메뉴 건너뛰기




Volumn 65, Issue 15, 2013, Pages 2070-2077

Molecular modeling in structural nano-toxicology: Interactions of nano-particles with nano-machinery of cells

Author keywords

Comparable sizes of nanoparticles; Computational predictions; Inhibition of nano mechanisms; Molecular interactions; Nano bio interactions; Oxidative damage

Indexed keywords

COMBINED DIAGNOSTICS; COMPUTATIONAL ANALYSIS; COMPUTATIONAL MOLECULAR MODELING; COMPUTATIONAL PREDICTIONS; INTRACELLULAR ORGANELLE; LONG-TERM EFFECTS; OXIDATIVE DAMAGE; SCIENCE AND TECHNOLOGY;

EID: 84888878340     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2013.05.005     Document Type: Review
Times cited : (52)

References (92)
  • 1
    • 0002982888 scopus 로고
    • There's plenty of room at the bottom
    • Feynman R.P. There's plenty of room at the bottom. Eng. Sci. 1960, 23:15.
    • (1960) Eng. Sci. , vol.23 , pp. 15
    • Feynman, R.P.1
  • 3
    • 84884507915 scopus 로고    scopus 로고
    • Linking micro- and macro-evolution at the cell type level: a view from the lophotrochozoan Platynereis dumerilii
    • N 20
    • Simakov Oleg, Larsson Tomas A., Arendt Detlev Linking micro- and macro-evolution at the cell type level: a view from the lophotrochozoan Platynereis dumerilii. Briefings in Functional Genomics first published online November 20, 2012, 10.1093/bfgp/els049.
    • (2012) Briefings in Functional Genomics first published online
    • Simakov, O.1    Larsson, T.A.2    Arendt, D.3
  • 5
    • 84885757504 scopus 로고    scopus 로고
    • Applying quantitative structure-activity relationship approaches to nanotoxicology: Current status and future potential
    • Available online 16 November 2012, ISSN 0300-483X
    • Winkler David A., Mombelli Enrico, Pietroiusti Antonio, Tran Lang, Worth Andrew, Fadel Bengt, McCall Maxine J. Applying quantitative structure-activity relationship approaches to nanotoxicology: Current status and future potential. Toxicology 2012, Available online 16 November 2012, ISSN 0300-483X, http://dx.doi.org/10.1016/j.tox.2012.11.005. (http://www.sciencedirect.com/science/article/pii/S0300483X12003976).
    • (2012) Toxicology
    • Winkler, D.A.1    Mombelli, E.2    Pietroiusti, A.3    Tran, L.4    Worth, A.5    Fadel, B.6    McCall, M.J.7
  • 6
    • 39849096578 scopus 로고    scopus 로고
    • Passive transport of C-60 fullerenes through a lipid membrane: a molecular dynamics simulation study
    • Bedrov D., Smith G.D., Davande H., Li L.W. Passive transport of C-60 fullerenes through a lipid membrane: a molecular dynamics simulation study. J. Phys. Chem. B 2008, 112:2078-2084.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 2078-2084
    • Bedrov, D.1    Smith, G.D.2    Davande, H.3    Li, L.W.4
  • 7
    • 34248396444 scopus 로고    scopus 로고
    • A molecular dynamics simulation study of C-60 fullerenes inside a dimyristoylphosphatidylcholine lipid bilayer
    • Li L.W., Davande H., Bedrov D., Smith G.D. A molecular dynamics simulation study of C-60 fullerenes inside a dimyristoylphosphatidylcholine lipid bilayer. J. Phys. Chem. B 2007, 111:4067-4072.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 4067-4072
    • Li, L.W.1    Davande, H.2    Bedrov, D.3    Smith, G.D.4
  • 8
    • 34047178622 scopus 로고    scopus 로고
    • Translocation of C-60 and its derivatives across a lipid bilayer
    • Qiao R., Roberts A.P., Mount A.S., Klaine S.J., Ke P.C. Translocation of C-60 and its derivatives across a lipid bilayer. Nano Lett. 2007, 7:614-619.
    • (2007) Nano Lett. , vol.7 , pp. 614-619
    • Qiao, R.1    Roberts, A.P.2    Mount, A.S.3    Klaine, S.J.4    Ke, P.C.5
  • 10
    • 58149142802 scopus 로고    scopus 로고
    • Molecular dynamics study of a nanotube-binding amphiphilic helical peptide at different water/hydrophobic interfaces
    • Chiu C.C., Dieckmann G.R., Nielsen S.O. Molecular dynamics study of a nanotube-binding amphiphilic helical peptide at different water/hydrophobic interfaces. J. Phys. Chem. B 2008, 112:16326-16333.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 16326-16333
    • Chiu, C.C.1    Dieckmann, G.R.2    Nielsen, S.O.3
  • 11
    • 70349330483 scopus 로고    scopus 로고
    • Binding free energy calculation of peptides to carbon nanotubes using molecular dynamics with a linear interaction energy approach
    • Kyani A., Goliaei B. Binding free energy calculation of peptides to carbon nanotubes using molecular dynamics with a linear interaction energy approach. J. Mol. Struct. (THEOCHEM) 2009, 913:63-69.
    • (2009) J. Mol. Struct. (THEOCHEM) , vol.913 , pp. 63-69
    • Kyani, A.1    Goliaei, B.2
  • 12
    • 0037197880 scopus 로고    scopus 로고
    • Molecular dynamics analysis of a buckyball-antibody complex
    • Noon W.H., Kong Y.F., Ma J.P. Molecular dynamics analysis of a buckyball-antibody complex. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:6466-6470.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6466-6470
    • Noon, W.H.1    Kong, Y.F.2    Ma, J.P.3
  • 13
    • 67549151161 scopus 로고    scopus 로고
    • Role of peptide-peptide interactions in stabilizing peptide-wrapped single-walled carbon nanotubes: a molecular dynamics study
    • Chiu C.C., Dieckmann G.R., Nielsen S.O. Role of peptide-peptide interactions in stabilizing peptide-wrapped single-walled carbon nanotubes: a molecular dynamics study. Biopolymers 2009, 92:156-163.
    • (2009) Biopolymers , vol.92 , pp. 156-163
    • Chiu, C.C.1    Dieckmann, G.R.2    Nielsen, S.O.3
  • 14
    • 28444495986 scopus 로고    scopus 로고
    • C60 binds to and deforms nucleotides
    • Zhao X., Striolo A., Cummings P.T. C60 binds to and deforms nucleotides. Biophys. J. 2005, 89:3856-3862.
    • (2005) Biophys. J. , vol.89 , pp. 3856-3862
    • Zhao, X.1    Striolo, A.2    Cummings, P.T.3
  • 15
    • 0141856420 scopus 로고    scopus 로고
    • Spontaneous insertion of DNA oligonucleotides into carbon nanotubes
    • Gao H.J., Kong Y., Cui D.X., Ozkan C.S. Spontaneous insertion of DNA oligonucleotides into carbon nanotubes. Nano Lett. 2003, 3:471-473.
    • (2003) Nano Lett. , vol.3 , pp. 471-473
    • Gao, H.J.1    Kong, Y.2    Cui, D.X.3    Ozkan, C.S.4
  • 16
    • 19944408630 scopus 로고    scopus 로고
    • Carbon nanotube interaction with DNA
    • Lu G., Maragakis P., Kaxiras E. Carbon nanotube interaction with DNA. Nano Lett. 2005, 5:897-900.
    • (2005) Nano Lett. , vol.5 , pp. 897-900
    • Lu, G.1    Maragakis, P.2    Kaxiras, E.3
  • 18
    • 79955668060 scopus 로고    scopus 로고
    • Nanomaterials in biological environment: a review of computer modelling studies
    • Makarucha A.J., Todorova N., Yarovsky I. Nanomaterials in biological environment: a review of computer modelling studies. Eur. Biophys. J. 2011, 40:103-115.
    • (2011) Eur. Biophys. J. , vol.40 , pp. 103-115
    • Makarucha, A.J.1    Todorova, N.2    Yarovsky, I.3
  • 19
    • 84878099108 scopus 로고    scopus 로고
    • Biosafety and Bioapplication of Nanomaterials by Designing Protein-Nanoparticle Interactions
    • Yang S.-T., Liu Y., Wang Y.-W., Cao A. Biosafety and Bioapplication of Nanomaterials by Designing Protein-Nanoparticle Interactions. Small 2013, 9:1635-1653. 10.1002/smll.201201492.
    • (2013) Small , vol.9 , pp. 1635-1653
    • Yang, S.-T.1    Liu, Y.2    Wang, Y.-W.3    Cao, A.4
  • 21
    • 55549144296 scopus 로고    scopus 로고
    • 3D QSAR CoMFA/CoMSIA, molecular docking and molecular dynamics studies of fullerene-based HIV-1 PR inhibitors
    • Durdagi S., Mavromoustakos T., Papadopoulos M.G. 3D QSAR CoMFA/CoMSIA, molecular docking and molecular dynamics studies of fullerene-based HIV-1 PR inhibitors. Bioorg. Med. Chem. Lett. 2008, 18:6283-6289.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 6283-6289
    • Durdagi, S.1    Mavromoustakos, T.2    Papadopoulos, M.G.3
  • 22
    • 55749100817 scopus 로고    scopus 로고
    • Computational design of novel fullerene analogues as potential HIV-1 PR inhibitors: analysis of the binding interactions between fullerene inhibitors and HIV-1 PR residues using 3D QSAR, molecular docking and molecular dynamics simulations
    • Durdagi S., Mavromoustakos T., Chronakis N., Papadopoulos M.G. Computational design of novel fullerene analogues as potential HIV-1 PR inhibitors: analysis of the binding interactions between fullerene inhibitors and HIV-1 PR residues using 3D QSAR, molecular docking and molecular dynamics simulations. Bioorg. Med. Chem. 2008, 16:9957-9974.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 9957-9974
    • Durdagi, S.1    Mavromoustakos, T.2    Chronakis, N.3    Papadopoulos, M.G.4
  • 23
    • 77958495541 scopus 로고    scopus 로고
    • The quantitative structure activity relationships for predicting HIV protease inhibition by substituted fullerenes
    • Martin D., Karelson M. The quantitative structure activity relationships for predicting HIV protease inhibition by substituted fullerenes. Lett. Drug Des. Discov. 2010, 7:587-595.
    • (2010) Lett. Drug Des. Discov. , vol.7 , pp. 587-595
    • Martin, D.1    Karelson, M.2
  • 25
    • 0032025417 scopus 로고    scopus 로고
    • Effects of C-60, a fullerene, on the activities of glutathione S-transferase and glutathione-related enzymes in rodent and human livers
    • Iwata N., Mukai T., Yamakoshi Y.N., Hara S., Yanase T., Shoji M., Endo T., Miyata N. Effects of C-60, a fullerene, on the activities of glutathione S-transferase and glutathione-related enzymes in rodent and human livers. Fullerene Sci. Technol. 1998, 6:213-226.
    • (1998) Fullerene Sci. Technol. , vol.6 , pp. 213-226
    • Iwata, N.1    Mukai, T.2    Yamakoshi, Y.N.3    Hara, S.4    Yanase, T.5    Shoji, M.6    Endo, T.7    Miyata, N.8
  • 26
    • 0027244713 scopus 로고
    • Inhibition of the Hiv-1 protease by fullerene derivatives - model-building studies and experimental-verification
    • Friedman S.H., Decamp D.L., Sijbesma R.P., Srdanov G., Wudl F., Kenyon G.L. Inhibition of the Hiv-1 protease by fullerene derivatives - model-building studies and experimental-verification. J. Am. Chem. Soc. 1993, 115:6506-6509.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6506-6509
    • Friedman, S.H.1    Decamp, D.L.2    Sijbesma, R.P.3    Srdanov, G.4    Wudl, F.5    Kenyon, G.L.6
  • 27
    • 84882454844 scopus 로고
    • Bucky-ball based inhibitors of the HIV protease - 2nd-generation design and model studies
    • (A1184-A1184)
    • Friedman S.H., Decamp D.L., Sijbesma R.P., Srdanov G., Wudl F., Kenyon G.L. Bucky-ball based inhibitors of the HIV protease - 2nd-generation design and model studies. FASEB J. 1993, 7. (A1184-A1184).
    • (1993) FASEB J. , vol.7
    • Friedman, S.H.1    Decamp, D.L.2    Sijbesma, R.P.3    Srdanov, G.4    Wudl, F.5    Kenyon, G.L.6
  • 29
    • 84855196452 scopus 로고    scopus 로고
    • Binding of novel fullerene inhibitors to HIV-1 protease: insight through molecular dynamics and molecular mechanics Poisson-Boltzmann surface area calculations
    • Tzoupis H., Leonis G., Durdagi S., Mouchlis V., Mavromoustakos T., Papadopoulos M.G. Binding of novel fullerene inhibitors to HIV-1 protease: insight through molecular dynamics and molecular mechanics Poisson-Boltzmann surface area calculations. J. Comput. Aided Mol. Des. 2011, 25:959-976.
    • (2011) J. Comput. Aided Mol. Des. , vol.25 , pp. 959-976
    • Tzoupis, H.1    Leonis, G.2    Durdagi, S.3    Mouchlis, V.4    Mavromoustakos, T.5    Papadopoulos, M.G.6
  • 30
    • 77956295819 scopus 로고    scopus 로고
    • Structure-based design of carbon nanotubes as HIV-1 protease inhibitors: atomistic and coarse-grained simulations
    • Cheng Y., Li D., Ji B., Shi X., Gao H. Structure-based design of carbon nanotubes as HIV-1 protease inhibitors: atomistic and coarse-grained simulations. J. Mol. Graph. Model. 2010, 29:171-177.
    • (2010) J. Mol. Graph. Model. , vol.29 , pp. 171-177
    • Cheng, Y.1    Li, D.2    Ji, B.3    Shi, X.4    Gao, H.5
  • 31
    • 84868491550 scopus 로고    scopus 로고
    • Binding of single walled carbon nanotube to WT and mutant HIV-1 proteases: analysis of flap dynamics and binding mechanism
    • Meher B.R., Wang Y. Binding of single walled carbon nanotube to WT and mutant HIV-1 proteases: analysis of flap dynamics and binding mechanism. J. Mol. Graph. Model. 2012, 38:430-445.
    • (2012) J. Mol. Graph. Model. , vol.38 , pp. 430-445
    • Meher, B.R.1    Wang, Y.2
  • 32
    • 76149114231 scopus 로고    scopus 로고
    • SMILES-based optimal descriptors: QSAR analysis of fullerene-based HIV-1 PR inhibitors by means of balance of correlations
    • Toropov A.A., Toropova A.P., Benfenati E., Leszczynska D., Leszczynski J. SMILES-based optimal descriptors: QSAR analysis of fullerene-based HIV-1 PR inhibitors by means of balance of correlations. J. Comput. Chem. 2010, 31:381-392.
    • (2010) J. Comput. Chem. , vol.31 , pp. 381-392
    • Toropov, A.A.1    Toropova, A.P.2    Benfenati, E.3    Leszczynska, D.4    Leszczynski, J.5
  • 33
    • 0037431964 scopus 로고    scopus 로고
    • Molecular dynamics study of the connection between flap closing and binding of fullerene-based inhibitors of the HIV-1 protease
    • Zhu Z., Schuster D.I., Tuckerman M.E. Molecular dynamics study of the connection between flap closing and binding of fullerene-based inhibitors of the HIV-1 protease. Biochemistry 2003, 42:1326-1333.
    • (2003) Biochemistry , vol.42 , pp. 1326-1333
    • Zhu, Z.1    Schuster, D.I.2    Tuckerman, M.E.3
  • 34
    • 84878023128 scopus 로고    scopus 로고
    • Interactions Between Proteins and Carbon-Based Nanoparticles: Exploring the Origin of Nanotoxicity at the Molecular Level
    • Zuo G., Kang S.-g., Xiu P., Zhao Y., Zhou R. Interactions Between Proteins and Carbon-Based Nanoparticles: Exploring the Origin of Nanotoxicity at the Molecular Level. Small 2013, 9:1546-1556. 10.1002/smll.201201381.
    • (2013) Small , vol.9 , pp. 1546-1556
    • Zuo, G.1    Kang, S.-G.2    Xiu, P.3    Zhao, Y.4    Zhou, R.5
  • 36
    • 41949103776 scopus 로고    scopus 로고
    • Is the mobility of the pore walls and water molecules in the selectivity filter of KcsA channel functionally important?
    • Kraszewski S., Yesylevskyy S.O., Boiteux C., Ramseyer C., Kharkyanen V.N. Is the mobility of the pore walls and water molecules in the selectivity filter of KcsA channel functionally important?. Phys. Chem. Chem. Phys. 2008, 10:2249-2255.
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2249-2255
    • Kraszewski, S.1    Yesylevskyy, S.O.2    Boiteux, C.3    Ramseyer, C.4    Kharkyanen, V.N.5
  • 37
    • 34347371786 scopus 로고    scopus 로고
    • Ion conductance vs. pore gating and selectivity in KcsA channel: modeling achievements and perspectives
    • Boiteux C., Kraszewski S., Ramseyer C., Girardet C. Ion conductance vs. pore gating and selectivity in KcsA channel: modeling achievements and perspectives. J. Mol. Model. 2007, 13:699-713.
    • (2007) J. Mol. Model. , vol.13 , pp. 699-713
    • Boiteux, C.1    Kraszewski, S.2    Ramseyer, C.3    Girardet, C.4
  • 38
    • 0346118922 scopus 로고    scopus 로고
    • Single-walled carbon nanotubes are a new class of ion channel blockers
    • Park K.H., Chhowalla M., Iqbal Z., Sesti F. Single-walled carbon nanotubes are a new class of ion channel blockers. J. Biol. Chem. 2003, 278:50212-50216.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50212-50216
    • Park, K.H.1    Chhowalla, M.2    Iqbal, Z.3    Sesti, F.4
  • 39
    • 77955537865 scopus 로고    scopus 로고
    • Affinity of C60 neat fullerenes with membrane proteins: a computational study on potassium channels
    • Kraszewski S., Tarek M., Treptow W., Ramseyer C. Affinity of C60 neat fullerenes with membrane proteins: a computational study on potassium channels. ACS Nano 2010, 4:4158-4164.
    • (2010) ACS Nano , vol.4 , pp. 4158-4164
    • Kraszewski, S.1    Tarek, M.2    Treptow, W.3    Ramseyer, C.4
  • 42
    • 40949095723 scopus 로고    scopus 로고
    • Single walled carbon nanotubes (SWCNT) affect cell physiology and cell architecture
    • Kaiser J.P., Wick P., Manser P., Spohn P., Bruinink A. Single walled carbon nanotubes (SWCNT) affect cell physiology and cell architecture. J. Mater. Sci. Mater. Med. 2008, 19:1523-1527.
    • (2008) J. Mater. Sci. Mater. Med. , vol.19 , pp. 1523-1527
    • Kaiser, J.P.1    Wick, P.2    Manser, P.3    Spohn, P.4    Bruinink, A.5
  • 43
    • 10044268634 scopus 로고    scopus 로고
    • Effect of single wall carbon nanotubes on human HEK293 cells
    • Cui D.X., Tian F.R., Ozkan C.S., Wang M., Gao H.J. Effect of single wall carbon nanotubes on human HEK293 cells. Toxicol. Lett. 2005, 155:73-85.
    • (2005) Toxicol. Lett. , vol.155 , pp. 73-85
    • Cui, D.X.1    Tian, F.R.2    Ozkan, C.S.3    Wang, M.4    Gao, H.J.5
  • 46
    • 43649093128 scopus 로고    scopus 로고
    • Microtubule architecture: inspiration for novel carbon nanotube-based biomimetic materials
    • Pampaloni F., Florin E.L. Microtubule architecture: inspiration for novel carbon nanotube-based biomimetic materials. Trends Biotechnol. 2008, 26:302-310.
    • (2008) Trends Biotechnol. , vol.26 , pp. 302-310
    • Pampaloni, F.1    Florin, E.L.2
  • 47
    • 60949091201 scopus 로고    scopus 로고
    • Tubulin encapsulation of carbon nanotubes into functional hybrid assemblies
    • Dinu C.Z., Bale S.S., Zhu G.Y., Dordick J.S. Tubulin encapsulation of carbon nanotubes into functional hybrid assemblies. Small 2009, 5:310-315.
    • (2009) Small , vol.5 , pp. 310-315
    • Dinu, C.Z.1    Bale, S.S.2    Zhu, G.Y.3    Dordick, J.S.4
  • 52
    • 33845667408 scopus 로고    scopus 로고
    • Single-walled carbon nanotube (SWCNT)-induced interstitial fibrosis in the lungs of rats is associated with increased levels of PDGF mRNA and the formation of unique intercellular carbon structures that bridge alveolar macrophages in situ
    • Mangum J.B., Turpin E.A., Antao-Menezes A., Cesta M.F., Bermudez E., Bonner J.C. Single-walled carbon nanotube (SWCNT)-induced interstitial fibrosis in the lungs of rats is associated with increased levels of PDGF mRNA and the formation of unique intercellular carbon structures that bridge alveolar macrophages in situ. Part. Fibre Toxicol. 2006, 3:15.
    • (2006) Part. Fibre Toxicol. , vol.3 , pp. 15
    • Mangum, J.B.1    Turpin, E.A.2    Antao-Menezes, A.3    Cesta, M.F.4    Bermudez, E.5    Bonner, J.C.6
  • 54
    • 84888881164 scopus 로고    scopus 로고
    • The cell as a collection of protein machines
    • Alberts B. The cell as a collection of protein machines. Biofutur 1998, 42-44.
    • (1998) Biofutur , pp. 42-44
    • Alberts, B.1
  • 55
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 1998, 92:291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 57
    • 34247222694 scopus 로고    scopus 로고
    • Visualizing the uptake of C-60 to the cytoplasm and nucleaus of human monocyte-derived macrophage cells using energy-filtered transmission electron microscopy and electron tomography
    • Porter A.E., Gass M., Muller K., Skepper J.N., Midgley P., Welland M. Visualizing the uptake of C-60 to the cytoplasm and nucleaus of human monocyte-derived macrophage cells using energy-filtered transmission electron microscopy and electron tomography. Environ. Sci. Technol. 2007, 41:3012-3017.
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 3012-3017
    • Porter, A.E.1    Gass, M.2    Muller, K.3    Skepper, J.N.4    Midgley, P.5    Welland, M.6
  • 58
    • 34547094848 scopus 로고    scopus 로고
    • Functionalized fullerenes mediate photodynamic killing of cancer cells: type I versus type II photochemical mechanism
    • Mroz P., Pawlak A., Satti M., Lee H., Wharton T., Gali H., Sarna T., Hamblin M.R. Functionalized fullerenes mediate photodynamic killing of cancer cells: type I versus type II photochemical mechanism. Free Radic. Biol. Med. 2007, 43:711-719.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 711-719
    • Mroz, P.1    Pawlak, A.2    Satti, M.3    Lee, H.4    Wharton, T.5    Gali, H.6    Sarna, T.7    Hamblin, M.R.8
  • 60
    • 33744780459 scopus 로고    scopus 로고
    • Uptake of C60 by human monocyte macrophages, its localization and implications for toxicity: studied by high resolution electron microscopy and electron tomography
    • Porter A.E., Muller K., Skepper J., Midgley P., Welland M. Uptake of C60 by human monocyte macrophages, its localization and implications for toxicity: studied by high resolution electron microscopy and electron tomography. Acta Biomater. 2006, 2:409-419.
    • (2006) Acta Biomater. , vol.2 , pp. 409-419
    • Porter, A.E.1    Muller, K.2    Skepper, J.3    Midgley, P.4    Welland, M.5
  • 61
    • 4344671232 scopus 로고    scopus 로고
    • Simulation of DNA-nanotube interactions
    • Gao H.J., Kong Y. Simulation of DNA-nanotube interactions. Annu. Rev. Mater. Res. 2004, 34:123-150.
    • (2004) Annu. Rev. Mater. Res. , vol.34 , pp. 123-150
    • Gao, H.J.1    Kong, Y.2
  • 63
    • 31144459816 scopus 로고    scopus 로고
    • AFM imaging of wrapped multiwall carbon nanotube in DNA
    • Takahashi H., Numao S., Bandow S., Iijima S. AFM imaging of wrapped multiwall carbon nanotube in DNA. Chem. Phys. Lett. 2006, 418:535-539.
    • (2006) Chem. Phys. Lett. , vol.418 , pp. 535-539
    • Takahashi, H.1    Numao, S.2    Bandow, S.3    Iijima, S.4
  • 65
    • 58549095468 scopus 로고    scopus 로고
    • Fullerene (C-60) forms stable complex with nucleic acid base guanine
    • Shukla M.K., Leszczynski J. Fullerene (C-60) forms stable complex with nucleic acid base guanine. Chem. Phys. Lett. 2009, 469:207-209.
    • (2009) Chem. Phys. Lett. , vol.469 , pp. 207-209
    • Shukla, M.K.1    Leszczynski, J.2
  • 66
    • 84870479153 scopus 로고    scopus 로고
    • A large-scale association study for nanoparticle C60 uncovers mechanisms of nanotoxicity disrupting the native conformations of DNA/RNA
    • Xu X., Wang X., Li Y., Wang Y., Yang L. A large-scale association study for nanoparticle C60 uncovers mechanisms of nanotoxicity disrupting the native conformations of DNA/RNA. Nucleic Acids Res. 2012, 40:7622-7632.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 7622-7632
    • Xu, X.1    Wang, X.2    Li, Y.3    Wang, Y.4    Yang, L.5
  • 67
    • 63649139652 scopus 로고    scopus 로고
    • Free energy landscape of a DNA-carbon nanotube hybrid using replica exchange molecular dynamics
    • Johnson R.R., Kohlmeyer A., Johnson A.T., Klein M.L. Free energy landscape of a DNA-carbon nanotube hybrid using replica exchange molecular dynamics. Nano Lett. 2009, 9:537-541.
    • (2009) Nano Lett. , vol.9 , pp. 537-541
    • Johnson, R.R.1    Kohlmeyer, A.2    Johnson, A.T.3    Klein, M.L.4
  • 70
    • 0002990922 scopus 로고    scopus 로고
    • Functionalization of carbon nanotubes for biocompatibility and biomolecular recognition
    • Shim M., Kam N.W.S., Chen R.J., Li Y.M., Dai H.J. Functionalization of carbon nanotubes for biocompatibility and biomolecular recognition. Nano Lett. 2002, 2:285-288.
    • (2002) Nano Lett. , vol.2 , pp. 285-288
    • Shim, M.1    Kam, N.W.S.2    Chen, R.J.3    Li, Y.M.4    Dai, H.J.5
  • 71
    • 82155170573 scopus 로고    scopus 로고
    • Adsorption of villin headpiece onto graphene, carbon nanotube, and C60: effect of contacting surface curvatures on binding affinity
    • Zuo G., Zhou X., Huang Q., Fang H.P., Zhou R.H. Adsorption of villin headpiece onto graphene, carbon nanotube, and C60: effect of contacting surface curvatures on binding affinity. J. Phys. Chem. C 2011, 115:23323-23328.
    • (2011) J. Phys. Chem. C , vol.115 , pp. 23323-23328
    • Zuo, G.1    Zhou, X.2    Huang, Q.3    Fang, H.P.4    Zhou, R.H.5
  • 72
    • 84865790649 scopus 로고    scopus 로고
    • How do proteins unfold upon adsorption on nanoparticle surfaces?
    • Pan H., Qin M., Meng W., Cao Y., Wang W. How do proteins unfold upon adsorption on nanoparticle surfaces?. Langmuir 2012, 28:12779-12787.
    • (2012) Langmuir , vol.28 , pp. 12779-12787
    • Pan, H.1    Qin, M.2    Meng, W.3    Cao, Y.4    Wang, W.5
  • 73
    • 36649017886 scopus 로고    scopus 로고
    • Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
    • Asuri P., Bale S.S., Pangule R.C., Shah D.A., Kane R.S., Dordick J.S. Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes. Langmuir 2007, 23:12318-12321.
    • (2007) Langmuir , vol.23 , pp. 12318-12321
    • Asuri, P.1    Bale, S.S.2    Pangule, R.C.3    Shah, D.A.4    Kane, R.S.5    Dordick, J.S.6
  • 74
    • 84876711391 scopus 로고    scopus 로고
    • Amphiphilic amino acids: a key to adsorbing proteins to nanopatterned surfaces?
    • Hung A., Mager M., Hembury M., Stellacci F., Stevens M.M., Yarovsky I. Amphiphilic amino acids: a key to adsorbing proteins to nanopatterned surfaces?. Chem. Sci. 2013, 4:928-937.
    • (2013) Chem. Sci. , vol.4 , pp. 928-937
    • Hung, A.1    Mager, M.2    Hembury, M.3    Stellacci, F.4    Stevens, M.M.5    Yarovsky, I.6
  • 75
    • 84871807890 scopus 로고    scopus 로고
    • Non-destructive inhibition of metallofullerenol Gd@C(82)(OH)(22) on WW domain: implication on signal transduction pathway
    • Kang S.G., Huynh T., Zhou R. Non-destructive inhibition of metallofullerenol Gd@C(82)(OH)(22) on WW domain: implication on signal transduction pathway. Sci. Rep. 2012, 2:957.
    • (2012) Sci. Rep. , vol.2 , pp. 957
    • Kang, S.G.1    Huynh, T.2    Zhou, R.3
  • 76
    • 84875773487 scopus 로고    scopus 로고
    • Binding preference of carbon nanotube over proline-rich motif ligand on SH3-domain: a comparison with different force fields
    • Shi B., Zuo G., Xiu P., Zhou R. Binding preference of carbon nanotube over proline-rich motif ligand on SH3-domain: a comparison with different force fields. J. Phys. Chem. B 2013, 117:3541-3547.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 3541-3547
    • Shi, B.1    Zuo, G.2    Xiu, P.3    Zhou, R.4
  • 77
    • 80052581373 scopus 로고    scopus 로고
    • Differential nano-bio interactions and toxicity effects of pristine versus functionalized graphene
    • Sasidharan A., Panchakarla L.S., Chandran P., Menon D., Nair S., Rao C.N., Koyakutty M. Differential nano-bio interactions and toxicity effects of pristine versus functionalized graphene. Nanoscale 2011, 3:2461-2464.
    • (2011) Nanoscale , vol.3 , pp. 2461-2464
    • Sasidharan, A.1    Panchakarla, L.S.2    Chandran, P.3    Menon, D.4    Nair, S.5    Rao, C.N.6    Koyakutty, M.7
  • 79
    • 78650754795 scopus 로고    scopus 로고
    • Plugging into proteins: poisoning protein function by a hydrophobic nanoparticle
    • Zuo G., Huang Q., Wei G., Zhou R., Fang H. Plugging into proteins: poisoning protein function by a hydrophobic nanoparticle. ACS Nano 2010, 4:7508-7514.
    • (2010) ACS Nano , vol.4 , pp. 7508-7514
    • Zuo, G.1    Huang, Q.2    Wei, G.3    Zhou, R.4    Fang, H.5
  • 80
    • 84886024673 scopus 로고    scopus 로고
    • Metallofullerenol Gd@C(8)(2)(OH)(2)(2) distracts the proline-rich-motif from putative binding on the SH3 domain
    • Kang S.G., Huynh T., Zhou R. Metallofullerenol Gd@C(8)(2)(OH)(2)(2) distracts the proline-rich-motif from putative binding on the SH3 domain. Nanoscale 2013, 5:2703-2712.
    • (2013) Nanoscale , vol.5 , pp. 2703-2712
    • Kang, S.G.1    Huynh, T.2    Zhou, R.3
  • 81
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • Lundqvist M., Stigler J., Elia G., Lynch I., Cedervall T., Dawson K.A. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:14265-14270.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14265-14270
    • Lundqvist, M.1    Stigler, J.2    Elia, G.3    Lynch, I.4    Cedervall, T.5    Dawson, K.A.6
  • 84
    • 56449122424 scopus 로고    scopus 로고
    • The influence of protein adsorption on nanoparticle association with cultured endothelial cells
    • Ehrenberg M.S., Friedman A.E., Finkelstein J.N., Oberdorster G., McGrath J.L. The influence of protein adsorption on nanoparticle association with cultured endothelial cells. Biomaterials 2009, 30:603-610.
    • (2009) Biomaterials , vol.30 , pp. 603-610
    • Ehrenberg, M.S.1    Friedman, A.E.2    Finkelstein, J.N.3    Oberdorster, G.4    McGrath, J.L.5
  • 85
    • 84873853768 scopus 로고    scopus 로고
    • Biomolecular coronas provide the biological identity of nanosized materials
    • Monopoli M.P., Aberg C., Salvati A., Dawson K.A. Biomolecular coronas provide the biological identity of nanosized materials. Nat. Nanotechnol. 2012, 7:779-786.
    • (2012) Nat. Nanotechnol. , vol.7 , pp. 779-786
    • Monopoli, M.P.1    Aberg, C.2    Salvati, A.3    Dawson, K.A.4
  • 86
    • 84883887168 scopus 로고    scopus 로고
    • Effects of particle size and surface modification on cellular uptake and biodistribution of polymeric nanoparticles for drug delivery
    • Kulkarni S.A., Feng S.S. Effects of particle size and surface modification on cellular uptake and biodistribution of polymeric nanoparticles for drug delivery. Pharm. Res. 2013, 10.1007/s11095-012-0958-3.
    • (2013) Pharm. Res.
    • Kulkarni, S.A.1    Feng, S.S.2
  • 87
    • 33751519372 scopus 로고    scopus 로고
    • Oxidized phosphatidylserine-CD36 interactions play an essential role in macrophage-dependent phagocytosis of apoptotic cells
    • Greenberg M.E., Sun M., Zhang R., Febbraio M., Silverstein R., Hazen S.L. Oxidized phosphatidylserine-CD36 interactions play an essential role in macrophage-dependent phagocytosis of apoptotic cells. J. Exp. Med. 2006, 203:2613-2625.
    • (2006) J. Exp. Med. , vol.203 , pp. 2613-2625
    • Greenberg, M.E.1    Sun, M.2    Zhang, R.3    Febbraio, M.4    Silverstein, R.5    Hazen, S.L.6
  • 91
    • 80052200967 scopus 로고    scopus 로고
    • Enzymatic degradation of multiwalled carbon nanotubes
    • Zhao Y., Allen B.L., Star A. Enzymatic degradation of multiwalled carbon nanotubes. J. Phys. Chem. A 2011, 115:9536-9544.
    • (2011) J. Phys. Chem. A , vol.115 , pp. 9536-9544
    • Zhao, Y.1    Allen, B.L.2    Star, A.3
  • 92
    • 79960199378 scopus 로고    scopus 로고
    • Fullerene sorting proteins
    • Calvaresi M., Zerbetto F. Fullerene sorting proteins. Nanoscale 2011, 3:2873-2881.
    • (2011) Nanoscale , vol.3 , pp. 2873-2881
    • Calvaresi, M.1    Zerbetto, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.