메뉴 건너뛰기




Volumn 266, Issue 1, 1997, Pages 144-159

Time-resolved synchrotron x-ray 'footprinting', a new approach to the study of nucleic acid structure and function: Application to Protein-DNA interactions and RNA folding

Author keywords

Footprinting; Kinetics; RNA folding; Synchrotron; X rays

Indexed keywords

HYDROXYL RADICAL; MAGNESIUM ION; PROTOZOAL RNA; RIBOZYME; SCAVENGER; THIOUREA;

EID: 0031566962     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0775     Document Type: Article
Times cited : (143)

References (81)
  • 1
    • 0029007094 scopus 로고
    • The time dependence of chemical modification reveals slow steps in the folding of a group I ribozyme
    • Banerjee A. R., Turner D. H. The time dependence of chemical modification reveals slow steps in the folding of a group I ribozyme. Biochemistry. 34:1995;6504-6512.
    • (1995) Biochemistry , vol.34 , pp. 6504-6512
    • Banerjee, A.R.1    Turner, D.H.2
  • 2
    • 0027434244 scopus 로고
    • Thermal unfolding of a group I ribozyme: The low-temperature transition is primarily disruption of tertiary structure
    • Banerjee A. R., Jaeger J. A., Turner D. H. Thermal unfolding of a group I ribozyme: the low-temperature transition is primarily disruption of tertiary structure. Biochemistry. 32:1993;153-163.
    • (1993) Biochemistry , vol.32 , pp. 153-163
    • Banerjee, A.R.1    Jaeger, J.A.2    Turner, D.H.3
  • 6
    • 0002913693 scopus 로고
    • Ionizing radiation in mammalian cells
    • I. Farhatazis, & M.A. Rodgers. TX: VCH Pubs
    • Biagolow J. E. Ionizing radiation in mammalian cells. Farhatazis I., Rodgers M. A. Radiation Chemistry Principles & Applications. 1987;VCH Pubs, TX.
    • (1987) Radiation Chemistry Principles & Applications
    • Biagolow, J.E.1
  • 7
    • 0027295486 scopus 로고
    • Modulation of the stability of a lac repressor mediated looped complex by temperature and ions: Allosteric regulation by chloride
    • Brenowitz M., Jamison E. Modulation of the stability of a lac repressor mediated looped complex by temperature and ions: allosteric regulation by chloride. Biochemistry. 32:1993;8693-8701.
    • (1993) Biochemistry , vol.32 , pp. 8693-8701
    • Brenowitz, M.1    Jamison, E.2
  • 8
    • 0001444289 scopus 로고
    • DNase I footprint analysis of protein-DNA binding
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, & K. Struhl. New York: John Wiley and Sons
    • Brenowitz M., Senear D. F. DNase I footprint analysis of protein-DNA binding. Ausubel F. M., Brent R, Kingston R. E., Moore D. D., Seidman J. G., Smith J. A., Struhl K. Current Protocols in Molecular Biology. 1989;John Wiley and Sons, New York.
    • (1989) Current Protocols in Molecular Biology
    • Brenowitz, M.1    Senear, D.F.2
  • 9
    • 0022437260 scopus 로고
    • Quantitative DNase footprint titration: A method for studying protein-DNA interactions
    • Brenowitz M., Senear D. F., Shea M. A., Ackers G. K. Quantitative DNase footprint titration: a method for studying protein-DNA interactions. Methods. Enzymol. 130:1986;132-181.
    • (1986) Methods. Enzymol. , vol.130 , pp. 132-181
    • Brenowitz, M.1    Senear, D.F.2    Shea, M.A.3    Ackers, G.K.4
  • 10
    • 0025874018 scopus 로고
    • The stability of a lac repressor mediated looped complex
    • Brenowitz M., Pickar A., Jamison E. The stability of a lac repressor mediated looped complex. Biochemistry. 30:1991;5986-5998.
    • (1991) Biochemistry , vol.30 , pp. 5986-5998
    • Brenowitz, M.1    Pickar, A.2    Jamison, E.3
  • 12
    • 0023666166 scopus 로고
    • The unusual conformation adopted by the adenine tracts in kinetoplast DNA
    • Burkhoff A. M., Tullius T. D. The unusual conformation adopted by the adenine tracts in kinetoplast DNA. Cell. 48:1987;935-943.
    • (1987) Cell , vol.48 , pp. 935-943
    • Burkhoff, A.M.1    Tullius, T.D.2
  • 13
    • 0002627604 scopus 로고
    • Radiation chemistry of the liquid state: (1) Water and homogeneous aqueous solutions
    • I. Farhatazis, & M.A. Rodgers. TX: VCH Pubs
    • Buxton G. V. Radiation chemistry of the liquid state: (1) water and homogeneous aqueous solutions. Farhatazis I., Rodgers M. A. Radiation Chemistry Principles & Applications.1987;VCH Pubs, TX.
    • (1987) Radiation Chemistry Principles & Applications
    • Buxton, G.V.1
  • 15
    • 0003017978 scopus 로고
    • Structure and mechanism of the large catalytic RNAs: Group I and group II introns and ribonuclease
    • R.F. Gesteland, & J. F Atkins. New York: Cold Spring Harbor Laboratory PressCold Spring Harbor
    • Cech T. R. Structure and mechanism of the large catalytic RNAs: group I and group II introns and ribonuclease. Gesteland R. F., Atkins J. F. The RNA World. 1993;Cold Spring Harbor Laboratory PressCold Spring Harbor, New York.
    • (1993) The RNA World
    • Cech, T.R.1
  • 16
    • 0028441183 scopus 로고
    • Representation of the secondary and tertiary structure of group I introns
    • Cech T. R., Damberger S. H., Gutell R. R. Representation of the secondary and tertiary structure of group I introns. Nature. Struct. Biol. 1:1994;273-280.
    • (1994) Nature. Struct. Biol. , vol.1 , pp. 273-280
    • Cech, T.R.1    Damberger, S.H.2    Gutell, R.R.3
  • 17
    • 0025023607 scopus 로고
    • Iron(II)-ethylenediaminetraacetic acid catalyzed cleavage of RNA and DNA oligonucleotides: Similar reactivity toward single- and double-stranded forms
    • Celander D. C., Cech T. R. Iron(II)-ethylenediaminetraacetic acid catalyzed cleavage of RNA and DNA oligonucleotides: similar reactivity toward single- and double-stranded forms. Biochemistry. 29:1990;1355-1361.
    • (1990) Biochemistry , vol.29 , pp. 1355-1361
    • Celander, D.C.1    Cech, T.R.2
  • 18
    • 0025963132 scopus 로고
    • Visualizing the higher order folding of a catalytic RNA molecule
    • Celander D. C., Cech T. R. Visualizing the higher order folding of a catalytic RNA molecule. Science. 251:1991;401-407.
    • (1991) Science , vol.251 , pp. 401-407
    • Celander, D.C.1    Cech, T.R.2
  • 19
    • 0027049570 scopus 로고
    • Analysis of the role of phosphate oxygens in the group I intron from Tetrahymena
    • Christian E. L., Yarus M. Analysis of the role of phosphate oxygens in the group I intron from Tetrahymena. J. Mol. Biol. 228:1992;743-758.
    • (1992) J. Mol. Biol. , vol.228 , pp. 743-758
    • Christian, E.L.1    Yarus, M.2
  • 20
    • 0027247579 scopus 로고
    • Metal coordination sites that contribute to structure and catalysis in the group I intron fromTetrahymena
    • Christian E. L., Yarus M. Metal coordination sites that contribute to structure and catalysis in the group I intron fromTetrahymena. Biochemistry. 32:1993;4475-4480.
    • (1993) Biochemistry , vol.32 , pp. 4475-4480
    • Christian, E.L.1    Yarus, M.2
  • 21
    • 0016169138 scopus 로고
    • The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNA
    • Crothers D. M., Cole P. E., Hilbers C. W., Shulman R. G. The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNA. J. Mol. Biol. 87:1974;63-88.
    • (1974) J. Mol. Biol. , vol.87 , pp. 63-88
    • Crothers, D.M.1    Cole, P.E.2    Hilbers, C.W.3    Shulman, R.G.4
  • 24
    • 0022461871 scopus 로고
    • Characterization of free radical-induced base damage in DNA at biologically relevant levels
    • Dizdaroglu M., Bergtold D. S. Characterization of free radical-induced base damage in DNA at biologically relevant levels. Anal. Biochem. 156:1986;182-188.
    • (1986) Anal. Biochem. , vol.156 , pp. 182-188
    • Dizdaroglu, M.1    Bergtold, D.S.2
  • 25
    • 0029258956 scopus 로고
    • Self-assembly of a group I intron active site from its component tertiary structural domains
    • Doudna J. A., Cech T. R. Self-assembly of a group I intron active site from its component tertiary structural domains. RNA. 1:1995;36-45.
    • (1995) RNA , vol.1 , pp. 36-45
    • Doudna, J.A.1    Cech, T.R.2
  • 26
    • 0021823854 scopus 로고
    • Sites of gamma radiation-induced DNA strand breaks after alkali treatment
    • Duplaa A. M., Teoule R. Sites of gamma radiation-induced DNA strand breaks after alkali treatment. Int. J. Radiat. Biol. 48:1985;19-32.
    • (1985) Int. J. Radiat. Biol. , vol.48 , pp. 19-32
    • Duplaa, A.M.1    Teoule, R.2
  • 27
    • 0018138536 scopus 로고
    • Sequence of the lacI gene
    • Farabaugh P. J. Sequence of the lacI gene. Nature. 274:1978;765-769.
    • (1978) Nature , vol.274 , pp. 765-769
    • Farabaugh, P.J.1
  • 29
    • 0024432780 scopus 로고
    • A conserved base-pair within the helix P4 of the Tetrahymena ribozyme helps to form the tertiary structure required for self-splicing
    • Flor P. J., Flanegan J. B., Cech T. R. A conserved base-pair within the helix P4 of the Tetrahymena ribozyme helps to form the tertiary structure required for self-splicing. EMBO J. 8:1989;3391-3399.
    • (1989) EMBO J. , vol.8 , pp. 3391-3399
    • Flor, P.J.1    Flanegan, J.B.2    Cech, T.R.3
  • 31
    • 0018199224 scopus 로고
    • DNase footprinting: A simple method for the detection of protein-DNA binding specificity
    • Galas D., Schmitz A. DNase footprinting: a simple method for the detection of protein-DNA binding specificity. Nucl. Acids Res. 5:1978;3157-3170.
    • (1978) Nucl. Acids Res. , vol.5 , pp. 3157-3170
    • Galas, D.1    Schmitz, A.2
  • 32
    • 0024976556 scopus 로고
    • Metal-ion requirements for sequence-specific endoribonuclease activity of the Tetrahymena ribozyme
    • Grosshans C. A., Cech T. R. Metal-ion requirements for sequence-specific endoribonuclease activity of the Tetrahymena ribozyme. Biochemistry. 28:1989;6888-6894.
    • (1989) Biochemistry , vol.28 , pp. 6888-6894
    • Grosshans, C.A.1    Cech, T.R.2
  • 33
    • 0026498015 scopus 로고
    • Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. Possible thermodynamic origins of the "glutamate effect" on protein-DNA interactions
    • Ha J. H., Capp M. W., Hohenwalter M. D., Baskerville M., Record M. T. Jr. Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. Possible thermodynamic origins of the "glutamate effect" on protein-DNA interactions. J. Mol. Biol. 228:1992;252-264.
    • (1992) J. Mol. Biol. , vol.228 , pp. 252-264
    • Ha, J.H.1    Capp, M.W.2    Hohenwalter, M.D.3    Baskerville, M.4    Record M.T., Jr.5
  • 34
    • 0025035281 scopus 로고
    • Footprinting protein-DNA complexes with gamma-rays
    • Hayes J. J., Kam L., Tullius T. D. Footprinting protein-DNA complexes with gamma-rays. Methods Enzymol. 186:1990;545-549.
    • (1990) Methods Enzymol. , vol.186 , pp. 545-549
    • Hayes, J.J.1    Kam, L.2    Tullius, T.D.3
  • 35
    • 0026338178 scopus 로고
    • Folding of group I introns from bacteriophage T4 involves internalization of the catalytic core
    • Heuer T. S., Chandry P. S., Belfort M., Celander D. W., Cech T. R. Folding of group I introns from bacteriophage T4 involves internalization of the catalytic core. Proc. Natl Acad. Sci. USA. 88:1991;11105-11109.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 11105-11109
    • Heuer, T.S.1    Chandry, P.S.2    Belfort, M.3    Celander, D.W.4    Cech, T.R.5
  • 36
    • 0001145764 scopus 로고
    • The combination of hemoglobin with oxygen and with carbon monoxide
    • Hill A. V. The combination of hemoglobin with oxygen and with carbon monoxide. Biochem. J. 7:1913;471-480.
    • (1913) Biochem. J. , vol.7 , pp. 471-480
    • Hill, A.V.1
  • 38
    • 0029806242 scopus 로고    scopus 로고
    • Quantitative kinetics footprinting of protein-DNA association reactions
    • Hsieh M., Brenowitz M. Quantitative kinetics footprinting of protein-DNA association reactions. Methods Enzymol. 274:1996;478-492.
    • (1996) Methods Enzymol. , vol.274 , pp. 478-492
    • Hsieh, M.1    Brenowitz, M.2
  • 39
    • 0028231061 scopus 로고
    • A molecular model of the inducer binding domain of the galactose repressor of Escherichia coli
    • Hsieh M., Hensley P., Brenowitz M., Fetrow J. S. A molecular model of the inducer binding domain of the galactose repressor of Escherichia coli. J. Biol. Chem. 269:1994;13825-13835.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13825-13835
    • Hsieh, M.1    Hensley, P.2    Brenowitz, M.3    Fetrow, J.S.4
  • 40
    • 0024967388 scopus 로고
    • Catalytic activity is retained in the Tetrahymena group I intron despite removal of the large extension of element P5
    • Joyce G. F., van der Horst G., Inoue T. Catalytic activity is retained in the Tetrahymena group I intron despite removal of the large extension of element P5. Nucl. Acids. Res. 17:1989;7879-7889.
    • (1989) Nucl. Acids. Res. , vol.17 , pp. 7879-7889
    • Joyce, G.F.1    Van Der Horst, G.2    Inoue, T.3
  • 41
    • 0026680555 scopus 로고
    • A stable solid that generates hydroxyl radical upon dissolution in aqueous solutions: Reaction with proteins and nucleic acid
    • King P. A., Anderson V. E., Edwards J. O., Gustafson G., Plumb R. C., Suggs J. W. A stable solid that generates hydroxyl radical upon dissolution in aqueous solutions: reaction with proteins and nucleic acid. J. Am. Chem. Soc. 114:1992;5430-5432.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5430-5432
    • King, P.A.1    Anderson, V.E.2    Edwards, J.O.3    Gustafson, G.4    Plumb, R.C.5    Suggs, J.W.6
  • 43
    • 0002193871 scopus 로고
    • Primary products in radiation chemistry
    • I. Farhatazis, & M.A. Rodgers. TX: VCH Pubs.
    • Klassen N. V. Primary products in radiation chemistry. Farhatazis I., Rodgers M. A. Radiation Chemistry Principles & Applications. 1987;VCH Pubs. TX.
    • (1987) Radiation Chemistry Principles & Applications
    • Klassen, N.V.1
  • 45
    • 0026769027 scopus 로고
    • Analysis of site-specific interaction parameters in protein-DNA complexes
    • Koblan K. S., Bain D. L., Beckett D., Shea M. A., Ackers G. K. Analysis of site-specific interaction parameters in protein-DNA complexes. Methods Enzymol. 210:1982;405-425.
    • (1982) Methods Enzymol. , vol.210 , pp. 405-425
    • Koblan, K.S.1    Bain, D.L.2    Beckett, D.3    Shea, M.A.4    Ackers, G.K.5
  • 46
    • 0028239266 scopus 로고
    • Two major tertiary folding transitions of the Tetrahymena catalytic RNA
    • Laggerbauer B., Murphy F. L., Cech T. R. Two major tertiary folding transitions of the Tetrahymena catalytic RNA. EMBO J. 13:1994;2699-2676.
    • (1994) EMBO J. , vol.13 , pp. 2699-2676
    • Laggerbauer, B.1    Murphy, F.L.2    Cech, T.R.3
  • 47
    • 0024359787 scopus 로고
    • Defining the inside and outside of a catalytic RNA molecule
    • Latham J. A., Cech T. R. Defining the inside and outside of a catalytic RNA molecule. Science. 245:1989;276-282.
    • (1989) Science , vol.245 , pp. 276-282
    • Latham, J.A.1    Cech, T.R.2
  • 49
    • 0025678737 scopus 로고
    • Modeling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis
    • Michel F., Westhof E. Modeling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis. J. Mol. Biol. 216:1990;585-610.
    • (1990) J. Mol. Biol. , vol.216 , pp. 585-610
    • Michel, F.1    Westhof, E.2
  • 50
    • 0025134897 scopus 로고
    • Phylogenetic and genetic evidence for base triples in the catalytic domain of group I introns
    • Michel F., Ellington A. D., Couture S., Szostak J. W. Phylogenetic and genetic evidence for base triples in the catalytic domain of group I introns. Nature. 347:1990;578-580.
    • (1990) Nature , vol.347 , pp. 578-580
    • Michel, F.1    Ellington, A.D.2    Couture, S.3    Szostak, J.W.4
  • 51
    • 0027173193 scopus 로고
    • An independently folding domain of RNA tertiary structure within the Tetrahymena ribozyme
    • Murphy F. L., Cech T. R. An independently folding domain of RNA tertiary structure within the Tetrahymena ribozyme. Biochemistry. 32:1993;5291-5300.
    • (1993) Biochemistry , vol.32 , pp. 5291-5300
    • Murphy, F.L.1    Cech, T.R.2
  • 52
    • 0028301674 scopus 로고
    • GAAA tetraloop and conserved bulge stabilize tertiary structure of a group I intron domain
    • Murphy F. L., Cech T. R. GAAA tetraloop and conserved bulge stabilize tertiary structure of a group I intron domain. J. Mol. Biol. 236:1994;49-63.
    • (1994) J. Mol. Biol. , vol.236 , pp. 49-63
    • Murphy, F.L.1    Cech, T.R.2
  • 53
    • 0027985820 scopus 로고
    • Coaxially stacked RNA helices in the catalytic center of the Tetrahymena ribozyme
    • Murphy F. L., Wang Y.-H., Griffith J. D., Cech T. R. Coaxially stacked RNA helices in the catalytic center of the Tetrahymena ribozyme. Science. 265:1994;1709-1712.
    • (1994) Science , vol.265 , pp. 1709-1712
    • Murphy, F.L.1    Wang, Y.-H.2    Griffith, J.D.3    Cech, T.R.4
  • 54
    • 0029080688 scopus 로고
    • Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter
    • Petri V., Hsieh M., Brenowitz M. Thermodynamic and kinetic characterization of the binding of the TATA binding protein to the adenovirus E4 promoter. Biochemistry. 34:1995;9977-9984.
    • (1995) Biochemistry , vol.34 , pp. 9977-9984
    • Petri, V.1    Hsieh, M.2    Brenowitz, M.3
  • 55
    • 0026807036 scopus 로고
    • Using hydroxyl radical to probe DNA structure
    • Price M. A., Tullius T. D. Using hydroxyl radical to probe DNA structure. Methods Enzymol. 212:1992;194-219.
    • (1992) Methods Enzymol. , vol.212 , pp. 194-219
    • Price, M.A.1    Tullius, T.D.2
  • 56
    • 0027389742 scopus 로고
    • How the structure of an adenine tract depends on sequence context: A new model for the structure of TnAn DNA sequences
    • Price M. A., Tullius T. D. How the structure of an adenine tract depends on sequence context: a new model for the structure of TnAn DNA sequences. Biochemistry. 32:1993;127-136.
    • (1993) Biochemistry , vol.32 , pp. 127-136
    • Price, M.A.1    Tullius, T.D.2
  • 57
    • 0026729278 scopus 로고
    • RNA substrate binding site in the catalytic core of the Tetrahymena ribozyme
    • Pyle A. M., Murphy F. L., Cech T. R. RNA substrate binding site in the catalytic core of the Tetrahymena ribozyme. Nature. 358:1992;123-128.
    • (1992) Nature , vol.358 , pp. 123-128
    • Pyle, A.M.1    Murphy, F.L.2    Cech, T.R.3
  • 59
    • 0018297601 scopus 로고
    • The interaction of RNA polymerase and lac repressor with the lac control region
    • Schmitz A., Galas D. The interaction of RNA polymerase and lac repressor with the lac control region. Nucl. Acids Res. 6:1979;111-137.
    • (1979) Nucl. Acids Res. , vol.6 , pp. 111-137
    • Schmitz, A.1    Galas, D.2
  • 60
    • 0028173030 scopus 로고
    • Crystal structure of LacI member PurR, bound to DNA: Minor groove binding by α helices
    • Schumacher M. A., Choi K. Y., Zalkin H., Brennen R. G. Crystal structure of LacI member PurR, bound to DNA: minor groove binding by α helices. Science. 266:1994;763-769.
    • (1994) Science , vol.266 , pp. 763-769
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennen, R.G.4
  • 61
    • 0011196407 scopus 로고
    • A new method for DNA footprinting by photolysis of methyl- and adenosyl-cobalamin bound to DNA
    • Sclavi B., Newman J., Chance M. R., Brenowitz M. A new method for DNA footprinting by photolysis of methyl- and adenosyl-cobalamin bound to DNA. Biophys. J. 66:1994;A155.
    • (1994) Biophys. J. , vol.66 , pp. 155
    • Sclavi, B.1    Newman, J.2    Chance, M.R.3    Brenowitz, M.4
  • 62
    • 0011197683 scopus 로고
    • New methods for time-resolved footprinting
    • Sclavi B., Chance M., Brenowitz M. New methods for time-resolved footprinting. Biophys. J. 68:1995;A296.
    • (1995) Biophys. J. , vol.68 , pp. 296
    • Sclavi, B.1    Chance, M.2    Brenowitz, M.3
  • 63
    • 0011244256 scopus 로고    scopus 로고
    • The application of synchrotron X-ray radiation to the development of time resolved methods for the study of RNA folding
    • Sclavi B., Woodson S., Sullivan M., Chance M., Brenowitz M. The application of synchrotron X-ray radiation to the development of time resolved methods for the study of RNA folding. Biophys. J. 70:1996;A443.
    • (1996) Biophys. J. , vol.70 , pp. 443
    • Sclavi, B.1    Woodson, S.2    Sullivan, M.3    Chance, M.4    Brenowitz, M.5
  • 64
    • 0026653485 scopus 로고
    • Simultaneous analysis for testing of models and parameter estimation
    • Senear D. F., Bolen D. W. Simultaneous analysis for testing of models and parameter estimation. Methods Enzymol. 210:1992;463-481.
    • (1992) Methods Enzymol. , vol.210 , pp. 463-481
    • Senear, D.F.1    Bolen, D.W.2
  • 66
    • 0017144014 scopus 로고
    • Phosphate ester cleavage in ribose-5-phosphate induced by OH radicals in deoxygenated aqueous solution. The effect of Fe(II) and Fe(III) ions
    • Stelter L., Von Sonntag C., Schulte-Frohlinde D. Phosphate ester cleavage in ribose-5-phosphate induced by OH radicals in deoxygenated aqueous solution. The effect of Fe(II) and Fe(III) ions. Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 29:1976;255-269.
    • (1976) Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. , vol.29 , pp. 255-269
    • Stelter, L.1    Von Sonntag, C.2    Schulte-Frohlinde, D.3
  • 67
    • 0027997554 scopus 로고
    • Correlation of DNA conformational changes with the cooperative binding of cI-repressor of bacteriophage λ
    • Strahs D., Brenowitz M. Correlation of DNA conformational changes with the cooperative binding of cI-repressor of bacteriophage λ J. Mol. Biol. 244:1994;494-510.
    • (1994) J. Mol. Biol. , vol.244 , pp. 494-510
    • Strahs, D.1    Brenowitz, M.2
  • 69
    • 0001268975 scopus 로고
    • Hydroxyl radical footprinting: High-resolution information about DNA-protein contacts and application to λ repressor and Cro protein
    • Tullius T. D., Dombroski B. A. Hydroxyl radical footprinting: high-resolution information about DNA-protein contacts and application to λ repressor and Cro protein. Proc. Natl Acad. Sci. USA. 83:1986;5469-5473.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 5469-5473
    • Tullius, T.D.1    Dombroski, B.A.2
  • 70
    • 0023623752 scopus 로고
    • Hydroxyl radical footprinting: A high resolution method for mapping protein-DNA contacts
    • Tullius T. D., Dombroski B. A., Churchill M. E., Kam L. Hydroxyl radical footprinting: a high resolution method for mapping protein-DNA contacts. Methods Enzymol. 155:1987;537-558.
    • (1987) Methods Enzymol. , vol.155 , pp. 537-558
    • Tullius, T.D.1    Dombroski, B.A.2    Churchill, M.E.3    Kam, L.4
  • 71
    • 0026017131 scopus 로고
    • Reconstitution of a group I intron self-splicing reaction with an activator RNA
    • van der Horst G., Christian A., Inoue T. Reconstitution of a group I intron self-splicing reaction with an activator RNA. Proc. Natl Acad. Sci. USA. 88:1991;184-188.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 184-188
    • Van Der Horst, G.1    Christian, A.2    Inoue, T.3
  • 73
    • 0017530102 scopus 로고
    • The reaction of OH radicals with D-ribose in deoxygenated and oxygenated aqueous solution
    • von Sonntag C., Dizdaroglu M. The reaction of OH radicals with D-ribose in deoxygenated and oxygenated aqueous solution. Carbohydr. Res. 58:1977;21-30.
    • (1977) Carbohydr. Res. , vol.58 , pp. 21-30
    • Von Sonntag, C.1    Dizdaroglu, M.2
  • 74
    • 0017921516 scopus 로고
    • Radiation-induced degradation of the sugar in model compounds and in DNA
    • von Sonntag C., Schulte-Frohlinde D. Radiation-induced degradation of the sugar in model compounds and in DNA. Mol. Biol. Biochem. Biophys. 27:1978;204-226.
    • (1978) Mol. Biol. Biochem. Biophys , vol.27 , pp. 204-226
    • Von Sonntag, C.1    Schulte-Frohlinde, D.2
  • 75
    • 0026517751 scopus 로고
    • Tertiary structure around the guanosine-binding site of the Tetrahymena ribozyme
    • Wang J.-F., Cech T. R. Tertiary structure around the guanosine-binding site of the Tetrahymena ribozyme. Science. 256:1992;526-529.
    • (1992) Science , vol.256 , pp. 526-529
    • Wang, J.-F.1    Cech, T.R.2
  • 76
    • 0028105774 scopus 로고
    • Metal ion dependence of active-site structure of the Tetrahymena ribozyme revealed by site-specific photo-cross-linking
    • Wang J.-F., Cech T. R. Metal ion dependence of active-site structure of the Tetrahymena ribozyme revealed by site-specific photo-cross-linking. J. Am. Chem. Soc. 116:1994;4178-4182.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4178-4182
    • Wang, J.-F.1    Cech, T.R.2
  • 77
    • 0026724966 scopus 로고
    • A family of bacterial regulators homologous to gal and lac repressors
    • Weickert M. J., Adhya S. A family of bacterial regulators homologous to gal and lac repressors. J. Biol. Chem. 267:1992;15869-15874.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15869-15874
    • Weickert, M.J.1    Adhya, S.2
  • 78
    • 0027991626 scopus 로고
    • Kinetic intermediates in RNA folding
    • Zarrinkar P. P., Williamson J. R. Kinetic intermediates in RNA folding. Science. 265:1994;918-924.
    • (1994) Science , vol.265 , pp. 918-924
    • Zarrinkar, P.P.1    Williamson, J.R.2
  • 79
    • 0029874598 scopus 로고    scopus 로고
    • The kinetic folding pathway of the Tetrahymena ribozyme reveals possible similarities between RNA and protein folding
    • Zarrinkar P. P., Williamson J. R. The kinetic folding pathway of the Tetrahymena ribozyme reveals possible similarities between RNA and protein folding. Nature Struct. Biol. 3:1996a;432-438.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 432-438
    • Zarrinkar, P.P.1    Williamson, J.R.2
  • 80
    • 0029864990 scopus 로고    scopus 로고
    • The P9.1-P9.2 peripheral extension helps guide folding of the Tetrahymena ribozyme
    • Zarrinkar P. P., Williamson J. R. The P9.1-P9.2 peripheral extension helps guide folding of the Tetrahymena ribozyme. Nucl. Acids Res. 24:1996b;854-858.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 854-858
    • Zarrinkar, P.P.1    Williamson, J.R.2
  • 81
    • 0024285808 scopus 로고
    • Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: Enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes
    • Zaug A. J., Grosshans C. A., Cech T. R. Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes. Biochemistry. 27:1988;8924-8931.
    • (1988) Biochemistry , vol.27 , pp. 8924-8931
    • Zaug, A.J.1    Grosshans, C.A.2    Cech, T.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.