메뉴 건너뛰기




Volumn 6, Issue NOV, 2013, Pages

Alzheimer's disease-associated peptide Aβ42 mobilizes ER Ca2+ via InsP3R-dependent and -independent mechanisms

Author keywords

A Oligomers; Alzheimer's disease; Calcium Ca2+; Endoplasmic reticulum ER; Insp3 Receptors InsP3Rs; InsP3 IP3

Indexed keywords

AMYLOID BETA PROTEIN; CALCIUM ION; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; PHOSPHOLIPASE C; RYANODINE RECEPTOR;

EID: 84888320149     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2013.00036     Document Type: Article
Times cited : (39)

References (76)
  • 1
    • 0038452658 scopus 로고    scopus 로고
    • Changes in intracellular calcium and glutathione in astrocytes as the primary mechanism of amyloid neurotoxicity
    • Abramov, A. Y., Canevari, L., and Duchen, M. R. (2003). Changes in intracellular calcium and glutathione in astrocytes as the primary mechanism of amyloid neurotoxicity. J. Neurosci. 23, 5088-5095.
    • (2003) J. Neurosci , vol.23 , pp. 5088-5095
    • Abramov, A.Y.1    Canevari, L.2    Duchen, M.R.3
  • 2
    • 1642499152 scopus 로고    scopus 로고
    • Beta-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase
    • doi: 10.1523/JNEUROSCI.4042-03.2004
    • Abramov, A. Y., Canevari, L., and Duchen, M. R. (2004a). Beta-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase. J. Neurosci. 24, 565-575. doi: 10.1523/JNEUROSCI.4042-03.2004
    • (2004) J. Neurosci , vol.24 , pp. 565-575
    • Abramov, A.Y.1    Canevari, L.2    Duchen, M.R.3
  • 3
    • 10044244916 scopus 로고    scopus 로고
    • Calcium signals induced by amyloid beta peptide and their consequences in neurons and astrocytes in culture
    • doi: 10.1016/j.bbamcr. 2004.09.006
    • Abramov, A. Y., Canevari, L., and Duchen, M. R. (2004b). Calcium signals induced by amyloid beta peptide and their consequences in neurons and astrocytes in culture. Biochim. Biophys. Acta 1742, 81-87. doi: 10.1016/j.bbamcr. 2004.09.006
    • (2004) Biochim. Biophys. Acta , vol.1742 , pp. 81-87
    • Abramov, A.Y.1    Canevari, L.2    Duchen, M.R.3
  • 4
    • 67649342203 scopus 로고    scopus 로고
    • Endoplasmic reticulum and mitochondria interplay mediates apoptotic cell death: Relevance to Parkinson's disease
    • doi: 10.1016/j.neuint.2009.04.004
    • Arduino, D. M., Esteves, A. R., Cardoso, S. M., and Oliveira, C. R. (2009). Endoplasmic reticulum and mitochondria interplay mediates apoptotic cell death: relevance to Parkinson's disease. Neurochem. Int. 55, 341-348. doi: 10.1016/j.neuint.2009.04.004
    • (2009) Neurochem. Int , vol.55 , pp. 341-348
    • Arduino, D.M.1    Esteves, A.R.2    Cardoso, S.M.3    Oliveira, C.R.4
  • 5
    • 34547214510 scopus 로고    scopus 로고
    • Abeta ion channels. Prospects for treating Alzheimer's disease with Abeta channel blockers
    • doi: 10.1016/j.bbamem.2007.03.014
    • Arispe, N., Diaz, J. C., and Simakova, O. (2007). Abeta ion channels. Prospects for treating Alzheimer's disease with Abeta channel blockers. Biochim. Biophys. Acta 1768, 1952-1965. doi: 10.1016/j.bbamem.2007.03.014
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1952-1965
    • Arispe, N.1    Diaz, J.C.2    Simakova, O.3
  • 6
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein Abeta1-40 in bilayer membranes
    • doi: 10.1073/pnas.90.22.10573
    • Arispe, N., Pollard, H. B., and Rojas, E. (1993). Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein Abeta1-40 in bilayer membranes. Proc. Natl. Acad. Sci. U.S.A. 90, 10573-10577. doi: 10.1073/pnas.90.22.10573
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 7
    • 79960882442 scopus 로고    scopus 로고
    • Intraneuronal Abeta as a trigger for neuron loss: Can this be translated into human pathology?
    • doi: 10.1042/BST0390857
    • Bayer, T. A., and Wirths, O. (2011). Intraneuronal Abeta as a trigger for neuron loss: can this be translated into human pathology? Biochem. Soc. Trans. 39, 857-861. doi: 10.1042/BST0390857
    • (2011) Biochem. Soc. Trans , vol.39 , pp. 857-861
    • Bayer, T.A.1    Wirths, O.2
  • 8
    • 77949899089 scopus 로고    scopus 로고
    • Calcium hypothesis of Alzheimer's disease
    • doi: 10.1007/s00424-009-0736-1
    • Berridge, M. J. (2010). Calcium hypothesis of Alzheimer's disease. Pflugers Arch. 459, 441-449. doi: 10.1007/s00424-009-0736-1
    • (2010) Pflugers Arch , vol.459 , pp. 441-449
    • Berridge, M.J.1
  • 9
    • 0028009714 scopus 로고
    • Caffeine-induced inhibition of inositol(1,4,5)-trisphosphate-gated calcium channels from cerebellum
    • doi: 10.1091/mbc.5.1.97
    • Bezprozvanny, I., Bezprozvannaya, S., Ehrlich, B. E. (1994). Caffeine-induced inhibition of inositol(1,4,5)-trisphosphate-gated calcium channels from cerebellum. Mol. Biol. Cell 5, 97. doi: 10.1091/mbc.5.1.97
    • (1994) Mol. Biol. Cell , vol.5 , pp. 97
    • Bezprozvanny, I.1    Bezprozvannaya, S.2    Ehrlich, B.E.3
  • 10
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • doi: 10.1016/j.tins.2008.06.005
    • Bezprozvanny, I., and Mattson, M. P. (2008). Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci. 31, 454-463. doi: 10.1016/j.tins.2008.06.005
    • (2008) Trends Neurosci , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 11
    • 5144220474 scopus 로고    scopus 로고
    • Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule
    • doi: 10.1073/pnas.0405941101
    • Blanchard, B. J., Chen, A., Rozeboom, L. M., Stafford, K. A., Weigele, P., and Ingram, V. M. (2004). Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule. Proc. Natl. Acad. Sci. U.S.A. 101, 14326-14332. doi: 10.1073/pnas.0405941101
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 14326-14332
    • Blanchard, B.J.1    Chen, A.2    Rozeboom, L.M.3    Stafford, K.A.4    Weigele, P.5    Ingram, V.M.6
  • 12
    • 3843148352 scopus 로고    scopus 로고
    • Prefibrillar amyloid protein aggregates share common features of cytotoxicity
    • doi: 10.1074/jbc.M400348200
    • Bucciantini, M., Calloni, G., Chiti, F., Formigli, L., Nosi, D., Dobson, C. M., et al. (2004). Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J. Biol. Chem. 279, 31374-31382. doi: 10.1074/jbc.M400348200
    • (2004) J. Biol. Chem , vol.279 , pp. 31374-31382
    • Bucciantini, M.1    Calloni, G.2    Chiti, F.3    Formigli, L.4    Nosi, D.5    Dobson, C.M.6
  • 13
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • doi: 10.1038/416507a
    • Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., et al. (2002). Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511. doi: 10.1038/416507a
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 14
    • 63649147251 scopus 로고    scopus 로고
    • Amyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: Resolving a controversy
    • doi: 10.1007/s12640-009-9033-1
    • Capone, R., Quiroz, F. G., Prangkio, P., Saluja, I., Sauer, A. M., Bautista, M. R., et al. (2009). Amyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: resolving a controversy. Neurotox. Res. 16, 1-13. doi: 10.1007/s12640-009-9033-1
    • (2009) Neurotox. Res , vol.16 , pp. 1-13
    • Capone, R.1    Quiroz, F.G.2    Prangkio, P.3    Saluja, I.4    Sauer, A.M.5    Bautista, M.R.6
  • 15
    • 0242424155 scopus 로고    scopus 로고
    • Self-assembly of Abeta1-42 into globular neurotoxins
    • doi: 10.1021/bi030029q
    • Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., et al. (2003). Self-assembly of Abeta1-42 into globular neurotoxins. Biochemistry 42, 12749-12760. doi: 10.1021/bi030029q
    • (2003) Biochemistry , vol.42 , pp. 12749-12760
    • Chromy, B.A.1    Nowak, R.J.2    Lambert, M.P.3    Viola, K.L.4    Chang, L.5    Velasco, P.T.6
  • 16
    • 77957326921 scopus 로고    scopus 로고
    • Oxidative stress and its implications for future treatments and management of Alzheimer disease
    • Clark, T. A., Lee, H. P., Rolston, R. K., Zhu, X., Marlatt, M. W., Castellani, R. J., et al. (2010). Oxidative stress and its implications for future treatments and management of Alzheimer disease. Int. J. Biomed. Sci. 6, 225-227.
    • (2010) Int. J. Biomed. Sci , vol.6 , pp. 225-227
    • Clark, T.A.1    Lee, H.P.2    Rolston, R.K.3    Zhu, X.4    Marlatt, M.W.5    Castellani, R.J.6
  • 17
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • doi: 10.1038/nn1372
    • Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., et al. (2005). Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat. Neurosci. 8, 79-84. doi: 10.1038/nn1372
    • (2005) Nat. Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3    Shankar, G.M.4    Kuskowski, M.A.5    Selkoe, D.J.6
  • 18
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • doi: 10.1083/jcb.200604016
    • Csordas, G., Renken, C., Varnai, P., Walter, L., Weaver, D., Buttle, K. F., et al. (2006). Structural and functional features and significance of the physical linkage between ER and mitochondria. J. Cell Biol. 174, 915-921. doi: 10.1083/jcb.200604016
    • (2006) J. Cell Biol , vol.174 , pp. 915-921
    • Csordas, G.1    Renken, C.2    Varnai, P.3    Walter, L.4    Weaver, D.5    Buttle, K.F.6
  • 19
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • doi: 10.1074/jbc.M201750200
    • Dahlgren, K. N., Manelli, A. M., Stine, W. B. Jr., Baker, L. K., Krafft, G. A., and Ladu, M. J. (2002). Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 277, 32046-32053. doi: 10.1074/jbc.M201750200
    • (2002) J. Biol. Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 20
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an NMDA receptor-dependent mechanism that is blocked by the Alzheimer's drug memantine
    • doi: 10.1074/jbc.M607483200
    • De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K. L., Fernandez, S. J., Ferreira, S. T., et al. (2007). Abeta oligomers induce neuronal oxidative stress through an NMDA receptor-dependent mechanism that is blocked by the Alzheimer's drug memantine. J. Biol. Chem. 282, 11590-11601. doi: 10.1074/jbc.M607483200
    • (2007) J. Biol. Chem , vol.282 , pp. 11590-11601
    • de Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.L.4    Fernandez, S.J.5    Ferreira, S.T.6
  • 21
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • doi: 10.1074/jbc.M500997200
    • Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., and Glabe, C. G. (2005). Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280, 17294-17300. doi: 10.1074/jbc.M500997200
    • (2005) J. Biol. Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 22
    • 84874590326 scopus 로고    scopus 로고
    • 2+ release from the endoplasmic reticulum by stimulated production of inositol trisphosphate
    • doi: 10.1523/JNEUROSCI.4367-12.2013
    • 2+ release from the endoplasmic reticulum by stimulated production of inositol trisphosphate. J. Neurosci. 33, 3824-3833. doi: 10.1523/JNEUROSCI.4367-12.2013
    • (2013) J. Neurosci , vol.33 , pp. 3824-3833
    • Demuro, A.1    Parker, I.2
  • 23
    • 77951251848 scopus 로고    scopus 로고
    • Calcium signaling and amyloid toxicity in Alzheimer disease
    • doi: 10.1074/jbc.R109.080895
    • Demuro, A., Parker, I., and Stutzmann, G. E. (2010). Calcium signaling and amyloid toxicity in Alzheimer disease. J. Biol. Chem. 285, 12463-12468. doi: 10.1074/jbc.R109.080895
    • (2010) J. Biol. Chem , vol.285 , pp. 12463-12468
    • Demuro, A.1    Parker, I.2    Stutzmann, G.E.3
  • 24
    • 84855750207 scopus 로고    scopus 로고
    • Single-channel Ca(2+) imaging implicates Aβ1-42 amyloid pores in Alzheimerandapos's disease pathology
    • doi: 10.1083/jcb.201104133
    • Demuro, A., Smith, M., and Parker, I. (2011). Single-channel Ca(2+) imaging implicates Aβ1-42 amyloid pores in Alzheimerandapos's disease pathology. J. Cell Biol. 195, 515-524. doi: 10.1083/jcb.201104133
    • (2011) J. Cell Biol , vol.195 , pp. 515-524
    • Demuro, A.1    Smith, M.2    Parker, I.3
  • 25
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • doi: 10.1038/nature02261
    • Dobson, C. M. (2003). Protein folding and misfolding. Nature 426, 884-890. doi: 10.1038/nature02261
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 26
    • 2642541799 scopus 로고    scopus 로고
    • 2+ release through ryanodine and inositol 1,4,5-triphosphate receptors in the neurotoxic effects induced by the amyloid-beta peptide
    • doi: 10.1002/jnr.20135
    • 2+ release through ryanodine and inositol 1,4,5-triphosphate receptors in the neurotoxic effects induced by the amyloid-beta peptide. J. Neurosci. Res. 76, 872-880. doi: 10.1002/jnr.20135
    • (2004) J. Neurosci. Res , vol.76 , pp. 872-880
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.3
  • 27
    • 43649083316 scopus 로고    scopus 로고
    • The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway
    • doi: 10.1016/j.nbd.2008.02.003
    • Ferreiro, E., Oliveira, C. R., and Pereira, C. M. (2008). The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway. Neurobiol. Dis. 30, 331-342. doi: 10.1016/j.nbd.2008.02.003
    • (2008) Neurobiol. Dis , vol.30 , pp. 331-342
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.M.3
  • 28
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • doi: 10.1016/j.nbd.2006.05.011
    • Ferreiro, E., Resende, R., Costa, R., Oliveira, C. R., and Pereira, C. M. (2006). An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol. Dis. 23, 669-678. doi: 10.1016/j.nbd.2006.05.011
    • (2006) Neurobiol. Dis , vol.23 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.M.5
  • 29
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Abeta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • doi: 10.1073/pnas. 1834302100
    • Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., et al. (2003). Alzheimer's disease-affected brain: presence of oligomeric Abeta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. U.S.A. 100, 10417-10422. doi: 10.1073/pnas. 1834302100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6
  • 30
    • 0029670616 scopus 로고    scopus 로고
    • Beta-amyloid peptide blocks the fast-inactivating K+ current in rat hippocampal neurons
    • doi: 10.1016/S0006-3495(96)79570-X
    • Good, T. A., Smith, D. O., and Murphy, R. M. (1996). Beta-amyloid peptide blocks the fast-inactivating K+ current in rat hippocampal neurons. Biophys. J. 70, 296-304. doi: 10.1016/S0006-3495(96)79570-X
    • (1996) Biophys. J , vol.70 , pp. 296-304
    • Good, T.A.1    Smith, D.O.2    Murphy, R.M.3
  • 31
    • 47749095383 scopus 로고    scopus 로고
    • Linking calcium to Abeta and Alzheimer's disease
    • doi: 10.1016/j.neuron.2008.07.013
    • Green, K. N., and Laferla, F. M. (2008). Linking calcium to Abeta and Alzheimer's disease. Neuron 59, 190-194. doi: 10.1016/j.neuron.2008.07.013
    • (2008) Neuron , vol.59 , pp. 190-194
    • Green, K.N.1    Laferla, F.M.2
  • 32
  • 33
    • 0030891662 scopus 로고    scopus 로고
    • Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid beta-peptide
    • doi: 10.1097/00001756-199612200-00074
    • Guo, Q., Furukawa, K., Sopher, B. L., Pham, D. G., Xie, J., Robinson, N., et al. (1996). Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid beta-peptide. Neuroreport 8, 379-383. doi: 10.1097/00001756-199612200-00074
    • (1996) Neuroreport , vol.8 , pp. 379-383
    • Guo, Q.1    Furukawa, K.2    Sopher, B.L.3    Pham, D.G.4    Xie, J.5    Robinson, N.6
  • 34
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • doi: 10.1126/science.1072994
    • Hardy, J., and Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356. doi: 10.1126/science.1072994
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 36
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • doi: 10.1016/0092-8674(93)90635-4
    • Jarrett, J. T., and Lansbury, P. T. Jr. (1993). Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058. doi: 10.1016/0092-8674(93)90635-4
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 37
    • 80051760335 scopus 로고    scopus 로고
    • In situ measurements of the formation and morphology of intracellular beta-amyloid fibrils by super-resolution fluorescence imaging
    • doi: 10.1021/ja201651w
    • Kaminski Schierle, G. S., Van De Linde, S., Erdelyi, M., Esbjorner, E. K., Klein, T., Rees, E., et al. (2011). In situ measurements of the formation and morphology of intracellular beta-amyloid fibrils by super-resolution fluorescence imaging. J. Am. Chem. Soc. 133, 12902-12905. doi: 10.1021/ja201651w
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 12902-12905
    • Kaminski, S.G.S.1    Van De Linde, S.2    Erdelyi, M.3    Esbjorner, E.K.4    Klein, T.5    Rees, E.6
  • 38
    • 22144492630 scopus 로고    scopus 로고
    • Disruption of calcium homeostasis in the pathogenesis of Alzheimer's disease and other conformational diseases
    • doi: 10.2174/1567205043332234
    • Kawahara, M. (2004). Disruption of calcium homeostasis in the pathogenesis of Alzheimer's disease and other conformational diseases. Curr. Alzheimer Res. 1, 87-95. doi: 10.2174/1567205043332234
    • (2004) Curr. Alzheimer Res , vol.1 , pp. 87-95
    • Kawahara, M.1
  • 39
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • doi: 10.1126/science.1079469
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., et al. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489. doi: 10.1126/science.1079469
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6
  • 40
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformationdependent activity of soluble amyloid oligomers in protein misfolding diseases
    • doi: 10.1074/jbc.C400260200
    • Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E., et al. (2004). Permeabilization of lipid bilayers is a common conformationdependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 279, 46363-46366. doi: 10.1074/jbc.C400260200
    • (2004) J. Biol. Chem , 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
  • 41
    • 33748792254 scopus 로고    scopus 로고
    • Beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons
    • doi: 10.1074/jbc.M605081200
    • Kelly, B. L., and Ferreira, A. (2006). beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons. J. Biol. Chem. 281, 28079-28089. doi: 10.1074/jbc.M605081200
    • (2006) J. Biol. Chem , vol.281 , pp. 28079-28089
    • Kelly, B.L.1    Ferreira, A.2
  • 42
    • 0024954067 scopus 로고
    • Calcium, membranes, aging, and Alzheimer's disease. Introduction and overview
    • doi: 10.1111/j.1749-6632.1989.tb12485.x
    • Khachaturian, Z. S. (1989). Calcium, membranes, aging, and Alzheimer's disease. Introduction and overview. Ann. N.Y. Acad. Sci. 568, 1-4. doi: 10.1111/j.1749-6632.1989.tb12485.x
    • (1989) Ann. N.Y. Acad. Sci , vol.568 , pp. 1-4
    • Khachaturian, Z.S.1
  • 43
    • 0028651951 scopus 로고
    • Calcium hypothesis of Alzheimer's disease and brain aging
    • doi: 10.1111/j.1749-6632.1994.tb44398.x
    • Khachaturian, Z. S. (1994). Calcium hypothesis of Alzheimer's disease and brain aging. Ann. N.Y. Acad. Sci. 747, 1-11. doi: 10.1111/j.1749-6632.1994.tb44398.x
    • (1994) Ann. N.Y. Acad. Sci , vol.747 , pp. 1-11
    • Khachaturian, Z.S.1
  • 44
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo
    • doi: 10.1038/nm1234
    • Klyubin, I., Walsh, D. M., Lemere, C. A., Cullen, W. K., Shankar, G. M., Betts, V., et al. (2005). Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat. Med. 11, 556-561. doi: 10.1038/nm1234
    • (2005) Nat. Med , vol.11 , pp. 556-561
    • Klyubin, I.1    Walsh, D.M.2    Lemere, C.A.3    Cullen, W.K.4    Shankar, G.M.5    Betts, V.6
  • 45
    • 79953061290 scopus 로고    scopus 로고
    • Protection against Abeta-mediated rapid disruption of synaptic plasticity and memory by memantine
    • doi: 10.1016/j.neurobiolaging.2009.04.005
    • Klyubin, I., Wang, Q., Reed, M. N., Irving, E. A., Upton, N., Hofmeister, J., et al. (2009). Protection against Abeta-mediated rapid disruption of synaptic plasticity and memory by memantine. Neurobiol. Aging 32, 614-623. doi: 10.1016/j.neurobiolaging.2009.04.005
    • (2009) Neurobiol. Aging , vol.32 , pp. 614-623
    • Klyubin, I.1    Wang, Q.2    Reed, M.N.3    Irving, E.A.4    Upton, N.5    Hofmeister, J.6
  • 46
    • 79953061290 scopus 로고    scopus 로고
    • Protection against Abeta-mediated rapid disruption of synaptic plasticity and memory by memantine
    • doi: 10.1016/j.neurobiolaging.2009.04.005
    • Klyubin, I., Wang, Q., Reed, M. N., Irving, E. A., Upton, N., Hofmeister, J., et al. (2011). Protection against Abeta-mediated rapid disruption of synaptic plasticity and memory by memantine. Neurobiol. Aging 32, 614-623. doi: 10.1016/j.neurobiolaging.2009.04.005
    • (2011) Neurobiol. Aging , vol.32 , pp. 614-623
    • Klyubin, I.1    Wang, Q.2    Reed, M.N.3    Irving, E.A.4    Upton, N.5    Hofmeister, J.6
  • 47
    • 77957785420 scopus 로고    scopus 로고
    • Neurotoxicity of Alzheimer's disease Abeta peptides is induced by small changes in the Abeta42 to Abeta40 ratio
    • doi: 10.1038/emboj.2010.211
    • Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., et al. (2010). Neurotoxicity of Alzheimer's disease Abeta peptides is induced by small changes in the Abeta42 to Abeta40 ratio. EMBO J. 29, 3408-3420. doi: 10.1038/emboj.2010.211
    • (2010) EMBO J , vol.29 , pp. 3408-3420
    • Kuperstein, I.1    Broersen, K.2    Benilova, I.3    Rozenski, J.4    Jonckheere, W.5    Debulpaep, M.6
  • 48
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • doi: 10.1073/pnas.95.11.6448
    • Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., et al. (1998). Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U.S.A. 95, 6448-6453. doi: 10.1073/pnas.95.11.6448
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 50
    • 0029921096 scopus 로고    scopus 로고
    • Molecular membrane interactions of a phospholipid metabolite. Implications for Alzheimer's disease pathophysiology
    • doi: 10.1111/j.17496632.1996.tb34447.x
    • Mason, R. P., Trumbore, M. W., and Pettegrew, J. W. (1996). Molecular membrane interactions of a phospholipid metabolite. Implications for Alzheimer's disease pathophysiology. Ann. N.Y. Acad. Sci. 777, 368-373. doi: 10.1111/j.17496632.1996.tb34447.x
    • (1996) Ann. N.Y. Acad. Sci , vol.777 , pp. 368-373
    • Mason, R.P.1    Trumbore, M.W.2    Pettegrew, J.W.3
  • 52
    • 0028987055 scopus 로고
    • Beta-Amyloid peptide decreases membrane fluidity
    • doi: 10.1016/0006-8993(94)01463-R
    • Mueller, W. E., Koch, S., Eckert, A., Hartmann, H., and Scheuer, K. (1995). beta-Amyloid peptide decreases membrane fluidity. Brain Res. 674, 133-136. doi: 10.1016/0006-8993(94)01463-R
    • (1995) Brain Res , vol.674 , pp. 133-136
    • Mueller, W.E.1    Koch, S.2    Eckert, A.3    Hartmann, H.K.4
  • 53
    • 0026073544 scopus 로고
    • Caffeine inhibits inositol trisphosphate-mediated liberation of intracellular calcium in Xenopus oocytes
    • Parker, I., and Ivorra, I. (1991). Caffeine inhibits inositol trisphosphate-mediated liberation of intracellular calcium in Xenopus oocytes. J Physiol 433, 229-240.
    • (1991) J Physiol , vol.433 , pp. 229-240
    • Parker, I.1    Ivorra, I.2
  • 54
    • 0034747316 scopus 로고    scopus 로고
    • Correlation between Abetax-40-, Abetax-42-, and Abetax-43-containing amyloid plaques and cognitive decline
    • doi: 10.1001/archneur.58.12.2025
    • Parvathy, S., Davies, P., Haroutunian, V., Purohit, D. P., Davis, K. L., Mohs, R. C., et al. (2001). Correlation between Abetax-40-, Abetax-42-, and Abetax-43-containing amyloid plaques and cognitive decline. Arch. Neurol. 58, 2025-2032. doi: 10.1001/archneur.58.12.2025
    • (2001) Arch. Neurol , vol.58 , pp. 2025-2032
    • Parvathy, S.1    Davies, P.2    Haroutunian, V.3    Purohit, D.P.4    Davis, K.L.5    Mohs, R.C.6
  • 55
    • 0038420824 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1,4,5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels
    • doi: 10.1016/S0143-4160(03)00026-5
    • Peppiatt, C. M., Collins, T. J., Mackenzie, L., Conway, S. J., Holmes, A. B., Bootman, M. D., et al. (2003). 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1,4,5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels. Cell Calcium 34, 97-108. doi: 10.1016/S0143-4160(03)00026-5
    • (2003) Cell Calcium , vol.34 , pp. 97-108
    • Peppiatt, C.M.1    Collins, T.J.2    Mackenzie, L.3    Conway, S.J.4    Holmes, A.B.5    Bootman, M.D.6
  • 56
    • 4344671140 scopus 로고    scopus 로고
    • Calmidazolium and arachidonate activate a calcium entry pathway that is distinct from store-operated calcium influx in
    • doi: 10.1042/BJ20040097
    • Peppiatt, C. M., Holmes, A. M., Seo, J. T., Bootman, M. D., Collins, T. J., McDonald, F., et al. (2004). Calmidazolium and arachidonate activate a calcium entry pathway that is distinct from store-operated calcium influx in HeLa cells. Biochem. J. 381, 929-939. doi: 10.1042/BJ20040097
    • (2004) HeLa Cells. Biochem. J , vol.381 , pp. 929-939
    • Peppiatt, C.M.1    Holmes, A.M.2    Seo, J.T.3    Bootman, M.D.4    Collins, T.J.5    McDonald, F.6
  • 57
    • 1442323991 scopus 로고    scopus 로고
    • Intraneuronal amyloid-beta1-42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death
    • doi: 10.1046/j.1471-4159.2003.02227.x
    • Pierrot, N., Ghisdal, P., Caumont, A. S., and Octave, J. N. (2004). Intraneuronal amyloid-beta1-42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death. J. Neurochem. 88, 1140-1150. doi: 10.1046/j.1471-4159.2003.02227.x
    • (2004) J. Neurochem , vol.88 , pp. 1140-1150
    • Pierrot, N.1    Ghisdal, P.2    Caumont, A.S.3    Octave, J.N.4
  • 58
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • doi: 10.1016/j.neuroscience.2008.06.036
    • Resende, R., Ferreiro, E., Pereira, C., and Resende De Oliveira, C. (2008). Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death. Neuroscience 155, 725-737. doi: 10.1016/j.neuroscience.2008.06.036
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Resende De Oliveira, C.4
  • 59
    • 36749014118 scopus 로고    scopus 로고
    • Synaptic memory mechanisms: Alzheimer's disease amyloid beta-peptide-induced dysfunction
    • doi: 10.1042/BST0351219
    • Rowan, M. J., Klyubin, I., Wang, Q., Hu, N. W., and Anwyl, R. (2007). Synaptic memory mechanisms: Alzheimer's disease amyloid beta-peptide-induced dysfunction. Biochem. Soc. Trans. 35, 1219-1223. doi: 10.1042/BST0351219
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 1219-1223
    • Rowan, M.J.1    Klyubin, I.2    Wang, Q.3    Hu, N.W.4    Anwyl, R.5
  • 60
    • 33646485088 scopus 로고    scopus 로고
    • Early and late cytotoxic effects of external application of the Alzheimer's Abeta result from the initial formation and function of Abeta ion channels
    • doi: 10.1021/bi060148g
    • Simakova, O., and Arispe, N. J. (2006). Early and late cytotoxic effects of external application of the Alzheimer's Abeta result from the initial formation and function of Abeta ion channels. Biochemistry 45, 5907-5915. doi: 10.1021/bi060148g
    • (2006) Biochemistry , vol.45 , pp. 5907-5915
    • Simakova, O.1    Arispe, N.J.2
  • 61
    • 0031007450 scopus 로고    scopus 로고
    • Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor
    • doi: 10.1093/emboj/16.11.3078
    • Sugawara, H., Kurosaki, M., Takata, M., and Kurosaki, T. (1997). Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor. EMBO J. 16, 3078-3088. doi: 10.1093/emboj/16.11.3078
    • (1997) EMBO J , vol.16 , pp. 3078-3088
    • Sugawara, H.1    Kurosaki, M.2    Takata, M.3    Kurosaki, T.4
  • 62
    • 0031665799 scopus 로고    scopus 로고
    • 2+ signalling: Problems and pitfalls
    • doi: 10.1016/S0165-6147(98)01243-7
    • 2+ signalling: problems and pitfalls. Trends Pharmacol. Sci. 19, 370-375. doi: 10.1016/S0165-6147(98)01243-7
    • (1998) Trends Pharmacol. Sci , vol.19 , pp. 370-375
    • Taylor, C.W.1    Broad, L.M.2
  • 63
    • 78751662442 scopus 로고    scopus 로고
    • The role of G protein-coupled receptors in the pathology of Alzheimer's disease
    • doi: 10.1038/nrn2977
    • Thathiah, A., and De Strooper, B. (2011). The role of G protein-coupled receptors in the pathology of Alzheimer's disease. Nat. Rev. Neurosci. 12, 73-87. doi: 10.1038/nrn2977
    • (2011) Nat. Rev. Neurosci , vol.12 , pp. 73-87
    • Thathiah, A.1    de Strooper, B.2
  • 64
    • 0027097839 scopus 로고
    • 2+ signal in mouse pancreatic acinar cells by blocking inositol trisphosphate production
    • 2+ signal in mouse pancreatic acinar cells by blocking inositol trisphosphate production. J. Biol. Chem. 267, 23467-23470.
    • (1992) J. Biol. Chem , vol.267 , pp. 23467-23470
    • Toescu, E.C.1    O'Neill, S.C.2    Petersen, O.H.3    Eisner, D.A.4
  • 65
    • 0034747253 scopus 로고    scopus 로고
    • Calcium puffs are generic InsP(3)-activated elementary calcium signals and are downregulated by prolonged hormonal stimulation to inhibit cellular calcium responses
    • Tovey, S. C., De Smet, P., Lipp, P., Thomas, D., Young, K. W., Missiaen, L., et al. (2001). Calcium puffs are generic InsP(3)-activated elementary calcium signals and are downregulated by prolonged hormonal stimulation to inhibit cellular calcium responses. J. Cell. Sci. 114, 3979-3989.
    • (2001) J. Cell. Sci , vol.114 , pp. 3979-3989
    • Tovey, S.C.1    de Smet, P.2    Lipp, P.3    Thomas, D.4    Young, K.W.5    Missiaen, L.6
  • 67
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • doi: 10.1002/jnr.22640
    • Umeda, T., Tomiyama, T., Sakama, N., Tanaka, S., Lambert, M. P., Klein, W. L., 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. doi: 10.1002/jnr.22640
    • (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    Klein, W.L.6
  • 68
    • 12944314765 scopus 로고    scopus 로고
    • Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons
    • doi: 10.1152/physrev.00004.2004
    • Verkhratsky, A. (2005). Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons. Physiol. Rev. 85, 201-279. doi: 10.1152/physrev.00004.2004
    • (2005) Physiol. Rev , vol.85 , pp. 201-279
    • Verkhratsky, A.1
  • 69
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • doi: 10.1038/416535a
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., et al. (2002). Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539. doi: 10.1038/416535a
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6
  • 70
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid betapeptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • doi: 10.1523/JNEUROSCI.1633-03.2004
    • Wang, Q., Walsh, D. M., Rowan, M. J., Selkoe, D. J., and Anwyl, R. (2004). Block of long-term potentiation by naturally secreted and synthetic amyloid betapeptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J. Neurosci. 24, 3370-3378. doi: 10.1523/JNEUROSCI.1633-03.2004
    • (2004) J. Neurosci , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 71
    • 26944437967 scopus 로고    scopus 로고
    • Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration
    • doi: 10.1016/j.nbd.2005.03.007
    • Whalen, B. M., Selkoe, D. J., and Hartley, D. M. (2005). Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration. Neurobiol. Dis. 20, 254-266. doi: 10.1016/j.nbd.2005.03.007
    • (2005) Neurobiol. Dis , vol.20 , pp. 254-266
    • Whalen, B.M.1    Selkoe, D.J.2    Hartley, D.M.3
  • 72
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: Intraneuronal accumulation of the beta-amyloid peptide-the first step of a fatal cascade
    • doi: 10.1111/j.14714159.2004.02737.x
    • Wirths, O., Multhaup, G., and Bayer, T. A. (2004). A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide-the first step of a fatal cascade. J. Neurochem. 91, 513-520. doi: 10.1111/j.14714159.2004.02737.x
    • (2004) J. Neurochem , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 73
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • doi: 10.1172/JCI26373
    • Xu, C., Bailly-Maitre, B., and Reed, J. C. (2005). Endoplasmic reticulum stress: cell life and death decisions. J. Clin. Invest. 115, 2656-2664. doi: 10.1172/JCI26373
    • (2005) J. Clin. Invest , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 74
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • doi: 10.1073/pnas.0903563106
    • Yao, J., Irwin, R. W., Zhao, L., Nilsen, J., Hamilton, R. T., and Brinton, R. D. (2009). Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 106, 14670-14675. doi: 10.1073/pnas.0903563106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 75
    • 52449103780 scopus 로고    scopus 로고
    • Amyloid oligomer conformation in a group of natively folded proteins
    • doi: 10.1371/journal.pone.0003235
    • Yoshiike, Y., Minai, R., Matsuo, Y., Chen, Y. R., Kimura, T., and Takashima, A. (2008). Amyloid oligomer conformation in a group of natively folded proteins. PLoS ONE 3:e3235. doi: 10.1371/journal.pone.0003235
    • (2008) PLoS ONE , vol.3
    • Yoshiike, Y.1    Minai, R.2    Matsuo, Y.3    Chen, Y.R.4    Kimura, T.5    Takashima, A.6
  • 76
    • 78650944520 scopus 로고    scopus 로고
    • APP processing in Alzheimer's disease
    • doi: 10.1186/1756-6606-4-3
    • Zhang, Y. W., Thompson, R., Zhang, H., and Xu, H. (2011). APP processing in Alzheimer's disease. Mol Brain 4, 3. doi: 10.1186/1756-6606-4-3
    • (2011) Mol Brain , vol.4 , pp. 3
    • Zhang, Y.W.1    Thompson, R.2    Zhang, H.3    Xu, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.