메뉴 건너뛰기




Volumn 9, Issue 8, 2003, Pages 907-918

Ribozyme speed limits

Author keywords

Catalysis; Deoxyribozyme; Enzymatic mechanism; Ribozyme; RNA cleavage; RNA transesterification

Indexed keywords

DEOXYRIBOZYME; ORGANOPHOSPHATE; RIBOZYME; RNA;

EID: 0041702195     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1261/rna.5680603     Document Type: Review
Times cited : (178)

References (68)
  • 2
    • 0029410712 scopus 로고
    • Mapping the transition state for ATP hydrolysis: Implications for enzymatic catalysis
    • Admiraal, S.J. and Herschlag, D. 1995. Mapping the transition state for ATP hydrolysis: Implications for enzymatic catalysis. Chem. Biol. 2: 729-739.
    • (1995) Chem. Biol. , vol.2 , pp. 729-739
    • Admiraal, S.J.1    Herschlag, D.2
  • 3
    • 0029788767 scopus 로고    scopus 로고
    • Base catalysis and leaving group dependence in intramolecular alcoholysis of uridine 3′-(aryl phosphorothioate)s
    • Almer, H. and Strömberg, R. 1996. Base catalysis and leaving group dependence in intramolecular alcoholysis of uridine 3′-(aryl phosphorothioate)s. J. Am. Chem. Soc. 118: 7921-7928.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7921-7928
    • Almer, H.1    Strömberg, R.2
  • 4
    • 0041751850 scopus 로고
    • The kinetics of hydrolysis of ribonucleic acid
    • Bacher, J.E. and Kauzmann, W. 1952. The kinetics of hydrolysis of ribonucleic acid. J. Am. Chem. Soc. 74: 3779-3786.
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 3779-3786
    • Bacher, J.E.1    Kauzmann, W.2
  • 5
    • 77956945325 scopus 로고
    • Chemical basis of biological phosphoryl transfer
    • (ed. P.D. Boyer), Academic Press, New York
    • Benkovic, S.J. and Schray, K.J. 1970. Chemical basis of biological phosphoryl transfer. In The enzymes, 3rd ed., Vol. VIII (ed. P.D. Boyer), pp. 201-238, Academic Press, New York.
    • (1970) The Enzymes, 3rd Ed. , vol.8 , pp. 201-238
    • Benkovic, S.J.1    Schray, K.J.2
  • 6
    • 0000917638 scopus 로고    scopus 로고
    • In vitro selection of catalytic polynucleotides
    • Breaker, R.R. 1997. In vitro selection of catalytic polynucleotides. Chem. Rev. 97: 371-390.
    • (1997) Chem. Rev. , vol.97 , pp. 371-390
    • Breaker, R.R.1
  • 8
    • 12044259685 scopus 로고
    • How do imidazole groups catalyze the cleavage of RNA in enzyme models and in enzymes? Evidence from "negative catalysis"
    • Breslow, R. 1991. How do imidazole groups catalyze the cleavage of RNA in enzyme models and in enzymes? Evidence from "negative catalysis." Acc. Chem. Res. 24: 317-324.
    • (1991) Acc. Chem. Res. , vol.24 , pp. 317-324
    • Breslow, R.1
  • 9
    • 0006963422 scopus 로고
    • Nucleotides. Part X. Some observations on the structure and chemical behaviour of the nucleic acids
    • Brown, D.M. and Todd, A.R. 1952. Nucleotides. Part X. Some observations on the structure and chemical behaviour of the nucleic acids. J. Chem. Soc. 52-58.
    • (1952) J. Chem. Soc. , pp. 52-58
    • Brown, D.M.1    Todd, A.R.2
  • 10
    • 85088606076 scopus 로고
    • The action of ribonuclease on simple esters of the monoribonucleotides
    • -. 1953. The action of ribonuclease on simple esters of the monoribonucleotides. J. Chem. Soc. 2040-2049.
    • (1953) J. Chem. Soc. , pp. 2040-2049
    • Brown, D.M.1
  • 11
    • 0001135385 scopus 로고
    • Hydrolysis of esters of monoribonucleotides
    • Brown, D.M., Magrath, D.I., Neilson, A.H., and Todd, A.R. 1956. Hydrolysis of esters of monoribonucleotides. Nature 177: 1124-1125.
    • (1956) Nature , vol.177 , pp. 1124-1125
    • Brown, D.M.1    Magrath, D.I.2    Neilson, A.H.3    Todd, A.R.4
  • 12
    • 0040362704 scopus 로고    scopus 로고
    • Chemical basis for enzyme catalysis
    • Bruice, T.C. and Benkovic, S.J. 2000. Chemical basis for enzyme catalysis. Biochemistry 39: 6267-6274.
    • (2000) Biochemistry , vol.39 , pp. 6267-6274
    • Bruice, T.C.1    Benkovic, S.J.2
  • 13
    • 0029861361 scopus 로고    scopus 로고
    • One- and two-metal ion catalysis of the hydrolysis of adenosine 3′-alkyl phosphate esters. Models for one- and two-metal ion catalysis of RNA hydrolysis
    • Bruice, T.C., Tsubouchi, A., Dempcy, R.O., and Olson, L.P. 1996. One- and two-metal ion catalysis of the hydrolysis of adenosine 3′-alkyl phosphate esters. Models for one- and two-metal ion catalysis of RNA hydrolysis. J. Am. Chem. Soc. 118: 9867-9875.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9867-9875
    • Bruice, T.C.1    Tsubouchi, A.2    Dempcy, R.O.3    Olson, L.P.4
  • 14
    • 0035367070 scopus 로고    scopus 로고
    • Structure and function of the small ribozymes
    • Butcher, S.E. 2001. Structure and function of the small ribozymes. Curr. Opin. Struct. Biol. 11: 315-320.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 315-320
    • Butcher, S.E.1
  • 15
    • 0029869856 scopus 로고    scopus 로고
    • Solution structure of loop A from the hairpin ribozyme from tobacco ringspot virus satellite
    • Cai, Z. and Tinoco Jr., I. 1996. Solution structure of loop A from the hairpin ribozyme from tobacco ringspot virus satellite. Biochemistry 35: 6026-6036.
    • (1996) Biochemistry , vol.35 , pp. 6026-6036
    • Cai, Z.1    Tinoco I., Jr.2
  • 18
    • 0034708334 scopus 로고    scopus 로고
    • Structure and function of the hairpin ribozyme
    • Fedor, M.J. 2000. Structure and function of the hairpin ribozyme. J. Mol. Biol. 297: 269-291.
    • (2000) J. Mol. Biol. , vol.297 , pp. 269-291
    • Fedor, M.J.1
  • 20
    • 0002455712 scopus 로고
    • Mechanistic principles of enzyme-catalyzed cleavage of phosphodiester bonds
    • (eds. S.M. Linn et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Gerlt, J.A. 1993. Mechanistic principles of enzyme-catalyzed cleavage of phosphodiester bonds. In Nucleases, 2nd ed. (eds. S.M. Linn et al.), pp. 1-34. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) Nucleases, 2nd Ed. , pp. 1-34
    • Gerlt, J.A.1
  • 21
    • 0000085698 scopus 로고
    • Hydration and dehydration of phosphoric acid derivatives: Free energies of formation of the pentacoordinate intermediates for phosphate ester hydrolysis and of monomeric metaphosphate
    • Guthrie, J.P. 1977. Hydration and dehydration of phosphoric acid derivatives: Free energies of formation of the pentacoordinate intermediates for phosphate ester hydrolysis and of monomeric metaphosphate. J. Am. Chem. Soc. 99: 3991-4001.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 3991-4001
    • Guthrie, J.P.1
  • 22
    • 0014022993 scopus 로고
    • Thermodynamics of proton dissociation in dilute aqueous solution, V. An entropy titration study of adenosine, pentoses, hexoses, and related compounds
    • Izatt, R.M., Rytting, J.H., Hansen, L.D., and Christensen, J.J. 1966. Thermodynamics of proton dissociation in dilute aqueous solution, V. An entropy titration study of adenosine, pentoses, hexoses, and related compounds. J. Am. Chem. Soc. 88: 2641-2645.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 2641-2645
    • Izatt, R.M.1    Rytting, J.H.2    Hansen, L.D.3    Christensen, J.J.4
  • 23
    • 0000875209 scopus 로고
    • Interconversion and phosphoester hydrolysis of 2′,5′- and 3′,5′-dinucleoside monophosphates: Kinetics and mechanisms
    • Järvinen, P., Oivanen, M., and Lönnberg, H. 1991. Interconversion and phosphoester hydrolysis of 2′,5′- and 3′,5′-dinucleoside monophosphates: Kinetics and mechanisms. J. Org. Chem. 56: 5396-5401.
    • (1991) J. Org. Chem. , vol.56 , pp. 5396-5401
    • Järvinen, P.1    Oivanen, M.2    Lönnberg, H.3
  • 25
    • 33746204093 scopus 로고    scopus 로고
    • Enzyme mechanisms, models, and mimics
    • Kirby, A.J. 1996. Enzyme mechanisms, models, and mimics. Angew. Chem. Int. Ed. Engl. 35: 707-724.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 707-724
    • Kirby, A.J.1
  • 26
    • 37049072666 scopus 로고
    • General and specific acid/base catalysis of the hydrolysis and interconversion of ribonucleoside 2′- and 3′-phosphotriesters: Kinetics and mechanisms of the reactions of 5′-O-pivaloyluridine 2′- and 3′-dimethylphosphates
    • Kosonen, M. and Lönnberg, H. 1995. General and specific acid/base catalysis of the hydrolysis and interconversion of ribonucleoside 2′- and 3′-phosphotriesters: kinetics and mechanisms of the reactions of 5′-O-pivaloyluridine 2′- and 3′-dimethylphosphates. J. Chem. Soc. Perkin Trans. 2: 1203-1209.
    • (1995) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1203-1209
    • Kosonen, M.1    Lönnberg, H.2
  • 27
    • 0028865468 scopus 로고
    • Cleavage properties of an oligonudeotide containing a bridged internucleotide 5′-phosphorothioate RNA linkage
    • Kuimelis, R.G. and McLaughlin, L.W. 1995. Cleavage properties of an oligonudeotide containing a bridged internucleotide 5′-phosphorothioate RNA linkage. Nucleic Acids Res. 23: 4753-4760.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4753-4760
    • Kuimelis, R.G.1    McLaughlin, L.W.2
  • 28
    • 0035869008 scopus 로고    scopus 로고
    • Structure, folding and activity of the VS ribozyme: Importance of the 2-3-6 helical junction
    • Lafontaine, D.A., Norman, D.G., and Lilley, D.M.J. 2001. Structure, folding and activity of the VS ribozyme: Importance of the 2-3-6 helical junction. EMBO J. 20: 1415-1424.
    • (2001) EMBO J. , vol.20 , pp. 1415-1424
    • Lafontaine, D.A.1    Norman, D.G.2    Lilley, D.M.J.3
  • 29
    • 0038475923 scopus 로고    scopus 로고
    • Substrate specificity and reaction kinetics of an X-motif ribozyme
    • Lazarev, D., Puskarz, I., and Breaker, R.R. 2003. Substrate specificity and reaction kinetics of an X-motif ribozyme. RNA 9: 688-697.
    • (2003) RNA , vol.9 , pp. 688-697
    • Lazarev, D.1    Puskarz, I.2    Breaker, R.R.3
  • 30
    • 0030747007 scopus 로고    scopus 로고
    • a shift at the active site of a lead-dependent ribozyme
    • a shift at the active site of a lead-dependent ribozyme. J. Am. Chem. Soc. 119: 6621-6628.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6621-6628
    • Legault, P.1    Pardi, A.2
  • 31
    • 0033575087 scopus 로고    scopus 로고
    • Kinetics of RNA degradation by specific base catalysis of transesterification involving the 2′-hydroxyl group
    • Li, Y. and Breaker, R.R. 1999. Kinetics of RNA degradation by specific base catalysis of transesterification involving the 2′-hydroxyl group. J. Am. Chem. Soc. 121: 5364-5372.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5364-5372
    • Li, Y.1    Breaker, R.R.2
  • 32
    • 0010835929 scopus 로고
    • Nonexistence of dianionic pentacovalent intermediates in an ab initio study of the base-catalyzed hydrolysis of ethylene phosphate
    • Lim C., and Karplus, M. 1990. Nonexistence of dianionic pentacovalent intermediates in an ab initio study of the base-catalyzed hydrolysis of ethylene phosphate. J. Am. Chem. Soc. 112: 5872-5873.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5872-5873
    • Lim, C.1    Karplus, M.2
  • 34
    • 0006120328 scopus 로고
    • The mechanism of the alkaline hydrolysis of ribonucleic acids
    • Lipkin, D., Talbert, P.T., and Cohn, M. 1954. The mechanism of the alkaline hydrolysis of ribonucleic acids. J. Am. Chem. Soc. 76:2871-2872.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 2871-2872
    • Lipkin, D.1    Talbert, P.T.2    Cohn, M.3
  • 36
    • 0003467672 scopus 로고
    • Acids and bases
    • John Wiley & Sons, New York
    • March, J. 1992. Acids and bases. In Advanced organic chemistry, 4th ed., pp, 248-272. John Wiley & Sons, New York.
    • (1992) Advanced Organic Chemistry, 4th Ed. , pp. 248-272
    • March, J.1
  • 37
    • 0034712097 scopus 로고    scopus 로고
    • General acid-base catalysis in the mechanism of a hepatitis δ virus ribozyme
    • Nakano, S.-I., Chadalavada, D.M., and Bevilacqua, P.C. 2000. General acid-base catalysis in the mechanism of a hepatitis δ virus ribozyme. Science 287: 1493-1497.
    • (2000) Science , vol.287 , pp. 1493-1497
    • Nakano, S.-I.1    Chadalavada, D.M.2    Bevilacqua, P.C.3
  • 38
    • 0001127361 scopus 로고
    • Hydrolytic reactions of the diastereomeric phosphoromonothioate analogs of uridylyl(3′,5′)uridine: Kinetics and mechanisms for desulfurization, phosphoester hydrolysis, and transesterification to the 2′,5′-isomers
    • Oivanen, M., Ora, M., Almer, H., Strömberg, R., and Lönnberg, H. 1995. Hydrolytic reactions of the diastereomeric phosphoromonothioate analogs of uridylyl(3′,5′)uridine: Kinetics and mechanisms for desulfurization, phosphoester hydrolysis, and transesterification to the 2′,5′-isomers. J. Org. Chem. 60: 5620-5627.
    • (1995) J. Org. Chem. , vol.60 , pp. 5620-5627
    • Oivanen, M.1    Ora, M.2    Almer, H.3    Strömberg, R.4    Lönnberg, H.5
  • 39
    • 0001055719 scopus 로고    scopus 로고
    • Kinetics and mechanisms for the cleavage and isomerization of the phosphodiester bonds of RNA by bronsted acids and bases
    • Oivanen, M., Kuusela, S., and Lönnberg, H. 1998. Kinetics and mechanisms for the cleavage and isomerization of the phosphodiester bonds of RNA by bronsted acids and bases. Chem. Rev. 98: 961-990.
    • (1998) Chem. Rev. , vol.98 , pp. 961-990
    • Oivanen, M.1    Kuusela, S.2    Lönnberg, H.3
  • 40
    • 0030902181 scopus 로고    scopus 로고
    • Unifying the current data on the mechanism of cleavage-transesterification of RNA
    • Perreault, D.M. and Anslyn, E. 1997. Unifying the current data on the mechanism of cleavage-transesterification of RNA. Angew. Chem. Int. Ed. Engl. 36: 432-450.
    • (1997) Angew. Chem. Int. Ed. Engl. , vol.36 , pp. 432-450
    • Perreault, D.M.1    Anslyn, E.2
  • 41
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines, R.T. 1998. Ribonuclease A. Chem. Rev. 98: 1045-1066.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 42
    • 77956909282 scopus 로고
    • Bovine pancreatic ribonuclease
    • (ed. P. Boyer). Academic Press, New York
    • Richards, R.M. and Wyckoff, H.M. 1971. Bovine pancreatic ribonuclease. In The enzymes, vol. 4 (ed. P. Boyer), pp. 647-806. Academic Press, New York.
    • (1971) The Enzymes , vol.4 , pp. 647-806
    • Richards, R.M.1    Wyckoff, H.M.2
  • 43
    • 0003458038 scopus 로고
    • Physical properties of nucleotides: Charge densities, pK values, spectra, and tautomerism
    • Springer-Verlag, New York
    • Saenger, W. 1984. Physical properties of nucleotides: Charge densities, pK values, spectra, and tautomerism. In Principles of nucleic acid structure, pp. 105-115. Springer-Verlag, New York.
    • (1984) Principles of Nucleic Acid Structure , pp. 105-115
    • Saenger, W.1
  • 44
    • 0030898510 scopus 로고    scopus 로고
    • A general purpose RNA-cleaving DNA enzyme
    • Santoro, S.W. and Joyce, G.F. 1997. A general purpose RNA-cleaving DNA enzyme. Proc. Natl. Acad. Sci. 94: 4262-4266.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 4262-4266
    • Santoro, S.W.1    Joyce, G.F.2
  • 45
    • 0033555778 scopus 로고    scopus 로고
    • A re-investigation of the thio effect at the hammerhead cleavage site
    • Scott, E.C. and Uhlenbeck, O.C. 1999. A re-investigation of the thio effect at the hammerhead cleavage site. Nucleic Acids Res. 27: 479-484.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 479-484
    • Scott, E.C.1    Uhlenbeck, O.C.2
  • 46
    • 0033325108 scopus 로고    scopus 로고
    • Biophysical and biochemical investigations of RNA catalysis in the hammerhead ribozyme
    • Scott, W.G. 1999. Biophysical and biochemical investigations of RNA catalysis in the hammerhead ribozyme. Q. Rev. Biophys. 32: 241-284.
    • (1999) Q. Rev. Biophys. , vol.32 , pp. 241-284
    • Scott, W.G.1
  • 47
    • 0026758924 scopus 로고
    • Phenyl ester of adenosine 3′-phosphate as a novel probe for the rate-limiting step in RNA hydrolysis
    • Shiiba, T. and Komiyama, M. 1992. Phenyl ester of adenosine 3′-phosphate as a novel probe for the rate-limiting step in RNA hydrolysis. Tetrahedron Lett. 33: 5571-5574.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 5571-5574
    • Shiiba, T.1    Komiyama, M.2
  • 48
    • 0036314853 scopus 로고    scopus 로고
    • Identification of the catalytic subdomain of the VS ribozyme and evidence for remarkable sequence tolerance in the active site loop
    • Sood, V.D. and Collins, R.A. 2002. Identification of the catalytic subdomain of the VS ribozyme and evidence for remarkable sequence tolerance in the active site loop. J. Mol. Biol. 320: 443-454.
    • (2002) J. Mol. Biol. , vol.320 , pp. 443-454
    • Sood, V.D.1    Collins, R.A.2
  • 49
    • 0032831634 scopus 로고    scopus 로고
    • Relationship between internucleotide linkage geometry and the stability of RNA
    • Soukup, G.A. and Breaker, R.R. 1999. Relationship between internucleotide linkage geometry and the stability of RNA. RNA 5: 1308-1325.
    • (1999) RNA , vol.5 , pp. 1308-1325
    • Soukup, G.A.1    Breaker, R.R.2
  • 50
    • 0031828144 scopus 로고    scopus 로고
    • Hammerhead ribozyme kinetics
    • Stage-Zimmermann, T.K. and Uhlenbeck, O.C. 1998. Hammerhead ribozyme kinetics. RNA 4: 875-889.
    • (1998) RNA , vol.4 , pp. 875-889
    • Stage-Zimmermann, T.K.1    Uhlenbeck, O.C.2
  • 51
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T.A. and Steitz, J.A. 1993. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. 90: 6498-6502.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 52
    • 0030810710 scopus 로고    scopus 로고
    • Examination of the catalytic fitness of the hammerhead ribozyme by in vitro selection
    • Tang, J. and Breaker, R.R. 1997. Examination of the catalytic fitness of the hammerhead ribozyme by in vitro selection. RNA 3: 914-925.
    • (1997) RNA , vol.3 , pp. 914-925
    • Tang, J.1    Breaker, R.R.2
  • 53
    • 0034705119 scopus 로고    scopus 로고
    • Structural diversity of self-cleaving ribozymes
    • -. 2000. Structural diversity of self-cleaving ribozymes. Proc. Natl. Acad. Sci. 97: 5784-5789.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 5784-5789
    • Tang, J.1
  • 54
    • 0030844830 scopus 로고    scopus 로고
    • Organization and expression of the hepatitis δ virus genome
    • Taylor, J.M. 1997. Organization and expression of the hepatitis δ virus genome. Semin. Virol. 8: 59-64.
    • (1997) Semin. Virol. , vol.8 , pp. 59-64
    • Taylor, J.M.1
  • 55
    • 23044505158 scopus 로고
    • Mechanism and catalysis of nucleophilic substitution in phosphate esters
    • Thatcher, G.R.J. and Kluger, R. 1989. Mechanism and catalysis of nucleophilic substitution in phosphate esters. Adv. Phys. Org. Chem. 25: 99-265.
    • (1989) Adv. Phys. Org. Chem. , vol.25 , pp. 99-265
    • Thatcher, G.R.J.1    Kluger, R.2
  • 57
    • 0029818441 scopus 로고    scopus 로고
    • Synthesis and properties of diuridine phosphate analogues containing thio and amino modifications
    • Thomson, J.B., Patel, B.K., Jimenez, V., Eckart, K., and Eckstein, F. 1996. Synthesis and properties of diuridine phosphate analogues containing thio and amino modifications. J. Org. Chem. 61: 6273-6281.
    • (1996) J. Org. Chem. , vol.61 , pp. 6273-6281
    • Thomson, J.B.1    Patel, B.K.2    Jimenez, V.3    Eckart, K.4    Eckstein, F.5
  • 58
    • 0001229651 scopus 로고    scopus 로고
    • Inorganic mimics of ribonucleases and ribozymes: From random cleavage to sequence-specific chemistry to catalytic antisense drugs
    • Trawick, B.N., Daniher, A.T., and Bashkin, J.K. 1998. Inorganic mimics of ribonucleases and ribozymes: From random cleavage to sequence-specific chemistry to catalytic antisense drugs. Chem. Rev. 98: 939-960.
    • (1998) Chem. Rev. , vol.98 , pp. 939-960
    • Trawick, B.N.1    Daniher, A.T.2    Bashkin, J.K.3
  • 60
    • 0036161836 scopus 로고    scopus 로고
    • Ribozyme activity in the genomic and antigenomic RNA strands of hepatitis δ virus
    • Wadkins T.S., and Been, M.D. 2002. Ribozyme activity in the genomic and antigenomic RNA strands of hepatitis δ virus. Cell Mol. Life Sci. 59: 112-125.
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 112-125
    • Wadkins, T.S.1    Been, M.D.2
  • 61
    • 0031995580 scopus 로고    scopus 로고
    • The hairpin ribozyme: Structure, assembly and catalysis
    • Walter, N.G. and Burke, J.M. 1998. The hairpin ribozyme: Structure, assembly and catalysis. Curr. Opin. Chem. Biol. 2: 24-30.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 24-30
    • Walter, N.G.1    Burke, J.M.2
  • 62
    • 0031860104 scopus 로고    scopus 로고
    • Crystallographic structures of the hammerhead ribozyme: Relationship to ribozyme folding and catalysis
    • Wedekind, J.E. and McKay, D.B. 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
  • 63
    • 0002920388 scopus 로고
    • Pseudo-rotation in the hydrolysis of phosphate esters
    • Westheimer, F.H. 1968. Pseudo-rotation in the hydrolysis of phosphate esters. Acc. Chem. Res. 1: 70-78.
    • (1968) Acc. Chem. Res. , vol.1 , pp. 70-78
    • Westheimer, F.H.1
  • 64
    • 0023099216 scopus 로고
    • Why nature chose phosphates
    • -. 1987. Why nature chose phosphates. Science 235 1173-1178.
    • (1987) Science , vol.235 , pp. 1173-1178
    • Westheimer, F.H.1
  • 66
    • 0032853242 scopus 로고    scopus 로고
    • In vitro selection of functional nucleic acids
    • Wilson, D.S. and Szostak, J. W. 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
  • 67
    • 11544373758 scopus 로고    scopus 로고
    • The hydrolysis of RNA: From theoretical calculations to the hammerhead ribozyme-mediated cleavage of RNA
    • Zhou, D.-M. and Taira, K. 1998. The hydrolysis of RNA: From theoretical calculations to the hammerhead ribozyme-mediated cleavage of RNA. Chem. Rev. 98: 991-1026.
    • (1998) Chem. Rev. , vol.98 , pp. 991-1026
    • Zhou, D.-M.1    Taira, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.