메뉴 건너뛰기




Volumn 31, Issue 3, 2014, Pages 670-683

Population PKPD modeling of BACE1 inhibitor-induced reduction in Aβ levels in vivo and correlation to in vitro potency in primary cortical neurons from mouse and guinea pig

Author keywords

Alzheimer's disease; amyloid peptide; brain; cerebrospinal fluid; pharmacokinetic pharmacodynamic modeling

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; BETA SECRETASE 1; BETA SECRETASE INHIBITOR; BRAIN PROTEIN; PLASMA PROTEIN;

EID: 84895459713     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-013-1189-y     Document Type: Article
Times cited : (10)

References (60)
  • 1
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
    • 1:STN:280:DyaL2c3ks1altQ%3D%3D 6610841 10.1212/WNL.34.7.939
    • McKhann G, Drachman D, Folstein M, Katzman R, Price D, Stadlan EM. Clinical diagnosis of Alzheimer's disease: report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology. 1984;34(7):939-44.
    • (1984) Neurology , vol.34 , Issue.7 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 2
    • 75449102536 scopus 로고    scopus 로고
    • Alzheimer's disease
    • 1:CAS:528:DC%2BC3cXht1aqt7s%3D 20107219 10.1056/NEJMra0909142
    • Querfurth HW, LaFerla FM. Alzheimer's disease. N Engl J Med. 2010;362(4):329-44.
    • (2010) N Engl J Med , vol.362 , Issue.4 , pp. 329-344
    • Querfurth, H.W.1    Laferla, F.M.2
  • 3
    • 84858225391 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Alzheimer's Association 10.1016/j.jalz.2012.02.001
    • Alzheimer's Association. Alzheimer's disease facts and figures. Alzheimers Dement. 2012;8(2):131-68.
    • (2012) Alzheimers Dement , vol.8 , Issue.2 , pp. 131-168
  • 4
    • 67651180986 scopus 로고    scopus 로고
    • The amyloid hypothesis for Alzheimer's disease: A critical reappraisal
    • 1:CAS:528:DC%2BD1MXpsFOmu70%3D 19457065 10.1111/j.1471-4159.2009.06181.x
    • Hardy J. The amyloid hypothesis for Alzheimer's disease: a critical reappraisal. J Neurochem. 2009;110(4):1129-34.
    • (2009) J Neurochem , vol.110 , Issue.4 , pp. 1129-1134
    • Hardy, J.1
  • 5
    • 80052266213 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis for Alzheimer's disease: An appraisal for the development of therapeutics
    • 1:CAS:528:DC%2BC3MXhtVelsL3L 21852788 10.1038/nrd3505
    • Karran E, Mercken M, De Strooper B. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat Rev Drug Discov. 2011;10(9):698-712.
    • (2011) Nat Rev Drug Discov , vol.10 , Issue.9 , pp. 698-712
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 6
    • 84655164279 scopus 로고    scopus 로고
    • Gamma-Secretase inhibitors and modulators for Alzheimer's disease
    • 1:CAS:528:DC%2BC38XhsFyns70%3D 3254709 22122056 10.1111/j.1471-4159.2011. 07501.x
    • Wolfe MS. gamma-Secretase inhibitors and modulators for Alzheimer's disease. J Neurochem. 2012;120 Suppl 1:89-98.
    • (2012) J Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 89-98
    • Wolfe, M.S.1
  • 7
    • 84859610500 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid β-protein
    • 1:CAS:528:DC%2BC38Xht1Klsr3J 22482449 10.1016/B978-0-12-385883-2.00012-6
    • Walsh DM, Teplow DB. Alzheimer's disease and the amyloid β-protein. Prog Mol Biol Transl Sci. 2012;107:101-24.
    • (2012) Prog Mol Biol Transl Sci , vol.107 , pp. 101-124
    • Walsh, D.M.1    Teplow, D.B.2
  • 8
    • 79955663580 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing
    • 1:CAS:528:DC%2BC3MXmsFCmt7w%3D 21413990 10.1111/j.1471-4159.2011.07248.x
    • Lichtenthaler SF, Haass C, Steiner H. Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing. J Neurochem. 2011;117(5):779-96.
    • (2011) J Neurochem , vol.117 , Issue.5 , pp. 779-796
    • Lichtenthaler, S.F.1    Haass, C.2    Steiner, H.3
  • 9
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • 1:CAS:528:DC%2BD38Xls1Cju7s%3D 12130773 10.1126/science.1072994
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 2002;297(5580):353- 6.
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 10
    • 0028169925 scopus 로고
    • Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ 42(43)
    • 1:CAS:528:DyaK2cXlsFCkt74%3D 8043280 10.1016/0896-6273(94)90458-8
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ 42(43). Neuron. 1994;13(1):45-53.
    • (1994) Neuron , vol.13 , Issue.1 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 11
    • 0028945660 scopus 로고
    • Evidence that Aβ 42 is the real culprit in Alzheimer's disease
    • 1:CAS:528:DyaK2MXltFeqsL8%3D 7695227 10.1002/ana.410370303
    • Younkin SG. Evidence that Aβ 42 is the real culprit in Alzheimer's disease. Ann Neurol. 1995;37(3):287-8.
    • (1995) Ann Neurol , vol.37 , Issue.3 , pp. 287-288
    • Younkin, S.G.1
  • 12
    • 0033452874 scopus 로고    scopus 로고
    • Genes and mechanisms involved in β-amyloid generation and Alzheimer's disease
    • 1:STN:280:DC%2BD3c7hslSjtA%3D%3D 10.1007/s004060050098
    • Steiner H, Capell A, Leimer U, Haass C. Genes and mechanisms involved in β-amyloid generation and Alzheimer's disease. Eur Arch Psychiatr Clin Neurosci. 1999;249(6):266-70.
    • (1999) Eur Arch Psychiatr Clin Neurosci , vol.249 , Issue.6 , pp. 266-270
    • Steiner, H.1    Capell, A.2    Leimer, U.3    Haass, C.4
  • 13
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer's disease: Strategies for disease modification
    • 1:CAS:528:DC%2BC3cXlsVWjsrw%3D 20431570 10.1038/nrd2896
    • Citron M. Alzheimer's disease: strategies for disease modification. Nat Rev Drug Discov. 2010;9(5):387-98.
    • (2010) Nat Rev Drug Discov , vol.9 , Issue.5 , pp. 387-398
    • Citron, M.1
  • 14
    • 77956419098 scopus 로고    scopus 로고
    • REVIEW: Gamma-Secretase inhibitors for the treatment of Alzheimer's disease: The current state
    • 1:CAS:528:DC%2BC3cXht1GjtbbK 20560993 10.1111/j.1755-5949.2010.00164.x
    • Panza F, Frisardi V, Imbimbo BP, Capurso C, Logroscino G, Sancarlo D, et al. REVIEW: gamma-Secretase inhibitors for the treatment of Alzheimer's disease: the current state. CNS Neurosci Ther. 2010;16(5):272-84.
    • (2010) CNS Neurosci Ther , vol.16 , Issue.5 , pp. 272-284
    • Panza, F.1    Frisardi, V.2    Imbimbo, B.P.3    Capurso, C.4    Logroscino, G.5    Sancarlo, D.6
  • 15
    • 70350059834 scopus 로고    scopus 로고
    • Recent advances in the identification of gamma-secretase inhibitors to clinically test the Aβ oligomer hypothesis of Alzheimer's disease
    • 1:CAS:528:DC%2BD1MXhtVWktbvN 19694467 10.1021/jm900188z
    • Kreft AF, Martone R, Porte A. Recent advances in the identification of gamma-secretase inhibitors to clinically test the Aβ oligomer hypothesis of Alzheimer's disease. J Med Chem. 2009;52(20):6169-88.
    • (2009) J Med Chem , vol.52 , Issue.20 , pp. 6169-6188
    • Kreft, A.F.1    Martone, R.2    Porte, A.3
  • 16
    • 84878012448 scopus 로고    scopus 로고
    • Has inhibition of Aβ production adequately been tested as therapeutic approach in mild AD? A model-based meta-analysis of γ-secretase inhibitor data
    • 10.1007/s00228-012-1459-3 23288352
    • Niva C, Parkinson J, Olsson F, van Schaick EA, Lundkvist J, Visser SAG. Has inhibition of Aβ production adequately been tested as therapeutic approach in mild AD? A model-based meta-analysis of γ-secretase inhibitor data. Eur J Clin Pharmacol. 2013. doi: 10.1007/s00228-012-1459-3.
    • (2013) Eur J Clin Pharmacol
    • Niva, C.1    Parkinson, J.2    Olsson, F.3    Van Schaick, E.A.4    Lundkvist, J.5    Visser, S.A.G.6
  • 17
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp 2) as β-secretase
    • 1:CAS:528:DyaK1MXnt1Chsrs%3D 10656250 10.1006/mcne.1999.0811
    • Hussain I, Powell D, Howlett DR, Tew DG, Meek TD, Chapman C, et al. Identification of a novel aspartic protease (Asp 2) as β-secretase. Mol Cell Neurosci. 1999;14(6):419-27.
    • (1999) Mol Cell Neurosci , vol.14 , Issue.6 , pp. 419-427
    • Hussain, I.1    Powell, D.2    Howlett, D.R.3    Tew, D.G.4    Meek, T.D.5    Chapman, C.6
  • 18
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein β-secretase from human brain
    • 1:CAS:528:DyaK1MXotFKlsrc%3D 10591214 10.1038/990114
    • Sinha S, Anderson JP, Barbour R, Basi GS, Caccavello R, Davis D, et al. Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature. 1999;402(6761):537-40.
    • (1999) Nature , vol.402 , Issue.6761 , pp. 537-540
    • Sinha, S.1    Anderson, J.P.2    Barbour, R.3    Basi, G.S.4    Caccavello, R.5    Davis, D.6
  • 19
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • 1:CAS:528:DyaK1MXntFWit74%3D 10531052 10.1126/science.286.5440.735
    • Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, Denis P, et al. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 1999;286(5440):735-41.
    • (1999) Science , vol.286 , Issue.5440 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5    Denis, P.6
  • 20
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
    • 1:CAS:528:DyaK1MXotFKmu7k%3D 10591213 10.1038/990107
    • Yan R, Bienkowski MJ, Shuck ME, Miao H, Tory MC, Pauley AM, et al. Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity. Nature. 1999;402(6761):533-7.
    • (1999) Nature , vol.402 , Issue.6761 , pp. 533-537
    • Yan, R.1    Bienkowski, M.J.2    Shuck, M.E.3    Miao, H.4    Tory, M.C.5    Pauley, A.M.6
  • 21
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein
    • 1:CAS:528:DC%2BD3cXhsFCrsr4%3D 26455 10677483 10.1073/pnas.97.4.1456
    • Lin X, Koelsch G, Wu S, Downs D, Dashti A, Tang J. Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein. Proc Natl Acad Sci U S A. 2000;97(4):1456-60.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.4 , pp. 1456-1460
    • Lin, X.1    Koelsch, G.2    Wu, S.3    Downs, D.4    Dashti, A.5    Tang, J.6
  • 22
    • 42149130900 scopus 로고    scopus 로고
    • BACE1 structure and function in health and Alzheimer's disease
    • 1:CAS:528:DC%2BD1cXkt1als70%3D 18393796 10.2174/156720508783954758
    • Cole SL, Vassar R. BACE1 structure and function in health and Alzheimer's disease. Curr Alzheimer Res. 2008;5(2):100-20.
    • (2008) Curr Alzheimer Res , vol.5 , Issue.2 , pp. 100-120
    • Cole, S.L.1    Vassar, R.2
  • 23
    • 34250847115 scopus 로고    scopus 로고
    • The proteins BACE1 and BACE2 and β-secretase activity in normal and Alzheimer's disease brain
    • 1:CAS:528:DC%2BD2sXls1SnsLc%3D 17511655
    • Stockley JH, O'Neill C. The proteins BACE1 and BACE2 and β-secretase activity in normal and Alzheimer's disease brain. Biochem Soc Trans. 2007;35(Pt 3):574-6.
    • (2007) Biochem Soc Trans , vol.35 , Issue.PART 3 , pp. 574-576
    • Stockley, J.H.1    O'Neill, C.2
  • 25
    • 84864471159 scopus 로고    scopus 로고
    • A mutation in APP protects against Alzheimer's disease and age-related cognitive decline
    • 1:CAS:528:DC%2BC38XhtFWmt73M 22801501 10.1038/nature11283
    • Jonsson T, Atwal JK, Steinberg S, Snaedal J, Jonsson PV, Bjornsson S, et al. A mutation in APP protects against Alzheimer's disease and age-related cognitive decline. Nature. 2012;488(7409):96-9.
    • (2012) Nature , vol.488 , Issue.7409 , pp. 96-99
    • Jonsson, T.1    Atwal, J.K.2    Steinberg, S.3    Snaedal, J.4    Jonsson, P.V.5    Bjornsson, S.6
  • 26
    • 34548847452 scopus 로고    scopus 로고
    • Partial reduction of BACE1 has dramatic effects on Alzheimer plaque and synaptic pathology in APP Transgenic Mice
    • 1:CAS:528:DC%2BD2sXpslGjt74%3D 17616527 10.1074/jbc.M611687200
    • McConlogue L, Buttini M, Anderson JP, Brigham EF, Chen KS, Freedman SB, et al. Partial reduction of BACE1 has dramatic effects on Alzheimer plaque and synaptic pathology in APP Transgenic Mice. J Biol Chem. 2007;282(36):26326-34.
    • (2007) J Biol Chem , vol.282 , Issue.36 , pp. 26326-26334
    • McConlogue, L.1    Buttini, M.2    Anderson, J.P.3    Brigham, E.F.4    Chen, K.S.5    Freedman, S.B.6
  • 27
    • 33845515686 scopus 로고    scopus 로고
    • BACE1 inhibition reduces endogenous Aβ and alters APP processing in wild-type mice
    • 1:CAS:528:DC%2BD2sXjsFGrtQ%3D%3D 17083447 10.1111/j.1471-4159.2006.04178. x
    • Nishitomi K, Sakaguchi G, Horikoshi Y, Gray AJ, Maeda M, Hirata-Fukae C, et al. BACE1 inhibition reduces endogenous Aβ and alters APP processing in wild-type mice. J Neurochem. 2006;99(6):1555-63.
    • (2006) J Neurochem , vol.99 , Issue.6 , pp. 1555-1563
    • Nishitomi, K.1    Sakaguchi, G.2    Horikoshi, Y.3    Gray, A.J.4    Maeda, M.5    Hirata-Fukae, C.6
  • 28
    • 84868562686 scopus 로고    scopus 로고
    • Design and synthesis of β-Site Amyloid Precursor Protein Cleaving Enzyme (BACE1) inhibitors with in vivo brain reduction of β-Amyloid peptides
    • 1:CAS:528:DC%2BC38Xht1OmtL%2FM 22924815 10.1021/jm3009025
    • Swahn BM, Kolmodin K, Karlstrom S, von Berg S, Soderman P, Holenz J, et al. Design and synthesis of β-Site Amyloid Precursor Protein Cleaving Enzyme (BACE1) inhibitors with in vivo brain reduction of β-Amyloid peptides. J Med Chem. 2012;55(21):9346-61.
    • (2012) J Med Chem , vol.55 , Issue.21 , pp. 9346-9361
    • Swahn, B.M.1    Kolmodin, K.2    Karlstrom, S.3    Von Berg, S.4    Soderman, P.5    Holenz, J.6
  • 29
    • 84870337419 scopus 로고    scopus 로고
    • Discovery of AZD3839, a potent and selective BACE1 clinical candidate for the treatment of Alzheimers Disease
    • 1:CAS:528:DC%2BC38XhslGjs7fE 23048024 10.1074/jbc.M112.409110
    • Jeppsson F, Eketjall S, Janson J, Karlstrom S, Gustavsson S, Olsson LL, et al. Discovery of AZD3839, a potent and selective BACE1 clinical candidate for the treatment of Alzheimers Disease. J Biol Chem. 2012;287(49):41245-57.
    • (2012) J Biol Chem , vol.287 , Issue.49 , pp. 41245-41257
    • Jeppsson, F.1    Eketjall, S.2    Janson, J.3    Karlstrom, S.4    Gustavsson, S.5    Olsson, L.L.6
  • 30
    • 81555204259 scopus 로고    scopus 로고
    • Quantitative pharmacokinetic/pharmacodynamic analyses suggest that the 129/SVE mouse is a suitable preclinical pharmacology model for identifying small-molecule gamma-secretase inhibitors
    • 1:CAS:528:DC%2BC38XjtVSksLs%3D 21930801 10.1124/jpet.111.186791
    • Lu Y, Zhang L, Nolan CE, Becker SL, Atchison K, Robshaw AE, et al. Quantitative pharmacokinetic/pharmacodynamic analyses suggest that the 129/SVE mouse is a suitable preclinical pharmacology model for identifying small-molecule gamma-secretase inhibitors. J Pharmacol Exp Ther. 2011;339(3):922-34.
    • (2011) J Pharmacol Exp Ther , vol.339 , Issue.3 , pp. 922-934
    • Lu, Y.1    Zhang, L.2    Nolan, C.E.3    Becker, S.L.4    Atchison, K.5    Robshaw, A.E.6
  • 31
    • 33750128392 scopus 로고    scopus 로고
    • Macrocyclic inhibitors of β-secretase: Functional activity in an animal model
    • 1:CAS:528:DC%2BD28XptVymtbw%3D 17034118 10.1021/jm060884i
    • Stachel SJ, Coburn CA, Sankaranarayanan S, Price EA, Wu G, Crouthamel M, et al. Macrocyclic inhibitors of β-secretase: functional activity in an animal model. J Med Chem. 2006;49(21):6147-50.
    • (2006) J Med Chem , vol.49 , Issue.21 , pp. 6147-6150
    • Stachel, S.J.1    Coburn, C.A.2    Sankaranarayanan, S.3    Price, E.A.4    Wu, G.5    Crouthamel, M.6
  • 32
    • 34547566031 scopus 로고    scopus 로고
    • Discovery of isonicotinamide derived β-secretase inhibitors: In vivo reduction of β-amyloid
    • 1:CAS:528:DC%2BD2sXms1Cisrw%3D 17583334 10.1021/jm070272d
    • Stanton MG, Stauffer SR, Gregro AR, Steinbeiser M, Nantermet P, Sankaranarayanan S, et al. Discovery of isonicotinamide derived β-secretase inhibitors: in vivo reduction of β-amyloid. J Med Chem. 2007;50(15):3431-3.
    • (2007) J Med Chem , vol.50 , Issue.15 , pp. 3431-3433
    • Stanton, M.G.1    Stauffer, S.R.2    Gregro, A.R.3    Steinbeiser, M.4    Nantermet, P.5    Sankaranarayanan, S.6
  • 33
    • 77955863408 scopus 로고    scopus 로고
    • A noncompetitive BACE1 inhibitor TAK-070 ameliorates Aβ pathology and behavioral deficits in a mouse model of Alzheimer's disease
    • 1:CAS:528:DC%2BC3cXhtFWms73E 20720123 10.1523/JNEUROSCI.2884-10.2010
    • Fukumoto H, Takahashi H, Tarui N, Matsui J, Tomita T, Hirode M, et al. A noncompetitive BACE1 inhibitor TAK-070 ameliorates Aβ pathology and behavioral deficits in a mouse model of Alzheimer's disease. J Neurosci. 2010;30(33):11157-66.
    • (2010) J Neurosci , vol.30 , Issue.33 , pp. 11157-11166
    • Fukumoto, H.1    Takahashi, H.2    Tarui, N.3    Matsui, J.4    Tomita, T.5    Hirode, M.6
  • 34
    • 79551633353 scopus 로고    scopus 로고
    • β-secretase inhibitor GRL-8234 rescues age-related cognitive decline in APP transgenic mice
    • 1:CAS:528:DC%2BC3MXhvFSmsbY%3D 21059748 10.1096/fj.10-167213
    • Chang WP, Huang X, Downs D, Cirrito JR, Koelsch G, Holtzman DM, et al. β-secretase inhibitor GRL-8234 rescues age-related cognitive decline in APP transgenic mice. FASEB J. 2011;25(2):775-84.
    • (2011) FASEB J , vol.25 , Issue.2 , pp. 775-784
    • Chang, W.P.1    Huang, X.2    Downs, D.3    Cirrito, J.R.4    Koelsch, G.5    Holtzman, D.M.6
  • 35
    • 84864120319 scopus 로고    scopus 로고
    • CSF Aβ As An Effect Biomarker for Brain Aβ Lowering Verified by Quantitative Preclinical Analyses
    • Lu Y, Riddell D, Hajos-Korcsok E, Bales K, Wood KM, Nolan CE, et al. CSF Aβ As An Effect Biomarker For Brain Aβ Lowering Verified by Quantitative Preclinical Analyses. J Pharmacol Exp Ther. 2012;342(2):366-75.
    • (2012) J Pharmacol Exp Ther , vol.342 , Issue.2 , pp. 366-375
    • Lu, Y.1    Riddell, D.2    Hajos-Korcsok, E.3    Bales, K.4    Wood, K.M.5    Nolan, C.E.6
  • 36
    • 84859788625 scopus 로고    scopus 로고
    • Discovery of cyclic sulfone hydroxyethylamines as potent and selective β-site APP-cleaving enzyme 1 (BACE1) inhibitors: Structure-based design and in vivo reduction of amyloid β-peptides
    • 1:CAS:528:DC%2BC38XjtVCqsLs%3D 22380629 10.1021/jm300069y
    • Rueeger H, Lueoend R, Rogel O, Rondeau JM, Mobitz H, Machauer R, et al. Discovery of cyclic sulfone hydroxyethylamines as potent and selective β-site APP-cleaving enzyme 1 (BACE1) inhibitors: structure-based design and in vivo reduction of amyloid β-peptides. J Med Chem. 2012;55(7):3364-86.
    • (2012) J Med Chem , vol.55 , Issue.7 , pp. 3364-3386
    • Rueeger, H.1    Lueoend, R.2    Rogel, O.3    Rondeau, J.M.4    Mobitz, H.5    Machauer, R.6
  • 37
    • 84867590777 scopus 로고    scopus 로고
    • Establishing the relationship between in vitro potency, pharmacokinetic, and pharmacodynamic parameters in a series of orally available, hydroxyethylamine-derived β-secretase inhibitors
    • 1:CAS:528:DC%2BC38XhsFKktbrE 22911925 10.1124/jpet.112.197954
    • Wood S, Wen PH, Zhang J, Zhu L, Luo Y, Babu-Khan S, et al. Establishing the relationship between in vitro potency, pharmacokinetic, and pharmacodynamic parameters in a series of orally available, hydroxyethylamine-derived β-secretase inhibitors. J Pharmacol Exp Ther. 2012;343(2):460-7.
    • (2012) J Pharmacol Exp Ther , vol.343 , Issue.2 , pp. 460-467
    • Wood, S.1    Wen, P.H.2    Zhang, J.3    Zhu, L.4    Luo, Y.5    Babu-Khan, S.6
  • 38
    • 84867516398 scopus 로고    scopus 로고
    • Design and preparation of a potent series of hydroxyethylamine containing β-secretase inhibitors that demonstrate robust reduction of central β-amyloid
    • 1:CAS:528:DC%2BC38XkvFOnt78%3D 22468639 10.1021/jm300119p
    • Weiss MM, Williamson T, Babu-Khan S, Bartberger MD, Brown J, Chen K, et al. Design and preparation of a potent series of hydroxyethylamine containing β-secretase inhibitors that demonstrate robust reduction of central β-amyloid. J Med Chem. 2012;55(21):9009-24.
    • (2012) J Med Chem , vol.55 , Issue.21 , pp. 9009-9024
    • Weiss, M.M.1    Williamson, T.2    Babu-Khan, S.3    Bartberger, M.D.4    Brown, J.5    Chen, K.6
  • 39
    • 84867590210 scopus 로고    scopus 로고
    • Design and synthesis of potent, orally efficacious hydroxyethylamine derived β-site amyloid precursor protein cleaving enzyme (BACE1) inhibitors
    • 1:CAS:528:DC%2BC38XkvFOnsbg%3D 22468684 10.1021/jm300118s
    • Dineen TA, Weiss MM, Williamson T, Acton P, Babu-Khan S, Bartberger MD, et al. Design and synthesis of potent, orally efficacious hydroxyethylamine derived β-site amyloid precursor protein cleaving enzyme (BACE1) inhibitors. J Med Chem. 2012;55(21):9025-44.
    • (2012) J Med Chem , vol.55 , Issue.21 , pp. 9025-9044
    • Dineen, T.A.1    Weiss, M.M.2    Williamson, T.3    Acton, P.4    Babu-Khan, S.5    Bartberger, M.D.6
  • 40
    • 84868543653 scopus 로고    scopus 로고
    • New Aminoimidazoles as β-Secretase (BACE-1) inhibitors showing amyloid-β (Aβ) lowering in Brain
    • 1:CAS:528:DC%2BC38XhsVagtLfI 23017051 10.1021/jm300991n
    • Gravenfors Y, Viklund J, Blid J, Ginman T, Karlstrom S, Kihlstrom J, et al. New Aminoimidazoles as β-Secretase (BACE-1) inhibitors showing amyloid-β (Aβ) lowering in Brain. J Med Chem. 2012;55(21):9297-311.
    • (2012) J Med Chem , vol.55 , Issue.21 , pp. 9297-9311
    • Gravenfors, Y.1    Viklund, J.2    Blid, J.3    Ginman, T.4    Karlstrom, S.5    Kihlstrom, J.6
  • 41
    • 59149083352 scopus 로고    scopus 로고
    • First demonstration of cerebrospinal fluid and plasma Aβ lowering with oral administration of a β-site amyloid precursor protein-cleaving enzyme 1 inhibitor in nonhuman primates
    • 1:CAS:528:DC%2BD1MXisFyltw%3D%3D 18854490 10.1124/jpet.108.143628
    • Sankaranarayanan S, Holahan MA, Colussi D, Crouthamel MC, Devanarayan V, Ellis J, et al. First demonstration of cerebrospinal fluid and plasma Aβ lowering with oral administration of a β-site amyloid precursor protein-cleaving enzyme 1 inhibitor in nonhuman primates. J Pharmacol Exp Ther. 2009;328(1):131-40.
    • (2009) J Pharmacol Exp Ther , vol.328 , Issue.1 , pp. 131-140
    • Sankaranarayanan, S.1    Holahan, M.A.2    Colussi, D.3    Crouthamel, M.C.4    Devanarayan, V.5    Ellis, J.6
  • 42
    • 81255143061 scopus 로고    scopus 로고
    • Robust central reduction of amyloid-β in humans with an orally available, non-peptidic β-secretase inhibitor
    • 1:CAS:528:DC%2BC3MXhsFaksL7F 22090477 10.1523/JNEUROSCI.3647-11.2011
    • May PC, Dean RA, Lowe SL, Martenyi F, Sheehan SM, Boggs LN, et al. Robust central reduction of amyloid-β in humans with an orally available, non-peptidic β-secretase inhibitor. J Neurosci. 2011;31(46):16507-16.
    • (2011) J Neurosci , vol.31 , Issue.46 , pp. 16507-16516
    • May, P.C.1    Dean, R.A.2    Lowe, S.L.3    Martenyi, F.4    Sheehan, S.M.5    Boggs, L.N.6
  • 43
    • 84857365050 scopus 로고    scopus 로고
    • Aminoimidazoles as BACE-1 inhibitors: The challenge to achieve in vivo brain efficacy
    • 1:CAS:528:DC%2BC38XitFyhsL0%3D 22325942 10.1016/j.bmcl.2012.01.079
    • Swahn BM, Holenz J, Kihlstrom J, Kolmodin K, Lindstrom J, Plobeck N, et al. Aminoimidazoles as BACE-1 inhibitors: the challenge to achieve in vivo brain efficacy. Bioorg Med Chem Lett. 2012;22(5):1854-9.
    • (2012) Bioorg Med Chem Lett , vol.22 , Issue.5 , pp. 1854-1859
    • Swahn, B.M.1    Holenz, J.2    Kihlstrom, J.3    Kolmodin, K.4    Lindstrom, J.5    Plobeck, N.6
  • 44
    • 79956145323 scopus 로고    scopus 로고
    • High-throughput analysis of standardized pharmacokinetic studies in the rat using sample pooling and UPLC-MS/MS
    • 1:CAS:528:DC%2BC3MXmsFWku7s%3D 21530131 10.1016/j.jpba.2011.03.042
    • Bueters T, Dahlstrom J, Kvalvagnaes K, Betner I, Briem S. High-throughput analysis of standardized pharmacokinetic studies in the rat using sample pooling and UPLC-MS/MS. J Pharm Biomed Anal. 2011;55(5):1120-6.
    • (2011) J Pharm Biomed Anal , vol.55 , Issue.5 , pp. 1120-1126
    • Bueters, T.1    Dahlstrom, J.2    Kvalvagnaes, K.3    Betner, I.4    Briem, S.5
  • 45
    • 0014314845 scopus 로고
    • Brain and choroid plexus blood volumes in vertebrates
    • 1:STN:280:DyaE3M%2Fls1GmsA%3D%3D 5758880 10.1016/0010-406X(68)90641-5
    • Heisey SR. Brain and choroid plexus blood volumes in vertebrates. Comp Biochem Physiol. 1968;26(2):489-98.
    • (1968) Comp Biochem Physiol , vol.26 , Issue.2 , pp. 489-498
    • Heisey, S.R.1
  • 46
    • 14344264538 scopus 로고    scopus 로고
    • P-glycoprotein and mutlidrug resistance-associated proteins limit the brain uptake of saquinavir in mice
    • 1:CAS:528:DC%2BD2MXitVOgs7k%3D 15528451 10.1124/jpet.104.076216
    • Park S, Sinko PJ. P-glycoprotein and mutlidrug resistance-associated proteins limit the brain uptake of saquinavir in mice. J Pharmacol Exp Ther. 2005;312(3):1249-56.
    • (2005) J Pharmacol Exp Ther , vol.312 , Issue.3 , pp. 1249-1256
    • Park, S.1    Sinko, P.J.2
  • 48
    • 66649119187 scopus 로고    scopus 로고
    • Development of a high-throughput brain slice method for studying drug distribution in the central nervous system
    • 1:CAS:528:DC%2BD1MXmslamu70%3D 19299522 10.1124/dmd.108.026377
    • Friden M, Ducrozet F, Middleton B, Antonsson M, Bredberg U, Hammarlund-Udenaes M. Development of a high-throughput brain slice method for studying drug distribution in the central nervous system. Drug Metab Dispos. 2009;37(6):1226-33.
    • (2009) Drug Metab Dispos , vol.37 , Issue.6 , pp. 1226-1233
    • Friden, M.1    Ducrozet, F.2    Middleton, B.3    Antonsson, M.4    Bredberg, U.5    Hammarlund-Udenaes, M.6
  • 49
    • 0027769745 scopus 로고
    • Comparison of four basic models of indirect pharmacodynamic responses
    • 1:CAS:528:DyaK2cXitlGhsb0%3D 8133465 10.1007/BF01061691
    • Dayneka NL, Garg V, Jusko WJ. Comparison of four basic models of indirect pharmacodynamic responses. J Pharmacokinet Biopharm. 1993;21(4):457-78.
    • (1993) J Pharmacokinet Biopharm , vol.21 , Issue.4 , pp. 457-478
    • Dayneka, N.L.1    Garg, V.2    Jusko, W.J.3
  • 50
    • 33644878338 scopus 로고    scopus 로고
    • The novel β-secretase inhibitor KMI-429 reduces amyloid β peptide production in amyloid precursor protein transgenic and wild-type mice
    • 1:CAS:528:DC%2BD28XntVShsA%3D%3D 16336629 10.1111/j.1471-4159.2005.03576. x
    • Asai M, Hattori C, Iwata N, Saido TC, Sasagawa N, Szabo B, et al. The novel β-secretase inhibitor KMI-429 reduces amyloid β peptide production in amyloid precursor protein transgenic and wild-type mice. J Neurochem. 2006;96(2):533-40.
    • (2006) J Neurochem , vol.96 , Issue.2 , pp. 533-540
    • Asai, M.1    Hattori, C.2    Iwata, N.3    Saido, T.C.4    Sasagawa, N.5    Szabo, B.6
  • 51
    • 80055104131 scopus 로고    scopus 로고
    • A technique for serial collection of cerebrospinal fluid from the cisterna magna in mouse
    • Nov
    • Liu L, Duff K. A technique for serial collection of cerebrospinal fluid from the cisterna magna in mouse. J Vis Exp 2008 Nov 10;(21).
    • (2008) J Vis Exp , vol.10 , Issue.21
    • Liu, L.1    Duff, K.2
  • 52
    • 77957882573 scopus 로고    scopus 로고
    • Design of an orally efficacious hydroxyethylamine (HEA) BACE-1 inhibitor in a preclinical animal model
    • 1:CAS:528:DC%2BC3cXht1KrsbjP 20833041 10.1016/j.bmcl.2010.08.102
    • Truong AP, Toth G, Probst GD, Sealy JM, Bowers S, Wone DW, et al. Design of an orally efficacious hydroxyethylamine (HEA) BACE-1 inhibitor in a preclinical animal model. Bioorg Med Chem Lett. 2010;20(21):6231-6.
    • (2010) Bioorg Med Chem Lett , vol.20 , Issue.21 , pp. 6231-6236
    • Truong, A.P.1    Toth, G.2    Probst, G.D.3    Sealy, J.M.4    Bowers, S.5    Wone, D.W.6
  • 53
    • 84870692858 scopus 로고    scopus 로고
    • Integrating experimentation and quantitative modeling to enhance discovery of Beta amyloid lowering therapeutics for Alzheimer's disease
    • Lu Y. Integrating experimentation and quantitative modeling to enhance discovery of Beta amyloid lowering therapeutics for Alzheimer's disease. Front Pharmacol. 2012;3(177):1-6.
    • (2012) Front Pharmacol , vol.3 , Issue.177 , pp. 1-6
    • Lu, Y.1
  • 54
    • 33847065994 scopus 로고    scopus 로고
    • Mechanism-based pharmacokinetic-pharmacodynamic modeling for the prediction of in vivo drug concentration-effect relationships -application in drug candidate selection and lead optimization
    • (2nd Ed.) "ADME-Tox: The Fate of Drugs in the Body". Editors Bernard Testa and Han van de Waterbeemd
    • Danhof M, Van der Graaf PH, Jonker DM, Visser SAG, Zuideveld KP. Mechanism-based pharmacokinetic-pharmacodynamic modeling for the prediction of in vivo drug concentration-effect relationships -application in drug candidate selection and lead optimization. 2007. Comprehensive Medicinal Chemistry (2nd Ed.) Volume 5: "ADME-Tox: The Fate of Drugs in the Body". Editors Bernard Testa and Han van de Waterbeemd.
    • (2007) Comprehensive Medicinal Chemistry , vol.5
    • Danhof, M.1    Van Der Graaf, P.H.2    Jonker, D.M.3    Sag, V.4    Zuideveld, K.P.5
  • 55
    • 84883213203 scopus 로고    scopus 로고
    • The virtue of translational PKPD modeling in drug discovery: Selecting the right clinical candidate while sparing animal lives
    • 10.1016/j.drudis.2013.05.001 23665277
    • Bueters T, Ploeger BA, Visser SA. The virtue of translational PKPD modeling in drug discovery: selecting the right clinical candidate while sparing animal lives. Drug Discov Today. 2013. doi: 10.1016/j.drudis.2013.05.001.
    • (2013) Drug Discov Today
    • Bueters, T.1    Ploeger, B.A.2    Visser, S.A.3
  • 56
    • 45049086920 scopus 로고    scopus 로고
    • Flavonols and flavones as BACE-1 inhibitors: Structure-activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features
    • 1:CAS:528:DC%2BD1cXkvFWqurw%3D 18295609 10.1016/j.bbagen.2008.01.017
    • Shimmyo Y, Kihara T, Akaike A, Niidome T, Sugimoto H. Flavonols and flavones as BACE-1 inhibitors: structure-activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features. Biochim Biophys Acta. 2008;1780(5):819-25.
    • (2008) Biochim Biophys Acta , vol.1780 , Issue.5 , pp. 819-825
    • Shimmyo, Y.1    Kihara, T.2    Akaike, A.3    Niidome, T.4    Sugimoto, H.5
  • 57
    • 0344129030 scopus 로고    scopus 로고
    • Guinea-pig primary cell cultures provide a model to study expression and amyloidogenic processing of endogenous amyloid precursor protein
    • 1:CAS:528:DyaK1MXnsVKgurw%3D 10619481 10.1016/S0306-4522(99)00390-5
    • Beck M, Bruckner MK, Holzer M, Kaap S, Pannicke T, Arendt T, et al. Guinea-pig primary cell cultures provide a model to study expression and amyloidogenic processing of endogenous amyloid precursor protein. Neuroscience. 2000;95(1):243-54.
    • (2000) Neuroscience , vol.95 , Issue.1 , pp. 243-254
    • Beck, M.1    Bruckner, M.K.2    Holzer, M.3    Kaap, S.4    Pannicke, T.5    Arendt, T.6
  • 58
    • 10644265978 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of BACE1: Investigation into the putative species-specificity for β- And β'-cleavage sites by human and murine BACE1
    • 1:CAS:528:DC%2BD2MXmslah 15584902 10.1111/j.1471-4159.2004.02764.x
    • Yang HC, Chai X, Mosior M, Kohn W, Boggs LN, Erickson JA, et al. Biochemical and kinetic characterization of BACE1: investigation into the putative species-specificity for β- and β'-cleavage sites by human and murine BACE1. J Neurochem. 2004;91(6):1249-59.
    • (2004) J Neurochem , vol.91 , Issue.6 , pp. 1249-1259
    • Yang, H.C.1    Chai, X.2    Mosior, M.3    Kohn, W.4    Boggs, L.N.5    Erickson, J.A.6
  • 59
    • 0035960535 scopus 로고    scopus 로고
    • The functional gamma-secretase inhibitor prevents production of amyloid β 1-34 in human and murine cell lines
    • 1:CAS:528:DC%2BD3MXosFKqs7g%3D 11716984 10.1016/S0304-3940(01)02369-2
    • Vandermeeren M, Geraerts M, Pype S, Dillen L, Van Hove C, Mercken M. The functional gamma-secretase inhibitor prevents production of amyloid β 1-34 in human and murine cell lines. Neurosci Lett. 2001;315(3):145-8.
    • (2001) Neurosci Lett , vol.315 , Issue.3 , pp. 145-148
    • Vandermeeren, M.1    Geraerts, M.2    Pype, S.3    Dillen, L.4    Van Hove, C.5    Mercken, M.6
  • 60
    • 79551679201 scopus 로고    scopus 로고
    • Pharmacodynamic-pharmacokinetic integration as a guide to medicinal chemistry
    • 1:CAS:528:DC%2BC3MXkslSnurw%3D 21320067 10.2174/156802611794480864
    • Gabrielsson J, Fjellstrom O, Ulander J, Rowley M, Van Der Graaf PH. Pharmacodynamic-pharmacokinetic integration as a guide to medicinal chemistry. Curr Top Med Chem. 2011;11(4):404-18.
    • (2011) Curr Top Med Chem , vol.11 , Issue.4 , pp. 404-418
    • Gabrielsson, J.1    Fjellstrom, O.2    Ulander, J.3    Rowley, M.4    Van Der Graaf, P.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.