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Volumn 7, Issue 3, 2013, Pages 288-294

Site-specific and effective immobilization of proteins by Npu DnaE split-intein mediated protein trans-splicing reaction

Author keywords

Protein chip; Protein immobilization; Split intein

Indexed keywords

BACTERIA; GOLD; MOLECULAR BIOLOGY; SELF ASSEMBLED MONOLAYERS; SUBSTRATES;

EID: 84884526032     PISSN: 19760280     EISSN: 20927843     Source Type: Journal    
DOI: 10.1007/s13206-013-7312-7     Document Type: Article
Times cited : (8)

References (26)
  • 1
    • 78650420189 scopus 로고    scopus 로고
    • Identifying and validating biomarkers for Alzheimer's disease
    • Humpel, C. Identifying and validating biomarkers for Alzheimer's disease. Trends Biotechnol. 29, 26-32 (2011).
    • (2011) Trends Biotechnol. , vol.29 , pp. 26-32
    • Humpel, C.1
  • 2
    • 52949132641 scopus 로고    scopus 로고
    • Peptide microarrays: next generation biochips for detection, diagnostics and high-throughput screening
    • Uttamchandani, M. & Yao, S. Q. Peptide microarrays: next generation biochips for detection, diagnostics and high-throughput screening. Curr. Pharm. Des. 14, 2428-2438 (2008).
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 2428-2438
    • Uttamchandani, M.1    Yao, S.Q.2
  • 3
    • 47249109457 scopus 로고    scopus 로고
    • Protein biochip array technology for cytokine profiling predicts etanercept responsiveness in rheumatoid arthritis
    • Fabre, S. et al. Protein biochip array technology for cytokine profiling predicts etanercept responsiveness in rheumatoid arthritis. Clin. Exp. Immunol. 153, 188-195 (2008).
    • (2008) Clin. Exp. Immunol. , vol.153 , pp. 188-195
    • Fabre, S.1
  • 4
    • 56449093214 scopus 로고    scopus 로고
    • Magnetic bead based immunoassay for autonomous detection of toxins
    • Kwon, Y. et al. Magnetic bead based immunoassay for autonomous detection of toxins. Anal. Chem. 80, 8416-8423 (2008).
    • (2008) Anal. Chem. , vol.80 , pp. 8416-8423
    • Kwon, Y.1
  • 5
    • 84866975687 scopus 로고    scopus 로고
    • Optimized magnetic bead-based immunoassay for automated detection of protein toxins
    • Jung, D.-H., Min, K., Jeon, Y., Jang, W. & Kwon, Y. Optimized magnetic bead-based immunoassay for automated detection of protein toxins. BioChip Journal6, 293-298 (2012).
    • (2012) BioChip Journal , vol.6 , pp. 293-298
    • Jung, D.-H.1    Min, K.2    Jeon, Y.3    Jang, W.4    Kwon, Y.5
  • 6
    • 79955020764 scopus 로고    scopus 로고
    • Preparation and characterization of non-covalently immobilized amylosucrase using a pH-dependent autoprecipitating carrier
    • Wang, R., Kim, J. H., Kim, B. S., Park, C. S. & Yoo, S. H. Preparation and characterization of non-covalently immobilized amylosucrase using a pH-dependent autoprecipitating carrier. Bioresour. Technol. 102, 6370-6374 (2011).
    • (2011) Bioresour. Technol. , vol.102 , pp. 6370-6374
    • Wang, R.1    Kim, J.H.2    Kim, B.S.3    Park, C.S.4    Yoo, S.H.5
  • 7
    • 53249115573 scopus 로고    scopus 로고
    • Recent Advances in Controlled Immobilization of Proteins onto the Surface of the Solid Substrate and Its Possible Application to Proteomics
    • Nakanishi, K., Sakiyama, T., Kumada, Y., Imamura, K. & Imanaka, H. Recent Advances in Controlled Immobilization of Proteins onto the Surface of the Solid Substrate and Its Possible Application to Proteomics. Current Proteomics5, 161-175 (2008).
    • (2008) Current Proteomics , vol.5 , pp. 161-175
    • Nakanishi, K.1    Sakiyama, T.2    Kumada, Y.3    Imamura, K.4    Imanaka, H.5
  • 8
    • 0242266929 scopus 로고    scopus 로고
    • Reduced nonspecific adsorption on covalently immobilized protein surfaces using poly (ethylene oxide) containing blocking agents
    • Frederix, F. et al. Reduced nonspecific adsorption on covalently immobilized protein surfaces using poly (ethylene oxide) containing blocking agents. Journal of Biochemical and Biophysical Methods58, 67-74 (2004).
    • (2004) Journal of Biochemical and Biophysical Methods , vol.58 , pp. 67-74
    • Frederix, F.1
  • 9
    • 84871851252 scopus 로고    scopus 로고
    • Specific Enzyme Immobilization Approaches and Their Application with Nanomaterials
    • Liu, W., Wang, L. & Jiang, R. Specific Enzyme Immobilization Approaches and Their Application with Nanomaterials. Topics in Catalysis55, 1146-1156 (2012).
    • (2012) Topics in Catalysis , vol.55 , pp. 1146-1156
    • Liu, W.1    Wang, L.2    Jiang, R.3
  • 10
    • 0036199649 scopus 로고    scopus 로고
    • Peptide chips for the quantitative evaluation of protein kinase activity
    • Houseman, B. T., Huh, J. H., Kron, S. J. & Mrksich, M. Peptide chips for the quantitative evaluation of protein kinase activity. Nat. Biotechnol. 20, 270-274 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 270-274
    • Houseman, B.T.1    Huh, J.H.2    Kron, S.J.3    Mrksich, M.4
  • 11
    • 79959913133 scopus 로고    scopus 로고
    • Protein microarrays: novel developments and applications
    • Berrade, L., Garcia, A. E. & Camarero, J. A. Protein microarrays: novel developments and applications. Pharmaceutical Research28, 1480-1499 (2011).
    • (2011) Pharmaceutical Research , vol.28 , pp. 1480-1499
    • Berrade, L.1    Garcia, A.E.2    Camarero, J.A.3
  • 12
    • 33746311225 scopus 로고    scopus 로고
    • Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing
    • Kwon, Y., Coleman, M. A. & Camarero, J. A. Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing. Angew. Chem. Int. Ed. Engl. 45, 1726-1729 (2006).
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 1726-1729
    • Kwon, Y.1    Coleman, M.A.2    Camarero, J.A.3
  • 13
    • 60749092724 scopus 로고    scopus 로고
    • The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction
    • Zettler, J., Schutz, V. & Mootz, H. D. The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction. FEBS Letters583, 909-914 (2009).
    • (2009) FEBS Letters , vol.583 , pp. 909-914
    • Zettler, J.1    Schutz, V.2    Mootz, H.D.3
  • 14
    • 0035814803 scopus 로고    scopus 로고
    • Characterization of a naturally occurring trans-splicing intein from Synechocystis sp. PCC6803
    • Martin, D. D., Xu, M. Q. & Evans, T. C., Jr. Characterization of a naturally occurring trans-splicing intein from Synechocystis sp. PCC6803. Biochemistry40, 1393-1402 (2001).
    • (2001) Biochemistry , vol.40 , pp. 1393-1402
    • Martin, D.D.1    Xu, M.Q.2    Evans Jr., T.C.3
  • 15
    • 0037881919 scopus 로고    scopus 로고
    • Zinc ion effects on individual Ssp DnaE intein splicing steps: regulating pathway progression
    • Nichols, N. M., Benner, J. S., Martin, D. D. & Evans, T. C., Jr. Zinc ion effects on individual Ssp DnaE intein splicing steps: regulating pathway progression. Biochemistry42, 5301-5311 (2003).
    • (2003) Biochemistry , vol.42 , pp. 5301-5311
    • Nichols, N.M.1    Benner, J.S.2    Martin, D.D.3    Evans Jr., T.C.4
  • 16
    • 65249091343 scopus 로고    scopus 로고
    • In vivo and in vitro protein ligation by naturally occurring and engineered split DnaE inteins
    • Aranko, A. S., Zuger, S., Buchinger, E. & Iwai, H. In vivo and in vitro protein ligation by naturally occurring and engineered split DnaE inteins. PLoS One4, e5185 (2009).
    • (2009) PLoS One , vol.4
    • Aranko, A.S.1    Zuger, S.2    Buchinger, E.3    Iwai, H.4
  • 17
    • 77957907731 scopus 로고    scopus 로고
    • Protein trans-splicing and its use in structural biology: opportunities and limitations
    • Volkmann, G. & Iwai, H. Protein trans-splicing and its use in structural biology: opportunities and limitations. Mol. Biosyst. 6, 2110-2121 (2010).
    • (2010) Mol. Biosyst. , vol.6 , pp. 2110-2121
    • Volkmann, G.1    Iwai, H.2
  • 18
    • 67349189136 scopus 로고    scopus 로고
    • Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification
    • Oeemig, J. S., Aranko, A. S., Djupsjobacka, J., Heinamaki, K. & Iwai, H. Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification. FEBS Letters583, 1451-1456 (2009).
    • (2009) FEBS Letters , vol.583 , pp. 1451-1456
    • Oeemig, J.S.1    Aranko, A.S.2    Djupsjobacka, J.3    Heinamaki, K.4    Iwai, H.5
  • 19
    • 0037117516 scopus 로고    scopus 로고
    • Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands
    • Hodneland, C. D., Lee, Y. S., Min, D. H. & Mrksich, M. Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands. Proc. Natl. Acad. Sci. USA99, 5048-5052 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5048-5052
    • Hodneland, C.D.1    Lee, Y.S.2    Min, D.H.3    Mrksich, M.4
  • 20
    • 4744345464 scopus 로고    scopus 로고
    • Antibody arrays prepared by cutinase-mediated immobilization on self-assembled monolayers
    • Kwon, Y., Han, Z., Karatan, E., Mrksich, M. & Kay, B. K. Antibody arrays prepared by cutinase-mediated immobilization on self-assembled monolayers. Anal. Chem. 76, 5713-5720 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 5713-5720
    • Kwon, Y.1    Han, Z.2    Karatan, E.3    Mrksich, M.4    Kay, B.K.5
  • 21
    • 0036749243 scopus 로고    scopus 로고
    • Application of self-assembly techniques in the design of biocompatible protein microarray surfaces
    • Schaeferling, M. et al. Application of self-assembly techniques in the design of biocompatible protein microarray surfaces. Electrophoresis23, 3097-3105 (2002).
    • (2002) Electrophoresis , vol.23 , pp. 3097-3105
    • Schaeferling, M.1
  • 22
    • 66249090167 scopus 로고    scopus 로고
    • Using "click" chemistry to prepare SAM substrates to study stem cell adhesion
    • Hudalla, G. A. & Murphy, W. L. Using "click" chemistry to prepare SAM substrates to study stem cell adhesion. Langmuir25, 5737-5746, doi: 10. 1021/la804077t (2009).
    • (2009) Langmuir , vol.25 , pp. 5737-5746
    • Hudalla, G.A.1    Murphy, W.L.2
  • 23
    • 46749090560 scopus 로고    scopus 로고
    • Recent developments in the site-specific immobilization of proteins onto solid supports
    • Camarero, J. A. Recent developments in the site-specific immobilization of proteins onto solid supports. Biopolymers90, 450-458 (2008).
    • (2008) Biopolymers , vol.90 , pp. 450-458
    • Camarero, J.A.1
  • 24
    • 33846116576 scopus 로고    scopus 로고
    • Site-Specific Protein Modification through CuI-Catalyzed 1,2,3-Triazole Formation and Its Implementation in Protein Microarray Fabrication
    • Lin, P.-C. et al. Site-Specific Protein Modification through CuI-Catalyzed 1, 2, 3-Triazole Formation and Its Implementation in Protein Microarray Fabrication. Angewandte Chemie118, 4392-4396 (2006).
    • (2006) Angewandte Chemie , vol.118 , pp. 4392-4396
    • Lin, P.-C.1
  • 25
    • 0035884143 scopus 로고    scopus 로고
    • High-resolution and high-throughput protocols for measuring drug/human serum albumin interactions using BIACORE
    • Rich, R. L., Day, Y. S., Morton, T. A. & Myszka, D. G. High-resolution and high-throughput protocols for measuring drug/human serum albumin interactions using BIACORE. Anal. Biochem. 296, 197-207 (2001).
    • (2001) Anal. Biochem. , vol.296 , pp. 197-207
    • Rich, R.L.1    Day, Y.S.2    Morton, T.A.3    Myszka, D.G.4
  • 26
    • 67650472128 scopus 로고    scopus 로고
    • Traceless protein splicing utilizing evolved split inteins
    • Lockless, S. W. & Muir, T. W. Traceless protein splicing utilizing evolved split inteins. Proc. Natl. Acad. Sci. USA106, 10999-11004 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10999-11004
    • Lockless, S.W.1    Muir, T.W.2


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