메뉴 건너뛰기




Volumn 11, Issue 8, 2010, Pages 1018-1031

Cholesterol, Alzheimer's Disease, Prion disorders: A ménage à trois?

Author keywords

Alzheimer's disease; Cholesterol esters; Lipid rafts; Modulators of cholesterol homeostasis; Plasma membrane; Prion disorders; Protein misfolding diseases

Indexed keywords

3 DECYLDIMETHYLSILYL N [2 (4 METHYLPHENYL) 1 PHENYLETHYL]PROPIONAMIDE; AMYLOID; AMYLOID BETA PROTEIN; AVASIMIBE; CHLORPROMAZINE; CHOLESTEROL; CHOLESTEROL ESTER; CP 113818; EVEROLIMUS; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; HYPOCHOLESTEROLEMIC AGENT; LIPID; LIPOPROTEIN; MEPACRINE; PIOGLITAZONE; PROGESTERONE; UNCLASSIFIED DRUG; VERAPAMIL;

EID: 77956898343     PISSN: 13894501     EISSN: None     Source Type: Journal    
DOI: 10.2174/138945010791591386     Document Type: Article
Times cited : (15)

References (128)
  • 1
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nature Rev Neurosci 2003; 4: 49-60.
    • (2003) Nature Rev Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 3
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk WE; Pettegrew JW, Abraham D.J. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem 1989; 37: 1273-1281.
    • (1989) J Histochem Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 4
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • Naiki H, Higuchi K, Hosokawa M, Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 1989; 177: 244-249.
    • (1989) Anal Biochem , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 5
    • 0032883766 scopus 로고    scopus 로고
    • Impairment of membrane transport and signal transduction systems by amyloidogenic proteins
    • Mattson MP. Impairment of membrane transport and signal transduction systems by amyloidogenic proteins. Methods Enzymol 1999; 309: 733-768.
    • (1999) Methods Enzymol , vol.309 , pp. 733-768
    • Mattson, M.P.1
  • 6
    • 34548726211 scopus 로고    scopus 로고
    • Generic cell dysfunction in neurodegenerative disorders: Role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity
    • Stefani M. Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity. Neuroscientist 2007; 13: 519-531.
    • (2007) Neuroscientist , vol.13 , pp. 519-531
    • Stefani, M.1
  • 7
    • 0026524681 scopus 로고
    • Evidence for changes in the Alzheimer's disease brain cortical membrane structure mediated by cholesterol
    • Mason RP, Shoemaker WJ, Shajenko L, Chambers TE, Herbette LG. Evidence for changes in the Alzheimer's disease brain cortical membrane structure mediated by cholesterol. Aging 1992; 13: 413-419.
    • (1992) Aging , vol.13 , pp. 413-419
    • Mason, R.P.1    Shoemaker, W.J.2    Shajenko, L.3    Chambers, T.E.4    Herbette, L.G.5
  • 8
    • 14844321855 scopus 로고    scopus 로고
    • Cholesterol homeostasis failure as a unifying cause of synaptic degeneration
    • Koudinov AL, Koudinova NV. Cholesterol homeostasis failure as a unifying cause of synaptic degeneration. J Neurol Sci 2005; 229: 233-240.
    • (2005) J Neurol Sci , vol.229 , pp. 233-240
    • Koudinov, A.L.1    Koudinova, N.V.2
  • 10
    • 58149220667 scopus 로고    scopus 로고
    • Cholesterol in Alzheimer's Disease: Unresolved Questions
    • Stefani M, Liguri G. Cholesterol in Alzheimer's Disease: Unresolved Questions. Curr Alzh Res 2009; 6: 15-29.
    • (2009) Curr Alzh Res , vol.6 , pp. 15-29
    • Stefani, M.1    Liguri, G.2
  • 11
    • 0036793543 scopus 로고    scopus 로고
    • Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AßP (1-40) and (1-42) peptides
    • Arispe N, Doh M. Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AßP (1-40) and (1-42) peptides. FASEB J 2002; 16: 1526-1536.
    • (2002) FASEB J , vol.16 , pp. 1526-1536
    • Arispe, N.1    Doh, M.2
  • 12
    • 0036752519 scopus 로고    scopus 로고
    • Protein misfolding in Alzheimer's and Parkinson's disease: Genetics and molecular mechanisms
    • Forloni G, Terreni L, Bertani I, et al. Protein misfolding in Alzheimer's and Parkinson's disease: genetics and molecular mechanisms. Neurobiol Aging 2002; 23: 957-976.
    • (2002) Neurobiol Aging , vol.23 , pp. 957-976
    • Forloni, G.1    Terreni, L.2    Bertani, I.3
  • 13
    • 33846419488 scopus 로고    scopus 로고
    • Lipid raft microdomains and neurotransmitter signalling
    • Allen JA, Halverson-Tamboli RA, Rasenick MM. Lipid raft microdomains and neurotransmitter signalling. Nat Rev 2007; 8: 128-140.
    • (2007) Nat Rev , vol.8 , pp. 128-140
    • Allen, J.A.1    Halverson-Tamboli, R.A.2    Rasenick, M.M.3
  • 14
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
    • Kojro E, Gimpl G, Lammich S, März W, Fahrenholz F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10. 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    März, W.4    Fahrenholz, F.5
  • 15
    • 10344263931 scopus 로고    scopus 로고
    • Neuronal membrane cholesterol loss enhances amyloid peptide generation
    • Abad-Rodriguez J, Ledesma MD, Craessaerts K, et al. Neuronal membrane cholesterol loss enhances amyloid peptide generation. J Cell Biol (2004; 167: 953-960.
    • (2004) J Cell Biol , vol.167 , pp. 953-960
    • Abad-Rodriguez, J.1    Ledesma, M.D.2    Craessaerts, K.3
  • 16
    • 31444454174 scopus 로고    scopus 로고
    • The role of seladin- 1/DHCR24 in cholesterol biosynthesis, APP processing and Aβ generation in vivo
    • Crameri A, Biondi E, Kuehnle K, et al. The role of seladin- 1/DHCR24 in cholesterol biosynthesis, APP processing and Aβ generation in vivo. EMBO J 2006; 25: 432-443.
    • (2006) EMBO J , vol.25 , pp. 432-443
    • Crameri, A.1    Biondi, E.2    Kuehnle, K.3
  • 17
    • 64949147821 scopus 로고    scopus 로고
    • Central nervous system: Cholesterol turnover, brain development and neurodegeneration
    • Dietschy JM. Central nervous system: cholesterol turnover, brain development and neurodegeneration. Biol Chem 2009; 390: 287-293.
    • (2009) Biol Chem , vol.390 , pp. 287-293
    • Dietschy, J.M.1
  • 18
    • 1442308949 scopus 로고    scopus 로고
    • Adipocyte cholesterol balance in obesity
    • Le Lay S, Ferre P, Dugail I. Adipocyte cholesterol balance in obesity. Biochem Soc Trans 2004; 32: 103-106.
    • (2004) Biochem Soc Trans , vol.32 , pp. 103-106
    • Le, L.S.1    Ferre, P.2    Dugail, I.3
  • 19
    • 0036667737 scopus 로고    scopus 로고
    • Insights into lipid raft structure and formation from experiments in model membranes
    • London E. Insights into lipid raft structure and formation from experiments in model membranes. Curr Opin Struc Biol 2002; 12: 480-486.
    • (2002) Curr Opin Struc Biol , vol.12 , pp. 480-486
    • London, E.1
  • 22
    • 0025065068 scopus 로고
    • Regulation of phospholipid biosynthesis during cholesterol influx and high density lipoprotein-mediated cholesterol efflux in macrophages
    • Schmitz G, Beuck M, Fischer H, Nowicka G, Robenek H. Regulation of phospholipid biosynthesis during cholesterol influx and high density lipoprotein-mediated cholesterol efflux in macrophages. J Lipid Res 1990; 31: 1741-1752.
    • (1990) J Lipid Res , vol.31 , pp. 1741-1752
    • Schmitz, G.1    Beuck, M.2    Fischer, H.3    Nowicka, G.4    Robenek, H.5
  • 23
    • 0032817267 scopus 로고    scopus 로고
    • Sphingomyelin and related lipids: Structure, occurrence, biosynthesis and analysis
    • Ridgway ND, Byers DM, Cook HW, Storey MK. Sphingomyelin and related lipids: structure, occurrence, biosynthesis and analysis. Prog Lipid Res 1999; 38: 337-360.
    • (1999) Prog Lipid Res , vol.38 , pp. 337-360
    • Ridgway, N.D.1    Byers, D.M.2    Cook, H.W.3    Storey, M.K.4
  • 24
    • 2542488501 scopus 로고    scopus 로고
    • Lipid rafts-protein association and the regulation of protein activity
    • Lucero HA, Robbins PW. Lipid rafts-protein association and the regulation of protein activity. Arch Biochem Biophys 2004; 426: 208-224.
    • (2004) Arch Biochem Biophys , vol.426 , pp. 208-224
    • Lucero, H.A.1    Robbins, P.W.2
  • 25
    • 0042160147 scopus 로고    scopus 로고
    • Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: Some APP in large complexes
    • Rouvinski A, Gahali-Sassa I, Stavb I, et al. Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: some APP in large complexes. Biochem Biophys Res Com 2003; 308: 750-758.
    • (2003) Biochem Biophys Res Com , vol.308 , pp. 750-758
    • Rouvinski, A.1    Gahali-Sassa, I.2    Stavb, I.3
  • 26
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons K, Ehehalt R. Cholesterol, lipid rafts, and disease. J Clin Invest 2002; 110: 597-603.
    • (2002) J Clin Invest , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 27
    • 31844442585 scopus 로고    scopus 로고
    • Pani and Dessì Eds., New York, NY, USA: Kluwer Academic/Plenum Publisher
    • Dessi S, Batetta B. In: Cell Growth and Cholesterol Esters; Pani and Dessì Eds. New York, NY, USA: Kluwer Academic/Plenum Publisher 2004; pp 1-10.
    • (2004) Cell Growth and Cholesterol Esters , pp. 1-10
    • Dessi, S.1    Batetta, B.2
  • 28
    • 33748428356 scopus 로고    scopus 로고
    • Pani and Dessì Eds. New York, NY, USA: Kluwer Academic/Plenum Publisher
    • Dessi S, Batetta B. In: Cell Growth and Cholesterol Esters; Pani and Dessì Eds. New York, NY, USA: Kluwer Academic/Plenum Publisher 2004; pp 25-33.
    • (2004) Cell Growth and Cholesterol Esters , pp. 25-33
    • Dessi, S.1    Batetta, B.2
  • 29
    • 0015890890 scopus 로고
    • Familial hypercholesteroleia: Identification of a defect in the regulation of 3-hydroxy-3- methylglutaryl coenzyme A reductase activity associated with overproduction of cholesterol
    • Goldstein JL, Brown MS. Familial hypercholesteroleia: Identification of a defect in the regulation of 3-hydroxy-3- methylglutaryl coenzyme A reductase activity associated with overproduction of cholesterol. Proc Natl Acad Sci USA 1973; 70: 2804-2808.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 2804-2808
    • Goldstein, J.L.1    Brown, M.S.2
  • 30
    • 0013321009 scopus 로고
    • Familial hypercholesterolemia: Defective binding of lipoproteins to cultured fibroblasts associated with impaired regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity
    • Brown MS, Goldstein JL. Familial hypercholesterolemia: defective binding of lipoproteins to cultured fibroblasts associated with impaired regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity. Proc Natl Acad Sci USA 1974; 71: 788-792.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 788-792
    • Brown, M.S.1    Goldstein, J.L.2
  • 31
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS, Goldstein JL. A receptor-mediated pathway for cholesterol homeostasis. Science 1986; 232: 34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 32
    • 0034604350 scopus 로고    scopus 로고
    • Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes
    • Nohturfft A, Yabe D, Goldstein JL, Brown MS, Espenshade PJ. Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes. Cell 2000; 102: 315-323.
    • (2000) Cell , vol.102 , pp. 315-323
    • Nohturfft, A.1    Yabe, D.2    Goldstein, J.L.3    Brown, M.S.4    Espenshade, P.J.5
  • 33
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • Yang T, Espenshade PJ, Wright ME, et al. Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 2002; 110: 489-500.
    • (2002) Cell , vol.110 , pp. 489-500
    • Yang, T.1    Espenshade, P.J.2    Wright, M.E.3
  • 34
    • 33745307534 scopus 로고    scopus 로고
    • The life cycle of neutral lipids: Synthesis, storage and degradation
    • Athenstaedt K, Daum G. The life cycle of neutral lipids: synthesis, storage and degradation. Cell Mol Life Sci 2006; 63: 1355-1369.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1355-1369
    • Athenstaedt, K.1    Daum, G.2
  • 35
    • 76049095353 scopus 로고    scopus 로고
    • Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N- terminal sequence
    • Igarashi M, Osuga J, Isshiki M, et al. Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N- terminal sequence. J Lipid Res 2010; 51: 274-285.
    • (2010) J Lipid Res , vol.51 , pp. 274-285
    • Igarashi, M.1    Osuga, J.2    Isshiki, M.3
  • 36
    • 0036424016 scopus 로고    scopus 로고
    • Cholesterol trafficking in the secretory and endocytic systems
    • Prinz W. Cholesterol trafficking in the secretory and endocytic systems. Sem Cell Dev Biol 2002; 13: 197-203.
    • (2002) Sem Cell Dev Biol , vol.13 , pp. 197-203
    • Prinz, W.1
  • 37
    • 28444479505 scopus 로고    scopus 로고
    • Role of cholesterol and lipid organization in disease
    • Maxfield FR, Tabas I. Role of cholesterol and lipid organization in disease. Nature 2005; 438: 36-45.
    • (2005) Nature , vol.438 , pp. 36-45
    • Maxfield, F.R.1    Tabas, I.2
  • 38
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin S, Parton RG. Lipid droplets: a unified view of a dynamic organelle. Nature Rev Mol Cell Biol 2006; 7: 373-378.
    • (2006) Nature Rev Mol Cell Biol , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 39
    • 61549115335 scopus 로고    scopus 로고
    • A role for lipid droplets in inter-membrane lipid traffic
    • Zehmer JK, Huang Y, Peng G, et al. A role for lipid droplets in inter-membrane lipid traffic. Proteomics 2009; 9: 914-921.
    • (2009) Proteomics , vol.9 , pp. 914-921
    • Zehmer, J.K.1    Huang, Y.2    Peng, G.3
  • 40
    • 0035289932 scopus 로고    scopus 로고
    • Macrophage foam cells and atherosclerosis
    • Kruth HS. Macrophage foam cells and atherosclerosis. Front Biosci 2001; 6: 429-455.
    • (2001) Front Biosci , vol.6 , pp. 429-455
    • Kruth, H.S.1
  • 41
    • 53149099668 scopus 로고    scopus 로고
    • Regulated association of caveolins to lipid droplets during differentiation of 3T3-L1 adipocytes
    • Blouin CM, Le LS, Lasnier F, Dugail I, Hajduch E. Regulated association of caveolins to lipid droplets during differentiation of 3T3-L1 adipocytes. Biochem Biophys Res Commun 2008; 376: 331-335.
    • (2008) Biochem Biophys Res Commun , vol.376 , pp. 331-335
    • Blouin, C.M.1    Le, L.S.2    Lasnier, F.3    Dugail, I.4    Hajduch, E.5
  • 42
    • 0035809931 scopus 로고    scopus 로고
    • Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell
    • Fujimoto T, Kogo H, Ishiguro K, Tauchi K, Nomura R. Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell. J Cell Biol 2001; 152: 1079-1085.
    • (2001) J Cell Biol , vol.152 , pp. 1079-1085
    • Fujimoto, T.1    Kogo, H.2    Ishiguro, K.3    Tauchi, K.4    Nomura, R.5
  • 43
    • 33846678695 scopus 로고    scopus 로고
    • The ABCA subfamily-gene and protein structures, functions and associated hereditary diseases
    • Albrecht C, Viturro EP. The ABCA subfamily-gene and protein structures, functions and associated hereditary diseases. Pflugers Arch 2007; 453: 581-589.
    • (2007) Pflugers Arch , vol.453 , pp. 581-589
    • Albrecht, C.1    Viturro, E.P.2
  • 46
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin, Notch, and the genesis and treatment of Alzheimer's disease
    • Selkoe DJ. Presenilin, Notch, and the genesis and treatment of Alzheimer's disease. Proc Natl Acad Sci USA 2001; 98: 11039-11041.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 47
    • 0034049944 scopus 로고    scopus 로고
    • Proteolytic processing and cell biological functions of the amyloid precursor protein
    • De Strooper B, Annaert W. Proteolytic processing and cell biological functions of the amyloid precursor protein. J Cell Sci 2000; 113: 1857-1870.
    • (2000) J Cell Sci , vol.113 , pp. 1857-1870
    • de Strooper, B.1    Annaert, W.2
  • 48
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases-new features and familiar faces
    • Esler WP, Wolfe MS. A portrait of Alzheimer secretases-new features and familiar faces. Science 2001; 293: 1449-1454.
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 49
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by α-, β- and γ- secretases
    • Nunan J, Small DH. Regulation of APP cleavage by α-, β- and γ- secretases. FEBS Lett 2000; 483: 6-10.
    • (2000) FEBS Lett , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 51
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 2003; 160: 113-123.
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 52
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion diseases
    • Harris DA. Cellular biology of prion diseases. Clin Microbiol Rev 1999; 12: 429-444.
    • (1999) Clin Microbiol Rev , vol.12 , pp. 429-444
    • Harris, D.A.1
  • 53
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey B, Raymond GJ. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J Biol Chem 1991; 266: 18217-18223.
    • (1991) J Biol Chem , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 54
    • 13244295520 scopus 로고    scopus 로고
    • The highways and byways of prion protein trafficking
    • Campana V, Sarnataro D, Zurzolo C. The highways and byways of prion protein trafficking. Trends Cell Biol 2005; 15: 102-111.
    • (2005) Trends Cell Biol , vol.15 , pp. 102-111
    • Campana, V.1    Sarnataro, D.2    Zurzolo, C.3
  • 58
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • Chiesa R, Harris DA. Prion diseases: what is the neurotoxic molecule? Neurobiol Dis 2001; 8: 743-763.
    • (2001) Neurobiol Dis , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 59
    • 0027405573 scopus 로고
    • Processing of a cellular prion protein: Identification of N- and C-terminal cleavage sites
    • Harris DA, Huber MT, van Dijken P, et al. Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry 1993; 32: 1009-1016.
    • (1993) Biochemistry , vol.32 , pp. 1009-1016
    • Harris, D.A.1    Huber, M.T.2    van Dijken, P.3
  • 60
    • 0031765769 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues
    • Jimenez-Huete A, Lievens PMJ, Vidal R, et al. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues. Am J Pathol 1998; 153: 1561-1572.
    • (1998) Am J Pathol , vol.153 , pp. 1561-1572
    • Jimenez-Huete, A.1    Lievens, P.M.J.2    Vidal, R.3
  • 61
    • 42149140619 scopus 로고    scopus 로고
    • Regulation of beta APP and PrPc cleavage by alpha-secretase: Mechanistic and therapeutic perspectives
    • Vincent B, Cisse MA, Sunyach C, Guillot-Sestier MV, Checler F. Regulation of beta APP and PrPc cleavage by alpha-secretase: mechanistic and therapeutic perspectives. Curr Alzheimer Res 2008; 5: 202-211.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 202-211
    • Vincent, B.1    Cisse, M.A.2    Sunyach, C.3    Guillot-Sestier, M.V.4    Checler, F.5
  • 62
    • 18044377435 scopus 로고    scopus 로고
    • Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein
    • Hooper NM. Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein. Biochem Soc Trans 2005; 33: 335-338.
    • (2005) Biochem Soc Trans , vol.33 , pp. 335-338
    • Hooper, N.M.1
  • 63
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • Kamal A, Stokin GB, Yang Z, Xia CH, Goldstein LS. Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron 2000; 28: 449-459.
    • (2000) Neuron , vol.28 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.3    Xia, C.H.4    Goldstein, L.S.5
  • 64
    • 9144274938 scopus 로고    scopus 로고
    • Amyloid-beta degradation: The forgotten half of Alzheimer's disease
    • Whitaker C, Eckman C, Almeida C, et al. Amyloid-beta degradation: the forgotten half of Alzheimer's disease. J Alzheimer Dis 2003; 5: 491-497.
    • (2003) J Alzheimer Dis , vol.5 , pp. 491-497
    • Whitaker, C.1    Eckman, C.2    Almeida, C.3
  • 65
    • 34547400403 scopus 로고    scopus 로고
    • Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein
    • Parkin ET, Watt NT, Hussain I, et al. Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein. Proc Natl Acad Sci USA 2007; 104: 11062-11067.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11062-11067
    • Parkin, E.T.1    Watt, N.T.2    Hussain, I.3
  • 66
    • 34347215068 scopus 로고    scopus 로고
    • Prion protein and prion diseases: The good and the bad
    • Malcolm J, Gains A, LeBlanc AC. Prion protein and prion diseases: the good and the bad. Can J Neurol Sci 2007; 34: 126-145.
    • (2007) Can J Neurol Sci , vol.34 , pp. 126-145
    • Malcolm, J.1    Gains, A.2    Leblanc, A.C.3
  • 68
    • 15544374091 scopus 로고    scopus 로고
    • The conflicting role of brain cholesterol in Alzheimer's disease: Lessons from the brain plasminogen system
    • Ledesma MD, Dotti CG. The conflicting role of brain cholesterol in Alzheimer's disease: lessons from the brain plasminogen system. Biochem Soc Symp 2005; 72: 129-138.
    • (2005) Biochem Soc Symp , vol.72 , pp. 129-138
    • Ledesma, M.D.1    Dotti, C.G.2
  • 69
    • 34547315810 scopus 로고    scopus 로고
    • Alzheimer's Disease: Cholesterol, membrane rafts, isoprenoids and statins
    • Reid PC, Urano Y, Kodama T, Hamakubo T. Alzheimer's Disease: cholesterol, membrane rafts, isoprenoids and statins. J Cell Mol Med 2007; 11: 383-392.
    • (2007) J Cell Mol Med , vol.11 , pp. 383-392
    • Reid, P.C.1    Urano, Y.2    Kodama, T.3    Hamakubo, T.4
  • 70
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos, A, Scott M, Semenov A, et al. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J Cell Biol 1995; 129: 121-32.
    • (1995) J Cell Biol , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3
  • 71
    • 2442483932 scopus 로고    scopus 로고
    • Squalestatin cures prion-infected neurons and protects against prion neurotoxicity
    • Bate C, Salmona M, Diomede L, Williams A. Squalestatin cures prion-infected neurons and protects against prion neurotoxicity. J Biol Chem 2004; 279: 14983-14990.
    • (2004) J Biol Chem , vol.279 , pp. 14983-14990
    • Bate, C.1    Salmona, M.2    Diomede, L.3    Williams, A.4
  • 72
    • 33746890495 scopus 로고    scopus 로고
    • Simvastatin prolongs survival times in prion infections of the central nervous system
    • Mok SW, Thelen KM, Riemer C, et al. Simvastatin prolongs survival times in prion infections of the central nervous system. Biochem Biophys Res Commun 2006; 348: 697-702.
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 697-702
    • Mok, S.W.1    Thelen, K.M.2    Riemer, C.3
  • 73
    • 34247589262 scopus 로고    scopus 로고
    • Simvastatin treatment prolongs the survival of scrapie-infected mice
    • Kempster S, Bate C, Williams A. Simvastatin treatment prolongs the survival of scrapie-infected mice. Neuroreport 2006; 18: 479-482.
    • (2006) Neuroreport , vol.18 , pp. 479-482
    • Kempster, S.1    Bate, C.2    Williams, A.3
  • 74
    • 33846821715 scopus 로고    scopus 로고
    • Cholesterol synthesis inhibitors protect against platelet-activating factor-induced neuronal damage
    • Doi:10.1186/1742-2094-4-5
    • Bate C, Rumbold L, Williams A. Cholesterol synthesis inhibitors protect against platelet-activating factor-induced neuronal damage. J Neuroinflam 2007, 4:5. Doi:10.1186/1742-2094-4-5.
    • (2007) J Neuroinflam , vol.4 , pp. 5
    • Bate, C.1    Rumbold, L.2    Williams, A.3
  • 75
    • 45149109366 scopus 로고    scopus 로고
    • Induced neuroprotection independently from PrPSc accumulation in a mouse model for prion disease treated with simvastatin
    • Haviv Y, Avrahami D, Ovadia H, et al. Induced neuroprotection independently from PrPSc accumulation in a mouse model for prion disease treated with simvastatin. Arch Neurol 2008; 65: 762-773.
    • (2008) Arch Neurol , vol.65 , pp. 762-773
    • Haviv, Y.1    Avrahami, D.2    Ovadia, H.3
  • 76
    • 63149151206 scopus 로고    scopus 로고
    • A systems approach to prion disease
    • Doi:10.1038/msb
    • Hwang D, Lee IY, Yoo H, et al. A systems approach to prion disease. Mol Syst Biol 2009; 5:252. Doi:10.1038/msb.2009.10.
    • (2009) Mol Syst Biol , vol.5 , pp. 252
    • Hwang, D.1    Lee, I.Y.2    Yoo, H.3
  • 77
    • 42149186322 scopus 로고    scopus 로고
    • Comprehensive transcriptional profiling of prion infection in mouse models reveals networks of responsive genes
    • Doi:10.1186/1471-2164-9-114
    • Sorensen G, Medina S, Parchaliuk D, et al. Comprehensive transcriptional profiling of prion infection in mouse models reveals networks of responsive genes. BMC Genom 2008; 9:114. Doi:10.1186/1471-2164-9-114.
    • (2008) BMC Genom , vol.9 , pp. 114
    • Sorensen, G.1    Medina, S.2    Parchaliuk, D.3    Et al.4
  • 78
    • 71449102371 scopus 로고    scopus 로고
    • Prion-induced activation of cholesterogenic gene expression by SREBP2 in neuronal cells
    • Bach, C.; Gilch S.; Rost R, et al. Prion-induced activation of cholesterogenic gene expression by SREBP2 in neuronal cells. J Biol Chem 2009; 284: 31260-31269.
    • (2009) J Biol Chem , vol.284 , pp. 31260-31269
    • Bach, C.1    Gilch, S.2    Rost, R.3
  • 81
    • 22844431778 scopus 로고    scopus 로고
    • Statin use and the risk of incident dementia: The cardiovascular health study
    • Rea TD, Breitner JC, Psaty BM. Statin use and the risk of incident dementia: the cardiovascular health study. Arch Neurol 2005; 62: 1047-1051.
    • (2005) Arch Neurol , vol.62 , pp. 1047-1051
    • Rea, T.D.1    Breitner, J.C.2    Psaty, B.M.3
  • 82
    • 34249825804 scopus 로고    scopus 로고
    • Effect of HMG-CoA Reductase Inhibitors on [beta]-Amyloid Peptide Levels: Implications For Alzheimer's Disease
    • Höglund K, Blennow K. Effect of HMG-CoA Reductase Inhibitors on [beta]-Amyloid Peptide Levels: Implications for Alzheimer's Disease. CNS Drugs 2007; 21: 449-462.
    • (2007) CNS Drugs , vol.21 , pp. 449-462
    • Höglund, K.1    Blennow, K.2
  • 83
    • 34548291482 scopus 로고    scopus 로고
    • Statin therapy is associated with reduced neuropathologic changes of Alzheimer disease
    • Li G, Larson EB, Sonnen JA, et al. Statin therapy is associated with reduced neuropathologic changes of Alzheimer disease. Neurology 2007; 69: 878-885.
    • (2007) Neurology , vol.69 , pp. 878-885
    • Li, G.1    Larson, E.B.2    Sonnen, J.A.3
  • 84
    • 43249094747 scopus 로고    scopus 로고
    • Statins, incident Alzheimer disease, change in cognitive function, and neuro- pathology
    • Arvanitakis Z, Schneider JA, Wilson RS, et al. Statins, incident Alzheimer disease, change in cognitive function, and neuro- pathology. Neurology 2008; 70: 1795-1802.
    • (2008) Neurology , vol.70 , pp. 1795-1802
    • Arvanitakis, Z.1    Schneider, J.A.2    Wilson, R.S.3
  • 87
    • 33845892752 scopus 로고    scopus 로고
    • Systematic meta-analyses of Alzheimer disease genetic association studies: The AlzGene database
    • Bertram L, McQueen MB, Mullin K, Blacker D, Tanzi RE. Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database. Nat Genet 2007; 39: 17-23.
    • (2007) Nat Genet , vol.39 , pp. 17-23
    • Bertram, L.1    McQueen, M.B.2    Mullin, K.3    Blacker, D.4    Tanzi, R.E.5
  • 88
    • 10744223627 scopus 로고    scopus 로고
    • Genetic association of acyl-coenzyme A: Cholesterol acyltransferase with cerebrospinal fluid cholesterol levels, brain amyloid load, and risk for Alzheimer's disease
    • Wollmer MA, Streffer JR, Tsolaki M, et al. Genetic association of acyl-coenzyme A: cholesterol acyltransferase with cerebrospinal fluid cholesterol levels, brain amyloid load, and risk for Alzheimer's disease. Mol Psychiatry 2003; 8: 635-638.
    • (2003) Mol Psychiatry , vol.8 , pp. 635-638
    • Wollmer, M.A.1    Streffer, J.R.2    Tsolaki, M.3
  • 89
    • 5144227934 scopus 로고    scopus 로고
    • The ACAT inhibitor CP-113,818 markedly reduces amyloid pathology in a mouse model of Alzheimer's disease
    • Hutter-Paier B, Huttunen HJ, Puglielli L, et al. The ACAT inhibitor CP-113,818 markedly reduces amyloid pathology in a mouse model of Alzheimer's disease. Neuron 2004; 44: 227-238.
    • (2004) Neuron , vol.44 , pp. 227-238
    • Hutter-Paier, B.1    Huttunen, H.J.2    Puglielli, L.3
  • 90
    • 34047268145 scopus 로고    scopus 로고
    • Knockdown of ACAT-1 reduces amyloidogenic processing of APP
    • Huttunen HJ, Greco C, Kovacs DM. Knockdown of ACAT-1 reduces amyloidogenic processing of APP. FEBS Lett 2007; 581: 1688-1692.
    • (2007) FEBS Lett , vol.581 , pp. 1688-1692
    • Huttunen, H.J.1    Greco, C.2    Kovacs, D.M.3
  • 91
    • 40449110086 scopus 로고    scopus 로고
    • ACAT as a drug target for Alzheimer's disease
    • Huttunen HJ, Kovacs DM. ACAT as a drug target for Alzheimer's disease. Neurodegener Dis 2008; 5: 212-214.
    • (2008) Neurodegener Dis , vol.5 , pp. 212-214
    • Huttunen, H.J.1    Kovacs, D.M.2
  • 93
    • 38849086036 scopus 로고    scopus 로고
    • Overexpression of ABCA1 reduces amyloid deposition in the PDAPP mouse model of Alzheimer disease
    • Wahrle SE, Jiang H, Parsadanian M, et al. Overexpression of ABCA1 reduces amyloid deposition in the PDAPP mouse model of Alzheimer disease. J Clin Invest 2008; 118: 671-682.
    • (2008) J Clin Invest , vol.118 , pp. 671-682
    • Wahrle, S.E.1    Jiang, H.2    Parsadanian, M.3
  • 94
    • 74949103451 scopus 로고    scopus 로고
    • Altered cholesterol ester cycle in skin fibroblasts from patients with Alzheimer's disease
    • Pani A, Dessì S, Diaz G, et al. Altered cholesterol ester cycle in skin fibroblasts from patients with Alzheimer's disease. J Alzheimer Dis 2009; 18: 829-841.
    • (2009) J Alzheimer Dis , vol.18 , pp. 829-841
    • Pani, A.1    Dessì, S.2    Diaz, G.3
  • 95
    • 70749123387 scopus 로고    scopus 로고
    • Accumulation of neutral lipids in peripheral blood mononuclear cells as a distintive trait of Alzheimer patients and asymptomatic subjects at risk of disease
    • Doi:10.1186/1741-7015-7-66
    • [95] Pani A, Mandas A, Diaz G, et al. Accumulation of neutral lipids in peripheral blood mononuclear cells as a distintive trait of Alzheimer patients and asymptomatic subjects at risk of disease. BMC Med 2009; 7: 66. Doi:10.1186/1741-7015-7-66.
    • (2009) BMC Med , vol.7 , pp. 66
    • Pani, A.1    Mandas, A.2    Diaz, G.3
  • 96
    • 35848930063 scopus 로고    scopus 로고
    • Accumulation of cholesterol esters in ex vivo lymphocytes from scrapie-susceptible sheep and in scrapie-infected mouse neuroblastoma cell lines
    • Pani A, Norfo C, Abete C, et al. Accumulation of cholesterol esters in ex vivo lymphocytes from scrapie-susceptible sheep and in scrapie-infected mouse neuroblastoma cell lines. Am J Infect Dis 2007; 3: 165-168.
    • (2007) Am J Infect Dis , vol.3 , pp. 165-168
    • Pani, A.1    Norfo, C.2    Abete, C.3
  • 97
    • 70049118212 scopus 로고    scopus 로고
    • Cholesterol metabolism in brain and skin fibroblasts from sarda breed sheep with scrapie-resistant and scrapie-susceptible genotypes
    • Pani A, Abete C, Norfo C, et al. Cholesterol metabolism in brain and skin fibroblasts from sarda breed sheep with scrapie-resistant and scrapie-susceptible genotypes. Am J Infect Dis 2007; 3:143-150.
    • (2007) Am J Infect Dis , vol.3 , pp. 143-150
    • Pani, A.1    Abete, C.2    Norfo, C.3
  • 98
    • 75849161806 scopus 로고    scopus 로고
    • ACAT, Cav1 and PrP expression in scrapie susceptible and resistant sheep
    • Orrù CD, Abete C, Cannas MD, et al. ACAT, Cav1 and PrP expression in scrapie susceptible and resistant sheep. Cent Eur J Biol 2010; 5: 31-37.
    • (2010) Cent Eur J Biol , vol.5 , pp. 31-37
    • Orrù, C.D.1    Abete, C.2    Cannas, M.D.3
  • 99
    • 41549105318 scopus 로고    scopus 로고
    • Sequestration of free cholesterol in cell membranes by prions correlates with cytoplasmic phospho- lipase A2 activation
    • Doi:10.1186/1741-7007-6-8
    • Bate B, Tayebi M, Williams A. Sequestration of free cholesterol in cell membranes by prions correlates with cytoplasmic phospho- lipase A2 activation. BMC Biol 2008; 6: 8. Doi:10.1186/1741-7007-6-8.
    • (2008) BMC Biol , vol.6 , pp. 8
    • Bate, B.1    Tayebi, M.2    Williams, A.3
  • 100
    • 35848936977 scopus 로고    scopus 로고
    • Anti-prion activity of cholesterol esterification modulators: A comparative study in ex vivo sheep fibroblasts and lymphocytes and in mouse neuroblastoma cell lines
    • Pani A, Norfo C, Abete C, et al. Anti-prion activity of cholesterol esterification modulators: a comparative study in ex vivo sheep fibroblasts and lymphocytes and in mouse neuroblastoma cell lines. Antimicrob Agents Chemother 2007; 51: 4141-4147.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 4141-4147
    • Pani, A.1    Norfo, C.2    Abete, C.3
  • 101
    • 77952096872 scopus 로고    scopus 로고
    • In vitro synergistic anti- prion effect of cholesterol ester modulators in combination with chlorpromazine and quinacrine
    • Orrù CD, Cannas MD, Vascellari S, et al. In vitro synergistic anti- prion effect of cholesterol ester modulators in combination with chlorpromazine and quinacrine. Cent Eur J Biol 2010; 5: 151-165.
    • (2010) Cent Eur J Biol , vol.5 , pp. 151-165
    • Orrù, C.D.1    Cannas, M.D.2    Vascellari, S.3
  • 102
    • 36749073968 scopus 로고    scopus 로고
    • Cell division modulates prion accumulation in cultured cells
    • Ghaemmaghami S, Phuan PW, Perkins B, et al. Cell division modulates prion accumulation in cultured cells. Proc Natl Acad Sci USA 2007; 104: 17971-17976.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 17971-17976
    • Ghaemmaghami, S.1    Phuan, P.W.2    Perkins, B.3
  • 104
    • 0030943621 scopus 로고    scopus 로고
    • Acyl-coenzyme A:Cholesterol acyltransferase
    • Chang TY, Chang CC, Cheng D. Acyl-coenzyme A:cholesterol acyltransferase. Annu Rev Biochem 1997; 66: 613-638.
    • (1997) Annu Rev Biochem , vol.66 , pp. 613-638
    • Chang, T.Y.1    Chang, C.C.2    Cheng, D.3
  • 105
    • 0034672691 scopus 로고    scopus 로고
    • Mammalian acyl- CoA:Cholesterol acyltransferases
    • Buhman KF, Accad M, Farese RV. Mammalian acyl- CoA:cholesterol acyltransferases. Biochim Biophys Acta 2000; 1529: 142-154.
    • (2000) Biochim Biophys Acta , vol.1529 , pp. 142-154
    • Buhman, K.F.1    Accad, M.2    Farese, R.V.3
  • 106
    • 0034987223 scopus 로고    scopus 로고
    • Roles of acylcoenzyme A:Cholesterol acyltransferase-1 and -2
    • Chang TY, Chang CC, Lin S, et al. Roles of acylcoenzyme A:cholesterol acyltransferase-1 and -2. Curr Opin Lipidol 2001; 12: 289-296.
    • (2001) Curr Opin Lipidol , vol.12 , pp. 289-296
    • Chang, T.Y.1    Chang, C.C.2    Lin, S.3
  • 107
    • 41849091490 scopus 로고    scopus 로고
    • Intraventricular pentosan polysulphate in human prion diseases: An observational study in the UK
    • Bone I, Belton L, Walker AS, Darbyshire J. Intraventricular pentosan polysulphate in human prion diseases: an observational study in the UK. Eur J Neurol 2008; 15: 458-464.
    • (2008) Eur J Neurol , vol.15 , pp. 458-464
    • Bone, I.1    Belton, L.2    Walker, A.S.3    Darbyshire, J.4
  • 108
    • 0035908839 scopus 로고    scopus 로고
    • Old drugs to treat new variant Creutzfeldt-Jakob disease
    • Love R. Old drugs to treat new variant Creutzfeldt-Jakob disease. Lancet 2001; 358: 563-574.
    • (2001) Lancet , vol.358 , pp. 563-574
    • Love, R.1
  • 109
    • 42049122359 scopus 로고    scopus 로고
    • Systematic review of therapeutic interventions in human prion disease
    • Stewart LA, Rydzewska LHM, Keogh GF, Knight RSG. Systematic review of therapeutic interventions in human prion disease. Neurology 2008; 70: 1272-1281.
    • (2008) Neurology , vol.70 , pp. 1272-1281
    • Stewart, L.A.1    Rydzewska, L.H.M.2    Keogh, G.F.3    Knight, R.S.G.4
  • 110
    • 77954558825 scopus 로고    scopus 로고
    • Alzheimer's disease therapeutic research: The path forward
    • Doi:10.1186/alzrt2
    • Aisen PS. Alzheimer's disease therapeutic research: the path forward. Alzh Res Ther 2009; 1:2. Doi:10.1186/alzrt2
    • (2009) Alzh Res Ther , vol.1 , pp. 2
    • Aisen, P.S.1
  • 111
    • 62149105940 scopus 로고    scopus 로고
    • Safety and efficacy of quinacrine in human prion disease (PRION-1 study): A patient- preference trial
    • Collinge J, Gorham M, Hudson F, et al. Safety and efficacy of quinacrine in human prion disease (PRION-1 study): a patient- preference trial. Lancet Neurol 2009; 8: 334-344.
    • (2009) Lancet Neurol , vol.8 , pp. 334-344
    • Collinge, J.1    Gorham, M.2    Hudson, F.3
  • 112
    • 67649795561 scopus 로고    scopus 로고
    • Recent advances in prion chemotherapeutics
    • Sim VL, Caughey B. Recent advances in prion chemotherapeutics. Infect Dis Drug Targets 2009; 9: 81-91.
    • (2009) Infect Dis Drug Targets , vol.9 , pp. 81-91
    • Sim, V.L.1    Caughey, B.2
  • 114
    • 33745926817 scopus 로고    scopus 로고
    • Tricyclic antidepressants, quinacrine and a novel, synthetic chimera thereof clear prions by destabilizing detergent-resistant membrane compartments
    • Klingenstein R, Lober S, Kujala P, et al. Tricyclic antidepressants, quinacrine and a novel, synthetic chimera thereof clear prions by destabilizing detergent-resistant membrane compartments. J Neurochem 2006; 98: 748-759.
    • (2006) J Neurochem , vol.98 , pp. 748-759
    • Klingenstein, R.1    Lober, S.2    Kujala, P.3
  • 115
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
    • Doh-ura K, Iwaki T, Caughey B. Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J Virol 2000; 74: 4894-4897.
    • (2000) J Virol , vol.74 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 116
    • 33750980390 scopus 로고    scopus 로고
    • Drug-induced activation of SREBP-controlled lipogenic gene expression in CNS- related cell lines: Marked differences between various antipsychotic drugs
    • Fernø J, Skrede S, Vik-Mo AO, Havic B, Steen VD. Drug-induced activation of SREBP-controlled lipogenic gene expression in CNS- related cell lines: marked differences between various antipsychotic drugs. BMC Neurosci 2006; 7: 69-80.
    • (2006) BMC Neurosci , vol.7 , pp. 69-80
    • Fernø, J.1    Skrede, S.2    Vik-Mo, A.O.3    Havic, B.4    Steen, V.D.5
  • 117
    • 70350719357 scopus 로고    scopus 로고
    • Psychotropic drugs up- regulate the expression of cholesterol transport proteins including ApoE in cultured human CNS- and liver cells
    • Doi:10.1186/1471-2210-9-10
    • Vik-Mo AO, Fernø J, Skrede S, Steen VM. Psychotropic drugs up- regulate the expression of cholesterol transport proteins including ApoE in cultured human CNS- and liver cells. BMC Pharmacol 2009; 9:10. Doi:10.1186/1471-2210-9-10.
    • (2009) BMC Pharmacol , vol.9 , pp. 10
    • Vik-Mo, A.O.1    Fernø, J.2    Skrede, S.3    Steen, V.M.4
  • 118
    • 20844435988 scopus 로고    scopus 로고
    • Effects of sirolimus on mesangial cell cholesterol homeostasis: A novel mechanism for its action against lipid-mediated injury in renal allografts
    • Varghese Z, Fernando R, Moorhead JF, Powis SH, Ruan XZ. Effects of sirolimus on mesangial cell cholesterol homeostasis: a novel mechanism for its action against lipid-mediated injury in renal allografts. Am J Physiol Renal Physiol 2005; 289: 43-48.
    • (2005) Am J Physiol Renal Physiol , vol.289 , pp. 43-48
    • Varghese, Z.1    Fernando, R.2    Moorhead, J.F.3    Powis, S.H.4    Ruan, X.Z.5
  • 119
    • 0027096635 scopus 로고
    • Progesterone blocks cholesterol translocation from lysosomes
    • Butler JD, Banchette-Mackie J, Golden E, et al. Progesterone blocks cholesterol translocation from lysosomes. J Biol Chem 1992; 267: 23797-23805.
    • (1992) J Biol Chem , vol.267 , pp. 23797-23805
    • Butler, J.D.1    Banchette-Mackie, J.2    Golden, E.3
  • 120
    • 0031013536 scopus 로고    scopus 로고
    • Role of multidrug resistance P-glycoproteins in cholesterol esterification
    • Debry P, Nash EA, Neklason DW, Metherall JE. Role of multidrug resistance P-glycoproteins in cholesterol esterification. J Biol Chem 1997; 272: 1026-1031.
    • (1997) J Biol Chem , vol.272 , pp. 1026-1031
    • Debry, P.1    Nash, E.A.2    Neklason, D.W.3    Metherall, J.E.4
  • 121
    • 0038433334 scopus 로고    scopus 로고
    • Effects of troglitazone on intracellular cholesterol distribution and cholesterol-dependent cell functions in MA-10 Leydig tumor cells
    • Freeman DA, Romero A. Effects of troglitazone on intracellular cholesterol distribution and cholesterol-dependent cell functions in MA-10 Leydig tumor cells. Biochem Pharmacol 2003; 66: 307-313.
    • (2003) Biochem Pharmacol , vol.66 , pp. 307-313
    • Freeman, D.A.1    Romero, A.2
  • 122
    • 71849099881 scopus 로고    scopus 로고
    • Amyloid beta and APP as biomarkers for. Alzheimer's disease
    • Zetterberg H, Blennow K, Hanse E. Amyloid beta and APP as biomarkers for. Alzheimer's disease. Exp Gerontol 2010; 45: 23-29.
    • (2010) Exp Gerontol , vol.45 , pp. 23-29
    • Zetterberg, H.1    Blennow, K.2    Hanse, E.3
  • 123
    • 2542502430 scopus 로고    scopus 로고
    • ApoE genotype accounts for the vast majority of AD risk and AD pathology
    • Raber J, Huang Y, Ashford JW. ApoE genotype accounts for the vast majority of AD risk and AD pathology. Neurobiol Aging 2004; 25: 641-650.
    • (2004) Neurobiol Aging , vol.25 , pp. 641-650
    • Raber, J.1    Huang, Y.2    Ashford, J.W.3
  • 124
    • 47049119998 scopus 로고    scopus 로고
    • Biomarkers for cognitive impairment and dementia in elderly people
    • Sonnen JA, Montin KS, Quinn JF, et al. Biomarkers for cognitive impairment and dementia in elderly people. Lancet Neurol 2008; 7: 704-714.
    • (2008) Lancet Neurol , vol.7 , pp. 704-714
    • Sonnen, J.A.1    Montin, K.S.2    Quinn, J.F.3
  • 125
    • 8344278010 scopus 로고    scopus 로고
    • Acyl coenzyme A:Cholesterol acyltransferase inhibitors as hypolipidemic and antiatherosclerotic drugs
    • Alegret M, Llaverias G, Silvestre JS. Acyl coenzyme A:cholesterol acyltransferase inhibitors as hypolipidemic and antiatherosclerotic drugs. Methods Find Exp Clin Pharmacol 2004; 26: 563-586.
    • (2004) Methods Find Exp Clin Pharmacol , vol.26 , pp. 563-586
    • Alegret, M.1    Llaverias, G.2    Silvestre, J.S.3
  • 126
    • 44049085833 scopus 로고    scopus 로고
    • A multimeric quinacrine conjugate as a potential inhibitor of Alzheimer's β-amyloid fibril formation
    • Dolphin GT, Chierici S, Ouberai M, Dumy P, Garcia J. A multimeric quinacrine conjugate as a potential inhibitor of Alzheimer's β-amyloid fibril formation. ChemBioChem 2008; 9: 952-963.
    • (2008) ChemBioChem , vol.9 , pp. 952-963
    • Dolphin, G.T.1    Chierici, S.2    Ouberai, M.3    Dumy, P.4    Garcia, J.5
  • 127
    • 77957952943 scopus 로고    scopus 로고
    • CJD (Creutzfeldt-Jakob disease) quinacrine study. Available at:, [accessed March 4, 2009]
    • CJD (Creutzfeldt-Jakob disease) quinacrine study. Available at: http://clinicaltrials.gov/ct2/show/NCT00183092 [accessed March 4, 2009].
  • 128
    • 79959479102 scopus 로고    scopus 로고
    • Efficacy of PPAR-gamma agonist pioglitazone in mild Alzheimer disease
    • Nov 16 [Epub Ahead of Print] Doi:10.1016/jneurobiolaging
    • Sato T, Hanyu H, Hirao K, et al. Efficacy of PPAR-gamma agonist pioglitazone in mild Alzheimer disease. Neurobiol Aging 2009; Nov 16 [Epub ahead of print] Doi:10.1016/jneurobiolaging. 2009.10.009.
    • (2009) Neurobiol Aging
    • Sato, T.1    Hanyu, H.2    Hirao, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.