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Volumn 7, Issue 3, 2012, Pages

Amyloid precursor protein (app) mediated regulation of ganglioside homeostasis linking alzheimer's disease pathology with ganglioside metabolism

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; GANGLIOSIDE; GANGLIOSIDE GD3 SYNTHASE; GANGLIOSIDE GM3; PROTEIN FE65; SYNTHETASE; UNCLASSIFIED DRUG; ALPHA N ACETYLNEURAMINATE ALPHA 2,8 SIALYLTRANSFERASE; ALPHA-N-ACETYLNEURAMINATE ALPHA-2,8-SIALYLTRANSFERASE; PRESENILIN 1; PRESENILIN 2; SIALYLTRANSFERASE; SMALL INTERFERING RNA;

EID: 84859038034     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0034095     Document Type: Article
Times cited : (50)

References (72)
  • 1
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
    • Selkoe DJ, (2004) Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 6: 1054-1061.
    • (2004) Nat Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 3
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein beta-secretase from human brain
    • Sinha S, Anderson JP, Barbour R, Basi GS, Caccavello R, et al. (1999) Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature 402: 537-540.
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1    Anderson, J.P.2    Barbour, R.3    Basi, G.S.4    Caccavello, R.5
  • 4
    • 57649174625 scopus 로고    scopus 로고
    • Intramembrane proteolysis by gamma-secretase
    • Steiner H, Fluhrer R, Haass C, (2008) Intramembrane proteolysis by gamma-secretase. J Biol Chem 283: 29627-29631.
    • (2008) J Biol Chem , vol.283 , pp. 29627-29631
    • Steiner, H.1    Fluhrer, R.2    Haass, C.3
  • 5
    • 53749105377 scopus 로고    scopus 로고
    • Presenilins: members of the gamma-secretase quartets, but part-time soloists too
    • Wakabayashi T, De Strooper B, (2008) Presenilins: members of the gamma-secretase quartets, but part-time soloists too. Physiology (Bethesda) 23: 194-204.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 194-204
    • Wakabayashi, T.1    De Strooper, B.2
  • 6
    • 13844255273 scopus 로고    scopus 로고
    • Molecular biology and genetics of Alzheimer's disease
    • St George-Hyslop PH, Petit A, (2005) Molecular biology and genetics of Alzheimer's disease. C R Biol 328: 119-130.
    • (2005) C R Biol , vol.328 , pp. 119-130
    • St George-Hyslop, P.H.1    Petit, A.2
  • 7
    • 0001504829 scopus 로고    scopus 로고
    • Simvastatin strongly reduces levels of Alzheimer's disease beta -amyloid peptides Abeta 42 and Abeta 40 in vitro and in vivo
    • Fassbender K, Simons M, Bergmann C, Stroick M, Lutjohann D, et al. (2001) Simvastatin strongly reduces levels of Alzheimer's disease beta-amyloid peptides Abeta 42 and Abeta 40 in vitro and in vivo. Proc Natl Acad Sci U S A 98: 5856-5861.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5856-5861
    • Fassbender, K.1    Simons, M.2    Bergmann, C.3    Stroick, M.4    Lutjohann, D.5
  • 8
    • 0347318065 scopus 로고    scopus 로고
    • Cholesterol and the biology of Alzheimer's disease
    • Wolozin B, (2004) Cholesterol and the biology of Alzheimer's disease. Neuron 41: 7-10.
    • (2004) Neuron , vol.41 , pp. 7-10
    • Wolozin, B.1
  • 9
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • Kovacs DM, Fausett HJ, Page KJ, Kim TW, Moir RD, et al. (1996) Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nat Med 2: 224-229.
    • (1996) Nat Med , vol.2 , pp. 224-229
    • Kovacs, D.M.1    Fausett, H.J.2    Page, K.J.3    Kim, T.W.4    Moir, R.D.5
  • 10
    • 28644451007 scopus 로고    scopus 로고
    • Regulation of cholesterol and sphingomyelin metabolism by amyloid-beta and presenilin
    • Grimm MO, Grimm HS, Patzold AJ, Zinser EG, Halonen R, et al. (2005) Regulation of cholesterol and sphingomyelin metabolism by amyloid-beta and presenilin. Nat Cell Biol 7: 1118-1123.
    • (2005) Nat Cell Biol , vol.7 , pp. 1118-1123
    • Grimm, M.O.1    Grimm, H.S.2    Patzold, A.J.3    Zinser, E.G.4    Halonen, R.5
  • 11
    • 53049089639 scopus 로고    scopus 로고
    • Direct and potent regulation of gamma-secretase by its lipid microenvironment
    • Osenkowski P, Ye W, Wang R, Wolfe MS, Selkoe DJ, (2008) Direct and potent regulation of gamma-secretase by its lipid microenvironment. J Biol Chem 283: 22529-22540.
    • (2008) J Biol Chem , vol.283 , pp. 22529-22540
    • Osenkowski, P.1    Ye, W.2    Wang, R.3    Wolfe, M.S.4    Selkoe, D.J.5
  • 12
    • 34748897213 scopus 로고    scopus 로고
    • Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1
    • Liu Q, Zerbinatti CV, Zhang J, Hoe HS, Wang B, et al. (2007) Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1. Neuron 56: 66-78.
    • (2007) Neuron , vol.56 , pp. 66-78
    • Liu, Q.1    Zerbinatti, C.V.2    Zhang, J.3    Hoe, H.S.4    Wang, B.5
  • 13
    • 55749095544 scopus 로고    scopus 로고
    • Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid beta-protein fibrillogenesis
    • Yamamoto N, Matsubara T, Sato T, Yanagisawa K, (2008) Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid beta-protein fibrillogenesis. Biochim Biophys Acta 1778: 2717-2726.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2717-2726
    • Yamamoto, N.1    Matsubara, T.2    Sato, T.3    Yanagisawa, K.4
  • 14
    • 67649453609 scopus 로고    scopus 로고
    • Elimination of GD3 synthase improves memory and reduces amyloid-beta plaque load in transgenic mice
    • Bernardo A, Harrison FE, McCord M, Zhao J, Bruchey A, et al. (2009) Elimination of GD3 synthase improves memory and reduces amyloid-beta plaque load in transgenic mice. Neurobiol Aging 30: 1777-1791.
    • (2009) Neurobiol Aging , vol.30 , pp. 1777-1791
    • Bernardo, A.1    Harrison, F.E.2    McCord, M.3    Zhao, J.4    Bruchey, A.5
  • 15
    • 79851485651 scopus 로고    scopus 로고
    • Pathological significance of ganglioside clusters in Alzheimer's disease
    • Yanagisawa K, (2011) Pathological significance of ganglioside clusters in Alzheimer's disease. J Neurochem.
    • (2011) J Neurochem
    • Yanagisawa, K.1
  • 16
    • 79952136169 scopus 로고    scopus 로고
    • Formation of Toxic Amyloid Fibrils by Amyloid beta-Protein on Ganglioside Clusters
    • Matsuzaki K, (2011) Formation of Toxic Amyloid Fibrils by Amyloid beta-Protein on Ganglioside Clusters. Int J Alzheimers Dis 2011: 956104.
    • (2011) Int J Alzheimers Dis , vol.2011 , pp. 956104
    • Matsuzaki, K.1
  • 18
    • 34548329395 scopus 로고    scopus 로고
    • The metabolism and function of sphingolipids and glycosphingolipids
    • Lahiri S, Futerman AH, (2007) The metabolism and function of sphingolipids and glycosphingolipids. Cell Mol Life Sci 64: 2270-2284.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2270-2284
    • Lahiri, S.1    Futerman, A.H.2
  • 20
    • 13244272410 scopus 로고    scopus 로고
    • Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains
    • Molander-Melin M, Blennow K, Bogdanovic N, Dellheden B, Mansson JE, et al. (2005) Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains. J Neurochem 92: 171-182.
    • (2005) J Neurochem , vol.92 , pp. 171-182
    • Molander-Melin, M.1    Blennow, K.2    Bogdanovic, N.3    Dellheden, B.4    Mansson, J.E.5
  • 21
    • 35148814075 scopus 로고    scopus 로고
    • Genotype-related changes of ganglioside composition in brain regions of transgenic mouse models of Alzheimer's disease
    • Barrier L, Ingrand S, Damjanac M, Rioux Bilan A, Hugon J, et al. (2007) Genotype-related changes of ganglioside composition in brain regions of transgenic mouse models of Alzheimer's disease. Neurobiol Aging 28: 1863-1872.
    • (2007) Neurobiol Aging , vol.28 , pp. 1863-1872
    • Barrier, L.1    Ingrand, S.2    Damjanac, M.3    Rioux Bilan, A.4    Hugon, J.5
  • 22
    • 6044221306 scopus 로고    scopus 로고
    • GM1 ganglioside regulates the proteolysis of amyloid precursor protein
    • Zha Q, Ruan Y, Hartmann T, Beyreuther K, Zhang D, (2004) GM1 ganglioside regulates the proteolysis of amyloid precursor protein. Mol Psychiatry 9: 946-952.
    • (2004) Mol Psychiatry , vol.9 , pp. 946-952
    • Zha, Q.1    Ruan, Y.2    Hartmann, T.3    Beyreuther, K.4    Zhang, D.5
  • 23
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K, Odaka A, Suzuki N, Ihara Y, (1995) GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease. Nat Med 1: 1062-1066.
    • (1995) Nat Med , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 24
    • 13744255467 scopus 로고    scopus 로고
    • GM1 ganglioside-mediated accumulation of amyloid beta-protein on cell membranes
    • Wakabayashi M, Okada T, Kozutsumi Y, Matsuzaki K, (2005) GM1 ganglioside-mediated accumulation of amyloid beta-protein on cell membranes. Biochem Biophys Res Commun 328: 1019-1023.
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 1019-1023
    • Wakabayashi, M.1    Okada, T.2    Kozutsumi, Y.3    Matsuzaki, K.4
  • 25
    • 34447255463 scopus 로고    scopus 로고
    • Formation of toxic fibrils of Alzheimer's amyloid beta-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component
    • Okada T, Wakabayashi M, Ikeda K, Matsuzaki K, (2007) Formation of toxic fibrils of Alzheimer's amyloid beta-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component. J Mol Biol 371: 481-489.
    • (2007) J Mol Biol , vol.371 , pp. 481-489
    • Okada, T.1    Wakabayashi, M.2    Ikeda, K.3    Matsuzaki, K.4
  • 26
    • 13044278313 scopus 로고    scopus 로고
    • Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency
    • Herreman A, Hartmann D, Annaert W, Saftig P, Craessaerts K, et al. (1999) Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency. Proc Natl Acad Sci U S A 96: 11872-11877.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11872-11877
    • Herreman, A.1    Hartmann, D.2    Annaert, W.3    Saftig, P.4    Craessaerts, K.5
  • 27
    • 0037444574 scopus 로고    scopus 로고
    • gamma-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation
    • Herreman A, Van Gassen G, Bentahir M, Nyabi O, Craessaerts K, et al. (2003) gamma-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation. J Cell Sci 116: 1127-1136.
    • (2003) J Cell Sci , vol.116 , pp. 1127-1136
    • Herreman, A.1    Van Gassen, G.2    Bentahir, M.3    Nyabi, O.4    Craessaerts, K.5
  • 28
    • 0028099263 scopus 로고
    • Membrane lipids of adult human brain: lipid composition of frontal and temporal lobe in subjects of age 20 to 100 years
    • Svennerholm L, Bostrom K, Jungbjer B, Olsson L, (1994) Membrane lipids of adult human brain: lipid composition of frontal and temporal lobe in subjects of age 20 to 100 years. J Neurochem 63: 1802-1811.
    • (1994) J Neurochem , vol.63 , pp. 1802-1811
    • Svennerholm, L.1    Bostrom, K.2    Jungbjer, B.3    Olsson, L.4
  • 29
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: proteasome of the membrane?
    • Kopan R, Ilagan MX, (2004) Gamma-secretase: proteasome of the membrane? Nat Rev Mol Cell Biol 5: 499-504.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 30
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D, Eckman C, Jensen M, Song X, Citron M, et al. (1996) Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat Med 2: 864-870.
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5
  • 31
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • von Rotz RC, Kohli BM, Bosset J, Meier M, Suzuki T, et al. (2004) The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J Cell Sci 117: 4435-4448.
    • (2004) J Cell Sci , vol.117 , pp. 4435-4448
    • von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5
  • 32
    • 33745584643 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes
    • Hebert SS, Serneels L, Tolia A, Craessaerts K, Derks C, et al. (2006) Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes. EMBO Rep 7: 739-745.
    • (2006) EMBO Rep , vol.7 , pp. 739-745
    • Hebert, S.S.1    Serneels, L.2    Tolia, A.3    Craessaerts, K.4    Derks, C.5
  • 33
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration
    • Selkoe D, Kopan R, (2003) Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu Rev Neurosci 26: 565-597.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 34
    • 34447640166 scopus 로고    scopus 로고
    • The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice
    • Ring S, Weyer SW, Kilian SB, Waldron E, Pietrzik CU, et al. (2007) The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice. J Neurosci 27: 7817-7826.
    • (2007) J Neurosci , vol.27 , pp. 7817-7826
    • Ring, S.1    Weyer, S.W.2    Kilian, S.B.3    Waldron, E.4    Pietrzik, C.U.5
  • 35
    • 0032401578 scopus 로고    scopus 로고
    • The deletion of the C-terminal tail and addition of an endoplasmic reticulum targeting signal to Alzheimer's amyloid precursor protein change its localization, secretion, and intracellular proteolysis
    • Kouchi Z, Kinouchi T, Sorimachi H, Ishiura S, Suzuki K, (1998) The deletion of the C-terminal tail and addition of an endoplasmic reticulum targeting signal to Alzheimer's amyloid precursor protein change its localization, secretion, and intracellular proteolysis. Eur J Biochem 258: 291-300.
    • (1998) Eur J Biochem , vol.258 , pp. 291-300
    • Kouchi, Z.1    Kinouchi, T.2    Sorimachi, H.3    Ishiura, S.4    Suzuki, K.5
  • 36
    • 0030900187 scopus 로고    scopus 로고
    • Deletion of an endosomal/lysosomal targeting signal promotes the secretion of Alzheimer's disease amyloid precursor protein (APP)
    • Ono Y, Kinouchi T, Sorimachi H, Ishiura S, Suzuki K, (1997) Deletion of an endosomal/lysosomal targeting signal promotes the secretion of Alzheimer's disease amyloid precursor protein (APP). J Biochem 121: 585-590.
    • (1997) J Biochem , vol.121 , pp. 585-590
    • Ono, Y.1    Kinouchi, T.2    Sorimachi, H.3    Ishiura, S.4    Suzuki, K.5
  • 37
    • 35548994599 scopus 로고    scopus 로고
    • Serum insensitive, intranuclear protein delivery by the multipurpose cationic lipid SAINT-2
    • van der Gun BT, Monami A, Laarmann S, Rasko T, Slaska-Kiss K, et al. (2007) Serum insensitive, intranuclear protein delivery by the multipurpose cationic lipid SAINT-2. J Control Release 123: 228-238.
    • (2007) J Control Release , vol.123 , pp. 228-238
    • van der Gun, B.T.1    Monami, A.2    Laarmann, S.3    Rasko, T.4    Slaska-Kiss, K.5
  • 38
    • 45549093275 scopus 로고    scopus 로고
    • Independent inhibition of Alzheimer disease beta- and gamma-secretase cleavage by lowered cholesterol levels
    • Grimm MO, Grimm HS, Tomic I, Beyreuther K, Hartmann T, et al. (2008) Independent inhibition of Alzheimer disease beta- and gamma-secretase cleavage by lowered cholesterol levels. J Biol Chem 283: 11302-11311.
    • (2008) J Biol Chem , vol.283 , pp. 11302-11311
    • Grimm, M.O.1    Grimm, H.S.2    Tomic, I.3    Beyreuther, K.4    Hartmann, T.5
  • 39
  • 40
    • 0028181256 scopus 로고
    • Polarized secretion of beta-amyloid precursor protein and amyloid beta-peptide in MDCK cells
    • Haass C, Koo EH, Teplow DB, Selkoe DJ, (1994) Polarized secretion of beta-amyloid precursor protein and amyloid beta-peptide in MDCK cells. Proc Natl Acad Sci U S A 91: 1564-1568.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1564-1568
    • Haass, C.1    Koo, E.H.2    Teplow, D.B.3    Selkoe, D.J.4
  • 41
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • Hu X, Crick SL, Bu G, Frieden C, Pappu RV, et al. (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci U S A 106: 20324-20329.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5
  • 42
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides
    • Hartmann T, Bieger SC, Bruhl B, Tienari PJ, Ida N, et al. (1997) Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides. Nat Med 3: 1016-1020.
    • (1997) Nat Med , vol.3 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Bruhl, B.3    Tienari, P.J.4    Ida, N.5
  • 43
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook DG, Forman MS, Sung JC, Leight S, Kolson DL, et al. (1997) Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat Med 3: 1021-1023.
    • (1997) Nat Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5
  • 44
    • 0038037751 scopus 로고    scopus 로고
    • gamma-Secretase cleavage site specificity differs for intracellular and secretory amyloid beta
    • Grimm HS, Beher D, Lichtenthaler SF, Shearman MS, Beyreuther K, et al. (2003) gamma-Secretase cleavage site specificity differs for intracellular and secretory amyloid beta. J Biol Chem 278: 13077-13085.
    • (2003) J Biol Chem , vol.278 , pp. 13077-13085
    • Grimm, H.S.1    Beher, D.2    Lichtenthaler, S.F.3    Shearman, M.S.4    Beyreuther, K.5
  • 46
    • 0032557170 scopus 로고    scopus 로고
    • Inhibition of secreted phospholipases A2 by annexin V. Competition for anionic phospholipid interfaces allows an assessment of the relative interfacial affinities of secreted phospholipases A2
    • Buckland AG, Wilton DC, (1998) Inhibition of secreted phospholipases A2 by annexin V. Competition for anionic phospholipid interfaces allows an assessment of the relative interfacial affinities of secreted phospholipases A2. Biochim Biophys Acta 1391: 367-376.
    • (1998) Biochim Biophys Acta , vol.1391 , pp. 367-376
    • Buckland, A.G.1    Wilton, D.C.2
  • 47
    • 52049113661 scopus 로고    scopus 로고
    • Cholesterol binding to amyloid-beta fibrils: a TEM study
    • Harris JR, (2008) Cholesterol binding to amyloid-beta fibrils: a TEM study. Micron 39: 1192-1196.
    • (2008) Micron , vol.39 , pp. 1192-1196
    • Harris, J.R.1
  • 48
    • 18844428601 scopus 로고    scopus 로고
    • GM1 ganglioside and the seeding of amyloid in Alzheimer's disease: endogenous seed for Alzheimer amyloid
    • Yanagisawa K, (2005) GM1 ganglioside and the seeding of amyloid in Alzheimer's disease: endogenous seed for Alzheimer amyloid. Neuroscientist 11: 250-260.
    • (2005) Neuroscientist , vol.11 , pp. 250-260
    • Yanagisawa, K.1
  • 49
    • 0035870150 scopus 로고    scopus 로고
    • Characterization of high-affinity binding between gangliosides and amyloid beta-protein
    • Ariga T, Kobayashi K, Hasegawa A, Kiso M, Ishida H, et al. (2001) Characterization of high-affinity binding between gangliosides and amyloid beta-protein. Arch Biochem Biophys 388: 225-230.
    • (2001) Arch Biochem Biophys , vol.388 , pp. 225-230
    • Ariga, T.1    Kobayashi, K.2    Hasegawa, A.3    Kiso, M.4    Ishida, H.5
  • 50
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Sudhof TC, (2001) A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293: 115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 51
    • 55549113149 scopus 로고    scopus 로고
    • Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2
    • Radzimanowski J, Simon B, Sattler M, Beyreuther K, Sinning I, et al. (2008) Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2. EMBO Rep 9: 1134-1140.
    • (2008) EMBO Rep , vol.9 , pp. 1134-1140
    • Radzimanowski, J.1    Simon, B.2    Sattler, M.3    Beyreuther, K.4    Sinning, I.5
  • 52
    • 23044510465 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide
    • Tamboli IY, Prager K, Barth E, Heneka M, Sandhoff K, et al. (2005) Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide. J Biol Chem 280: 28110-28117.
    • (2005) J Biol Chem , vol.280 , pp. 28110-28117
    • Tamboli, I.Y.1    Prager, K.2    Barth, E.3    Heneka, M.4    Sandhoff, K.5
  • 53
    • 0035921427 scopus 로고    scopus 로고
    • The discrepancy between presenilin subcellular localization and gamma-secretase processing of amyloid precursor protein
    • Cupers P, Bentahir M, Craessaerts K, Orlans I, Vanderstichele H, et al. (2001) The discrepancy between presenilin subcellular localization and gamma-secretase processing of amyloid precursor protein. J Cell Biol 154: 731-740.
    • (2001) J Cell Biol , vol.154 , pp. 731-740
    • Cupers, P.1    Bentahir, M.2    Craessaerts, K.3    Orlans, I.4    Vanderstichele, H.5
  • 54
    • 79954592687 scopus 로고    scopus 로고
    • Docosahexaenoic Acid Reduces Amyloid {beta} Production via Multiple Pleiotropic Mechanisms
    • Grimm MO, Kuchenbecker J, Grösgen S, Burg VK, Hundsdorfer B, et al. (2011) Docosahexaenoic Acid Reduces Amyloid {beta} Production via Multiple Pleiotropic Mechanisms. J Biol Chem 286: 14028-14039.
    • (2011) J Biol Chem , vol.286 , pp. 14028-14039
    • Grimm, M.O.1    Kuchenbecker, J.2    Grösgen, S.3    Burg, V.K.4    Hundsdorfer, B.5
  • 55
    • 68249128437 scopus 로고    scopus 로고
    • Gangliosides determine the amyloid pathology of Alzheimer's disease
    • Oikawa N, Yamaguchi H, Ogino K, Taki T, Yuyama K, et al. (2009) Gangliosides determine the amyloid pathology of Alzheimer's disease. Neuroreport 20: 1043-1046.
    • (2009) Neuroreport , vol.20 , pp. 1043-1046
    • Oikawa, N.1    Yamaguchi, H.2    Ogino, K.3    Taki, T.4    Yuyama, K.5
  • 56
    • 28044454975 scopus 로고    scopus 로고
    • Enhanced susceptibility to kainate-induced seizures, neuronal apoptosis, and death in mice lacking gangliotetraose gangliosides: protection with LIGA 20, a membrane-permeant analog of GM1
    • Wu G, Lu ZH, Wang J, Wang Y, Xie X, et al. (2005) Enhanced susceptibility to kainate-induced seizures, neuronal apoptosis, and death in mice lacking gangliotetraose gangliosides: protection with LIGA 20, a membrane-permeant analog of GM1. J Neurosci 25: 11014-11022.
    • (2005) J Neurosci , vol.25 , pp. 11014-11022
    • Wu, G.1    Lu, Z.H.2    Wang, J.3    Wang, Y.4    Xie, X.5
  • 57
    • 80052953970 scopus 로고    scopus 로고
    • Amyloid-beta induced toxicity involves ganglioside expression and is sensitive to GM1 neuroprotective action
    • Kreutz F, Frozza RL, Breier AC, de Oliveira VA, Horn AP, et al. (2011) Amyloid-beta induced toxicity involves ganglioside expression and is sensitive to GM1 neuroprotective action. Neurochem Int 59: 648-655.
    • (2011) Neurochem Int , vol.59 , pp. 648-655
    • Kreutz, F.1    Frozza, R.L.2    Breier, A.C.3    de Oliveira, V.A.4    Horn, A.P.5
  • 58
    • 83455162605 scopus 로고    scopus 로고
    • Intracranial V. cholerae Sialidase Protects against Excitotoxic Neurodegeneration
    • Dhanushkodi A, McDonald MP, (2011) Intracranial V. cholerae Sialidase Protects against Excitotoxic Neurodegeneration. PLoS One 6: e29285.
    • (2011) PLoS One , vol.6
    • Dhanushkodi, A.1    McDonald, M.P.2
  • 59
    • 0034329291 scopus 로고    scopus 로고
    • Mice with combined gene knock-outs reveal essential and partially redundant functions of amyloid precursor protein family members
    • Heber S, Herms J, Gajic V, Hainfellner J, Aguzzi A, et al. (2000) Mice with combined gene knock-outs reveal essential and partially redundant functions of amyloid precursor protein family members. J Neurosci 20: 7951-7963.
    • (2000) J Neurosci , vol.20 , pp. 7951-7963
    • Heber, S.1    Herms, J.2    Gajic, V.3    Hainfellner, J.4    Aguzzi, A.5
  • 60
    • 0027519411 scopus 로고
    • Gangliosides can activate human alternative complement pathway
    • Oshima H, Soma G, Mizuno D, (1993) Gangliosides can activate human alternative complement pathway. Int Immunol 5: 1349-1351.
    • (1993) Int Immunol , vol.5 , pp. 1349-1351
    • Oshima, H.1    Soma, G.2    Mizuno, D.3
  • 61
    • 0015456046 scopus 로고
    • Interaction of triiodide anion with gangliosides in aqueous iodine
    • Yohe HC, Rosenberg A, (1972) Interaction of triiodide anion with gangliosides in aqueous iodine. Chem Phys Lipids 9: 279-294.
    • (1972) Chem Phys Lipids , vol.9 , pp. 279-294
    • Yohe, H.C.1    Rosenberg, A.2
  • 63
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida N, Hartmann T, Pantel J, Schroder J, Zerfass R, et al. (1996) Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J Biol Chem 271: 22908-22914.
    • (1996) J Biol Chem , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5
  • 65
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ, (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37: 911-917.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 66
    • 0034293714 scopus 로고    scopus 로고
    • GM1-gangliosidosis in a cross-bred dog confirmed by detection of GM1-ganglioside using electrospray ionisation-tandem mass spectrometry
    • Whitfield P, Johnson AW, Dunn KA, Delauche AJ, Winchester BG, et al. (2000) GM1-gangliosidosis in a cross-bred dog confirmed by detection of GM1-ganglioside using electrospray ionisation-tandem mass spectrometry. Acta Neuropathol (Berl) 100: 409-414.
    • (2000) Acta Neuropathol (Berl) , vol.100 , pp. 409-414
    • Whitfield, P.1    Johnson, A.W.2    Dunn, K.A.3    Delauche, A.J.4    Winchester, B.G.5
  • 68
    • 0018720271 scopus 로고
    • A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels
    • Switzer RC 3rd, Merril CR, Shifrin S, (1979) A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal Biochem 98: 231-237.
    • (1979) Anal Biochem , vol.98 , pp. 231-237
    • Switzer III, R.C.1    Merril, C.R.2    Shifrin, S.3
  • 69
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, et al. (2002) Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J Biol Chem 277: 32046-32053.
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5
  • 70
    • 0023039167 scopus 로고
    • Ganglioside biosynthesis in rat liver. Characterization of three sialyltransferases
    • Busam K, Decker K, (1986) Ganglioside biosynthesis in rat liver. Characterization of three sialyltransferases. Eur J Biochem 160: 23-30.
    • (1986) Eur J Biochem , vol.160 , pp. 23-30
    • Busam, K.1    Decker, K.2
  • 71
    • 0041589436 scopus 로고    scopus 로고
    • Partial purification and characterization of gamma-secretase from post-mortem human brain
    • Farmery MR, Tjernberg LO, Pursglove SE, Bergman A, Winblad B, et al. (2003) Partial purification and characterization of gamma-secretase from post-mortem human brain. J Biol Chem 278: 24277-24284.
    • (2003) J Biol Chem , vol.278 , pp. 24277-24284
    • Farmery, M.R.1    Tjernberg, L.O.2    Pursglove, S.E.3    Bergman, A.4    Winblad, B.5
  • 72
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2


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