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Volumn 34, Issue 4, 2013, Pages 1383-1390

The effect of graphene oxide on conformation change, aggregation and cytotoxicity of HIV-1 regulatory protein (Vpr)

Author keywords

Aggregation; Conformation change; Cytotoxicity; Graphene oxide; Hydrophobic interaction; Vpr13 33

Indexed keywords

CONFORMATION CHANGE; GRAPHENE OXIDES; GRAPHITE SURFACES; HELICAL CONFORMATION; HYDROPHOBIC INTERACTIONS; ION CHANNEL; LARGE UNILAMELLAR VESICLES; MTT ASSAYS; NEUROBLASTOMA CELLS; PORE FORMING; PREFERENTIAL ADSORPTION; REGULATORY PROTEIN; SHEET STRUCTURE; T CELLS; VIRAL PROTEINS; VPR13-33;

EID: 84870342653     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2012.10.067     Document Type: Article
Times cited : (53)

References (52)
  • 1
    • 17644446136 scopus 로고    scopus 로고
    • A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly
    • Lombardo E., Ramírez J.C., Agbandje-McKenna M., Almendral J.M. A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly. J Virol 2000, 74:3804-3814.
    • (2000) J Virol , vol.74 , pp. 3804-3814
    • Lombardo, E.1    Ramírez, J.C.2    Agbandje-McKenna, M.3    Almendral, J.M.4
  • 2
    • 79952748653 scopus 로고    scopus 로고
    • Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion
    • Donald J.E., Zhang Y., Fiorin G., Carnevale V., Slochower D.R., Gai F., et al. Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion. Proc Natl Acad Sci U S A 2011, 108:3958-3963.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3958-3963
    • Donald, J.E.1    Zhang, Y.2    Fiorin, G.3    Carnevale, V.4    Slochower, D.R.5    Gai, F.6
  • 3
    • 79952409054 scopus 로고    scopus 로고
    • Rhesus rotavirus entry into a polarized epithelium is endocytosis dependent and involves sequential VP4 conformational changes
    • Wolf M., Vo P.T., Greenberg H.B. Rhesus rotavirus entry into a polarized epithelium is endocytosis dependent and involves sequential VP4 conformational changes. J Virol 2011, 85:2492-2503.
    • (2011) J Virol , vol.85 , pp. 2492-2503
    • Wolf, M.1    Vo, P.T.2    Greenberg, H.B.3
  • 4
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • Bewley C.A., Louis J.M., Ghirlando R., Clore G.M. Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J Biol Chem 2002, 277:14238-14245.
    • (2002) J Biol Chem , vol.277 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 5
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 2001, 70:777-810.
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 6
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White J.M. Viral and cellular membrane fusion proteins. Annu Rev Physiol 1990, 52:675-697.
    • (1990) Annu Rev Physiol , vol.52 , pp. 675-697
    • White, J.M.1
  • 7
    • 70350746423 scopus 로고    scopus 로고
    • Physical aspects of viral membrane fusion
    • Laura W., Keith W. Physical aspects of viral membrane fusion. The Scientific World J 2009, 9:764-780.
    • (2009) The Scientific World J , vol.9 , pp. 764-780
    • Laura, W.1    Keith, W.2
  • 8
    • 0037418426 scopus 로고    scopus 로고
    • Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers
    • Ostuni E., Grzybowski B.A., Mrksich M., Roberts C.S., Whitesides G.M. Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers. Langmuir 2003, 19:1861-1872.
    • (2003) Langmuir , vol.19 , pp. 1861-1872
    • Ostuni, E.1    Grzybowski, B.A.2    Mrksich, M.3    Roberts, C.S.4    Whitesides, G.M.5
  • 9
    • 68649092815 scopus 로고    scopus 로고
    • Molecular-level evidence of the surface-induced transformation of peptide structures revealed by scanning tunneling microscopy
    • Mao X., Wang Y., Liu L., Niu L., Yang Y., Wang C. Molecular-level evidence of the surface-induced transformation of peptide structures revealed by scanning tunneling microscopy. Langmuir 2009, 25:8849-8853.
    • (2009) Langmuir , vol.25 , pp. 8849-8853
    • Mao, X.1    Wang, Y.2    Liu, L.3    Niu, L.4    Yang, Y.5    Wang, C.6
  • 10
    • 21244462685 scopus 로고    scopus 로고
    • Protein structural perturbation and aggregation on homogeneous surfaces
    • Sethuraman A., Belfort G. Protein structural perturbation and aggregation on homogeneous surfaces. Biophys J 2005, 88:1322-1333.
    • (2005) Biophys J , vol.88 , pp. 1322-1333
    • Sethuraman, A.1    Belfort, G.2
  • 11
    • 0026558240 scopus 로고
    • Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of conserved residues in cell fusion
    • Horvath C., Lamb R. Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of conserved residues in cell fusion. J Virol 1992, 66:2443-2455.
    • (1992) J Virol , vol.66 , pp. 2443-2455
    • Horvath, C.1    Lamb, R.2
  • 12
    • 0032515995 scopus 로고    scopus 로고
    • Extracellular HIV-1 virus protein R causes a large inward current and cell death in cultured hippocampal neurons: implications for AIDS pathology
    • Piller S.C., Jans P., Gage P.W., Jans D.A. Extracellular HIV-1 virus protein R causes a large inward current and cell death in cultured hippocampal neurons: implications for AIDS pathology. Proc Natl Acad Sci U S A 1998, 95:4595-4600.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4595-4600
    • Piller, S.C.1    Jans, P.2    Gage, P.W.3    Jans, D.A.4
  • 13
    • 0028892209 scopus 로고
    • Functional analysis of HIV-1 Vpr: identification of determinants essential for subcellular localization
    • Mahalingam S., Collman R.G., Patel M., Monken C.E., Srinivasan A. Functional analysis of HIV-1 Vpr: identification of determinants essential for subcellular localization. Virology 1995, 212:331-339.
    • (1995) Virology , vol.212 , pp. 331-339
    • Mahalingam, S.1    Collman, R.G.2    Patel, M.3    Monken, C.E.4    Srinivasan, A.5
  • 14
    • 9044243753 scopus 로고    scopus 로고
    • Vpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers
    • Piller S., Ewart G., Premkumar A., Cox G., Gage P. Vpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers. Proc Natl Acad Sci U S A 1996, 93:111.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 111
    • Piller, S.1    Ewart, G.2    Premkumar, A.3    Cox, G.4    Gage, P.5
  • 15
    • 69449108433 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr: functions and molecular interactions
    • Romani B., Engelbrecht S. Human immunodeficiency virus type 1 Vpr: functions and molecular interactions. J Gen Virol 2009, 90:1795-1805.
    • (2009) J Gen Virol , vol.90 , pp. 1795-1805
    • Romani, B.1    Engelbrecht, S.2
  • 16
    • 0032947291 scopus 로고    scopus 로고
    • The amino-terminal region of Vpr from human immunodeficiency virus type 1 forms ion channels and kills neurons
    • Piller S.C., Ewart G.D., Jans D.A., Gage P.W., Cox G.B. The amino-terminal region of Vpr from human immunodeficiency virus type 1 forms ion channels and kills neurons. J Virol 1999, 73:4230-4238.
    • (1999) J Virol , vol.73 , pp. 4230-4238
    • Piller, S.C.1    Ewart, G.D.2    Jans, D.A.3    Gage, P.W.4    Cox, G.B.5
  • 17
    • 0033485383 scopus 로고    scopus 로고
    • NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr
    • Wecker K., Roques B. NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr. Eur J Biochem 1999, 266:359-369.
    • (1999) Eur J Biochem , vol.266 , pp. 359-369
    • Wecker, K.1    Roques, B.2
  • 18
    • 0034817996 scopus 로고    scopus 로고
    • Solution structure of human immunodeficiency virus type 1 Vpr (13-33) peptide in micelles
    • Engler A., Stangler T., Willbold D. Solution structure of human immunodeficiency virus type 1 Vpr (13-33) peptide in micelles. Eur J Biochem 2001, 268:389-395.
    • (2001) Eur J Biochem , vol.268 , pp. 389-395
    • Engler, A.1    Stangler, T.2    Willbold, D.3
  • 19
  • 20
    • 77950466838 scopus 로고    scopus 로고
    • Vpr and its interactions with cellular proteins. HIV interactions with host cell proteins
    • Planelles V., Benichou S. Vpr and its interactions with cellular proteins. HIV interactions with host cell proteins. Curr Top Microbiol Immunol 2009, 177-200.
    • (2009) Curr Top Microbiol Immunol , pp. 177-200
    • Planelles, V.1    Benichou, S.2
  • 21
    • 0031967149 scopus 로고    scopus 로고
    • The putative alpha helix 2 of human immunodeficiency virus type 1 Vpr contains a determinant which is responsible for the nuclear translocation of proviral DNA in growth-arrested cells
    • Nie Z., Bergeron D., Subbramanian R.A., Yao X.J., Checroune F., Rougeau N., et al. The putative alpha helix 2 of human immunodeficiency virus type 1 Vpr contains a determinant which is responsible for the nuclear translocation of proviral DNA in growth-arrested cells. J Virol 1998, 72:4104-4115.
    • (1998) J Virol , vol.72 , pp. 4104-4115
    • Nie, Z.1    Bergeron, D.2    Subbramanian, R.A.3    Yao, X.J.4    Checroune, F.5    Rougeau, N.6
  • 22
    • 0028840657 scopus 로고
    • Mutagenic analysis of human immunodeficiency virus type 1 Vpr: role of a predicted N-terminal alpha-helical structure in Vpr nuclear localization and virion incorporation
    • Yao X.J., Subbramanian R.A., Rougeau N., Boisvert F., Bergeron D., Cohen E.A. Mutagenic analysis of human immunodeficiency virus type 1 Vpr: role of a predicted N-terminal alpha-helical structure in Vpr nuclear localization and virion incorporation. J Virol 1995, 69:7032-7044.
    • (1995) J Virol , vol.69 , pp. 7032-7044
    • Yao, X.J.1    Subbramanian, R.A.2    Rougeau, N.3    Boisvert, F.4    Bergeron, D.5    Cohen, E.A.6
  • 23
    • 0033755616 scopus 로고    scopus 로고
    • Functional role of residues corresponding to helical domain II (amino acids 35 to 46) of human immunodeficiency virus type 1 Vpr
    • Singh S.P., Tomkowicz B., Lai D., Cartas M., Mahalingam S., Kalyanaraman V.S., et al. Functional role of residues corresponding to helical domain II (amino acids 35 to 46) of human immunodeficiency virus type 1 Vpr. J Virol 2000, 74:10650-10657.
    • (2000) J Virol , vol.74 , pp. 10650-10657
    • Singh, S.P.1    Tomkowicz, B.2    Lai, D.3    Cartas, M.4    Mahalingam, S.5    Kalyanaraman, V.S.6
  • 24
    • 79953848334 scopus 로고    scopus 로고
    • HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic intervention
    • Kogan M., Rappaport J. HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic intervention. Retrovirology 2011, 8:25.
    • (2011) Retrovirology , vol.8 , pp. 25
    • Kogan, M.1    Rappaport, J.2
  • 25
    • 4544322878 scopus 로고    scopus 로고
    • Structure-functional analysis of human immunodeficiency virus type 1 (HIV-1) Vpr: role of leucine residues on Vpr-mediated transactivation and virus replication
    • Thotala D., Schafer E.A., Majumder B., Janket M.L., Wagner M., Srinivasan A., et al. Structure-functional analysis of human immunodeficiency virus type 1 (HIV-1) Vpr: role of leucine residues on Vpr-mediated transactivation and virus replication. Virology 2004, 328:89-100.
    • (2004) Virology , vol.328 , pp. 89-100
    • Thotala, D.1    Schafer, E.A.2    Majumder, B.3    Janket, M.L.4    Wagner, M.5    Srinivasan, A.6
  • 26
    • 0033882196 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr contains two leucine-rich helices that mediate glucocorticoid receptor coactivation independently of its effects on G2 cell cycle arrest
    • Sherman M.P., de Noronha C.M.C., Pearce D., Greene W.C. Human immunodeficiency virus type 1 Vpr contains two leucine-rich helices that mediate glucocorticoid receptor coactivation independently of its effects on G2 cell cycle arrest. J Virol 2000, 74:8159-8165.
    • (2000) J Virol , vol.74 , pp. 8159-8165
    • Sherman, M.P.1    de Noronha, C.M.C.2    Pearce, D.3    Greene, W.C.4
  • 27
    • 50249123111 scopus 로고    scopus 로고
    • PEGylated nanographene oxide for delivery of water-insoluble cancer drugs
    • Liu Z., Robinson J.T., Sun X., Dai H. PEGylated nanographene oxide for delivery of water-insoluble cancer drugs. J Am Chem Soc 2008, 130:10876-10877.
    • (2008) J Am Chem Soc , vol.130 , pp. 10876-10877
    • Liu, Z.1    Robinson, J.T.2    Sun, X.3    Dai, H.4
  • 28
    • 80053633118 scopus 로고    scopus 로고
    • Cytotoxicity of graphene oxide and graphene in human erythrocytes and skin fibroblasts
    • Liao K.H.K., Lin Y.S., Macosko C.W., Haynes C.L. Cytotoxicity of graphene oxide and graphene in human erythrocytes and skin fibroblasts. ACS Appl Mater Inter 2011, 3:2607-2615.
    • (2011) ACS Appl Mater Inter , vol.3 , pp. 2607-2615
    • Liao, K.H.K.1    Lin, Y.S.2    Macosko, C.W.3    Haynes, C.L.4
  • 29
    • 79751518967 scopus 로고    scopus 로고
    • Interaction of peptides with graphene oxide and its application for real-time monitoring of protease activity
    • Zhang M., Yin B.C., Wang X.F., Ye B.C. Interaction of peptides with graphene oxide and its application for real-time monitoring of protease activity. Chem Commun 2011, 47:2399-2401.
    • (2011) Chem Commun , vol.47 , pp. 2399-2401
    • Zhang, M.1    Yin, B.C.2    Wang, X.F.3    Ye, B.C.4
  • 30
    • 84855447240 scopus 로고    scopus 로고
    • Assembly of graphene oxide-enzyme conjugates through hydrophobic interaction
    • Zhang Y., Zhang J., Huang X., Zhou X., Wu H., Guo S. Assembly of graphene oxide-enzyme conjugates through hydrophobic interaction. Small 2012, 8:154-159.
    • (2012) Small , vol.8 , pp. 154-159
    • Zhang, Y.1    Zhang, J.2    Huang, X.3    Zhou, X.4    Wu, H.5    Guo, S.6
  • 31
    • 84862833623 scopus 로고    scopus 로고
    • A general approach for monitoring peptide-protein interactions based on graphene-peptide complex
    • Lu C.H., Li J., Zhang X.L., Zheng A.X., Yang H.H., Chen X., et al. A general approach for monitoring peptide-protein interactions based on graphene-peptide complex. Anal Chem 2011, 83:7276-7282.
    • (2011) Anal Chem , vol.83 , pp. 7276-7282
    • Lu, C.H.1    Li, J.2    Zhang, X.L.3    Zheng, A.X.4    Yang, H.H.5    Chen, X.6
  • 33
    • 78449275182 scopus 로고    scopus 로고
    • Chemical functionalization of graphene enabled by phage displayed peptides
    • Cui Y., Kim S.N., Jones S.E., Wissler L.L., Naik R.R., McAlpine M.C. Chemical functionalization of graphene enabled by phage displayed peptides. Nano Lett 2010, 10:4559-4565.
    • (2010) Nano Lett , vol.10 , pp. 4559-4565
    • Cui, Y.1    Kim, S.N.2    Jones, S.E.3    Wissler, L.L.4    Naik, R.R.5    McAlpine, M.C.6
  • 35
    • 84861409508 scopus 로고    scopus 로고
    • Graphenes prepared by Staudenmaier, Hofmann and Hummers methods with consequent thermal exfoliation exhibit very different electrochemical properties
    • Poh H.L., Sanek F., Ambrosi A., Zhao G.J., Sofer Z., Pumera M. Graphenes prepared by Staudenmaier, Hofmann and Hummers methods with consequent thermal exfoliation exhibit very different electrochemical properties. Nanoscale 2012, 4:3515-3522.
    • (2012) Nanoscale , vol.4 , pp. 3515-3522
    • Poh, H.L.1    Sanek, F.2    Ambrosi, A.3    Zhao, G.J.4    Sofer, Z.5    Pumera, M.6
  • 36
    • 71949110860 scopus 로고    scopus 로고
    • Chaperon-mediated single molecular approach toward modulating A beta peptide aggregation
    • Liu L., Zhang L., Mao X.B., Niu L., Yang Y.L., Wang C. Chaperon-mediated single molecular approach toward modulating A beta peptide aggregation. Nano Lett 2009, 9:4066-4072.
    • (2009) Nano Lett , vol.9 , pp. 4066-4072
    • Liu, L.1    Zhang, L.2    Mao, X.B.3    Niu, L.4    Yang, Y.L.5    Wang, C.6
  • 37
    • 83755178092 scopus 로고    scopus 로고
    • Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies
    • Mao X.B., Wang C.X., Wu X.K., Ma X.J., Liu L., Zhang L., et al. Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies. Proc Natl Acad Sci U S A 2011, 108:19605-19610.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 19605-19610
    • Mao, X.B.1    Wang, C.X.2    Wu, X.K.3    Ma, X.J.4    Liu, L.5    Zhang, L.6
  • 38
    • 33847620805 scopus 로고    scopus 로고
    • Transformation of the amyloidogenic peptide amylin (20-29) into its corresponding peptoid and retropeptoid: access to both an amyloid inhibitor and template for self-assembled supramolecular tapes
    • Elgersma R.C., Mulder G.E., Kruijtzer J.A.W., Posthuma G., Rijkers D.T.S., Liskamp R.M.J. Transformation of the amyloidogenic peptide amylin (20-29) into its corresponding peptoid and retropeptoid: access to both an amyloid inhibitor and template for self-assembled supramolecular tapes. Bioorg Med Chem Lett 2007, 17:1837-1842.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 1837-1842
    • Elgersma, R.C.1    Mulder, G.E.2    Kruijtzer, J.A.W.3    Posthuma, G.4    Rijkers, D.T.S.5    Liskamp, R.M.J.6
  • 39
    • 67349128044 scopus 로고    scopus 로고
    • Amyloid beta (1-42) folding multiplicity and single-molecule binding behavior studied with STM
    • Ma X.J., Liu L., Mao X.B., Niu L., Deng K., Wu W.H., et al. Amyloid beta (1-42) folding multiplicity and single-molecule binding behavior studied with STM. J Mol Biol 2009, 388:894-901.
    • (2009) J Mol Biol , vol.388 , pp. 894-901
    • Ma, X.J.1    Liu, L.2    Mao, X.B.3    Niu, L.4    Deng, K.5    Wu, W.H.6
  • 40
    • 67650756419 scopus 로고    scopus 로고
    • Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy
    • Mao X.B., Ma X.J., Liu L., Niu L., Yang Y.L., Wang C. Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy. J Struct Biol 2009, 167:209-215.
    • (2009) J Struct Biol , vol.167 , pp. 209-215
    • Mao, X.B.1    Ma, X.J.2    Liu, L.3    Niu, L.4    Yang, Y.L.5    Wang, C.6
  • 41
    • 27944467440 scopus 로고    scopus 로고
    • Nonfibrous β-structured aggregation of an Aβ model peptide (Ad-2α) on GM1/DPPC mixed monolayer
    • Kawasaki T., Asaoka K., Mihara H., Okahata Y. Nonfibrous β-structured aggregation of an Aβ model peptide (Ad-2α) on GM1/DPPC mixed monolayer. Surf J Colloid Inter Sci 2006, 294:295-303.
    • (2006) Surf J Colloid Inter Sci , vol.294 , pp. 295-303
    • Kawasaki, T.1    Asaoka, K.2    Mihara, H.3    Okahata, Y.4
  • 42
    • 84863715767 scopus 로고    scopus 로고
    • Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties
    • Li C., Adamcik J., Mezzenga R. Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties. Nat Nanotechnol 2012, 7:421-427.
    • (2012) Nat Nanotechnol , vol.7 , pp. 421-427
    • Li, C.1    Adamcik, J.2    Mezzenga, R.3
  • 43
    • 77954637757 scopus 로고    scopus 로고
    • In vitro formation of amyloid from α-Synuclein is dominated by reactions at hydrophobic interfaces
    • Pronchik J., He X., Giurleo J.T., Talaga D.S. In vitro formation of amyloid from α-Synuclein is dominated by reactions at hydrophobic interfaces. J Am Chem Soc 2010, 132:9797-9803.
    • (2010) J Am Chem Soc , vol.132 , pp. 9797-9803
    • Pronchik, J.1    He, X.2    Giurleo, J.T.3    Talaga, D.S.4
  • 45
    • 78650251003 scopus 로고    scopus 로고
    • Distribution and biocompatibility studies of graphene oxide in mice after intravenous administration
    • Zhang X., Yin J., Peng C., Hu W., Zhu Z., Li W., et al. Distribution and biocompatibility studies of graphene oxide in mice after intravenous administration. Carbon 2011, 49:986-995.
    • (2011) Carbon , vol.49 , pp. 986-995
    • Zhang, X.1    Yin, J.2    Peng, C.3    Hu, W.4    Zhu, Z.5    Li, W.6
  • 47
    • 78651073259 scopus 로고    scopus 로고
    • In vitro toxicity evaluation of graphene oxide on A549 cells
    • Chang Y., Yang S.T., Liu J.H., Dong E., Wang Y., Cao A., et al. In vitro toxicity evaluation of graphene oxide on A549 cells. Toxicol Lett 2011, 200:201-210.
    • (2011) Toxicol Lett , vol.200 , pp. 201-210
    • Chang, Y.1    Yang, S.T.2    Liu, J.H.3    Dong, E.4    Wang, Y.5    Cao, A.6
  • 49
    • 54949098149 scopus 로고    scopus 로고
    • Mechanically strong, electrically conductive, and biocompatible graphene paper
    • Chen H., Müller M.B., Gilmore K.J., Wallace G.G., Li D. Mechanically strong, electrically conductive, and biocompatible graphene paper. Adv Mater 2008, 20:3557-3561.
    • (2008) Adv Mater , vol.20 , pp. 3557-3561
    • Chen, H.1    Müller, M.B.2    Gilmore, K.J.3    Wallace, G.G.4    Li, D.5
  • 50
    • 77149135601 scopus 로고    scopus 로고
    • Interfacing live cells with nanocarbon substrates
    • Agarwal S., Zhou X., Ye F., He Q., Chen G.C.K., Soo J., et al. Interfacing live cells with nanocarbon substrates. Langmuir 2010, 26:2244-2247.
    • (2010) Langmuir , vol.26 , pp. 2244-2247
    • Agarwal, S.1    Zhou, X.2    Ye, F.3    He, Q.4    Chen, G.C.K.5    Soo, J.6
  • 51
    • 77951158188 scopus 로고    scopus 로고
    • Biocompatible, robust free-standing paper composed of a TWEEN/graphene composite
    • Park S., Mohanty N., Suk J.W., Nagaraja A., An J., Piner R.D., et al. Biocompatible, robust free-standing paper composed of a TWEEN/graphene composite. Adv Mater 2010, 22:1736-1740.
    • (2010) Adv Mater , vol.22 , pp. 1736-1740
    • Park, S.1    Mohanty, N.2    Suk, J.W.3    Nagaraja, A.4    An, J.5    Piner, R.D.6
  • 52
    • 84873084737 scopus 로고    scopus 로고
    • Behavior and toxicity of graphene and its functionalized derivatives in biological systems
    • Yang K., Li Y., Tan X., Peng R., Liu Z. Behavior and toxicity of graphene and its functionalized derivatives in biological systems. Small 2012, 10.1002/smll.201201417.
    • (2012) Small
    • Yang, K.1    Li, Y.2    Tan, X.3    Peng, R.4    Liu, Z.5


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