메뉴 건너뛰기




Volumn 408, Issue 1, 2011, Pages 86-94

Favorably orienting recombinant proteins to develop amperometric biosensors to diagnose Chagas' disease

Author keywords

American trypanosomiasis biosensor; Amperometric biosensor; Chagas' disease biosensor; Chimeric protein; Molecule directed attachment

Indexed keywords

BIOSENSORS; ECONOMIC AND SOCIAL EFFECTS; ENZYMES; RECOMBINANT PROTEINS; REUSABILITY; SIGNAL TO NOISE RATIO;

EID: 77958456845     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.09.002     Document Type: Article
Times cited : (16)

References (45)
  • 2
    • 34247149375 scopus 로고    scopus 로고
    • Electrochemical immunosensor using p-aminophenol redox cycling by hydrazine combined with a low background current
    • Das J., Jo K., Lee J.W., Yang H. Electrochemical immunosensor using p-aminophenol redox cycling by hydrazine combined with a low background current. Anal. Chem. 2007, 79:2790-2796.
    • (2007) Anal. Chem. , vol.79 , pp. 2790-2796
    • Das, J.1    Jo, K.2    Lee, J.W.3    Yang, H.4
  • 3
    • 33846660052 scopus 로고    scopus 로고
    • Endotoxin detection in a competitive electrochemical assay: synthesis of a suitable endotoxin conjugate
    • Priano G., Pallarola D., Battaglini F. Endotoxin detection in a competitive electrochemical assay: synthesis of a suitable endotoxin conjugate. Anal. Biochem. 2007, 362:108-116.
    • (2007) Anal. Biochem. , vol.362 , pp. 108-116
    • Priano, G.1    Pallarola, D.2    Battaglini, F.3
  • 4
    • 41549106353 scopus 로고    scopus 로고
    • Assembling amperometric biosensors for clinical diagnostics
    • Belluzo M.S., Ribone M.E., Lagier C.M. Assembling amperometric biosensors for clinical diagnostics. Sensors 2008, 8:1366-1399.
    • (2008) Sensors , vol.8 , pp. 1366-1399
    • Belluzo, M.S.1    Ribone, M.E.2    Lagier, C.M.3
  • 6
    • 63649149974 scopus 로고    scopus 로고
    • Detection of glucose based on direct electron transfer reaction of glucose oxidase immobilized on highly ordered polyaniline nanotubes
    • Wang Z., Liu S., Wu P., Cai C. Detection of glucose based on direct electron transfer reaction of glucose oxidase immobilized on highly ordered polyaniline nanotubes. Anal. Chem. 2009, 81:1638-1645.
    • (2009) Anal. Chem. , vol.81 , pp. 1638-1645
    • Wang, Z.1    Liu, S.2    Wu, P.3    Cai, C.4
  • 7
    • 70450014859 scopus 로고    scopus 로고
    • Simultaneous and label-free determination of wild-type and mutant p53 at a single surface plasmon resonance chip preimmobilized with consensus DNA and monoclonal antibody
    • Wang Y., Zhu X., Wu M., Xia N., Wang J., Zhou F. Simultaneous and label-free determination of wild-type and mutant p53 at a single surface plasmon resonance chip preimmobilized with consensus DNA and monoclonal antibody. Anal. Chem. 2009, 81:8441-8446.
    • (2009) Anal. Chem. , vol.81 , pp. 8441-8446
    • Wang, Y.1    Zhu, X.2    Wu, M.3    Xia, N.4    Wang, J.5    Zhou, F.6
  • 9
    • 21644444010 scopus 로고    scopus 로고
    • Real-time QCM-D immunoassay through oriented antibody immobilization using cross-linked hydrogel biointerfaces
    • Carrigan S.D., Scott G., Tabrizian M. Real-time QCM-D immunoassay through oriented antibody immobilization using cross-linked hydrogel biointerfaces. Langmuir 2005, 21:5966-5973.
    • (2005) Langmuir , vol.21 , pp. 5966-5973
    • Carrigan, S.D.1    Scott, G.2    Tabrizian, M.3
  • 10
    • 33847196810 scopus 로고    scopus 로고
    • Aptamer-based detection of plasma proteins by an electrochemical assay coupled to magnetic beads
    • Centi S., Tombelli S., Minunni M., Mascini M. Aptamer-based detection of plasma proteins by an electrochemical assay coupled to magnetic beads. Anal. Chem. 2007, 79:1466-1473.
    • (2007) Anal. Chem. , vol.79 , pp. 1466-1473
    • Centi, S.1    Tombelli, S.2    Minunni, M.3    Mascini, M.4
  • 11
  • 14
    • 32844474969 scopus 로고    scopus 로고
    • Amperometric bioelectrode for specific human immunoglobulin G determination: optimization of the method to diagnose American trypanosomiasis
    • Ribone M.E., Belluzo M.S., Pagani D., Marcipar I.S., Lagier C.M. Amperometric bioelectrode for specific human immunoglobulin G determination: optimization of the method to diagnose American trypanosomiasis. Anal. Biochem. 2006, 350:61-70.
    • (2006) Anal. Biochem. , vol.350 , pp. 61-70
    • Ribone, M.E.1    Belluzo, M.S.2    Pagani, D.3    Marcipar, I.S.4    Lagier, C.M.5
  • 15
    • 22044447503 scopus 로고    scopus 로고
    • Continuous-flow/stopped-flow system for enzyme immunoassay using a rotating bioreactor: determination of Chagas disease
    • Salinas E., Torriero A.A., Battaglini F., Sanz M.I., Olsina R., Raba J. Continuous-flow/stopped-flow system for enzyme immunoassay using a rotating bioreactor: determination of Chagas disease. Biosens. Bioelectron. 2005, 21:313-321.
    • (2005) Biosens. Bioelectron. , vol.21 , pp. 313-321
    • Salinas, E.1    Torriero, A.A.2    Battaglini, F.3    Sanz, M.I.4    Olsina, R.5    Raba, J.6
  • 16
    • 65849309476 scopus 로고    scopus 로고
    • Chagas disease: a neglected emergency [editorial], Lancet 373 1820
    • Chagas disease: a neglected emergency [editorial], Lancet 373 (2009) 1820.
    • (2009)
  • 17
    • 77958506637 scopus 로고    scopus 로고
    • World Health Organization, Control of Chagas disease, Second report of the WHO Expert Committee Available from
    • World Health Organization, Control of Chagas disease, Second report of the WHO Expert Committee, 2002, Available from: http://whqlibdoc.who.int/trs/WHO_TRS_905.pdf.
    • (2002)
  • 19
    • 77953028103 scopus 로고    scopus 로고
    • Chagas disease: a Latin American health problem becoming a world health problem
    • Schmunis G.A., Yadon Z.E. Chagas disease: a Latin American health problem becoming a world health problem. Acta Trop. 2010, 115:14-21.
    • (2010) Acta Trop. , vol.115 , pp. 14-21
    • Schmunis, G.A.1    Yadon, Z.E.2
  • 21
    • 73949128576 scopus 로고    scopus 로고
    • Congenital Chagas disease: estimating the potential risk in the United States
    • Yadon Z.E., Schmunis G.A. Congenital Chagas disease: estimating the potential risk in the United States. Am. J. Trop. Med. Hyg. 2009, 81:927-933.
    • (2009) Am. J. Trop. Med. Hyg. , vol.81 , pp. 927-933
    • Yadon, Z.E.1    Schmunis, G.A.2
  • 22
    • 74249107668 scopus 로고    scopus 로고
    • Recognizing and meeting the challenge of Chagas disease in the USA
    • Bowling J., Walter E.A. Recognizing and meeting the challenge of Chagas disease in the USA. Expert Rev. Anti-Infect. Ther. 2009, 7:1223-1234.
    • (2009) Expert Rev. Anti-Infect. Ther. , vol.7 , pp. 1223-1234
    • Bowling, J.1    Walter, E.A.2
  • 28
    • 0033958622 scopus 로고    scopus 로고
    • Multiepitope synthetic peptide and recombinant protein for the detection of antibodies to Trypanosoma cruzi in patients with treated or untreated Chagas' disease
    • Houghton R.L., Benson D.R., Reynolds L., McNeill P., Sleath P., Lodes M., Skeiky Y.A., Badaro R., Krettli A.U., Reed S.G. Multiepitope synthetic peptide and recombinant protein for the detection of antibodies to Trypanosoma cruzi in patients with treated or untreated Chagas' disease. J. Infect. Dis. 2000, 181:325-330.
    • (2000) J. Infect. Dis. , vol.181 , pp. 325-330
    • Houghton, R.L.1    Benson, D.R.2    Reynolds, L.3    McNeill, P.4    Sleath, P.5    Lodes, M.6    Skeiky, Y.A.7    Badaro, R.8    Krettli, A.U.9    Reed, S.G.10
  • 29
    • 0034979327 scopus 로고    scopus 로고
    • Chagas disease: recombinant Trypanosoma cruzi antigens for serological diagnosis
    • da Silveira J.F., Umezawa E.S., Luquetti A.O. Chagas disease: recombinant Trypanosoma cruzi antigens for serological diagnosis. Trends Parasitol. 2001, 17:286-291.
    • (2001) Trends Parasitol. , vol.17 , pp. 286-291
    • da Silveira, J.F.1    Umezawa, E.S.2    Luquetti, A.O.3
  • 30
    • 67249127989 scopus 로고    scopus 로고
    • Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
    • Camussone C., Gonzalez V., Belluzo M.S., Pujato N., Ribone M.E., Lagier C.M., Marcipar I.S. Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis. Clin. Vaccine Immunol. 2009, 16:899-905.
    • (2009) Clin. Vaccine Immunol. , vol.16 , pp. 899-905
    • Camussone, C.1    Gonzalez, V.2    Belluzo, M.S.3    Pujato, N.4    Ribone, M.E.5    Lagier, C.M.6    Marcipar, I.S.7
  • 34
    • 78651145402 scopus 로고
    • Growth and differentiation in Trypanosoma cruzi: I, origin of metacyclic trypanosomes in liquid media
    • Camargo M.E. Growth and differentiation in Trypanosoma cruzi: I, origin of metacyclic trypanosomes in liquid media. Rev. Inst. Med. Trop. Sao Paulo 1964, 12:93-100.
    • (1964) Rev. Inst. Med. Trop. Sao Paulo , vol.12 , pp. 93-100
    • Camargo, M.E.1
  • 35
    • 30744458092 scopus 로고    scopus 로고
    • Structure and thickness dependence of " molecular wiring" in nanostructured enzyme multilayers
    • Flexer V., Forzani E.S., Calvo E.J., Luduena S.J., Pietrasanta L.I. Structure and thickness dependence of " molecular wiring" in nanostructured enzyme multilayers. Anal. Chem. 2006, 78:399-407.
    • (2006) Anal. Chem. , vol.78 , pp. 399-407
    • Flexer, V.1    Forzani, E.S.2    Calvo, E.J.3    Luduena, S.J.4    Pietrasanta, L.I.5
  • 37
    • 1442264891 scopus 로고    scopus 로고
    • The diagnostic performance of recombinant Trypanosoma cruzi ribosomal P2β protein is influenced by its expression system
    • Marcipar I.S., Olivares M.L., Robles L., Dekanty A., Marcipar A., Silber A.M. The diagnostic performance of recombinant Trypanosoma cruzi ribosomal P2β protein is influenced by its expression system. Protein Expr. Purif. 2004, 34:1-7.
    • (2004) Protein Expr. Purif. , vol.34 , pp. 1-7
    • Marcipar, I.S.1    Olivares, M.L.2    Robles, L.3    Dekanty, A.4    Marcipar, A.5    Silber, A.M.6
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 0032004093 scopus 로고    scopus 로고
    • Application of an ELISA-elution assay as a screening tool for dissociation of yolk antibody-antigen complexes
    • Kummer A., Li-Chan E.C. Application of an ELISA-elution assay as a screening tool for dissociation of yolk antibody-antigen complexes. J. Immunol. Methods 1998, 211:125-137.
    • (1998) J. Immunol. Methods , vol.211 , pp. 125-137
    • Kummer, A.1    Li-Chan, E.C.2
  • 44
    • 0029783436 scopus 로고    scopus 로고
    • Immunoblot assay using excreted-secreted antigens of Trypanosoma cruzi in serodiagnosis of congenital, acute, and chronic Chagas' disease
    • Umezawa E.S., Nascimento M.S., Kesper N., Coura J.R., Borges-Pereira J., Junqueira A.C., Camargo M.E. Immunoblot assay using excreted-secreted antigens of Trypanosoma cruzi in serodiagnosis of congenital, acute, and chronic Chagas' disease. J. Clin. Microbiol. 1996, 34:2143-2147.
    • (1996) J. Clin. Microbiol. , vol.34 , pp. 2143-2147
    • Umezawa, E.S.1    Nascimento, M.S.2    Kesper, N.3    Coura, J.R.4    Borges-Pereira, J.5    Junqueira, A.C.6    Camargo, M.E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.