메뉴 건너뛰기




Volumn 416, Issue 2, 2011, Pages 174-179

Immuno-rolling circle amplification using a multibinding fusion protein

Author keywords

Antigen detection; Biotin acceptor peptide; Fusion protein; Immuno RCA

Indexed keywords

ANTIBODIES; BINDING ENERGY; BIOACTIVITY; BIOMARKERS; BODY FLUIDS; COENZYMES; DISEASES; ESCHERICHIA COLI; PEPTIDES; POLYMERASE CHAIN REACTION;

EID: 80155192637     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.05.004     Document Type: Article
Times cited : (18)

References (24)
  • 2
    • 0026644604 scopus 로고
    • Immuno-PCR: Very sensitive antigen detection by means of specific antibody-DNA conjugates
    • T. Sano, C.L. Smith, C.R. Cantor, Immuno-PCR: very sensitive antigen detection by means of specific antibody-DNA conjugates, Science 258 (1992) 120-122.
    • (1992) Science , vol.258 , pp. 120-122
    • Sano, T.1    Smith, C.L.2    Cantor, C.R.3
  • 3
    • 44649202034 scopus 로고    scopus 로고
    • Homogeneous and label-free fluorescence detection of single-nucleotide polymorphism using target-primed branched rolling circle amplification
    • Y. Cheng, Z. Li, X. Zhang, B. Du, Y. Fan, Homogeneous and label-free fluorescence detection of single-nucleotide polymorphism using target-primed branched rolling circle amplification, Anal. Biochem. 378 (2008) 123-126.
    • (2008) Anal. Biochem. , vol.378 , pp. 123-126
    • Cheng, Y.1    Li, Z.2    Zhang, X.3    Du, B.4    Fan, Y.5
  • 4
    • 16744365916 scopus 로고    scopus 로고
    • L-RCA (ligation-rolling circle amplification): A general method for genotyping of single nucleotide polymorphisms (SNPs)
    • X. Qi, S. Bakht, K.M. Devos, M.D. Gale, A. Osbourn, L-RCA (ligation-rolling circle amplification): a general method for genotyping of single nucleotide polymorphisms (SNPs), Nucleic Acids Res. 29 (2001) e116.
    • (2001) Nucleic Acids Res. , vol.29
    • Qi, X.1    Bakht, S.2    Devos, K.M.3    Gale, M.D.4    Osbourn, A.5
  • 5
    • 63349086644 scopus 로고    scopus 로고
    • Sensitive isothermal detection of nucleic-acid sequence by primer generation-rolling circle amplification
    • T. Murakami, J. Sumaoka, M. Komiyama, Sensitive isothermal detection of nucleic-acid sequence by primer generation-rolling circle amplification, Nucleic Acids Res. 37 (2009) e19.
    • (2009) Nucleic Acids Res. , vol.37
    • Murakami, T.1    Sumaoka, J.2    Komiyama, M.3
  • 6
    • 0033635554 scopus 로고    scopus 로고
    • Detection of multiple allergen-specific IgEs on microarrays by immunoassay with rolling circle amplification
    • S. Wiltshire, S. O'Malley, J. Lambert, K. Kukanskis, D. Edgar, S.F. Kingsmore, B. Schweitzer, Detection of multiple allergen-specific IgEs on microarrays by immunoassay with rolling circle amplification, Clin. Chem. 46 (2000) 1990-1993.
    • (2000) Clin. Chem. , vol.46 , pp. 1990-1993
    • Wiltshire, S.1    O'Malley, S.2    Lambert, J.3    Kukanskis, K.4    Edgar, D.5    Kingsmore, S.F.6    Schweitzer, B.7
  • 8
    • 34248210769 scopus 로고    scopus 로고
    • Real-time rolling circle amplification for protein detection
    • DOI 10.1021/ac062186b
    • L. Yang, C.W. Fung, E.J. Cho, A.D. Ellington, Real-time rolling circle amplification for protein detection, Anal. Chem. 79 (2007) 3320-3329. (Pubitemid 46717163)
    • (2007) Analytical Chemistry , vol.79 , Issue.9 , pp. 3320-3329
    • Yang, L.1    Fung, C.W.2    Eun, J.C.3    Ellington, A.D.4
  • 9
    • 75749121072 scopus 로고    scopus 로고
    • Diffractometric detection of proteins using microbead-based rolling circle amplification
    • J. Lee, K. Icoz, A. Roberts, A.D. Ellington, C.A. Savran, Diffractometric detection of proteins using microbead-based rolling circle amplification, Anal. Chem. 82 (2010) 197-202.
    • (2010) Anal. Chem. , vol.82 , pp. 197-202
    • Lee, J.1    Icoz, K.2    Roberts, A.3    Ellington, A.D.4    Savran, C.A.5
  • 10
    • 43049102042 scopus 로고    scopus 로고
    • In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system
    • A. Predonzani, F. Arnoldi, A. Lopez-Requena, O.R. Burrone, In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system, BMC Biotechnol. 8 (2008) 41.
    • (2008) BMC Biotechnol. , vol.8 , pp. 41
    • Predonzani, A.1    Arnoldi, F.2    Lopez-Requena, A.3    Burrone, O.R.4
  • 11
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide- modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • P.J. Schatz, Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli, Biotechnology (NY) 11 (1993) 1138-1143. (Pubitemid 23307458)
    • (1993) Bio/Technology , vol.11 , Issue.10 , pp. 1138-1143
    • Schatz, P.J.1
  • 12
    • 0041649396 scopus 로고    scopus 로고
    • Metabolically biotinylated adenovirus for cell targeting, ligand screening, and vector purification
    • DOI 10.1016/S1525-0016(03)00213-2
    • M.B. Parrott, K.E. Adams, G.T. Mercier, H. Mok, S.K. Campos, M.A. Barry, Metabolically biotinylated adenovirus for cell targeting, ligand screening, and vector purification, Mol. Ther. 8 (2003) 688-700. (Pubitemid 37321698)
    • (2003) Molecular Therapy , vol.8 , Issue.4 , pp. 688-700
    • Parrott, M.B.1    Adams, K.E.2    Mercier, G.T.3    Mok, H.4    Campos, S.K.5    Barry, M.A.6
  • 13
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • D. Beckett, E. Kovaleva, P.J. Schatz, A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation, Protein Sci. 8 (1999) 921-929. (Pubitemid 29165423)
    • (1999) Protein Science , vol.8 , Issue.4 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 14
    • 0030561209 scopus 로고    scopus 로고
    • Construction of biotinylated firefly luciferases using biotin acceptor peptides
    • DOI 10.1006/abio.1996.0498
    • H. Tatsumi, S. Fukuda, M. Kikuchi, Y. Koyama, Construction of biotinylated firefly luciferases using biotin acceptor peptides, Anal. Biochem. 243 (1996) 176-180. (Pubitemid 26418593)
    • (1996) Analytical Biochemistry , vol.243 , Issue.1 , pp. 176-180
    • Tatsumi, H.1    Fukuda, S.2    Kikuchi, M.3    Koyama, Y.4
  • 18
    • 33845222271 scopus 로고    scopus 로고
    • Significance of elevated preoperative alpha-fetoprotein in postchemotherapy residual tumor resection for the disseminated germ cell tumors
    • DOI 10.1002/jso.20418
    • T. Kobayashi, M. Kawakita, T. Terachi, T. Habuchi, O. Ogawa, T. Kamoto, Significance of elevated preoperative alpha-fetoprotein in postchemotherapy residual tumor resection for the disseminated germ cell tumors, J. Surg. Oncol. 94 (2006) 619-623. (Pubitemid 44851924)
    • (2006) Journal of Surgical Oncology , vol.94 , Issue.7 , pp. 619-623
    • Kobayashi, T.1    Kawakita, M.2    Terachi, T.3    Habuchi, T.4    Ogawa, O.5    Kamoto, T.6
  • 19
    • 33644700414 scopus 로고    scopus 로고
    • Fabrication of an antibody microwell array with self-adhering antibody binding protein
    • DOI 10.1016/j.ab.2005.12.034, PII S0003269706000029
    • G. Tanaka, H. Funabashi, M. Mie, E. Kobatake, Fabrication of an antibody microwell array with self-adhering antibody binding protein, Anal. Biochem. 350 (2006) 298-303. (Pubitemid 43332832)
    • (2006) Analytical Biochemistry , vol.350 , Issue.2 , pp. 298-303
    • Tanaka, G.1    Funabashi, H.2    Mie, M.3    Kobatake, E.4
  • 20
    • 63349101189 scopus 로고    scopus 로고
    • Transduction of MyoD protein into myoblasts induces myogenic differentiation without addition of protein transduction domain
    • T. Noda, T. Fujino, M. Mie, E. Kobatake, Transduction of MyoD protein into myoblasts induces myogenic differentiation without addition of protein transduction domain, Biochem. Biophys. Res. Commun. 382 (2009) 473-477.
    • (2009) Biochem. Biophys. Res. Commun. , vol.382 , pp. 473-477
    • Noda, T.1    Fujino, T.2    Mie, M.3    Kobatake, E.4
  • 21
    • 0027200943 scopus 로고
    • Biotinylation of monoclonal antibodies prevents their ability to activate the classical pathway of complement
    • T.S. Jokiranta, S. Meri, Biotinylation of monoclonal antibodies prevents their ability to activate the classical pathway of complement, J. Immunol. 151 (1993) 2124-2131. (Pubitemid 23235685)
    • (1993) Journal of Immunology , vol.151 , Issue.4 , pp. 2124-2131
    • Jokiranta, T.S.1    Meri, S.2
  • 22
    • 50849128778 scopus 로고    scopus 로고
    • Application of highly sensitive, modified glass substrate-based immuno-PCR on the early detection of nasopharyngeal carcinoma
    • T.W. Wang, H.Y. Lu, P.J. Lou, F.H. Lin, Application of highly sensitive, modified glass substrate-based immuno-PCR on the early detection of nasopharyngeal carcinoma, Biomaterials 29 (2008) 4447-4454.
    • (2008) Biomaterials , vol.29 , pp. 4447-4454
    • Wang, T.W.1    Lu, H.Y.2    Lou, P.J.3    Lin, F.H.4
  • 23
    • 37049027703 scopus 로고    scopus 로고
    • Assessment of the diagnostic potential of immuno-RCA in 96-well ELISA plates for foot-and-mouth disease virus
    • DOI 10.1016/j.jviromet.2007.08.020, PII S0166093407003461
    • W. Van Dessel, F. Vandenbussche, M. Staes, N. Goris, K. De Clercq, Assessment of the diagnostic potential of immuno-RCA in 96-well ELISA plates for foot-and-mouth disease virus, J. Virol. Methods 147 (2008) 151-156. (Pubitemid 350250858)
    • (2008) Journal of Virological Methods , vol.147 , Issue.1 , pp. 151-156
    • Van Dessel, W.1    Vandenbussche, F.2    Staes, M.3    Goris, N.4    De Clercq, K.5
  • 24
    • 0028852614 scopus 로고
    • Application of a mimetic enzyme for the enzyme immunoassay for α-1-fetoprotein
    • Y.X. Ci, Y. Qin, W.B. Chang, Y.Z. Li, Application of a mimetic enzyme for the enzyme immunoassay for α-1-fetoprotein, Anal. Chim. Acta 300 (1995) 273-276.
    • (1995) Anal. Chim. Acta , vol.300 , pp. 273-276
    • Ci, Y.X.1    Qin, Y.2    Chang, W.B.3    Li, Y.Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.