메뉴 건너뛰기




Volumn 40, Issue 22, 2012, Pages 11777-11783

Selection is more intelligent than design: Improving the affinity of a bivalent ligand through directed evolution

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; BIVALENT APTAMER; MOLECULAR SCAFFOLD; THROMBIN; UNCLASSIFIED DRUG;

EID: 84871246567     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks899     Document Type: Article
Times cited : (74)

References (23)
  • 1
    • 77954757965 scopus 로고    scopus 로고
    • Multitasking with ubiquitin through multivalent interactions
    • Liu, F. and Walters, K. J. (2010) Multitasking with ubiquitin through multivalent interactions. Trends Biochem. Sci., 35, 352-360.
    • (2010) Trends Biochem. Sci , vol.35 , pp. 352-360
    • Liu, F.1    Walters, K.J.2
  • 2
    • 50249135564 scopus 로고    scopus 로고
    • Multivalency: The hallmark of antibodies used for optimization of tumor targeting by design
    • Deyev, S. M. and Lebedenko, E. N. (2008) Multivalency: the hallmark of antibodies used for optimization of tumor targeting by design. Bioessays, 30, 904-918.
    • (2008) Bioessays , vol.30 , pp. 904-918
    • Deyev, S.M.1    Lebedenko, E.N.2
  • 4
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. and Gold, L. (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science, 249, 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 5
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington, A. D. and Szostak, J. W. (1990) In vitro selection of RNA molecules that bind specific ligands. Nature, 346, 818-822.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 6
    • 0031686486 scopus 로고    scopus 로고
    • Recombination RNA evolution, and bifunctional RNA molecules isolated through chimeric SELEX
    • Burke, D. H. and Willis, J. H. (1998) Recombination, RNA evolution, and bifunctional RNA molecules isolated through chimeric SELEX. RNA, 4, 1165-1175.
    • (1998) RNA , vol.4 , pp. 1165-1175
    • Burke, D.H.1    Willis, J.H.2
  • 7
    • 38849122813 scopus 로고    scopus 로고
    • Multidomain targeting generates a high-affinity thrombin-inhibiting bivalent aptamer
    • Mü ller, J., Wulffen, B., Pö tzsch, B. and Mayer, G. (2007) Multidomain targeting generates a high-affinity thrombin-inhibiting bivalent aptamer. Chembiochem., 8, 2223-2226.
    • (2007) Chembiochem , vol.8 , pp. 2223-2226
    • Müller, J.1    Wulffen, B.2    Pötzsch, B.3    Mayer, G.4
  • 8
    • 46749136342 scopus 로고    scopus 로고
    • Self-assembled DNA nanostructures for distance-dependent multivalent ligand-protein binding
    • Rinker, S., Ke, Y., Liu, Y., Chhabra, R. and Yan, H. (2008) Self-assembled DNA nanostructures for distance-dependent multivalent ligand-protein binding. Nat. Nanotechnol., 3, 418-422.
    • (2008) Nat. Nanotechnol , vol.3 , pp. 418-422
    • Rinker, S.1    Ke, Y.2    Liu, Y.3    Chhabra, R.4    Yan, H.5
  • 9
    • 59849096632 scopus 로고    scopus 로고
    • Bivalent ligands with long nanometer-scale flexible linkers
    • Tian, L. and Heyduk, T. (2009) Bivalent ligands with long nanometer-scale flexible linkers. Biochemistry, 48, 264-275.
    • (2009) Biochemistry , vol.48 , pp. 264-275
    • Tian, L.1    Heyduk, T.2
  • 10
    • 40849142659 scopus 로고    scopus 로고
    • Improvement of aptamer affinity by dimerization
    • Hasegawa, H., Taira, K., Sode, K. and Ikebukuro, K. (2008) Improvement of aptamer affinity by dimerization. Sensors, 8, 1090-1098.
    • (2008) Sensors , vol.8 , pp. 1090-1098
    • Hasegawa, H.1    Taira, K.2    Sode, K.3    Ikebukuro, K.4
  • 11
    • 67649988369 scopus 로고    scopus 로고
    • Generation of highly specific aptamers via micromagnetic selection
    • Qian, J., Lou, X., Zhang, Y., Xiao, Y. and Soh, H. T. (2009) Generation of highly specific aptamers via micromagnetic selection. Anal. Chem., 81, 5490-5495.
    • (2009) Anal. Chem , vol.81 , pp. 5490-5495
    • Qian, J.1    Lou, X.2    Zhang, Y.3    Xiao, Y.4    Soh, H.T.5
  • 12
    • 81055124768 scopus 로고    scopus 로고
    • Probing the limits of aptamer affinity with a microfluidic SELEX platform
    • Ahmad, K. M., Oh, S. S., Kim, S., McClellen, F. M., Xiao, Y. and Soh, H. T. (2011) Probing the limits of aptamer affinity with a microfluidic SELEX platform. PLoS One, 6, e27051.
    • (2011) PLoS One , vol.6
    • Ahmad, K.M.1    Oh, S.S.2    Kim, S.3    McClellen, F.M.4    Xiao, Y.5    Soh, H.T.6
  • 13
    • 64649105841 scopus 로고    scopus 로고
    • Controlling the selection stringency of phage display using a microfluidic device
    • Liu, Y., Adams, J. D., Turner, K., Cochran, F. V., Gambhir, S. S. and Soh, H. T. (2009) Controlling the selection stringency of phage display using a microfluidic device. Lab Chip, 9, 1033-1036.
    • (2009) Lab Chip , vol.9 , pp. 1033-1036
    • Liu, Y.1    Adams, J.D.2    Turner, K.3    Cochran, F.V.4    Gambhir, S.S.5    Soh, H.T.6
  • 14
    • 34447345725 scopus 로고    scopus 로고
    • Appropriate calibration curve fitting in ligand binding assays
    • Findlay, J. W. and Dillard, R. F. (2007) Appropriate calibration curve fitting in ligand binding assays. AAPS J., 9, E260-267.
    • (2007) AAPS J , vol.9
    • Findlay, J.W.1    Dillard, R.F.2
  • 15
    • 0026575221 scopus 로고
    • Selection of single-stranded DNA molecules that bind and inhibit human thrombin
    • Bock, C., Griffin, L. C., Latham, J. A., Vermaas, E. H. and Toole, J. J. (1992) Selection of single-stranded DNA molecules that bind and inhibit human thrombin. Nature, 355, 564-566.
    • (1992) Nature , vol.355 , pp. 564-566
    • Bock, C.1    Griffin, L.C.2    Latham, J.A.3    Vermaas, E.H.4    Toole, J.J.5
  • 16
    • 0031563773 scopus 로고    scopus 로고
    • Oligonucleotide inhibitors of human thrombin that bind distinct epitopes
    • Tasset, D. M., Kubik, M. F. and Steiner, W. (1997) Oligonucleotide inhibitors of human thrombin that bind distinct epitopes. J. Mol. Biol., 272, 688-698.
    • (1997) J. Mol. Biol , vol.272 , pp. 688-698
    • Tasset, D.M.1    Kubik, M.F.2    Steiner, W.3
  • 17
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W. P. (1981) On the attribution and additivity of binding energies. Proc. Natl Acad. Sci. USA, 78, 4046-4050.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 18
    • 0034603154 scopus 로고    scopus 로고
    • Adaptive recognition by nucleic acid aptamers
    • Hermann, T. and Patel, D. J. (2000) Adaptive recognition by nucleic acid aptamers. Science, 287, 820-825.
    • (2000) Science , vol.287 , pp. 820-825
    • Hermann, T.1    Patel, D.J.2
  • 19
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res., 31, 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 21
    • 0027172294 scopus 로고
    • The structure of alpha-thrombin inhibited by a 15-mer single-stranded DNA aptamer
    • Padmanabhan, K., Padmanabhan, K., Ferrara, J. D., Sadler, J. E. and Tulinsky, A. (1993) The structure of alpha-thrombin inhibited by a 15-mer single-stranded DNA aptamer. J. Biol. Chem., 268, 17651-17654.
    • (1993) J. Biol. Chem , vol.268 , pp. 17651-17654
    • Padmanabhan, K.1    Padmanabhan, K.2    Ferrara, J.D.3    Sadler, J.E.4    Tulinsky, A.5
  • 22
    • 0031559579 scopus 로고    scopus 로고
    • Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer
    • Lin, Y. and Jayasena, S. D. (1997) Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. J. Mol. Biol., 271, 100-111.
    • (1997) J. Mol. Biol , vol.271 , pp. 100-111
    • Lin, Y.1    Jayasena, S.D.2
  • 23
    • 82955239904 scopus 로고    scopus 로고
    • Automated prediction of protein association rate constants
    • Qin, S., Pang, X. and Zhou, H.-X. (2011) Automated prediction of protein association rate constants. Structure, 19, 1744-1751.
    • (2011) Structure , vol.19 , pp. 1744-1751
    • Qin, S.1    Pang, X.2    Zhou, H.-X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.