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Volumn 9, Issue 8, 2014, Pages

β2-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH

Author keywords

[No Author keywords available]

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLGLYCEROL; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLSERINE; AMYLOID; BETA 2 MICROGLOBULIN; LIPID; LIPOSOME; LYSOBISPHOSPHATIDIC ACID; TRYPTOPHAN; UNCLASSIFIED DRUG; ARTIFICIAL MEMBRANE;

EID: 84905457722     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0104492     Document Type: Article
Times cited : (33)

References (91)
  • 1
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M (2012) The amyloid state of proteins in human diseases. Cell 148: 1188-1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 2
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F (1999) Analysis of protein aggregation kinetics. Method Enzymol 309: 256-274.
    • (1999) Method Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 3
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles TPJ, Waudby CA, Devlin GL, Cohen SIA, Aguzzi A, et al. (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326: 1533-1537.
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.J.1    Waudby, C.A.2    Devlin, G.L.3    Cohen, S.I.A.4    Aguzzi, A.5
  • 4
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue WF, Homans SW, Radford SE (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. PNAS 105: 8926-8931.
    • (2008) PNAS , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 5
    • 80053596817 scopus 로고    scopus 로고
    • 2-microglobulin amyloid assembly
    • 2-microglobulin amyloid assembly. FEBS J 278: 3868-3883.
    • (2011) FEBS J , vol.278 , pp. 3868-3883
    • Eichner, T.1    Radford, S.E.2
  • 7
    • 37549063068 scopus 로고    scopus 로고
    • Role of intermolecular forces in defining material properties of protein nanofibrils
    • Knowles TP, Fitzpatrick AW, Meehan S, Mott HR, Vendruscolo M, et al. (2007) Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318: 1900-1903.
    • (2007) Science , vol.318 , pp. 1900-1903
    • Knowles, T.P.1    Fitzpatrick, A.W.2    Meehan, S.3    Mott, H.R.4    Vendruscolo, M.5
  • 8
    • 84887899951 scopus 로고    scopus 로고
    • Assessing the causes and consequences of co-polymerization in amyloid formation
    • Sarell CJ, Stockley PG, Radford SE (2013) Assessing the causes and consequences of co-polymerization in amyloid formation. Prion 7: 359-368.
    • (2013) Prion , vol.7 , pp. 359-368
    • Sarell, C.J.1    Stockley, P.G.2    Radford, S.E.3
  • 9
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • DOI 10.1038/nature02998
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431: 805-810. (Pubitemid 39434070)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 10
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Abeta oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova I, Karran E, De Strooper B (2012) The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes. Nature Neurosci 15: 349-357.
    • (2012) Nature Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 11
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of alpha-synuclein
    • Cremades N, Cohen SIA, Deas E, Abramov AY, Chen AY, et al. (2012) Direct observation of the interconversion of normal and toxic forms of alpha-synuclein. Cell 149: 1048-1059.
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.A.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5
  • 12
    • 84856545963 scopus 로고    scopus 로고
    • Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1
    • Bucciantini M, Nosi D, Forzan M, Russo E, Calamai M, et al. (2012) Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J 26: 818-831.
    • (2012) FASEB J , vol.26 , pp. 818-831
    • Bucciantini, M.1    Nosi, D.2    Forzan, M.3    Russo, E.4    Calamai, M.5
  • 13
    • 84862701723 scopus 로고    scopus 로고
    • Fibrillar alpha-synuclein and huntingtin exon 1 assemblies are toxic to the cells
    • Pieri L, Madiona K, Bousset L, Melki R (2012) Fibrillar alpha-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys J 102: 2894-2905.
    • (2012) Biophys J , vol.102 , pp. 2894-2905
    • Pieri, L.1    Madiona, K.2    Bousset, L.3    Melki, R.4
  • 15
    • 77949278013 scopus 로고    scopus 로고
    • Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters
    • Xue WF, Hellewell AL, Hewitt EW, Radford SE (2010) Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters. Prion 4: 20-25.
    • (2010) Prion , vol.4 , pp. 20-25
    • Xue, W.F.1    Hellewell, A.L.2    Hewitt, E.W.3    Radford, S.E.4
  • 16
    • 78049290389 scopus 로고    scopus 로고
    • Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity
    • Stefani M (2010) Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity. FEBS J 277: 4602-4613.
    • (2010) FEBS J , vol.277 , pp. 4602-4613
    • Stefani, M.1
  • 17
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious oligomerization of the amyloidogenic proteins
    • Uversky VN (2010) Mysterious oligomerization of the amyloidogenic proteins. FEBS J 277: 2940-2953.
    • (2010) FEBS J , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 18
    • 84870565641 scopus 로고    scopus 로고
    • What does make an amyloid toxic: Morphology, structure or interaction with membrane?
    • Berthelot K, Cullin C, Lecomte S (2013) What does make an amyloid toxic: morphology, structure or interaction with membrane? Biochimie 95: 12-19.
    • (2013) Biochimie , vol.95 , pp. 12-19
    • Berthelot, K.1    Cullin, C.2    Lecomte, S.3
  • 19
    • 84868316813 scopus 로고    scopus 로고
    • Conformations of islet amyloid polypeptide monomers in a membrane environment: Implications for fibril formation
    • Duan M, Fan J, Huo S (2012) Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation. PLoS One 7: e47150.
    • (2012) PLoS One , vol.7
    • Duan, M.1    Fan, J.2    Huo, S.3
  • 20
    • 84867525379 scopus 로고    scopus 로고
    • Radiating amyloid fibril formation on the surface of lipid membranes through unit-assembly of oligomeric species of alpha-Synuclein
    • Lee JH, Hong CS, Lee S, Yang JE, Park YI, et al. (2012) Radiating amyloid fibril formation on the surface of lipid membranes through unit-assembly of oligomeric species of alpha-Synuclein. PLoS One 7: e47580.
    • (2012) PLoS One , vol.7
    • Lee, J.H.1    Hong, C.S.2    Lee, S.3    Yang, J.E.4    Park, Y.I.5
  • 21
    • 84867091546 scopus 로고    scopus 로고
    • Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation
    • Sciacca MFM, Brender JR, Lee DK, Ramamoorthy A (2012) Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation. Biochemistry 51: 7676-7684.
    • (2012) Biochemistry , vol.51 , pp. 7676-7684
    • Sciacca, M.F.M.1    Brender, J.R.2    Lee, D.K.3    Ramamoorthy, A.4
  • 22
    • 84866425464 scopus 로고    scopus 로고
    • The polyphenol EGCG inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution
    • Engel MFM, VandenAkker CC, Schleeger M, Velikov KP, Koenderink GH, et al. (2012) The polyphenol EGCG inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution. J Am Chem Soc 134: 14781-14788.
    • (2012) J Am Chem Soc , vol.134 , pp. 14781-14788
    • Engel, M.F.M.1    VandenAkker, C.C.2    Schleeger, M.3    Velikov, K.P.4    Koenderink, G.H.5
  • 23
    • 82555170657 scopus 로고    scopus 로고
    • Mechanism of membrane interaction and disruption by alpha-synuclein
    • Reynolds NP, Soragni A, Rabe M, Verdes D, Liverani E, et al. (2011) Mechanism of membrane interaction and disruption by alpha-synuclein. J Am Chem Soc 133: 19366-19375.
    • (2011) J Am Chem Soc , vol.133 , pp. 19366-19375
    • Reynolds, N.P.1    Soragni, A.2    Rabe, M.3    Verdes, D.4    Liverani, E.5
  • 24
    • 84865388990 scopus 로고    scopus 로고
    • Two-step mechanism of membrane disruption by Abeta through membrane fragmentation and pore formation
    • Sciacca MF, Kotler SA, Brender JR, Chen J, Lee DK, et al. (2012) Two-step mechanism of membrane disruption by Abeta through membrane fragmentation and pore formation. Biophys J 103: 702-710.
    • (2012) Biophys J , vol.103 , pp. 702-710
    • Sciacca, M.F.1    Kotler, S.A.2    Brender, J.R.3    Chen, J.4    Lee, D.K.5
  • 25
    • 80052747064 scopus 로고    scopus 로고
    • Abeta42 oligomers, but not fibrils, simultaneously bind to and cause damage to ganglioside-containing lipid membranes
    • Williams TL, Johnson BR, Urbanc B, Jenkins AT, Connell SD, et al. (2011) Abeta42 oligomers, but not fibrils, simultaneously bind to and cause damage to ganglioside-containing lipid membranes. Biochem J 439: 67-77.
    • (2011) Biochem J , vol.439 , pp. 67-77
    • Williams, T.L.1    Johnson, B.R.2    Urbanc, B.3    Jenkins, A.T.4    Connell, S.D.5
  • 26
    • 80053589341 scopus 로고    scopus 로고
    • Membrane and surface interactions of Alzheimer's Abeta peptide-insights into the mechanism of cytotoxicity
    • Williams TL, Serpell LC (2011) Membrane and surface interactions of Alzheimer's Abeta peptide-insights into the mechanism of cytotoxicity. FEBS J 278: 3905-3917.
    • (2011) FEBS J , vol.278 , pp. 3905-3917
    • Williams, T.L.1    Serpell, L.C.2
  • 28
    • 84860919373 scopus 로고    scopus 로고
    • Membrane trafficking pathways in Alzheimer's disease
    • Rajendran L, Annaert W (2012) Membrane trafficking pathways in Alzheimer's disease. Traffic 13: 759-770.
    • (2012) Traffic , vol.13 , pp. 759-770
    • Rajendran, L.1    Annaert, W.2
  • 30
    • 0022391603 scopus 로고
    • 2-microglobulin
    • DOI 10.1016/0006-291X(85)91948-5
    • Gejyo F, Yamada T, Odani S, Nakagawa Y, Arakawa M, et al. (1985) A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin. Biochem Biophys Res Commun 129: 701-706. (Pubitemid 15243930)
    • (1985) Biochemical and Biophysical Research Communications , vol.129 , Issue.3 , pp. 701-706
    • Gejyo, F.1    Yamada, T.2    Odani, S.3
  • 33
    • 0035955555 scopus 로고    scopus 로고
    • 2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
    • 2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J Mol Biol 313: 559-571.
    • (2001) J Mol Biol , vol.313 , pp. 559-571
    • Kad, N.M.1    Thomson, N.H.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5
  • 38
    • 0034994097 scopus 로고    scopus 로고
    • 2-microglobulin: A mechanism for the pathogenesis of dialysis associated amyloidosis
    • 2- microglobulin: a mechanism for the pathogenesis of dialysis associated amyloidosis. Amyloid 8: 94-100.
    • (2001) Amyloid , vol.8 , pp. 94-100
    • Hirakura, Y.1    Kagan, B.L.2
  • 39
    • 70349218072 scopus 로고    scopus 로고
    • Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis
    • Xue WF, Homans SW, Radford SE (2009) Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis. Protein Eng Des Sel 22: 489-496.
    • (2009) Protein Eng des Sel , vol.22 , pp. 489-496
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 40
    • 84890745009 scopus 로고    scopus 로고
    • An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior
    • Xue WF, Radford SE (2013) An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior. Biophys J 105: 2811-2819.
    • (2013) Biophys J , vol.105 , pp. 2811-2819
    • Xue, W.F.1    Radford, S.E.2
  • 41
    • 84870947924 scopus 로고    scopus 로고
    • Direct three-dimensional visualization of membrane disruption by amyloid fibrils
    • Milanesi L, Sheynis T, Xue WF, Orlova EV, Hellewell AL, et al. (2012) Direct three-dimensional visualization of membrane disruption by amyloid fibrils. PNAS 109: 20455-60.
    • (2012) PNAS , vol.109 , pp. 20455-20460
    • Milanesi, L.1    Sheynis, T.2    Xue, W.F.3    Orlova, E.V.4    Hellewell, A.L.5
  • 44
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • DOI 10.1038/32440
    • Kobayashi T, Stang E, Fang KS, de Moerloose P, Parton RG, et al. (1998) A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 392: 193-197. (Pubitemid 28162794)
    • (1998) Nature , vol.392 , Issue.6672 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    De Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 45
    • 0035042252 scopus 로고    scopus 로고
    • Localization of lysobisphosphatidic acid-rich membrane domains in late endosomes
    • DOI 10.1515/BC.2001.059
    • Kobayashi T, Startchev K, Whitney AJ, Gruenberg J (2001) Localization of lysobisphosphatidic acid-rich membrane domains in late endosomes. Biol Chem 382: 483-485. (Pubitemid 32372492)
    • (2001) Biological Chemistry , vol.382 , Issue.3 , pp. 483-485
    • Kobayashi, T.1    Startchev, K.2    Whitney, A.J.3    Gruenberg, J.4
  • 51
    • 0024039744 scopus 로고
    • Mechanism of fluorescence concentration quenching of carboxyfluorescein in liposomes - Energy-transfer to nonfluorescent dimers
    • Chen RF, Knutson JR (1988) Mechanism of fluorescence concentration quenching of carboxyfluorescein in liposomes - energy-transfer to nonfluorescent dimers. Anal Biochem 172: 61-77.
    • (1988) Anal Biochem , vol.172 , pp. 61-77
    • Chen, R.F.1    Knutson, J.R.2
  • 52
    • 24144461618 scopus 로고    scopus 로고
    • Direct visualization of membrane leakage induced by the antibiotic peptides: Maculatin, citropin, and aurein
    • DOI 10.1529/biophysj.105.066589
    • Ambroggio EE, Separovic F, Bowie JH, Fidelio GD, Bagatolli LA (2005) Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein. Biophys J 89: 1874-1881. (Pubitemid 41233542)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 1874-1881
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.H.3    Fidelio, G.D.4    Bagatolli, L.A.5
  • 54
    • 33750294048 scopus 로고    scopus 로고
    • Direct Observation of Oligomeric Species formed in the Early Stages of Amyloid Fibril Formation using Electrospray Ionisation Mass Spectrometry
    • DOI 10.1016/j.jmb.2006.08.081, PII S0022283606011399
    • Smith AM, Jahn TR, Ashcroft AE, Radford SE (2006) Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J Mol Biol 364: 9-19. (Pubitemid 44634528)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.1 , pp. 9-19
    • Smith, A.M.1    Jahn, T.R.2    Ashcroft, A.E.3    Radford, S.E.4
  • 55
    • 77950517128 scopus 로고    scopus 로고
    • Bis(monoacylglycero) phosphate and ganglioside GM1 spontaneously form small homogeneous vesicles at specific concentrations
    • Chebukati JN, Goff PC, Frederick TE, Fanucci GE (2010) Bis(monoacylglycero) phosphate and ganglioside GM1 spontaneously form small homogeneous vesicles at specific concentrations. Biochem Biophys Res Commu 394: 509-514.
    • (2010) Biochem Biophys Res Commu , vol.394 , pp. 509-514
    • Chebukati, J.N.1    Goff, P.C.2    Frederick, T.E.3    Fanucci, G.E.4
  • 56
    • 65549118370 scopus 로고    scopus 로고
    • Bis(monoacylglycero)phosphate forms stable small lamellar vesicle structures: Insights into vesicular body formation in endosomes
    • Frederick TE, Chebukati JN, Mair CE, Goff PC, Fanucci GE (2009) Bis(monoacylglycero)phosphate forms stable small lamellar vesicle structures: Insights into vesicular body formation in endosomes. Biophys J 96: 1847-1855.
    • (2009) Biophys J , vol.96 , pp. 1847-1855
    • Frederick, T.E.1    Chebukati, J.N.2    Mair, C.E.3    Goff, P.C.4    Fanucci, G.E.5
  • 57
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins - Quantitative- determination by fluorescence quenching studies
    • Eftink MR, Ghiron CA (1976) Exposure of tryptophanyl residues in proteins - quantitative-determination by fluorescence quenching studies. Biochemistry 15: 672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 58
    • 67649403750 scopus 로고    scopus 로고
    • Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: Insights on vesicle permeabilization and charge selectivity
    • Pieri L, Bucciantini M, Guasti P, Savistchenko J, Melki R, et al. (2009) Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity. Biophys J 96: 3319-3330.
    • (2009) Biophys J , vol.96 , pp. 3319-3330
    • Pieri, L.1    Bucciantini, M.2    Guasti, P.3    Savistchenko, J.4    Melki, R.5
  • 60
    • 0037031425 scopus 로고    scopus 로고
    • Ion specificity of micelles explained by ionic dispersion forces
    • DOI 10.1021/la0201220
    • Bostrom M, Williams DRM, Ninham BW (2002) Ion specificity of micelles explained by ionic dispersion forces. Langmuir 18: 6010-6014. (Pubitemid 35383322)
    • (2002) Langmuir , vol.18 , Issue.16 , pp. 6010-6014
    • Bostrom, M.1    Williams, D.R.M.2    Ninham, B.W.3
  • 61
    • 0015560502 scopus 로고
    • Long-range physical forces in biological milieu
    • Parsegia.Va (1973) Long-range physical forces in biological milieu. Annu Rev Biophys Bioeng 2: 221-255.
    • (1973) Annu Rev Biophys Bioeng , vol.2 , pp. 221-255
    • Parsegia, V.A.1
  • 62
    • 0034747216 scopus 로고    scopus 로고
    • 2H NMR-observable domains in phosphatidylserine/phosphatidylcholine lipid bilayers
    • Franzin CM, Macdonald PM (2001) Polylysine-induced H-2 NMR-observable domains in phosphatidylserine/phosphatidylcholine lipid bilayers. Biophys J 81: 3346-3362. (Pubitemid 33114393)
    • (2001) Biophysical Journal , vol.81 , Issue.6 , pp. 3346-3362
    • Franzin, C.M.1    Macdonald, P.M.2
  • 63
    • 0034077945 scopus 로고    scopus 로고
    • Effect of pH on the interfacial tension of lipid bilayer membrane
    • Petelska AD, Figaszewski ZA (2000) Effect of pH on the interfacial tension of lipid bilayer membrane. Biophys J 78: 812-817. (Pubitemid 30211838)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 812-817
    • Petelska, A.D.1    Figaszewski, Z.A.2
  • 64
    • 0016121227 scopus 로고
    • Novel stereoconfiguration in lyso-bis-phosphatidic acid of cultured BHK-cells
    • Brotheru J, Renkonen O (1974) Novel stereoconfiguration in lyso-bis-phosphatidic acid of cultured BHK-cells. Chem Phys Lipids 13: 178-182.
    • (1974) Chem Phys Lipids , vol.13 , pp. 178-182
    • Brotheru, J.1    Renkonen, O.2
  • 65
    • 77956267089 scopus 로고    scopus 로고
    • Effects of the endosomal lipid bis(monoacylglycero)phosphate on the thermotropic properties of DPPC: A H-2 NMR and spin label EPR study
    • Frederick TE, Goff PC, Mair CE, Farver RS, Long JR, et al. (2010) Effects of the endosomal lipid bis(monoacylglycero)phosphate on the thermotropic properties of DPPC: A H-2 NMR and spin label EPR study. Chem Phys Lipids 163: 703-711.
    • (2010) Chem Phys Lipids , vol.163 , pp. 703-711
    • Frederick, T.E.1    Goff, P.C.2    Mair, C.E.3    Farver, R.S.4    Long, J.R.5
  • 66
    • 0015843319 scopus 로고
    • Bis-(monoacylglyceryl)-phosphate of rat and human liver: Fatty acid composition and NMR spectroscopy
    • Wherrett JR, Huterer S (1973) Bis-(monoacylglyceryl)-phosphate of rat and human liver: fatty acid composition and NMR spectroscopy. Lipids 8: 531-533.
    • (1973) Lipids , vol.8 , pp. 531-533
    • Wherrett, J.R.1    Huterer, S.2
  • 67
    • 0018566708 scopus 로고
    • Metabolism of bis(monoacylglycero)phosphate in macrophages
    • Huterer S, Wherrett J (1979) Metabolism of bis(monoacylglycero)phosphate in macrophages. J Lipid Res 20: 966-973. (Pubitemid 10157710)
    • (1979) Journal of Lipid Research , vol.20 , Issue.8 , pp. 966-973
    • Huterer, S.1    Wherrett, J.2
  • 68
    • 0034331387 scopus 로고    scopus 로고
    • Bis(monoacylglycerol) phosphate in rat uterine stromal cells: Structural characterization and specific esterification of docosahexaenoic acid
    • Luquain C, Dolmazon R, Enderlin JM, Laugier C, Lagarde M, et al. (2000) Bis(monoacylglycerol) phosphate in rat uterine stromal cells: structural characterization and specific esterification of docosahexaenoic acid. Biochem J 351 Pt 3: 795-804.
    • (2000) Biochem J , vol.351 , Issue.PART 3 , pp. 795-804
    • Luquain, C.1    Dolmazon, R.2    Enderlin, J.M.3    Laugier, C.4    Lagarde, M.5
  • 69
    • 0016096338 scopus 로고
    • Isolation and characterisation of bisphosphatidic acid and its partially deacylated derivatives from cultured BHK-cells
    • Brotherus J, Renkonen O (1974) Isolation and characterisation of bisphosphatidic acid and its partially deacylated derivatives from cultured BHK-cells. Chem Phys Lipids 13: 11-20.
    • (1974) Chem Phys Lipids , vol.13 , pp. 11-20
    • Brotherus, J.1    Renkonen, O.2
  • 70
    • 0036027683 scopus 로고    scopus 로고
    • Cholesterol interactions with phospholipids in membranes
    • DOI 10.1016/S0163-7827(01)00020-0, PII S0163782701000200
    • Ohvo-Rekila H, Ramstedt B, Leppimaki P, Slotte JP (2002) Cholesterol interactions with phospholipids in membranes. Prog Lipid Res 41: 66-97. (Pubitemid 32998278)
    • (2002) Progress in Lipid Research , vol.41 , Issue.1 , pp. 66-97
    • Ohvo-Rekila, H.1    Ramstedt, B.2    Leppimaki, P.3    Peter, S.J.4
  • 72
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • DOI 10.1038/nrm1784, PII N1784
    • Zimmerberg J, Kozlov MM (2006) How proteins produce cellular membrane curvature. Nature Rev Mol Cell Biol 7: 9-19. (Pubitemid 43361568)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.1 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 73
    • 84861910758 scopus 로고    scopus 로고
    • Cholesterol mediates membrane curvature during fusion events
    • Ivankin A, Kuzmenko I, Gidalevitz D (2012) Cholesterol mediates membrane curvature during fusion events. Physical Rev Let 108: 238103.
    • (2012) Physical Rev Let , vol.108 , pp. 238103
    • Ivankin, A.1    Kuzmenko, I.2    Gidalevitz, D.3
  • 74
    • 84873098852 scopus 로고    scopus 로고
    • Vesicle fusion to planar membranes is enhanced by cholesterol and low temperature
    • Lee DE, Lew MG, Woodbury DJ (2013) Vesicle fusion to planar membranes is enhanced by cholesterol and low temperature. Chem Phys Lipids 166: 45-54.
    • (2013) Chem Phys Lipids , vol.166 , pp. 45-54
    • Lee, D.E.1    Lew, M.G.2    Woodbury, D.J.3
  • 75
    • 84876274935 scopus 로고    scopus 로고
    • Cytochrome c causes pore formation in cardiolipin-containing membranes
    • Bergstrom CL, Beales PA, Lv Y, Vanderlick TK, Groves JT (2013) Cytochrome c causes pore formation in cardiolipin-containing membranes. PNAS 110: 6269-6274.
    • (2013) PNAS , vol.110 , pp. 6269-6274
    • Bergstrom, C.L.1    Beales, P.A.2    Lv, Y.3    Vanderlick, T.K.4    Groves, J.T.5
  • 76
    • 70349481147 scopus 로고    scopus 로고
    • A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells
    • Cecchi C, Nichino D, Zampagni M, Bernacchioni C, Evangelisti E, et al. (2009) A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells. Biochim Biophys Acta 1788: 2204-2216.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2204-2216
    • Cecchi, C.1    Nichino, D.2    Zampagni, M.3    Bernacchioni, C.4    Evangelisti, E.5
  • 77
    • 84882936821 scopus 로고    scopus 로고
    • Embedding Abeta42 in heterogeneous membranes depends on cholesterol asymmetries
    • Liguori N, Nerenberg PS, Head-Gordon T (2013) Embedding Abeta42 in heterogeneous membranes depends on cholesterol asymmetries. Biophys J 105: 899-910.
    • (2013) Biophys J , vol.105 , pp. 899-910
    • Liguori, N.1    Nerenberg, P.S.2    Head-Gordon, T.3
  • 78
    • 84893825608 scopus 로고    scopus 로고
    • Associations between serum cholesterol levels and cerebral amyloidosis
    • Reed B, Villeneuve S, Mack W, Decarli C, Chui HC, et al. (2014) Associations between serum cholesterol levels and cerebral amyloidosis. JAMA Neurol 71: 195-200.
    • (2014) JAMA Neurol , vol.71 , pp. 195-200
    • Reed, B.1    Villeneuve, S.2    Mack, W.3    Decarli, C.4    Chui, H.C.5
  • 79
    • 84899490048 scopus 로고    scopus 로고
    • Cholesterol as a causative factor in Alzheimer's disease: A debatable hypothesis
    • Wood WG, Li L, Muller WE, Eckert GP (2014) Cholesterol as a causative factor in Alzheimer's disease: a debatable hypothesis. J Neurochem 129: 559-72.
    • (2014) J Neurochem , vol.129 , pp. 559-572
    • Wood, W.G.1    Li, L.2    Muller, W.E.3    Eckert, G.P.4
  • 81
    • 0036462411 scopus 로고    scopus 로고
    • pH homeostasis of cellular organelles
    • Demaurex N (2002) pH homeostasis of cellular organelles. News Physiol Sci 17: 1-5.
    • (2002) News Physiol Sci , vol.17 , pp. 1-5
    • Demaurex, N.1
  • 82
    • 0346850963 scopus 로고    scopus 로고
    • Abeta-mediated activation of the apoptotic cascade in cultured cortical neurones: A role for cathepsin-L
    • DOI 10.1016/S0197-4580(03)00034-4
    • Boland B, Campbell V (2004) Abeta-mediated activation of the apoptotic cascade in cultured cortical neurones: a role for cathepsin-L. Neurobiol Aging 25: 83-91. (Pubitemid 37522196)
    • (2004) Neurobiology of Aging , vol.25 , Issue.1 , pp. 83-91
    • Boland, B.1    Campbell, V.2
  • 83
    • 0035110055 scopus 로고    scopus 로고
    • Lysosomal membrane damage in soluble Abeta-mediated cell death in Alzheimer's disease
    • DOI 10.1006/nbdi.2000.0364
    • Ditaranto K, Tekirian TL, Yang AJ (2001) Lysosomal membrane damage in soluble Abeta-mediated cell death in Alzheimer's disease. Neurobio Dis 8: 19-31. (Pubitemid 32171815)
    • (2001) Neurobiology of Disease , vol.8 , Issue.1 , pp. 19-31
    • Ditaranto, K.1    Tekirian, T.L.2    Yang, A.J.3
  • 84
    • 77955841088 scopus 로고    scopus 로고
    • A role for p53 in the beta-amyloid-mediated regulation of the lysosomal system
    • Fogarty MP, McCormack RM, Noonan J, Murphy D, Gowran A, et al. (2010) A role for p53 in the beta-amyloid-mediated regulation of the lysosomal system. Neurobiol Aging 31: 1774-1786.
    • (2010) Neurobiol Aging , vol.31 , pp. 1774-1786
    • Fogarty, M.P.1    McCormack, R.M.2    Noonan, J.3    Murphy, D.4    Gowran, A.5
  • 85
    • 84876722731 scopus 로고    scopus 로고
    • Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis
    • Freeman D, Cedillos R, Choyke S, Lukic Z, McGuire K, et al. (2013) Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis. PLoS One 8: e62143.
    • (2013) PLoS One , vol.8
    • Freeman, D.1    Cedillos, R.2    Choyke, S.3    Lukic, Z.4    McGuire, K.5
  • 86
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, et al. (2008) The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nature Immunol 9: 857-865.
    • (2008) Nature Immunol , vol.9 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3    Stewart, C.R.4    Monks, B.G.5
  • 87
    • 0037077284 scopus 로고    scopus 로고
    • Apolipoprotein E4 potentiates amyloid beta peptide-induced lysosomal leakage and apoptosis in neuronal cells
    • DOI 10.1074/jbc.M112109200
    • Ji ZS, Miranda RD, Newhouse YM, Weisgraber KH, Huang Y, et al. (2002) Apolipoprotein E4 potentiates amyloid beta peptide-induced lysosomal leakage and apoptosis in neuronal cells. J Biol Chem 277: 21821-21828. (Pubitemid 34952334)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21821-21828
    • Ji, Z.-S.1    Dennis, M.R.2    Newhouse, Y.M.3    Weisgraberyadong, H.K.H.4    Mahley, R.W.5
  • 88
    • 84555187703 scopus 로고    scopus 로고
    • Visualization of co-localization in Abeta42-administered neuroblastoma cells reveals lysosome damage and autophagosome accumulation related to cell death
    • Soura V, Stewart-Parker M, Williams TL, Ratnayaka A, Atherton J, et al. (2012) Visualization of co-localization in Abeta42-administered neuroblastoma cells reveals lysosome damage and autophagosome accumulation related to cell death. Biochem J 441: 579-590.
    • (2012) Biochem J , vol.441 , pp. 579-590
    • Soura, V.1    Stewart-Parker, M.2    Williams, T.L.3    Ratnayaka, A.4    Atherton, J.5
  • 89
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • Umeda T, Tomiyama T, Sakama N, Tanaka S, Lambert MP, et al. (2011) Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo. J Neurosci Res 89: 1031-1042.
    • (2011) J Neurosci Res , vol.89 , pp. 1031-1042
    • Umeda, T.1    Tomiyama, T.2    Sakama, N.3    Tanaka, S.4    Lambert, M.P.5
  • 90
    • 80755163636 scopus 로고    scopus 로고
    • Biological function of the cellular lipid BMP-BMP as a key activator for cholesterol sorting and membrane digestion
    • Gallala HD, Sandhoff K (2011) Biological function of the cellular lipid BMP-BMP as a key activator for cholesterol sorting and membrane digestion. Neurochem Res 36: 1594-1600.
    • (2011) Neurochem Res , vol.36 , pp. 1594-1600
    • Gallala, H.D.1    Sandhoff, K.2
  • 91
    • 33846009077 scopus 로고    scopus 로고
    • pH-dependent formation of membranous cytoplasmic body-like structure of ganglioside G(M1)/bis(monoacylglycero)phosphate mixed membranes
    • Hayakawa T, Makino A, Murate M, Sugimoto I, Hashimoto Y, et al. (2007) pH-dependent formation of membranous cytoplasmic body-like structure of ganglioside G(M1)/bis(monoacylglycero)phosphate mixed membranes. Biophys J 92: L13-L15.
    • (2007) Biophys J , vol.92
    • Hayakawa, T.1    Makino, A.2    Murate, M.3    Sugimoto, I.4    Hashimoto, Y.5


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