LUNA S: A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein β-secretase. Cytogenet. Cell Genet. (2000) 89 177-184.
    • (2000) Cytogenet. Cell Genet. , vol.89 , pp. 177-184
    • Solans, A.1    Estivill, X.2    De La Luna, S.3
  • 24
    • 0034617199 scopus 로고    scopus 로고
    • Expression analysis of BACE2 in brain and peripheral tissues
    • BENNETT BD, BABU-KHAN S, LOELOFF R et al.: Expression analysis of BACE2 in brain and peripheral tissues. J. Biol. Chem. (2000) 275:20647-20651.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20647-20651
    • Bennett, B.D.1    Babu-Khan, S.2    Loeloff, R.3
  • 25
  • 26
    • 0036718272 scopus 로고    scopus 로고
    • β-Secretase protein and activity are increased in the neocortex in Alzheimer's disease
    • FUKUMOTO H, CHEUNG BS, HYMAN BT, IRIZARRY MC: β-Secretase protein and activity are increased in the neocortex in Alzheimer's disease. Arch. Neurol. (2002) 59:1381-1389.
    • (2002) Arch. Neurol. , vol.59 , pp. 1381-1389
    • Fukumoto, H.1    Cheung, B.S.2    Hyman, B.T.3    Irizarry, M.C.4
  • 28
    • 0037236622 scopus 로고    scopus 로고
    • Elevated β-secretase expression and enzymatic activity detected in sporadic Alzheimer's disease
    • YANG LB, LINDHOLM K, YAN R et al.: Elevated β-secretase expression and enzymatic activity detected in sporadic Alzheimer's disease. Nat. Med. (2003) 9:3-4.
    • (2003) Nat. Med. , vol.9 , pp. 3-4
    • Yang, L.B.1    Lindholm, K.2    Yan, R.3
  • 29
    • 0037113352 scopus 로고    scopus 로고
    • Levels of β-secretase BACE and α-secretase ADAM10 mRNAs in Alzheimer hippocampus
    • GATTA LB, ALBERTINI A, RAVID R, FINAZZI D: Levels of β-secretase BACE and α-secretase ADAM10 mRNAs in Alzheimer hippocampus. Neuroreport (2002) 15:2031-2033.
    • (2002) Neuroreport , vol.15 , pp. 2031-2033
    • Gatta, L.B.1    Albertini, A.2    Ravid, R.3    Finazzi, D.4
  • 30
    • 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) 4:231-232.
    • (2001) Nat. Neurosci. , vol.4 , pp. 231-232
    • Luo, Y.1    Bolon, B.2    Kahn, S.3
  • 31
    • 17344388652 scopus 로고    scopus 로고
    • BACE knockout mice are healthy despite lacking the primary β-secretase activity in brain: Implications for Alzheimer's disease therapeutics
    • ROBERDS SL, ANDERSON J, BASI G et al.: BACE knockout mice are healthy despite lacking the primary β-secretase activity in brain: implications for Alzheimer's disease therapeutics. Hum. Mol. Genet. (2001) 10:1317-1324.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1317-1324
    • Roberds, S.L.1    Anderson, J.2    Basi, G.3
  • 32
    • 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) 24:646-655.
    • (2003) Mol. Cell. Neurosci. , vol.24 , pp. 646-655
    • Harrison, S.M.1    Harper, A.J.2    Hawkins, J.3
  • 33
    • 0842325530 scopus 로고    scopus 로고
    • The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1
    • LICHTENTHALER SF, DOMINGUEZ DI, WESTMEYER GG et al.: The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1. J. Biol. Chem. (2003) 278 48713-48719.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48713-48719
    • Lichtenthaler, S.F.1    Dominguez, D.I.2    Westmeyer, G.G.3
  • 34
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • DE STROOPER B, SAFTIG P, GAESSAERTS K et al.: Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature (1998) 391:387-390.
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Gaessaerts, K.3
  • 35
    • 0038652102 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) 100:6382-6387.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6382-6387
    • Kimberly, W.T.1    Lavoie, M.J.2    Ostaszewski, B.L.3
  • 36
    • 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 9-12.
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 37
    • 0036861121 scopus 로고    scopus 로고
    • γ-Secretase: Characterization and implication for Alzheimer's disease therapy
    • XU M, LIA MT, HUANG Q et al.: γ-Secretase: characterization and implication for Alzheimer's disease therapy. Neurobiol. Aging (2002) 23:1023-1030.
    • (2002) Neurobiol. Aging , vol.23 , pp. 1023-1030
    • Xu, M.1    Lia, M.T.2    Huang, Q.3
  • 38
    • 0036898485 scopus 로고    scopus 로고
    • Alzheimer's disease γ-secretase: A complex story of GxGD-type presenilin proteases
    • HAASS C, STEINER H: Alzheimer's disease γ-secretase: a complex story of GxGD-type presenilin proteases. Trends Cell Biol. (2002) 12:556-562.
    • (2002) Trends Cell Biol. , vol.12 , pp. 556-562
    • Haass, C.1    Steiner, H.2
  • 39
    • 0041355557 scopus 로고    scopus 로고
    • Notch and presenilin: Regulated intramembrane proteolysis links development and degeneration
    • SELKOE D, KOPAN R: Notch and presenilin: regulated intramembrane proteolysis links development and degeneration. Ann. Rev. Neurosci. (2003) 26:565-597.
    • (2003) Ann. Rev. Neurosci. , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 40
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the amyloid plaques of Alzheimer's disease is increased in vivo by the presenilin-1 and -2 and APP mutations linked to familial Alzheimer's disease
    • SCHEUNER D, ECKMAN C, JENSEN M et al.: Secreted amyloid β-protein similar to that in the amyloid plaques of Alzheimer's disease is increased in vivo by the presenilin-1 and -2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. (1996 2 864-870.
    • (1996) Nat. Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 41
    • 0242331600 scopus 로고    scopus 로고
    • A presenilin dimer at the core of the γ-secretase enzyme: Insights from parallel analysis of Notch-1 and APP proteolysis
    • SCHROETER EH, ILAGAN MX, BRUNKAN AL et al.: A presenilin dimer at the core of the γ-secretase enzyme: insights from parallel analysis of Notch-1 and APP proteolysis. Proc. Natl. Acad. Sci. USA (2003) 100:13075-13080.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13075-13080
    • Schroeter, E.H.1    Ilagan, M.X.2    Brunkan, A.L.3
  • 42
    • 11144357241 scopus 로고    scopus 로고
    • A novel presenilin-1 mutation associated with Pick's disease but not β-amyloid plaques
    • DERMAUT B, KUMAR-SINGH S, ENGELBORGHS S et al.: A novel presenilin-1 mutation associated with Pick's disease but not β -amyloid plaques. Ann. Neurol. (2004) 55:617-626.
    • (2004) Ann. Neurol. , vol.55 , pp. 617-626
    • Dermaut, B.1    Kumar-Singh, S.2    Engelborghs, S.3
  • 43
    • 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) 89 629-639.
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1    Bronson, R.T.2    Chen, D.F.3
  • 44
    • 0031915681 scopus 로고    scopus 로고
    • A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity
    • WOLFE MS, CITRON M, DIEHL TS, XIA W, DONKOR IO, SELKOE DJ: A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity. J. Med. Chem. (1998) 41:6-9.
    • (1998) J. Med. Chem. , vol.41 , pp. 6-9
    • Wolfe, M.S.1    Citron, M.2    Diehl, T.S.3    Xia, W.4    Donkor, I.O.5    Selkoe, D.J.6
  • 45
    • 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) 76:173-181.
    • (2001) J. Neurochem. , vol.76 , pp. 173-181
    • Dovey, H.F.1    John, V.2    Anderson, J.P.3
  • 46
    • 0038476561 scopus 로고    scopus 로고
    • The γ-secretase inhibitor N-(N-(3,5-difluorophenacetyl)-L-alanyl)-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 CA, PALLANTE G et al.: The γ-secretase inhibitor N-(N-(3,5-difluorophenacetyl)-L-alanyl)-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) 305:864-871.
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , pp. 864-871
    • Lanz, T.A.1    Himes, C.A.2    Pallante, G.3
  • 47
    • 5744242532 scopus 로고    scopus 로고
    • Presenilins in memory, Alzheimer's disease, and therapy
    • MARJAUX E, HARTMANN D, DE STROOPER B: Presenilins in memory, Alzheimer's disease, and therapy. Neuron (2004) 42:189-192.
    • (2004) Neuron , vol.42 , pp. 189-192
    • Marjaux, E.1    Hartmann, D.2    De Strooper, B.3
  • 48
    • 11144355129 scopus 로고    scopus 로고
    • Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits β-amyloid peptide production and alters lymphopoiesis and intestinal cell differentation
    • WONG GT, MANFRA D, POULET FM et al.: Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits β-amyloid peptide production and alters lymphopoiesis and intestinal cell differentation. J. Biol. Chem. (2004) 279:12876-12882.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12876-12882
    • Wong, G.T.1    Manfra, D.2    Poulet, F.M.3
  • 49
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent α-secretase competes with β-secretase for cleavage of amyloid-β precursor protein in the transgolgi network
    • SKOVRONSKY DM, MOORE DB, MILLA ME, DOMS RW, LEE VM-Y: Protein kinase C-dependent α-secretase competes with β-secretase for cleavage of amyloid-β precursor protein in the transgolgi network. J. Biol. Chem. (2000) 275:2568-2575.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.-Y.5
  • 50
    • 0037474447 scopus 로고    scopus 로고
    • Putative function of ADAM9, ADAM10, and ADAM17 as APP α-secretase
    • MASASHI A, HATTORI C, SZABO B et al.: Putative function of ADAM9, ADAM10, and ADAM17 as APP α-secretase. Biochem. Biophys. Res. Commun. (2003) 301:231-235.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 231-235
    • Masashi, A.1    Hattori, C.2    Szabo, B.3
  • 52
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer's disease mouse model
    • POSTINA R, SCHROEDER A, DEWACHTER I et al.: A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer's disease mouse model. J. Clin. Invest. (2004) 113:1456-1464.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1456-1464
    • Postina, R.1    Schroeder, A.2    Dewachter, I.3
  • 53
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloproteinase ADAM10 is essential for Notch signalling but not for α-secretase activity in fibroblasts
    • HARTMANN D, DE STROOPER B, SERNEELS L et al.: The disintegrin/metalloproteinase ADAM10 is essential for Notch signalling but not for α-secretase activity in fibroblasts. Hum. Mol. Genet. (2002) 11:2615-2624.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2615-2624
    • Hartmann, D.1    De Strooper, B.2    Serneels, L.3
  • 54
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM10
    • KOJRO E, GIMPL G, LAMMICH S, MARZ W, FAHRENHOLZ F: Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM10. Proc. Natl. Acad. Sci. USA (2001) 98 5815-5820.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 55
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer's disease associated with 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors
    • WOLOZIN B, KELLMAN W, RUOSSEAU P, CELESIA GG, SIEGEL G: Decreased prevalence of Alzheimer's disease associated with 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors. Arch. Neurol. (2000) 57:1439-1443.
    • (2000) Arch. Neurol. , vol.57 , pp. 1439-1443
    • Wolozin, B.1    Kellman, W.2    Ruosseau, P.3    Celesia, G.G.4    Siegel, G.5
  • 57
    • 0036126850 scopus 로고    scopus 로고
    • Use of lipid-lowering agents, indication bias, and the risk of dementia in community-dwelling elderly people
    • ROCKWOOD K, KIRKLAND S, HOGAN DB et al.: Use of lipid-lowering agents, indication bias, and the risk of dementia in community-dwelling elderly people. Arch. Neurol. (2002) 59 223-227.
    • (2002) Arch. Neurol. , vol.59 , pp. 223-227
    • Rockwood, K.1    Kirkland, S.2    Hogan, D.B.3
  • 58
    • 0942278990 scopus 로고    scopus 로고
    • Association between statin use and Alzheimer's disease
    • ZAMRINI E, MCGWIN G, ROSEMAN JM: Association between statin use and Alzheimer's disease. Neuroepidemiology (2004) 23 94-98.
    • (2004) Neuroepidemiology , vol.23 , pp. 94-98
    • Zamrini, E.1    McGwin, G.2    Roseman, J.M.3
  • 59
    • 0037122704 scopus 로고    scopus 로고
    • Design of substrate-based inhibitors of human β-secretase
    • TUNG JS, DAVIS DL, ANDERSON JP et al.: Design of substrate-based inhibitors of human β-secretase. J. Med. Chem. (2002) 45:259-262.
    • (2002) J. Med. Chem. , vol.45 , pp. 259-262
    • Tung, J.S.1    Davis, D.L.2    Anderson, J.P.3
  • 60
    • 0034965645 scopus 로고    scopus 로고
    • Statin-derived tetrapeptide inhibitors of β-secretase
    • NO AUTHORS LISTED
    • NO AUTHORS LISTED: Statin-derived tetrapeptide inhibitors of β-secretase. Expert Opin. Ther. Patents (2001) 11 6):1047-1050.
    • (2001) Expert Opin. Ther. Patents , vol.11 , Issue.6 , pp. 1047-1050
  • 61
    • 0037740743 scopus 로고    scopus 로고
    • Design and synthesis of statine-based permeable peptidomimetic inhibitors of human β secretase
    • HOM RK, FANG LY, MAMO S et al.: Design and synthesis of statine-based permeable peptidomimetic inhibitors of human β secretase. J. Med. Chem. (2003) 46:1799-1802.
    • (2003) J. Med. Chem. , vol.46 , pp. 1799-1802
    • Hom, R.K.1    Fang, L.Y.2    Mamo, S.3
  • 62
    • 9144267815 scopus 로고    scopus 로고
    • Design and synthesis of hydroxyethylene-based peptidomimetic inhibitors of human β-secretase
    • HOM RK, GAILUNAS AF, MAMO S et al.: Design and synthesis of hydroxyethylene-based peptidomimetic inhibitors of human β-secretase. J. Med. Chem. (2004) 47:158-164.
    • (2004) J. Med. Chem. , vol.47 , pp. 158-164
    • Hom, R.K.1    Gailunas, A.F.2    Mamo, S.3
  • 64
    • 0034633995 scopus 로고    scopus 로고
    • Proteolytic activation of recombinant pro-memapsin 2 (pro-β-secretase) studied with new fluorogenic substrates
    • [Erratum Biochemistry (2000) 39:16263]
    • ERMOLIEFF J, LOY JA, KOELSCH G, TANG J: Proteolytic activation of recombinant pro-memapsin 2 (pro-β-secretase) studied with new fluorogenic substrates. Biochemistry (2000) 39 12450-12456 [Erratum Biochemistry (2000) 39:16263].
    • (2000) Biochemistry , vol.39 , pp. 12450-12456
    • Ermolieff, J.1    Loy, J.A.2    Koelsch, G.3    Tang, J.4
  • 65
    • 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) 39:8698-8704.
    • (2000) Biochemistry , vol.39 , pp. 8698-8704
    • Shearman, M.S.1    Beher, D.2    Clarke, E.E.3
  • 66
    • 0035942322 scopus 로고    scopus 로고
    • Biochemical characterization of the γ-secretase activity that produces β-amyloid peptides
    • ZHANG L, SONG L, TERRACINA G, LIU Y, PRAMANIK B, PARKER E: Biochemical characterization of the γ-secretase activity that produces β-amyloid peptides. Biochemistry (2001) 40:5049-5055.
    • (2001) Biochemistry , vol.40 , pp. 5049-5055
    • Zhang, L.1    Song, L.2    Terracina, G.3    Liu, Y.4    Pramanik, B.5    Parker, E.6
  • 67
    • 5744246473 scopus 로고    scopus 로고
    • β-amyloid reductions in brain, plasma and CSF of a transgenic mouse model of Alzheimer's disease with a γ-secretase inhibitor
    • BARTEN DM, GUSS VL, CORSA JA et al.: β-amyloid reductions in brain, plasma and CSF of a transgenic mouse model of Alzheimer's disease with a γ-secretase inhibitor. Neurobiol. Aging (2004) 25(S2):S82.
    • (2004) Neurobiol. Aging , vol.25 , Issue.SUPPL. 2
    • Barten, D.M.1    Guss, V.L.2    Corsa, J.A.3
  • 68
    • 5744250730 scopus 로고    scopus 로고
    • Safety tolerability, and changes in plasma and cerebrospinal fluid amyloid β concentrations after administration of a functional γ-secretase inhibitor in healthy volunteers
    • SIEMERS E, DEAN RA, SATTERWHITE J et al.: Safety, tolerability, and changes in plasma and cerebrospinal fluid amyloid β concentrations after administration of a functional γ -secretase inhibitor in healthy volunteers. Neurobiol. Aging (2004 25 S2):S569-S570.
    • (2004) Neurobiol. Aging , vol.25 , Issue.SUPPL. 2
    • Siemers, E.1    Dean, R.A.2    Satterwhite, J.3
  • 71
    • 0036014124 scopus 로고    scopus 로고
    • A Phase I study of AIT-082 in healthy elderly volunteers
    • GRUNDMAN M, FARLOW M, PEAVY G et al.: A Phase I study of AIT-082 in healthy elderly volunteers. J. Mol. Neurosci. (2002) 18:283-293.
    • (2002) J. Mol. Neurosci. , vol.18 , pp. 283-293
    • Grundman, M.1    Farlow, M.2    Peavy, G.3
  • 72
    • 0038631907 scopus 로고    scopus 로고
    • A multicenter, randomized, placebo-controlled, multiple-dose, safety and pharmacokinetic study of AIT-082 (Neotrofin) in mild Alzheimer's disease patients
    • GRUNDMAN M, CAPPARELLI E, KIM HT et al.: A multicenter, randomized, placebo-controlled, multiple-dose, safety and pharmacokinetic study of AIT-082 (Neotrofin) in mild Alzheimer's disease patients. Life Sci. (2003) 73:539-553.
    • (2003) Life Sci. , vol.73 , pp. 539-553
    • Grundman, M.1    Capparelli, E.2    Kim, H.T.3
  • 73
    • 0037232314 scopus 로고    scopus 로고
    • Prion diseases: Update on therapeutic patents, 1999-2002
    • LARNER AJ, DORAN M: Prion diseases: update on therapeutic patents, 1999-2002. Expert Opin. Ther. Patents (2003) 13 1):67-78.
    • (2003) Expert Opin. Ther. Patents , vol.13 , Issue.1 , pp. 67-78
    • Larner, A.J.1    Doran, M.2
  • 74
    • 0141618463 scopus 로고    scopus 로고
    • Synthesis of potent β-secretase inhibitors containing a hydroxyethylamine dipeptide isostere and their structure-activity relationship studies
    • TAMAMURA H, KATO T, OTAKA A, FUJII N: Synthesis of potent β-secretase inhibitors containing a hydroxyethylamine dipeptide isostere and their structure-activity relationship studies. Org. Biomol. Chem. (2003) 1:2468-2473.
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 2468-2473
    • Tamamura, H.1    Kato, T.2    Otaka, A.3    Fujii, N.4
  • 75
    • 0344927114 scopus 로고    scopus 로고
    • KMI-008, a novel β-secretase inhibitor containing a hydroxymethylcarbonyl isostere as a transition-state mimic: Design and synthesis of substrate-based octapeptides
    • SHUTO D, KASAI S, KIMURA T et al.: KMI-008, a novel β-secretase inhibitor containing a hydroxymethylcarbonyl isostere as a transition-state mimic: design and synthesis of substrate-based octapeptides. Bioorg. Med. Chem. Lett. (2003) 13:4273-4276.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 4273-4276
    • Shuto, D.1    Kasai, S.2    Kimura, T.3
  • 76
    • 5744255125 scopus 로고    scopus 로고
    • In vivo inhibition of brain Aβ level by memapsin 2 (β-secretase) inhibitors
    • CHANG W-P, KOELSCH G, WONG S et al.: In vivo inhibition of brain Aβ level by memapsin 2 (β-secretase) inhibitors. Neurobiol. Aging (2004) 25(S2):S581.
    • (2004) Neurobiol. Aging , vol.25 , Issue.SUPPL. 2
    • Chang, W.-P.1    Koelsch, G.2    Wong, S.3
  • 77
    • 5744253338 scopus 로고    scopus 로고
    • A role for APP and BACE1 in cognition
    • WONG PC, CAI H, LAIRD FM et al.: A role for APP and BACE1 in cognition. Neurobiol. Aging (2004) 25(S2):S2.
    • (2004) Neurobiol. Aging , vol.25 , Issue.SUPPL. 2
    • Wong, P.C.1    Cai, H.2    Laird, F.M.3
  • 78
    • 0035829592 scopus 로고    scopus 로고
    • 42 independently of cyclooxygenase activity
    • 42 independently of cyclooxygenase activity. Nature (2001) 414:212-216.
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1    Eriksen, J.L.2    Pas, P.3
  • 80
    • 5744220886 scopus 로고    scopus 로고
    • Cholinesterase inhibitor use at a cognitive function clinic
    • 14,18
    • LARNER AJ: Cholinesterase inhibitor use at a cognitive function clinic. Prog. Neurol. Psychiatr. (2004) 8 4):14,18,20.
    • (2004) Prog. Neurol. Psychiatr. , vol.8 , Issue.4 , pp. 20
    • Larner, A.J.1
  • 81
    • 0038100154 scopus 로고    scopus 로고
    • Antibodies against β-amyloid slow cognitive decline in Alzheimer's disease
    • HOCK C, KONIETZKO U, STREFFER JR et al.: Antibodies against β-amyloid slow cognitive decline in Alzheimer's disease. Neuron (2003) 38:547-554.
    • (2003) Neuron , vol.38 , pp. 547-554
    • Hock, C.1    Konietzko, U.2    Streffer, J.R.3
  • 82
    • 5744234114 scopus 로고    scopus 로고
    • Neuropsychological, CSF, and neuropathological effects of Aβ immunotherapy (AN1792) of Alzheimer's disease in an interrupted trial
    • GILMAN S, KOLLER M, BLACK RS et al.: Neuropsychological, CSF, and neuropathological effects of Aβ immunotherapy (AN1792) of Alzheimer's disease in an interrupted trial. Neurobiol. Aging (2004) 25(S2):S84.
    • (2004) Neurobiol. Aging , vol.25 , Issue.SUPPL. 2
    • Gilman, S.1    Koller, M.2    Black, R.S.3
  • 83
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer's disease after immunization with amyloid-β peptide: A case report
    • NICOLL JAR, WILKINSON D, HOLMES C, STEART P, MARKHAM H, WELLER RO: Neuropathology of human Alzheimer's disease after immunization with amyloid-β peptide: a case report. Nat. Med. (2003) 9 448-452.
    • (2003) Nat. Med. , vol.9 , pp. 448-452
    • Nicoll, J.A.R.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 84
    • 1042265187 scopus 로고    scopus 로고
    • Neuropathology and pathogenesis of encephalitis following amyolid-β immunization in Alzheimer's disease
    • FERRER I, BRADA-ROVIRA M, SANCHEZ-GUERRA ML, REY JL, COSTA-JUSSA F: Neuropathology and pathogenesis of encephalitis following amyolid-β immunization in Alzheimer's disease. Brain Pathol. (2004) 14:11-20.
    • (2004) Brain Pathol. , vol.14 , pp. 11-20
    • Ferrer, I.1    Brada-Rovira, M.2    Sanchez-Guerra, M.L.3    Rey, J.L.4    Costa-Jussa, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.