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Volumn 7, Issue , 2016, Pages

Protein-targeted corona phase molecular recognition

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA 2 MACROGLOBULIN; APOLIPOPROTEIN A1; C REACTIVE PROTEIN; FIBRINOGEN; HAPTOGLOBIN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN M; SINGLE WALLED NANOTUBE; TRANSFERRIN; CARBON NANOTUBE; PLASMA PROTEIN; POLYMER; PROTEIN CORONA;

EID: 84953896950     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10241     Document Type: Article
Times cited : (175)

References (70)
  • 1
    • 0031191655 scopus 로고    scopus 로고
    • Signaling recognition events with fluorescent sensors and switches
    • de Silva, A. P. et al. Signaling recognition events with fluorescent sensors and switches. Chem. Rev. 97, 1515-1566 (1997).
    • (1997) Chem. Rev , vol.97 , pp. 1515-1566
    • De Silva, A.P.1
  • 2
    • 0035801512 scopus 로고    scopus 로고
    • Sensing a paradigm shift in the field of molecular recognition: From selective to differential receptors
    • Lavigne, J. J. & Anslyn, E. V. Sensing a paradigm shift in the field of molecular recognition: from selective to differential receptors. Angew. Chem. Int. Ed. 40, 3118-3130 (2001).
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 3118-3130
    • Lavigne, J.J.1    Anslyn, E.V.2
  • 3
    • 0037450936 scopus 로고    scopus 로고
    • Imprinted polymers: Artificial molecular recognition materials with applications in synthesis and catalysis
    • Alexander, C., Davidson, L. & Hayes, W. Imprinted polymers: artificial molecular recognition materials with applications in synthesis and catalysis. Tetrahedron 59, 2025-2057 (2003).
    • (2003) Tetrahedron , vol.59 , pp. 2025-2057
    • Alexander, C.1    Davidson, L.2    Hayes, W.3
  • 4
    • 41949093553 scopus 로고    scopus 로고
    • Directed assembly metallocyclic supramolecular systems for molecular recognition and chemical sensing. Coord
    • Kumar, A., Sun, S.-S. & Lees, A. J. Directed assembly metallocyclic supramolecular systems for molecular recognition and chemical sensing. Coord. Chem. Rev. 252, 922-939 (2008).
    • (2008) Chem. Rev , vol.252 , pp. 922-939
    • Kumar, A.1    Sun, S.-S.2    Lees, A.J.3
  • 6
    • 76649107349 scopus 로고    scopus 로고
    • Large-Area spatially ordered arrays of gold nanoparticles directed by lithographically confined DNA origami
    • Hung, A. M. et al. Large-Area spatially ordered arrays of gold nanoparticles directed by lithographically confined DNA origami. Nat. Nano 5, 121-126 (2010).
    • (2010) Nat. Nano , vol.5 , pp. 121-126
    • Hung, A.M.1
  • 7
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler, G. & Milstein, C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495-497 (1975).
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 8
    • 28444484636 scopus 로고    scopus 로고
    • Aptamers-basic research, drug development, and clinical applications
    • Proske, D., Blank, M., Buhmann, R. & Resch, A. Aptamers-basic research, drug development, and clinical applications. Appl. Microbiol. Biotechnol. 69, 367-374 (2005).
    • (2005) Appl. Microbiol. Biotechnol , vol.69 , pp. 367-374
    • Proske, D.1    Blank, M.2    Buhmann, R.3    Resch, A.4
  • 9
    • 0028873867 scopus 로고
    • Molecular imprinting in cross-linked materials with the aid of molecular templates- a way towards artificial antibodies
    • Wulff, G. Molecular imprinting in cross-linked materials with the aid of molecular templates- a way towards artificial antibodies. Angew. Chem. Int. Ed. 34, 1812-1832 (1995).
    • (1995) Angew. Chem. Int. Ed , vol.34 , pp. 1812-1832
    • Wulff, G.1
  • 10
    • 79954579317 scopus 로고    scopus 로고
    • Recent advances in molecular imprinting technology: Current status, challenges and highlighted applications
    • Chen, L., Xu, S. & Li, J. Recent advances in molecular imprinting technology: current status, challenges and highlighted applications. Chem. Soc. Rev. 40, 2922-2942 (2011).
    • (2011) Chem. Soc. Rev , vol.40 , pp. 2922-2942
    • Chen, L.1    Xu, S.2    Li, J.3
  • 11
    • 84920670201 scopus 로고    scopus 로고
    • A pharmacokinetic model of a tissue implantable insulin sensor
    • Bisker, G., Iverson, N. M., Ahn, J. & Strano, M. S. A pharmacokinetic model of a tissue implantable insulin sensor. Adv. Healthc. Mater. 4, 87-97 (2015).
    • (2015) Adv. Healthc. Mater , vol.4 , pp. 87-97
    • Bisker, G.1    Iverson, N.M.2    Ahn, J.3    Strano, M.S.4
  • 12
    • 84898852234 scopus 로고    scopus 로고
    • Recent advances in molecular recognition based on nanoengineered platforms
    • Mu, B. et al. Recent advances in molecular recognition based on nanoengineered platforms. Acc. Chem. Res. 47, 979-988 (2014).
    • (2014) Acc. Chem. Res , vol.47 , pp. 979-988
    • Mu, B.1
  • 13
    • 84888865228 scopus 로고    scopus 로고
    • Carbon nanotubes as optical biomedical sensors
    • Kruss, S. et al. Carbon nanotubes as optical biomedical sensors. Adv. Drug Deliv. Rev. 65, 1933-1950 (2013).
    • (2013) Adv. Drug Deliv. Rev , vol.65 , pp. 1933-1950
    • Kruss, S.1
  • 14
    • 84907487586 scopus 로고    scopus 로고
    • Experimental tools to study molecular recognition within the nanoparticle corona
    • Landry, M. et al. Experimental tools to study molecular recognition within the nanoparticle corona. Sensors 14, 16196-16211 (2014).
    • (2014) Sensors , vol.14 , pp. 16196-16211
    • Landry, M.1
  • 15
    • 84888386417 scopus 로고    scopus 로고
    • In vivo biosensing via tissue-localizable near-infraredfluorescent single-walled carbon nanotubes
    • Iverson, N. M. et al. In vivo biosensing via tissue-localizable near-infraredfluorescent single-walled carbon nanotubes. Nat. Nano 8, 873-880 (2013).
    • (2013) Nat. Nano , vol.8 , pp. 873-880
    • Iverson, N.M.1
  • 16
    • 84890446448 scopus 로고    scopus 로고
    • Molecular recognition using corona phase complexes made of synthetic polymers adsorbed on carbon nanotubes
    • Zhang, J. et al. Molecular recognition using corona phase complexes made of synthetic polymers adsorbed on carbon nanotubes. Nat. Nano 8, 959-968 (2013).
    • (2013) Nat. Nano , vol.8 , pp. 959-968
    • Zhang, J.1
  • 17
    • 84892686766 scopus 로고    scopus 로고
    • Neurotransmitter detection using corona phase molecular recognition on fluorescent single-walled carbon nanotube sensors
    • Kruss, S. et al. Neurotransmitter detection using corona phase molecular recognition on fluorescent single-walled carbon nanotube sensors. J. Am. Chem. Soc. 136, 713-724 (2013).
    • (2013) J. Am. Chem. Soc , vol.136 , pp. 713-724
    • Kruss, S.1
  • 18
    • 70449574483 scopus 로고    scopus 로고
    • A route to brightly fluorescent carbon nanotubes for nearinfrared imaging in mice
    • Welsher, K. et al. A route to brightly fluorescent carbon nanotubes for nearinfrared imaging in mice. Nat. Nano 4, 773-780 (2009).
    • (2009) Nat. Nano , vol.4 , pp. 773-780
    • Welsher, K.1
  • 19
    • 84939562328 scopus 로고    scopus 로고
    • A ratiometric sensor using single chirality near-infrared fluorescent carbon nanotubes: Application to in vivo monitoring
    • Giraldo, J. P. et al. A ratiometric sensor using single chirality near-infrared fluorescent carbon nanotubes: application to in vivo monitoring. Small 11, 3973-3984 (2015).
    • (2015) Small , vol.11 , pp. 3973-3984
    • Giraldo, J.P.1
  • 20
    • 84943541556 scopus 로고    scopus 로고
    • Protein functionalized carbon nanomaterials for biomedical applications
    • Oliveira, S. F. et al. Protein functionalized carbon nanomaterials for biomedical applications. Carbon 95, 767-779 (2015).
    • (2015) Carbon , vol.95 , pp. 767-779
    • Oliveira, S.F.1
  • 21
    • 84946240356 scopus 로고    scopus 로고
    • 2d equation-of-state model for corona phase molecular recognition on singlewalled carbon nanotube and graphene surfaces
    • Ulissi, Z. W., Zhang, J., Sresht, V., Blankschtein, D. & Strano, M. S. 2D equation-of-state model for corona phase molecular recognition on singlewalled carbon nanotube and graphene surfaces. Langmuir 31, 628-636 (2014).
    • (2014) Langmuir , vol.31 , pp. 628-636
    • Ulissi, Z.W.1    Zhang, J.2    Sresht, V.3    Blankschtein, D.4    Strano, M.S.5
  • 22
    • 0032860385 scopus 로고    scopus 로고
    • Aptamers: An emerging class of molecules that rival antibodies in diagnostics
    • Jayasena, S. D. Aptamers: an emerging class of molecules that rival antibodies in diagnostics. Clin. Chem. 45, 1628-1650 (1999).
    • (1999) Clin. Chem , vol.45 , pp. 1628-1650
    • Jayasena, S.D.1
  • 23
    • 84934983330 scopus 로고    scopus 로고
    • A mathematical formulation and solution of the cophmore inverse problem for helically wrapping polymer corona phases on cylindrical substrates
    • Bisker, G. et al. A mathematical formulation and solution of the cophmore inverse problem for helically wrapping polymer corona phases on cylindrical substrates. J Phys. Chem. C 119, 13876-13886 (2015).
    • (2015) J Phys. Chem. C , vol.119 , pp. 13876-13886
    • Bisker, G.1
  • 24
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: The long and uncertain path to clinical utility
    • Rifai, N., Gillette, M. A. & Carr, S. A. Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat. Biotech. 24, 971-983 (2006).
    • (2006) Nat. Biotech , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 25
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L. & Hunter, C. L. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteom. 5, 573-588 (2006).
    • (2006) Mol. Cell. Proteom , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 26
    • 41649100689 scopus 로고    scopus 로고
    • Mining the plasma proteome for cancer biomarkers
    • Hanash, S. M., Pitteri, S. J. & Faca, V. M. Mining the plasma proteome for cancer biomarkers. Nature 452, 571-579 (2008).
    • (2008) Nature , vol.452 , pp. 571-579
    • Hanash, S.M.1    Pitteri, S.J.2    Faca, V.M.3
  • 27
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L. & Anderson, N. G. The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteom. 1, 845-867 (2002).
    • (2002) Mol. Cell. Proteom , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 28
    • 27144513329 scopus 로고    scopus 로고
    • Multiplexed electrical detection of cancer markers with nanowire sensor arrays
    • Zheng, G., Patolsky, F., Cui, Y., Wang, W. U. & Lieber, C. M. Multiplexed electrical detection of cancer markers with nanowire sensor arrays. Nat. Biotech. 23, 1294-1301 (2005).
    • (2005) Nat. Biotech , vol.23 , pp. 1294-1301
    • Zheng, G.1    Patolsky, F.2    Cui, Y.3    Wang, W.U.4    Lieber, C.M.5
  • 29
    • 70349897865 scopus 로고    scopus 로고
    • Quantitative and qualitative evaluation of adsorption/desorption of bovine serum albumin on hydrophilic and hydrophobic surfaces
    • Jeyachandran, Y. L., Mielczarski, E., Rai, B. & Mielczarski, J. A. Quantitative and qualitative evaluation of adsorption/desorption of bovine serum albumin on hydrophilic and hydrophobic surfaces. Langmuir 25, 11614-11620 (2009).
    • (2009) Langmuir , vol.25 , pp. 11614-11620
    • Jeyachandran, Y.L.1    Mielczarski, E.2    Rai, B.3    Mielczarski, J.A.4
  • 30
    • 1842530289 scopus 로고    scopus 로고
    • A new interpretation of serum albumin surface passivation
    • Sweryda-Krawiec, B., Devaraj, H., Jacob, G. & Hickman, J. J. A new interpretation of serum albumin surface passivation. Langmuir 20, 2054-2056 (2004).
    • (2004) Langmuir , vol.20 , pp. 2054-2056
    • Sweryda-Krawiec, B.1    Devaraj, H.2    Jacob, G.3    Hickman, J.J.4
  • 31
    • 79951624828 scopus 로고    scopus 로고
    • Highresolution visualization of fibrinogen molecules and fibrin fibers with atomic force microscopy
    • Yermolenko, I. S., Lishko, V. K., Ugarova, T. P. & Magonov, S. N. Highresolution visualization of fibrinogen molecules and fibrin fibers with atomic force microscopy. Biomacromolecules 12, 370-379 (2010).
    • (2010) Biomacromolecules , vol.12 , pp. 370-379
    • Yermolenko, I.S.1    Lishko, V.K.2    Ugarova, T.P.3    Magonov, S.N.4
  • 32
    • 9644254415 scopus 로고    scopus 로고
    • The thrombin-fibrinogen interaction
    • Scheraga, H. A. The thrombin-fibrinogen interaction. Biophys. Chem. 112, 117-130 (2004).
    • (2004) Biophys. Chem , vol.112 , pp. 117-130
    • Scheraga, H.A.1
  • 33
    • 84928950400 scopus 로고    scopus 로고
    • Comparative dynamics and sequence dependence of DNA and RNA binding to single walled carbon nanotubes
    • Landry, M. P. et al. Comparative dynamics and sequence dependence of DNA and RNA binding to single walled carbon nanotubes. J. Phys. Chem. C 119, 10048-10058 (2015).
    • (2015) J. Phys. Chem. C , vol.119 , pp. 10048-10058
    • Landry, M.P.1
  • 34
    • 15544375926 scopus 로고    scopus 로고
    • Band gap fluorescence from individual single-walled carbon nanotubes
    • O'Connell, M. J. et al. Band gap fluorescence from individual single-walled carbon nanotubes. Science 297, 593-596 (2002).
    • (2002) Science , vol.297 , pp. 593-596
    • O'Connell, M.J.1
  • 35
    • 18244392180 scopus 로고    scopus 로고
    • The optical resonances in carbon nanotubes arise from excitons
    • Wang, F., Dukovic, G., Brus, L. E. & Heinz, T. F. The optical resonances in carbon nanotubes arise from excitons. Science 308, 838-841 (2005).
    • (2005) Science , vol.308 , pp. 838-841
    • Wang, F.1    Dukovic, G.2    Brus, L.E.3    Heinz, T.F.4
  • 36
    • 34249897738 scopus 로고    scopus 로고
    • Solvatochromism in single-walled carbon nanotubes
    • Choi, J. H. & Strano, M. S. Solvatochromism in single-walled carbon nanotubes. Appl. Phys. Lett. 90, 223114 (2007).
    • (2007) Appl. Phys. Lett , vol.90 , pp. 223114
    • Choi, J.H.1    Strano, M.S.2
  • 37
    • 84874407600 scopus 로고    scopus 로고
    • A kinetic model for the deterministic prediction of gel-based single-chirality single-walled carbon nanotube separation
    • Tvrdy, K. et al. A kinetic model for the deterministic prediction of gel-based single-chirality single-walled carbon nanotube separation. ACS Nano 7, 1779-1789 (2013).
    • (2013) ACS Nano , vol.7 , pp. 1779-1789
    • Tvrdy, K.1
  • 38
    • 84867815939 scopus 로고    scopus 로고
    • A structure-function relationship for the optical modulation of phenyl boronic acid-grafted, polyethylene glycol-wrapped single-walled carbon nanotubes
    • Mu, B. et al. A structure-function relationship for the optical modulation of phenyl boronic acid-grafted, polyethylene glycol-wrapped single-walled carbon nanotubes. J. Am. Chem. Soc. 134, 17620-17627 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 17620-17627
    • Mu, B.1
  • 39
    • 84882264768 scopus 로고    scopus 로고
    • Charge transfer structurereactivity dependence of fullerene-single-walled carbon nanotube heterojunctions
    • Hilmer, A. J., Tvrdy, K., Zhang, J. & Strano, M. S. Charge transfer structurereactivity dependence of fullerene-single-walled carbon nanotube heterojunctions. J. Am. Chem. Soc. 135, 11901-11910 (2013).
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 11901-11910
    • Hilmer, A.J.1    Tvrdy, K.2    Zhang, J.3    Strano, M.S.4
  • 40
    • 31544453347 scopus 로고    scopus 로고
    • Optical detection of DNA conformational polymorphism on single-walled carbon nanotubes
    • Heller, D. A. et al. Optical detection of DNA conformational polymorphism on single-walled carbon nanotubes. Science 311, 508-511 (2006).
    • (2006) Science , vol.311 , pp. 508-511
    • Heller, D.A.1
  • 45
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • Mosesson, M. W. Fibrinogen and fibrin structure and functions. J. Thromb. Haemost. 3, 1894-1904 (2005).
    • (2005) J. Thromb. Haemost , vol.3 , pp. 1894-1904
    • Mosesson, M.W.1
  • 46
    • 20444421544 scopus 로고    scopus 로고
    • Interpretation of protein adsorption: Surface-induced conformational changes
    • Roach, P., Farrar, D. & Perry, C. C. Interpretation of protein adsorption: surface-induced conformational changes. J. Am. Chem. Soc. 127, 8168-8173 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 47
    • 84945409784 scopus 로고    scopus 로고
    • Chirality dependent corona phase molecular recognition of DNA-wrapped carbon nanotubes
    • Salem, D. P. et al. Chirality dependent corona phase molecular recognition of DNA-wrapped carbon nanotubes. Carbon 97, 147-153 (2016).
    • (2016) Carbon , vol.97 , pp. 147-153
    • Salem, D.P.1
  • 48
    • 20144389731 scopus 로고    scopus 로고
    • Spectroscopy of single-And double-wall carbon nanotubes in different environments
    • Hertel, T. et al. Spectroscopy of single-And double-wall carbon nanotubes in different environments. Nano Lett. 5, 511-514 (2005).
    • (2005) Nano Lett , vol.5 , pp. 511-514
    • Hertel, T.1
  • 49
    • 0037147175 scopus 로고    scopus 로고
    • Structure-Assigned optical spectra of single-walled carbon nanotubes
    • Bachilo, S. M. et al. Structure-Assigned optical spectra of single-walled carbon nanotubes. Science 298, 2361-2366 (2002).
    • (2002) Science , vol.298 , pp. 2361-2366
    • Bachilo, S.M.1
  • 50
    • 0030768931 scopus 로고    scopus 로고
    • The hill equation revisited: Uses and misuses
    • Weiss, J. N. The Hill equation revisited: uses and misuses. FASEB J. 11, 835-841 (1997).
    • (1997) FASEB J , vol.11 , pp. 835-841
    • Weiss, J.N.1
  • 51
    • 36849008599 scopus 로고    scopus 로고
    • Excitonic transition energies in single-walled carbon nanotubes: Dependence on environmental dielectric constant
    • Ohno, Y. et al. Excitonic transition energies in single-walled carbon nanotubes: dependence on environmental dielectric constant. Phys. Status Solidi (b) 244, 4002-4005 (2007).
    • (2007) Phys. Status Solidi (B) , vol.244 , pp. 4002-4005
    • Ohno, Y.1
  • 52
    • 84874938533 scopus 로고    scopus 로고
    • Effect of medium dielectric constant on the physical properties of single-walled carbon nanotubes
    • Gao, J., Gomulya, W. & Loi, M. A. Effect of medium dielectric constant on the physical properties of single-walled carbon nanotubes. Chem. Phys. 413, 35-38 (2013).
    • (2013) Chem. Phys , vol.413 , pp. 35-38
    • Gao, J.1    Gomulya, W.2    Loi, M.A.3
  • 53
    • 11144314296 scopus 로고    scopus 로고
    • Near-infrared optical sensors based on single-walled carbon nanotubes
    • Barone, P. W., Baik, S., Heller, D. A. & Strano, M. S. Near-infrared optical sensors based on single-walled carbon nanotubes. Nat. Mater. 4, 86-92 (2005).
    • (2005) Nat. Mater , vol.4 , pp. 86-92
    • Barone, P.W.1    Baik, S.2    Heller, D.A.3    Strano, M.S.4
  • 54
    • 1042269718 scopus 로고    scopus 로고
    • Review article: Albumin as a drug-biological effects of albumin unrelated to oncotic pressure
    • Evans, T. W. Review article: albumin as a drug-biological effects of albumin unrelated to oncotic pressure. Aliment. Pharmacol. Ther. 16, 6-11 (2002).
    • (2002) Aliment. Pharmacol. Ther , vol.16 , pp. 6-11
    • Evans, T.W.1
  • 55
    • 84925655077 scopus 로고    scopus 로고
    • Selective assembly of DNA-conjugated single-walled carbon nanotubes from the vascular secretome
    • Gong, X., Sharma, A. K., Strano, M. S. & Mukhopadhyay, D. Selective assembly of DNA-conjugated single-walled carbon nanotubes from the vascular secretome. ACS Nano 8, 9126-9136 (2014).
    • (2014) ACS Nano , vol.8 , pp. 9126-9136
    • Gong, X.1    Sharma, A.K.2    Strano, M.S.3    Mukhopadhyay, D.4
  • 56
    • 34249893994 scopus 로고    scopus 로고
    • Mammalian pharmacokinetics of carbon nanotubes using intrinsic near-infrared fluorescence
    • Cherukuri, P. et al. Mammalian pharmacokinetics of carbon nanotubes using intrinsic near-infrared fluorescence. Proc. Natl Acad. Sci. 103, 18882-18886 (2006).
    • (2006) Proc. Natl Acad. Sci , vol.103 , pp. 18882-18886
    • Cherukuri, P.1
  • 57
    • 0006018892 scopus 로고
    • A circular dichroism technique for the study of adsorbed protein structure
    • McMillin, C. R. & Walton, A. G. A circular dichroism technique for the study of adsorbed protein structure. J. Colloid Interface Sci. 48, 345-349 (1974).
    • (1974) J. Colloid Interface Sci , vol.48 , pp. 345-349
    • McMillin, C.R.1    Walton, A.G.2
  • 58
    • 0016169865 scopus 로고
    • Determination of the helix and b form of proteins in aqueous solution by circular dichroism
    • Chen, Y.-H., Yang, J. T. & Chau, K. H. Determination of the helix and b form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359 (1974).
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 59
    • 33746063216 scopus 로고    scopus 로고
    • Racemic single-walled carbon nanotubes exhibit circular dichroism when wrapped with DNA
    • Dukovic, G. et al. Racemic single-walled carbon nanotubes exhibit circular dichroism when wrapped with DNA. J. Am. Chem. Soc. 128, 9004-9005 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 9004-9005
    • Dukovic, G.1
  • 60
    • 84869441941 scopus 로고    scopus 로고
    • Structure and function of glucose binding proteinsingle walled carbon nanotube complexes
    • McNicholas, T. P. et al. Structure and function of glucose binding proteinsingle walled carbon nanotube complexes. Small 8, 3510-3516 (2012).
    • (2012) Small , vol.8 , pp. 3510-3516
    • McNicholas, T.P.1
  • 61
    • 84939833105 scopus 로고    scopus 로고
    • Mechanism of immobilized protein a binding to immunoglobulin g on nanosensor array surfaces
    • Nelson, J. T. et al. Mechanism of immobilized protein A binding to immunoglobulin G on nanosensor array surfaces. Anal. Chem. 87, 8186-8193 (2015).
    • (2015) Anal. Chem , vol.87 , pp. 8186-8193
    • Nelson, J.T.1
  • 62
    • 34548606427 scopus 로고    scopus 로고
    • Spm analysis of fibrinogen adsorption on solid surfaces
    • Choukourov, A., Grinevich, A., Saito, N. & Takai, O. SPM analysis of fibrinogen adsorption on solid surfaces. Surf. Sci. 601, 3948-3951 (2007).
    • (2007) Surf. Sci , vol.601 , pp. 3948-3951
    • Choukourov, A.1    Grinevich, A.2    Saito, N.3    Takai, O.4
  • 63
    • 43949164704 scopus 로고
    • Chapter 13 principles underlying the role of adsorbed plasma proteins in blood interactions with foreign materials
    • Horbett, T. A. Chapter 13 principles underlying the role of adsorbed plasma proteins in blood interactions with foreign materials. Cardiovasc. Pathol. 2, 137-148 (1993).
    • (1993) Cardiovasc. Pathol , vol.2 , pp. 137-148
    • Horbett, T.A.1
  • 64
    • 33947413127 scopus 로고    scopus 로고
    • Viscoelastic properties of fibrinogen adsorbed to the surface of biomaterials used in blood-contacting medical devices
    • Weber, N., Pesnell, A., Bolikal, D., Zeltinger, J. & Kohn, J. Viscoelastic properties of fibrinogen adsorbed to the surface of biomaterials used in blood-contacting medical devices. Langmuir 23, 3298-3304 (2007).
    • (2007) Langmuir , vol.23 , pp. 3298-3304
    • Weber, N.1    Pesnell, A.2    Bolikal, D.3    Zeltinger, J.4    Kohn, J.5
  • 65
    • 84874655615 scopus 로고    scopus 로고
    • Viscoelastic properties of fibrinogen adsorbed onto poly(ethylene terephthalate) surfaces by qcm-d
    • Doliska, A., Ribitsch, V., Stana Kleinschek, K. & Strnad, S. Viscoelastic properties of fibrinogen adsorbed onto poly(ethylene terephthalate) surfaces by QCM-D. Carbohydr. Polym. 93, 246-255 (2013).
    • (2013) Carbohydr. Polym , vol.93 , pp. 246-255
    • Doliska, A.1    Ribitsch, V.2    Stana Kleinschek, K.3    Strnad, S.4
  • 66
    • 84870671867 scopus 로고    scopus 로고
    • Cryo-tem of soft molecular assemblies
    • Danino, D. Cryo-TEM of soft molecular assemblies. Curr. Opin. Colloid Interface Sci. 17, 316-329 (2012).
    • (2012) Curr. Opin. Colloid Interface Sci , vol.17 , pp. 316-329
    • Danino, D.1
  • 68
    • 0032691940 scopus 로고    scopus 로고
    • Viscoelastic acoustic response of layered polymer films at fluid-solid interfaces: Continuum mechanics approach
    • Voinova, M. V., Rodahl, M., Jonson, M. & Kasemo, B. Viscoelastic acoustic response of layered polymer films at fluid-solid interfaces: continuum mechanics approach. Phys. Scr. 59, 391 (1999).
    • (1999) Phys. Scr , vol.59 , pp. 391
    • Voinova, M.V.1    Rodahl, M.2    Jonson, M.3    Kasemo, B.4
  • 69
    • 0036161285 scopus 로고    scopus 로고
    • A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation
    • Hoök, F. et al. A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation. Colloids Surf. B Biointerfaces 24, 155-170 (2002).
    • (2002) Colloids Surf. B Biointerfaces , vol.24 , pp. 155-170
    • Hoök, F.1
  • 70
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D., Schwarz, E., Komaromy, M. & Wall, R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142 (1984).
    • (1984) J. Mol. Biol , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4


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