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Volumn 1862, Issue 2, 2016, Pages 213-222

Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson peptide targeting brain gangliosides

Author keywords

Alzheimer; Amyloid pore; Calcium; Ganglioside; Ion channel; Parkinson; Synuclein; amyloid peptide

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN[1-42]; CALCIUM ION; CHIMERIC PROTEIN; GANGLIOSIDE;

EID: 84949487128     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2015.11.012     Document Type: Article
Times cited : (21)

References (82)
  • 4
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: pathogenicity and therapeutic perspectives
    • Aguzzi A., O'Connor T. Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nat. Rev. Drug Discov. 2010, 9:237-248.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 5
    • 77957782470 scopus 로고    scopus 로고
    • Biology of amyloid: structure, function, and regulation
    • Greenwald J., Riek R. Biology of amyloid: structure, function, and regulation. Structure 2010, 18:1244-1260.
    • (2010) Structure , vol.18 , pp. 1244-1260
    • Greenwald, J.1    Riek, R.2
  • 6
    • 84863988708 scopus 로고    scopus 로고
    • A molecular history of the amyloidoses
    • Buxbaum J.N., Linke R.P. A molecular history of the amyloidoses. J. Mol. Biol. 2012, 421:142-159.
    • (2012) J. Mol. Biol. , vol.421 , pp. 142-159
    • Buxbaum, J.N.1    Linke, R.P.2
  • 8
    • 3042833662 scopus 로고    scopus 로고
    • Alzheimer's disease pathogenesis and therapeutic interventions
    • Parihar M.S., Hemnani T. Alzheimer's disease pathogenesis and therapeutic interventions. J. Clin. Neurosci. 2004, 11:456-467.
    • (2004) J. Clin. Neurosci. , vol.11 , pp. 456-467
    • Parihar, M.S.1    Hemnani, T.2
  • 9
    • 84891864287 scopus 로고    scopus 로고
    • Open questions for Alzheimer's disease immunotherapy
    • Golde T.E. Open questions for Alzheimer's disease immunotherapy. Alzheimers Res. Ther. 2014, 6:3.
    • (2014) Alzheimers Res. Ther. , vol.6 , pp. 3
    • Golde, T.E.1
  • 10
    • 84893787111 scopus 로고    scopus 로고
    • Why Alzheimer trials fail: removing soluble oligomeric beta amyloid is essential, inconsistent, and difficult
    • Rosenblum W.I. Why Alzheimer trials fail: removing soluble oligomeric beta amyloid is essential, inconsistent, and difficult. Neurobiol. Aging 2014, 35:969-974.
    • (2014) Neurobiol. Aging , vol.35 , pp. 969-974
    • Rosenblum, W.I.1
  • 13
    • 0030964397 scopus 로고    scopus 로고
    • Aging and Alzheimer's disease: lessons from the Nun Study
    • Snowdon D.A. Aging and Alzheimer's disease: lessons from the Nun Study. The Gerontologist 1997, 37:150-156.
    • (1997) The Gerontologist , vol.37 , pp. 150-156
    • Snowdon, D.A.1
  • 14
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe C.G. Structural classification of toxic amyloid oligomers. J. Biolumin. Chemilumin. 2008, 283:29639-29643.
    • (2008) J. Biolumin. Chemilumin. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 15
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction
    • Mucke L., Selkoe D.J. Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction. Cold Spring Harb. Perspect. Med. 2012, 2:a006338.
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2 , pp. a006338
    • Mucke, L.1    Selkoe, D.J.2
  • 16
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - a decade of discovery
    • Walsh D.M., Selkoe D.J. A beta oligomers - a decade of discovery. J. Neurochem. 2007, 101:1172-1184.
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 17
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-beta annular protofibrils evade fibrillar fate in Alzheimer disease brain
    • Lasagna-Reeves C.A., Glabe C.G., Kayed R. Amyloid-beta annular protofibrils evade fibrillar fate in Alzheimer disease brain. J. Biolumin. Chemilumin. 2011, 286:22122-22130.
    • (2011) J. Biolumin. Chemilumin. , vol.286 , pp. 22122-22130
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 19
    • 0030966536 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid beta-protein forms Zn(2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons
    • Kawahara M., Arispe N., Kuroda Y., Rojas E. Alzheimer's disease amyloid beta-protein forms Zn(2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons. Biophys. J. 1997, 73:67-75.
    • (1997) Biophys. J. , vol.73 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 21
    • 34547203205 scopus 로고    scopus 로고
    • Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm
    • Lal R., Lin H., Quist A.P. Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm. Biochim. Biophys. Acta 2007, 1768:1966-1975.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1966-1975
    • Lal, R.1    Lin, H.2    Quist, A.P.3
  • 22
    • 84904700172 scopus 로고    scopus 로고
    • Interaction of Alzheimer's beta-amyloid peptides with cholesterol: mechanistic insights into amyloid pore formation
    • Di Scala C., Chahinian H., Yahi N., Garmy N., Fantini J. Interaction of Alzheimer's beta-amyloid peptides with cholesterol: mechanistic insights into amyloid pore formation. Biochemistry 2014, 53:4489-4502.
    • (2014) Biochemistry , vol.53 , pp. 4489-4502
    • Di Scala, C.1    Chahinian, H.2    Yahi, N.3    Garmy, N.4    Fantini, J.5
  • 23
    • 22144492630 scopus 로고    scopus 로고
    • Disruption of calcium homeostasis in the pathogenesis of Alzheimer's disease and other conformational diseases
    • Kawahara M. Disruption of calcium homeostasis in the pathogenesis of Alzheimer's disease and other conformational diseases. Curr. Alzheimer Res. 2004, 1:87-95.
    • (2004) Curr. Alzheimer Res. , vol.1 , pp. 87-95
    • Kawahara, M.1
  • 24
    • 0027374494 scopus 로고
    • A new hypothesis for the mechanism of amyloid toxicity, based on the calcium channel activity of amyloid beta protein (A beta P) in phospholipid bilayer membranes
    • Pollard H.B., Rojas E., Arispe N. A new hypothesis for the mechanism of amyloid toxicity, based on the calcium channel activity of amyloid beta protein (A beta P) in phospholipid bilayer membranes. Ann. N. Y. Acad. Sci. 1993, 695:165-168.
    • (1993) Ann. N. Y. Acad. Sci. , vol.695 , pp. 165-168
    • Pollard, H.B.1    Rojas, E.2    Arispe, N.3
  • 26
    • 79851485651 scopus 로고    scopus 로고
    • Pathological significance of ganglioside clusters in Alzheimer's disease
    • Yanagisawa K. Pathological significance of ganglioside clusters in Alzheimer's disease. J. Neurochem. 2011, 116:806-812.
    • (2011) J. Neurochem. , vol.116 , pp. 806-812
    • Yanagisawa, K.1
  • 27
    • 77956994435 scopus 로고    scopus 로고
    • Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases
    • Fantini J., Yahi N. Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases. Expert Rev. Mol. Med. 2010, 12:e27.
    • (2010) Expert Rev. Mol. Med. , vol.12 , pp. e27
    • Fantini, J.1    Yahi, N.2
  • 28
    • 42749095305 scopus 로고    scopus 로고
    • Driving force of binding of amyloid beta-protein to lipid bilayers
    • Ikeda K., Matsuzaki K. Driving force of binding of amyloid beta-protein to lipid bilayers. Biochem. Biophys. Res. Commun. 2008, 370:525-529.
    • (2008) Biochem. Biophys. Res. Commun. , vol.370 , pp. 525-529
    • Ikeda, K.1    Matsuzaki, K.2
  • 29
    • 84899068704 scopus 로고    scopus 로고
    • Soluble Abeta oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes
    • Hong S., Ostaszewski B.L., Yang T., O'Malley T.T., Jin M., Yanagisawa K., Li S., Bartels T., Selkoe D.J. Soluble Abeta oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes. Neuron 2014, 82:308-319.
    • (2014) Neuron , vol.82 , pp. 308-319
    • Hong, S.1    Ostaszewski, B.L.2    Yang, T.3    O'Malley, T.T.4    Jin, M.5    Yanagisawa, K.6    Li, S.7    Bartels, T.8    Selkoe, D.J.9
  • 31
    • 72649096531 scopus 로고    scopus 로고
    • Up-and-down topological mode of amyloid beta-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters
    • Utsumi M., Yamaguchi Y., Sasakawa H., Yamamoto N., Yanagisawa K., Kato K. Up-and-down topological mode of amyloid beta-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters. Glycoconj. J. 2009, 26:999-1006.
    • (2009) Glycoconj. J. , vol.26 , pp. 999-1006
    • Utsumi, M.1    Yamaguchi, Y.2    Sasakawa, H.3    Yamamoto, N.4    Yanagisawa, K.5    Kato, K.6
  • 32
    • 77949360652 scopus 로고    scopus 로고
    • How cholesterol constrains glycolipid conformation for optimal recognition of Alzheimer's beta amyloid peptide (Abeta1-40)
    • Yahi N., Aulas A., Fantini J. How cholesterol constrains glycolipid conformation for optimal recognition of Alzheimer's beta amyloid peptide (Abeta1-40). PLoS One 2010, 5:e9079.
    • (2010) PLoS One , vol.5 , pp. e9079
    • Yahi, N.1    Aulas, A.2    Fantini, J.3
  • 33
    • 84880168276 scopus 로고    scopus 로고
    • Binding and aggregation mechanism of amyloid beta-peptides onto the GM1 ganglioside-containing lipid membrane
    • Hoshino T., Mahmood M.I., Mori K., Matsuzaki K. Binding and aggregation mechanism of amyloid beta-peptides onto the GM1 ganglioside-containing lipid membrane. J. Phys. Chem. B 2013, 117:8085-8094.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 8085-8094
    • Hoshino, T.1    Mahmood, M.I.2    Mori, K.3    Matsuzaki, K.4
  • 34
    • 84916219015 scopus 로고    scopus 로고
    • Comparison between the aggregation of human and rodent amyloid beta-proteins in GM1 ganglioside clusters
    • Ueno H., Yamaguchi T., Fukunaga S., Okada Y., Yano Y., Hoshino M., Matsuzaki K. Comparison between the aggregation of human and rodent amyloid beta-proteins in GM1 ganglioside clusters. Biochemistry 2014, 53:7523-7530.
    • (2014) Biochemistry , vol.53 , pp. 7523-7530
    • Ueno, H.1    Yamaguchi, T.2    Fukunaga, S.3    Okada, Y.4    Yano, Y.5    Hoshino, M.6    Matsuzaki, K.7
  • 35
    • 33847022701 scopus 로고    scopus 로고
    • GM1 specifically interacts with alpha-synuclein and inhibits fibrillation
    • Martinez Z., Zhu M., Han S., Fink A.L. GM1 specifically interacts with alpha-synuclein and inhibits fibrillation. Biochemistry 2007, 46:1868-1877.
    • (2007) Biochemistry , vol.46 , pp. 1868-1877
    • Martinez, Z.1    Zhu, M.2    Han, S.3    Fink, A.L.4
  • 36
    • 79954534373 scopus 로고    scopus 로고
    • Molecular basis for the glycosphingolipid-binding specificity of alpha-synuclein: key role of tyrosine 39 in membrane insertion
    • Fantini J., Yahi N. Molecular basis for the glycosphingolipid-binding specificity of alpha-synuclein: key role of tyrosine 39 in membrane insertion. J. Mol. Biol. 2011, 408:654-669.
    • (2011) J. Mol. Biol. , vol.408 , pp. 654-669
    • Fantini, J.1    Yahi, N.2
  • 37
    • 84872356587 scopus 로고    scopus 로고
    • Ganglioside-embedding small bicelles for probing membrane-landing processes of intrinsically disordered proteins
    • Yamaguchi T., Uno T., Uekusa Y., Yagi-Utsumi M., Kato K. Ganglioside-embedding small bicelles for probing membrane-landing processes of intrinsically disordered proteins. Chem. Commun. (Camb.) 2013, 49:1235-1237.
    • (2013) Chem. Commun. (Camb.) , vol.49 , pp. 1235-1237
    • Yamaguchi, T.1    Uno, T.2    Uekusa, Y.3    Yagi-Utsumi, M.4    Kato, K.5
  • 40
    • 84929057233 scopus 로고    scopus 로고
    • Deciphering the glycolipid code of Alzheimer's and Parkinson's amyloid proteins allowed the creation of a universal ganglioside-binding Peptide
    • Yahi N., Fantini J. Deciphering the glycolipid code of Alzheimer's and Parkinson's amyloid proteins allowed the creation of a universal ganglioside-binding Peptide. PLoS One 2014, 9:e104751.
    • (2014) PLoS One , vol.9 , pp. e104751
    • Yahi, N.1    Fantini, J.2
  • 41
    • 0029670048 scopus 로고    scopus 로고
    • Zn2+ interaction with Alzheimer amyloid beta protein calcium channels
    • Arispe N., Pollard H.B., Rojas E. Zn2+ interaction with Alzheimer amyloid beta protein calcium channels. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:1710-1715.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1710-1715
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 42
    • 0001282871 scopus 로고    scopus 로고
    • Amyloid beta protein-(1-42) forms calcium-permeable, Zn2+-sensitive channel
    • Rhee S.K., Quist A.P., Lal R. Amyloid beta protein-(1-42) forms calcium-permeable, Zn2+-sensitive channel. J. Biolumin. Chemilumin. 1998, 273:13379-13382.
    • (1998) J. Biolumin. Chemilumin. , vol.273 , pp. 13379-13382
    • Rhee, S.K.1    Quist, A.P.2    Lal, R.3
  • 44
    • 0032213018 scopus 로고    scopus 로고
    • HIV-1-induced perturbations of glycosphingolipid metabolism are cell-specific and can be detected at early stages of HIV-1 infection
    • Fantini J., Tamalet C., Hammache D., Tourres C., Duclos N., Yahi N. HIV-1-induced perturbations of glycosphingolipid metabolism are cell-specific and can be detected at early stages of HIV-1 infection. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 1998, 19:221-229.
    • (1998) J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. , vol.19 , pp. 221-229
    • Fantini, J.1    Tamalet, C.2    Hammache, D.3    Tourres, C.4    Duclos, N.5    Yahi, N.6
  • 45
    • 0032502939 scopus 로고    scopus 로고
    • Modification of the Coomassie brilliant blue staining method for sphingolipids and sphingolipid synthesis inhibitors on silica gel thin-layer plate
    • Abe A. Modification of the Coomassie brilliant blue staining method for sphingolipids and sphingolipid synthesis inhibitors on silica gel thin-layer plate. Anal. Biochem. 1998, 258:149-150.
    • (1998) Anal. Biochem. , vol.258 , pp. 149-150
    • Abe, A.1
  • 46
  • 47
    • 0032466618 scopus 로고    scopus 로고
    • Interaction of the neuronal marker dye FM1-43 with lipid membranes. Thermodynamics and lipid ordering
    • Schote U., Seelig J. Interaction of the neuronal marker dye FM1-43 with lipid membranes. Thermodynamics and lipid ordering. Biochim. Biophys. Acta 1998, 1415:135-146.
    • (1998) Biochim. Biophys. Acta , vol.1415 , pp. 135-146
    • Schote, U.1    Seelig, J.2
  • 49
    • 0032488531 scopus 로고    scopus 로고
    • Human erythrocyte glycolipids promote HIV-1 envelope glycoprotein-mediated fusion of CD4+ cells
    • Puri A., Hug P., Munoz-Barroso I., Blumenthal R. Human erythrocyte glycolipids promote HIV-1 envelope glycoprotein-mediated fusion of CD4+ cells. Biochem. Biophys. Res. Commun. 1998, 242:219-225.
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 219-225
    • Puri, A.1    Hug, P.2    Munoz-Barroso, I.3    Blumenthal, R.4
  • 50
    • 0037063687 scopus 로고    scopus 로고
    • L- and d-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol (PDMP) inhibit neurite outgrowth from SH-SY5Y cells
    • Hynds D.L., Takehana A., Inokuchi J., Snow D.M. l- and d-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol (PDMP) inhibit neurite outgrowth from SH-SY5Y cells. Neuroscience 2002, 114:731-744.
    • (2002) Neuroscience , vol.114 , pp. 731-744
    • Hynds, D.L.1    Takehana, A.2    Inokuchi, J.3    Snow, D.M.4
  • 51
    • 0026658630 scopus 로고
    • Glycosylation pathways in the biosynthesis of gangliosides in melanoma and neuroblastoma cells: relative glycosyltransferase levels determine ganglioside patterns
    • Ruan S., Lloyd K.O. Glycosylation pathways in the biosynthesis of gangliosides in melanoma and neuroblastoma cells: relative glycosyltransferase levels determine ganglioside patterns. Cancer Res. 1992, 52:5725-5731.
    • (1992) Cancer Res. , vol.52 , pp. 5725-5731
    • Ruan, S.1    Lloyd, K.O.2
  • 53
    • 34047269583 scopus 로고    scopus 로고
    • GM1-ganglioside-induced Abeta assembly on synaptic membranes of cultured neurons
    • Yamamoto N., Fukata Y., Fukata M., Yanagisawa K. GM1-ganglioside-induced Abeta assembly on synaptic membranes of cultured neurons. Biochim. Biophys. Acta 2007, 1768:1128-1137.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1128-1137
    • Yamamoto, N.1    Fukata, Y.2    Fukata, M.3    Yanagisawa, K.4
  • 55
    • 84884538771 scopus 로고    scopus 로고
    • Cholesterol accelerates the binding of Alzheimer's beta-amyloid peptide to ganglioside GM1 through a universal hydrogen-bond-dependent sterol tuning of glycolipid conformation
    • Fantini J., Yahi N., Garmy N. Cholesterol accelerates the binding of Alzheimer's beta-amyloid peptide to ganglioside GM1 through a universal hydrogen-bond-dependent sterol tuning of glycolipid conformation. Front. Physiol. 2013, 4:120.
    • (2013) Front. Physiol. , vol.4 , pp. 120
    • Fantini, J.1    Yahi, N.2    Garmy, N.3
  • 56
    • 77449085703 scopus 로고    scopus 로고
    • Altered ion channel formation by the Parkinson's-disease-linked E46K mutant of alpha-synuclein is corrected by GM3 but not by GM1 gangliosides
    • Di Pasquale E., Fantini J., Chahinian H., Maresca M., Taieb N., Yahi N. Altered ion channel formation by the Parkinson's-disease-linked E46K mutant of alpha-synuclein is corrected by GM3 but not by GM1 gangliosides. J. Mol. Biol. 2010, 397:202-218.
    • (2010) J. Mol. Biol. , vol.397 , pp. 202-218
    • Di Pasquale, E.1    Fantini, J.2    Chahinian, H.3    Maresca, M.4    Taieb, N.5    Yahi, N.6
  • 57
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: amyloid pores from pathogenic mutations
    • Lashuel H.A., Hartley D., Petre B.M., Walz T., Lansbury P.T. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002, 418:291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 58
    • 84877625957 scopus 로고    scopus 로고
    • Deleterious effects of soluble amyloid-beta oligomers on multiple steps of synaptic vesicle trafficking
    • Park J., Jang M., Chang S. Deleterious effects of soluble amyloid-beta oligomers on multiple steps of synaptic vesicle trafficking. Neurobiol. Dis. 2013, 55:129-139.
    • (2013) Neurobiol. Dis. , vol.55 , pp. 129-139
    • Park, J.1    Jang, M.2    Chang, S.3
  • 59
    • 34548833278 scopus 로고    scopus 로고
    • Imaging synaptic vesicle exocytosis and endocytosis with FM dyes
    • Gaffield M.A., Betz W.J. Imaging synaptic vesicle exocytosis and endocytosis with FM dyes. Nat. Protoc. 2006, 1:2916-2921.
    • (2006) Nat. Protoc. , vol.1 , pp. 2916-2921
    • Gaffield, M.A.1    Betz, W.J.2
  • 60
    • 0030950504 scopus 로고    scopus 로고
    • Occurrence of two types of secretory vesicles in the human neuroblastoma SH-SY5Y
    • Goodall A.R., Danks K., Walker J.H., Ball S.G., Vaughan P.F. Occurrence of two types of secretory vesicles in the human neuroblastoma SH-SY5Y. J. Neurochem. 1997, 68:1542-1552.
    • (1997) J. Neurochem. , vol.68 , pp. 1542-1552
    • Goodall, A.R.1    Danks, K.2    Walker, J.H.3    Ball, S.G.4    Vaughan, P.F.5
  • 61
    • 0025777881 scopus 로고
    • Potassium- and carbachol-evoked release of [3H]noradrenaline from human neuroblastoma cells, SH-SY5Y
    • Murphy N.P., Ball S.G., Vaughan P.F. Potassium- and carbachol-evoked release of [3H]noradrenaline from human neuroblastoma cells, SH-SY5Y. J. Neurochem. 1991, 56:1810-1815.
    • (1991) J. Neurochem. , vol.56 , pp. 1810-1815
    • Murphy, N.P.1    Ball, S.G.2    Vaughan, P.F.3
  • 62
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: mechanistic insight from model systems
    • Butterfield S.M., Lashuel H.A. Amyloidogenic protein-membrane interactions: mechanistic insight from model systems. Angew. Chem. 2010, 49:5628-5654.
    • (2010) Angew. Chem. , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 63
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology
    • Lin H., Bhatia R., Lal R. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J. 2001, 15:2433-2444.
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 64
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R., Sokolov Y., Edmonds B., McIntire T.M., Milton S.C., Hall J.E., Glabe C.G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biolumin. Chemilumin. 2004, 279:46363-46366.
    • (2004) J. Biolumin. Chemilumin. , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 65
    • 34547152918 scopus 로고    scopus 로고
    • Role of gangliosides in Alzheimer's disease
    • Yanagisawa K. Role of gangliosides in Alzheimer's disease. Biochim. Biophys. Acta 2007, 1768:1943-1951.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1943-1951
    • Yanagisawa, K.1
  • 66
    • 33748513877 scopus 로고    scopus 로고
    • Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells
    • Fantini J., Garmy N., Yahi N. Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells. Biochemistry 2006, 45:10957-10962.
    • (2006) Biochemistry , vol.45 , pp. 10957-10962
    • Fantini, J.1    Garmy, N.2    Yahi, N.3
  • 67
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins
    • Mahfoud R., Garmy N., Maresca M., Yahi N., Puigserver A., Fantini J. Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins. J. Biolumin. Chemilumin. 2002, 277:11292-11296.
    • (2002) J. Biolumin. Chemilumin. , vol.277 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Puigserver, A.5    Fantini, J.6
  • 68
    • 33746925586 scopus 로고    scopus 로고
    • Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13
    • Williamson M.P., Suzuki Y., Bourne N.T., Asakura T. Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13. Biochem. J. 2006, 397:483-490.
    • (2006) Biochem. J. , vol.397 , pp. 483-490
    • Williamson, M.P.1    Suzuki, Y.2    Bourne, N.T.3    Asakura, T.4
  • 69
    • 33751076517 scopus 로고    scopus 로고
    • Histidines 13 and 14 in the Abeta sequence are targets for inhibition of Alzheimer's disease abeta ion channel and cytotoxicity
    • Diaz J.C., Linnehan J., Pollard H., Arispe N. Histidines 13 and 14 in the Abeta sequence are targets for inhibition of Alzheimer's disease abeta ion channel and cytotoxicity. Biol. Res. 2006, 39:447-460.
    • (2006) Biol. Res. , vol.39 , pp. 447-460
    • Diaz, J.C.1    Linnehan, J.2    Pollard, H.3    Arispe, N.4
  • 70
    • 84865049615 scopus 로고    scopus 로고
    • Sphingolipids: critical players in Alzheimer's disease
    • van Echten-Deckert G., Walter J. Sphingolipids: critical players in Alzheimer's disease. Prog. Lipid Res. 2012, 51:378-393.
    • (2012) Prog. Lipid Res. , vol.51 , pp. 378-393
    • van Echten-Deckert, G.1    Walter, J.2
  • 71
    • 0028099263 scopus 로고
    • Membrane lipids of adult human brain: lipid composition of frontal and temporal lobe in subjects of age 20 to 100years
    • Svennerholm L., Boström K., Jungbjer B., Olsson L. Membrane lipids of adult human brain: lipid composition of frontal and temporal lobe in subjects of age 20 to 100years. J. Neurochem. 1994, 63:1802-1811.
    • (1994) J. Neurochem. , vol.63 , pp. 1802-1811
    • Svennerholm, L.1    Boström, K.2    Jungbjer, B.3    Olsson, L.4
  • 74
    • 0023802111 scopus 로고
    • GM1 ganglioside protects nucleus basalis from excitotoxin damage: reduced cortical cholinergic losses and animal mortality
    • Mahadik S.P., Vilim F., Korenovsky A., Karpiak S.E. GM1 ganglioside protects nucleus basalis from excitotoxin damage: reduced cortical cholinergic losses and animal mortality. J. Neurosci. Res. 1988, 20:479-483.
    • (1988) J. Neurosci. Res. , vol.20 , pp. 479-483
    • Mahadik, S.P.1    Vilim, F.2    Korenovsky, A.3    Karpiak, S.E.4
  • 75
    • 79960453030 scopus 로고    scopus 로고
    • The fusogenic tilted peptide (67-78) of alpha-synuclein is a cholesterol binding domain
    • Fantini J., Carlus D., Yahi N. The fusogenic tilted peptide (67-78) of alpha-synuclein is a cholesterol binding domain. Biochim. Biophys. Acta 2011, 1808:2343-2351.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2343-2351
    • Fantini, J.1    Carlus, D.2    Yahi, N.3
  • 77
    • 0026570528 scopus 로고
    • Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 1992, 12:376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 78
    • 71549116093 scopus 로고    scopus 로고
    • Sphingolipid/cholesterol regulation of neurotransmitter receptor conformation and function
    • Fantini J., Barrantes F.J. Sphingolipid/cholesterol regulation of neurotransmitter receptor conformation and function. Biochim. Biophys. Acta 2009, 1788:2345-2361.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2345-2361
    • Fantini, J.1    Barrantes, F.J.2
  • 79
    • 85046914841 scopus 로고    scopus 로고
    • Peptide delivery to the brain via adsorptive-mediated endocytosis: advances with SynB vectors
    • Drin G., Rousselle C., Scherrmann J.M., Rees A.R., Temsamani J. Peptide delivery to the brain via adsorptive-mediated endocytosis: advances with SynB vectors. AAPS PharmSci 2002, 4:E26.
    • (2002) AAPS PharmSci , vol.4 , pp. E26
    • Drin, G.1    Rousselle, C.2    Scherrmann, J.M.3    Rees, A.R.4    Temsamani, J.5
  • 82
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • Glabe C.G. Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem. Sci. 2004, 29:542-547.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 542-547
    • Glabe, C.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.