메뉴 건너뛰기




Volumn 8, Issue 10, 2002, Pages 1242-1252

A biosensor for theophylline based on fluorescence detection of ligand-induced hammerhead ribozyme cleavage

Author keywords

Activity assay; Asthma; Bronchodilator; Catalytic RNA; Fluorescence resonance energy transfer; RNA conformational change

Indexed keywords

CAFFEINE; LIGAND; RIBOZYME; THEOPHYLLINE;

EID: 0036795275     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838202028066     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 0031463467 scopus 로고    scopus 로고
    • Ion-induced folding of the hammerhead ribozyme: A fluorescence resonance energy transfer study
    • Bassi GS, Murchie AI, Walter F, Clegg RM, Lilley DM. 1997. Ion-induced folding of the hammerhead ribozyme: A fluorescence resonance energy transfer study. EMBO J 16:7481-7489.
    • (1997) EMBO J , vol.16 , pp. 7481-7489
    • Bassi, G.S.1    Murchie, A.I.2    Walter, F.3    Clegg, R.M.4    Lilley, D.M.5
  • 3
    • 0036469778 scopus 로고    scopus 로고
    • Engineered allosteric ribozymes as biosensor components
    • Breaker RR. 2002. Engineered allosteric ribozymes as biosensor components. Curr Opin Biotechnol 13:31-39.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 31-39
    • Breaker, R.R.1
  • 4
    • 0030877619 scopus 로고    scopus 로고
    • Hammerhead ribozymes with a faster cleavage rate
    • Clouet-d'Orval B, Uhlenbeck OC. 1997. Hammerhead ribozymes with a faster cleavage rate. Biochemistry 36:9087-9092.
    • (1997) Biochemistry , vol.36 , pp. 9087-9092
    • Clouet-d'Orval, B.1    Uhlenbeck, O.C.2
  • 5
    • 0034848444 scopus 로고    scopus 로고
    • Detection of small organic analytes by fluorescing molecular switches
    • Frauendorf C, Jaschke A. 2001. Detection of small organic analytes by fluorescing molecular switches. Bioorg Med Chem 9:2521-2524.
    • (2001) Bioorg Med Chem , vol.9 , pp. 2521-2524
    • Frauendorf, C.1    Jaschke, A.2
  • 6
    • 0023840230 scopus 로고
    • ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg J, Dunn JJ. 1988. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J Bacteriol 170:1245-1253.
    • (1988) J Bacteriol , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 7
    • 0020519588 scopus 로고
    • Theophylline. A "state of the art" review
    • Hendeles L, Weinberger M. 1983. Theophylline. A "state of the art" review. Pharmacotherapy 3:2-44.
    • (1983) Pharmacotherapy , vol.3 , pp. 2-44
    • Hendeles, L.1    Weinberger, M.2
  • 8
    • 0033863669 scopus 로고    scopus 로고
    • High-throughput screening: New technology for the 21st century
    • Hertzberg RP, Pope AJ. 2000. High-throughput screening: New technology for the 21st century. Curr Opin Chem Biol 4:445-451.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 445-451
    • Hertzberg, R.P.1    Pope, A.J.2
  • 9
    • 0028224199 scopus 로고
    • High-resolution molecular discrimination by RNA
    • Jenison RD, Gill SC, Pardi A, Polisky B. 1994. High-resolution molecular discrimination by RNA. Science 263:1425-1429.
    • (1994) Science , vol.263 , pp. 1425-1429
    • Jenison, R.D.1    Gill, S.C.2    Pardi, A.3    Polisky, B.4
  • 11
    • 0035909052 scopus 로고    scopus 로고
    • Tertiary structure stability of the hairpin ribozyme in its natural and minimal forms: Different energetic contributions from a ribose zipper motif
    • Klostermeier D, Millar DP. 2001. Tertiary structure stability of the hairpin ribozyme in its natural and minimal forms: Different energetic contributions from a ribose zipper motif. Biochemistry 40:11211-11218.
    • (2001) Biochemistry , vol.40 , pp. 11211-11218
    • Klostermeier, D.1    Millar, D.P.2
  • 12
    • 0032755647 scopus 로고    scopus 로고
    • Allosteric selection of ribozymes that respond to the second messengers cGMP and cAMP
    • Koizumi M, Soukup GA, Kerr JN, Breaker RR. 1999. Allosteric selection of ribozymes that respond to the second messengers cGMP and cAMP. Nat Struct Biol 6:1062-1071.
    • (1999) Nat Struct Biol , vol.6 , pp. 1062-1071
    • Koizumi, M.1    Soukup, G.A.2    Kerr, J.N.3    Breaker, R.R.4
  • 14
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews DH, Sabina J, Zuker M, Turner DH. 1999. Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J Mol Biol 288:911-940.
    • (1999) J Mol Biol , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 15
    • 0034255512 scopus 로고    scopus 로고
    • Ribozyme-mediated inhibition of HIV 1 suggests nucleolar trafficking of HIV-1 RNA
    • Michienzi A, Cagnon L, Bahner I, Rossi JJ. 2000. Ribozyme-mediated inhibition of HIV 1 suggests nucleolar trafficking of HIV-1 RNA. Proc Natl Acad Sci USA 97:8955-8960.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8955-8960
    • Michienzi, A.1    Cagnon, L.2    Bahner, I.3    Rossi, J.J.4
  • 16
    • 0036277266 scopus 로고    scopus 로고
    • Effects of the concomitant administration of tamsulosin (0.8 mg/day) on the pharmacokinetic and safety profile of theophylline (5 mg/kg): A placebo-controlled evaluation
    • Miyazawa Y, Starkey LP, Forrest A, Schentag JJ, Kamimura H, Swarz H, Ito Y. 2002. Effects of the concomitant administration of tamsulosin (0.8 mg/day) on the pharmacokinetic and safety profile of theophylline (5 mg/kg): A placebo-controlled evaluation. J Internat Med Res 30:34-43.
    • (2002) J Internat Med Res , vol.30 , pp. 34-43
    • Miyazawa, Y.1    Starkey, L.P.2    Forrest, A.3    Schentag, J.J.4    Kamimura, H.5    Swarz, H.6    Ito, Y.7
  • 17
    • 0036293201 scopus 로고    scopus 로고
    • A pH-dependent conformational change, rather than the chemical step, appears to be rate-limiting in the hammerhead ribozyme cleavage reaction
    • Murray JB, Dunham CM, Scott WG. 2002. A pH-dependent conformational change, rather than the chemical step, appears to be rate-limiting in the hammerhead ribozyme cleavage reaction. J Mol Biol 315:121-130.
    • (2002) J Mol Biol , vol.315 , pp. 121-130
    • Murray, J.B.1    Dunham, C.M.2    Scott, W.G.3
  • 18
    • 0034732989 scopus 로고    scopus 로고
    • Location of cyanine-3 on double-stranded DNA: Importance for fluorescence resonance energy transfer studies
    • Norman DG, Grainger RJ, Uhrin D, Lilley DM. 2000. Location of cyanine-3 on double-stranded DNA: Importance for fluorescence resonance energy transfer studies. Biochemistry 39:6317-6324.
    • (2000) Biochemistry , vol.39 , pp. 6317-6324
    • Norman, D.G.1    Grainger, R.J.2    Uhrin, D.3    Lilley, D.M.4
  • 19
    • 0037154091 scopus 로고    scopus 로고
    • Reaction pathway of the trans-acting hepatitis delta virus ribozyme: A conformational change accompanies catalysis
    • Pereira MJ, Harris DA, Rueda D, Walter NG. 2002. Reaction pathway of the trans-acting hepatitis delta virus ribozyme: A conformational change accompanies catalysis. Biochemistry 41:730-740.
    • (2002) Biochemistry , vol.41 , pp. 730-740
    • Pereira, M.J.1    Harris, D.A.2    Rueda, D.3    Walter, N.G.4
  • 20
    • 0030467890 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of ribozyme kinetics reveals the mode of action of a facilitator oligonucleotide
    • Perkins TA, Wolf DE, Goodchild J. 1996. Fluorescence resonance energy transfer analysis of ribozyme kinetics reveals the mode of action of a facilitator oligonucleotide. Biochemistry 35:16370-16377.
    • (1996) Biochemistry , vol.35 , pp. 16370-16377
    • Perkins, T.A.1    Wolf, D.E.2    Goodchild, J.3
  • 21
    • 0028063567 scopus 로고
    • Three-dimensional structure of a hammerhead ribozyme
    • Pley HW, Flaherty KM, McKay DB. 1994. Three-dimensional structure of a hammerhead ribozyme. Nature 372:68-74.
    • (1994) Nature , vol.372 , pp. 68-74
    • Pley, H.W.1    Flaherty, K.M.2    McKay, D.B.3
  • 22
    • 0034655587 scopus 로고    scopus 로고
    • Design and optimization of effector-activated ribozyme ligases
    • Robertson MP, Ellington AD. 2000. Design and optimization of effector-activated ribozyme ligases. Nucleic Acids Res 28:1751-1759.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1751-1759
    • Robertson, M.P.1    Ellington, A.D.2
  • 26
    • 0029073091 scopus 로고
    • The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage
    • Scott WG, Finch JT, Klug A. 1995. The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage. Cell 81:991-1002.
    • (1995) Cell , vol.81 , pp. 991-1002
    • Scott, W.G.1    Finch, J.T.2    Klug, A.3
  • 27
    • 0035070585 scopus 로고    scopus 로고
    • Immobilized RNA switches for the analysis of complex chemical and biological mixtures
    • Seetharaman S, Zivarts M, Sudarsan N, Breaker RR. 2001. Immobilized RNA switches for the analysis of complex chemical and biological mixtures. Nat Biotechnol 19:336-341.
    • (2001) Nat Biotechnol , vol.19 , pp. 336-341
    • Seetharaman, S.1    Zivarts, M.2    Sudarsan, N.3    Breaker, R.R.4
  • 28
    • 0032834899 scopus 로고    scopus 로고
    • Rapid kinetic characterization of hammerhead ribozymes by real-time monitoring of fluorescence resonance energy transfer (FRET)
    • Singh KK, Parwaresch R, Krupp G. 1999. Rapid kinetic characterization of hammerhead ribozymes by real-time monitoring of fluorescence resonance energy transfer (FRET). RNA 5:1348-1356.
    • (1999) RNA , vol.5 , pp. 1348-1356
    • Singh, K.K.1    Parwaresch, R.2    Krupp, G.3
  • 29
    • 0033565475 scopus 로고    scopus 로고
    • Design of allosteric hammerhead ribozymes activated by ligand-induced structure stabilization
    • Soukup GA, Breaker RR. 1999a. Design of allosteric hammerhead ribozymes activated by ligand-induced structure stabilization. Structure Fold Des 7:783-791.
    • (1999) Structure Fold Des , vol.7 , pp. 783-791
    • Soukup, G.A.1    Breaker, R.R.2
  • 30
    • 0033616774 scopus 로고    scopus 로고
    • Engineering precision RNA molecular switches
    • Soukup GA, Breaker RR. 1999b. Engineering precision RNA molecular switches. Proc Natl Acad Sci USA 96:3584-3589.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3584-3589
    • Soukup, G.A.1    Breaker, R.R.2
  • 33
    • 0035001974 scopus 로고    scopus 로고
    • Generating new ligand-binding RNAs by affinity maturation and disintegration of allosteric ribozymes
    • Soukup GA, DeRose EC, Koizumi M, Breaker RR. 2001. Generating new ligand-binding RNAs by affinity maturation and disintegration of allosteric ribozymes. RNA 7:524-536.
    • (2001) RNA , vol.7 , pp. 524-536
    • Soukup, G.A.1    DeRose, E.C.2    Koizumi, M.3    Breaker, R.R.4
  • 34
    • 0034640131 scopus 로고    scopus 로고
    • Altering molecular recognition of RNA aptamers by allosteric selection
    • Soukup GA, Emilsson GA, Breaker RR. 2000. Altering molecular recognition of RNA aptamers by allosteric selection. J Mol Biol 298:623-632.
    • (2000) J Mol Biol , vol.298 , pp. 623-632
    • Soukup, G.A.1    Emilsson, G.A.2    Breaker, R.R.3
  • 35
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • van Roessel P, Brand AH. 2002. Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins. Nat Cell Biol 4:E15-E20.
    • (2002) Nat Cell Biol , vol.4
    • Van Roessel, P.1    Brand, A.H.2
  • 36
    • 0034808071 scopus 로고    scopus 로고
    • Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer
    • Walter NG. 2001. Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer. Methods 25:19-30.
    • (2001) Methods , vol.25 , pp. 19-30
    • Walter, N.G.1
  • 37
    • 0030969442 scopus 로고    scopus 로고
    • Real-time monitoring of hairpin ribozyme kinetics through base-specific quenching of fluorescein-labeled substrates
    • Walter NG, Burke JM. 1997. Real-time monitoring of hairpin ribozyme kinetics through base-specific quenching of fluorescein-labeled substrates. RNA 3:392-404.
    • (1997) RNA , vol.3 , pp. 392-404
    • Walter, N.G.1    Burke, J.M.2
  • 38
    • 0033656580 scopus 로고    scopus 로고
    • Fluorescence assays to study structure, dynamics, and function of RNA and RNA-ligand complexes
    • Walter NG, Burke JM. 2000. Fluorescence assays to study structure, dynamics, and function of RNA and RNA-ligand complexes. Methods Enzymol 317:409-440.
    • (2000) Methods Enzymol , vol.317 , pp. 409-440
    • Walter, N.G.1    Burke, J.M.2
  • 39
    • 0032979707 scopus 로고    scopus 로고
    • Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction
    • Walter NG, Burke JM, Millar DP. 1999. Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction. Nat Struct Biol 6:544-549.
    • (1999) Nat Struct Biol , vol.6 , pp. 544-549
    • Walter, N.G.1    Burke, J.M.2    Millar, D.P.3
  • 40
    • 0032522574 scopus 로고    scopus 로고
    • Tertiary structure formation in the hairpin ribozyme monitored by fluorescence resonance energy transfer
    • Walter NG, Hampel KJ, Brown KM, Burke JM. 1998, Tertiary structure formation in the hairpin ribozyme monitored by fluorescence resonance energy transfer. EMBO J 17:2378-2391.
    • (1998) EMBO J , vol.17 , pp. 2378-2391
    • Walter, N.G.1    Hampel, K.J.2    Brown, K.M.3    Burke, J.M.4
  • 41
    • 14244273876 scopus 로고    scopus 로고
    • In the fluorescent spotlight: Global and local conformational changes of small catalytic RNAs
    • Walter NG, Harris DA, Pereira MJ, Rueda D. 2002. In the fluorescent spotlight: Global and local conformational changes of small catalytic RNAs. Biopolymers 61:224-242.
    • (2002) Biopolymers , vol.61 , pp. 224-242
    • Walter, N.G.1    Harris, D.A.2    Pereira, M.J.3    Rueda, D.4
  • 42
    • 0031860104 scopus 로고    scopus 로고
    • Crystallographic structures of the hammerhead ribozyme: Relationship to ribozyme folding and catalysis
    • Wedekind JE, McKay DB. 1998. Crystallographic structures of the hammerhead ribozyme: Relationship to ribozyme folding and catalysis. Annu Rev Biophys Biomol Struct 27:475-502.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 475-502
    • Wedekind, J.E.1    McKay, D.B.2
  • 43
    • 0032853242 scopus 로고    scopus 로고
    • In vitro selection of functional nucleic acids
    • Wilson DS, Szostak JW. 1999. In vitro selection of functional nucleic acids. Annu Rev Biochem 68:611-647.
    • (1999) Annu Rev Biochem , vol.68 , pp. 611-647
    • Wilson, D.S.1    Szostak, J.W.2
  • 45
    • 0037165996 scopus 로고    scopus 로고
    • Correlating structural dynamics and function in single ribozyme molecules
    • Zhuang X, Kim H, Pereira MJ, Babcock HP, Walter NG, Chu S. 2002. Correlating structural dynamics and function in single ribozyme molecules. Science 296:1473-1476.
    • (2002) Science , vol.296 , pp. 1473-1476
    • Zhuang, X.1    Kim, H.2    Pereira, M.J.3    Babcock, H.P.4    Walter, N.G.5    Chu, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.