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Volumn 30, Issue 32, 2014, Pages 9789-9796

Insight into the inhibition effect of acidulated serum albumin on amyloid β-protein fibrillogenesis and cytotoxicity

Author keywords

[No Author keywords available]

Indexed keywords

BODY FLUIDS; CYTOTOXICITY; GLYCOPROTEINS; NEURODEGENERATIVE DISEASES;

EID: 84906224657     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la5025197     Document Type: Article
Times cited : (38)

References (57)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimers disease: Genes, proteins, and therapy
    • Selkoe, D. J. Alzheimers disease: genes, proteins, and therapy Physiol. Rev. 2001, 81, 26
    • (2001) Physiol. Rev. , vol.81 , pp. 26
    • Selkoe, D.J.1
  • 2
    • 84888359848 scopus 로고    scopus 로고
    • Omega-3 fatty acids regulate the interaction of the Alzheimers abeta(25-35) peptide with lipid membranes
    • Vitiello, G.; Di Marino, S.; DUrsi, A. M.; DErrico, G. Omega-3 fatty acids regulate the interaction of the Alzheimers abeta(25-35) peptide with lipid membranes Langmuir 2013, 29, 14239-14245
    • (2013) Langmuir , vol.29 , pp. 14239-14245
    • Vitiello, G.1    Di Marino, S.2    Dursi, A.M.3    Derrico, G.4
  • 3
    • 70349923038 scopus 로고    scopus 로고
    • Alzheimers disease: From pathology to therapeutic approaches
    • Jakob-Roetne, R.; Jacobsen, H. Alzheimers disease: from pathology to therapeutic approaches Angew. Chem., Int. Ed. 2009, 48, 3030-3059
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 3030-3059
    • Jakob-Roetne, R.1    Jacobsen, H.2
  • 5
    • 84864273268 scopus 로고    scopus 로고
    • PEGylated nanoparticles bind to and alter amyloid-beta peptide conformation: Toward engineering of functional nanomedicines for Alzheimers disease
    • Brambilla, D. PEGylated nanoparticles bind to and alter amyloid-beta peptide conformation: toward engineering of functional nanomedicines for Alzheimers disease ACS Nano 2012, 6, 5897-5908
    • (2012) ACS Nano , vol.6 , pp. 5897-5908
    • Brambilla, D.1
  • 6
    • 84884263393 scopus 로고    scopus 로고
    • Membrane-mediated neuroprotection by curcumin from amyloid-beta-peptide- induced toxicity
    • Thapa, A.; Vernon, B. C.; De la Pena, K.; Soliz, G.; Moreno, H. A.; Lopez, G. P.; Chi, E. Y. Membrane-mediated neuroprotection by curcumin from amyloid-beta-peptide-induced toxicity Langmuir 2013, 29, 11713-11723
    • (2013) Langmuir , vol.29 , pp. 11713-11723
    • Thapa, A.1    Vernon, B.C.2    De La Pena, K.3    Soliz, G.4    Moreno, H.A.5    Lopez, G.P.6    Chi, E.Y.7
  • 7
    • 84870614632 scopus 로고    scopus 로고
    • Negatively charged gold nanoparticles inhibit Alzheimers amyloid-beta fibrillization, induce fibril dissociation, and mitigate neurotoxicity
    • Liao, Y. H.; Chang, Y. J.; Yoshiike, Y.; Chang, Y. C.; Chen, Y. R. Negatively charged gold nanoparticles inhibit Alzheimers amyloid-beta fibrillization, induce fibril dissociation, and mitigate neurotoxicity Small 2012, 8, 3631-3639
    • (2012) Small , vol.8 , pp. 3631-3639
    • Liao, Y.H.1    Chang, Y.J.2    Yoshiike, Y.3    Chang, Y.C.4    Chen, Y.R.5
  • 8
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimers disease amyloid hypothesis: A genetic perspective
    • Tanzi, R. E.; Bertram, L. Twenty years of the Alzheimers disease amyloid hypothesis: a genetic perspective Cell 2005, 120, 545-555
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 9
    • 84872571866 scopus 로고    scopus 로고
    • Effective targeting of Abeta to macrophages by sonochemically prepared surface-modified protein microspheres
    • Richman, M.; Perelman, A.; Gertler, A.; Rahimipour, S. Effective targeting of Abeta to macrophages by sonochemically prepared surface-modified protein microspheres Biomacromolecules 2013, 14, 110-116
    • (2013) Biomacromolecules , vol.14 , pp. 110-116
    • Richman, M.1    Perelman, A.2    Gertler, A.3    Rahimipour, S.4
  • 11
    • 84865733428 scopus 로고    scopus 로고
    • Aggregation pathways of the amyloid beta(1-42) peptide depend on its colloidal stability and ordered beta-sheet stacking
    • Jiang, D.; Rauda, I.; Han, S.; Chen, S.; Zhou, F. Aggregation pathways of the amyloid beta(1-42) peptide depend on its colloidal stability and ordered beta-sheet stacking Langmuir 2012, 28, 12711-12721
    • (2012) Langmuir , vol.28 , pp. 12711-12721
    • Jiang, D.1    Rauda, I.2    Han, S.3    Chen, S.4    Zhou, F.5
  • 13
    • 84860112219 scopus 로고    scopus 로고
    • Structure, orientation, and surface interaction of Alzheimer amyloid-beta peptides on the graphite
    • Yu, X.; Wang, Q.; Lin, Y.; Zhao, J.; Zhao, C.; Zheng, J. Structure, orientation, and surface interaction of Alzheimer amyloid-beta peptides on the graphite Langmuir 2012, 28, 6595-6605
    • (2012) Langmuir , vol.28 , pp. 6595-6605
    • Yu, X.1    Wang, Q.2    Lin, Y.3    Zhao, J.4    Zhao, C.5    Zheng, J.6
  • 14
    • 84865007775 scopus 로고    scopus 로고
    • Human Serum albumin can regulate amyloid-beta peptide fiber growth in the brain interstitium: Implications for Alzheimer disease
    • Stanyon, H. F.; Viles, J. H. Human Serum albumin can regulate amyloid-beta peptide fiber growth in the brain interstitium: implications for Alzheimer disease J. Biol. Chem. 2012, 287, 28163-28168
    • (2012) J. Biol. Chem. , vol.287 , pp. 28163-28168
    • Stanyon, H.F.1    Viles, J.H.2
  • 19
    • 84878234966 scopus 로고    scopus 로고
    • Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils
    • Palhano, F. L.; Lee, J.; Grimster, N. P.; Kelly, J. W. Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils J. Am. Chem. Soc. 2013, 135, 7503-7510
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 7503-7510
    • Palhano, F.L.1    Lee, J.2    Grimster, N.P.3    Kelly, J.W.4
  • 20
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula, M.; Kayed, R.; Milton, S.; Glabe, C. G. Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct J. Biol. Chem. 2007, 282, 10311-10324
    • (2007) J. Biol. Chem. , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 21
    • 84862826842 scopus 로고    scopus 로고
    • Effect of surface-functionalized nanoparticles on the elongation phase of beta-amyloid (1-40) fibrillogenesis
    • Chan, H. M.; Xiao, L.; Yeung, K. M.; Ho, S. L.; Zhao, D.; Chan, W. H.; Li, H. W. Effect of surface-functionalized nanoparticles on the elongation phase of beta-amyloid (1-40) fibrillogenesis Biomaterials 2012, 33, 4443-4450
    • (2012) Biomaterials , vol.33 , pp. 4443-4450
    • Chan, H.M.1    Xiao, L.2    Yeung, K.M.3    Ho, S.L.4    Zhao, D.5    Chan, W.H.6    Li, H.W.7
  • 22
    • 70350348150 scopus 로고    scopus 로고
    • Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-L-cysteine capped quantum dots
    • Xiao, L.; Zhao, D.; Chan, W. H.; Choi, M. M.; Li, H. W. Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-L-cysteine capped quantum dots Biomaterials 2010, 31, 91-98
    • (2010) Biomaterials , vol.31 , pp. 91-98
    • Xiao, L.1    Zhao, D.2    Chan, W.H.3    Choi, M.M.4    Li, H.W.5
  • 24
    • 72249108028 scopus 로고    scopus 로고
    • Human serum albumin inhibits Abeta fibrillization through a "monomer-competitor" mechanism
    • Milojevic, J.; Raditsis, A.; Melacini, G. Human serum albumin inhibits Abeta fibrillization through a "monomer-competitor" mechanism Biophys. J. 2009, 97, 2585-2594
    • (2009) Biophys. J. , vol.97 , pp. 2585-2594
    • Milojevic, J.1    Raditsis, A.2    Melacini, G.3
  • 27
    • 85081820432 scopus 로고    scopus 로고
    • Detection of Aβ aggregation and inhibition by dual functions of gold nanoplasmic particles: Catalytic activator and optical reporter
    • Inhee, C.; Lee, P.; Rapid, L. Detection of Aβ aggregation and inhibition by dual functions of gold nanoplasmic particles: catalytic activator and optical reporter ACS Nano 2013, 7, 10
    • (2013) ACS Nano , vol.7 , pp. 10
    • Inhee, C.1    Lee, P.2    Rapid, L.3
  • 30
    • 0023191678 scopus 로고
    • Serum and cerebrospinal fluid proteins and the blood-brain barrier in Alzheimers disease and multi-infarct dementia
    • Elovaara, I.; Palo, J.; Erkinjuntti, T.; Sulkava, R. Serum and cerebrospinal fluid proteins and the blood-brain barrier in Alzheimers disease and multi-infarct dementia Eur. J. Neurol. 1987, 26, 229-234
    • (1987) Eur. J. Neurol. , vol.26 , pp. 229-234
    • Elovaara, I.1    Palo, J.2    Erkinjuntti, T.3    Sulkava, R.4
  • 32
    • 84875545405 scopus 로고    scopus 로고
    • Influence of the physiochemical properties of superparamagnetic iron oxide nanoparticles on amyloid beta protein fibrillation in solution
    • Mahmoudi, M.; Quinlan-Pluck, F.; Monopoli, M. P.; Sheibani, S.; Vali, H.; Dawson, K. A.; Lynch, I. Influence of the physiochemical properties of superparamagnetic iron oxide nanoparticles on amyloid beta protein fibrillation in solution ACS Chem. Neurosci. 2013, 4, 475-485
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 475-485
    • Mahmoudi, M.1    Quinlan-Pluck, F.2    Monopoli, M.P.3    Sheibani, S.4    Vali, H.5    Dawson, K.A.6    Lynch, I.7
  • 33
    • 84875350549 scopus 로고    scopus 로고
    • The role of surface functionality in determining nanoparticle cytotoxicity
    • Kim, S. T.; Saha, K.; Kim, C.; Rotello, V. M. The role of surface functionality in determining nanoparticle cytotoxicity Acc. Chem. Res. 2013, 46, 681-691
    • (2013) Acc. Chem. Res. , vol.46 , pp. 681-691
    • Kim, S.T.1    Saha, K.2    Kim, C.3    Rotello, V.M.4
  • 34
    • 36348989570 scopus 로고    scopus 로고
    • Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-β-peptide aggregation
    • Santa-María, I.; Hernández, F.; Moreno, F. J.; Avila, J. Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-β-peptide aggregation Neurosci. Lett. 2007, 429, 91-94
    • (2007) Neurosci. Lett. , vol.429 , pp. 91-94
    • Santa-María, I.1    Hernández, F.2    Moreno, F.J.3    Avila, J.4
  • 35
    • 67849088523 scopus 로고    scopus 로고
    • Protein adsorption and cell adhesion on cationic, neutral, and anionic 2-methacryloyloxyethyl phosphorylcholine copolymer surfaces
    • Xu, Y.; Takai, M.; Ishihara, K. Protein adsorption and cell adhesion on cationic, neutral, and anionic 2-methacryloyloxyethyl phosphorylcholine copolymer surfaces Biomaterials 2009, 30, 4930-4938
    • (2009) Biomaterials , vol.30 , pp. 4930-4938
    • Xu, Y.1    Takai, M.2    Ishihara, K.3
  • 36
    • 83355162676 scopus 로고    scopus 로고
    • High throughput atmospheric pressure plasma-induced graft polymerization for identifying protein-resistant surfaces
    • Gu, M.; Kilduff, J. E.; Belfort, G. High throughput atmospheric pressure plasma-induced graft polymerization for identifying protein-resistant surfaces Biomaterials 2012, 33, 1261-1270
    • (2012) Biomaterials , vol.33 , pp. 1261-1270
    • Gu, M.1    Kilduff, J.E.2    Belfort, G.3
  • 37
    • 85081815927 scopus 로고
    • J. Trypsin purification by affinity binding to small unilamellar liposomes
    • D.Powers, J. Trypsin purification by affinity binding to small unilamellar liposomes Biotechnol. Bioeng. 1990, 36, 14
    • (1990) Biotechnol. Bioeng. , vol.36 , pp. 14
    • Powers, D.1
  • 38
    • 84866661019 scopus 로고    scopus 로고
    • Structures of bovine, equine and leporine serum albumin
    • Bujacz, A. Structures of bovine, equine and leporine serum albumin Acta Crystallogr., Sect. D 2012, 68, 1278-12789
    • (2012) Acta Crystallogr., Sect. D , vol.68 , pp. 1278-12789
    • Bujacz, A.1
  • 40
    • 0032831760 scopus 로고    scopus 로고
    • Toxicity of protein aggregates in PC12 cells: 3-(4,5-dimethylthiazol-2- yl)-2,5-diphenyltetrazolium bromide assay
    • Shearman, M. S. Toxicity of protein aggregates in PC12 cells: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay Methods Enzymol. 1999, 309, 716-723
    • (1999) Methods Enzymol. , vol.309 , pp. 716-723
    • Shearman, M.S.1
  • 41
    • 84887015310 scopus 로고    scopus 로고
    • Dual-functional nanoparticles targeting amyloid plaques in the brains of Alzheimers disease mice
    • Zhang, C.; Wan, X.; Zheng, X.; Shao, X.; Liu, Q.; Zhang, Q.; Qian, Y. Dual-functional nanoparticles targeting amyloid plaques in the brains of Alzheimers disease mice Biomaterials 2014, 35, 456-465
    • (2014) Biomaterials , vol.35 , pp. 456-465
    • Zhang, C.1    Wan, X.2    Zheng, X.3    Shao, X.4    Liu, Q.5    Zhang, Q.6    Qian, Y.7
  • 42
    • 84901795888 scopus 로고    scopus 로고
    • Mo polyoxometalate nanoclusters capable of inhibiting the aggregation of Abeta-peptide associated with Alzheimers disease
    • Chen, Q.; Yang, L.; Zheng, C.; Zheng, W.; Zhang, J.; Zhou, Y.; Liu, J. Mo polyoxometalate nanoclusters capable of inhibiting the aggregation of Abeta-peptide associated with Alzheimers disease Nanoscale 2014, 6, 6886-6897
    • (2014) Nanoscale , vol.6 , pp. 6886-6897
    • Chen, Q.1    Yang, L.2    Zheng, C.3    Zheng, W.4    Zhang, J.5    Zhou, Y.6    Liu, J.7
  • 43
    • 84155163206 scopus 로고    scopus 로고
    • Modulation of fibril formation by a beta-sheet breaker peptide ligand: An electrochemical approach
    • Veloso, A. J.; Kerman, K. Modulation of fibril formation by a beta-sheet breaker peptide ligand: an electrochemical approach Bioelectrochemistry 2012, 84, 49-52
    • (2012) Bioelectrochemistry , vol.84 , pp. 49-52
    • Veloso, A.J.1    Kerman, K.2
  • 44
    • 84155164900 scopus 로고    scopus 로고
    • Inhibition of amyloid peptide fragment Aβ25-35 fibrillogenesis and toxicity by N-terminal β-amino acid-containing esapeptides: Is taurine moiety essential for in vivo effects?
    • Giordano, C.; Sansone, A.; Masi, A.; Masci, A.; Mosca, L.; Chiaraluce, R.; Pasquo, A.; Consalvi, V. Inhibition of amyloid peptide fragment Aβ25-35 fibrillogenesis and toxicity by N-terminal β-amino acid-containing esapeptides: is taurine moiety essential for in vivo effects? Chem. Biol. Drug. Des. 2012, 79, 30-37
    • (2012) Chem. Biol. Drug. Des. , vol.79 , pp. 30-37
    • Giordano, C.1    Sansone, A.2    Masi, A.3    Masci, A.4    Mosca, L.5    Chiaraluce, R.6    Pasquo, A.7    Consalvi, V.8
  • 45
    • 84874022077 scopus 로고    scopus 로고
    • S14G-humanin inhibits Abeta1-42 fibril formation, disaggregates preformed fibrils, and protects against Abeta-induced cytotoxicity in vitro
    • Zhang, W.; Du, Y.; Bai, M.; Xi, Y.; Li, Z.; Miao, J. S14G-humanin inhibits Abeta1-42 fibril formation, disaggregates preformed fibrils, and protects against Abeta-induced cytotoxicity in vitro J. Pept. Sci. 2013, 19, 159-165
    • (2013) J. Pept. Sci. , vol.19 , pp. 159-165
    • Zhang, W.1    Du, Y.2    Bai, M.3    Xi, Y.4    Li, Z.5    Miao, J.6
  • 46
    • 77956698237 scopus 로고    scopus 로고
    • Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimers disease research
    • Jan, A.; Hartley, D. M.; Lashuel, H. A. Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimers disease research Nat. Protoc. 2010, 5, 1186-1209
    • (2010) Nat. Protoc. , vol.5 , pp. 1186-1209
    • Jan, A.1    Hartley, D.M.2    Lashuel, H.A.3
  • 47
    • 84884630099 scopus 로고    scopus 로고
    • Human LilrB2 is a beta-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimers model
    • Kim, T.; Vidal, G. S.; Djurisic, M.; William, C. M.; Birnbaum, M. E.; Garcia, K. C.; Hyman, B. T.; Shatz, C. J. Human LilrB2 is a beta-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimers model Science 2013, 341, 1399-1404
    • (2013) Science , vol.341 , pp. 1399-1404
    • Kim, T.1    Vidal, G.S.2    Djurisic, M.3    William, C.M.4    Birnbaum, M.E.5    Garcia, K.C.6    Hyman, B.T.7    Shatz, C.J.8
  • 48
    • 84055176288 scopus 로고    scopus 로고
    • C-terminal tetrapeptides inhibit Abeta42-induced neurotoxicity primarily through specific interaction at the N-terminus of Abeta42
    • Li, H.; Du, Z.; Lopes, D. H.; Fradinger, E. A.; Wang, C.; Bitan, G. C-terminal tetrapeptides inhibit Abeta42-induced neurotoxicity primarily through specific interaction at the N-terminus of Abeta42 J. Med. Chem. 2011, 54, 8451-8460
    • (2011) J. Med. Chem. , vol.54 , pp. 8451-8460
    • Li, H.1    Du, Z.2    Lopes, D.H.3    Fradinger, E.A.4    Wang, C.5    Bitan, G.6
  • 49
    • 0033531797 scopus 로고    scopus 로고
    • Laminin inhibits both Aβ40 and Aβ42 fibril formation but does not affect Aβ40 or Aβ42-induced cytotoxicity in PC12 cells
    • Monji, A.; Tashiro, K.-i.; Yoshida, I.; Kaname, H.; Hayashi, Y.; Matsuda, K.; Tashiro, N. Laminin inhibits both Aβ40 and Aβ42 fibril formation but does not affect Aβ40 or Aβ42-induced cytotoxicity in PC12 cells Neurosci. Lett. 1999, 266, 85-88
    • (1999) Neurosci. Lett. , vol.266 , pp. 85-88
    • Monji, A.1    Tashiro, K.-I.2    Yoshida, I.3    Kaname, H.4    Hayashi, Y.5    Matsuda, K.6    Tashiro, N.7
  • 52
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the Aggregation Kinetics of Amyloid Peptides
    • Pellarin, R.; Caflisch, A. Interpreting the Aggregation Kinetics of Amyloid Peptides J. Mol. Biol. 2006, 360, 882-892
    • (2006) J. Mol. Biol. , vol.360 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 53
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimers amyloid peptide Aβ
    • Wood, S. J.; Maleeff, B.; Hart, T.; Wetzel, R. Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimers amyloid peptide Aβ J. Mol. Biol. 1996, 256, 870-877
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4
  • 54
    • 84885156655 scopus 로고    scopus 로고
    • Mapping the interactions between the Alzheimers Abeta-peptide and human serum albumin beyond domain resolution
    • Algamal, M.; Milojevic, J.; Jafari, N.; Zhang, W.; Melacini, G. Mapping the interactions between the Alzheimers Abeta-peptide and human serum albumin beyond domain resolution Biophys. J. 2013, 105, 1700-1709
    • (2013) Biophys. J. , vol.105 , pp. 1700-1709
    • Algamal, M.1    Milojevic, J.2    Jafari, N.3    Zhang, W.4    Melacini, G.5
  • 55
    • 58249138904 scopus 로고    scopus 로고
    • The effect of solvents on the conformations of amyloid beta-peptide (1-42) studied by molecular dynamics simulation
    • Yang, C.; Li, J. Y.; Li, Y.; Zhu, X. L. The effect of solvents on the conformations of amyloid beta-peptide (1-42) studied by molecular dynamics simulation J. Mol. Struct. 2009, 895, 1-8
    • (2009) J. Mol. Struct. , vol.895 , pp. 1-8
    • Yang, C.1    Li, J.Y.2    Li, Y.3    Zhu, X.L.4
  • 56
    • 77649137571 scopus 로고    scopus 로고
    • Effects of ligand density on hydrophobic charge induction chromatography: Molecular dynamics simulation
    • Zhang, L.; Zhao, G.; Sun, Y. Effects of ligand density on hydrophobic charge induction chromatography: molecular dynamics simulation J. Phys. Chem. B 2010, 114, 2203-2211
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2203-2211
    • Zhang, L.1    Zhao, G.2    Sun, Y.3
  • 57
    • 67650096377 scopus 로고    scopus 로고
    • Molecular insight into protein conformational transition in hydrophobic charge induction chromatography: A molecular dynamics simulation
    • Zhang, L.; Zhao, G.; Sun, Y. Molecular insight into protein conformational transition in hydrophobic charge induction chromatography: a molecular dynamics simulation J. Phys. Chem. B 2009, 113, 6873-6880
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6873-6880
    • Zhang, L.1    Zhao, G.2    Sun, Y.3


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