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Volumn 6, Issue 12, 2015, Pages 1972-1980

Soluble Prion Protein Binds Isolated Low Molecular Weight Amyloid-β Oligomers Causing Cytotoxicity Inhibition

Author keywords

Alzheimer's disease; Amyloid ; Neurotoxicity; Oligomers; Prion Protein

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; OLIGOMER; RECOMBINANT PRION PROTEIN; RECOMBINANT PROTEIN; TETRAMER; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; CALCEIN; FLUORESCEIN DERIVATIVE; LACTATE DEHYDROGENASE; PRION; PROTEIN BINDING;

EID: 84950301397     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/acschemneuro.5b00229     Document Type: Article
Times cited : (19)

References (59)
  • 1
    • 84857642949 scopus 로고    scopus 로고
    • The toxic A beta oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic A beta oligomer and Alzheimer's disease: an emperor in need of clothes Nat. Neurosci. 15, 349-357 10.1038/nn.3028
    • (2012) Nat. Neurosci. , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • 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 10.1126/science.1072994
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 4
    • 45449091418 scopus 로고    scopus 로고
    • Amyloidogenesis of natively unfolded proteins
    • Uversky, V. N. (2008) Amyloidogenesis of natively unfolded proteins Curr. Alzheimer Res. 5, 260-287 10.2174/156720508784533312
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 260-287
    • Uversky, V.N.1
  • 5
    • 0028172886 scopus 로고
    • Beta-Amyloid Neurotoxicity Requires Fibril Formation and Is Inhibited by Congo Red
    • Lorenzo, A. and Yankner, B. A. (1994) Beta-Amyloid Neurotoxicity Requires Fibril Formation and Is Inhibited by Congo Red Proc. Natl. Acad. Sci. U. S. A. 91, 12243-12247 10.1073/pnas.91.25.12243
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 6
    • 0027490070 scopus 로고
    • The lack of accumulation of senile plaques or amyloid burden in Alzheimer's disease suggests a dynamic balance between amyloid deposition and resolution
    • Hyman, B. T., Marzloff, K., and Arriagada, P. V. (1993) The lack of accumulation of senile plaques or amyloid burden in Alzheimer's disease suggests a dynamic balance between amyloid deposition and resolution J. Neuropathol. Exp. Neurol. 52, 594-600 10.1097/00005072-199311000-00006
    • (1993) J. Neuropathol. Exp. Neurol. , vol.52 , pp. 594-600
    • Hyman, B.T.1    Marzloff, K.2    Arriagada, P.V.3
  • 8
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., and Selkoe, D. J. (2006) Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: a potent role for trimers J. Physiol. 572, 477-492 10.1113/jphysiol.2005.103754
    • (2006) J. Physiol. , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 9
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo Nature 416, 535-539 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    Rowan, M.J.7    Selkoe, D.J.8
  • 10
    • 84930642322 scopus 로고    scopus 로고
    • Effects of Aβ exposure on long-term associative memory and its neuronal mechanisms in a defined neuronal network
    • Ford, L., Crossley, M., Williams, T. L., Thorpe, J. R., Serpell, L. C., and Kemenes, G. (2015) Effects of Aβ exposure on long-term associative memory and its neuronal mechanisms in a defined neuronal network Sci. Rep. 5, 10614 10.1038/srep10614
    • (2015) Sci. Rep. , vol.5 , pp. 10614
    • Ford, L.1    Crossley, M.2    Williams, T.L.3    Thorpe, J.R.4    Serpell, L.C.5    Kemenes, G.6
  • 11
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande, A., Mina, E., Glabe, C., and Busciglio, J. (2006) Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons J. Neurosci. 26, 6011-6018 10.1523/JNEUROSCI.1189-06.2006
    • (2006) J. Neurosci. , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 12
    • 78650331032 scopus 로고    scopus 로고
    • The effect of Alzheimer's Abeta aggregation state on the permeation of biomimetic lipid vesicles
    • Williams, T. L., Day, I. J., and Serpell, L. C. (2010) The effect of Alzheimer's Abeta aggregation state on the permeation of biomimetic lipid vesicles Langmuir 26, 17260-17268 10.1021/la101581g
    • (2010) Langmuir , vol.26 , pp. 17260-17268
    • Williams, T.L.1    Day, I.J.2    Serpell, L.C.3
  • 13
    • 80053589341 scopus 로고    scopus 로고
    • Membrane and surface interactions of Alzheimer's Abeta peptide - Insights into the mechanism of cytotoxicity
    • Williams, T. L. and Serpell, L. C. (2011) Membrane and surface interactions of Alzheimer's Abeta peptide - insights into the mechanism of cytotoxicity FEBS J. 278, 3905-3917 10.1111/j.1742-4658.2011.08228.x
    • (2011) FEBS J. , vol.278 , pp. 3905-3917
    • Williams, T.L.1    Serpell, L.C.2
  • 16
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., and Strittmatter, S. M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers Nature 457, 1128-1132 10.1038/nature07761
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 18
    • 84863011560 scopus 로고    scopus 로고
    • Cellular prion protein is essential for oligomeric amyloid-beta-induced neuronal cell death
    • Kudo, W., Lee, H. P., Zou, W. Q., Wang, X., Perry, G., Zhu, X., Smith, M. A., Petersen, R. B., and Lee, H. G. (2012) Cellular prion protein is essential for oligomeric amyloid-beta-induced neuronal cell death Hum. Mol. Genet. 21, 1138-1144 10.1093/hmg/ddr542
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1138-1144
    • Kudo, W.1    Lee, H.P.2    Zou, W.Q.3    Wang, X.4    Perry, G.5    Zhu, X.6    Smith, M.A.7    Petersen, R.B.8    Lee, H.G.9
  • 23
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-β
    • Kessels, H. W., Nguyen, L. N., Nabavi, S., and Malinow, R. (2010) The prion protein as a receptor for amyloid-β Nature 466, E3 10.1038/nature09217
    • (2010) Nature , vol.466 , pp. E3
    • Kessels, H.W.1    Nguyen, L.N.2    Nabavi, S.3    Malinow, R.4
  • 26
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-beta (Abeta) oligomers: Role of N-terminal residues
    • Chen, S., Yadav, S. P., and Surewicz, W. K. (2010) Interaction between human prion protein and amyloid-beta (Abeta) oligomers: role OF N-terminal residues J. Biol. Chem. 285, 26377-26383 10.1074/jbc.M110.145516
    • (2010) J. Biol. Chem. , vol.285 , pp. 26377-26383
    • Chen, S.1    Yadav, S.P.2    Surewicz, W.K.3
  • 28
    • 84866930442 scopus 로고    scopus 로고
    • Soluble prion protein inhibits amyloid-beta (Abeta) fibrillization and toxicity
    • Nieznanski, K., Choi, J. K., Chen, S., Surewicz, K., and Surewicz, W. K. (2012) Soluble prion protein inhibits amyloid-beta (Abeta) fibrillization and toxicity J. Biol. Chem. 287, 33104-33108 10.1074/jbc.C112.400614
    • (2012) J. Biol. Chem. , vol.287 , pp. 33104-33108
    • Nieznanski, K.1    Choi, J.K.2    Chen, S.3    Surewicz, K.4    Surewicz, W.K.5
  • 29
    • 84877144645 scopus 로고    scopus 로고
    • The cellular prion protein traps Alzheimer's Abeta in an oligomeric form and disassembles amyloid fibers
    • Younan, N. D., Sarell, C. J., Davies, P., Brown, D. R., and Viles, J. H. (2013) The cellular prion protein traps Alzheimer's Abeta in an oligomeric form and disassembles amyloid fibers FASEB J. 27, 1847-1858 10.1096/fj.12-222588
    • (2013) FASEB J. , vol.27 , pp. 1847-1858
    • Younan, N.D.1    Sarell, C.J.2    Davies, P.3    Brown, D.R.4    Viles, J.H.5
  • 31
    • 80055101575 scopus 로고    scopus 로고
    • Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides
    • Rahimi, F., Maiti, P., and Bitan, G. (2009) Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides J. Visualized Exp. e1071 10.3791/1071
    • (2009) J. Visualized Exp. , pp. e1071
    • Rahimi, F.1    Maiti, P.2    Bitan, G.3
  • 32
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • Fancy, D. A. and Kodadek, T. (1999) Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light Proc. Natl. Acad. Sci. U. S. A. 96, 6020-6024 10.1073/pnas.96.11.6020
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 33
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid beta-protein oligomers
    • Ono, K., Condron, M. M., and Teplow, D. B. (2009) Structure-neurotoxicity relationships of amyloid beta-protein oligomers Proc. Natl. Acad. Sci. U. S. A. 106, 14745-14750 10.1073/pnas.0905127106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 35
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., and Klein, W. L. (2003) Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss Proc. Natl. Acad. Sci. U. S. A. 100, 10417-10422 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    Krafft, G.A.7    Klein, W.L.8
  • 37
    • 84875503806 scopus 로고    scopus 로고
    • Cellular prion protein and Alzheimer disease: Link to oligomeric amyloid-beta and neuronal cell death
    • Kudo, W., Petersen, R. B., and Lee, H. G. (2013) Cellular prion protein and Alzheimer disease: link to oligomeric amyloid-beta and neuronal cell death Prion 7, 114-116 10.4161/pri.22848
    • (2013) Prion , vol.7 , pp. 114-116
    • Kudo, W.1    Petersen, R.B.2    Lee, H.G.3
  • 38
    • 58149339635 scopus 로고    scopus 로고
    • Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity
    • Hung, L. W., Ciccotosto, G. D., Giannakis, E., Tew, D. J., Perez, K., Masters, C. L., Cappai, R., Wade, J. D., and Barnham, K. J. (2008) Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity J. Neurosci. 28, 11950-11958 10.1523/JNEUROSCI.3916-08.2008
    • (2008) J. Neurosci. , vol.28 , pp. 11950-11958
    • Hung, L.W.1    Ciccotosto, G.D.2    Giannakis, E.3    Tew, D.J.4    Perez, K.5    Masters, C.L.6    Cappai, R.7    Wade, J.D.8    Barnham, K.J.9
  • 40
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., and Selkoe, D. J. (2006) Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers J. Physiol. 572, 477-492 10.1113/jphysiol.2005.103754
    • (2006) J. Physiol. , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 42
    • 77950219248 scopus 로고    scopus 로고
    • Elucidation of amyloid beta-protein oligomerization mechanisms: Discrete molecular dynamics study
    • Urbanc, B., Betnel, M., Cruz, L., Bitan, G., and Teplow, D. B. (2010) Elucidation of amyloid beta-protein oligomerization mechanisms: discrete molecular dynamics study J. Am. Chem. Soc. 132, 4266-4280 10.1021/ja9096303
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4266-4280
    • Urbanc, B.1    Betnel, M.2    Cruz, L.3    Bitan, G.4    Teplow, D.B.5
  • 43
    • 84859605341 scopus 로고    scopus 로고
    • Dimer formation enhances structural differences between amyloid beta-protein (1-40) and (1-42): An explicit-solvent molecular dynamics study
    • Barz, B. and Urbanc, B. (2012) Dimer formation enhances structural differences between amyloid beta-protein (1-40) and (1-42): an explicit-solvent molecular dynamics study PLoS One 7, e34345 10.1371/journal.pone.0034345
    • (2012) PLoS One , vol.7 , pp. e34345
    • Barz, B.1    Urbanc, B.2
  • 45
    • 34250326780 scopus 로고    scopus 로고
    • Role of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: A discrete molecular dynamics study
    • Yun, S., Urbanc, B., Cruz, L., Bitan, G., Teplow, D. B., and Stanley, H. E. (2007) Role of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: a discrete molecular dynamics study Biophys. J. 92, 4064-4077 10.1529/biophysj.106.097766
    • (2007) Biophys. J. , vol.92 , pp. 4064-4077
    • Yun, S.1    Urbanc, B.2    Cruz, L.3    Bitan, G.4    Teplow, D.B.5    Stanley, H.E.6
  • 47
    • 0242412140 scopus 로고    scopus 로고
    • Plasma A[beta]40 and A[beta]42 and Alzheimer's disease: Relation to age, mortality, and risk
    • Mayeux, R., Honig, L. S., Tang, M. X., Manly, J., Stern, Y., Schupf, N., and Mehta, P. D. (2003) Plasma A[beta]40 and A[beta]42 and Alzheimer's disease: relation to age, mortality, and risk Neurology 61, 1185-1190 10.1212/01.WNL.0000091890.32140.8F
    • (2003) Neurology , vol.61 , pp. 1185-1190
    • Mayeux, R.1    Honig, L.S.2    Tang, M.X.3    Manly, J.4    Stern, Y.5    Schupf, N.6    Mehta, P.D.7
  • 48
    • 77955862738 scopus 로고    scopus 로고
    • Amyloid peptide pores and the beta sheet conformation
    • Kagan, B. L. and Thundimadathil, J. (2010) Amyloid peptide pores and the beta sheet conformation Adv. Exp. Med. Biol. 677, 150-167 10.1007/978-1-4419-6327-7
    • (2010) Adv. Exp. Med. Biol. , vol.677 , pp. 150-167
    • Kagan, B.L.1    Thundimadathil, J.2
  • 49
    • 34548788549 scopus 로고    scopus 로고
    • Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • Jang, H., Zheng, J., and Nussinov, R. (2007) Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process Biophys. J. 93, 1938-1949 10.1529/biophysj.107.110148
    • (2007) Biophys. J. , vol.93 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 50
    • 78649529340 scopus 로고    scopus 로고
    • Beta-Barrel topology of Alzheimer's beta-amyloid ion channels
    • Jang, H., Arce, F. T., Ramachandran, S., Capone, R., Lal, R., and Nussinov, R. (2010) beta-Barrel topology of Alzheimer's beta-amyloid ion channels J. Mol. Biol. 404, 917-934 10.1016/j.jmb.2010.10.025
    • (2010) J. Mol. Biol. , vol.404 , pp. 917-934
    • Jang, H.1    Arce, F.T.2    Ramachandran, S.3    Capone, R.4    Lal, R.5    Nussinov, R.6
  • 51
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., and Selkoe, D. J. (2011) Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration Proc. Natl. Acad. Sci. U. S. A. 108, 5819-5824 10.1073/pnas.1017033108
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 53
    • 77954927651 scopus 로고    scopus 로고
    • Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity
    • Ono, K., Condron, M. M., and Teplow, D. B. (2010) Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity J. Biol. Chem. 285, 23186-23197 10.1074/jbc.M109.086496
    • (2010) J. Biol. Chem. , vol.285 , pp. 23186-23197
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 54
    • 84903860334 scopus 로고    scopus 로고
    • Role of N-terminal residues in Abeta interactions with integrin receptor and cell surface
    • Venkatasubramaniam, A., Drude, A., and Good, T. (2014) Role of N-terminal residues in Abeta interactions with integrin receptor and cell surface Biochim. Biophys. Acta, Biomembr. 1838, 2568-2577 10.1016/j.bbamem.2014.06.011
    • (2014) Biochim. Biophys. Acta, Biomembr. , vol.1838 , pp. 2568-2577
    • Venkatasubramaniam, A.1    Drude, A.2    Good, T.3
  • 55
    • 84878245350 scopus 로고    scopus 로고
    • Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid beta-protein
    • Meral, D. and Urbanc, B. (2013) Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid beta-protein J. Mol. Biol. 425, 2260-2275 10.1016/j.jmb.2013.03.010
    • (2013) J. Mol. Biol. , vol.425 , pp. 2260-2275
    • Meral, D.1    Urbanc, B.2
  • 56
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W. K. (1999) Membrane environment alters the conformational structure of the recombinant human prion protein J. Biol. Chem. 274, 36859-36865 10.1074/jbc.274.52.36859
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 58
    • 84938632487 scopus 로고    scopus 로고
    • Heme Stabilization of alpha-Synuclein Oligomers during Amyloid Fibril Formation
    • Hayden, E. Y., Kaur, P., Williams, T. L., Matsui, H., Yeh, S. R., and Rousseau, D. L. (2015) Heme Stabilization of alpha-Synuclein Oligomers during Amyloid Fibril Formation Biochemistry 54, 4599-4610 10.1021/acs.biochem.5b00280
    • (2015) Biochemistry , vol.54 , pp. 4599-4610
    • Hayden, E.Y.1    Kaur, P.2    Williams, T.L.3    Matsui, H.4    Yeh, S.R.5    Rousseau, D.L.6
  • 59
    • 4444223736 scopus 로고    scopus 로고
    • Effect of extracellular acid-base disturbances on the intracellular pH of neurones cultured from rat medullary raphe or hippocampus
    • Bouyer, P., Bradley, S. R., Zhao, J., Wang, W., Richerson, G. B., and Boron, W. F. (2004) Effect of extracellular acid-base disturbances on the intracellular pH of neurones cultured from rat medullary raphe or hippocampus J. Physiol. 559, 85-101 10.1113/jphysiol.2004.067793
    • (2004) J. Physiol. , vol.559 , pp. 85-101
    • Bouyer, P.1    Bradley, S.R.2    Zhao, J.3    Wang, W.4    Richerson, G.B.5    Boron, W.F.6


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