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Volumn 40, Issue 3, 2012, Pages 941-955

Luminescent detection of DNA-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; DNA BINDING PROTEIN; EXONUCLEASE;

EID: 84863116694     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr763     Document Type: Review
Times cited : (90)

References (88)
  • 1
    • 0028843508 scopus 로고
    • Molecular medicine. Transcription factors
    • Papavassiliou, A. G. (1995) Molecular medicine. Transcription factors. N. Engl. J. Med., 332, 45-47.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 45-47
    • Papavassiliou, A.G.1
  • 2
    • 0030854907 scopus 로고    scopus 로고
    • Transcription factors, normal myeloid development, and leukemia
    • Tenen, D. G., Hromas, R., Licht, J. D. and Zhang, D.-E. (1997) Transcription factors, normal myeloid development, and leukemia. Blood, 90, 489-519.
    • (1997) Blood , vol.90 , pp. 489-519
    • Tenen, D.G.1    Hromas, R.2    Licht, J.D.3    Zhang, D.-E.4
  • 3
    • 33846622099 scopus 로고    scopus 로고
    • Transcription factors in myeloid development: Balancing differentiation with transformation
    • Rosenbauer, F. and Tenen, D. G. (2007) Transcription factors in myeloid development: balancing differentiation with transformation. Nat. Rev. Immunol., 7, 105-117.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 105-117
    • Rosenbauer, F.1    Tenen, D.G.2
  • 4
    • 0345017786 scopus 로고    scopus 로고
    • Transcription factors in liver development, differentiation, and regeneration
    • Costa, R. H., Kalinichenko, V. V., Holterman, A.-X. L. and Wang, X. (2003) Transcription factors in liver development, differentiation, and regeneration. Hepatology, 38, 1331-1347.
    • (2003) Hepatology , vol.38 , pp. 1331-1347
    • Costa, R.H.1    Kalinichenko, V.V.2    Holterman, A.-X.L.3    Wang, X.4
  • 5
    • 0019877067 scopus 로고
    • A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: Application to components of the Escherichia coli lactose operon regulatory system
    • Garner, M. M. and Revzin, A. (1981) A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system. Nucleic Acids Res., 9, 3047-3060.
    • (1981) Nucleic Acids Res , vol.9 , pp. 3047-3060
    • Garner, M.M.1    Revzin, A.2
  • 6
    • 0018199224 scopus 로고
    • DNAase footprinting a simple method for the detection of protein-DNA binding specificity
    • Galas, D. J. and Schmitz, A. (1978) DNAase footprinting a simple method for the detection of protein-DNA binding specificity. Nucleic Acids Res., 5, 3157-3170.
    • (1978) Nucleic Acids Res , vol.5 , pp. 3157-3170
    • Galas, D.J.1    Schmitz, A.2
  • 7
    • 0015367077 scopus 로고
    • Enzyme-linked immunosorbent assay, elisa
    • Engvall, E. and Perlmann, P. (1972) Enzyme-Linked Immunosorbent Assay, Elisa. J. Immunol., 109, 129-135.
    • (1972) J. Immunol , vol.109 , pp. 129-135
    • Engvall, E.1    Perlmann, P.2
  • 8
    • 0023658615 scopus 로고
    • Footprinting DNA-protein complexes in situ following gel retardation assays using 1, 10-phenanthroline-copper ion: Escherichia coli RNA polymerase-lac promoter complexes
    • Kuwabara, M. and Sigman, D. S. (1987) Footprinting DNA-protein complexes in situ following gel retardation assays using 1, 10-phenanthroline-copper ion: Escherichia coli RNA polymerase-lac promoter complexes. Biochemistry, 26, 7234-7238.
    • (1987) Biochemistry , vol.26 , pp. 7234-7238
    • Kuwabara, M.1    Sigman, D.S.2
  • 9
    • 0000524403 scopus 로고
    • Map of distamycin, netropsin, and actinomycin binding sites on heterogeneous DNA: DNA cleavage-inhibition patterns with methidiumpropyl-EDTA. Fe(II)
    • Van Dyke, M. W., Hertzberg, R. P. and Dervan, P. B. (1982) Map of distamycin, netropsin, and actinomycin binding sites on heterogeneous DNA: DNA cleavage-inhibition patterns with methidiumpropyl-EDTA. Fe(II). Proc. Natl Acad. Sci. USA, 79, 5470-5474.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5470-5474
    • Van Dyke, M.W.1    Hertzberg, R.P.2    Dervan, P.B.3
  • 10
    • 0023623752 scopus 로고
    • Hydroxyl radical footprinting: A high-resolution method for mapping protein-DNA contacts
    • Tullius, T. D., Dombroski, B. A., Churchill, M. E. A. and Kam, L. (1987) Hydroxyl radical footprinting: a high-resolution method for mapping protein-DNA contacts. Methods Enzymol., 155, 537-558.
    • (1987) Methods Enzymol , vol.155 , pp. 537-558
    • Tullius, T.D.1    Dombroski, B.A.2    Churchill, M.E.A.3    Kam, L.4
  • 11
    • 0026485796 scopus 로고
    • Template-directed interference footprinting of cytosine contacts in a protein-DNA complex: Potent interference by 5-aza-20-deoxycytidine
    • Hayashibara, K. C. and Verdine, G. L. (1992) Template-directed interference footprinting of cytosine contacts in a protein-DNA complex: potent interference by 5-aza-20-deoxycytidine. Biochemistry, 31, 11265-11273.
    • (1992) Biochemistry , vol.31 , pp. 11265-11273
    • Hayashibara, K.C.1    Verdine, G.L.2
  • 12
    • 0030919292 scopus 로고    scopus 로고
    • Ludwig Brand, M. L. J. (ed.) Academic Press, Amsterdam
    • Hill, J. J. and Royer, C. A. (1997) In Ludwig Brand, M. L. J. (ed. ), Methods in Enzymol, Vol. 278. Academic Press, Amsterdam, pp. 390-416.
    • (1997) Methods in Enzymol , vol.278 , pp. 390-416
    • Hill, J.J.1    Royer, C.A.2
  • 13
    • 0025261344 scopus 로고
    • Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction
    • Heyduk, T. and Lee, J. C. (1990) Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction. Proc. Natl Acad. Sci. USA, 87, 1744-1748.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1744-1748
    • Heyduk, T.1    Lee, J.C.2
  • 14
    • 0035810698 scopus 로고    scopus 로고
    • Allosteric regulation of the cAMP receptor protein
    • Harman, J. G. (2001) Allosteric regulation of the cAMP receptor protein. Biochim. Biophys. Acta, 1547, 1-17.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 1-17
    • Harman, J.G.1
  • 15
    • 0030893492 scopus 로고    scopus 로고
    • Anaerobic citrate metabolism and its regulation in enterobacteria
    • Bott, M. (1997) Anaerobic citrate metabolism and its regulation in enterobacteria. Arch. Microbiol., 167, 78-88.
    • (1997) Arch. Microbiol , vol.167 , pp. 78-88
    • Bott, M.1
  • 16
    • 0027429065 scopus 로고
    • The galactose regulon of Escherichia coli
    • Weickert, M. J. and Adhya, S. (1993) The galactose regulon of Escherichia coli. Mol. Microbiol., 10, 245-251.
    • (1993) Mol. Microbiol , vol.10 , pp. 245-251
    • Weickert, M.J.1    Adhya, S.2
  • 17
    • 0029943025 scopus 로고    scopus 로고
    • Simultaneous binding and bending of promoter DNA by the TATA binding protein: Real time kinetic measurements
    • Parkhurst, K. M., Brenowitz, M. and Parkhurst, L. J. (1996) Simultaneous binding and bending of promoter DNA by the TATA binding protein: real time kinetic measurements. Biochemistry, 35, 7459-7465.
    • (1996) Biochemistry , vol.35 , pp. 7459-7465
    • Parkhurst, K.M.1    Brenowitz, M.2    Parkhurst, L.J.3
  • 18
  • 19
    • 0037204724 scopus 로고    scopus 로고
    • Connections and regulation of the human estrogen receptor
    • McDonnell, D. P. and Norris, J. D. (2002) Connections and regulation of the human estrogen receptor. Science, 296, 1642-1644.
    • (2002) Science , vol.296 , pp. 1642-1644
    • McDonnell, D.P.1    Norris, J.D.2
  • 20
    • 0023968137 scopus 로고
    • Two functional estrogen response elements are located upstream of the major chicken vitellogenin gene
    • Burch, J. B., Evans, M. I., Friedman, T. M. and O'Malley, P. J. (1988) Two functional estrogen response elements are located upstream of the major chicken vitellogenin gene. Mol. Cell. Biol., 8, 1123-1131.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 1123-1131
    • Burch, J.B.1    Evans, M.I.2    Friedman, T.M.3    O'Malley, P.J.4
  • 21
    • 0039174562 scopus 로고    scopus 로고
    • Equilibrium binding of single-stranded DNA with herpes simplex virus type I-coded single-stranded DNA-binding protein. ICP8
    • Gourves, A. S., Tanguy Le Gac, N., Villani, G., Boehmer, P. E. and Johnson, N. P. (2000) Equilibrium binding of single-stranded DNA with herpes simplex virus type I-coded single-stranded DNA-binding protein. ICP8. J. Biol. Chem., 275, 10864-10869.
    • (2000) J. Biol. Chem , vol.275 , pp. 10864-10869
    • Gourves, A.S.1    Tanguy Le Gac, N.2    Villani, G.3    Boehmer, P.E.4    Johnson, N.P.5
  • 22
    • 0034687674 scopus 로고    scopus 로고
    • DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume
    • Lima, L. M. T. R., Foguel, D. and Silva, J. L. (2000) DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume. Proc. Natl Acad. Sci. USA, 97, 14289-14294.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14289-14294
    • Lima, L.M.T.R.1    Foguel, D.2    Silva, J.L.3
  • 23
    • 35449004399 scopus 로고    scopus 로고
    • John, J. C. and Detrich, H. W. III (eds) Academic Press, Amsterdam
    • LiCata, V. J. and Wowor, A. J. (2008) In John, J. C. and Detrich, H. W. III (eds), Methods Cell Biol, Vol. 84. Academic Press, Amsterdam, pp. 243-262.
    • (2008) Methods Cell Biol , vol.84 , pp. 243-262
    • Licata, V.J.1    Wowor, A.J.2
  • 24
    • 0032078362 scopus 로고    scopus 로고
    • Molecular beacon probes combined with amplification by NASBA enable homogeneous, real-time detection of RNA
    • Leone, G., vanGemen, B., Schoen, C. D., van Schijndel, H. and Kramer, F. R. (1998) Molecular beacon probes combined with amplification by NASBA enable homogeneous, real-time detection of RNA. Nucleic Acids Res., 26, 2150-2155.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2150-2155
    • Leone, G.1    Van Gemen, B.2    Schoen, C.D.3    Van Schijndel, H.4    Kramer, F.R.5
  • 26
    • 0029670262 scopus 로고    scopus 로고
    • Molecular beacons: Probes that fluoresce upon hybridization
    • Tyagi, S. and Kramer, F. R. (1996) Molecular beacons: probes that fluoresce upon hybridization. Nat. Biotechnol., 14, 303-308.
    • (1996) Nat. Biotechnol , vol.14 , pp. 303-308
    • Tyagi, S.1    Kramer, F.R.2
  • 27
    • 0034677706 scopus 로고    scopus 로고
    • Molecular beacons: A novel approach to detect protein-DNA interactions
    • Li, J. J., Fang, X., Schuster, S. M. and Tan, W. (2000) Molecular beacons: a novel approach to detect protein-DNA interactions. Angew. Chem. Int. Ed., 39, 1049-1052.
    • (2000) Angew. Chem. Int. Ed , vol.39 , pp. 1049-1052
    • Li, J.J.1    Fang, X.2    Schuster, S.M.3    Tan, W.4
  • 28
    • 0028246888 scopus 로고
    • Escherichia Coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • Lohman, T. M. and Ferrari, M. E. (1994) Escherichia Coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities. Ann. Rev. Biochem., 63, 527-570.
    • (1994) Ann. Rev. Biochem , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 29
    • 0001380278 scopus 로고    scopus 로고
    • Using molecular beacons to probe molecular interactions between lactate dehydrogenase and single-stranded DNA
    • Fang, X., Li, J. J. and Tan, W. (2000) Using molecular beacons to probe molecular interactions between lactate dehydrogenase and single-stranded DNA. Anal. Chem., 72, 3280-3285.
    • (2000) Anal. Chem , vol.72 , pp. 3280-3285
    • Fang, X.1    Li, J.J.2    Tan, W.3
  • 30
    • 0036172005 scopus 로고    scopus 로고
    • Molecular beacons for detecting DNA binding proteins
    • Heyduk, T. and Heyduk, E. (2002) Molecular beacons for detecting DNA binding proteins. Nat. Biotechnol., 20, 171-176.
    • (2002) Nat. Biotechnol , vol.20 , pp. 171-176
    • Heyduk, T.1    Heyduk, E.2
  • 31
    • 0037402264 scopus 로고    scopus 로고
    • Molecular beacons for detecting DNA binding proteins: Mechanism of action
    • Heyduk, E. (2003) Molecular beacons for detecting DNA binding proteins: mechanism of action. Anal. Biochem., 316, 1-10.
    • (2003) Anal. Biochem , vol.316 , pp. 1-10
    • Heyduk, E.1
  • 32
    • 1242316192 scopus 로고    scopus 로고
    • Unimolecular beacons for the detection of DNA-binding proteins
    • Knoll, E. and Heyduk, T. (2004) Unimolecular beacons for the detection of DNA-binding proteins. Anal. Chem., 76, 1156-1164.
    • (2004) Anal. Chem , vol.76 , pp. 1156-1164
    • Knoll, E.1    Heyduk, T.2
  • 33
    • 0033150948 scopus 로고    scopus 로고
    • Oligonucleotide aptamers that recognize small molecules
    • Famulok, M. (1999) Oligonucleotide aptamers that recognize small molecules. Curr. Opin. Struct. Biol., 9, 324-329.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 324-329
    • Famulok, M.1
  • 34
    • 0033797244 scopus 로고    scopus 로고
    • Nucleic acid aptamers from selection in vitro to applications in vivo
    • Famulok, M., Mayer, G. and Blind, M. (2000) Nucleic acid aptamers from selection in vitro to applications in vivo. Accounts Chem. Res., 33, 591-599.
    • (2000) Accounts Chem. Res , vol.33 , pp. 591-599
    • Famulok, M.1    Mayer, G.2    Blind, M.3
  • 35
    • 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
  • 36
    • 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
  • 37
    • 0031102380 scopus 로고    scopus 로고
    • Nucleic acid selection and the challenge of combinatorial chemistry
    • Osborne, S. E. and Ellington, A. D. (1997) Nucleic acid selection and the challenge of combinatorial chemistry. Chem. Rev., 97, 349-370.
    • (1997) Chem. Rev , vol.97 , pp. 349-370
    • Osborne, S.E.1    Ellington, A.D.2
  • 38
  • 39
    • 48749112317 scopus 로고    scopus 로고
    • Protein detection with aptamer biosensors
    • Strehlitz, B., Nikolaus, N. and Stoltenburg, R. (2008) Protein detection with aptamer biosensors. Sensors, 8, 4296-4307.
    • (2008) Sensors , vol.8 , pp. 4296-4307
    • Strehlitz, B.1    Nikolaus, N.2    Stoltenburg, R.3
  • 40
    • 40849146978 scopus 로고    scopus 로고
    • Aptamer-based biosensors. TrAC Trend
    • Song, S., Wang, L., Li, J., Fan, C. and Zhao, J. (2008) Aptamer-based biosensors. TrAC Trend. Anal. Chem., 27, 108-117.
    • (2008) Anal. Chem , vol.27 , pp. 108-117
    • Song, S.1    Wang, L.2    Li, J.3    Fan, C.4    Zhao, J.5
  • 41
    • 38849087269 scopus 로고    scopus 로고
    • Surface immobilization methods for aptamer diagnostic applications
    • Balamurugan, S., Obubuafo, A., Soper, S. and Spivak, D. (2008) Surface immobilization methods for aptamer diagnostic applications. Anal. Bioanal. Chem., 390, 1009-1021.
    • (2008) Anal. Bioanal. Chem , vol.390 , pp. 1009-1021
    • Balamurugan, S.1    Obubuafo, A.2    Soper, S.3    Spivak, D.4
  • 42
    • 35148840942 scopus 로고    scopus 로고
    • Functional aptamers and aptazymes in biotechnology diagnostics, and therapy
    • Famulok, M., Hartig, J. S. and Mayer, G. (2007) Functional aptamers and aptazymes in biotechnology, diagnostics, and therapy. Chem. Rev., 107, 3715-3743.
    • (2007) Chem. Rev , vol.107 , pp. 3715-3743
    • Famulok, M.1    Hartig, J.S.2    Mayer, G.3
  • 44
    • 34548331295 scopus 로고    scopus 로고
    • Electronic aptamer-based sensors
    • Willner, I. and Zayats, M. (2007) Electronic aptamer-based sensors. Angew. Chem. Int. Ed., 46, 6408-6418.
    • (2007) Angew. Chem. Int. Ed , vol.46 , pp. 6408-6418
    • Willner, I.1    Zayats, M.2
  • 45
    • 0034086583 scopus 로고    scopus 로고
    • Molecular beacon aptamer fluoresces in the presence of Tat protein of HIV-1
    • Yamamoto, R., Baba, T. and Kumar, P. K. (2000) Molecular beacon aptamer fluoresces in the presence of Tat protein of HIV-1. Genes Cells, 5, 389-396.
    • (2000) Genes Cells , vol.5 , pp. 389-396
    • Yamamoto, R.1    Baba, T.2    Kumar, P.K.3
  • 46
    • 0034051357 scopus 로고    scopus 로고
    • A novel RNA motif that binds efficiently and specifically to the Tat protein of HIV and inhibits the trans-activation by Tat of transcription in vitro and in vivo
    • Yamamoto, R., Katahira, M., Nishikawa, S., Baba, T., Taira, K. and Kumar, P. K. R. (2000) A novel RNA motif that binds efficiently and specifically to the Tat protein of HIV and inhibits the trans-activation by Tat of transcription in vitro and in vivo. Genes Cells, 5, 371-388.
    • (2000) Genes Cells , vol.5 , pp. 371-388
    • Yamamoto, R.1    Katahira, M.2    Nishikawa, S.3    Baba, T.4    Taira, K.5    Kumar, P.K.R.6
  • 47
    • 0035879386 scopus 로고    scopus 로고
    • Aptamer beacons for the direct detection of proteins
    • Hamaguchi, N., Ellington, A. and Stanton, M. (2001) Aptamer beacons for the direct detection of proteins. Anal. Biochem., 294, 126-131.
    • (2001) Anal. Biochem , vol.294 , pp. 126-131
    • Hamaguchi, N.1    Ellington, A.2    Stanton, M.3
  • 48
  • 49
    • 0027172294 scopus 로고
    • The structure of alpha-thrombin inhibited by a 15-mer single-stranded DNA aptamer
    • Padmanabhan, K., Padmanabhan, K. P., 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.P.2    Ferrara, J.D.3    Sadler, J.E.4    Tulinsky, A.5
  • 50
    • 0027467617 scopus 로고
    • Thrombin-binding DNA aptamer forms a unimolecular quadruplex structure in solution
    • Macaya, R. F., Schultze, P., Smith, F. W., Roe, J. A. and Feigon, J. (1993) Thrombin-binding DNA aptamer forms a unimolecular quadruplex structure in solution. Proc. Natl Acad. Sci. USA, 90, 3745-3749.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3745-3749
    • MacAya, R.F.1    Schultze, P.2    Smith, F.W.3    Roe, J.A.4    Feigon, J.5
  • 51
    • 0036297293 scopus 로고    scopus 로고
    • Molecular aptamer beacons for real-time protein recognition
    • Li, J. J., Fang, X. and Tan, W. (2002) Molecular aptamer beacons for real-time protein recognition. Biochem. Biophys. Res. Commun., 292, 31-40.
    • (2002) Biochem. Biophys. Res. Commun , vol.292 , pp. 31-40
    • Li, J.J.1    Fang, X.2    Tan, W.3
  • 52
    • 0037462083 scopus 로고    scopus 로고
    • Structure-switching signaling aptamers
    • Nutiu, R. and Li, Y. (2003) Structure-switching signaling aptamers. J. Am. Chem. Soc., 125, 4771-4778.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 4771-4778
    • Nutiu, R.1    Li, Y.2
  • 53
    • 13844308093 scopus 로고    scopus 로고
    • Nucleic acid-based fluorescence sensors for detecting proteins
    • Heyduk, E. and Heyduk, T. (2005) Nucleic acid-based fluorescence sensors for detecting proteins. Anal. Chem., 77, 1147-1156.
    • (2005) Anal. Chem , vol.77 , pp. 1147-1156
    • Heyduk, E.1    Heyduk, T.2
  • 54
    • 28444491961 scopus 로고    scopus 로고
    • Light-switching excimer probes for rapid protein monitoring in complex biological fluids
    • Yang, C. J., Jockusch, S., Vicens, M., Turro, N. J. and Tan, W. (2005) Light-switching excimer probes for rapid protein monitoring in complex biological fluids. Proc. Natl Acad. Sci. USA, 102, 17278-17283.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17278-17283
    • Yang, C.J.1    Jockusch, S.2    Vicens, M.3    Turro, N.J.4    Tan, W.5
  • 55
    • 2942682928 scopus 로고    scopus 로고
    • Regulation of PDGF and its receptors in fibrotic diseases
    • Bonner, J. C. (2004) Regulation of PDGF and its receptors in fibrotic diseases. Cytokine Growth F. R., 15, 255-273.
    • (2004) Cytokine Growth F. R , vol.15 , pp. 255-273
    • Bonner, J.C.1
  • 56
    • 46149087993 scopus 로고    scopus 로고
    • R Regulation of tumor angiogenesis and metastasis by FGF and PDGF signaling pathways
    • Cao, Y., Cao, R. and Hedlund, E.-M. (2008) R Regulation of tumor angiogenesis and metastasis by FGF and PDGF signaling pathways. J. Mol. Med., 86, 785-789.
    • (2008) J. Mol. Med , vol.86 , pp. 785-789
    • Cao, Y.1    Cao, R.2    Hedlund, E.-M.3
  • 57
    • 33748793979 scopus 로고    scopus 로고
    • Signaling aptamers created using fluorescent nucleotide analogues
    • Katilius, E., Katiliene, Z. and Woodbury, N. W. (2006) Signaling aptamers created using fluorescent nucleotide analogues. Anal. Chem., 78, 6484-6489.
    • (2006) Anal. Chem , vol.78 , pp. 6484-6489
    • Katilius, E.1    Katiliene, Z.2    Woodbury, N.W.3
  • 59
    • 71649110756 scopus 로고    scopus 로고
    • Fluorescence aptasensor based on competitive-binding for human neutrophil elastase detection
    • He, J. L., Wu, Z. S., Zhang, S. B., Shen, G. L. and Yu, R. Q. (2010) Fluorescence aptasensor based on competitive-binding for human neutrophil elastase detection. Talanta, 80, 1264-1268.
    • (2010) Talanta , vol.80 , pp. 1264-1268
    • He, J.L.1    Wu, Z.S.2    Zhang, S.B.3    Shen, G.L.4    Yu, R.Q.5
  • 60
    • 0028826936 scopus 로고
    • Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition
    • Lin, Y., Padmapriya, A., Morden, K. M. and Jayasena, S. D. (1995) Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition. Proc. Natl Acad. Sci. USA, 92, 11044-11048.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11044-11048
    • Lin, Y.1    Padmapriya, A.2    Morden, K.M.3    Jayasena, S.D.4
  • 61
    • 4444352520 scopus 로고    scopus 로고
    • Signaling aptamer/protein binding by a molecular light switch complex
    • Jiang, Y., Fang, X. and Bai, C. (2004) Signaling aptamer/protein binding by a molecular light switch complex. Anal. Chem., 76, 5230-5235.
    • (2004) Anal. Chem , vol.76 , pp. 5230-5235
    • Jiang, Y.1    Fang, X.2    Bai, C.3
  • 63
    • 0028946629 scopus 로고
    • Interaction of dimeric intercalating dyes with single-stranded DNA
    • Rye, H. S. and Glazer, A. N. (1995) Interaction of dimeric intercalating dyes with single-stranded DNA. Nucleic Acids Res., 23, 1215-1222.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1215-1222
    • Rye, H.S.1    Glazer, A.N.2
  • 64
    • 33644676039 scopus 로고    scopus 로고
    • Detection of oncoprotein platelet-derived growth factor using a fluorescent signaling complex of an aptamer and TOTO
    • Zhou, C., Jiang, Y., Hou, S., Ma, B., Fang, X. and Li, M. (2006) Detection of oncoprotein platelet-derived growth factor using a fluorescent signaling complex of an aptamer and TOTO. Anal. Bioanal. Chem., 384, 1175-1180.
    • (2006) Anal. Bioanal. Chem , vol.384 , pp. 1175-1180
    • Zhou, C.1    Jiang, Y.2    Hou, S.3    Ma, B.4    Fang, X.5    Li, M.6
  • 65
    • 33845492343 scopus 로고    scopus 로고
    • Sensitive detection of protein by an aptamer-based label-free fluorescing molecular switch
    • Li, B., Wei, H. and Dong, S. (2007) Sensitive detection of protein by an aptamer-based label-free fluorescing molecular switch. Chem. Commun., 73-75.
    • (2007) Chem. Commun. , pp. 73-75
    • Li, B.1    Wei, H.2    Dong, S.3
  • 66
    • 0014202608 scopus 로고
    • A fluorescent complex between ethidium bromide and nucleic acids. Physical-chemical characterization
    • LePecq, J. B. and Paoletti, C. (1967) A fluorescent complex between ethidium bromide and nucleic acids. Physical-chemical characterization. J. Mol. Biol., 27, 87-106.
    • (1967) J. Mol. Biol , vol.27 , pp. 87-106
    • Lepecq, J.B.1    Paoletti, C.2
  • 67
    • 19744382860 scopus 로고    scopus 로고
    • Exonuclease III protection assay with FRET probe for detecting DNA-binding proteins
    • Wang, J., Li, T., Guo, X. and Lu, Z. (2005) Exonuclease III protection assay with FRET probe for detecting DNA-binding proteins. Nucleic Acids Res., 33, e23.
    • (2005) Nucleic Acids Res , vol.33
    • Wang, J.1    Li, T.2    Guo, X.3    Lu, Z.4
  • 68
    • 0034746919 scopus 로고    scopus 로고
    • NF-kB: A key role in inflammatory diseases
    • Tak, P. P. and Firestein, G. S. (2001) NF-kB: a key role in inflammatory diseases. J. Clin. Invest., 107, 7-11.
    • (2001) J. Clin. Invest , vol.107 , pp. 7-11
    • Tak, P.P.1    Firestein, G.S.2
  • 69
    • 0036781052 scopus 로고    scopus 로고
    • NF-[kappa]B regulation in the immune system
    • Li, Q. and Verma, I. M. (2002) NF-[kappa]B regulation in the immune system. Nat. Rev. Immunol., 2, 725-734.
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 70
    • 3843052483 scopus 로고    scopus 로고
    • Nuclear factor-kB: Its role in health and disease
    • Kumar, A., Takada, Y., Boriek, A. M. and Aggarwal, B. B. (2004) Nuclear factor-kB: its role in health and disease. J. Mol. Med., 82, 434-448.
    • (2004) J. Mol. Med , vol.82 , pp. 434-448
    • Kumar, A.1    Takada, Y.2    Boriek, A.M.3    Aggarwal, B.B.4
  • 71
    • 49049120374 scopus 로고    scopus 로고
    • Fluorescence recovery assay for the detection of protein-DNA binding
    • Xu, X., Zhao, Z., Qin, L., Wei, W., Levine, J. E. and Mirkin, C. A. (2008) Fluorescence recovery assay for the detection of protein-DNA binding. Anal. Chem., 80, 5616-5621.
    • (2008) Anal. Chem , vol.80 , pp. 5616-5621
    • Xu, X.1    Zhao, Z.2    Qin, L.3    Wei, W.4    Levine, J.E.5    Mirkin, C.A.6
  • 72
    • 79960592998 scopus 로고    scopus 로고
    • A highly selective, label-free, homogenous luminescent switch-on probe for the detection of nanomolar transcription factor NF-kb
    • Ma, D.-L., Xu, T., Chan, D. S.-H., Man, B. Y.-W., Fong, W.-F. and Leung, C.-H. (2011) A highly selective, label-free, homogenous luminescent switch-on probe for the detection of nanomolar transcription factor NF-kb. Nucleic Acids Res., 39, e67.
    • (2011) Nucleic Acids Res , vol.39
    • Ma, D.-L.1    Xu, T.2    Chan, D.S.-H.3    Man, B.Y.-W.4    Fong, W.-F.5    Leung, C.-H.6
  • 73
    • 18044387257 scopus 로고    scopus 로고
    • Oridonin, a diterpenoid purified from Rabdosia rubescens, inhibits the proliferation of cells from lymphoid malignancies in association with blockade of the NF-kB signal pathways
    • Ikezoe, T., Yang, Y., Bandobashi, K., Saito, T., Takemoto, S., Machida, H., Togitani, K., Koeffler, H. P. and Taguchi, H. (2005) Oridonin, a diterpenoid purified from Rabdosia rubescens, inhibits the proliferation of cells from lymphoid malignancies in association with blockade of the NF-kB signal pathways. Mol. Cancer Ther., 4, 578-586.
    • (2005) Mol. Cancer Ther , vol.4 , pp. 578-586
    • Ikezoe, T.1    Yang, Y.2    Bandobashi, K.3    Saito, T.4    Takemoto, S.5    MacHida, H.6    Togitani, K.7    Koeffler, H.P.8    Taguchi, H.9
  • 74
    • 23044504665 scopus 로고    scopus 로고
    • Novel mechanism of inhibition of nuclear factor-kB DNA-binding activity by diterpenoids isolated from isodon rubescens
    • Leung, C.-H., Grill, S. P., Lam, W., Han, Q.-B., Sun, H.-D. and Cheng, Y.-C. (2005) Novel mechanism of inhibition of nuclear factor-kB DNA-binding activity by diterpenoids isolated from isodon rubescens. Mol. Pharmacol., 68, 286-297.
    • (2005) Mol. Pharmacol , vol.68 , pp. 286-297
    • Leung, C.-H.1    Grill, S.P.2    Lam, W.3    Han, Q.-B.4    Sun, H.-D.5    Cheng, Y.-C.6
  • 75
    • 81455133459 scopus 로고    scopus 로고
    • Fluorescent DNA-based enzyme sensors
    • in press doi:10. 1039/C0CS00162G
    • Dai, N. and Kool, E. T. (2011) Fluorescent DNA-based enzyme sensors. Chem. Soc. Rev., in press, doi:10. 1039/C0CS00162G.
    • (2011) Chem. Soc. Rev
    • Dai, N.1    Kool, E.T.2
  • 77
    • 59649112891 scopus 로고    scopus 로고
    • Fluorescent labeling of biomolecules with organic probes
    • Gonçalves, M. S. T. (2008) Fluorescent labeling of biomolecules with organic probes. Chem. Rev., 109, 190-212.
    • (2008) Chem. Rev , vol.109 , pp. 190-212
    • Gonçalves, M.S.T.1
  • 80
    • 33947607759 scopus 로고    scopus 로고
    • A novel detection of single-stranded DNA binding protein based on ss-DNA modified chip using surface plasmon resonance microscopy
    • Lu, J. Q., Xu, M. B., Zhou, X. W., Xu, J. G. and Tao, Q. (2007) A novel detection of single-stranded DNA binding protein based on ss-DNA modified chip using surface plasmon resonance microscopy. Chin. Chem. Lett., 18, 441-444.
    • (2007) Chin. Chem. Lett , vol.18 , pp. 441-444
    • Lu, J.Q.1    Xu, M.B.2    Zhou, X.W.3    Xu, J.G.4    Tao, Q.5
  • 81
    • 0037432163 scopus 로고    scopus 로고
    • A modified sensor chip for surface plasmon resonance enables a rapid determination of sequence specificity of DNA-binding proteins
    • Hao, D., Ohme-Takagi, M. and Yamasaki, K. (2003) A modified sensor chip for surface plasmon resonance enables a rapid determination of sequence specificity of DNA-binding proteins. FEBS Lett., 536, 151-156.
    • (2003) FEBS Lett , vol.536 , pp. 151-156
    • Hao, D.1    Ohme-Takagi, M.2    Yamasaki, K.3
  • 82
    • 77956909524 scopus 로고    scopus 로고
    • Double recognition of oligonucleotide and protein in the detection of DNA methylation with surface plasmon resonance biosensors
    • Pan, S., Xu, J., Shu, Y., Wang, F., Xia, W., Ding, Q., Xu, T., Zhao, C., Zhang, M., Huang, P. et al. (2010) Double recognition of oligonucleotide and protein in the detection of DNA methylation with surface plasmon resonance biosensors. Biosens. Bioelectron., 26, 850-853.
    • (2010) Biosens. Bioelectron , vol.26 , pp. 850-853
    • Pan, S.1    Xu, J.2    Shu, Y.3    Wang, F.4    Xia, W.5    Ding, Q.6    Xu, T.7    Zhao, C.8    Zhang, M.9    Huang, P.10
  • 83
    • 33847668930 scopus 로고    scopus 로고
    • Characterization of protein-DNA interactions using surface plasmon resonance spectroscopy with various assay schemes
    • Teh, H. F., Peh, W. Y. X., Su, X. and Thomsen, J. S. (2007) Characterization of protein-DNA interactions using surface plasmon resonance spectroscopy with various assay schemes. Biochemistry, 46, 2127-2135.
    • (2007) Biochemistry , vol.46 , pp. 2127-2135
    • Teh, H.F.1    Peh, W.Y.X.2    Su, X.3    Thomsen, J.S.4
  • 84
    • 33847063852 scopus 로고    scopus 로고
    • Effects of small molecular inhibitors on the binding between HIV-1 reverse transcriptase and DNA as revealed by SPR biosensor
    • Wu, L., Zhang, Q., Su, L., Huang, M., Zhao, J. and Yang, M. (2007) Effects of small molecular inhibitors on the binding between HIV-1 reverse transcriptase and DNA as revealed by SPR biosensor. Sens. Actuators, B, B122, 243-252.
    • (2007) Sens. Actuators B , vol.B122 , pp. 243-252
    • Wu, L.1    Zhang, Q.2    Su, L.3    Huang, M.4    Zhao, J.5    Yang, M.6
  • 85
    • 33947594154 scopus 로고    scopus 로고
    • Evaluation of two-and three-dimensional streptavidin binding platforms for surface plasmon resonance spectroscopy studies of DNA hybridization and protein-DNA binding
    • Yang, N., Su, X., Tjong, V. and Knoll, W. (2007) Evaluation of two-and three-dimensional streptavidin binding platforms for surface plasmon resonance spectroscopy studies of DNA hybridization and protein-DNA binding. Biosens. Bioelectron., 22, 2700-2706.
    • (2007) Biosens. Bioelectron , vol.22 , pp. 2700-2706
    • Yang, N.1    Su, X.2    Tjong, V.3    Knoll, W.4
  • 87
    • 1842580880 scopus 로고    scopus 로고
    • Parallel, quantitative measurement of protein binding to a 120-element double-stranded DNA array in real time using surface plasmon resonance microscopy
    • Shumaker-Parry, J. S., Aebersold, R. and Campbell, C. T. (2004) Parallel, quantitative measurement of protein binding to a 120-element double-stranded DNA array in real time using surface plasmon resonance microscopy. Anal. Chem., 76, 2071-2082.
    • (2004) Anal. Chem , vol.76 , pp. 2071-2082
    • Shumaker-Parry, J.S.1    Aebersold, R.2    Campbell, C.T.3
  • 88
    • 41949095838 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer in near-infrared fluorescent oligonucleotide probes for detecting protein-DNA interactions
    • Zhang, S., Metelev, V., Tabatadze, D., Zamecnik, P. C. and Bogdanov, A. Jr (2008) Fluorescence resonance energy transfer in near-infrared fluorescent oligonucleotide probes for detecting protein-DNA interactions. Proc. Natl Acad. Sci. USA, 105, 4156-4161.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 4156-4161
    • Zhang, S.1    Metelev, V.2    Tabatadze, D.3    Zamecnik, P.C.4    Bogdanov Jr., A.5


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