메뉴 건너뛰기




Volumn , Issue , 2008, Pages 1-27

Investigations on Fluorine-Labeled Ribonucleic Acids by 19F NMR Spectroscopy

Author keywords

19F NMR spectroscopy; Biomolecules; Chemical shift; Fluorinated nucleobases; Fluorinated ribose units; Nucleic acid structure

Indexed keywords


EID: 77950593478     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527623112.ch1     Document Type: Chapter
Times cited : (8)

References (55)
  • 1
    • 85027842129 scopus 로고    scopus 로고
    • Chapter in On-line Textbook, Biophysical Society
    • Gerig, J. T., Fluorine, N. M. R., Chapter in On-line Textbook, Biophysical Society, 2001, (http://www.biophysics.org/img/jtg2001-2.pdf).
    • (2001)
    • Gerig, J.T.1    Fluorine, N.M.R.2
  • 2
    • 0017224909 scopus 로고
    • Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate binding
    • Hull, W. E., Sykes, B. D., Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate binding. Biochemistry 1976, 15, 1535-1546.
    • (1976) Biochemistry , vol.15 , pp. 1535-1546
    • Hull, W.E.1    Sykes, B.D.2
  • 4
    • 0033631853 scopus 로고    scopus 로고
    • The H2 18O solvent-induced isotope shift in 19F NMR
    • Arnold, J. R. P., Fisher, J. The H2 18O solvent-induced isotope shift in 19F NMR. J. Magn. Reson. 2000. 142: 1-10.
    • (2000) J. Magn. Reson , vol.142 , pp. 1-10
    • Arnold, J.R.P.1    Fisher, J.2
  • 5
    • 0346031092 scopus 로고    scopus 로고
    • Observation of 18O solvent-induced isotope shifts in 19F NMR signals
    • Arnold, J. R. P., Fisher, J., Observation of 18O solvent-induced isotope shifts in 19F NMR signals. Chem. Commun. 1998, 1859-1860.
    • (1998) Chem. Commun. , pp. 1859-1860
    • Arnold, J.R.P.1    Fisher, J.2
  • 6
    • 0025093242 scopus 로고
    • The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate: Application to fluorotryptophan labelling to the H{thorn}-ATPase of Escherichia coli and NMR studies
    • Kim, H.-W., Perez, J. A., Ferguson, S. J., Campbell, I. D. The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate: Application to fluorotryptophan labelling to the H{thorn}-ATPase of Escherichia coli and NMR studies. FEBS Lett. 1990. 272: 34-36.
    • (1990) FEBS Lett , vol.272 , pp. 34-36
    • Kim, H.-W.1    Perez, J.A.2    Ferguson, S.J.3    Campbell, I.D.4
  • 7
    • 0042307439 scopus 로고    scopus 로고
    • Selective incorporation of 19F-labeled Trp side chains for NMRspectroscopy-based ligand-protein interaction studies
    • Leone, M., Rodriguez-Mias, R. A., Pellecchia, M., Selective incorporation of 19F-labeled Trp side chains for NMRspectroscopy-based ligand-protein interaction studies. Chembiochem 2003, 4, 649-650.
    • (2003) Chembiochem , vol.4 , pp. 649-650
    • Leone, M.1    Rodriguez-Mias, R.A.2    Pellecchia, M.3
  • 8
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren, C. J., Anthony-Cahill, S. J.,Griffith, M. C., Schultz, P. G., A general method for site-specific incorporation of unnatural amino acids into proteins. Science 1989, 244, 182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 9
    • 0031937870 scopus 로고    scopus 로고
    • Expansion of the genetic code: Site-directed p-fluoro-phenylalanine incorporation inEscherichia coli
    • Furter, R. Expansion of the genetic code: Site-directed p-fluoro-phenylalanine incorporation inEscherichia coli. Protein Sci. 1998. 7: 419-426.
    • (1998) Protein Sci , vol.7 , pp. 419-426
    • Furter, R.1
  • 10
    • 33846809165 scopus 로고    scopus 로고
    • Site-specific incorporation of a 19F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity
    • Jackson, J. C., Hammill, J. T., Mehl, R. A. Site-specific incorporation of a 19F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity. J. Am. Chem. Soc. 2007. 129: 1160-1166.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 1160-1166
    • Jackson, J.C.1    Hammill, J.T.2    Mehl, R.A.3
  • 11
    • 33747801406 scopus 로고    scopus 로고
    • 19F NMRstudies of the native and denatured states of green fluorescent protein
    • Khan, F., Kuprov, I., Craggs, T. D., Hore, P. J., Jackson, S. E. 19F NMRstudies of the native and denatured states of green fluorescent protein. J. Am. Chem. Soc. 2006. 128: 10729-10737.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10729-10737
    • Khan, F.1    Kuprov, I.2    Craggs, T.D.3    Hore, P.J.4    Jackson, S.E.5
  • 12
    • 9644284454 scopus 로고    scopus 로고
    • Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR Studies
    • Shu, Q., Frieden, C. Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR Studies. J. Mol. Biol. 2005. 345: 599-610.
    • (2005) J. Mol. Biol , vol.345 , pp. 599-610
    • Shu, Q.1    Frieden, C.2
  • 13
    • 33646160625 scopus 로고    scopus 로고
    • Structural studies of Bcl-xL/ligand complexes using 19F NMR
    • Yu, L., Hajduk, P. J., Mack, J., Olejniczak, E.T., Structural studies of Bcl-xL/ligand complexes using 19F NMR. J. Biomol. NMR 2006, V34, 221-227.
    • (2006) J. Biomol. NMR , vol.34 V , pp. 221-227
    • Yu, L.1    Hajduk, P.J.2    Mack, J.3    Olejniczak, E.T.4
  • 15
    • 25444475544 scopus 로고    scopus 로고
    • Sensitivity improvement in 19F NMR-based screening experiments: Theoretical considerations and experimental applications
    • Dalvit, C., Mongelli, N., Papeo, G., Giordano, P., Veronesi, M., Moskau, D., Kummerle, R. Sensitivity improvement in 19F NMR-based screening experiments: Theoretical considerations and experimental applications. J. Am. Chem. Soc. 2005. 127: 13380-13385.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 13380-13385
    • Dalvit, C.1    Mongelli, N.2    Papeo, G.3    Giordano, P.4    Veronesi, M.5    Moskau, D.6    Kummerle, R.7
  • 18
    • 0038207989 scopus 로고    scopus 로고
    • Fluorine-NMR experiments for highthroughput screening: Theoretical aspects, practical considerations, and range of applicability
    • Dalvit, C., Fagerness, P. E., Hadden, D. T. A., Sarver, R. W., Stockman, B. J., Fluorine-NMR experiments for highthroughput screening: Theoretical aspects, practical considerations, and range of applicability. J. Am. Chem. Soc., 2003, 125, 7696-7703.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7696-7703
    • Dalvit, C.1    Fagerness, P.E.2    Hadden, D.T.A.3    Sarver, R.W.4    Stockman, B.J.5
  • 19
    • 0037030693 scopus 로고    scopus 로고
    • NMR-based screening with competition water-ligand observed via gradient spectroscopy experiments: Detection of high-affinity ligands
    • Dalvit, C., Fasolini, M., Flocco, M., Knapp, S., Pevarello, P., Veronesi, M. NMR-based screening with competition water-ligand observed via gradient spectroscopy experiments: Detection of high-affinity ligands. J. Med. Chem. 2002. 45: 2610-2614.
    • (2002) J. Med. Chem , vol.45 , pp. 2610-2614
    • Dalvit, C.1    Fasolini, M.2    Flocco, M.3    Knapp, S.4    Pevarello, P.5    Veronesi, M.6
  • 21
    • 0036893645 scopus 로고    scopus 로고
    • Fluorine-NMR Competition binding experiments for high-throughput screening of large compound mixtures
    • Dalvit, C., Flocco, M., Veronesi, M., Stockman, B. J., Fluorine-NMR Competition binding experiments for high-throughput screening of large compound mixtures. J. Comb. Chem. 2002, 5, 605-611.
    • (2002) J. Comb. Chem. , vol.5 , pp. 605-611
    • Dalvit, C.1    Flocco, M.2    Veronesi, M.3    Stockman, B.J.4
  • 22
    • 19944422116 scopus 로고    scopus 로고
    • Rapid NMR-based functional screening and IC50 measurements performed at unprecedentedly low enzyme concentration
    • Dalvit, C., Papeo, G., Mongelli, N., Giordano, P., Saccardo, B., Costa, A., Veronesi, M., Ko, S. Y. Rapid NMR-based functional screening and IC50 measurements performed at unprecedentedly low enzyme concentration. Drug Dev. Res. 2005. 64: 105-113.
    • (2005) Drug Dev. Res , vol.64 , pp. 105-113
    • Dalvit, C.1    Papeo, G.2    Mongelli, N.3    Giordano, P.4    Saccardo, B.5    Costa, A.6    Veronesi, M.7    Ko, S.Y.8
  • 23
    • 0024284771 scopus 로고
    • Partial assignment of resonances in the fluorine-19 nuclear magnetic resonance spectra of 5-fluorouracil-substituted transfer RNAs
    • Hardin, C. C., Gollnick, P., Horowitz, J., Partial assignment of resonances in the fluorine-19 nuclear magnetic resonance spectra of 5-fluorouracil-substituted transfer RNAs. Biochemistry 1988, 27, 487-495.
    • (1988) Biochemistry , vol.27 , pp. 487-495
    • Hardin, C.C.1    Gollnick, P.2    Horowitz, J.3
  • 24
    • 0020586494 scopus 로고
    • Isolation characterization of two 5-fluorouracil-substituted Escherichia coli initiator methionine transfer ribonucleic acids
    • Hills, D. C., Cotten, M. L., Horowitz, J., Isolation characterization of two 5-fluorouracil-substituted Escherichia coli initiator methionine transfer ribonucleic acids. Biochemistry 1983, 22, 1113-1122.
    • (1983) Biochemistry , vol.22 , pp. 1113-1122
    • Hills, D.C.1    Cotten, M.L.2    Horowitz, J.3
  • 25
    • 0030930750 scopus 로고    scopus 로고
    • Localization of the major ethidium bromide binding site on tRNA
    • Chu, W. C., Liu, J. C., Horowitz, J. Localization of the major ethidium bromide binding site on tRNA. Nucleic Acids Res. 1997. 25: 3944-3949.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3944-3949
    • Chu, W.C.1    Liu, J.C.2    Horowitz, J.3
  • 26
    • 0026457631 scopus 로고
    • Correlations between fluorine-19 nuclear magnetic resonance chemical shift and the secondary and tertiary structure of 5-fluorouracil-substituted tRNA
    • Chu, W.-C., Kintanar, A., Horowitz, J. Correlations between fluorine-19 nuclear magnetic resonance chemical shift and the secondary and tertiary structure of 5-fluorouracil-substituted tRNA. J. Mol. Biol. 1992. 227: 1173-1181.
    • (1992) J. Mol. Biol , vol.227 , pp. 1173-1181
    • Chu, W.-C.1    Kintanar, A.2    Horowitz, J.3
  • 27
    • 0026468016 scopus 로고
    • Fluorine-19 nuclear magnetic resonance as a probe of the solution structure of mutants of 5-fluorouracil-substituted Escherichia coli valine tRNA
    • Chu, W.-C., Feiz, V., Derrick, W. B., Horowitz, J. Fluorine-19 nuclear magnetic resonance as a probe of the solution structure of mutants of 5-fluorouracil-substituted Escherichia coli valine tRNA. J. Mol. Biol. 1992. 227: 1164-1172.
    • (1992) J. Mol. Biol , vol.227 , pp. 1164-1172
    • Chu, W.-C.1    Feiz, V.2    Derrick, W.B.3    Horowitz, J.4
  • 28
    • 0026344312 scopus 로고
    • Fluorine-19 NMR studies of the thermal unfolding of 5-fluorouracil-substituted Escherichia coli valine transfer RNA
    • Chu, W.-C., Horowitz, J. Fluorine-19 NMR studies of the thermal unfolding of 5-fluorouracil-substituted Escherichia coli valine transfer RNA. FEBS Lett. 1991. 295: 159-162.
    • (1991) FEBS Lett , vol.295 , pp. 159-162
    • Chu, W.-C.1    Horowitz, J.2
  • 29
    • 0025804403 scopus 로고
    • Recognition of Escherichia coli valine transfer RNA by its cognate synthetase: a fluorine-19 NMR study
    • Chu, W. C., Horowitz, J., Recognition of Escherichia coli valine transfer RNA by its cognate synthetase: a fluorine-19 NMR study. Biochemistry 1991, 30, 1655-1663.
    • (1991) Biochemistry , vol.30 , pp. 1655-1663
    • Chu, W.C.1    Horowitz, J.2
  • 30
    • 0023019264 scopus 로고
    • Fluorine-19 nuclear magnetic resonance studies of the structure of 5-fluorouracil-substituted Escherichia coli transfer RNA
    • Hardin, C. C., Gollnick, P., Kallenbach, N. R., Cohn, M., Horowitz, J., Fluorine-19 nuclear magnetic resonance studies of the structure of 5-fluorouracil-substituted Escherichia coli transfer RNA. Biochemistry 1986, 25, 5699-5709.
    • (1986) Biochemistry , vol.25 , pp. 5699-5709
    • Hardin, C.C.1    Gollnick, P.2    Kallenbach, N.R.3    Cohn, M.4    Horowitz, J.5
  • 31
    • 0022596896 scopus 로고
    • Fluorine-19 nuclear magnetic resonance study of codon-anticodon interaction in 5-fluorouracil-substituted E. coli transfer RNAs.
    • Gollnick, P., Hardin, C. C., Horowitz, J. Fluorine-19 nuclear magnetic resonance study of codon-anticodon interaction in 5-fluorouracil-substituted E. coli transfer RNAs. Nucleic Acids Res. 1986. 14: 4659-4672.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4659-4672
    • Gollnick, P.1    Hardin, C.C.2    Horowitz, J.3
  • 32
    • 0016301485 scopus 로고
    • Isolation and partial characterization of Escherichia coli valine transfer RNA with uridine and uridine-derived residues replaced by 5-fluorouridine
    • Horowitz, J., Ching-Nan, O., Ishaq, M., Ofengand, J., Bierbaum, J. Isolation and partial characterization of Escherichia coli valine transfer RNA with uridine and uridine-derived residues replaced by 5-fluorouridine. J. Mol. Biol. 1974. 88: 301-304.
    • (1974) J. Mol. Biol , vol.88 , pp. 301-304
    • Horowitz, J.1    Ching-Nan, O.2    Ishaq, M.3    Ofengand, J.4    Bierbaum, J.5
  • 33
    • 0017368182 scopus 로고
    • 19F nuclear magnetic resonance of 5-fluorouridine-substituted tRNA1Val from Escherichia coli
    • Horowitz, J., Ofengand, J., Daniel,W. E. Jr., Cohn, M. 19F nuclear magnetic resonance of 5-fluorouridine-substituted tRNA1Val from Escherichia coli. J. Biol. Chem. 1977. 252: 4418-4420.
    • (1977) J. Biol. Chem , vol.252 , pp. 4418-4420
    • Horowitz, J.1    Ofengand, J.2    Daniel Jr., W.E.3    Cohn, M.4
  • 34
    • 0023645650 scopus 로고
    • Mobility of individual 5-fluorouridine residues in 5-fluorouracil-substituted Escherichia coli valine transfer RNA: A 19F nuclear magnetic resonance relaxation study
    • Hardin, C. C., Horowitz, J. Mobility of individual 5-fluorouridine residues in 5-fluorouracil-substituted Escherichia coli valine transfer RNA: A 19F nuclear magnetic resonance relaxation study. J. Mol. Biol. 1987. 197: 555-569.
    • (1987) J. Mol. Biol , vol.197 , pp. 555-569
    • Hardin, C.C.1    Horowitz, J.2
  • 35
    • 0024432461 scopus 로고
    • 19F NMR of 5-fluorouracil-substituted transfer RNA transcribed in vitro: resonance assignment of fluorouracil-guanine base pairs
    • Chu, W.-C., Horowitz, J. 19F NMR of 5-fluorouracil-substituted transfer RNA transcribed in vitro: resonance assignment of fluorouracil-guanine base pairs. Nucleic Acids Res. 1989. 17: 7241-7252.
    • (1989) Nucleic Acids Res , vol.17 , pp. 7241-7252
    • Chu, W.-C.1    Horowitz, J.2
  • 36
    • 0242444679 scopus 로고    scopus 로고
    • Dynamic modes of the flipped-out cytosine during HhaI methyltransferase-DNA interactions in solution
    • Klimasauskas, S., Szyperski, T., Serva, S., Wuthrich, K. Dynamic modes of the flipped-out cytosine during HhaI methyltransferase-DNA interactions in solution. EMBO J. 1998. 17: 317-324.
    • (1998) EMBO J , vol.17 , pp. 317-324
    • Klimasauskas, S.1    Szyperski, T.2    Serva, S.3    Wuthrich, K.4
  • 37
    • 0029073091 scopus 로고
    • The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism forRNAcatalytic cleavage
    • Scott, W. G., Finch, J. T., Klug, A., The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism forRNAcatalytic cleavage.Cell 1995, 81, 991-1002.
    • (1995) Cell , vol.81 , pp. 991-1002
    • Scott, W.G.1    Finch, J.T.2    Klug, A.3
  • 38
    • 33746228126 scopus 로고    scopus 로고
    • Tertiary contacts distant from the active site prime a ribozyme for catalysis
    • Martick, M., Scott,W. G., Tertiary contacts distant from the active site prime a ribozyme for catalysis. Cell 2007, 126, 309-320.
    • (2007) Cell , vol.126 , pp. 309-320
    • Martick, M.1    Scott, W.G.2
  • 39
    • 0035826822 scopus 로고    scopus 로고
    • Dissection of the ion-induced folding of the hammerhead ribozyme using 19F NMR
    • USA
    • Hammann, C., Norman, D. G., Lilley, D. M. J., Dissection of the ion-induced folding of the hammerhead ribozyme using 19F NMR. Proc. Natl. Acad. Sci. USA 2001 98, 5503-5508.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 5503-5508
    • Hammann, C.1    Norman, D.G.2    Lilley, D.M.J.3
  • 42
    • 0031552350 scopus 로고    scopus 로고
    • Solution structure of the HIV-2 TARargininamide complex
    • Brodsky, A. S., Williamson, J. R. Solution structure of the HIV-2 TARargininamide complex. J. Mol. Biol. 1997. 267: 624-639.
    • (1997) J. Mol. Biol , vol.267 , pp. 624-639
    • Brodsky, A.S.1    Williamson, J.R.2
  • 43
    • 0029852357 scopus 로고    scopus 로고
    • Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge
    • Aboul-ela, F., Karn, J., Varani, G., Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge. NucleicAcids Res. 1996, 24, 3974-3981.
    • (1996) NucleicAcids Res , vol.24 , pp. 3974-3981
    • Aboul-ela, F.1    Karn, J.2    Varani, G.3
  • 44
    • 4644322804 scopus 로고    scopus 로고
    • Enzymatic synthesis and 19F NMR studies of 2-fluoroadenine-substituted RNA
    • Scott, L. G., Geierstanger, B. H., Williamson, J. R., Hennig, M. Enzymatic synthesis and 19F NMR studies of 2-fluoroadenine-substituted RNA. J. Am. Chem. Soc. 2004. 126: 11776-11777.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 11776-11777
    • Scott, L.G.1    Geierstanger, B.H.2    Williamson, J.R.3    Hennig, M.4
  • 45
    • 33646596900 scopus 로고    scopus 로고
    • Measurement of long-range 1H-19F scalar coupling constants and their glycosidic torsion dependence in 5-fluoropyrimidine-substituted RNA
    • Hennig, M., Munzarova, M. L., Bermel, W., Scott, L. G., Sklenar, V., Williamson, J. R. Measurement of long-range 1H-19F scalar coupling constants and their glycosidic torsion dependence in 5-fluoropyrimidine-substituted RNA. J. Am. Chem. Soc. 2006. 128: 5851-5858.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 5851-5858
    • Hennig, M.1    Munzarova, M.L.2    Bermel, W.3    Scott, L.G.4    Sklenar, V.5    Williamson, J.R.6
  • 46
    • 0034743770 scopus 로고    scopus 로고
    • Measurement application of 1H-19F dipolar couplings in the structure determination of 20-fluorolabeled RNA
    • Luy, B., Marino, J. P., Measurement application of 1H-19F dipolar couplings in the structure determination of 20-fluorolabeled RNA. J. Biomol. NMR 2001, 20, 39-47.
    • (2001) J. Biomol. NMR , vol.20 , pp. 39-47
    • Luy, B.1    Marino, J.P.2
  • 47
    • 0034130999 scopus 로고    scopus 로고
    • Filamentous bacteriophage for aligning RNA, DNA,and proteins for measurement of nuclear magnetic resonance dipolar coupling interactions
    • Hansen, M. R., Hanson, P., Pardi, A. Filamentous bacteriophage for aligning RNA, DNA,and proteins for measurement of nuclear magnetic resonance dipolar coupling interactions. Methods Enzymol. 2000. 317: 220-240.
    • (2000) Methods Enzymol , vol.317 , pp. 220-240
    • Hansen, M.R.1    Hanson, P.2    Pardi, A.3
  • 48
    • 0037225166 scopus 로고    scopus 로고
    • Bistable Secondary structures of small RNAs and their structural probing by comparative imino proton NMR spectroscopy
    • Höbartner, C., Micura, R., Bistable Secondary structures of small RNAs and their structural probing by comparative imino proton NMR spectroscopy. J. Mol. Biol. 2003, 325, 421-431.
    • (2003) J. Mol. Biol. , vol.325 , pp. 421-431
    • Höbartner, C.1    Micura, R.2
  • 49
    • 23944461060 scopus 로고    scopus 로고
    • Ribose 20-F labeling: A simple tool for the characterization of RNA secondary structure equilibria by 19F NMR spectroscopy
    • Kreutz, C., Kählig, H., Konrat, R., Micura, R. Ribose 20-F labeling: A simple tool for the characterization of RNA secondary structure equilibria by 19F NMR spectroscopy. J. Am. Chem. Soc. 2005. 127: 11558-11559.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 11558-11559
    • Kreutz, C.1    Käahlig, H.2    Konrat, R.3    Micura, R.4
  • 50
    • 33746238117 scopus 로고    scopus 로고
    • A general approach for the identification of site-specific RNA binders by 19F NMR spectroscopy: Proof of concept
    • Kreutz, C., Käahlig, H., Konrat, R., Micura, R. A general approach for the identification of site-specific RNA binders by 19F NMR spectroscopy: Proof of concept. Angew. Chem. Int. Ed. 2006. 45: 3450-3453.
    • (2006) Angew. Chem. Int. Ed , vol.45 , pp. 3450-3453
    • Kreutz, C.1    Käahlig, H.2    Konrat, R.3    Micura, R.4
  • 51
    • 0034603154 scopus 로고    scopus 로고
    • Adaptive recognition by nucleic acid aptamers
    • Hermann, T., Patel, D. J., Adaptive recognition by nucleic acid aptamers. Science 2000, 287, 820-825.
    • (2000) Science , vol.287 , pp. 820-825
    • Hermann, T.1    Patel, D.J.2
  • 52
    • 0031688019 scopus 로고    scopus 로고
    • Solution structure of the tobramycin-RNA aptamer complex
    • Jiang, L., Patel, D. J. Solution structure of the tobramycin-RNA aptamer complex. Nat. Struct. Biol. 1998. 5: 769-774.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 769-774
    • Jiang, L.1    Patel, D.J.2
  • 53
    • 0030971745 scopus 로고    scopus 로고
    • Solution structures of 5-fluorouracilsubstituted RNA duplexes containing G-U wobble base pairs
    • Sahasrabudhe, P. V., Gmeiner, W. H., Solution structures of 5-fluorouracilsubstituted RNA duplexes containing G-U wobble base pairs. Biochemistry 1997, 36, 5981-5991.
    • (1997) Biochemistry , vol.36 , pp. 5981-5991
    • Sahasrabudhe, P.V.1    Gmeiner, W.H.2
  • 54
    • 0016291368 scopus 로고
    • Nucleoside conformations. 16. Nuclear magnetic resonance and circular dichroism studies on pyrimidine-20-fluoro-20-deoxyribonucleosides
    • Blandin, M., Tran Dinh, S., Catlin, J. C., Guschlbauer, W., Nucleoside conformations. 16. Nuclear magnetic resonance and circular dichroism studies on pyrimidine-20-fluoro-20-deoxyribonucleosides. Biochim. Biophys. Acta 1974, 361, 249-256.
    • (1974) Biochim. Biophys. Acta , vol.361 , pp. 249-256
    • Blandin, M.1    Tran Dinh, S.2    Catlin, J.C.3    Guschlbauer, W.4
  • 55
    • 0030768418 scopus 로고    scopus 로고
    • Structural comparison of oligoribonucleotides and their 20-deoxy-20-fluoro analogs by heteronuclear NMR spectroscopy
    • Reif, B., Wittmann, V., Schwalbe, H., Griesinger, C., Wörner, K., Jahn-Hofmann, K. W. E. J., Bermel, W., Structural comparison of oligoribonucleotides and their 20-deoxy-20-fluoro analogs by heteronuclear NMR spectroscopy. Helv. Chim. Acta 1997, 80, 1952-1971.
    • (1997) Helv. Chim. Acta , vol.80 , pp. 1952-1971
    • Reif, B.1    Wittmann, V.2    Schwalbe, H.3    Griesinger, C.4    Wörner, K.5    Hofmann, K.W.E.J.6    Bermel, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.