메뉴 건너뛰기




Volumn 340, Issue 2, 2004, Pages 233-251

Role of an active site guanine in hairpin ribozyme catalysis probed by exogenous nucleobase rescue

Author keywords

catalytic mechanism; electrostatic stabilization; general acid base catalysis; hairpin ribozyme; HDV, hepatitis delta virus; NB, nucleobase; RNA catalysis; VS, Varkud satellite

Indexed keywords

ACID; CYTOSINE; GUANINE; NUCLEIC ACID BASE; RIBOZYME;

EID: 2942577491     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.067     Document Type: Article
Times cited : (85)

References (63)
  • 1
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction methods
    • Noller H.F., Hoffarth V., Zimniak L. Unusual resistance of peptidyl transferase to protein extraction methods. Science. 256:1992;1416-1419
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 2
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P., Hansen J., Ban N., Moore P., Steitz T. The structural basis of ribosome activity in peptide bond synthesis. Science. 289:2000;920-930
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.4    Steitz, T.5
  • 4
    • 0034708334 scopus 로고    scopus 로고
    • Structure and function of the hairpin ribozyme
    • Fedor M.J. Structure and function of the hairpin ribozyme. J. Mol. Biol. 297:2000;269-291
    • (2000) J. Mol. Biol. , vol.297 , pp. 269-291
    • Fedor, M.J.1
  • 5
    • 1642580826 scopus 로고    scopus 로고
    • The Varkud satellite ribozyme
    • Lilley D.M. The Varkud satellite ribozyme. RNA. 10:2004;151-158
    • (2004) RNA , vol.10 , pp. 151-158
    • Lilley, D.M.1
  • 6
    • 0035997396 scopus 로고    scopus 로고
    • Catalytic strategies of the hepatitis delta virus ribozymes
    • Shih I.H., Been M.D. Catalytic strategies of the hepatitis delta virus ribozymes. Annu. Rev. Biochem. 71:2002;887-917
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 887-917
    • Shih, I.H.1    Been, M.D.2
  • 7
    • 0032497521 scopus 로고    scopus 로고
    • Crystal structure of a hepatitis delta virus ribozyme
    • Ferré-D'Amaré A.R., Zhou K., Doudna J.A. Crystal structure of a hepatitis delta virus ribozyme. Nature. 395:1998;567-574
    • (1998) Nature , vol.395 , pp. 567-574
    • Ferré-D'Amaré, A.R.1    Zhou, K.2    Doudna, J.A.3
  • 8
    • 0035848837 scopus 로고    scopus 로고
    • Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis
    • Rupert P.B., Ferré-D'Amaré A.R. Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis. Nature. 410:2001;780-786
    • (2001) Nature , vol.410 , pp. 780-786
    • Rupert, P.B.1    Ferré-D'Amaré, A.R.2
  • 10
    • 0036753229 scopus 로고    scopus 로고
    • Two decades of RNA catalysis
    • DeRose V. Two decades of RNA catalysis. Chem. Biol. 9:2002;961-969
    • (2002) Chem. Biol. , vol.9 , pp. 961-969
    • Derose, V.1
  • 11
    • 0036601149 scopus 로고    scopus 로고
    • The role of metal ions in RNA catalysis
    • Fedor M.J. The role of metal ions in RNA catalysis. Curr. Opin. Struct. Biol. 12:2002;289-295
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 289-295
    • Fedor, M.J.1
  • 13
    • 0037418547 scopus 로고    scopus 로고
    • Mechanistic considerations for general acid-base catalysis by RNA: Revisiting the mechanism of the hairpin ribozyme
    • Bevilacqua P.C. Mechanistic considerations for general acid-base catalysis by RNA: revisiting the mechanism of the hairpin ribozyme. Biochemistry. 42:2003;2259-2265
    • (2003) Biochemistry , vol.42 , pp. 2259-2265
    • Bevilacqua, P.C.1
  • 14
    • 0347763707 scopus 로고    scopus 로고
    • Catalytic roles for proton transfer and protonation in ribozymes
    • Bevilacqua P.C., Brown T.S., Nakano S., Yajima R. Catalytic roles for proton transfer and protonation in ribozymes. Biopolymers. 73:2004;90-109
    • (2004) Biopolymers , vol.73 , pp. 90-109
    • Bevilacqua, P.C.1    Brown, T.S.2    Nakano, S.3    Yajima, R.4
  • 15
    • 0023055382 scopus 로고
    • Nucleotide sequence and newly formed phosphodiester bond of spontaneously ligated satellite tobacco ringspot virus RNA
    • Buzayan J.M., Hampel A., Bruening G. Nucleotide sequence and newly formed phosphodiester bond of spontaneously ligated satellite tobacco ringspot virus RNA. Nucl. Acids Res. 14:1986;9729-9743
    • (1986) Nucl. Acids Res. , vol.14 , pp. 9729-9743
    • Buzayan, J.M.1    Hampel, A.2    Bruening, G.3
  • 17
    • 0025335881 scopus 로고
    • Two autolytic processing reactions of a satellite RNA proceed with inversion of configuration
    • van Tol H., Buzayan J.M., Feldstein P.A., Eckstein F., Bruening G. Two autolytic processing reactions of a satellite RNA proceed with inversion of configuration. Nucl. Acids Res. 18:1990;1971-1975
    • (1990) Nucl. Acids Res. , vol.18 , pp. 1971-1975
    • Van Tol, H.1    Buzayan, J.M.2    Feldstein, P.A.3    Eckstein, F.4    Bruening, G.5
  • 18
    • 0031215134 scopus 로고    scopus 로고
    • An unusual pH-independent and metal-ion-independent mechanism for hairpin ribozyme catalysis
    • Nesbitt S., Hegg L.A., Fedor M.J. An unusual pH-independent and metal-ion-independent mechanism for hairpin ribozyme catalysis. Chem. Biol. 4:1997;619-630
    • (1997) Chem. Biol. , vol.4 , pp. 619-630
    • Nesbitt, S.1    Hegg, L.A.2    Fedor, M.J.3
  • 19
    • 0031194873 scopus 로고    scopus 로고
    • A unique mechanism for RNA catalysis: The role of metal cofactors in hairpin ribozyme cleavage
    • Hampel A., Cowan J.A. A unique mechanism for RNA catalysis: the role of metal cofactors in hairpin ribozyme cleavage. Chem. Biol. 4:1997;513-517
    • (1997) Chem. Biol. , vol.4 , pp. 513-517
    • Hampel, A.1    Cowan, J.A.2
  • 20
    • 0030967825 scopus 로고    scopus 로고
    • Metal ions play a passive role in the hairpin ribozyme catalysed reaction
    • Young K.J., Gill F., Grasby J.A. Metal ions play a passive role in the hairpin ribozyme catalysed reaction. Nucl. Acids Res. 25:1997;3760-3766
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3760-3766
    • Young, K.J.1    Gill, F.2    Grasby, J.A.3
  • 21
    • 0032192761 scopus 로고    scopus 로고
    • The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone
    • Murray J.B., Seyhan A.A., Walter N.G., Burke J.M., Scott W.G. The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone. Chem. Biol. 5:1998;587-595
    • (1998) Chem. Biol. , vol.5 , pp. 587-595
    • Murray, J.B.1    Seyhan, A.A.2    Walter, N.G.3    Burke, J.M.4    Scott, W.G.5
  • 23
    • 0037016023 scopus 로고    scopus 로고
    • Energetics of hydrogen bond networks in RNA: Hydrogen bonds surrounding G+1 and U42 are the major determinants for the tertiary structure stability of the hairpin ribozyme
    • Klostermeier D., Millar D.P. Energetics of hydrogen bond networks in RNA: hydrogen bonds surrounding G+1 and U42 are the major determinants for the tertiary structure stability of the hairpin ribozyme. Biochemistry. 41:2002;14095-14102
    • (2002) Biochemistry , vol.41 , pp. 14095-14102
    • Klostermeier, D.1    Millar, D.P.2
  • 24
    • 0036237379 scopus 로고    scopus 로고
    • Rescue of an abasic hairpin ribozyme by cationic nucleobases. Evidence for a novel mechanism of RNA catalysis
    • Lebruska L.L., Kuzmine I.I., Fedor M.J. Rescue of an abasic hairpin ribozyme by cationic nucleobases. Evidence for a novel mechanism of RNA catalysis. Chem. Biol. 9:2002;465-473
    • (2002) Chem. Biol. , vol.9 , pp. 465-473
    • Lebruska, L.L.1    Kuzmine, I.I.2    Fedor, M.J.3
  • 26
    • 0036863323 scopus 로고    scopus 로고
    • The hairpin ribozyme: From crystal structure to function
    • Ferré-D'Amaré A.R., Rupert P.B. The hairpin ribozyme: from crystal structure to function. Biochem. Soc. Trans. 30:2001;1105-1109
    • (2001) Biochem. Soc. Trans. , vol.30 , pp. 1105-1109
    • Ferré-D'Amaré, A.R.1    Rupert, P.B.2
  • 27
    • 0014519165 scopus 로고
    • Kinetic and equilibrium studies of the ribonuclease-catalyzed hydrolysis of uridine 2′,3′-cyclic phosphate
    • del Rosario E.J., Hammes G.G. Kinetic and equilibrium studies of the ribonuclease-catalyzed hydrolysis of uridine 2′, 3′-cyclic phosphate. Biochemistry. 8:1969;1884-1889
    • (1969) Biochemistry , vol.8 , pp. 1884-1889
    • Del Rosario, E.J.1    Hammes, G.G.2
  • 28
    • 0017018406 scopus 로고
    • a-values of functional groups in enzymes: Improper deductions from the pH-dependence of steady-state parameters
    • a-values of functional groups in enzymes: improper deductions from the pH-dependence of steady-state parameters. CRC Crit. Rev. Biochem. 4:1976;165-173
    • (1976) CRC Crit. Rev. Biochem. , vol.4 , pp. 165-173
    • Knowles, J.R.1
  • 29
    • 0034712097 scopus 로고    scopus 로고
    • General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme
    • Nakano S., Chadalavada D., Bevilacqua P. General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme. Science. 287:2000;1493-1497
    • (2000) Science , vol.287 , pp. 1493-1497
    • Nakano, S.1    Chadalavada, D.2    Bevilacqua, P.3
  • 30
    • 0035793217 scopus 로고    scopus 로고
    • A pH-sensitive RNA tertiary interaction affects self-cleavage activity of the HDV ribozymes in the absence of added divalent metal ion
    • Wadkins T.S., Shih I., Perrotta A.T., Been M.D. A pH-sensitive RNA tertiary interaction affects self-cleavage activity of the HDV ribozymes in the absence of added divalent metal ion. J. Mol. Biol. 305:2001;1045-1055
    • (2001) J. Mol. Biol. , vol.305 , pp. 1045-1055
    • Wadkins, T.S.1    Shih, I.2    Perrotta, A.T.3    Been, M.D.4
  • 31
    • 0034757632 scopus 로고    scopus 로고
    • Investigation of adenosine base ionization in the hairpin ribozyme by nucleotide analog interference mapping
    • Ryder S.P., Oyelere A.K., Padilla J.L., Klostermeier D., Millar D.P., Strobel S.A. Investigation of adenosine base ionization in the hairpin ribozyme by nucleotide analog interference mapping. RNA. 7:2001;1454-1463
    • (2001) RNA , vol.7 , pp. 1454-1463
    • Ryder, S.P.1    Oyelere, A.K.2    Padilla, J.L.3    Klostermeier, D.4    Millar, D.P.5    Strobel, S.A.6
  • 32
    • 0024478059 scopus 로고
    • Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
    • Toney M., Kirsch J. Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science. 243:1989;485-488
    • (1989) Science , vol.243 , pp. 485-488
    • Toney, M.1    Kirsch, J.2
  • 33
    • 0027008407 scopus 로고
    • Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant
    • Toney M., Kirsch J. Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant. Protein Sci. 1:1992;107-119
    • (1992) Protein Sci. , vol.1 , pp. 107-119
    • Toney, M.1    Kirsch, J.2
  • 34
    • 0033215448 scopus 로고    scopus 로고
    • Imidazole rescue of a cytosine mutation in a self-cleaving ribozyme
    • Perrotta A.T., Shih I., Been M.D. Imidazole rescue of a cytosine mutation in a self-cleaving ribozyme. Science. 286:1999;123-126
    • (1999) Science , vol.286 , pp. 123-126
    • Perrotta, A.T.1    Shih, I.2    Been, M.D.3
  • 35
    • 0035852640 scopus 로고    scopus 로고
    • Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage
    • Shih I.H., Been M.D. Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage. Proc. Natl Acad. Sci. USA. 98:2001;1489-1494
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1489-1494
    • Shih, I.H.1    Been, M.D.2
  • 36
    • 0032552962 scopus 로고    scopus 로고
    • A core folding model for catalysis by the hammerhead ribozyme accounts for its extraordinary sensitivity to abasic mutations
    • Peracchi A., Karpeisky A., Maloney L., Beigelman L., Herschlag D. A core folding model for catalysis by the hammerhead ribozyme accounts for its extraordinary sensitivity to abasic mutations. Biochemistry. 37:1998;14765-14775
    • (1998) Biochemistry , vol.37 , pp. 14765-14775
    • Peracchi, A.1    Karpeisky, A.2    Maloney, L.3    Beigelman, L.4    Herschlag, D.5
  • 37
    • 0029859191 scopus 로고    scopus 로고
    • Rescue of abasic hammerhead ribozymes by exogenous addition of specific bases
    • Peracchi A., Beigelman L., Usman N., Herschlag D. Rescue of abasic hammerhead ribozymes by exogenous addition of specific bases. Proc. Natl Acad. Sci. USA. 93:1996;11522-11527
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11522-11527
    • Peracchi, A.1    Beigelman, L.2    Usman, N.3    Herschlag, D.4
  • 38
    • 0031758565 scopus 로고    scopus 로고
    • Structure-function relationships in the hammerhead ribozyme probed by base rescue
    • Peracchi A., Matulic-Adamic J., Wang S., Beigelman L., Herschlag D. Structure-function relationships in the hammerhead ribozyme probed by base rescue. RNA. 4:1998;1332-1346
    • (1998) RNA , vol.4 , pp. 1332-1346
    • Peracchi, A.1    Matulic-Adamic, J.2    Wang, S.3    Beigelman, L.4    Herschlag, D.5
  • 39
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease a
    • Raines R.T. Ribonuclease A. Chem. Rev. 98:1998;1045-1066
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 40
    • 0033600553 scopus 로고    scopus 로고
    • Tertiary structure stabilization promotes hairpin ribozyme ligation
    • Fedor M.J. Tertiary structure stabilization promotes hairpin ribozyme ligation. Biochemistry. 38:1999;11040-11050
    • (1999) Biochemistry , vol.38 , pp. 11040-11050
    • Fedor, M.J.1
  • 41
    • 0033525467 scopus 로고    scopus 로고
    • The internal equilibrium of the hairpin ribozyme: Temperature, ion and pH effects
    • Nesbitt S.M., Erlacher H.A., Fedor M.J. The internal equilibrium of the hairpin ribozyme: temperature, ion and pH effects. J. Mol. Biol. 286:1999;1009-1024
    • (1999) J. Mol. Biol. , vol.286 , pp. 1009-1024
    • Nesbitt, S.M.1    Erlacher, H.A.2    Fedor, M.J.3
  • 42
    • 0028837570 scopus 로고
    • Kinetics and thermodynamics of intermolecular catalysis by hairpin ribozymes
    • Hegg L.A., Fedor M.J. Kinetics and thermodynamics of intermolecular catalysis by hairpin ribozymes. Biochemistry. 34:1995;15813-15828
    • (1995) Biochemistry , vol.34 , pp. 15813-15828
    • Hegg, L.A.1    Fedor, M.J.2
  • 43
    • 0000375053 scopus 로고
    • Concerning the relationship between the strength of acids and their capacity to preserve neutrality
    • Henderson L. Concerning the relationship between the strength of acids and their capacity to preserve neutrality. Am. J. Physiol. 21:1908;173-179
    • (1908) Am. J. Physiol. , vol.21 , pp. 173-179
    • Henderson, L.1
  • 44
    • 0034695408 scopus 로고    scopus 로고
    • The kinetic mechanism of the hairpin ribozyme in vivo: Influence of RNA helix stability on intracellular cleavage kinetics
    • Donahue C.P., Yadava R.S., Nesbitt S.M., Fedor M.J. The kinetic mechanism of the hairpin ribozyme in vivo: influence of RNA helix stability on intracellular cleavage kinetics. J. Mol. Biol. 295:2000;693-707
    • (2000) J. Mol. Biol. , vol.295 , pp. 693-707
    • Donahue, C.P.1    Yadava, R.S.2    Nesbitt, S.M.3    Fedor, M.J.4
  • 45
    • 0027153328 scopus 로고
    • Essential nucleotide sequences and secondary structure elements of the hairpin ribozyme
    • Berzal-Herranz A., Joseph S., Chowrira B.M., Butcher S.E., Burke J.M. Essential nucleotide sequences and secondary structure elements of the hairpin ribozyme. EMBO J. 12:1993;2567-2573
    • (1993) EMBO J. , vol.12 , pp. 2567-2573
    • Berzal-Herranz, A.1    Joseph, S.2    Chowrira, B.M.3    Butcher, S.E.4    Burke, J.M.5
  • 47
    • 0035916297 scopus 로고    scopus 로고
    • Importance of specific nucleotides in the folding of the natural form of the hairpin ribozyme
    • Wilson T.J., Zhao Z.Y., Maxwell K., Kontogiannis L., Lilley D.M. Importance of specific nucleotides in the folding of the natural form of the hairpin ribozyme. Biochemistry. 40:2001;2291-2302
    • (2001) Biochemistry , vol.40 , pp. 2291-2302
    • Wilson, T.J.1    Zhao, Z.Y.2    Maxwell, K.3    Kontogiannis, L.4    Lilley, D.M.5
  • 48
    • 0032832835 scopus 로고    scopus 로고
    • On the metal-ion-coordinating properties of the benzimidazolate residue in aqueous solution-extent of acidification of benzimidazole-(N3)H sites by (N1)-coordinated divalent metal ions
    • Kapinos L.E., Sigel H. On the metal-ion-coordinating properties of the benzimidazolate residue in aqueous solution-extent of acidification of benzimidazole-(N3)H sites by (N1)-coordinated divalent metal ions. Eur. J. Inorg. Chem. 1999;1781-1786
    • (1999) Eur. J. Inorg. Chem. , pp. 1781-1786
    • Kapinos, L.E.1    Sigel, H.2
  • 49
    • 0036019716 scopus 로고    scopus 로고
    • Comparison of the acid-base properties of purine derivatives in aqueous solution. Determination of intrinsic proton affinities of various basic sites
    • Kampf G., Kapinos L.E., Griesser R., Lippert B., Sigel H. Comparison of the acid-base properties of purine derivatives in aqueous solution. Determination of intrinsic proton affinities of various basic sites. J. Am. Chem. Soc. Perkins Trans. 2. 2002;1320-1327
    • (2002) J. Am. Chem. Soc. Perkins Trans. 2 , pp. 1320-1327
    • Kampf, G.1    Kapinos, L.E.2    Griesser, R.3    Lippert, B.4    Sigel, H.5
  • 50
    • 0035833978 scopus 로고    scopus 로고
    • Mechanistic characterization of the HDV genomic ribozyme: Assessing the catalytic and structural contributions of divalent metal ions within a multichannel reaction mechanism
    • Nakano S., Proctor D.J., Bevilacqua P.C. Mechanistic characterization of the HDV genomic ribozyme: assessing the catalytic and structural contributions of divalent metal ions within a multichannel reaction mechanism. Biochemistry. 40:2001;12022-12038
    • (2001) Biochemistry , vol.40 , pp. 12022-12038
    • Nakano, S.1    Proctor, D.J.2    Bevilacqua, P.C.3
  • 51
    • 0037452909 scopus 로고    scopus 로고
    • Mechanistic characterization of the HDV genomic ribozyme: Classifying the catalytic and structural metal ion sites within a multichannel reaction mechanism
    • Nakano S., Cerrone A.L., Bevilacqua P.C. Mechanistic characterization of the HDV genomic ribozyme: classifying the catalytic and structural metal ion sites within a multichannel reaction mechanism. Biochemistry. 42:2003;2982-2994
    • (2003) Biochemistry , vol.42 , pp. 2982-2994
    • Nakano, S.1    Cerrone, A.L.2    Bevilacqua, P.C.3
  • 52
    • 0024394458 scopus 로고
    • On the mechanism of catalysis by ribonuclease: Cleavage and isomerization of the dinucleotide UpU catalyzed by imidazole buffers
    • Anslyn E., Breslow R. On the mechanism of catalysis by ribonuclease: cleavage and isomerization of the dinucleotide UpU catalyzed by imidazole buffers. J. Am. Chem. Soc. 111:1989;4473-4482
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4473-4482
    • Anslyn, E.1    Breslow, R.2
  • 53
    • 0001036515 scopus 로고
    • The ionization and spectra of pyrimidines
    • chapt. 12. chapt. 12. E.G. Taylor. New York: Wiley
    • chapt. 12 Brown D.J. The ionization and spectra of pyrimidines. chapt. 12 Taylor E.G. The Pyrimidines. The Pyrimidines. vol. 52:1994;823-853 Wiley, New York
    • (1994) The Pyrimidines the Pyrimidines , vol.52 , pp. 823-853
    • Brown, D.J.1
  • 54
    • 0036249718 scopus 로고    scopus 로고
    • Metal ion binding and the folding of the hairpin ribozyme
    • Wilson T.J., Lilley D.M. Metal ion binding and the folding of the hairpin ribozyme. RNA. 8:2002;587-600
    • (2002) RNA , vol.8 , pp. 587-600
    • Wilson, T.J.1    Lilley, D.M.2
  • 55
    • 0038713248 scopus 로고    scopus 로고
    • A thermodynamic framework for the magnesium-dependent folding of RNA
    • Misra V.K., Shiman R., Draper D.E. A thermodynamic framework for the magnesium-dependent folding of RNA. Biopolymers. 69:2003;118-136
    • (2003) Biopolymers , vol.69 , pp. 118-136
    • Misra, V.K.1    Shiman, R.2    Draper, D.E.3
  • 57
    • 33847090209 scopus 로고
    • Intramolecular nondissociative proton transfer in aqueous solutions of tautomeric heterocycles: A temperature jump kinetic study
    • Bensaude O., Dreyfus M., Dodin G., Dubois J.E. Intramolecular nondissociative proton transfer in aqueous solutions of tautomeric heterocycles: a temperature jump kinetic study. J. Am. Chem. Soc. 99:1977;4438-4446
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 4438-4446
    • Bensaude, O.1    Dreyfus, M.2    Dodin, G.3    Dubois, J.E.4
  • 58
    • 0017130640 scopus 로고
    • Tautomerism in cytosine and 3-methylcytosine. A thermodynamic and kinetic study
    • Dreyfus M., Bensaude O., Dodin G., Dubois J.E. Tautomerism in cytosine and 3-methylcytosine. A thermodynamic and kinetic study. J. Am. Chem. Soc. 98:1976;6338-6349
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 6338-6349
    • Dreyfus, M.1    Bensaude, O.2    Dodin, G.3    Dubois, J.E.4
  • 60
    • 0032552882 scopus 로고    scopus 로고
    • Thermodynamic parameters for an expanded nearest-neighbor model for formation of RNA duplexes with Watson-Crick base pairs
    • Xia T., SantaLucia J.J., Burkard M., Kierzek R., Schroeder S., Jiao X., et al. Thermodynamic parameters for an expanded nearest-neighbor model for formation of RNA duplexes with Watson-Crick base pairs. Biochemistry. 37:1998;14719-14735
    • (1998) Biochemistry , vol.37 , pp. 14719-14735
    • Xia, T.1    Santalucia, J.J.2    Burkard, M.3    Kierzek, R.4    Schroeder, S.5    Jiao, X.6
  • 61
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews D.H., Sabina J., Zuker M., Turner D.H. Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol. 288:1999;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
  • 63


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.