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Volumn 872, Issue , 2015, Pages 7-25

Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: A review

Author keywords

Adsorption; Biosensors; Nanomaterials; Oxidase; Proteins

Indexed keywords

ADSORPTION; ANALYTIC EQUIPMENT; NANOSTRUCTURED MATERIALS; PROTEINS;

EID: 84928205743     PISSN: 00032670     EISSN: 18734324     Source Type: Journal    
DOI: 10.1016/j.aca.2014.10.031     Document Type: Review
Times cited : (211)

References (316)
  • 1
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • Nakanishi K., Sakiyama T., Imamura K. On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon. J. Biosci. Bioeng. 2001, 91:233-244.
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imamura, K.3
  • 2
    • 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. 2005, 127:8168-8173.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 3
    • 70349275154 scopus 로고    scopus 로고
    • Volumetric interpretation of protein adsorption: kinetics of protein-adsorption competition from binary solution
    • Barnthip N., Parhi P., Golas A., Vogler E.A. Volumetric interpretation of protein adsorption: kinetics of protein-adsorption competition from binary solution. Biomaterials 2009, 30:6495-6513.
    • (2009) Biomaterials , vol.30 , pp. 6495-6513
    • Barnthip, N.1    Parhi, P.2    Golas, A.3    Vogler, E.A.4
  • 5
    • 84886490160 scopus 로고    scopus 로고
    • Biosensor technology: recent advances in threat agent detection and medicine
    • Kirsch J., Siltanen C., Zhou Q., Revzin A., Simonian A. Biosensor technology: recent advances in threat agent detection and medicine. Chem. Soc. Rev. 2013, 42:8733-8768.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 8733-8768
    • Kirsch, J.1    Siltanen, C.2    Zhou, Q.3    Revzin, A.4    Simonian, A.5
  • 6
    • 84864289009 scopus 로고    scopus 로고
    • Biosensors for cardiac biomarkers detection: a review
    • Qureshi A., Gurbuz Y., Niazi J.H. Biosensors for cardiac biomarkers detection: a review. Sens. Actuators B 2012, 171-172:62-76.
    • (2012) Sens. Actuators B , pp. 62-76
    • Qureshi, A.1    Gurbuz, Y.2    Niazi, J.H.3
  • 7
    • 79957796589 scopus 로고    scopus 로고
    • How to design a biosensor
    • Ward W.K. How to design a biosensor. J. Diabetes Sci. Technol. 2007, 1:201-204.
    • (2007) J. Diabetes Sci. Technol. , vol.1 , pp. 201-204
    • Ward, W.K.1
  • 8
    • 0034275903 scopus 로고    scopus 로고
    • Configurations used in the design of screen-printed enzymatic biosensors. A review
    • Albareda-Sirvent M., Merkoçi A., Alegret S. Configurations used in the design of screen-printed enzymatic biosensors. A review. Sens. Actuators B 2000, 69:153-163.
    • (2000) Sens. Actuators B , vol.69 , pp. 153-163
    • Albareda-Sirvent, M.1    Merkoçi, A.2    Alegret, S.3
  • 9
    • 84878222888 scopus 로고    scopus 로고
    • Biosensors: sense and sensibility
    • Turner A.P.F. Biosensors: sense and sensibility. Chem. Soc. Rev. 2013, 42:3184-3196.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 3184-3196
    • Turner, A.P.F.1
  • 10
  • 11
    • 84878645267 scopus 로고    scopus 로고
    • Nanomaterials based electrochemical sensors for biomedical applications
    • Chen A., Chatterjee S. Nanomaterials based electrochemical sensors for biomedical applications. Chem. Soc. Rev. 2013, 42:5425-5438.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 5425-5438
    • Chen, A.1    Chatterjee, S.2
  • 12
    • 76549136166 scopus 로고    scopus 로고
    • Influence of nanoscale surface topography on protein adsorption and cellular response
    • Lord M.S., Foss M., Besenbacher F. Influence of nanoscale surface topography on protein adsorption and cellular response. Nano Today 2010, 5:66-78.
    • (2010) Nano Today , vol.5 , pp. 66-78
    • Lord, M.S.1    Foss, M.2    Besenbacher, F.3
  • 13
    • 0000040403 scopus 로고    scopus 로고
    • Influence of nanoscale surface topography and chemistry on the functional behaviour of an adsorbed model macromolecule
    • Sutherland D.S., Broberg M., Nygren H., Kasemo B. Influence of nanoscale surface topography and chemistry on the functional behaviour of an adsorbed model macromolecule. Macromol. Biosci. 2001, 1:270-273.
    • (2001) Macromol. Biosci. , vol.1 , pp. 270-273
    • Sutherland, D.S.1    Broberg, M.2    Nygren, H.3    Kasemo, B.4
  • 14
    • 79960221771 scopus 로고    scopus 로고
    • Electrostatic and dispersion interactions during protein adsorption on topographic nanostructures
    • Elter P., Lange R., Beck U. Electrostatic and dispersion interactions during protein adsorption on topographic nanostructures. Langmuir 2011, 27:8767-8775.
    • (2011) Langmuir , vol.27 , pp. 8767-8775
    • Elter, P.1    Lange, R.2    Beck, U.3
  • 15
    • 11144230048 scopus 로고    scopus 로고
    • Structure and function of enzymes adsorbed onto single-walled carbon nanotubes
    • Karajanagi S.S., Vertegel A.A., Kane R.S., Dordick J.S. Structure and function of enzymes adsorbed onto single-walled carbon nanotubes. Langmuir 2004, 20:11594-11599.
    • (2004) Langmuir , vol.20 , pp. 11594-11599
    • Karajanagi, S.S.1    Vertegel, A.A.2    Kane, R.S.3    Dordick, J.S.4
  • 17
    • 84890796816 scopus 로고    scopus 로고
    • Materials-based strategies for multi-enzyme immobilization and co-localization: a review
    • Jia F., Narasimhan B., Mallapragada S. Materials-based strategies for multi-enzyme immobilization and co-localization: a review. Biotechnol. Bioeng. 2014, 111:209-222.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 209-222
    • Jia, F.1    Narasimhan, B.2    Mallapragada, S.3
  • 18
    • 84905649040 scopus 로고    scopus 로고
    • Enzyme immobilization by adsorption: a review
    • Jesionowski T., Zdarta J., Krajewska B. Enzyme immobilization by adsorption: a review. Adsorption 2014, 20:801-821.
    • (2014) Adsorption , vol.20 , pp. 801-821
    • Jesionowski, T.1    Zdarta, J.2    Krajewska, B.3
  • 19
    • 84894434632 scopus 로고    scopus 로고
    • Covalent immobilization of proteins on 3D poly(acrylic acid) brushes: mechanism study and a more effective and controllable process
    • Qu Z., Chen K., Gu H., Xu H. Covalent immobilization of proteins on 3D poly(acrylic acid) brushes: mechanism study and a more effective and controllable process. Bioconjugate Chem. 2013, 25:370-378.
    • (2013) Bioconjugate Chem. , vol.25 , pp. 370-378
    • Qu, Z.1    Chen, K.2    Gu, H.3    Xu, H.4
  • 20
    • 84871742312 scopus 로고    scopus 로고
    • Computational, electrochemical, and spectroscopic, studies of acetycholinesterase covalently attached to carbon nanotubes
    • Cabral M.F., Barrios J.D., Kataoka E.M., Machado S.A.S., Carrilho E., Garcia C.D., Ayon A.A. Computational, electrochemical, and spectroscopic, studies of acetycholinesterase covalently attached to carbon nanotubes. Colloids Surf. B 2013, 103:624-629.
    • (2013) Colloids Surf. B , vol.103 , pp. 624-629
    • Cabral, M.F.1    Barrios, J.D.2    Kataoka, E.M.3    Machado, S.A.S.4    Carrilho, E.5    Garcia, C.D.6    Ayon, A.A.7
  • 21
    • 84888583708 scopus 로고    scopus 로고
    • Covalent immobilization of redox protein within the mesopores of transparent conducting electrodes
    • Müller V., Rathousky J., Fattakhova-Rohlfing D. Covalent immobilization of redox protein within the mesopores of transparent conducting electrodes. Electrochim. Acta 2014, 116:1-8.
    • (2014) Electrochim. Acta , vol.116 , pp. 1-8
    • Müller, V.1    Rathousky, J.2    Fattakhova-Rohlfing, D.3
  • 22
    • 0028295673 scopus 로고
    • Covalent immobilization of protein monolayers for biosensor applications
    • Williams R., Blanch H. Covalent immobilization of protein monolayers for biosensor applications. Biosens. Bioelectron. 1994, 9:159-167.
    • (1994) Biosens. Bioelectron. , vol.9 , pp. 159-167
    • Williams, R.1    Blanch, H.2
  • 23
    • 20444445785 scopus 로고    scopus 로고
    • Covalent attachment of glucose oxidase to an Au electrode modified with gold nanoparticles for use as glucose biosensor
    • Zhang S., Wang N., Yu H., Niu Y., Sun C. Covalent attachment of glucose oxidase to an Au electrode modified with gold nanoparticles for use as glucose biosensor. Bioelectrochemistry 2005, 67:15-22.
    • (2005) Bioelectrochemistry , vol.67 , pp. 15-22
    • Zhang, S.1    Wang, N.2    Yu, H.3    Niu, Y.4    Sun, C.5
  • 25
    • 28244452921 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs): a novel and versatile method for enzyme immobilization (a review)
    • Sheldon R., Schoevaart R., Van Langen L. Cross-linked enzyme aggregates (CLEAs): a novel and versatile method for enzyme immobilization (a review). Biocatal. Biotransform. 2005, 23:141-147.
    • (2005) Biocatal. Biotransform. , vol.23 , pp. 141-147
    • Sheldon, R.1    Schoevaart, R.2    Van Langen, L.3
  • 26
    • 0034682159 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase
    • Cao L., van Rantwijk F., Sheldon R.A. Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase. Org. Lett. 2000, 2:1361-1364.
    • (2000) Org. Lett. , vol.2 , pp. 1361-1364
    • Cao, L.1    van Rantwijk, F.2    Sheldon, R.A.3
  • 27
    • 33751158445 scopus 로고
    • Enzymes and other proteins entrapped in sol-gel materials
    • Avnir D., Braun S., Lev O., Ottolenghi M. Enzymes and other proteins entrapped in sol-gel materials. Chem. Mater. 1994, 6:1605-1614.
    • (1994) Chem. Mater. , vol.6 , pp. 1605-1614
    • Avnir, D.1    Braun, S.2    Lev, O.3    Ottolenghi, M.4
  • 28
    • 33947604975 scopus 로고    scopus 로고
    • Entrapment of biomolecules in sol-gel matrix for applications in biosensors: problems and future prospects
    • Gupta R., Chaudhury N. Entrapment of biomolecules in sol-gel matrix for applications in biosensors: problems and future prospects. Biosens. Bioelectron. 2007, 22:2387-2399.
    • (2007) Biosens. Bioelectron. , vol.22 , pp. 2387-2399
    • Gupta, R.1    Chaudhury, N.2
  • 30
    • 84893385179 scopus 로고    scopus 로고
    • Amperometric glucose biosensor based on layer-by-layer films of microperoxidase-11 and liposome-encapsulated glucose oxidase
    • Graça J.S., de Oliveira R.F., de Moraes M.L., Ferreira M. Amperometric glucose biosensor based on layer-by-layer films of microperoxidase-11 and liposome-encapsulated glucose oxidase. Bioelectrochemistry 2014, 96:37-42.
    • (2014) Bioelectrochemistry , vol.96 , pp. 37-42
    • Graça, J.S.1    de Oliveira, R.F.2    de Moraes, M.L.3    Ferreira, M.4
  • 32
    • 0022781496 scopus 로고
    • Adsorption of proteins from solution at the solid-liquid interface
    • Norde W. Adsorption of proteins from solution at the solid-liquid interface. Adv. Colloid Interface Sci. 1986, 25:267-340.
    • (1986) Adv. Colloid Interface Sci. , vol.25 , pp. 267-340
    • Norde, W.1
  • 33
    • 33746200227 scopus 로고
    • Globular proteins at solid/liquid interfaces
    • Haynes C.A., Norde W. Globular proteins at solid/liquid interfaces. Colloids Surf. B 1994, 2:517-566.
    • (1994) Colloids Surf. B , vol.2 , pp. 517-566
    • Haynes, C.A.1    Norde, W.2
  • 36
    • 79951770246 scopus 로고    scopus 로고
    • Understanding protein adsorption phenomena at solid surfaces
    • Rabe M., Verdes D., Seeger S. Understanding protein adsorption phenomena at solid surfaces. Adv. Colloid Interface Sci. 2011, 162:87-106.
    • (2011) Adv. Colloid Interface Sci. , vol.162 , pp. 87-106
    • Rabe, M.1    Verdes, D.2    Seeger, S.3
  • 38
    • 39749107963 scopus 로고    scopus 로고
    • Protein-nanoparticle interactions
    • Lynch I., Dawson K.A. Protein-nanoparticle interactions. Nano Today 2008, 3:40-47.
    • (2008) Nano Today , vol.3 , pp. 40-47
    • Lynch, I.1    Dawson, K.A.2
  • 39
    • 0020795163 scopus 로고
    • Proteins at solid-liquid interfaces a colloid-chemical review
    • Lyklema J. Proteins at solid-liquid interfaces a colloid-chemical review. Colloids Surf. 1984, 10:33-42.
    • (1984) Colloids Surf. , vol.10 , pp. 33-42
    • Lyklema, J.1
  • 40
    • 84898889702 scopus 로고    scopus 로고
    • Understanding enzymatic acceleration at nanoparticle interfaces: approaches and challenges
    • Johnson B.J., Russ Algar W., Malanoski A.P., Ancona M.G., Medintz I.L. Understanding enzymatic acceleration at nanoparticle interfaces: approaches and challenges. Nano Today 2014, 9:102-131.
    • (2014) Nano Today , vol.9 , pp. 102-131
    • Johnson, B.J.1    Russ Algar, W.2    Malanoski, A.P.3    Ancona, M.G.4    Medintz, I.L.5
  • 43
    • 84901500271 scopus 로고    scopus 로고
    • A review of block copolymer-based biomaterials that control protein and cell interactions
    • Bhushan B., Schricker S.R. A review of block copolymer-based biomaterials that control protein and cell interactions. J. Biomed. Mater. Res. Part A 2014, 102:2467-2480.
    • (2014) J. Biomed. Mater. Res. Part A , vol.102 , pp. 2467-2480
    • Bhushan, B.1    Schricker, S.R.2
  • 44
    • 79953162347 scopus 로고    scopus 로고
    • Recent applications of carbon-based nanomaterials in analytical chemistry: critical review
    • Scida K., Stege P.W., Haby G., Messina G.A., Garcia C.D. Recent applications of carbon-based nanomaterials in analytical chemistry: critical review. Anal. Chim. Acta 2011, 691:6-17.
    • (2011) Anal. Chim. Acta , vol.691 , pp. 6-17
    • Scida, K.1    Stege, P.W.2    Haby, G.3    Messina, G.A.4    Garcia, C.D.5
  • 45
    • 79960360793 scopus 로고    scopus 로고
    • Benefits and limitations of porous substrates as biosensors for protein adsorption
    • Lazzara T.D., Mey I., Steinem C., Janshoff A. Benefits and limitations of porous substrates as biosensors for protein adsorption. Anal. Chem. 2011, 83:5624-5630.
    • (2011) Anal. Chem. , vol.83 , pp. 5624-5630
    • Lazzara, T.D.1    Mey, I.2    Steinem, C.3    Janshoff, A.4
  • 47
    • 84894586361 scopus 로고    scopus 로고
    • Advances and challenges in biosensor-based diagnosis of infectious diseases
    • Sin M.L., Mach K.E., Wong P.K., Liao J.C. Advances and challenges in biosensor-based diagnosis of infectious diseases. Expert Rev. Mol. Diagn. 2014, 14:225-244.
    • (2014) Expert Rev. Mol. Diagn. , vol.14 , pp. 225-244
    • Sin, M.L.1    Mach, K.E.2    Wong, P.K.3    Liao, J.C.4
  • 48
    • 84901928677 scopus 로고    scopus 로고
    • Electrochemical biosensors for the determination of cardiovascular markers: a review
    • Pedrero M., Campuzano S., Pingarrón J.M. Electrochemical biosensors for the determination of cardiovascular markers: a review. Electroanalysis 2014, 26:1132-1153.
    • (2014) Electroanalysis , vol.26 , pp. 1132-1153
    • Pedrero, M.1    Campuzano, S.2    Pingarrón, J.M.3
  • 49
    • 84894492258 scopus 로고    scopus 로고
    • Biosensing methods for xanthine determination: a review
    • Pundir C.S., Devi R. Biosensing methods for xanthine determination: a review. Enzyme Microb. Technol. 2014, 57:55-62.
    • (2014) Enzyme Microb. Technol. , vol.57 , pp. 55-62
    • Pundir, C.S.1    Devi, R.2
  • 51
    • 37549018134 scopus 로고    scopus 로고
    • My voyage of discovery to proteins in flatland.and beyond
    • Norde W. My voyage of discovery to proteins in flatland.and beyond. Colloids Surf. B 2008, 61:1-9.
    • (2008) Colloids Surf. B , vol.61 , pp. 1-9
    • Norde, W.1
  • 52
    • 77950921585 scopus 로고    scopus 로고
    • Protein adsorption on a hydrophobic surface: a molecular dynamics study of lysozyme on graphite
    • Raffaini G., Ganazzoli F. Protein adsorption on a hydrophobic surface: a molecular dynamics study of lysozyme on graphite. Langmuir 2009, 26:5679-5689.
    • (2009) Langmuir , vol.26 , pp. 5679-5689
    • Raffaini, G.1    Ganazzoli, F.2
  • 53
    • 84908350436 scopus 로고    scopus 로고
    • Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
    • Benavidez T.E., Torrente D., Marucho M., Garcia C.D. Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential. J. Colloid Interface Sci. 2014, 435:164-170.
    • (2014) J. Colloid Interface Sci. , vol.435 , pp. 164-170
    • Benavidez, T.E.1    Torrente, D.2    Marucho, M.3    Garcia, C.D.4
  • 54
    • 39449110964 scopus 로고    scopus 로고
    • Calculating enzyme kinetic parameters from protein structures
    • Stein M., Gabdoulline R.R., Wade R.C. Calculating enzyme kinetic parameters from protein structures. Biochem. Soc. Trans. 2008, 36:51-54.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 51-54
    • Stein, M.1    Gabdoulline, R.R.2    Wade, R.C.3
  • 55
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading
    • Trott O., Olson A.J. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading. J. Comput. Chem. 2010, 31:455-461.
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 56
    • 80053903053 scopus 로고    scopus 로고
    • Nanomolar detection of glutamate at a biosensor based on screen-printed electrodes modified with carbon nanotubes
    • Khan R., Gorski W., Garcia C.D. Nanomolar detection of glutamate at a biosensor based on screen-printed electrodes modified with carbon nanotubes. Electroanalysis 2011, 23:2357-2363.
    • (2011) Electroanalysis , vol.23 , pp. 2357-2363
    • Khan, R.1    Gorski, W.2    Garcia, C.D.3
  • 57
    • 62649091715 scopus 로고    scopus 로고
    • The BAD project: data mining, database and prediction of protein adsorption on surfaces
    • Vasina E.N., Paszek E., Nicolau J.D.V., Nicolau D.V. The BAD project: data mining, database and prediction of protein adsorption on surfaces. Lab Chip 2009, 9:891-900.
    • (2009) Lab Chip , vol.9 , pp. 891-900
    • Vasina, E.N.1    Paszek, E.2    Nicolau, J.D.V.3    Nicolau, D.V.4
  • 59
    • 35348866182 scopus 로고    scopus 로고
    • Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D
    • Porollo A., Meller J. Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D. BMC Bioinf. 2007, 8:316.
    • (2007) BMC Bioinf. , vol.8 , pp. 316
    • Porollo, A.1    Meller, J.2
  • 62
    • 84856188436 scopus 로고    scopus 로고
    • Antibody adsorption and orientation on hydrophobic surfaces
    • Wiseman M.E., Frank C.W. Antibody adsorption and orientation on hydrophobic surfaces. Langmuir 2011, 28:1765-1774.
    • (2011) Langmuir , vol.28 , pp. 1765-1774
    • Wiseman, M.E.1    Frank, C.W.2
  • 63
    • 84864273278 scopus 로고    scopus 로고
    • Peptide adsorption on silica nanoparticles: evidence of hydrophobic interactions
    • Puddu V., Perry C.C. Peptide adsorption on silica nanoparticles: evidence of hydrophobic interactions. ACS Nano 2012, 6:6356-6363.
    • (2012) ACS Nano , vol.6 , pp. 6356-6363
    • Puddu, V.1    Perry, C.C.2
  • 64
    • 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
  • 65
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • Ghaemmaghami S., Oas T.G. Quantitative protein stability measurement in vivo. Nat. Struct. Mol. Biol. 2001, 8:879-882.
    • (2001) Nat. Struct. Mol. Biol. , vol.8 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 66
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson A.D., Murphy K.P. Protein structure and the energetics of protein stability. Chem. Rev. 1997, 97:1251-1268.
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 67
    • 84904288971 scopus 로고    scopus 로고
    • Energetics-based methods for protein folding and stability measurements
    • Geer M.A., Fitzgerald M.C. Energetics-based methods for protein folding and stability measurements. Annu. Rev. Anal. Chem. 2014, 7:209-228.
    • (2014) Annu. Rev. Anal. Chem. , vol.7 , pp. 209-228
    • Geer, M.A.1    Fitzgerald, M.C.2
  • 69
    • 0033275324 scopus 로고    scopus 로고
    • Conformational changes in proteins at interfaces: from solution to the interface, and back
    • Norde W., Giacomelli C.E. Conformational changes in proteins at interfaces: from solution to the interface, and back. Macromol. Symp. 1999, 145:125-136.
    • (1999) Macromol. Symp. , vol.145 , pp. 125-136
    • Norde, W.1    Giacomelli, C.E.2
  • 70
    • 84864968809 scopus 로고    scopus 로고
    • Interfacial behaviour of proteins with special reference to immunoglobulins. A physicochemical study
    • Norde W., Lyklema J. Interfacial behaviour of proteins with special reference to immunoglobulins. A physicochemical study. Adv. Colloid Interface Sci. 2012, 179-182:5-13.
    • (2012) Adv. Colloid Interface Sci. , pp. 5-13
    • Norde, W.1    Lyklema, J.2
  • 72
    • 17844402960 scopus 로고    scopus 로고
    • Influence of surface properties of carbon fibres on the adsorption of catalase
    • Pamuła E., Rouxhet P.G. Influence of surface properties of carbon fibres on the adsorption of catalase. Carbon 2005, 43:1432-1438.
    • (2005) Carbon , vol.43 , pp. 1432-1438
    • Pamuła, E.1    Rouxhet, P.G.2
  • 73
    • 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. 2005, 127:8168-8173.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 74
    • 20444483268 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography of proteins: III. Unfolding of proteins upon adsorption
    • Jungbauer A., Machold C., Hahn R. Hydrophobic interaction chromatography of proteins: III. Unfolding of proteins upon adsorption. J. Chromatogr. A 2005, 1079:221-228.
    • (2005) J. Chromatogr. A , vol.1079 , pp. 221-228
    • Jungbauer, A.1    Machold, C.2    Hahn, R.3
  • 75
    • 26844515684 scopus 로고    scopus 로고
    • Coating of poly(dimethylsiloxane) with n-dodecyl-[small beta]-d-maltoside to minimize nonspecific protein adsorption
    • Huang B., Wu H., Kim S., Zare R.N. Coating of poly(dimethylsiloxane) with n-dodecyl-[small beta]-d-maltoside to minimize nonspecific protein adsorption. Lab Chip 2005, 5:1005-1007.
    • (2005) Lab Chip , vol.5 , pp. 1005-1007
    • Huang, B.1    Wu, H.2    Kim, S.3    Zare, R.N.4
  • 76
    • 79952607947 scopus 로고    scopus 로고
    • Protein adsorption at charged surfaces: the role of electrostatic interactions and interfacial charge regulation
    • Hartvig R.A., van de Weert M., Østergaard J., Jorgensen L., Jensen H. Protein adsorption at charged surfaces: the role of electrostatic interactions and interfacial charge regulation. Langmuir 2011, 27:2634-2643.
    • (2011) Langmuir , vol.27 , pp. 2634-2643
    • Hartvig, R.A.1    van de Weert, M.2    Østergaard, J.3    Jorgensen, L.4    Jensen, H.5
  • 77
    • 10044277018 scopus 로고    scopus 로고
    • Protein adsorption onto silica nanoparticles: conformational changes depend on the particles' curvature and the protein stability
    • Lundqvist M., Sethson I., Jonsson B.H. Protein adsorption onto silica nanoparticles: conformational changes depend on the particles' curvature and the protein stability. Langmuir 2004, 20:10639-10647.
    • (2004) Langmuir , vol.20 , pp. 10639-10647
    • Lundqvist, M.1    Sethson, I.2    Jonsson, B.H.3
  • 79
    • 33746069408 scopus 로고    scopus 로고
    • Does the nanometre scale topography of titanium influence protein adsorption and cell proliferation?
    • Cai K., Bossert J., Jandt K.D. Does the nanometre scale topography of titanium influence protein adsorption and cell proliferation?. Colloids Surf. B 2006, 49:136-144.
    • (2006) Colloids Surf. B , vol.49 , pp. 136-144
    • Cai, K.1    Bossert, J.2    Jandt, K.D.3
  • 80
    • 33645459798 scopus 로고    scopus 로고
    • Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry
    • Roach P., Farrar D., Perry C.C. Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry. J. Am. Chem. Soc. 2006, 128:3939-3945.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 81
    • 36849090594 scopus 로고    scopus 로고
    • Protein adsorption on materials surfaces with nano-topography
    • Song W., Chen H. Protein adsorption on materials surfaces with nano-topography. Chin. Sci. Bull. 2007, 52:3169-3173.
    • (2007) Chin. Sci. Bull. , vol.52 , pp. 3169-3173
    • Song, W.1    Chen, H.2
  • 82
    • 84866154779 scopus 로고    scopus 로고
    • Effect of gold nanoparticle structure on the conformation and function of adsorbed proteins
    • Gagner J.E., Qian X., Lopez M.M., Dordick J.S., Siegel R.W. Effect of gold nanoparticle structure on the conformation and function of adsorbed proteins. Biomaterials 2012, 33:8503-8516.
    • (2012) Biomaterials , vol.33 , pp. 8503-8516
    • Gagner, J.E.1    Qian, X.2    Lopez, M.M.3    Dordick, J.S.4    Siegel, R.W.5
  • 84
    • 84894145782 scopus 로고    scopus 로고
    • Protein immobilization in hollow nanostructures and investigation of the adsorbed protein behavior
    • Qian X., Levenstein A., Gagner J.E., Dordick J.S., Siegel R.W. Protein immobilization in hollow nanostructures and investigation of the adsorbed protein behavior. Langmuir 2014, 30:1295-1303.
    • (2014) Langmuir , vol.30 , pp. 1295-1303
    • Qian, X.1    Levenstein, A.2    Gagner, J.E.3    Dordick, J.S.4    Siegel, R.W.5
  • 86
    • 34250897750 scopus 로고    scopus 로고
    • Modern biomaterials: a review-bulk properties and implications of surface modifications
    • Roach P., Eglin D., Rohde K., Perry C.C. Modern biomaterials: a review-bulk properties and implications of surface modifications. J. Mater. Sci. Mater. Med. 2007, 18:1263-1277.
    • (2007) J. Mater. Sci. Mater. Med. , vol.18 , pp. 1263-1277
    • Roach, P.1    Eglin, D.2    Rohde, K.3    Perry, C.C.4
  • 89
    • 0348170851 scopus 로고    scopus 로고
    • AFM study on protein immobilization on charged surfaces at the nanoscale: toward the fabrication of three-dimensional protein nanostructures
    • Zhou D., Wang X., Birch L., Rayment T., Abell C. AFM study on protein immobilization on charged surfaces at the nanoscale: toward the fabrication of three-dimensional protein nanostructures. Langmuir 2003, 19:10557-10562.
    • (2003) Langmuir , vol.19 , pp. 10557-10562
    • Zhou, D.1    Wang, X.2    Birch, L.3    Rayment, T.4    Abell, C.5
  • 90
    • 34247191269 scopus 로고    scopus 로고
    • Nanobiotechnology: protein-nanomaterial interactions
    • Kane R.S., Stroock A.D. Nanobiotechnology: protein-nanomaterial interactions. Biotechnol. Prog. 2007, 23:316-319.
    • (2007) Biotechnol. Prog. , vol.23 , pp. 316-319
    • Kane, R.S.1    Stroock, A.D.2
  • 92
    • 78649534150 scopus 로고    scopus 로고
    • AFM, SECM and QCM as useful analytical tools in the characterization of enzyme-based bioanalytical platforms
    • Casero E., Vazquez L., Parra-Alfambra A.M., Lorenzo E. AFM, SECM and QCM as useful analytical tools in the characterization of enzyme-based bioanalytical platforms. Analyst 2010, 135:1878-1903.
    • (2010) Analyst , vol.135 , pp. 1878-1903
    • Casero, E.1    Vazquez, L.2    Parra-Alfambra, A.M.3    Lorenzo, E.4
  • 93
    • 84862864640 scopus 로고    scopus 로고
    • Atomic force microscopy and analytical ultracentrifugation for probing nanomaterial protein interactions
    • Schaefer J., Schulze C., Marxer E.E.J., Schaefer U.F., Wohlleben W., Bakowsky U., Lehr C.-M. Atomic force microscopy and analytical ultracentrifugation for probing nanomaterial protein interactions. ACS Nano 2012, 6:4603-4614.
    • (2012) ACS Nano , vol.6 , pp. 4603-4614
    • Schaefer, J.1    Schulze, C.2    Marxer, E.E.J.3    Schaefer, U.F.4    Wohlleben, W.5    Bakowsky, U.6    Lehr, C.-M.7
  • 94
    • 84903398481 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase to nanostructured films of polystyrene-block-poly(2-vinylpyridine)
    • Bhakta S.A., Benavidez T.E., Garcia C.D. Immobilization of glucose oxidase to nanostructured films of polystyrene-block-poly(2-vinylpyridine). J. Colloid Interface Sci. 2014, 430:351-356.
    • (2014) J. Colloid Interface Sci. , vol.430 , pp. 351-356
    • Bhakta, S.A.1    Benavidez, T.E.2    Garcia, C.D.3
  • 97
    • 84901851737 scopus 로고    scopus 로고
    • Controlling protein adsorption on graphene for cryo-EM using low-energy hydrogen plasmas
    • Russo C.J., Passmore L.A. Controlling protein adsorption on graphene for cryo-EM using low-energy hydrogen plasmas. Nat. Methods 2014, 11:649-652.
    • (2014) Nat. Methods , vol.11 , pp. 649-652
    • Russo, C.J.1    Passmore, L.A.2
  • 99
    • 84855412140 scopus 로고    scopus 로고
    • Pressure-based approach for the analysis of protein adsorption in capillary electrophoresis
    • de Jong S., Krylov S.N. Pressure-based approach for the analysis of protein adsorption in capillary electrophoresis. Anal. Chem. 2012, 84:453-458.
    • (2012) Anal. Chem. , vol.84 , pp. 453-458
    • de Jong, S.1    Krylov, S.N.2
  • 102
    • 84898886012 scopus 로고    scopus 로고
    • Quantitative assessment of protein adsorption on microparticles with particle mass spectrometry
    • Xiong C., Zhou X., Zhang N., Zhan L., Chen S., Wang J., Peng W.-P., Chang H.-C., Nie Z. Quantitative assessment of protein adsorption on microparticles with particle mass spectrometry. Anal. Chem. 2014, 86:3876-3881.
    • (2014) Anal. Chem. , vol.86 , pp. 3876-3881
    • Xiong, C.1    Zhou, X.2    Zhang, N.3    Zhan, L.4    Chen, S.5    Wang, J.6    Peng, W.-P.7    Chang, H.-C.8    Nie, Z.9
  • 105
    • 84888877255 scopus 로고    scopus 로고
    • Combination of UV-vis spectroscopy and chemometrics to understand protein-nanomaterial conjugate: a case study on human serum albumin and gold nanoparticles
    • Wang Y., Ni Y.N. Combination of UV-vis spectroscopy and chemometrics to understand protein-nanomaterial conjugate: a case study on human serum albumin and gold nanoparticles. Talanta 2014, 119:320-330.
    • (2014) Talanta , vol.119 , pp. 320-330
    • Wang, Y.1    Ni, Y.N.2
  • 107
    • 79952773180 scopus 로고    scopus 로고
    • Characterizing protein activities on the lysozyme and nanodiamond complex prepared for bio applications
    • Perevedentseva E., Cai P.J., Chiu Y.C., Cheng C.L. Characterizing protein activities on the lysozyme and nanodiamond complex prepared for bio applications. Langmuir 2011, 27:1085-1091.
    • (2011) Langmuir , vol.27 , pp. 1085-1091
    • Perevedentseva, E.1    Cai, P.J.2    Chiu, Y.C.3    Cheng, C.L.4
  • 108
    • 0035862293 scopus 로고    scopus 로고
    • The adsorption-desorption cycle. Reversibility of the BSA-silica system
    • Giacomelli C.E., Norde W. The adsorption-desorption cycle. Reversibility of the BSA-silica system. J. Colloid Interface Sci. 2001, 233:234-240.
    • (2001) J. Colloid Interface Sci. , vol.233 , pp. 234-240
    • Giacomelli, C.E.1    Norde, W.2
  • 109
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases
    • Whitmore L., Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008, 89:392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 111
    • 80054015249 scopus 로고    scopus 로고
    • Effect of antibody immobilization strategies on the analytical performance of a surface plasmon resonance-based immunoassay
    • Vashist S.K., Dixit C.K., MacCraith B.D., O'Kennedy R. Effect of antibody immobilization strategies on the analytical performance of a surface plasmon resonance-based immunoassay. Analyst 2011, 136:4431-4436.
    • (2011) Analyst , vol.136 , pp. 4431-4436
    • Vashist, S.K.1    Dixit, C.K.2    MacCraith, B.D.3    O'Kennedy, R.4
  • 112
    • 84874968304 scopus 로고    scopus 로고
    • Development of a label-free immunosensor based on surface plasmon resonance technique for the detection of anti-Leishmania infantum antibodies in canine serum
    • Souto D.E.P., Silva J.V., Martins H.R., Reis A.B., Luz R.C.S., Kubota L.T., Damos F.S. Development of a label-free immunosensor based on surface plasmon resonance technique for the detection of anti-Leishmania infantum antibodies in canine serum. Biosens. Bioelectron. 2013, 46:22-29.
    • (2013) Biosens. Bioelectron. , vol.46 , pp. 22-29
    • Souto, D.E.P.1    Silva, J.V.2    Martins, H.R.3    Reis, A.B.4    Luz, R.C.S.5    Kubota, L.T.6    Damos, F.S.7
  • 113
    • 84893488642 scopus 로고    scopus 로고
    • Dip biosensor based on localized surface plasmon resonance at the tip of an optical fiber
    • Sciacca B., Monro T.M. Dip biosensor based on localized surface plasmon resonance at the tip of an optical fiber. Langmuir 2014, 30:946-954.
    • (2014) Langmuir , vol.30 , pp. 946-954
    • Sciacca, B.1    Monro, T.M.2
  • 114
    • 84893219181 scopus 로고    scopus 로고
    • Total internal reflection spectroscopy for studying soft matter
    • Woods D.A., Bain C.D. Total internal reflection spectroscopy for studying soft matter. Soft Matter 2014, 10:1071-1096.
    • (2014) Soft Matter , vol.10 , pp. 1071-1096
    • Woods, D.A.1    Bain, C.D.2
  • 115
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth A. Infrared spectroscopy of proteins. Biochim. Biophys. Acta Bioenerg. 2007, 1767:1073-1101.
    • (2007) Biochim. Biophys. Acta Bioenerg. , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 116
    • 84858054510 scopus 로고    scopus 로고
    • Effect of protein adsorption on the fluorescence of ultrasmall gold nanoclusters
    • Shang L., Brandholt S., Stockmar F., Trouillet V., Bruns M., Nienhaus G.U. Effect of protein adsorption on the fluorescence of ultrasmall gold nanoclusters. Small 2012, 8:661-665.
    • (2012) Small , vol.8 , pp. 661-665
    • Shang, L.1    Brandholt, S.2    Stockmar, F.3    Trouillet, V.4    Bruns, M.5    Nienhaus, G.U.6
  • 117
    • 25144473424 scopus 로고    scopus 로고
    • Gold nanoparticle-based competitive colorimetric assay for detection of protein-protein interactions
    • Tsai C.-S., Yu T.-B., Chen C.-T. Gold nanoparticle-based competitive colorimetric assay for detection of protein-protein interactions. Chem. Commun. 2005, 4273-4275.
    • (2005) Chem. Commun. , pp. 4273-4275
    • Tsai, C.-S.1    Yu, T.-B.2    Chen, C.-T.3
  • 118
    • 79952583790 scopus 로고    scopus 로고
    • Adsorption and conformation of serum albumin protein on gold nanoparticles investigated using dimensional measurements and in situ spectroscopic methods
    • Tsai D.-H., DelRio F.W., Keene A.M., Tyner K.M., MacCuspie R.I., Cho T.J., Zachariah M.R., Hackley V.A. Adsorption and conformation of serum albumin protein on gold nanoparticles investigated using dimensional measurements and in situ spectroscopic methods. Langmuir 2011, 27:2464-2477.
    • (2011) Langmuir , vol.27 , pp. 2464-2477
    • Tsai, D.-H.1    DelRio, F.W.2    Keene, A.M.3    Tyner, K.M.4    MacCuspie, R.I.5    Cho, T.J.6    Zachariah, M.R.7    Hackley, V.A.8
  • 119
    • 84883209044 scopus 로고    scopus 로고
    • Quantitation of IgG protein adsorption to gold nanoparticles using particle size measurement
    • Bell N.C., Minelli C., Shard A.G. Quantitation of IgG protein adsorption to gold nanoparticles using particle size measurement. Anal. Methods 2013, 5:4591-4601.
    • (2013) Anal. Methods , vol.5 , pp. 4591-4601
    • Bell, N.C.1    Minelli, C.2    Shard, A.G.3
  • 120
    • 77952542831 scopus 로고    scopus 로고
    • Determination of a setup correction function to obtain adsorption kinetic data at stagnation point flow conditions
    • Mora M.F., Reza Nejadnik M., Baylon-Cardiel J.L., Giacomelli C.E., Garcia C.D. Determination of a setup correction function to obtain adsorption kinetic data at stagnation point flow conditions. J. Colloid Interface Sci. 2010, 346:208-215.
    • (2010) J. Colloid Interface Sci. , vol.346 , pp. 208-215
    • Mora, M.F.1    Reza Nejadnik, M.2    Baylon-Cardiel, J.L.3    Giacomelli, C.E.4    Garcia, C.D.5
  • 121
    • 84888333200 scopus 로고    scopus 로고
    • Potential-assisted adsorption of bovine serum albumin onto optically transparent carbon electrodes
    • Benavidez T.E., Garcia C.D. Potential-assisted adsorption of bovine serum albumin onto optically transparent carbon electrodes. Langmuir 2013, 29:14154-14162.
    • (2013) Langmuir , vol.29 , pp. 14154-14162
    • Benavidez, T.E.1    Garcia, C.D.2
  • 124
    • 26844498737 scopus 로고    scopus 로고
    • Dynamic protein adsorption in microchannels by stop-flow and continuous flow
    • Lionello A., Josserand J., Jensen H., Girault H.H. Dynamic protein adsorption in microchannels by stop-flow and continuous flow. Lab Chip 2005, 5:1096-1103.
    • (2005) Lab Chip , vol.5 , pp. 1096-1103
    • Lionello, A.1    Josserand, J.2    Jensen, H.3    Girault, H.H.4
  • 125
    • 0029256589 scopus 로고
    • Adsorption-desorption of proteins on phospholipid polymer surfaces evaluated by dynamic contact angle measurement
    • Ueda T., Ishihara K., Nakabayashi N. Adsorption-desorption of proteins on phospholipid polymer surfaces evaluated by dynamic contact angle measurement. J. Biomed. Mater. Res. 1995, 29:381-387.
    • (1995) J. Biomed. Mater. Res. , vol.29 , pp. 381-387
    • Ueda, T.1    Ishihara, K.2    Nakabayashi, N.3
  • 126
    • 31944442534 scopus 로고    scopus 로고
    • Whey protein adsorption onto steel surfaces-effect of temperature flow rate, residence time and aggregation
    • Santos O., Nylander T., Paulsson M., Trägårdh C. Whey protein adsorption onto steel surfaces-effect of temperature flow rate, residence time and aggregation. J. Food Eng. 2006, 74:468-483.
    • (2006) J. Food Eng. , vol.74 , pp. 468-483
    • Santos, O.1    Nylander, T.2    Paulsson, M.3    Trägårdh, C.4
  • 127
    • 47949120059 scopus 로고    scopus 로고
    • Adsorption kinetics of cationic polyelectrolytes studied with stagnation point adsorption reflectometry and quartz crystal microgravimetry
    • Enarsson L.-E., WÃgberg L. Adsorption kinetics of cationic polyelectrolytes studied with stagnation point adsorption reflectometry and quartz crystal microgravimetry. Langmuir 2008, 24:7329-7337.
    • (2008) Langmuir , vol.24 , pp. 7329-7337
    • Enarsson, L.-E.1    WÃgberg, L.2
  • 128
    • 34547459511 scopus 로고    scopus 로고
    • Simultaneous quartz crystal microbalance-electrochemical impedance spectroscopy study on the adsorption of anti-human immunoglobulin G and its immunoreaction at nanomaterial-modified au electrode surfaces
    • Jia X., Xie Q., Zhang Y., Yao S. Simultaneous quartz crystal microbalance-electrochemical impedance spectroscopy study on the adsorption of anti-human immunoglobulin G and its immunoreaction at nanomaterial-modified au electrode surfaces. Anal. Sci. 2007, 23:689-696.
    • (2007) Anal. Sci. , vol.23 , pp. 689-696
    • Jia, X.1    Xie, Q.2    Zhang, Y.3    Yao, S.4
  • 129
    • 47749094613 scopus 로고    scopus 로고
    • Quartz crystal microbalance study of protein adsorption kinetics on poly(2-hydroxyethyl methacrylate)
    • Teichroeb J.H., Forrest J.A., Jones L.W., Chan J., Dalton K. Quartz crystal microbalance study of protein adsorption kinetics on poly(2-hydroxyethyl methacrylate). J. Colloid Interface Sci. 2008, 325:157-164.
    • (2008) J. Colloid Interface Sci. , vol.325 , pp. 157-164
    • Teichroeb, J.H.1    Forrest, J.A.2    Jones, L.W.3    Chan, J.4    Dalton, K.5
  • 130
    • 19744377798 scopus 로고    scopus 로고
    • Study of protein adsorption on polymer coatings surface by combining quartz crystal microbalance with electrochemical impedance methods
    • Zhang Y., Fung Y., Sun H., Zhu D., Yao S. Study of protein adsorption on polymer coatings surface by combining quartz crystal microbalance with electrochemical impedance methods. Sens. Actuators B 2005, 108:933-942.
    • (2005) Sens. Actuators B , vol.108 , pp. 933-942
    • Zhang, Y.1    Fung, Y.2    Sun, H.3    Zhu, D.4    Yao, S.5
  • 133
    • 85017789126 scopus 로고    scopus 로고
    • Optimizing the bioaffinity interaction between His-Tag proteins and Ni(II) surface sites, proteins at interfaces III state of the art
    • Valenti L.E., Herrera E., Stragliotto M.F., Martins V.L., Torresi R.M., Giacomelli C.E. Optimizing the bioaffinity interaction between His-Tag proteins and Ni(II) surface sites, proteins at interfaces III state of the art. Am. Chem. Soc. 2012, 37-53.
    • (2012) Am. Chem. Soc. , pp. 37-53
    • Valenti, L.E.1    Herrera, E.2    Stragliotto, M.F.3    Martins, V.L.4    Torresi, R.M.5    Giacomelli, C.E.6
  • 136
    • 79952145516 scopus 로고    scopus 로고
    • Chemical-vapor-deposition-based polymer substrates for spatially resolved analysis of protein binding by imaging ellipsometry
    • Ross A.M., Zhang D., Deng X., Chang S.L., Lahann J. Chemical-vapor-deposition-based polymer substrates for spatially resolved analysis of protein binding by imaging ellipsometry. Anal. Chem. 2011, 83:874-880.
    • (2011) Anal. Chem. , vol.83 , pp. 874-880
    • Ross, A.M.1    Zhang, D.2    Deng, X.3    Chang, S.L.4    Lahann, J.5
  • 137
    • 47349116299 scopus 로고    scopus 로고
    • Adsorption of the protein bovine serum albumin in a planar poly(acrylic acid) brush layer as measured by optical reflectometry
    • de Vos W.M., Biesheuvel P.M., de Keizer A., Kleijn J.M., Cohen Stuart M.A. Adsorption of the protein bovine serum albumin in a planar poly(acrylic acid) brush layer as measured by optical reflectometry. Langmuir 2008, 24:6575-6584.
    • (2008) Langmuir , vol.24 , pp. 6575-6584
    • de Vos, W.M.1    Biesheuvel, P.M.2    de Keizer, A.3    Kleijn, J.M.4    Cohen Stuart, M.A.5
  • 138
    • 0037039650 scopus 로고    scopus 로고
    • Reflectometry applied to electrochemically generated phenoxy radical adsorption monitoring
    • García G., García C.D., Ortiz P.I., De Pauli C.P. Reflectometry applied to electrochemically generated phenoxy radical adsorption monitoring. J. Electroanal. Chem. 2002, 519:53-59.
    • (2002) J. Electroanal. Chem. , vol.519 , pp. 53-59
    • García, G.1    García, C.D.2    Ortiz, P.I.3    De Pauli, C.P.4
  • 140
    • 77949474059 scopus 로고    scopus 로고
    • Electrostatic and hydrophobic interactions involved in CNT biofunctionalization with short ss-DNA
    • Carot M.L., Torresi R.M., Garcia C.D., Esplandiu M.J., Giacomelli C.E. Electrostatic and hydrophobic interactions involved in CNT biofunctionalization with short ss-DNA. J. Phys. Chem. C 2010, 114:4459-4465.
    • (2010) J. Phys. Chem. C , vol.114 , pp. 4459-4465
    • Carot, M.L.1    Torresi, R.M.2    Garcia, C.D.3    Esplandiu, M.J.4    Giacomelli, C.E.5
  • 143
    • 63749111814 scopus 로고    scopus 로고
    • An amperometric glucose biosensor based on the immobilization of glucose oxidase on the ZnO nanotubes
    • Kong T., Chen Y., Ye Y., Zhang K., Wang Z., Wang X. An amperometric glucose biosensor based on the immobilization of glucose oxidase on the ZnO nanotubes. Sens. Actuators B 2009, 138:344-350.
    • (2009) Sens. Actuators B , vol.138 , pp. 344-350
    • Kong, T.1    Chen, Y.2    Ye, Y.3    Zhang, K.4    Wang, Z.5    Wang, X.6
  • 144
    • 0036857345 scopus 로고    scopus 로고
    • Secondary structure of proteins adsorbed onto or embedded in polyelectrolyte multilayers
    • Schwinté P., Ball V., Szalontai B., Haikel Y., Voegel J.C., Schaaf P. Secondary structure of proteins adsorbed onto or embedded in polyelectrolyte multilayers. Biomacromolecules 2002, 3:1135-1143.
    • (2002) Biomacromolecules , vol.3 , pp. 1135-1143
    • Schwinté, P.1    Ball, V.2    Szalontai, B.3    Haikel, Y.4    Voegel, J.C.5    Schaaf, P.6
  • 145
    • 84900307345 scopus 로고    scopus 로고
    • Amperometric glucose biosensor based on Pt-Pd nanoparticles supported by reduced graphene oxide and integrated with glucose oxidase
    • Hossain M.F., Park J.Y. Amperometric glucose biosensor based on Pt-Pd nanoparticles supported by reduced graphene oxide and integrated with glucose oxidase. Electroanalysis 2014, 26:940-951.
    • (2014) Electroanalysis , vol.26 , pp. 940-951
    • Hossain, M.F.1    Park, J.Y.2
  • 147
    • 40449109054 scopus 로고    scopus 로고
    • Electrochemical glucose biosensors
    • Wang J. Electrochemical glucose biosensors. Chem. Rev. 2007, 108:814-825.
    • (2007) Chem. Rev. , vol.108 , pp. 814-825
    • Wang, J.1
  • 148
    • 79957866740 scopus 로고    scopus 로고
    • Adsorption of glucose oxidase to 3-D scaffolds of carbon nanotubes: analytical applications
    • Nejadnik M.R., Francis L., Garcia C.D. Adsorption of glucose oxidase to 3-D scaffolds of carbon nanotubes: analytical applications. Electroanalysis 2011, 23:1462-1469.
    • (2011) Electroanalysis , vol.23 , pp. 1462-1469
    • Nejadnik, M.R.1    Francis, L.2    Garcia, C.D.3
  • 149
    • 84873333974 scopus 로고    scopus 로고
    • Influence of surface adsorption on the interfacial electron transfer of flavin adenine dinucleotide and glucose oxidase at carbon nanotube and nitrogen-doped carbon nanotube electrodes
    • Goran J.M., Mantilla S.M., Stevenson K.J. Influence of surface adsorption on the interfacial electron transfer of flavin adenine dinucleotide and glucose oxidase at carbon nanotube and nitrogen-doped carbon nanotube electrodes. Anal. Chem. 2013, 85:1571-1581.
    • (2013) Anal. Chem. , vol.85 , pp. 1571-1581
    • Goran, J.M.1    Mantilla, S.M.2    Stevenson, K.J.3
  • 150
    • 84884172151 scopus 로고    scopus 로고
    • Glucose determination in beverages using carbon nanotube modified biosensor: an experiment for the undergraduate laboratory
    • Hobbs J.M., Patel N.N., Kim D.W., Rugutt J.K., Wanekaya A.K. Glucose determination in beverages using carbon nanotube modified biosensor: an experiment for the undergraduate laboratory. J. Chem. Educ. 2013, 90:1222-1226.
    • (2013) J. Chem. Educ. , vol.90 , pp. 1222-1226
    • Hobbs, J.M.1    Patel, N.N.2    Kim, D.W.3    Rugutt, J.K.4    Wanekaya, A.K.5
  • 151
    • 0037023085 scopus 로고    scopus 로고
    • Kinetics of irreversible adsorption with diffusion: application to biomolecule immobilization
    • Hibbert D.B., Gooding J.J., Erokhin P. kinetics of irreversible adsorption with diffusion: application to biomolecule immobilization. Langmuir 2002, 18:1770-1776.
    • (2002) Langmuir , vol.18 , pp. 1770-1776
    • Hibbert, D.B.1    Gooding, J.J.2    Erokhin, P.3
  • 153
    • 38749153207 scopus 로고    scopus 로고
    • A super highly sensitive glucose biosensor based on Au nanoparticles-AgCl@polyaniline hybrid material
    • Yan W., Feng X., Chen X., Hou W., Zhu J.-J. A super highly sensitive glucose biosensor based on Au nanoparticles-AgCl@polyaniline hybrid material. Biosens. Bioelectron. 2008, 23:925-931.
    • (2008) Biosens. Bioelectron. , vol.23 , pp. 925-931
    • Yan, W.1    Feng, X.2    Chen, X.3    Hou, W.4    Zhu, J.-J.5
  • 154
    • 84862800580 scopus 로고    scopus 로고
    • Direct electrochemistry of glucose oxidase immobilized on nanostructured gold thin films and its application to bioelectrochemical glucose sensor
    • Qiu C., Wang X., Liu X., Hou S., Ma H. Direct electrochemistry of glucose oxidase immobilized on nanostructured gold thin films and its application to bioelectrochemical glucose sensor. Electrochim. Acta 2012, 67:140-146.
    • (2012) Electrochim. Acta , vol.67 , pp. 140-146
    • Qiu, C.1    Wang, X.2    Liu, X.3    Hou, S.4    Ma, H.5
  • 155
    • 77949654798 scopus 로고    scopus 로고
    • Glucose biosensor based on graphite electrodes modified with glucose oxidase and colloidal gold nanoparticles
    • German N., Ramanaviciene A., Voronovic J., Ramanavicius A. Glucose biosensor based on graphite electrodes modified with glucose oxidase and colloidal gold nanoparticles. Microchim. Acta 2010, 168:221-229.
    • (2010) Microchim. Acta , vol.168 , pp. 221-229
    • German, N.1    Ramanaviciene, A.2    Voronovic, J.3    Ramanavicius, A.4
  • 156
    • 79953234742 scopus 로고    scopus 로고
    • Emerging transparent electrodes based on thin films of carbon nanotubes, graphene, and metallic nanostructures
    • Hecht D.S., Hu L., Irvin G. Emerging transparent electrodes based on thin films of carbon nanotubes, graphene, and metallic nanostructures. Adv. Mat. 2011, 23:1482-1513.
    • (2011) Adv. Mat. , vol.23 , pp. 1482-1513
    • Hecht, D.S.1    Hu, L.2    Irvin, G.3
  • 157
    • 79955470553 scopus 로고    scopus 로고
    • Thermal conductivity of carbon nanotubes and their polymer nanocomposites: a review
    • Han Z., Fina A. Thermal conductivity of carbon nanotubes and their polymer nanocomposites: a review. Prog. Polym. Sci. 2011, 36:914-944.
    • (2011) Prog. Polym. Sci. , vol.36 , pp. 914-944
    • Han, Z.1    Fina, A.2
  • 158
    • 76749095072 scopus 로고    scopus 로고
    • Assessing the strengths and weaknesses of various types of pre-treatments of carbon nanotubes on the properties of polymer/carbon nanotubes composites: a critical review
    • Bose S., Khare R.A., Moldenaers P. Assessing the strengths and weaknesses of various types of pre-treatments of carbon nanotubes on the properties of polymer/carbon nanotubes composites: a critical review. Polymer 2010, 51:975-993.
    • (2010) Polymer , vol.51 , pp. 975-993
    • Bose, S.1    Khare, R.A.2    Moldenaers, P.3
  • 161
    • 34547445627 scopus 로고    scopus 로고
    • Multiwall carbon nanotube elastomeric composites: a review
    • Liliane B. Multiwall carbon nanotube elastomeric composites: a review. Polymer 2007, 48:4907-4920.
    • (2007) Polymer , vol.48 , pp. 4907-4920
    • Liliane, B.1
  • 162
    • 16844377779 scopus 로고    scopus 로고
    • Characterization methods of carbon nanotubes: a review
    • Belin T., Epron F. Characterization methods of carbon nanotubes: a review. Mater. Sci. Eng. B 2005, 119:105-118.
    • (2005) Mater. Sci. Eng. B , vol.119 , pp. 105-118
    • Belin, T.1    Epron, F.2
  • 164
    • 69949120086 scopus 로고    scopus 로고
    • A glucose biosensor based on direct electrochemistry of glucose oxidase immobilized on nitrogen-doped carbon nanotubes
    • Deng S., Jian G., Lei J., Hu Z., Ju H. A glucose biosensor based on direct electrochemistry of glucose oxidase immobilized on nitrogen-doped carbon nanotubes. Biosens. Bioelectron. 2009, 25:373-377.
    • (2009) Biosens. Bioelectron. , vol.25 , pp. 373-377
    • Deng, S.1    Jian, G.2    Lei, J.3    Hu, Z.4    Ju, H.5
  • 165
    • 79952483874 scopus 로고    scopus 로고
    • A sensitive and stable biosensor based on the direct electrochemistry of glucose oxidase assembled layer-by-layer at the multiwall carbon nanotube-modified electrode
    • Deng C., Chen J., Nie Z., Si S. A sensitive and stable biosensor based on the direct electrochemistry of glucose oxidase assembled layer-by-layer at the multiwall carbon nanotube-modified electrode. Biosens. Bioelectron. 2010, 26:213-219.
    • (2010) Biosens. Bioelectron. , vol.26 , pp. 213-219
    • Deng, C.1    Chen, J.2    Nie, Z.3    Si, S.4
  • 166
    • 82555170633 scopus 로고    scopus 로고
    • Engineering of glucose oxidase for direct electron transfer via site-specific gold nanoparticle conjugation
    • Holland J.T., Lau C., Brozik S., Atanassov P., Banta S. Engineering of glucose oxidase for direct electron transfer via site-specific gold nanoparticle conjugation. J. Am. Chem. Soc. 2011, 133:19262-19265.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19262-19265
    • Holland, J.T.1    Lau, C.2    Brozik, S.3    Atanassov, P.4    Banta, S.5
  • 167
    • 79953882917 scopus 로고    scopus 로고
    • Efficient direct electron transfer with enzyme on a nanostructured carbon film fabricated with a maskless top-down UV/ozone process
    • Ueda A., Kato D., Kurita R., Kamata T., Inokuchi H., Umemura S., Hirono S., Niwa O. Efficient direct electron transfer with enzyme on a nanostructured carbon film fabricated with a maskless top-down UV/ozone process. J. Am. Chem. Soc. 2011, 133:4840-4846.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4840-4846
    • Ueda, A.1    Kato, D.2    Kurita, R.3    Kamata, T.4    Inokuchi, H.5    Umemura, S.6    Hirono, S.7    Niwa, O.8
  • 168
    • 84891822540 scopus 로고    scopus 로고
    • On the direct electron transfer, sensing, and enzyme activity in the glucose oxidase/carbon nanotubes system
    • Wooten M., Karra S., Zhang M., Gorski W. On the direct electron transfer, sensing, and enzyme activity in the glucose oxidase/carbon nanotubes system. Anal. Chem. 2014, 86:752-757.
    • (2014) Anal. Chem. , vol.86 , pp. 752-757
    • Wooten, M.1    Karra, S.2    Zhang, M.3    Gorski, W.4
  • 169
    • 4143072613 scopus 로고    scopus 로고
    • Direct electron transfer of glucose oxidase promoted by carbon nanotubes
    • Cai C., Chen J. Direct electron transfer of glucose oxidase promoted by carbon nanotubes. Anal. Biochem. 2004, 332:75-83.
    • (2004) Anal. Biochem. , vol.332 , pp. 75-83
    • Cai, C.1    Chen, J.2
  • 170
    • 79956070050 scopus 로고    scopus 로고
    • A biosensor prepared by co-entrapment of a glucose oxidase and a carbon nanotube within an electrochemically deposited redox polymer multilayer
    • Gao Q., Guo Y., Liu J., Yuan X., Qi H., Zhang C. A biosensor prepared by co-entrapment of a glucose oxidase and a carbon nanotube within an electrochemically deposited redox polymer multilayer. Bioelectrochemistry 2011, 81:109-113.
    • (2011) Bioelectrochemistry , vol.81 , pp. 109-113
    • Gao, Q.1    Guo, Y.2    Liu, J.3    Yuan, X.4    Qi, H.5    Zhang, C.6
  • 171
    • 4444273470 scopus 로고    scopus 로고
    • Glucose biosensor prepared by glucose oxidase encapsulated sol-gel and carbon-nanotube-modified basal plane pyrolytic graphite electrode
    • Salimi A., Compton R.G., Hallaj R. Glucose biosensor prepared by glucose oxidase encapsulated sol-gel and carbon-nanotube-modified basal plane pyrolytic graphite electrode. Anal. Biochem. 2004, 333:49-56.
    • (2004) Anal. Biochem. , vol.333 , pp. 49-56
    • Salimi, A.1    Compton, R.G.2    Hallaj, R.3
  • 172
    • 38148998755 scopus 로고    scopus 로고
    • Development of single-wall carbon nanotubes modified screen-printed electrode using a ferrocene-modified cationic surfactant for amperometric glucose biosensor applications
    • Sato N., Okuma H. Development of single-wall carbon nanotubes modified screen-printed electrode using a ferrocene-modified cationic surfactant for amperometric glucose biosensor applications. Sens. Actuators B 2008, 129:188-194.
    • (2008) Sens. Actuators B , vol.129 , pp. 188-194
    • Sato, N.1    Okuma, H.2
  • 174
    • 70349734865 scopus 로고    scopus 로고
    • Biocatalytic anode for glucose oxidation utilizing carbon nanotubes for direct electron transfer with glucose oxidase
    • Vaze A., Hussain N., Tang C., Leech D., Rusling J. Biocatalytic anode for glucose oxidation utilizing carbon nanotubes for direct electron transfer with glucose oxidase. Electrochem. Commun. 2009, 11:2004-2007.
    • (2009) Electrochem. Commun. , vol.11 , pp. 2004-2007
    • Vaze, A.1    Hussain, N.2    Tang, C.3    Leech, D.4    Rusling, J.5
  • 175
    • 84858153967 scopus 로고    scopus 로고
    • Amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode
    • Monosik R., Stredansky M., Luspai K., Magdolen P., Sturdik E. Amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode. Enzyme Microb. Technol. 2012, 50:227-232.
    • (2012) Enzyme Microb. Technol. , vol.50 , pp. 227-232
    • Monosik, R.1    Stredansky, M.2    Luspai, K.3    Magdolen, P.4    Sturdik, E.5
  • 176
    • 60549114855 scopus 로고    scopus 로고
    • Development of amperometric glucose biosensor based on glucose oxidase co-immobilized with multi-walled carbon nanotubes at low potential
    • Rahman M.M., Umar A., Sawada K. Development of amperometric glucose biosensor based on glucose oxidase co-immobilized with multi-walled carbon nanotubes at low potential. Sens. Actuators B 2009, 137:327-333.
    • (2009) Sens. Actuators B , vol.137 , pp. 327-333
    • Rahman, M.M.1    Umar, A.2    Sawada, K.3
  • 177
    • 65249137740 scopus 로고    scopus 로고
    • A glucose biosensor based on deposition of glucose oxidase onto crystalline gold nanoparticle modified carbon nanotube electrode
    • Rakhi R.B., Sethupathi K., Ramaprabhu S. A glucose biosensor based on deposition of glucose oxidase onto crystalline gold nanoparticle modified carbon nanotube electrode. J. Phys. Chem. B 2009, 113:3190-3194.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3190-3194
    • Rakhi, R.B.1    Sethupathi, K.2    Ramaprabhu, S.3
  • 178
    • 14344256125 scopus 로고    scopus 로고
    • Carbon-nanotube based electrochemical biosensors: a review
    • Wang J. Carbon-nanotube based electrochemical biosensors: a review. Electroanalysis 2005, 17:7-14.
    • (2005) Electroanalysis , vol.17 , pp. 7-14
    • Wang, J.1
  • 180
    • 33747447535 scopus 로고    scopus 로고
    • Optical properties and photonic devices of doped carbon nanotubes
    • Zhao J., Chen X., Xie J.R.H. Optical properties and photonic devices of doped carbon nanotubes. Anal. Chim. Acta 2006, 568:161-170.
    • (2006) Anal. Chim. Acta , vol.568 , pp. 161-170
    • Zhao, J.1    Chen, X.2    Xie, J.R.H.3
  • 181
    • 39649091200 scopus 로고    scopus 로고
    • Direct electrochemistry of glucose oxidase and biosensing for glucose based on boron-doped carbon nanotubes modified electrode
    • Deng C., Chen J., Chen X., Xiao C., Nie L., Yao S. Direct electrochemistry of glucose oxidase and biosensing for glucose based on boron-doped carbon nanotubes modified electrode. Biosens. Bioelectron. 2008, 23:1272-1277.
    • (2008) Biosens. Bioelectron. , vol.23 , pp. 1272-1277
    • Deng, C.1    Chen, J.2    Chen, X.3    Xiao, C.4    Nie, L.5    Yao, S.6
  • 183
    • 33748584326 scopus 로고    scopus 로고
    • Synergism of C5N six-membered ring and vapor-liquid-solid growth of CNx nanotubes with pyridine precursor
    • Chen H., Yang Y., Hu Z., Huo K., Ma Y., Chen Y., Wang X., Lu Y. Synergism of C5N six-membered ring and vapor-liquid-solid growth of CNx nanotubes with pyridine precursor. J. Phys. Chem. B 2006, 110:16422-16427.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 16422-16427
    • Chen, H.1    Yang, Y.2    Hu, Z.3    Huo, K.4    Ma, Y.5    Chen, Y.6    Wang, X.7    Lu, Y.8
  • 184
    • 84900856053 scopus 로고    scopus 로고
    • Electrochemical performance of electrospun free-standing nitrogen-doped carbon nanofibers and their application for glucose biosensing
    • Liu D., Zhang X., You T. Electrochemical performance of electrospun free-standing nitrogen-doped carbon nanofibers and their application for glucose biosensing. ACS Appl. Mater. Interfaces 2014, 6:6275-6280.
    • (2014) ACS Appl. Mater. Interfaces , vol.6 , pp. 6275-6280
    • Liu, D.1    Zhang, X.2    You, T.3
  • 185
    • 74249111942 scopus 로고    scopus 로고
    • A novel glucose biosensor based on glucose oxidase immobilized on AuPt nanoparticle-carbon nanotube-ionic liquid hybrid coated electrode
    • Zhang Y., Guo G., Zhao F., Mo Z., Xiao F., Zeng B. A novel glucose biosensor based on glucose oxidase immobilized on AuPt nanoparticle-carbon nanotube-ionic liquid hybrid coated electrode. Electroanalysis 2010, 22:223-228.
    • (2010) Electroanalysis , vol.22 , pp. 223-228
    • Zhang, Y.1    Guo, G.2    Zhao, F.3    Mo, Z.4    Xiao, F.5    Zeng, B.6
  • 186
    • 56049092009 scopus 로고    scopus 로고
    • Disposable biosensor based on immobilization of glucose oxidase at gold nanoparticles electrodeposited on indium tin oxide electrode
    • Wang J., Wang L., Di J., Tu Y. Disposable biosensor based on immobilization of glucose oxidase at gold nanoparticles electrodeposited on indium tin oxide electrode. Sens. Actuators B 2008, 135:283-288.
    • (2008) Sens. Actuators B , vol.135 , pp. 283-288
    • Wang, J.1    Wang, L.2    Di, J.3    Tu, Y.4
  • 187
    • 84867098967 scopus 로고    scopus 로고
    • Glucose biosensor based on glucose oxidase and gold nanoparticles of different sizes covered by polypyrrole layer
    • German N., Ramanavicius A., Voronovic J., Ramanaviciene A. Glucose biosensor based on glucose oxidase and gold nanoparticles of different sizes covered by polypyrrole layer. Colloids Surf. A 2012, 413:224-230.
    • (2012) Colloids Surf. A , vol.413 , pp. 224-230
    • German, N.1    Ramanavicius, A.2    Voronovic, J.3    Ramanaviciene, A.4
  • 188
    • 22944457193 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase on gold nanoparticles modified Au electrode for the construction of biosensor
    • Zhang S., Wang N., Niu Y., Sun C. Immobilization of glucose oxidase on gold nanoparticles modified Au electrode for the construction of biosensor. Sens. Actuators B 2005, 109:367-374.
    • (2005) Sens. Actuators B , vol.109 , pp. 367-374
    • Zhang, S.1    Wang, N.2    Niu, Y.3    Sun, C.4
  • 189
    • 79952490423 scopus 로고    scopus 로고
    • Amperometric glucose biosensor based on integration of glucose oxidase with platinum nanoparticles/ordered mesoporous carbon nanocomposite
    • Jiang X., Wu Y., Mao X., Cui X., Zhu L. Amperometric glucose biosensor based on integration of glucose oxidase with platinum nanoparticles/ordered mesoporous carbon nanocomposite. Sens. Actuators B 2011, 153:158-163.
    • (2011) Sens. Actuators B , vol.153 , pp. 158-163
    • Jiang, X.1    Wu, Y.2    Mao, X.3    Cui, X.4    Zhu, L.5
  • 190
    • 3042708176 scopus 로고    scopus 로고
    • Amperometric glucose biosensor based on adsorption of glucose oxidase at platinum nanoparticle-modified carbon nanotube electrode
    • Tang H., Chen J., Yao S., Nie L., Deng G., Kuang Y. Amperometric glucose biosensor based on adsorption of glucose oxidase at platinum nanoparticle-modified carbon nanotube electrode. Anal. Biochem. 2004, 331:89-97.
    • (2004) Anal. Biochem. , vol.331 , pp. 89-97
    • Tang, H.1    Chen, J.2    Yao, S.3    Nie, L.4    Deng, G.5    Kuang, Y.6
  • 191
    • 70349230816 scopus 로고    scopus 로고
    • Glucose biosensor based on immobilization of glucose oxidase in platinum nanoparticles/graphene/chitosan nanocomposite film
    • Wu H., Wang J., Kang X., Wang C., Wang D., Liu J., Aksay I.A., Lin Y. Glucose biosensor based on immobilization of glucose oxidase in platinum nanoparticles/graphene/chitosan nanocomposite film. Talanta 2009, 80:403-406.
    • (2009) Talanta , vol.80 , pp. 403-406
    • Wu, H.1    Wang, J.2    Kang, X.3    Wang, C.4    Wang, D.5    Liu, J.6    Aksay, I.A.7    Lin, Y.8
  • 192
    • 68149161818 scopus 로고    scopus 로고
    • Biosensor enhanced by glucose oxidase biomimetic membrane containing the platinum and silica nanoparticles
    • Ren X., Meng X., Tang F., Zhang L. Biosensor enhanced by glucose oxidase biomimetic membrane containing the platinum and silica nanoparticles. Mater. Sci. Eng. C 2009, 29:2234-2238.
    • (2009) Mater. Sci. Eng. C , vol.29 , pp. 2234-2238
    • Ren, X.1    Meng, X.2    Tang, F.3    Zhang, L.4
  • 193
    • 79952532841 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase and platinum on mesoporous silica nanoparticles for the fabrication of glucose biosensor
    • Li H., He J., Zhao Y., Wu D., Cai Y., Wei Q., Yang M. Immobilization of glucose oxidase and platinum on mesoporous silica nanoparticles for the fabrication of glucose biosensor. Electrochim. Acta 2011, 56:2960-2965.
    • (2011) Electrochim. Acta , vol.56 , pp. 2960-2965
    • Li, H.1    He, J.2    Zhao, Y.3    Wu, D.4    Cai, Y.5    Wei, Q.6    Yang, M.7
  • 194
    • 79960460989 scopus 로고    scopus 로고
    • A novel glucose biosensor based on direct electrochemistry of glucose oxidase incorporated in biomediated gold nanoparticles-carbon nanotubes composite film
    • Zhang H., Meng Z., Wang Q., Zheng J. A novel glucose biosensor based on direct electrochemistry of glucose oxidase incorporated in biomediated gold nanoparticles-carbon nanotubes composite film. Sens. Actuators B 2011, 158:23-27.
    • (2011) Sens. Actuators B , vol.158 , pp. 23-27
    • Zhang, H.1    Meng, Z.2    Wang, Q.3    Zheng, J.4
  • 195
    • 78751580665 scopus 로고    scopus 로고
    • A novel glucose sensor based on ordered mesoporous carbon-Au nanoparticles nanocomposites
    • Wang L., Bai J., Bo X., Zhang X., Guo L. A novel glucose sensor based on ordered mesoporous carbon-Au nanoparticles nanocomposites. Talanta 2011, 83:1386-1391.
    • (2011) Talanta , vol.83 , pp. 1386-1391
    • Wang, L.1    Bai, J.2    Bo, X.3    Zhang, X.4    Guo, L.5
  • 196
    • 84871767167 scopus 로고    scopus 로고
    • Graphene oxide as a matrix for the immobilization of glucose oxidase
    • Zhou L., Jiang Y., Gao J., Zhao X., Ma L. Graphene oxide as a matrix for the immobilization of glucose oxidase. Appl. Biochem. Biotechnol. 2012, 168:1635-1642.
    • (2012) Appl. Biochem. Biotechnol. , vol.168 , pp. 1635-1642
    • Zhou, L.1    Jiang, Y.2    Gao, J.3    Zhao, X.4    Ma, L.5
  • 197
    • 70350394842 scopus 로고    scopus 로고
    • Glucose oxidase-graphene-chitosan modified electrode for direct electrochemistry and glucose sensing
    • Kang X., Wang J., Wu H., Aksay I.A., Liu J., Lin Y. Glucose oxidase-graphene-chitosan modified electrode for direct electrochemistry and glucose sensing. Biosens. Bioelectron. 2009, 25:901-905.
    • (2009) Biosens. Bioelectron. , vol.25 , pp. 901-905
    • Kang, X.1    Wang, J.2    Wu, H.3    Aksay, I.A.4    Liu, J.5    Lin, Y.6
  • 198
    • 80053239590 scopus 로고    scopus 로고
    • An ultrasensitive electrochemical biosensor for glucose using CdTe-CdS core-shell quantum dot as ultrafast electron transfer relay between graphene-gold nanocomposite and gold nanoparticle
    • Zhiguo G., Shuping Y., Zaijun L., Xiulan S., Guangli W., Yinjun F., Junkang L. An ultrasensitive electrochemical biosensor for glucose using CdTe-CdS core-shell quantum dot as ultrafast electron transfer relay between graphene-gold nanocomposite and gold nanoparticle. Electrochim. Acta 2011, 56:9162-9167.
    • (2011) Electrochim. Acta , vol.56 , pp. 9162-9167
    • Zhiguo, G.1    Shuping, Y.2    Zaijun, L.3    Xiulan, S.4    Guangli, W.5    Yinjun, F.6    Junkang, L.7
  • 199
    • 78650627436 scopus 로고    scopus 로고
    • Enhanced direct electrochemistry of glucose oxidase and biosensing for glucose via synergy effect of graphene and CdS nanocrystals
    • Wang K., Liu Q., Guan Q.-M., Wu J., Li H.-N., Yan J.-J. Enhanced direct electrochemistry of glucose oxidase and biosensing for glucose via synergy effect of graphene and CdS nanocrystals. Biosens. Bioelectron. 2011, 26:2252-2257.
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 2252-2257
    • Wang, K.1    Liu, Q.2    Guan, Q.-M.3    Wu, J.4    Li, H.-N.5    Yan, J.-J.6
  • 201
    • 79952484847 scopus 로고    scopus 로고
    • An amperometric glucose biosensor based on layer-by-layer GOx-SWCNT conjugate/redox polymer multilayer on a screen-printed carbon electrode
    • Gao Q., Guo Y., Zhang W., Qi H., Zhang C. An amperometric glucose biosensor based on layer-by-layer GOx-SWCNT conjugate/redox polymer multilayer on a screen-printed carbon electrode. Sens. Actuators B 2011, 153:219-225.
    • (2011) Sens. Actuators B , vol.153 , pp. 219-225
    • Gao, Q.1    Guo, Y.2    Zhang, W.3    Qi, H.4    Zhang, C.5
  • 203
    • 61449143423 scopus 로고    scopus 로고
    • Electrochemistry and biosensing of glucose oxidase based on mesoporous carbons with different spatially ordered dimensions
    • You C., Xu X., Tian B., Kong J., Zhao D., Liu B. Electrochemistry and biosensing of glucose oxidase based on mesoporous carbons with different spatially ordered dimensions. Talanta 2009, 78:705-710.
    • (2009) Talanta , vol.78 , pp. 705-710
    • You, C.1    Xu, X.2    Tian, B.3    Kong, J.4    Zhao, D.5    Liu, B.6
  • 204
    • 41149145238 scopus 로고    scopus 로고
    • New horizons in spectroelectrochemical measurements: optically transparent carbon electrodes
    • Dai Y., Swain G.M., Porter M.D., Zak J. New horizons in spectroelectrochemical measurements: optically transparent carbon electrodes. Anal. Chem. 2008, 80:14-22.
    • (2008) Anal. Chem. , vol.80 , pp. 14-22
    • Dai, Y.1    Swain, G.M.2    Porter, M.D.3    Zak, J.4
  • 205
    • 84874863945 scopus 로고    scopus 로고
    • Ultrathin optically transparent carbon electrodes produced from layers of adsorbed proteins
    • Alharthi S.A., Benavidez T.E., Garcia C.D. Ultrathin optically transparent carbon electrodes produced from layers of adsorbed proteins. Langmuir 2013, 29:3320-3327.
    • (2013) Langmuir , vol.29 , pp. 3320-3327
    • Alharthi, S.A.1    Benavidez, T.E.2    Garcia, C.D.3
  • 206
    • 84880684754 scopus 로고    scopus 로고
    • Spectroscopic and electrochemical characterization of nanostructured optically transparent carbon electrodes
    • Benavidez T.E., Garcia C.D. Spectroscopic and electrochemical characterization of nanostructured optically transparent carbon electrodes. Electrophoresis 2013, 34:1998-2006.
    • (2013) Electrophoresis , vol.34 , pp. 1998-2006
    • Benavidez, T.E.1    Garcia, C.D.2
  • 209
    • 34548499561 scopus 로고    scopus 로고
    • A novel amperometric biosensor based on ZnO:Co nanoclusters for biosensing glucose
    • Zhao Z.W., Chen X.J., Tay B.K., Chen J.S., Han Z.J., Khor K.A. A novel amperometric biosensor based on ZnO:Co nanoclusters for biosensing glucose. Biosens. Bioelectron. 2007, 23:135-139.
    • (2007) Biosens. Bioelectron. , vol.23 , pp. 135-139
    • Zhao, Z.W.1    Chen, X.J.2    Tay, B.K.3    Chen, J.S.4    Han, Z.J.5    Khor, K.A.6
  • 210
    • 78049261939 scopus 로고    scopus 로고
    • ZnO based third generation biosensor
    • Gupta V. ZnO based third generation biosensor. Thin Solid Films 2010, 519:1141-1144.
    • (2010) Thin Solid Films , vol.519 , pp. 1141-1144
    • Gupta, V.1
  • 211
    • 79956340885 scopus 로고    scopus 로고
    • A glucose oxidase immobilization platform for glucose biosensor using ZnO hollow nanospheres
    • Fang B., Zhang C., Wang G., Wang M., Ji Y. A glucose oxidase immobilization platform for glucose biosensor using ZnO hollow nanospheres. Sens. Actuators B 2011, 155:304-310.
    • (2011) Sens. Actuators B , vol.155 , pp. 304-310
    • Fang, B.1    Zhang, C.2    Wang, G.3    Wang, M.4    Ji, Y.5
  • 212
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: a modern view of a classic enzyme
    • Veitch N.C. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 2004, 65:249-259.
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Veitch, N.C.1
  • 214
    • 79957793222 scopus 로고    scopus 로고
    • A label-free amperometric immunosensor based on horseradish peroxidase functionalized carbon nanotubes and bilayer gold nanoparticles
    • Liu S., Yuan R., Chai Y., Su H. A label-free amperometric immunosensor based on horseradish peroxidase functionalized carbon nanotubes and bilayer gold nanoparticles. Sens. Actuators B 2011, 156:388-394.
    • (2011) Sens. Actuators B , vol.156 , pp. 388-394
    • Liu, S.1    Yuan, R.2    Chai, Y.3    Su, H.4
  • 215
    • 84863676133 scopus 로고    scopus 로고
    • Graphene-oxide-based immunosensing through fluorescence quenching by peroxidase-catalyzed polymerization
    • Lim S.Y., Ahn J., Lee J.S., Kim M.-G., Park C.B. Graphene-oxide-based immunosensing through fluorescence quenching by peroxidase-catalyzed polymerization. Small 2012, 8:1994-1999.
    • (2012) Small , vol.8 , pp. 1994-1999
    • Lim, S.Y.1    Ahn, J.2    Lee, J.S.3    Kim, M.-G.4    Park, C.B.5
  • 216
    • 84870532152 scopus 로고    scopus 로고
    • Catalytic activity and stability of glucose oxidase/horseradish peroxidase co-confined in macroporous silica foam
    • Cao X., Li Y., Zhang Z., Yu J., Qian J., Liu S. Catalytic activity and stability of glucose oxidase/horseradish peroxidase co-confined in macroporous silica foam. Analyst 2012, 137:5785-5791.
    • (2012) Analyst , vol.137 , pp. 5785-5791
    • Cao, X.1    Li, Y.2    Zhang, Z.3    Yu, J.4    Qian, J.5    Liu, S.6
  • 218
    • 33847158789 scopus 로고    scopus 로고
    • A mediator-free amperometric hydrogen peroxide biosensor based on HRP immobilized on a nano-Au/poly 2, 6-pyridinediamine-coated electrode
    • Cao S., Yuan R., Chai Y., Zhang L., Li X., Gao F. A mediator-free amperometric hydrogen peroxide biosensor based on HRP immobilized on a nano-Au/poly 2, 6-pyridinediamine-coated electrode. Bioprocess. Biosyst. Eng. 2007, 30:71-78.
    • (2007) Bioprocess. Biosyst. Eng. , vol.30 , pp. 71-78
    • Cao, S.1    Yuan, R.2    Chai, Y.3    Zhang, L.4    Li, X.5    Gao, F.6
  • 219
    • 33644865654 scopus 로고    scopus 로고
    • Amperometric hydrogen peroxide biosensor based on the immobilization of horseradish peroxidase (hrp) on the layer-by-layer assembly films of gold colloidal nanoparticles and toluidine blue
    • Chen S., Yuan R., Chai Y., Xu L., Wang N., Li X., Zhang L. Amperometric hydrogen peroxide biosensor based on the immobilization of horseradish peroxidase (hrp) on the layer-by-layer assembly films of gold colloidal nanoparticles and toluidine blue. Electroanalysis 2006, 18:471-477.
    • (2006) Electroanalysis , vol.18 , pp. 471-477
    • Chen, S.1    Yuan, R.2    Chai, Y.3    Xu, L.4    Wang, N.5    Li, X.6    Zhang, L.7
  • 220
    • 33847625944 scopus 로고    scopus 로고
    • Amperometric hydrogen peroxide biosensor based on the immobilization of HRP on nano-Au/Thi/poly p-aminobenzene sulfonic acid)-modified glassy carbon electrode
    • Gao F., Yuan R., Chai Y., Chen S., Cao S., Tang M. Amperometric hydrogen peroxide biosensor based on the immobilization of HRP on nano-Au/Thi/poly p-aminobenzene sulfonic acid)-modified glassy carbon electrode. J. Biochem. Biophys. Methods 2007, 70:407-413.
    • (2007) J. Biochem. Biophys. Methods , vol.70 , pp. 407-413
    • Gao, F.1    Yuan, R.2    Chai, Y.3    Chen, S.4    Cao, S.5    Tang, M.6
  • 221
    • 0036558189 scopus 로고    scopus 로고
    • A method to construct a third-generation horseradish peroxidase biosensor: self-assembling gold nanoparticles to three-dimensional sol-gel network
    • Jia J., Wang B., Wu A., Cheng G., Li Z., Dong S. A method to construct a third-generation horseradish peroxidase biosensor: self-assembling gold nanoparticles to three-dimensional sol-gel network. Anal. Chem. 2002, 74:2217-2223.
    • (2002) Anal. Chem. , vol.74 , pp. 2217-2223
    • Jia, J.1    Wang, B.2    Wu, A.3    Cheng, G.4    Li, Z.5    Dong, S.6
  • 222
    • 7544240840 scopus 로고    scopus 로고
    • An amperometric hydrogen peroxide biosensor based on immobilizing horseradish peroxidase to a nano-Au monolayer supported by sol-gel derived carbon ceramic electrode
    • Lei C.-X., Hu S.-Q., Gao N., Shen G.-L., Yu R.-Q. An amperometric hydrogen peroxide biosensor based on immobilizing horseradish peroxidase to a nano-Au monolayer supported by sol-gel derived carbon ceramic electrode. Bioelectrochemistry 2004, 65:33-39.
    • (2004) Bioelectrochemistry , vol.65 , pp. 33-39
    • Lei, C.-X.1    Hu, S.-Q.2    Gao, N.3    Shen, G.-L.4    Yu, R.-Q.5
  • 223
    • 84855528185 scopus 로고    scopus 로고
    • Hydrogen peroxide biosensor based on gold nanoparticles/thionine/gold nanoparticles/multi-walled carbon nanotubes-chitosans composite film-modified electrode
    • Li S., Zhu X., Zhang W., Xie G., Feng W. Hydrogen peroxide biosensor based on gold nanoparticles/thionine/gold nanoparticles/multi-walled carbon nanotubes-chitosans composite film-modified electrode. Appl. Surf. Sci. 2012, 258:2802-2807.
    • (2012) Appl. Surf. Sci. , vol.258 , pp. 2802-2807
    • Li, S.1    Zhu, X.2    Zhang, W.3    Xie, G.4    Feng, W.5
  • 224
    • 33645966237 scopus 로고    scopus 로고
    • Direct electrochemistry of horseradish peroxidase immobilized on gold colloid/cysteine/Nafion-modified platinum disk electrode
    • Liu Y., Yuan R., Chai Y., Tang D., Dai J., Zhong X. Direct electrochemistry of horseradish peroxidase immobilized on gold colloid/cysteine/Nafion-modified platinum disk electrode. Sens. Actuators B 2006, 115:109-115.
    • (2006) Sens. Actuators B , vol.115 , pp. 109-115
    • Liu, Y.1    Yuan, R.2    Chai, Y.3    Tang, D.4    Dai, J.5    Zhong, X.6
  • 225
    • 20444436289 scopus 로고    scopus 로고
    • Electrochemically deposited chitosan hydrogel for horseradish peroxidase immobilization through gold nanoparticles self-assembly
    • Luo X.-L., Xu J.-J., Zhang Q., Yang G.-J., Chen H.-Y. Electrochemically deposited chitosan hydrogel for horseradish peroxidase immobilization through gold nanoparticles self-assembly. Biosens. Bioelectron. 2005, 21:190-196.
    • (2005) Biosens. Bioelectron. , vol.21 , pp. 190-196
    • Luo, X.-L.1    Xu, J.-J.2    Zhang, Q.3    Yang, G.-J.4    Chen, H.-Y.5
  • 227
    • 57249095764 scopus 로고    scopus 로고
    • Electrodeposition of gold nanoparticles on indium/tin oxide electrode for fabrication of a disposable hydrogen peroxide biosensor
    • Wang J., Wang L., Di J., Tu Y. Electrodeposition of gold nanoparticles on indium/tin oxide electrode for fabrication of a disposable hydrogen peroxide biosensor. Talanta 2009, 77:1454-1459.
    • (2009) Talanta , vol.77 , pp. 1454-1459
    • Wang, J.1    Wang, L.2    Di, J.3    Tu, Y.4
  • 228
    • 77955430569 scopus 로고    scopus 로고
    • An amperometric hydrogen peroxide biosensor based on the immobilization of HRP on multi-walled carbon nanotubes/electro-copolymerized nano-Pt-poly (neutral red) composite membrane
    • Zhang Y., Yuan R., Chai Y., Xiang Y., Hong C., Ran X. An amperometric hydrogen peroxide biosensor based on the immobilization of HRP on multi-walled carbon nanotubes/electro-copolymerized nano-Pt-poly (neutral red) composite membrane. Biochem. Eng. J. 2010, 51:102-109.
    • (2010) Biochem. Eng. J. , vol.51 , pp. 102-109
    • Zhang, Y.1    Yuan, R.2    Chai, Y.3    Xiang, Y.4    Hong, C.5    Ran, X.6
  • 229
    • 66349130442 scopus 로고    scopus 로고
    • Layer by layer immobilized horseradish peroxidase on zinc oxide nanorods for biosensing
    • Gu B., Xu C., Zhu G., Liu S., Chen L., Wang M., Zhu J. Layer by layer immobilized horseradish peroxidase on zinc oxide nanorods for biosensing. J. Phys. Chem. B. 2009, 113:6553-6557.
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 6553-6557
    • Gu, B.1    Xu, C.2    Zhu, G.3    Liu, S.4    Chen, L.5    Wang, M.6    Zhu, J.7
  • 230
    • 17144372617 scopus 로고    scopus 로고
    • Hydrogen peroxide sensor based on horseradish peroxidase immobilized on a silver nanoparticles/cysteamine/gold electrode
    • Ren C., Song Y., Li Z., Zhu G. Hydrogen peroxide sensor based on horseradish peroxidase immobilized on a silver nanoparticles/cysteamine/gold electrode. Anal. Bioanal. Chem. 2005, 381:1179-1185.
    • (2005) Anal. Bioanal. Chem. , vol.381 , pp. 1179-1185
    • Ren, C.1    Song, Y.2    Li, Z.3    Zhu, G.4
  • 231
    • 37449023688 scopus 로고    scopus 로고
    • Amperometric sensor for hydrogen peroxide based on electric wire composed of horseradish peroxidase and toluidine blue-multiwalled carbon nanotubes nanocomposite
    • Liu Y., Lei J., Ju H. Amperometric sensor for hydrogen peroxide based on electric wire composed of horseradish peroxidase and toluidine blue-multiwalled carbon nanotubes nanocomposite. Talanta 2008, 74:965-970.
    • (2008) Talanta , vol.74 , pp. 965-970
    • Liu, Y.1    Lei, J.2    Ju, H.3
  • 232
    • 54549089114 scopus 로고    scopus 로고
    • Dendritic silver/silicon dioxide nanocomposite modified electrodes for electrochemical sensing of hydrogen peroxide
    • Yuan P., Zhuo Y., Chai Y., Ju H. Dendritic silver/silicon dioxide nanocomposite modified electrodes for electrochemical sensing of hydrogen peroxide. Electroanalysis 2008, 20:1839-1844.
    • (2008) Electroanalysis , vol.20 , pp. 1839-1844
    • Yuan, P.1    Zhuo, Y.2    Chai, Y.3    Ju, H.4
  • 233
    • 84861906936 scopus 로고    scopus 로고
    • Development of an amperometric hydrogen peroxide biosensor based on the immobilization of horseradish peroxidase onto nickel ferrite nanoparticle-chitosan composite
    • Furkan Y., Emre Ç., Mehmet Ş., Abdülhadi B. Development of an amperometric hydrogen peroxide biosensor based on the immobilization of horseradish peroxidase onto nickel ferrite nanoparticle-chitosan composite. Nano-Micro Lett. 2011, 3:91-98.
    • (2011) Nano-Micro Lett. , vol.3 , pp. 91-98
    • Furkan, Y.1    Emre, Ç.2    Mehmet, Ş.3    Abdülhadi, B.4
  • 234
    • 81855198177 scopus 로고    scopus 로고
    • Fabrication of an electrochemical platform based on the self-assembly of graphene oxide-multiwall carbon nanotube nanocomposite and horseradish peroxidase: direct electrochemistry and electrocatalysis
    • Zhang Q., Yang S., Zhang J., Zhang L., Kang P., Li J., Xu J., Zhou H., Song X.-M. Fabrication of an electrochemical platform based on the self-assembly of graphene oxide-multiwall carbon nanotube nanocomposite and horseradish peroxidase: direct electrochemistry and electrocatalysis. Nanotechnology 2011, 22:494010.
    • (2011) Nanotechnology , vol.22 , pp. 494010
    • Zhang, Q.1    Yang, S.2    Zhang, J.3    Zhang, L.4    Kang, P.5    Li, J.6    Xu, J.7    Zhou, H.8    Song, X.-M.9
  • 235
    • 82355190204 scopus 로고    scopus 로고
    • A amperometric biosensor for hydrogen peroxide by adsorption of horseradish peroxidase onto single-walled carbon nanotubes
    • Wang Y., Du J., Li Y., Shan D., Zhou X., Xue Z., Lu X. A amperometric biosensor for hydrogen peroxide by adsorption of horseradish peroxidase onto single-walled carbon nanotubes. Colloids Surf. B 2012, 90:62-67.
    • (2012) Colloids Surf. B , vol.90 , pp. 62-67
    • Wang, Y.1    Du, J.2    Li, Y.3    Shan, D.4    Zhou, X.5    Xue, Z.6    Lu, X.7
  • 236
    • 72649092649 scopus 로고    scopus 로고
    • Glutathione peroxidases in different stages of carcinogenesis
    • Brigelius-Flohé R., Kipp A. Glutathione peroxidases in different stages of carcinogenesis. Biochim. Biophys. Acta, Gen. Subj. 2009, 1790:1555-1568.
    • (2009) Biochim. Biophys. Acta, Gen. Subj. , vol.1790 , pp. 1555-1568
    • Brigelius-Flohé, R.1    Kipp, A.2
  • 237
    • 78651518934 scopus 로고    scopus 로고
    • Immobilization of catalase via adsorption on poly(styrene-d-glycidylmethacrylate) grafted and tetraethyldiethylenetriamine ligand attached microbeads
    • Bayramoglu G., Karagoz B., Yilmaz M., Bicak N., Arica M.Y. Immobilization of catalase via adsorption on poly(styrene-d-glycidylmethacrylate) grafted and tetraethyldiethylenetriamine ligand attached microbeads. Bioresour. Technol. 2011, 102:3653-3661.
    • (2011) Bioresour. Technol. , vol.102 , pp. 3653-3661
    • Bayramoglu, G.1    Karagoz, B.2    Yilmaz, M.3    Bicak, N.4    Arica, M.Y.5
  • 240
    • 33846328380 scopus 로고    scopus 로고
    • Direct electrochemistry and electrocatalytic activity of catalase immobilized onto electrodeposited nano-scale islands of nickel oxide
    • Salimi A., Sharifi E., Noorbakhsh A., Soltanian S. Direct electrochemistry and electrocatalytic activity of catalase immobilized onto electrodeposited nano-scale islands of nickel oxide. Biophys. Chem. 2007, 125:540-548.
    • (2007) Biophys. Chem. , vol.125 , pp. 540-548
    • Salimi, A.1    Sharifi, E.2    Noorbakhsh, A.3    Soltanian, S.4
  • 241
    • 4544231687 scopus 로고    scopus 로고
    • Direct electrochemistry of catalase at a gold electrode modified with single-wall carbon nanotubes
    • Wang L., Wang J., Zhou F. Direct electrochemistry of catalase at a gold electrode modified with single-wall carbon nanotubes. Electroanalysis 2004, 16:627-632.
    • (2004) Electroanalysis , vol.16 , pp. 627-632
    • Wang, L.1    Wang, J.2    Zhou, F.3
  • 242
    • 78650355327 scopus 로고    scopus 로고
    • Adsorption kinetics of catalase to thin films of carbon nanotubes
    • Felhofer J.L., Caranto J.D., Garcia C.D. Adsorption kinetics of catalase to thin films of carbon nanotubes. Langmuir 2010, 26:17178-17183.
    • (2010) Langmuir , vol.26 , pp. 17178-17183
    • Felhofer, J.L.1    Caranto, J.D.2    Garcia, C.D.3
  • 243
    • 84887587488 scopus 로고    scopus 로고
    • Activity of catalase adsorbed to carbon nanotubes: effects of carbon nanotube surface properties
    • Zhang C., Luo S., Chen W. Activity of catalase adsorbed to carbon nanotubes: effects of carbon nanotube surface properties. Talanta 2013, 113:142-147.
    • (2013) Talanta , vol.113 , pp. 142-147
    • Zhang, C.1    Luo, S.2    Chen, W.3
  • 244
    • 84858962973 scopus 로고    scopus 로고
    • Electrochemical l-lactic acid sensor based on immobilized ZnO nanorods with lactate oxidase
    • Ibupoto Z.H., Shah S.M., Khun K., Willander M. Electrochemical l-lactic acid sensor based on immobilized ZnO nanorods with lactate oxidase. Sensors 2012, 12:2456-2466.
    • (2012) Sensors , vol.12 , pp. 2456-2466
    • Ibupoto, Z.H.1    Shah, S.M.2    Khun, K.3    Willander, M.4
  • 246
    • 38949120095 scopus 로고    scopus 로고
    • A lactate electrochemical biosensor with a titanate nanotube as direct electron transfer promoter
    • Mingli Y., Jin W., Huaqing L., Jian-Guo Z., Nianqiang Nick W. A lactate electrochemical biosensor with a titanate nanotube as direct electron transfer promoter. Nanotechnology 2008, 19:075502.
    • (2008) Nanotechnology , vol.19 , pp. 075502
    • Mingli, Y.1    Jin, W.2    Huaqing, L.3    Jian-Guo, Z.4    Nianqiang Nick, W.5
  • 247
    • 47149096751 scopus 로고    scopus 로고
    • Development of an amperometric l-lactate biosensor based on l-lactate oxidase immobilized through silica sol-gel film on multi-walled carbon nanotubes/platinum nanoparticle modified glassy carbon electrode
    • Huang J., Li J., Yang Y., Wang X., Wu B., J.-i.Anzai T., Osa, Chen Q. Development of an amperometric l-lactate biosensor based on l-lactate oxidase immobilized through silica sol-gel film on multi-walled carbon nanotubes/platinum nanoparticle modified glassy carbon electrode. Mater. Sci. Eng. C 2008, 28:1070-1075.
    • (2008) Mater. Sci. Eng. C , vol.28 , pp. 1070-1075
    • Huang, J.1    Li, J.2    Yang, Y.3    Wang, X.4    Wu, B.5    Anzai, J.-i.T.6    Osa, C.Q.7
  • 248
    • 80053338504 scopus 로고    scopus 로고
    • A novel l-lactate sensor based on enzyme electrode modified with ZnO nanoparticles and multiwall carbon nanotubes
    • Wang Y.T., Yu L., Wang J., Lou L., Du W.J., Zhu Z.Q., Peng H., Zhu J.Z. A novel l-lactate sensor based on enzyme electrode modified with ZnO nanoparticles and multiwall carbon nanotubes. J. Electroanal. Chem. 2011, 661:8-12.
    • (2011) J. Electroanal. Chem. , vol.661 , pp. 8-12
    • Wang, Y.T.1    Yu, L.2    Wang, J.3    Lou, L.4    Du, W.J.5    Zhu, Z.Q.6    Peng, H.7    Zhu, J.Z.8
  • 249
    • 80155134205 scopus 로고    scopus 로고
    • Amperometric detection of l-lactate using nitrogen-doped carbon nanotubes nodified with lactate oxidase
    • Goran J.M., Lyon J.L., Stevenson K.J. Amperometric detection of l-lactate using nitrogen-doped carbon nanotubes nodified with lactate oxidase. Anal. Chem. 2011, 83:8123-8129.
    • (2011) Anal. Chem. , vol.83 , pp. 8123-8129
    • Goran, J.M.1    Lyon, J.L.2    Stevenson, K.J.3
  • 250
    • 29244446773 scopus 로고    scopus 로고
    • Amperometric biosensor for hypoxanthine based on immobilized xanthine oxidase on nanocrystal gold-carbon paste electrodes
    • Agüí L., Manso J., Yáñez-Sedeño P., Pingarrón J.M. Amperometric biosensor for hypoxanthine based on immobilized xanthine oxidase on nanocrystal gold-carbon paste electrodes. Sens. Actuators B 2006, 113:272-280.
    • (2006) Sens. Actuators B , vol.113 , pp. 272-280
    • Agüí, L.1    Manso, J.2    Yáñez-Sedeño, P.3    Pingarrón, J.M.4
  • 251
    • 0030512972 scopus 로고    scopus 로고
    • Protein interactions with particulate teflon: implications for the foreign body response
    • Zardeneta G., Mukai H., Marker V., Milam S.B. Protein interactions with particulate teflon: implications for the foreign body response. J. Oral. Maxillofac. Surg. 1996, 54:873-878.
    • (1996) J. Oral. Maxillofac. Surg. , vol.54 , pp. 873-878
    • Zardeneta, G.1    Mukai, H.2    Marker, V.3    Milam, S.B.4
  • 252
    • 84858757459 scopus 로고    scopus 로고
    • Amperometric determination of xanthine in tea, coffee, and fish meat with graphite rod bound xanthine oxidase
    • Devi R., Narang J., Yadav S., Pundir C.S. Amperometric determination of xanthine in tea, coffee, and fish meat with graphite rod bound xanthine oxidase. J. Anal. Chem. 2012, 67:273-277.
    • (2012) J. Anal. Chem. , vol.67 , pp. 273-277
    • Devi, R.1    Narang, J.2    Yadav, S.3    Pundir, C.S.4
  • 253
    • 84862228530 scopus 로고    scopus 로고
    • Amperometric detection of hypoxanthine and xanthine by enzymatic amplification using a gold nanoparticles-carbon nanohorn hybrid as the carrier
    • Zhang L., Lei J., Zhang J., Ding L., Ju H. Amperometric detection of hypoxanthine and xanthine by enzymatic amplification using a gold nanoparticles-carbon nanohorn hybrid as the carrier. Analyst 2012, 137:3126-3131.
    • (2012) Analyst , vol.137 , pp. 3126-3131
    • Zhang, L.1    Lei, J.2    Zhang, J.3    Ding, L.4    Ju, H.5
  • 254
    • 79952817930 scopus 로고    scopus 로고
    • Construction and application of an amperometric xanthine biosensor based on zinc oxide nanoparticles-polypyrrole composite film
    • Devi R., Thakur M., Pundir C.S. Construction and application of an amperometric xanthine biosensor based on zinc oxide nanoparticles-polypyrrole composite film. Biosens. Bioelectron. 2011, 26:3420-3426.
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 3420-3426
    • Devi, R.1    Thakur, M.2    Pundir, C.S.3
  • 255
    • 67650260368 scopus 로고    scopus 로고
    • Xanthine oxidase/laponite nanoparticles immobilized on glassy carbon electrode: direct electron transfer and multielectrocatalysis
    • Shan D., Wang Y.-N., Xue H.-G., Cosnier S., Ding S.-N. Xanthine oxidase/laponite nanoparticles immobilized on glassy carbon electrode: direct electron transfer and multielectrocatalysis. Biosens. Bioelectron. 2009, 24:3556-3561.
    • (2009) Biosens. Bioelectron. , vol.24 , pp. 3556-3561
    • Shan, D.1    Wang, Y.-N.2    Xue, H.-G.3    Cosnier, S.4    Ding, S.-N.5
  • 256
    • 67650240555 scopus 로고    scopus 로고
    • Sensitive and selective xanthine amperometric sensors based on calcium carbonate nanoparticles
    • Shan D., Wang Y., Xue H., Cosnier S. Sensitive and selective xanthine amperometric sensors based on calcium carbonate nanoparticles. Sens. Actuators B 2009, 136:510-515.
    • (2009) Sens. Actuators B , vol.136 , pp. 510-515
    • Shan, D.1    Wang, Y.2    Xue, H.3    Cosnier, S.4
  • 257
    • 58149260241 scopus 로고    scopus 로고
    • Development of a high analytical performance-xanthine biosensor based on layered double hydroxides modified-electrode and investigation of the inhibitory effect by allopurinol
    • Shan D., Wang Y., Zhu M., Xue H., Cosnier S., Wang C. Development of a high analytical performance-xanthine biosensor based on layered double hydroxides modified-electrode and investigation of the inhibitory effect by allopurinol. Biosens. Bioelectron. 2009, 24:1171-1176.
    • (2009) Biosens. Bioelectron. , vol.24 , pp. 1171-1176
    • Shan, D.1    Wang, Y.2    Zhu, M.3    Xue, H.4    Cosnier, S.5    Wang, C.6
  • 258
    • 84954958929 scopus 로고
    • Purification and properties of a new enzyme l-glutamate oxidase, from Streptomyces sp. X-119-6 grown on wheat bran
    • Kusakabe H., Midorikawa Y., Fujishima T., Kuninaka A., Yoshino H. Purification and properties of a new enzyme l-glutamate oxidase, from Streptomyces sp. X-119-6 grown on wheat bran. Agric. Biol. Chem. 1983, 47:1323-1328.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 1323-1328
    • Kusakabe, H.1    Midorikawa, Y.2    Fujishima, T.3    Kuninaka, A.4    Yoshino, H.5
  • 260
    • 78649736867 scopus 로고    scopus 로고
    • Disposable biosensor based on immobilisation of glutamate oxidase on Pt nanoparticles modified Au nanowire array electrode
    • Jamal M., Xu J., Razeeb K.M. Disposable biosensor based on immobilisation of glutamate oxidase on Pt nanoparticles modified Au nanowire array electrode. Biosens. Bioelectron. 2010, 26:1420-1424.
    • (2010) Biosens. Bioelectron. , vol.26 , pp. 1420-1424
    • Jamal, M.1    Xu, J.2    Razeeb, K.M.3
  • 261
    • 84884945543 scopus 로고    scopus 로고
    • Glutamate oxidase biosensor based on mixed ceria and titania nanoparticles for the detection of glutamate in hypoxic environments
    • Özel R.E., Ispas C., Ganesana M., Leiter J.C., Andreescu S. Glutamate oxidase biosensor based on mixed ceria and titania nanoparticles for the detection of glutamate in hypoxic environments. Biosens. Bioelectron. 2014, 52:397-402.
    • (2014) Biosens. Bioelectron. , vol.52 , pp. 397-402
    • Özel, R.E.1    Ispas, C.2    Ganesana, M.3    Leiter, J.C.4    Andreescu, S.5
  • 262
    • 84874093240 scopus 로고    scopus 로고
    • Immobilization method to preserve enzyme specificity in biosensors: consequences for brain glutamate detection
    • Vasylieva N., Maucler C., Meiller A., Viscogliosi H., Lieutaud T., Barbier D., Marinesco S. Immobilization method to preserve enzyme specificity in biosensors: consequences for brain glutamate detection. Anal. Chem. 2013, 85:2507-2515.
    • (2013) Anal. Chem. , vol.85 , pp. 2507-2515
    • Vasylieva, N.1    Maucler, C.2    Meiller, A.3    Viscogliosi, H.4    Lieutaud, T.5    Barbier, D.6    Marinesco, S.7
  • 263
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba Y., Kumagai T., Yamamoto A., Yoshitsu H., Sugiyama M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 2006, 281:8981-8990.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 264
    • 0032855966 scopus 로고    scopus 로고
    • Slow-binding inhibition of mushroom (Agaricus bisporus) tyrosinase isoforms by tropolone
    • Espín J.C., Wichers H.J. Slow-binding inhibition of mushroom (Agaricus bisporus) tyrosinase isoforms by tropolone. J. Agric. Food. Chem. 1999, 47:2638-2644.
    • (1999) J. Agric. Food. Chem. , vol.47 , pp. 2638-2644
    • Espín, J.C.1    Wichers, H.J.2
  • 266
    • 84880953762 scopus 로고    scopus 로고
    • Three-dimensional graphene micropillar based electrochemical sensor for phenol detection
    • Liu F., Piao Y., Choi J.S., Seo T.S. Three-dimensional graphene micropillar based electrochemical sensor for phenol detection. Biosens. Bioelectron. 2013, 50:387-392.
    • (2013) Biosens. Bioelectron. , vol.50 , pp. 387-392
    • Liu, F.1    Piao, Y.2    Choi, J.S.3    Seo, T.S.4
  • 267
    • 42649100274 scopus 로고    scopus 로고
    • Electron transfer properties and electrocatalytic behavior of tyrosinase on ZnO nanorod
    • Chen L., Gu B., Zhu G., Wu Y., Liu S., Xu C. Electron transfer properties and electrocatalytic behavior of tyrosinase on ZnO nanorod. J. Electroanal. Chem. 2008, 617:7-13.
    • (2008) J. Electroanal. Chem. , vol.617 , pp. 7-13
    • Chen, L.1    Gu, B.2    Zhu, G.3    Wu, Y.4    Liu, S.5    Xu, C.6
  • 268
    • 0242583614 scopus 로고    scopus 로고
    • Mediator-free phenol sensor based on titania sol-gel encapsulation matrix for immobilization of tyrosinase by a vapor deposition method
    • Yu J., Liu S., Ju H. Mediator-free phenol sensor based on titania sol-gel encapsulation matrix for immobilization of tyrosinase by a vapor deposition method. Biosens. Bioelectron. 2003, 19:509-514.
    • (2003) Biosens. Bioelectron. , vol.19 , pp. 509-514
    • Yu, J.1    Liu, S.2    Ju, H.3
  • 269
    • 0034302474 scopus 로고    scopus 로고
    • Silica sol-gel composite film as an encapsulation matrix for the construction of an amperometric tyrosinase-based biosensor
    • Wang B., Zhang J., Dong S. Silica sol-gel composite film as an encapsulation matrix for the construction of an amperometric tyrosinase-based biosensor. Biosens. Bioelectron. 2000, 15:397-402.
    • (2000) Biosens. Bioelectron. , vol.15 , pp. 397-402
    • Wang, B.1    Zhang, J.2    Dong, S.3
  • 272
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers
    • Piontek K., Antorini M., Choinowski T. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers. J. Biol. Chem. 2002, 277:37663-37669.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3
  • 273
    • 33646528454 scopus 로고    scopus 로고
    • Laccase purification and characterization from Trametes trogii isolated in Tunisia: decolorization of textile dyes by the purified enzyme
    • Zouari-Mechichi H., Mechichi T., Dhouib A., Sayadi S., Martínez A.T., Martínez M.J. Laccase purification and characterization from Trametes trogii isolated in Tunisia: decolorization of textile dyes by the purified enzyme. Enzyme Microb. Technol. 2006, 39:141-148.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 141-148
    • Zouari-Mechichi, H.1    Mechichi, T.2    Dhouib, A.3    Sayadi, S.4    Martínez, A.T.5    Martínez, M.J.6
  • 274
    • 1242322589 scopus 로고    scopus 로고
    • Laccases: structure reactions, distribution
    • Claus H. Laccases: structure reactions, distribution. Micron 2004, 35:93-96.
    • (2004) Micron , vol.35 , pp. 93-96
    • Claus, H.1
  • 275
    • 84881506841 scopus 로고    scopus 로고
    • Laccase biosensor based on screen-printed electrode modified with thionine-carbon black nanocomposite, for bisphenol A detection
    • Portaccio M., Di Tuoro D., Arduini F., Moscone D., Cammarota M., Mita D.G., Lepore M. Laccase biosensor based on screen-printed electrode modified with thionine-carbon black nanocomposite, for bisphenol A detection. Electrochim. Acta 2013, 109:340-347.
    • (2013) Electrochim. Acta , vol.109 , pp. 340-347
    • Portaccio, M.1    Di Tuoro, D.2    Arduini, F.3    Moscone, D.4    Cammarota, M.5    Mita, D.G.6    Lepore, M.7
  • 277
    • 4043134375 scopus 로고    scopus 로고
    • Development of a biosensor for endocrine disrupting compounds based on tyrosinase entrapped within a poly(thionine) film
    • Dempsey, Diamond D., Collier A. Development of a biosensor for endocrine disrupting compounds based on tyrosinase entrapped within a poly(thionine) film. Biosens. Bioelectron. 2004, 20:367-377.
    • (2004) Biosens. Bioelectron. , vol.20 , pp. 367-377
    • Dempsey, D.D.1    Collier, A.2
  • 281
    • 79959827290 scopus 로고    scopus 로고
    • Cytochrome C biosensor-a model for gas sensing
    • Hulko M., Hospach I., Krasteva N., Nelles G. Cytochrome C biosensor-a model for gas sensing. Sensors 2011, 11:5968-5980.
    • (2011) Sensors , vol.11 , pp. 5968-5980
    • Hulko, M.1    Hospach, I.2    Krasteva, N.3    Nelles, G.4
  • 283
    • 79953694209 scopus 로고    scopus 로고
    • A molecular precursor approach to tunable porous tin-rich indium tin oxide with durable high electrical conductivity for bioelectronic devices
    • Aksu Y., Frasca S., Wollenberger U., Driess M., Thomas A. A molecular precursor approach to tunable porous tin-rich indium tin oxide with durable high electrical conductivity for bioelectronic devices. Chem. Mater. 2011, 23:1798-1804.
    • (2011) Chem. Mater. , vol.23 , pp. 1798-1804
    • Aksu, Y.1    Frasca, S.2    Wollenberger, U.3    Driess, M.4    Thomas, A.5
  • 285
    • 80755143097 scopus 로고    scopus 로고
    • Spectroelectrochemistry of cytochrome c and azurin immobilized in nanoporous antimony-doped tin oxide
    • Kwan P., Schmitt D., Volosin A.M., McIntosh C.L., Seo D.-K., Jones A.K. Spectroelectrochemistry of cytochrome c and azurin immobilized in nanoporous antimony-doped tin oxide. Chem. Commun. 2011, 47:12367-12369.
    • (2011) Chem. Commun. , vol.47 , pp. 12367-12369
    • Kwan, P.1    Schmitt, D.2    Volosin, A.M.3    McIntosh, C.L.4    Seo, D.-K.5    Jones, A.K.6
  • 288
    • 84858295212 scopus 로고    scopus 로고
    • Immbolization of uricase enzyme in Langmuir and Langmuir-Blodgett films of fatty acids: possible use as a uric acid sensor
    • Zanon N.C.M., Oliveira O.N., Caseli L. Immbolization of uricase enzyme in Langmuir and Langmuir-Blodgett films of fatty acids: possible use as a uric acid sensor. J. Colloid Interface Sci. 2012, 373:69-74.
    • (2012) J. Colloid Interface Sci. , vol.373 , pp. 69-74
    • Zanon, N.C.M.1    Oliveira, O.N.2    Caseli, L.3
  • 289
    • 80054026527 scopus 로고    scopus 로고
    • 2 detector for highly sensitive amperometric flow determination of uric acid
    • 2 detector for highly sensitive amperometric flow determination of uric acid. J. Pharm. Biomed. Anal. 2012, 57:125-132.
    • (2012) J. Pharm. Biomed. Anal. , vol.57 , pp. 125-132
    • Wang, Y.1    Hasebe, Y.2
  • 290
    • 84876902001 scopus 로고    scopus 로고
    • A novel zwitterionic copolymer with a short poly(methyl acrylic acid) block for improving both conjugation and separation efficiency of a protein without losing its bioactivity
    • Lin W., Zhang H., Wu J., Wang Z., Sun H., Yuan J., Chen S. A novel zwitterionic copolymer with a short poly(methyl acrylic acid) block for improving both conjugation and separation efficiency of a protein without losing its bioactivity. J. Mater. Chem. B 2013, 1:2482-2488.
    • (2013) J. Mater. Chem. B , vol.1 , pp. 2482-2488
    • Lin, W.1    Zhang, H.2    Wu, J.3    Wang, Z.4    Sun, H.5    Yuan, J.6    Chen, S.7
  • 291
    • 61449142543 scopus 로고    scopus 로고
    • Interaction of d-amino acid oxidase to carbon nanotubes: implications in the design of biosensors
    • Mora M.F., Giacomelli C.E., Garcia C.D. Interaction of d-amino acid oxidase to carbon nanotubes: implications in the design of biosensors. Anal. Chem. 2009, 81:1016-1022.
    • (2009) Anal. Chem. , vol.81 , pp. 1016-1022
    • Mora, M.F.1    Giacomelli, C.E.2    Garcia, C.D.3
  • 292
    • 84874071519 scopus 로고    scopus 로고
    • Antibody orientation on biosensor surfaces: a minireview
    • Trilling A.K., Beekwilder J., Zuilhof H. Antibody orientation on biosensor surfaces: a minireview. Analyst 2013, 138:1619-1627.
    • (2013) Analyst , vol.138 , pp. 1619-1627
    • Trilling, A.K.1    Beekwilder, J.2    Zuilhof, H.3
  • 294
    • 40649098187 scopus 로고    scopus 로고
    • A reusable piezoelectric immunosensor using antibody-adsorbed magnetic nanocomposite
    • Zhang Y., Wang H., Yan B., Zhang Y., Li J., Shen G., Yu R. A reusable piezoelectric immunosensor using antibody-adsorbed magnetic nanocomposite. J. Immunol. Methods 2008, 332:103-111.
    • (2008) J. Immunol. Methods , vol.332 , pp. 103-111
    • Zhang, Y.1    Wang, H.2    Yan, B.3    Zhang, Y.4    Li, J.5    Shen, G.6    Yu, R.7
  • 295
    • 77954632061 scopus 로고    scopus 로고
    • Diagnostic detection of human lung cancer-associated antigen using a gold nanoparticle-based electrochemical immunosensor
    • J.-a.A.Ho H.-C., Chang, Shih N.-Y., Wu L.-C., Chang Y.-F., Chen C.-C., Chou C. Diagnostic detection of human lung cancer-associated antigen using a gold nanoparticle-based electrochemical immunosensor. Anal. Chem. 2010, 82:5944-5950.
    • (2010) Anal. Chem. , vol.82 , pp. 5944-5950
    • Ho, J.-A.A.1    Chang, H.-C.2    Shih, N.-Y.3    Wu, L.-C.4    Chang, Y.-F.5    Chen, C.-C.6    Chou, C.7
  • 296
    • 84896987287 scopus 로고    scopus 로고
    • An ultrasensitive electrochemical immunosensor for carcinoembryonic antigen detection based on staphylococcal protein A-Au nanoparticle modified gold electrode
    • Zhou J., Du L., Zou L., Zou Y., Hu N., Wang P. An ultrasensitive electrochemical immunosensor for carcinoembryonic antigen detection based on staphylococcal protein A-Au nanoparticle modified gold electrode. Sens. Actuators B 2014, 197:220-227.
    • (2014) Sens. Actuators B , vol.197 , pp. 220-227
    • Zhou, J.1    Du, L.2    Zou, L.3    Zou, Y.4    Hu, N.5    Wang, P.6
  • 297
    • 84875304965 scopus 로고    scopus 로고
    • Immunosensor based on immobilization of antigenic peptide NS5A-1 from HCV and silk fibroin in nanostructured films
    • Moraes M.L., Lima L.R., Silva R.R., Cavicchioli M., Ribeiro S.J.L. Immunosensor based on immobilization of antigenic peptide NS5A-1 from HCV and silk fibroin in nanostructured films. Langmuir 2013, 29:3829-3834.
    • (2013) Langmuir , vol.29 , pp. 3829-3834
    • Moraes, M.L.1    Lima, L.R.2    Silva, R.R.3    Cavicchioli, M.4    Ribeiro, S.J.L.5
  • 298
    • 84901660449 scopus 로고    scopus 로고
    • Competitive electrochemical immunosensor for amyloid-beta 1-42 detection based on gold nanostructurated screen-printed carbon electrodes
    • Rama E.C., González-García M.B., Costa-García A. Competitive electrochemical immunosensor for amyloid-beta 1-42 detection based on gold nanostructurated screen-printed carbon electrodes. Sens. Actuators B 2014, 201:567-571.
    • (2014) Sens. Actuators B , vol.201 , pp. 567-571
    • Rama, E.C.1    González-García, M.B.2    Costa-García, A.3
  • 299
    • 54549095792 scopus 로고    scopus 로고
    • Amyloid-β detection with saccharide immobilized gold nanoparticle on carbon electrode
    • Chikae M., Fukuda T., Kerman K., Idegami K., Miura Y., Tamiya E. Amyloid-β detection with saccharide immobilized gold nanoparticle on carbon electrode. Bioelectrochemistry 2008, 74:118-123.
    • (2008) Bioelectrochemistry , vol.74 , pp. 118-123
    • Chikae, M.1    Fukuda, T.2    Kerman, K.3    Idegami, K.4    Miura, Y.5    Tamiya, E.6
  • 300
    • 27744541173 scopus 로고    scopus 로고
    • Electrocatalytic characteristics of uric acid oxidation at graphite-zeolite-modified electrode doped with iron(III)
    • Ardakani M.M., Akrami Z., Kazemian H., Zare H.R. Electrocatalytic characteristics of uric acid oxidation at graphite-zeolite-modified electrode doped with iron(III). J. Electroanal. Chem. 2006, 586:31-38.
    • (2006) J. Electroanal. Chem. , vol.586 , pp. 31-38
    • Ardakani, M.M.1    Akrami, Z.2    Kazemian, H.3    Zare, H.R.4
  • 301
    • 84923767145 scopus 로고    scopus 로고
    • Study of zeolite influence on analytical characteristics of urea biosensor based on ion-selective field-effect transistors
    • Shelyakina M., Soldatkin O., Arkhypova V., Kasap B., Akata B., Dzyadevych S. Study of zeolite influence on analytical characteristics of urea biosensor based on ion-selective field-effect transistors. Nanoscale Res. Lett. 2014, 9:124.
    • (2014) Nanoscale Res. Lett. , vol.9 , pp. 124
    • Shelyakina, M.1    Soldatkin, O.2    Arkhypova, V.3    Kasap, B.4    Akata, B.5    Dzyadevych, S.6
  • 303
    • 77957655027 scopus 로고    scopus 로고
    • Staining proteins: a simple method to increase the sensitivity of ellipsometric measurements in adsorption studies
    • Nejadnik M.R., Garcia C.D. Staining proteins: a simple method to increase the sensitivity of ellipsometric measurements in adsorption studies. Colloids Surf. B 2011, 82:253-257.
    • (2011) Colloids Surf. B , vol.82 , pp. 253-257
    • Nejadnik, M.R.1    Garcia, C.D.2
  • 304
    • 84870930685 scopus 로고    scopus 로고
    • Adsorption-desorption study of BSA conjugated silver nanoparticles (Ag/BSA NPs) on collagen immobilized substrates
    • Bhan C., Mandlewala R., Gebregeorgis A., Raghavan D. Adsorption-desorption study of BSA conjugated silver nanoparticles (Ag/BSA NPs) on collagen immobilized substrates. Langmuir 2012, 28:17043-17052.
    • (2012) Langmuir , vol.28 , pp. 17043-17052
    • Bhan, C.1    Mandlewala, R.2    Gebregeorgis, A.3    Raghavan, D.4
  • 305
  • 306
    • 44949099628 scopus 로고    scopus 로고
    • PH effects on BSA-dispersed carbon nanotubes studied by spectroscopy-enhanced composition evaluation techniques
    • Edri E., Regev O. pH effects on BSA-dispersed carbon nanotubes studied by spectroscopy-enhanced composition evaluation techniques. Anal. Chem. 2008, 80:4049-4054.
    • (2008) Anal. Chem. , vol.80 , pp. 4049-4054
    • Edri, E.1    Regev, O.2
  • 307
    • 84874818521 scopus 로고    scopus 로고
    • Interfacial structure and history dependent activity of immobilised antibodies in model pregnancy tests
    • Cowsill B.J., Waigh T.A., Eapen S., Davies R., Lu J.R. Interfacial structure and history dependent activity of immobilised antibodies in model pregnancy tests. Soft Matter 2012, 8:9847-9854.
    • (2012) Soft Matter , vol.8 , pp. 9847-9854
    • Cowsill, B.J.1    Waigh, T.A.2    Eapen, S.3    Davies, R.4    Lu, J.R.5
  • 308
    • 71949096526 scopus 로고    scopus 로고
    • Activity and thermal stability improvements of glucose oxidase upon adsorption on core-shell PMMA-BSA nanoparticles
    • He C., Liu J., Xie L., Zhang Q., Li C., Gui D., Zhang G., Wu C. Activity and thermal stability improvements of glucose oxidase upon adsorption on core-shell PMMA-BSA nanoparticles. Langmuir 2009, 25:13456-13460.
    • (2009) Langmuir , vol.25 , pp. 13456-13460
    • He, C.1    Liu, J.2    Xie, L.3    Zhang, Q.4    Li, C.5    Gui, D.6    Zhang, G.7    Wu, C.8
  • 309
    • 84861201411 scopus 로고    scopus 로고
    • A novel stable amperometric glucose biosensor based on the adsorption of glucose oxidase on poly(methyl methacrylate)-bovine serum albumin core-shell nanoparticles
    • He C., Liu J., Zhang Q., Wu C. A novel stable amperometric glucose biosensor based on the adsorption of glucose oxidase on poly(methyl methacrylate)-bovine serum albumin core-shell nanoparticles. Sens. Actuators B 2012, 166-167:802-808.
    • (2012) Sens. Actuators B , pp. 802-808
    • He, C.1    Liu, J.2    Zhang, Q.3    Wu, C.4
  • 310
    • 84857319068 scopus 로고    scopus 로고
    • Slow and remanent electric polarization of adsorbed BSA layer evidenced by neutron reflection
    • Koutsioubas A., Lairez D., Zalczer G., Cousin F. Slow and remanent electric polarization of adsorbed BSA layer evidenced by neutron reflection. Soft Matter 2012, 8:2638-2643.
    • (2012) Soft Matter , vol.8 , pp. 2638-2643
    • Koutsioubas, A.1    Lairez, D.2    Zalczer, G.3    Cousin, F.4
  • 311
    • 76849094649 scopus 로고    scopus 로고
    • Emerging nanotechnology-based strategies for the identification of microbial pathogenesis
    • Kaittanis C., Santra S., Perez J.M. Emerging nanotechnology-based strategies for the identification of microbial pathogenesis. Adv. Drug Deliver Rev. 2010, 62:408-423.
    • (2010) Adv. Drug Deliver Rev. , vol.62 , pp. 408-423
    • Kaittanis, C.1    Santra, S.2    Perez, J.M.3
  • 313
    • 84866420085 scopus 로고    scopus 로고
    • A High-affinity gold-binding camel antibody: antibody engineering for one-pot functionalization of gold nanoparticles as biointerface molecules
    • Hattori T., Umetsu M., Nakanishi T., Sawai S., Kikuchi S., Asano R., Kumagai I. A High-affinity gold-binding camel antibody: antibody engineering for one-pot functionalization of gold nanoparticles as biointerface molecules. Bioconjugate Chem. 2012, 23:1934-1944.
    • (2012) Bioconjugate Chem. , vol.23 , pp. 1934-1944
    • Hattori, T.1    Umetsu, M.2    Nakanishi, T.3    Sawai, S.4    Kikuchi, S.5    Asano, R.6    Kumagai, I.7
  • 314
    • 84883668831 scopus 로고    scopus 로고
    • Bovine serum albumin as an effective surface regulating biopolymer for morphology control of gold polyhedrons
    • Lee S.J., Scotti N., Ravasio N., Chung I.S., Song H. Bovine serum albumin as an effective surface regulating biopolymer for morphology control of gold polyhedrons. Cryst. Growth Des. 2013, 13:4131-4137.
    • (2013) Cryst. Growth Des. , vol.13 , pp. 4131-4137
    • Lee, S.J.1    Scotti, N.2    Ravasio, N.3    Chung, I.S.4    Song, H.5
  • 315
    • 84896754529 scopus 로고    scopus 로고
    • Novel trends in affinity biosensors: current challenges and perspectives
    • Arugula M.A., Simonian A. Novel trends in affinity biosensors: current challenges and perspectives. Meas. Sci. Technol. 2014, 25:032001.
    • (2014) Meas. Sci. Technol. , vol.25 , pp. 032001
    • Arugula, M.A.1    Simonian, A.2
  • 316
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: natural single-domain antibodies
    • Muyldermans S. Nanobodies: natural single-domain antibodies. Annu. Rev. Biochem. 2013, 82:775-797.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 775-797
    • Muyldermans, S.1


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