메뉴 건너뛰기




Volumn 1768, Issue 8, 2007, Pages 1952-1965

Aβ ion channels. Prospects for treating Alzheimer's disease with Aβ channel blockers

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA CHANNEL BLOCKER; AMYLOID BETA PROTEIN; BLOCKING AGENT; CALCIUM CHANNEL; ION CHANNEL; LIPOSOME; MEMBRANE RECEPTOR; PEPTIDE NA3; PEPTIDE NA7; UNCLASSIFIED DRUG; AGENTS AFFECTING WATER, MOLECULE OR ION TRANSPORT; CYTOTOXIN;

EID: 34547214510     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.03.014     Document Type: Review
Times cited : (173)

References (111)
  • 1
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid β-protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum
    • Arispe N., Rojas E., and Pollard H.B. Alzheimer disease amyloid β-protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 567-571
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 2
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson M.P. Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77 (1997) 1081-1132
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 3
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • Haass C., Schlossmacher M., Hung A.Y., et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359 (1992) 322-325
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1    Schlossmacher, M.2    Hung, A.Y.3
  • 5
    • 0032556830 scopus 로고    scopus 로고
    • A technical KO of amyloid-β peptide
    • Haass C., and Selkoe D. A technical KO of amyloid-β peptide. Nature 391 6665 (1998) 339-340
    • (1998) Nature , vol.391 , Issue.6665 , pp. 339-340
    • Haass, C.1    Selkoe, D.2
  • 6
    • 0029896354 scopus 로고    scopus 로고
    • Mechanism of neuronal degeneration in Alzheimer's disease. Review
    • Yankner B.A. Mechanism of neuronal degeneration in Alzheimer's disease. Review. Neuron 16 (1996) 921-932
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 7
    • 0034513214 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimer's disease. Is amyloid beta-protein the beginning or the end?
    • Yankner B.A. The pathogenesis of Alzheimer's disease. Is amyloid beta-protein the beginning or the end?. Ann. N. Y. Acad. Sci. 924 (2000) 26-28
    • (2000) Ann. N. Y. Acad. Sci. , vol.924 , pp. 26-28
    • Yankner, B.A.1
  • 8
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy J.A., and Higgins GA. Alzheimer's disease: the amyloid cascade hypothesis. Science 256 5054 (1992) 184-185
    • (1992) Science , vol.256 , Issue.5054 , pp. 184-185
    • Hardy, J.A.1    Higgins, GA.2
  • 9
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J.A., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 5580 (2002) 353-356
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.A.1    Selkoe, D.J.2
  • 10
    • 0024472693 scopus 로고
    • Neurotoxicity of a fragment of the amyloid precursor protein associated with Alzheimer's disease
    • Yankner B.A., Dawes L.R., Fisher S., Villa-Komaroff L., Oster-Granite M.L., and Neve R.L. Neurotoxicity of a fragment of the amyloid precursor protein associated with Alzheimer's disease. Science 245 (1989) 417-429
    • (1989) Science , vol.245 , pp. 417-429
    • Yankner, B.A.1    Dawes, L.R.2    Fisher, S.3    Villa-Komaroff, L.4    Oster-Granite, M.L.5    Neve, R.L.6
  • 11
    • 0031461082 scopus 로고    scopus 로고
    • Biology of Aβ amyloid in Alzheimer's disease
    • Wisniewski T., Ghiso J., and Frangione B. Biology of Aβ amyloid in Alzheimer's disease. Neurobiol. Dis. 4 (1997) 311-328
    • (1997) Neurobiol. Dis. , vol.4 , pp. 311-328
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 12
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
    • Seubert P., Vigo-Pelfrey C., Esch F., et al. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359 (1992) 325-327
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3
  • 13
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid β-protein by normal proteolytic processing
    • Shoji M., Golde T.E., Ghiso J., et al. Production of the Alzheimer amyloid β-protein by normal proteolytic processing. Science 258 (1992) 126-129
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1    Golde, T.E.2    Ghiso, J.3
  • 15
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid-β-peptide in the brain and cognitive decline
    • Naslund J., Haroutunian V., Mohs R., Davis K.L., Davies P., Greengard P., and Buxbaum J.D. Correlation between elevated levels of amyloid-β-peptide in the brain and cognitive decline. JAMA 283 (2000) 1571-1577
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6    Buxbaum, J.D.7
  • 16
    • 0035807829 scopus 로고    scopus 로고
    • Specific spatial learning deficits become severe with age in beta-amyloid precursor protein transgenic mice that harbor diffuse beta-amyloid deposits but do not form plaques
    • Koistinaho M., Ort M., Cimadevilla J.M., Vondrous R., Cordell B., Koistinaho J., et al. Specific spatial learning deficits become severe with age in beta-amyloid precursor protein transgenic mice that harbor diffuse beta-amyloid deposits but do not form plaques. Proc. Natl. Acad. Sci. U. S. A. 98 25 (2001) 14675-14680
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , Issue.25 , pp. 14675-14680
    • Koistinaho, M.1    Ort, M.2    Cimadevilla, J.M.3    Vondrous, R.4    Cordell, B.5    Koistinaho, J.6
  • 18
  • 19
    • 0028649480 scopus 로고
    • 2+ channels provides a mechanism for neuronal death in Alzheimer's disease
    • 2+ channels provides a mechanism for neuronal death in Alzheimer's disease. Ann. N.Y. Acad. Sci. 747 (1994) 256-266
    • (1994) Ann. N.Y. Acad. Sci. , vol.747 , pp. 256-266
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 20
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A., Mina E., Kayed R., Milton S.C., Parker I., and Glabe C.G. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Membr. Biol. 280 17 (2005) 17294-17300
    • (2005) J. Membr. Biol. , vol.280 , Issue.17 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 21
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Liberberg I., and Rydel R.E. β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12 (1992) 376-389
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Liberberg, I.5    Rydel, R.E.6
  • 23
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line
    • Kawahara M., Kuroda Y., Arispe N., and Rojas E. Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J. Biol. Chem. 275 19 (2000) 14077-14083
    • (2000) J. Biol. Chem. , vol.275 , Issue.19 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 24
    • 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. 1 (2004) 87-95
    • (2004) Curr. Alzheimer Res. , vol.1 , pp. 87-95
    • Kawahara, M.1
  • 25
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid b protein induces rapid cellular degeneration. A possible implication for calcium-uptake via AβP-channel
    • Bhathia R., Lin H., and Lal R. Fresh and globular amyloid b protein induces rapid cellular degeneration. A possible implication for calcium-uptake via AβP-channel. FASEB J. 14 9 (2000) 1233-1243
    • (2000) FASEB J. , vol.14 , Issue.9 , pp. 1233-1243
    • Bhathia, R.1    Lin, H.2    Lal, R.3
  • 26
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid β protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for A(P-channel-mediated cellular toxicity
    • Zhu Y.J., Lin H., and Lal R. Fresh and nonfibrillar amyloid β protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for A(P-channel-mediated cellular toxicity. FASEB J. 14 9 (2000) 1244-1254
    • (2000) FASEB J. , vol.14 , Issue.9 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3
  • 27
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid protein forms ion channels: implications for Alzheimer's disease pathophysiology
    • Lin H., Bhatia R., and Lal R. Amyloid protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J. 15 (2001) 2433-2444
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 28
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signaling in Alzheimer's disease
    • LaFerla F.M. Calcium dyshomeostasis and intracellular signaling in Alzheimer's disease. Nat. Rev., Neurosci. 3 (2002) 862-872
    • (2002) Nat. Rev., Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 29
    • 24644456470 scopus 로고    scopus 로고
    • Calcium dysregulation in Alzheimer's disease: recent advances gained from genetically modified animals
    • Smith I.F., Green K.N., and LaFerla F.M. Calcium dysregulation in Alzheimer's disease: recent advances gained from genetically modified animals. Cell Calcium 38 (2005) 427-437
    • (2005) Cell Calcium , vol.38 , pp. 427-437
    • Smith, I.F.1    Green, K.N.2    LaFerla, F.M.3
  • 31
    • 0025110182 scopus 로고
    • β-Amyloid increases the vulnerability of cultured cortical neurons to excitotoxic damage
    • Koh J.-Y., Yang L.L., and Cotman C.W. β-Amyloid increases the vulnerability of cultured cortical neurons to excitotoxic damage. Brain Res. 533 (1990) 315-320
    • (1990) Brain Res. , vol.533 , pp. 315-320
    • Koh, J.-Y.1    Yang, L.L.2    Cotman, C.W.3
  • 32
    • 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., and Glabe C.G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 279 45 (2004) 46363-46366
    • (2004) J. Biol. Chem. , vol.279 , Issue.45 , 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
  • 33
    • 1442351177 scopus 로고    scopus 로고
    • Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease
    • (Review)
    • Verdier Y., and Penke B. Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease. Curr. Protein Pept. Sci. 5 1 (2004) 19-31 (Review)
    • (2004) Curr. Protein Pept. Sci. , vol.5 , Issue.1 , pp. 19-31
    • Verdier, Y.1    Penke, B.2
  • 34
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease
    • (Review)
    • Verdier Y., Zarandi M., and Penke B. Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J. Pept. Sci. 10 5 (2004) 229-248 (Review)
    • (2004) J. Pept. Sci. , vol.10 , Issue.5 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 35
    • 0024990330 scopus 로고
    • Neurotropic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., and Kirschner D.A. Neurotropic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science 250 (1990) 279-282
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 36
    • 0029945024 scopus 로고    scopus 로고
    • Cellular MTT reduction distinguishes the mechanism of action of beta-amyloid from that of tachykini receptor peptides
    • Shearman M.S. Cellular MTT reduction distinguishes the mechanism of action of beta-amyloid from that of tachykini receptor peptides. Neuropeptides 30 (1996) 125-132
    • (1996) Neuropeptides , vol.30 , pp. 125-132
    • Shearman, M.S.1
  • 38
    • 0029998346 scopus 로고    scopus 로고
    • The serpin-enzyme complex receptor recognizes soluble, nontoxic amyloid-beta-peptide but not aggregated cytotoxic amyloid-beta-peptide
    • Boland K., Behrens M., Choi D., Manias K., and Perlmutter D.H. The serpin-enzyme complex receptor recognizes soluble, nontoxic amyloid-beta-peptide but not aggregated cytotoxic amyloid-beta-peptide. J. Biol. Chem. 271 (1996) 18032-18044
    • (1996) J. Biol. Chem. , vol.271 , pp. 18032-18044
    • Boland, K.1    Behrens, M.2    Choi, D.3    Manias, K.4    Perlmutter, D.H.5
  • 40
  • 41
    • 0028981561 scopus 로고
    • Neurotoxicity of Aβ amyloid protein in vitro is not altered by calcium channel blockade
    • Whitson J.S., and Appel S.H. Neurotoxicity of Aβ amyloid protein in vitro is not altered by calcium channel blockade. Neurobiol. Aging 16 (1995) 5-10
    • (1995) Neurobiol. Aging , vol.16 , pp. 5-10
    • Whitson, J.S.1    Appel, S.H.2
  • 43
    • 0032548943 scopus 로고    scopus 로고
    • Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides
    • McLaurin J., Franklin T., Fraser P.E., and Chakrabartty A. Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides. J. Biol. Chem. 273 8 (1998) 4506-4515
    • (1998) J. Biol. Chem. , vol.273 , Issue.8 , pp. 4506-4515
    • McLaurin, J.1    Franklin, T.2    Fraser, P.E.3    Chakrabartty, A.4
  • 44
    • 33751516396 scopus 로고    scopus 로고
    • Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure
    • Sokolov Y., Kozak J.A., Kayed R., Chanturiya A., Glabe C., and Hall J.E. Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure. J. Gen. Physiol. 128 (2006) 637-647
    • (2006) J. Gen. Physiol. , vol.128 , pp. 637-647
    • Sokolov, Y.1    Kozak, J.A.2    Kayed, R.3    Chanturiya, A.4    Glabe, C.5    Hall, J.E.6
  • 45
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes
    • Arispe N., Rojas E., and Pollard H.B. Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 10573-10577
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 10573-10577
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 46
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: current status
    • Kagan B.L., Hirakura Y., Azimov R., Azimova R., and Lin M.-C. The channel hypothesis of Alzheimer's disease: current status. Peptides 23 (2002) 1311-1315
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.-C.5
  • 47
    • 0033869674 scopus 로고    scopus 로고
    • Displacement currents associated with the insertion of Alzheimer disease amyloid β-peptide into planar bilayer membranes
    • Vargas J., Alarcon J.M., and Rojas E. Displacement currents associated with the insertion of Alzheimer disease amyloid β-peptide into planar bilayer membranes. Biophys. J. 79 (2000) 934-944
    • (2000) Biophys. J. , vol.79 , pp. 934-944
    • Vargas, J.1    Alarcon, J.M.2    Rojas, E.3
  • 50
    • 0028982292 scopus 로고
    • Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi E., Holzemann G., and Seelig J. Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252 5 (1995) 633-642
    • (1995) J. Mol. Biol. , vol.252 , Issue.5 , pp. 633-642
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 51
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes
    • Terzi E., Holzemann G., and Seelig J. Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes. Biochemistry 36 48 (1997) 14845-14852
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14845-14852
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 52
    • 30344445381 scopus 로고    scopus 로고
    • Ion channel formation by Alzheimer's disease amyloid β-peptide (Aβ40) in unilamellar liposomes is determined by anionic phospholipids
    • Alarcon J.M., Brito J.A., Hermosilla T., Atwater I., Mears D., and Rojas E. Ion channel formation by Alzheimer's disease amyloid β-peptide (Aβ40) in unilamellar liposomes is determined by anionic phospholipids. Peptides 27 (2006) 95-104
    • (2006) Peptides , vol.27 , pp. 95-104
    • Alarcon, J.M.1    Brito, J.A.2    Hermosilla, T.3    Atwater, I.4    Mears, D.5    Rojas, E.6
  • 53
    • 0030794309 scopus 로고    scopus 로고
    • Inhibition of the electrostatic interaction between beta-amyloid peptide and membranes prevents beta-amyloid-induced toxicity
    • Hertel C., Terzi E., Hauser N., Jakob-Rotne R., Seelig J., and Kemp J.A. Inhibition of the electrostatic interaction between beta-amyloid peptide and membranes prevents beta-amyloid-induced toxicity. Proc. Natl. Acad. Sci. U. S. A. 94 17 (1997) 9412-9416
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.17 , pp. 9412-9416
    • Hertel, C.1    Terzi, E.2    Hauser, N.3    Jakob-Rotne, R.4    Seelig, J.5    Kemp, J.A.6
  • 54
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer beta amyloid peptides with phospholipid membranes
    • McLaurin J., and Chakrabartty A. Characterization of the interactions of Alzheimer beta amyloid peptides with phospholipid membranes. Eur. J. Biochem. 245 (1997) 355-363
    • (1997) Eur. J. Biochem. , vol.245 , pp. 355-363
    • McLaurin, J.1    Chakrabartty, A.2
  • 55
    • 0034067706 scopus 로고    scopus 로고
    • Interaction of amyloid beta-protein with anionic phospholipids: possible involvement of Lys28 and C-terminus aliphatic amino acids
    • Chauhan A., Ray I., and Chauhan V.P. Interaction of amyloid beta-protein with anionic phospholipids: possible involvement of Lys28 and C-terminus aliphatic amino acids. Neurochem. Res. 25 3 (2000) 423-429
    • (2000) Neurochem. Res. , vol.25 , Issue.3 , pp. 423-429
    • Chauhan, A.1    Ray, I.2    Chauhan, V.P.3
  • 56
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's b-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • Bokvist M., Lindstrom F., Watts A., and Grobner G. Two types of Alzheimer's b-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335 (2004) 1039-1049
    • (2004) J. Mol. Biol. , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindstrom, F.2    Watts, A.3    Grobner, G.4
  • 57
    • 0035997228 scopus 로고    scopus 로고
    • Annexin 5 and apolipoprotein E2 protect against Alzheimer's Amyloid β Peptide cytotoxicity by competitive inhibition at a common phosphatidylserine interaction site
    • Lee G., Pollard H.B., and Arispe N. Annexin 5 and apolipoprotein E2 protect against Alzheimer's Amyloid β Peptide cytotoxicity by competitive inhibition at a common phosphatidylserine interaction site. Peptides 23 (2002) 1249-1263
    • (2002) Peptides , vol.23 , pp. 1249-1263
    • Lee, G.1    Pollard, H.B.2    Arispe, N.3
  • 58
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao H., Tuominen E.K., and Kinnunen P.K. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43 32 (2004) 10302-10307
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.2    Kinnunen, P.K.3
  • 59
    • 0035816709 scopus 로고    scopus 로고
    • Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid
    • Kakio A., Nishimoto S., Yanagisawa K., Kozutsumi Y., and Matsuzaki K. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 276 27 (2001) 24985-24990
    • (2001) J. Biol. Chem. , vol.276 , Issue.27 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 61
    • 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., and Ihara Y. GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease. Nat. Med. 1 10 (1995) 1062-1066
    • (1995) Nat. Med. , vol.1 , Issue.10 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 62
    • 18844428601 scopus 로고    scopus 로고
    • GM1 ganglioside and the seeding of amyloid in Alzheimer's disease: endogenous seed for Alzheimer amyloid
    • Yanagisawa K. GM1 ganglioside and the seeding of amyloid in Alzheimer's disease: endogenous seed for Alzheimer amyloid. Neuroscientist 11 3 (2005) 250-260
    • (2005) Neuroscientist , vol.11 , Issue.3 , pp. 250-260
    • Yanagisawa, K.1
  • 63
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation
    • Ji S.R., Wu Y., and Sui S.F. Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation. J. Biol. Chem. 277 8 (2002) 6273-6279
    • (2002) J. Biol. Chem. , vol.277 , Issue.8 , pp. 6273-6279
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 64
    • 2342442848 scopus 로고    scopus 로고
    • The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid β-peptide from liposomes prepared from brain membrane-like lipids
    • Tashima Y., Oe R., Lee S., Sugihara G., Chambers E.J., Takahashi M., and Yamada T. The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid β-peptide from liposomes prepared from brain membrane-like lipids. J. Biol. Chem. 279 17 (2004) 17587-17595
    • (2004) J. Biol. Chem. , vol.279 , Issue.17 , pp. 17587-17595
    • Tashima, Y.1    Oe, R.2    Lee, S.3    Sugihara, G.4    Chambers, E.J.5    Takahashi, M.6    Yamada, T.7
  • 65
    • 0031054785 scopus 로고    scopus 로고
    • The interaction between Alzheimer amyloid beta (1-40) peptide and ganglioside GM1-containing membranes
    • Choo-Smith L.-P., and Surewicz W.K. The interaction between Alzheimer amyloid beta (1-40) peptide and ganglioside GM1-containing membranes. FEBS Lett. 402 (1997) 95-98
    • (1997) FEBS Lett. , vol.402 , pp. 95-98
    • Choo-Smith, L.-P.1    Surewicz, W.K.2
  • 66
    • 0036451728 scopus 로고    scopus 로고
    • Cholesterol-dependent aggregation of amyloid beta-protein
    • Yanagisawa K., and Matsuzaki K. Cholesterol-dependent aggregation of amyloid beta-protein. Ann. N. Y. Acad. Sci. 977 (2002) 384-386
    • (2002) Ann. N. Y. Acad. Sci. , vol.977 , pp. 384-386
    • Yanagisawa, K.1    Matsuzaki, K.2
  • 68
    • 0027944284 scopus 로고
    • Theoretical models of the ion channel structure of amyloid-β-protein
    • Durrell S.R., Guy H.R., Arispe N., Rojas E., and Pollard H.B. Theoretical models of the ion channel structure of amyloid-β-protein. Biophys. J. 67 (1994) 2137-2145
    • (1994) Biophys. J. , vol.67 , pp. 2137-2145
    • Durrell, S.R.1    Guy, H.R.2    Arispe, N.3    Rojas, E.4    Pollard, H.B.5
  • 69
    • 1242269712 scopus 로고    scopus 로고
    • Architecture of the Alzheimer's AβP ion channel
    • Arispe N.J. Architecture of the Alzheimer's AβP ion channel. J. Membr. Biol. 197 1 (2004) 33-48
    • (2004) J. Membr. Biol. , vol.197 , Issue.1 , pp. 33-48
    • Arispe, N.J.1
  • 70
    • 0029670048 scopus 로고    scopus 로고
    • 2+ interaction with Alzheimer amyloid β protein calcium channels
    • 2+ interaction with Alzheimer amyloid β protein calcium channels. Proc. Natl. Acad. Sci. 93 (1996) 1710-1715
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 1710-1715
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 71
    • 0029586704 scopus 로고
    • Ion channel hypothesis for Alzheimer amyloid peptide neurotoxicity
    • Pollard H.B., Arispe N., and Rojas E. Ion channel hypothesis for Alzheimer amyloid peptide neurotoxicity. Cell. Mol. Neurobiol. 15 5 (1995) 513-526
    • (1995) Cell. Mol. Neurobiol. , vol.15 , Issue.5 , pp. 513-526
    • Pollard, H.B.1    Arispe, N.2    Rojas, E.3
  • 72
    • 0025334586 scopus 로고
    • Pursuing the structure and function of voltage-gated channels
    • Guy H.R., and Conti F. Pursuing the structure and function of voltage-gated channels. Trends Neurosci. 13 6 (1990) 201-206
    • (1990) Trends Neurosci. , vol.13 , Issue.6 , pp. 201-206
    • Guy, H.R.1    Conti, F.2
  • 73
    • 0027101951 scopus 로고
    • Modeling ion channel structure of cepropin
    • Durell S.R., Raghunathan G., and Guy H.R. Modeling ion channel structure of cepropin. Biophys. J. 63 (1992) 1623-1631
    • (1992) Biophys. J. , vol.63 , pp. 1623-1631
    • Durell, S.R.1    Raghunathan, G.2    Guy, H.R.3
  • 74
    • 0024007049 scopus 로고
    • Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes
    • Pollard H.B., and Rojas E. Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes. Proc. Natl. Acad. Sci. U. S. A. 85 9 (1988) 2974-2978
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , Issue.9 , pp. 2974-2978
    • Pollard, H.B.1    Rojas, E.2
  • 75
    • 0025160854 scopus 로고
    • Synexin (annexin VII): a cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes
    • Pollard H.B., Burns A.L., and Rojas E. Synexin (annexin VII): a cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes. J. Membr. Biol. 117 2 (1990) 101-112
    • (1990) J. Membr. Biol. , vol.117 , Issue.2 , pp. 101-112
    • Pollard, H.B.1    Burns, A.L.2    Rojas, E.3
  • 76
    • 0026399922 scopus 로고
    • Synexin. Molecular mechanism of calcium-dependent membrane fusion and voltage-dependent calcium-channel activity. Evidence in support of the "hydrophobic bridge hypothesis" for exocytotic membrane fusion
    • Pollard H.B., Rojas E., Pastor R.W., Rojas E.M., Guy H.R., and Burns A.L. Synexin. Molecular mechanism of calcium-dependent membrane fusion and voltage-dependent calcium-channel activity. Evidence in support of the "hydrophobic bridge hypothesis" for exocytotic membrane fusion. Ann. N. Y. Acad. Sci. 635 (1991) 328-351
    • (1991) Ann. N. Y. Acad. Sci. , vol.635 , pp. 328-351
    • Pollard, H.B.1    Rojas, E.2    Pastor, R.W.3    Rojas, E.M.4    Guy, H.R.5    Burns, A.L.6
  • 78
    • 0025635905 scopus 로고
    • Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes
    • Rojas E., Pollard H.B., Haigler H.T., Parra C., and Burns A.L. Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J. Biol. Chem. 265 34 (1990) 21207-21215
    • (1990) J. Biol. Chem. , vol.265 , Issue.34 , pp. 21207-21215
    • Rojas, E.1    Pollard, H.B.2    Haigler, H.T.3    Parra, C.4    Burns, A.L.5
  • 79
    • 0026578171 scopus 로고
    • Identification of annexins as calcium channels in biological membranes
    • Rojas E., Arispe N., Haigler H.T., Burns A.L., and Pollard H.B. Identification of annexins as calcium channels in biological membranes. Bone Miner. 17 2 (1992) 214-218
    • (1992) Bone Miner. , vol.17 , Issue.2 , pp. 214-218
    • Rojas, E.1    Arispe, N.2    Haigler, H.T.3    Burns, A.L.4    Pollard, H.B.5
  • 80
    • 0029792781 scopus 로고    scopus 로고
    • Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers
    • Arispe N., Rojas E., Genge B.R., Wu L.N., and Wuthier R.E. Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers. Biophys. J. 71 4 (1996) 1764-1775
    • (1996) Biophys. J. , vol.71 , Issue.4 , pp. 1764-1775
    • Arispe, N.1    Rojas, E.2    Genge, B.R.3    Wu, L.N.4    Wuthier, R.E.5
  • 81
    • 0033566369 scopus 로고    scopus 로고
    • Alzheimer amyloid beta peptide 1-42 channels: effect of solvent, pH, and congo red
    • Hirakura Y., Lin M.C., and Kagan B.L. Alzheimer amyloid beta peptide 1-42 channels: effect of solvent, pH, and congo red. J. Neurosci. Res. 57 (1999) 458-460
    • (1999) J. Neurosci. Res. , vol.57 , pp. 458-460
    • Hirakura, Y.1    Lin, M.C.2    Kagan, B.L.3
  • 82
    • 0034856924 scopus 로고    scopus 로고
    • Diversity of amyloid beta protein fragment [1-40] -formed channels
    • Kourie J.I., Henry C.L., and Farrelly P. Diversity of amyloid beta protein fragment [1-40] -formed channels. Cell. Mol. Neurobiol. 3 (2001) 255-284
    • (2001) Cell. Mol. Neurobiol. , vol.3 , pp. 255-284
    • Kourie, J.I.1    Henry, C.L.2    Farrelly, P.3
  • 83
    • 1942455221 scopus 로고    scopus 로고
    • Effects of sterols on β-amyloid peptide (AβP 1-40) channel formation and their properties in planar lipid membranes
    • Micelli S., Meleleo D., Picciarelli V., and Gallucci E. Effects of sterols on β-amyloid peptide (AβP 1-40) channel formation and their properties in planar lipid membranes. Biophys. J. 86 (2004) 2231-2237
    • (2004) Biophys. J. , vol.86 , pp. 2231-2237
    • Micelli, S.1    Meleleo, D.2    Picciarelli, V.3    Gallucci, E.4
  • 84
    • 0030966536 scopus 로고    scopus 로고
    • 2+-sensitive cation-selective channels across excited membrane patches from hypothalamic neurons
    • 2+-sensitive cation-selective channels across excited membrane patches from hypothalamic neurons. Biophys. J. 73 (1997) 67-75
    • (1997) Biophys. J. , vol.73 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 86
    • 0033600590 scopus 로고    scopus 로고
    • 2+ sensitive channels in reconstituted lipid vesicles
    • 2+ sensitive channels in reconstituted lipid vesicles. Biochemistry 38 (1999) 11189-11196
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.J.2    Lal, R.3
  • 87
    • 33845281853 scopus 로고
    • Physical properties of surfactant bilayer membranes: thermal transitions, elasticity, rigidity, cohesion and colloidal interactions
    • Evans E., and Needham D. Physical properties of surfactant bilayer membranes: thermal transitions, elasticity, rigidity, cohesion and colloidal interactions. J. Phys. Chem. 91 (1987) 4219-4228
    • (1987) J. Phys. Chem. , vol.91 , pp. 4219-4228
    • Evans, E.1    Needham, D.2
  • 88
    • 22144455300 scopus 로고    scopus 로고
    • Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide
    • Ambroggio E.E., Kim D.H., Separovic F., Barrow C.J., Barnham K.J., Bagatolli L.A., and Fidelio G.D. Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide. Biophys. J. 88 4 (2005) 2706-2713
    • (2005) Biophys. J. , vol.88 , Issue.4 , pp. 2706-2713
    • Ambroggio, E.E.1    Kim, D.H.2    Separovic, F.3    Barrow, C.J.4    Barnham, K.J.5    Bagatolli, L.A.6    Fidelio, G.D.7
  • 89
    • 0033615611 scopus 로고    scopus 로고
    • Hypoxic enhancement of quantal catecholamine secretion. Evidence for the involvement of amyloid beta-peptides
    • Taylor S.C., Batten T.C., and Peers C. Hypoxic enhancement of quantal catecholamine secretion. Evidence for the involvement of amyloid beta-peptides. J. Biol. Chem. 274 44 (1999) 31217-31222
    • (1999) J. Biol. Chem. , vol.274 , Issue.44 , pp. 31217-31222
    • Taylor, S.C.1    Batten, T.C.2    Peers, C.3
  • 90
    • 0035020810 scopus 로고    scopus 로고
    • Amyloid beta peptides mediate hypoxic augmentation of Ca(2+) channels
    • Green K.N., and Peers C. Amyloid beta peptides mediate hypoxic augmentation of Ca(2+) channels. J. Neurochem. 77 3 (2001) 953-956
    • (2001) J. Neurochem. , vol.77 , Issue.3 , pp. 953-956
    • Green, K.N.1    Peers, C.2
  • 91
    • 0024093449 scopus 로고
    • Glutamate neurotoxicity and diseases of the nervous system
    • Choi D.W. Glutamate neurotoxicity and diseases of the nervous system. Neuron 1 (1988) 623-634
    • (1988) Neuron , vol.1 , pp. 623-634
    • Choi, D.W.1
  • 92
    • 33646485088 scopus 로고    scopus 로고
    • Early and late cytotoxic effects of external application of the Alzheimer's Aβ result from the initial formation and function of ion channels
    • Simakova O., and Arispe N. Early and late cytotoxic effects of external application of the Alzheimer's Aβ result from the initial formation and function of ion channels. Biochemistry 45 (2006) 5907-5915
    • (2006) Biochemistry , vol.45 , pp. 5907-5915
    • Simakova, O.1    Arispe, N.2
  • 93
    • 33751076517 scopus 로고    scopus 로고
    • Histidines 13 and 14 in the Aβ sequence are targets for inhibition of Alzheimer's disease Aβ ion channel and cytotoxicity
    • Diaz J.C., Linnehan J., Pollard H., and Arispe N. Histidines 13 and 14 in the Aβ sequence are targets for inhibition of Alzheimer's disease Aβ ion channel and cytotoxicity. Biol. Res. 39 (2006) 447-460
    • (2006) Biol. Res. , vol.39 , pp. 447-460
    • Diaz, J.C.1    Linnehan, J.2    Pollard, H.3    Arispe, N.4
  • 95
    • 0028577208 scopus 로고
    • Immuno-histochemical evidence for apoptosis in Alzheimer's disease
    • Su J.H., Anderson A.J., Cummings B.J., and Cotman C.W. Immuno-histochemical evidence for apoptosis in Alzheimer's disease. NeuroReport 5 (1994) 2529-2533
    • (1994) NeuroReport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3    Cotman, C.W.4
  • 96
    • 0035917831 scopus 로고    scopus 로고
    • Activated caspase-3 expression in Alzheimer's and aged control brain: correlation with Alzheimer pathology
    • Su J.H., Zhao M., Anderson A.J., Srinivasan A., and Cotman C.W. Activated caspase-3 expression in Alzheimer's and aged control brain: correlation with Alzheimer pathology. Brain Res. 898 2 (2001) 350-357
    • (2001) Brain Res. , vol.898 , Issue.2 , pp. 350-357
    • Su, J.H.1    Zhao, M.2    Anderson, A.J.3    Srinivasan, A.4    Cotman, C.W.5
  • 98
    • 0035478618 scopus 로고    scopus 로고
    • Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima Y., Gotoh Y., Zieg J., Barrett T., Takano H., Flavell R., Davis R.J., Shirasaki Y., and Greenberg M.E. Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. J. Neurosci. 21 19 (2001) 7551-7560
    • (2001) J. Neurosci. , vol.21 , Issue.19 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6    Davis, R.J.7    Shirasaki, Y.8    Greenberg, M.E.9
  • 99
    • 0027166738 scopus 로고
    • Amyloid β peptides act directly on single neurons
    • Simmons M.A., and Schneider C.R. Amyloid β peptides act directly on single neurons. Neurosci. Lett. 150 (1993) 133-136
    • (1993) Neurosci. Lett. , vol.150 , pp. 133-136
    • Simmons, M.A.1    Schneider, C.R.2
  • 100
    • 0028176141 scopus 로고
    • β-amyloid increases choline conductance of PC12 cells: possible mechanism of toxicity in Alzheimer's disease
    • Galdzicki Z., Fukuyama R., Wadhwani K., Rapoport S., and Ehrenstein G. β-amyloid increases choline conductance of PC12 cells: possible mechanism of toxicity in Alzheimer's disease. Brain Res. 646 (1994) 332-336
    • (1994) Brain Res. , vol.646 , pp. 332-336
    • Galdzicki, Z.1    Fukuyama, R.2    Wadhwani, K.3    Rapoport, S.4    Ehrenstein, G.5
  • 102
    • 0028037404 scopus 로고
    • Amyloid β protein-induced irreversible current in rat cortical neurones
    • Furukawa K., Abe Y., and Akaike N. Amyloid β protein-induced irreversible current in rat cortical neurones. NeuroReport 5 (1994) 2016-2018
    • (1994) NeuroReport , vol.5 , pp. 2016-2018
    • Furukawa, K.1    Abe, Y.2    Akaike, N.3
  • 103
    • 0033808530 scopus 로고    scopus 로고
    • Amyloid peptide channels: blockade by zinc and inhibition by Congo red
    • Hirakura Y., Yiu W.W., Yamamoto A., and Kagan B.L. Amyloid peptide channels: blockade by zinc and inhibition by Congo red. Amyloid 7 (2000) 194-199
    • (2000) Amyloid , vol.7 , pp. 194-199
    • Hirakura, Y.1    Yiu, W.W.2    Yamamoto, A.3    Kagan, B.L.4
  • 104
    • 0035997224 scopus 로고    scopus 로고
    • Electrophysiologic properties of channels induced by Aβ25-35 in planar lipid bilayers
    • Lin M.-C., and Kagan B. Electrophysiologic properties of channels induced by Aβ25-35 in planar lipid bilayers. Peptides 23 7 (2002) 1215-1228
    • (2002) Peptides , vol.23 , Issue.7 , pp. 1215-1228
    • Lin, M.-C.1    Kagan, B.2
  • 107
    • 18244389436 scopus 로고    scopus 로고
    • The role of cerebral amyloid B accumulation in common forms of Alzheimer disease
    • Gandy S. The role of cerebral amyloid B accumulation in common forms of Alzheimer disease. J. Clin. Invest. 115 5 (2005) 1121-1129
    • (2005) J. Clin. Invest. , vol.115 , Issue.5 , pp. 1121-1129
    • Gandy, S.1
  • 108
    • 22144432331 scopus 로고    scopus 로고
    • S. Gandy, F.L. Heppner, Alzheimer's amyloid immunotherapy: quo vadis? http://neurology.thelancet.com vol. 4 (2005) 452-453.
  • 109
    • 29744454563 scopus 로고    scopus 로고
    • Breaking up (amyloid) is hard to do
    • Gandy S., and Heppner F.L. Breaking up (amyloid) is hard to do. PLoS Med. 2 12 (2005) e417
    • (2005) PLoS Med. , vol.2 , Issue.12
    • Gandy, S.1    Heppner, F.L.2
  • 110
    • 29644440011 scopus 로고    scopus 로고
    • Persistent amyloidosis following suppression of Aβ production in a transgenic model of Alzheimer disease
    • Jankowsky J.L., Slunt H.H., Gonzalez V., Savonenko A.V., Wen J.C., et al. Persistent amyloidosis following suppression of Aβ production in a transgenic model of Alzheimer disease. PLoS Med. 2 12 (2005) e355
    • (2005) PLoS Med. , vol.2 , Issue.12
    • Jankowsky, J.L.1    Slunt, H.H.2    Gonzalez, V.3    Savonenko, A.V.4    Wen, J.C.5
  • 111
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity
    • Geula C., Wu C.K., Saroff D., Lorenzo A., Yuan M., and Yankner B.A. Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity. Nat. Med. 4 7 (1998) 827-831
    • (1998) Nat. Med. , vol.4 , Issue.7 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.