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Volumn 165, Issue 3, 2004, Pages 937-948

A synthetic peptide blocking the apolipoprotein E/β-amyloid binding mitigates β-amyloid toxicity and fibril formation in vitro and reduces β-amyloid plaques in transgenic mice

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[12-28]; APOLIPOPROTEIN E; CHAPERONE; PROLINE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; VALINE;

EID: 4344659648     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)63355-X     Document Type: Article
Times cited : (140)

References (88)
  • 1
    • 0034701238 scopus 로고    scopus 로고
    • The origins of Alzheimer disease: A is for amyloid
    • Selkoe DJ: The origins of Alzheimer disease: a is for amyloid. JAMA 2000, 283:1615-1617
    • (2000) JAMA , vol.283 , pp. 1615-1617
    • Selkoe, D.J.1
  • 2
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease: Analysis of circular dichroism spectra
    • Barrow CJ, Yasuda A, Kenny PT, Zagorski MG: Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease: analysis of circular dichroism spectra. J Mol Biol 1992, 225:1075-1093
    • (1992) J Mol Biol , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 3
    • 0033569486 scopus 로고    scopus 로고
    • Molecular pathogenesis of apolipoprotein E-mediated amyloidosis in late-onset Alzheimer's disease
    • Tomiyama T, Corder EH, Mori H: Molecular pathogenesis of apolipoprotein E-mediated amyloidosis in late-onset Alzheimer's disease. Cell Mol Life Sci 1999, 56:268-279
    • (1999) Cell Mol Life Sci , vol.56 , pp. 268-279
    • Tomiyama, T.1    Corder, E.H.2    Mori, H.3
  • 5
    • 0028173205 scopus 로고
    • Amyloid-associated proteins α 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • Ma J, Yee A, Brewer Jr HB, Das S, Potter H: Amyloid-associated proteins α 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments. Nature 1994, 372:92-94
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer Jr., H.B.3    Das, S.4    Potter, H.5
  • 6
    • 0037015020 scopus 로고    scopus 로고
    • The Alzheimer's A β-peptide is deposited at sites of complement activation in pathologic deposits associated with aging and age-related macular degeneration
    • Johnson LV, Leitner WP, Rivest AJ, Staples MK, Radeke MJ, Anderson DH: The Alzheimer's A β-peptide is deposited at sites of complement activation in pathologic deposits associated with aging and age-related macular degeneration. Proc Natl Acad Sci USA 2002, 99:11830-11835
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11830-11835
    • Johnson, L.V.1    Leitner, W.P.2    Rivest, A.J.3    Staples, M.K.4    Radeke, M.J.5    Anderson, D.H.6
  • 9
    • 0027374047 scopus 로고
    • Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions
    • Rebeck GW, Reiter JS, Strickland DK, Hyman BT: Apolipoprotein E in sporadic Alzheimer's disease: allelic variation and receptor interactions. Neuron 1993, 11:575-580
    • (1993) Neuron , vol.11 , pp. 575-580
    • Rebeck, G.W.1    Reiter, J.S.2    Strickland, D.K.3    Hyman, B.T.4
  • 10
    • 0034931756 scopus 로고    scopus 로고
    • Alzheimer β amyloid deposition enhanced by ApoE ε 4 gene precedes neurofibrillary pathology in the frontal association cortex of non-demented senior subjects
    • Yamaguchi H, Sugihara S, Ogawa A, Oshima N, Ihara Y: Alzheimer β amyloid deposition enhanced by ApoE ε 4 gene precedes neurofibrillary pathology in the frontal association cortex of non-demented senior subjects. J Neuropathol Exp Neurol 2001, 60:731-739
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 731-739
    • Yamaguchi, H.1    Sugihara, S.2    Ogawa, A.3    Oshima, N.4    Ihara, Y.5
  • 11
    • 0029866177 scopus 로고    scopus 로고
    • The interaction between apolipoprotein E and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation
    • Golabek AA, Soto C, Vogel T, Wisniewski T: The interaction between apolipoprotein E and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation. J Biol Chem 1996, 271:10602-10606
    • (1996) J Biol Chem , vol.271 , pp. 10602-10606
    • Golabek, A.A.1    Soto, C.2    Vogel, T.3    Wisniewski, T.4
  • 16
    • 0029063033 scopus 로고
    • Amyloid β binding proteins in vitro and in normal human cerebrospinal fluid
    • Golabek AA, Marques M, Lalowski M, Wisniewski T: Amyloid β binding proteins in vitro and in normal human cerebrospinal fluid. Neurosci Lett 1995, 191:79-82
    • (1995) Neurosci Lett , vol.191 , pp. 79-82
    • Golabek, A.A.1    Marques, M.2    Lalowski, M.3    Wisniewski, T.4
  • 17
    • 0029938009 scopus 로고    scopus 로고
    • Interaction between human amphipathic apolipoproteins and amyloid β-peptide: Surface plasmon resonance studies
    • Shuvaev VV, Siest G: Interaction between human amphipathic apolipoproteins and amyloid β-peptide: surface plasmon resonance studies. FEBS Lett 1996, 383:9-12
    • (1996) FEBS Lett , vol.383 , pp. 9-12
    • Shuvaev, V.V.1    Siest, G.2
  • 20
    • 0000448998 scopus 로고    scopus 로고
    • Alzheimer Aβ neurotoxicity: Promotion by antichymotrypsin, apoE4; inhibition by Aβ-related peptides
    • Ma J, Brewer BH, Potter H, Brewer Jr HB: Alzheimer Aβ neurotoxicity: promotion by antichymotrypsin, apoE4; inhibition by Aβ-related peptides. Neurobiol Aging 1996, 17:773-780
    • (1996) Neurobiol Aging , vol.17 , pp. 773-780
    • Ma, J.1    Brewer, B.H.2    Potter, H.3    Brewer Jr., H.B.4
  • 21
    • 0023473545 scopus 로고
    • Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern
    • Gorevic PD, Castaño EM, Sarma R, Frangione B: Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern. Biochem Biophys Res Commun 1987, 147:854-862
    • (1987) Biochem Biophys Res Commun , vol.147 , pp. 854-862
    • Gorevic, P.D.1    Castaño, E.M.2    Sarma, R.3    Frangione, B.4
  • 24
    • 0034884382 scopus 로고    scopus 로고
    • Immunization with a non-toxic/non-fibrillar amyloid-β homologous peptide reduces Alzheimer's disease associated pathology in transgenic mice
    • Sigurdsson EM, Scholtzova H, Mehta P, Frangione B, Wisniewski T: Immunization with a non-toxic/non-fibrillar amyloid-β homologous peptide reduces Alzheimer's disease associated pathology in transgenic mice. Am J Pathol 2001, 159:439-447
    • (2001) Am J Pathol , vol.159 , pp. 439-447
    • Sigurdsson, E.M.1    Scholtzova, H.2    Mehta, P.3    Frangione, B.4    Wisniewski, T.5
  • 26
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • Stine WB, Dahlgren KN, Krafft GA, LaDu MJ: In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J Biol Chem 2003, 278:11612-11622
    • (2003) J Biol Chem , vol.278 , pp. 11612-11622
    • Stine, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 29
    • 0032080231 scopus 로고    scopus 로고
    • Glial fibrillary acidic protein-apolipoprotein E (apoE) transgenic mice: Astrocyte-specific expression and differing biological effects of astrocyte-secreted apoE3 and apoE4 lipoproteins
    • Sun YL, Wu S, Bu GJ, Onifade MK, Patel SN, LaDu MJ, Fagan AM, Holtzman DM: Glial fibrillary acidic protein-apolipoprotein E (apoE) transgenic mice: astrocyte-specific expression and differing biological effects of astrocyte-secreted apoE3 and apoE4 lipoproteins. J Neurosci 1998, 18:3261-3272
    • (1998) J Neurosci , vol.18 , pp. 3261-3272
    • Sun, Y.L.1    Wu, S.2    Bu, G.J.3    Onifade, M.K.4    Patel, S.N.5    LaDu, M.J.6    Fagan, A.M.7    Holtzman, D.M.8
  • 30
    • 0029865644 scopus 로고    scopus 로고
    • Alzheimer's soluble β-amyloid is conformationally modified by apolipoproteins in vitro
    • Soto C, Golabek AA, Wisniewski T, Castaño EM: Alzheimer's soluble β-amyloid is conformationally modified by apolipoproteins in vitro. Neuroreport 1996, 7:721-725
    • (1996) Neuroreport , vol.7 , pp. 721-725
    • Soto, C.1    Golabek, A.A.2    Wisniewski, T.3    Castaño, E.M.4
  • 31
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N, Fasman GD: Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969, 8:4108-4115
    • (1969) Biochemistry , vol.8 , pp. 4108-4115
    • Greenfield, N.1    Fasman, G.D.2
  • 32
    • 0026696116 scopus 로고
    • Analysis of circular dichroism spectrum of proteins using the convex constraint algorithim
    • Perczel A, Park K, Fasman GD: Analysis of circular dichroism spectrum of proteins using the convex constraint algorithim. Anal Biochem 1992, 203:83-93
    • (1992) Anal Biochem , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 33
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism
    • Manavalan P, Johnson C: Variable selection method improves the prediction of protein secondary structure from circular dichroism. Anal Biochem 1987, 167:76-85
    • (1987) Anal Biochem , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson, C.2
  • 34
    • 0026599616 scopus 로고
    • Extending CD spectra of proteins to 168nm improves the analysis for secondary structures
    • Toumadje A, Alcorn SW, Johnson C: Extending CD spectra of proteins to 168nm improves the analysis for secondary structures. Anal Biochem 1992, 200:321-331
    • (1992) Anal Biochem , vol.200 , pp. 321-331
    • Toumadje, A.1    Alcorn, S.W.2    Johnson, C.3
  • 35
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerma N, Woody RW: A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 1993, 209:32-44
    • (1993) Anal Biochem , vol.209 , pp. 32-44
    • Sreerma, N.1    Woody, R.W.2
  • 36
    • 0032527063 scopus 로고    scopus 로고
    • Induced expression of neuronal membrane attack complex and cell death by Alzheimer's β-amyloid peptide
    • Shen Y, Sullivan T, Lee CM, Meri S, Shiosaki K, Lin CW: Induced expression of neuronal membrane attack complex and cell death by Alzheimer's β-amyloid peptide. Brain Res 1998, 796:187-197
    • (1998) Brain Res , vol.796 , pp. 187-197
    • Shen, Y.1    Sullivan, T.2    Lee, C.M.3    Meri, S.4    Shiosaki, K.5    Lin, C.W.6
  • 37
    • 0037124108 scopus 로고    scopus 로고
    • Signaling events in amyloid β-peptide-induced neuronal death and insulin-like growth factor I protection
    • Wei WL, Wang XT, Kusiak JW: Signaling events in amyloid β-peptide-induced neuronal death and insulin-like growth factor I protection. J Biol Chem 2002, 277:17649-17656
    • (2002) J Biol Chem , vol.277 , pp. 17649-17656
    • Wei, W.L.1    Wang, X.T.2    Kusiak, J.W.3
  • 38
    • 0028921915 scopus 로고
    • Characterization of apolipoprotein J-Alzheimer's A β interaction
    • Matsubara E, Frangione B, Ghiso J: Characterization of apolipoprotein J-Alzheimer's A β interaction. J Biol Chem 1995, 270:7563-7567
    • (1995) J Biol Chem , vol.270 , pp. 7563-7567
    • Matsubara, E.1    Frangione, B.2    Ghiso, J.3
  • 39
    • 0015795516 scopus 로고
    • Labeling of proteins to high-specific radioactivities by conjugation to A 1-125-containing acylating agent: Application to radioimmunoassay
    • Bolton AE, Hunter WM: Labeling of proteins to high-specific radioactivities by conjugation to A 1-125-containing acylating agent: application to radioimmunoassay. Biochem J 1973, 133:529-538
    • (1973) Biochem J , vol.133 , pp. 529-538
    • Bolton, A.E.1    Hunter, W.M.2
  • 40
    • 0027344775 scopus 로고
    • Radioiodination of proteins using N-succinimidyl 4-hydroxy-3-iodobenzoate
    • Vaidyanathan G, Affleck DJ, Zalutsky MR: Radioiodination of proteins using N-succinimidyl 4-hydroxy-3-iodobenzoate. Bioconjug Chem 1993, 4:78-84
    • (1993) Bioconjug Chem , vol.4 , pp. 78-84
    • Vaidyanathan, G.1    Affleck, D.J.2    Zalutsky, M.R.3
  • 41
    • 4344616255 scopus 로고    scopus 로고
    • Preparation of avidin conjugates
    • Edited by Walker JM. Totowa NJ, Humana Press
    • Haugland RP, Bhalgat MK: Preparation of avidin conjugates. The Protein Protocols Handbook. Edited by Walker JM. Totowa NJ, Humana Press, 2002, pp 365-374
    • (2002) The Protein Protocols Handbook , pp. 365-374
    • Haugland, R.P.1    Bhalgat, M.K.2
  • 44
    • 0037180796 scopus 로고    scopus 로고
    • Long-term dendritic spine stability in the adult cortex
    • Grutzendler J, Kasthuri N, Gan WB: Long-term dendritic spine stability in the adult cortex. Nature 2002, 420:812-816
    • (2002) Nature , vol.420 , pp. 812-816
    • Grutzendler, J.1    Kasthuri, N.2    Gan, W.B.3
  • 49
    • 0022429302 scopus 로고
    • Guidelines on the recognition of pain, distress, and discomfort in experimental animals and an hypothesis for assessment
    • Morton DB, Griffiths PH: Guidelines on the recognition of pain, distress, and discomfort in experimental animals and an hypothesis for assessment. Vet Rec 1985, 116:431-436
    • (1985) Vet Rec , vol.116 , pp. 431-436
    • Morton, D.B.1    Griffiths, P.H.2
  • 53
    • 0032756213 scopus 로고    scopus 로고
    • Behavioral changes in transgenic mice expressing both amyloid precursor protein and presenilin-1 mutations: Lack of association with amyloid deposits
    • Holcomb LA, Gordon MN, Jantzen P, Hsiao K, Duff K, Morgan D: Behavioral changes in transgenic mice expressing both amyloid precursor protein and presenilin-1 mutations: lack of association with amyloid deposits. Behav Genet 1999, 29:177-185
    • (1999) Behav Genet , vol.29 , pp. 177-185
    • Holcomb, L.A.1    Gordon, M.N.2    Jantzen, P.3    Hsiao, K.4    Duff, K.5    Morgan, D.6
  • 54
    • 0034736182 scopus 로고    scopus 로고
    • Quantitative histological analysis of amyloid deposition in Alzheimer's double transgenic mouse brain
    • Wengenack TM, Whelan S, Curran GL, Duff KE, Poduslo JF: Quantitative histological analysis of amyloid deposition in Alzheimer's double transgenic mouse brain. Neuroscience 2000, 101:939-944
    • (2000) Neuroscience , vol.101 , pp. 939-944
    • Wengenack, T.M.1    Whelan, S.2    Curran, G.L.3    Duff, K.E.4    Poduslo, J.F.5
  • 59
    • 0025327731 scopus 로고
    • Unbiased stereological estimation of the number of neurons in the human hippocampus
    • West MJ, Gundersen HJG: Unbiased stereological estimation of the number of neurons in the human hippocampus. J Comp Neurol 1990, 296:1-22
    • (1990) J Comp Neurol , vol.296 , pp. 1-22
    • West, M.J.1    Gundersen, H.J.G.2
  • 60
    • 0026339976 scopus 로고
    • Unbiased stereological estimation of the total number of neurons in the subdivisions of the rat hippocampus using the optical fractionator
    • West MJ, Slomianka L, Gundersen HJG: Unbiased stereological estimation of the total number of neurons in the subdivisions of the rat hippocampus using the optical fractionator. Anat Rec 1991, 231:482-497
    • (1991) Anat Rec , vol.231 , pp. 482-497
    • West, M.J.1    Slomianka, L.2    Gundersen, H.J.G.3
  • 64
    • 0001792809 scopus 로고    scopus 로고
    • Antibodies directed to the carboxyl terminus of amyloid β-peptide recognize sequence epitopes and distinct immunoreactive ' deposits in Alzheimer's disease brain
    • Jimenez-Huete A, Alfonso P, Soto C, Albar JP, Rabano A, Ghiso J, Frangione B: Antibodies directed to the carboxyl terminus of amyloid β-peptide recognize sequence epitopes and distinct immunoreactive ' deposits in Alzheimer's disease brain. Alzheimers Rep 1998, 1:41-47
    • (1998) Alzheimers Rep , vol.1 , pp. 41-47
    • Jimenez-Huete, A.1    Alfonso, P.2    Soto, C.3    Albar, J.P.4    Rabano, A.5    Ghiso, J.6    Frangione, B.7
  • 65
    • 0026542786 scopus 로고
    • Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski T, Frangione B: Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci Lett 1992, 135:235-238
    • (1992) Neurosci Lett , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 67
    • 0032995727 scopus 로고    scopus 로고
    • Receptor-mediated transport of human amyloid β-protein 1-40 and 1-42 at the blood-brain barrier
    • Poduslo JF, Curran GL, Sanyal B, Selkoe DJ: Receptor-mediated transport of human amyloid β-protein 1-40 and 1-42 at the blood-brain barrier. Neurobiol Dis 1999, 6:190-199
    • (1999) Neurobiol Dis , vol.6 , pp. 190-199
    • Poduslo, J.F.1    Curran, G.L.2    Sanyal, B.3    Selkoe, D.J.4
  • 68
    • 0030752566 scopus 로고    scopus 로고
    • Neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Gearing M, Nash F: Neuropathologic assessment of Alzheimer's disease. Neurology 1997, 49:S14-S16
    • (1997) Neurology , vol.49
    • Mirra, S.S.1    Gearing, M.2    Nash, F.3
  • 73
    • 0035116442 scopus 로고    scopus 로고
    • Growth arrest of individual senile plaques in a model of Alzheimer's disease observed by in vivo multiphoton microscopy
    • Christie RH, Bacskai BJ, Zipfel WR, Williams RM, Kajdasz ST, Webb WW, Hyman BT: Growth arrest of individual senile plaques in a model of Alzheimer's disease observed by in vivo multiphoton microscopy. J Neurosci 2001, 21:858-864
    • (2001) J Neurosci , vol.21 , pp. 858-864
    • Christie, R.H.1    Bacskai, B.J.2    Zipfel, W.R.3    Williams, R.M.4    Kajdasz, S.T.5    Webb, W.W.6    Hyman, B.T.7
  • 76
    • 0030604067 scopus 로고    scopus 로고
    • Cerebrovascular transport of Alzheimer's amyloid β and apolipoproteins J and E: Possible anti-amyloidogenic role of the blood-brain barrier
    • Zlokovic BV: Cerebrovascular transport of Alzheimer's amyloid β and apolipoproteins J and E: possible anti-amyloidogenic role of the blood-brain barrier. Life Sci 1996, 59:1483-1497
    • (1996) Life Sci , vol.59 , pp. 1483-1497
    • Zlokovic, B.V.1
  • 77
    • 0035082722 scopus 로고    scopus 로고
    • Amyloid β40/42 clearance across the blood-brain barrier following intra-ventricular injections in wild-type, apoE knock-out and human apoE3 or E4 expressing transgenic mice
    • Ji Y, Permanne B, Sigurdsson EM, Holtzman DM, Wisniewski T: Amyloid β40/42 clearance across the blood-brain barrier following intra-ventricular injections in wild-type, apoE knock-out and human apoE3 or E4 expressing transgenic mice. J Alzheimer Dis 2001, 3:23-30
    • (2001) J Alzheimer Dis , vol.3 , pp. 23-30
    • Ji, Y.1    Permanne, B.2    Sigurdsson, E.M.3    Holtzman, D.M.4    Wisniewski, T.5
  • 78
    • 85030825322 scopus 로고    scopus 로고
    • Early and marked increase in a-β deposition in PDAPP mice in the absence of both apoe and clusterin: Evidence for a cooperative role in a-β clearance in vivo
    • Washington, DC, Society for Neuroscience, Program No. 666.14
    • DeMattos RB, O'Dell M, Taylor JW, Parsadanian M, Bales KR, Paul SM, Holtzman DM: Early and marked increase in a-β deposition in PDAPP mice in the absence of both apoe and clusterin: evidence for a cooperative role in a-β clearance in vivo. 2003 Abstract Viewer/ Itinerary Planner. Washington, DC, Society for Neuroscience, 2003, Program No. 666.14
    • (2003) 2003 Abstract Viewer/Itinerary Planner
    • DeMattos, R.B.1    O'Dell, M.2    Taylor, J.W.3    Parsadanian, M.4    Bales, K.R.5    Paul, S.M.6    Holtzman, D.M.7
  • 82
  • 83
    • 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, 98:9312-9317
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9312-9317
    • Doerfler, P.1    Shearman, M.S.2    Perlmutter, R.M.3
  • 86
    • 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, 3:688-694
    • (2002) EMBO Rep , vol.3 , pp. 688-694
    • Geling, A.1    Steiner, H.2    Willem, M.3    Bally-Cuif, L.4    Haass, C.5
  • 88
    • 0038476561 scopus 로고    scopus 로고
    • The γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-L-alanyl]- S-phenylglycine t-butyl ester reduces A beta levels in vivo in plasma and cerebrospinal fluid in young (plaque-free) and aged (plaque-bearing) Tg2576 mice
    • Lanz TA, Himes CS, Pallante G, Adams L, Yamazaki S, Amore B, Merchant KM: The γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S- phenylglycine t-butyl ester reduces A beta 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.S.2    Pallante, G.3    Adams, L.4    Yamazaki, S.5    Amore, B.6    Merchant, K.M.7


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