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Volumn 10, Issue 1, 2003, Pages 5-14

In search of an RNA replicase ribozyme

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EID: 0037256766     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(03)00003-6     Document Type: Review
Times cited : (56)

References (64)
  • 2
    • 0000693204 scopus 로고    scopus 로고
    • Small ribozymes
    • R.F. Gesteland, T.R. Cech, & J.F. Atkins. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 265-286.pp
    • McKay D.B., Wedekind J.E. Small ribozymes. Gesteland R.F., Cech T.R., Atkins J.F. The RNA World. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 265-286.pp.
    • (1999) The RNA World
    • McKay, D.B.1    Wedekind, J.E.2
  • 3
    • 0002671710 scopus 로고    scopus 로고
    • Group I and group II ribozymes as RNPs: Clues to the past and guides to the future
    • R.F. Gesteland, T.R. Cech, & J.F. Atkins. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press. 451-485.pp
    • Lambowitz A.M., Caprara M.G. Group I and group II ribozymes as RNPs. clues to the past and guides to the future Gesteland R.F., Cech T.R., Atkins J.F. The RNA World. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 451-485.pp.
    • (1999) The RNA World
    • Lambowitz, A.M.1    Caprara, M.G.2
  • 4
    • 0003120548 scopus 로고    scopus 로고
    • Ribonuclease P
    • R.F. Gesteland, T.R. Cech, & J.F. Atkins. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press. 351-380.pp
    • Altman S., Kirsebom L. Ribonuclease P. Gesteland R.F., Cech T.R., Atkins J.F. The RNA World. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 351-380.pp.
    • (1999) The RNA World
    • Altman, S.1    Kirsebom, L.2
  • 5
    • 0033779905 scopus 로고    scopus 로고
    • Ribonuclease P: A ribonucleoprotein enzyme
    • Kurz J.C., Fierke C.A. Ribonuclease P. a ribonucleoprotein enzyme Curr. Opin. Chem. Biol. 4:2000;553-558.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 553-558
    • Kurz, J.C.1    Fierke, C.A.2
  • 6
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • Noller H.F., Hoffarth V., Zimniak L. Unusual resistance of peptidyl transferase to protein extraction procedures. Science. 256:1992;1416-1419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 7
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. 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.B.4    Steitz, T.A.5
  • 8
    • 0017232521 scopus 로고
    • Coenzymes as fossils of an earlier metabolic state
    • White H.B. III. Coenzymes as fossils of an earlier metabolic state. J. Mol. Evol. 7:1976;101-104.
    • (1976) J. Mol. Evol. , vol.7 , pp. 101-104
    • White H.B. III1
  • 9
    • 0028932883 scopus 로고
    • Structures of DNA and RNA polymerases and their interactions with nucleic acid substrates
    • Arnold E., Ding J., Hughes S.H., Hostomsky Z. Structures of DNA and RNA polymerases and their interactions with nucleic acid substrates. Curr. Opin. Struct. Biol. 5:1995;27-38.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 27-38
    • Arnold, E.1    Ding, J.2    Hughes, S.H.3    Hostomsky, Z.4
  • 10
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • Brautigam C.A., Steitz T.A. Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol. 8:1998;54-63.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 54-63
    • Brautigam, C.A.1    Steitz, T.A.2
  • 12
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer, and ddCTP
    • Pelletier H., Sawaya M.R., Kumar A., Wilson S.H., Kraut J. Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer, and ddCTP. Science. 264:1994;1891-1903.
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 13
    • 0030592095 scopus 로고    scopus 로고
    • Structure of Taq polymerase with DNA at the polymerase active site
    • Eom S.H., Wang J., Steitz T.A. Structure of Taq polymerase with DNA at the polymerase active site. Nature. 382:1996;278-281.
    • (1996) Nature , vol.382 , pp. 278-281
    • Eom, S.H.1    Wang, J.2    Steitz, T.A.3
  • 14
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublié S., Tabor S., Long A.M., Richardson C.C., Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature. 391:1998;251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 15
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • Li Y., Korolev S., Waksman G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I. structural basis for nucleotide incorporation EMBO J. 17:1998;7514-7525.
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 16
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang H., Chopra R., Verdine G.L., Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase. implications for drug resistance Science. 282:1998;1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 17
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol α family DNA polymerase
    • Franklin M.C., Wang J., Steitz T.A. Structure of the replicating complex of a pol α family DNA polymerase. Cell. 105:2001;657-667.
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 18
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya M.R., Prasad R., Wilson S.H., Kraut J., Pelletier H. Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA. evidence for an induced fit mechanism Biochemistry. 36:1997;11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 19
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer J.R., Mao C., Braman J.C., Beese L.S. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature. 391:1998;304-307.
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 20
    • 0027231782 scopus 로고
    • Structure of DNA polymerase I Klenow fragment bound to duplex DNA
    • Beese L.S., Derbyshire V., Steitz T.A. Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science. 260:1993;352-355.
    • (1993) Science , vol.260 , pp. 352-355
    • Beese, L.S.1    Derbyshire, V.2    Steitz, T.A.3
  • 22
    • 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
  • 23
    • 0026717535 scopus 로고
    • Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong X.-P., Onrust R., O'Donnell M., Kuriyan J. Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme. a sliding DNA clamp Cell. 69:1992;425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.-P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 24
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S.R., Kong X.-P., Gary S., Burgers P.M., Kuriyan J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell. 79:1994;1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.R.1    Kong, X.-P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 25
    • 0032520210 scopus 로고    scopus 로고
    • Processivity of DNA polymerases: Two mechanisms, one goal
    • Kelmann Z., Hurwitz J., O'Donnell M. Processivity of DNA polymerases. two mechanisms, one goal Structure. 6:1998;121-125.
    • (1998) Structure , vol.6 , pp. 121-125
    • Kelmann, Z.1    Hurwitz, J.2    O'Donnell, M.3
  • 26
    • 0029784881 scopus 로고    scopus 로고
    • A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity
    • Minnick D.T., Astatke M., Joyce C.M., Kunkel T.A. A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. J. Biol. Chem. 271:1996;24954-24961.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24954-24961
    • Minnick, D.T.1    Astatke, M.2    Joyce, C.M.3    Kunkel, T.A.4
  • 27
    • 0027179827 scopus 로고
    • Short gap-filling synthesis by DNA polymerase β is processive
    • Singhal R.K., Wilson S.H. Short gap-filling synthesis by DNA polymerase β is processive. J. Biol. Chem. 268:1993;15906-15911.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15906-15911
    • Singhal, R.K.1    Wilson, S.H.2
  • 28
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with DNA: Implications for catalytic mechanism, processivity, and fidelity
    • Pelletier H., Sawaya M.R., Wolfle W., Wilson S.H., Kraut J. Crystal structures of human DNA polymerase β complexed with DNA. implications for catalytic mechanism, processivity, and fidelity Biochemistry. 35:1996;12742-12761.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 29
    • 0023512002 scopus 로고
    • Nonenzymatic template-directed synthesis of informational macromolecules
    • Joyce G.F. Nonenzymatic template-directed synthesis of informational macromolecules. Cold Spring Harb. Symp. Quant. Biol. 52:1987;41-51.
    • (1987) Cold Spring Harb. Symp. Quant. Biol. , vol.52 , pp. 41-51
    • Joyce, G.F.1
  • 30
    • 0002622819 scopus 로고    scopus 로고
    • Prospects for understanding the origin of the RNA world
    • R.F. Gesteland, T.R. Cech, & J.F. Atkins. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 49-77.pp
    • Joyce G.F., Orgel L.E. Prospects for understanding the origin of the RNA world. Gesteland R.F., Cech T.R., Atkins J.F. The RNA World. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 49-77.pp.
    • (1999) The RNA World
    • Joyce, G.F.1    Orgel, L.E.2
  • 31
    • 0033792511 scopus 로고    scopus 로고
    • Gene structure and function of the 2′-5′-oligoadenylate synthase family
    • Justesen J., Hartmann R., Kjeldgaard N.O. Gene structure and function of the 2′-5′-oligoadenylate synthase family. Cell. Mol. Life Sci. 57:2000;1593-1612.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1593-1612
    • Justesen, J.1    Hartmann, R.2    Kjeldgaard, N.O.3
  • 33
    • 0000328668 scopus 로고
    • Substituent control of the poly(C)-directed oligomerization of guanosine 5′-phophorimidazolide
    • Inoue T., Orgel L.E. Substituent control of the poly(C)-directed oligomerization of guanosine 5′-phophorimidazolide. J. Am. Chem. Soc. 103:1981;7666-7667.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7666-7667
    • Inoue, T.1    Orgel, L.E.2
  • 34
    • 0020370504 scopus 로고
    • Oligomerization of (guanosine 5′-phosphor)-2-methylimidazole on poly(C): An RNA polymerase model
    • Inoue T., Orgel L.E. Oligomerization of (guanosine 5′-phosphor)-2-methylimidazole on poly(C). An RNA polymerase model J. Mol. Biol. 162:1982;201-217.
    • (1982) J. Mol. Biol. , vol.162 , pp. 201-217
    • Inoue, T.1    Orgel, L.E.2
  • 35
    • 0021770666 scopus 로고
    • Non-enzymatic template-directed synthesis on RNA random copolymers: Poly(C,U) templates
    • Joyce G.F., Inoue T., Orgel L.E. Non-enzymatic template-directed synthesis on RNA random copolymers. poly(C,U) templates J. Mol. Biol. 176:1984;279-306.
    • (1984) J. Mol. Biol. , vol.176 , pp. 279-306
    • Joyce, G.F.1    Inoue, T.2    Orgel, L.E.3
  • 36
    • 0023042024 scopus 로고
    • Non-enzymic template-directed synthesis on RNA random copolymers: Poly(C,G) templates
    • Joyce G.F., Orgel L.E. Non-enzymic template-directed synthesis on RNA random copolymers. poly(C,G) templates J. Mol. Biol. 188:1986;433-441.
    • (1986) J. Mol. Biol. , vol.188 , pp. 433-441
    • Joyce, G.F.1    Orgel, L.E.2
  • 37
    • 0027105556 scopus 로고
    • Nonenzymatic template-directed synthesis on oligodeoxycytidylate sequences in hairpin oligonucleotides
    • Wu T., Orgel L.E. Nonenzymatic template-directed synthesis on oligodeoxycytidylate sequences in hairpin oligonucleotides. J. Am. Chem. Soc. 114:1992;317-322.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 317-322
    • Wu, T.1    Orgel, L.E.2
  • 38
    • 0027105883 scopus 로고
    • Nonenzymatic template-directed synthesis on hairpin oligonucleotides. 2. Templates containing cytidine and guanosine residues
    • Wu T., Orgel L.E. Nonenzymatic template-directed synthesis on hairpin oligonucleotides. 2. Templates containing cytidine and guanosine residues. J. Am. Chem. Soc. 114:1992;5496-5501.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5496-5501
    • Wu, T.1    Orgel, L.E.2
  • 39
    • 0027105883 scopus 로고
    • Nonenzymatic template-directed synthesis on hairpin oligonucleotides. 3. Incorporation of adenosine and uridine residues
    • Wu T., Orgel L.E. Nonenzymatic template-directed synthesis on hairpin oligonucleotides. 3. Incorporation of adenosine and uridine residues. J. Am. Chem. Soc. 114:1992;7963-7969.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7963-7969
    • Wu, T.1    Orgel, L.E.2
  • 40
    • 0021770899 scopus 로고
    • Template-directed synthesis on the pentanucleotide CpCpGpCpC
    • Inoue T., Joyce G.F., Grzeskowiak K., Orgel L.E. Template-directed synthesis on the pentanucleotide CpCpGpCpC. J. Mol. Biol. 178:1984;669-676.
    • (1984) J. Mol. Biol. , vol.178 , pp. 669-676
    • Inoue, T.1    Joyce, G.F.2    Grzeskowiak, K.3    Orgel, L.E.4
  • 41
    • 0030003509 scopus 로고    scopus 로고
    • Kinetic and mechanistic analysis of nonenzymatic, template-directed oligoribonucleotide ligation
    • Rohatgi R., Bartel D.P., Szostak J.W. Kinetic and mechanistic analysis of nonenzymatic, template-directed oligoribonucleotide ligation. J. Am. Chem. Soc. 118:1996;3332-3339.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3332-3339
    • Rohatgi, R.1    Bartel, D.P.2    Szostak, J.W.3
  • 42
    • 0029915714 scopus 로고    scopus 로고
    • Nonenzymatic, template-directed ligation of oligoribonucleotides is highly regioselective for the formation of 3′-5′ phosphodiester bonds
    • Rohatgi R., Bartel D.P., Szostak J.W. Nonenzymatic, template-directed ligation of oligoribonucleotides is highly regioselective for the formation of 3′-5′ phosphodiester bonds. J. Am. Chem. Soc. 118:1996;3340-3344.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3340-3344
    • Rohatgi, R.1    Bartel, D.P.2    Szostak, J.W.3
  • 43
    • 0027488624 scopus 로고
    • Isolation of new ribozymes from a large pool of random sequences
    • Bartel D.P., Szostak J.W. Isolation of new ribozymes from a large pool of random sequences. Science. 261:1993;1411-1418.
    • (1993) Science , vol.261 , pp. 1411-1418
    • Bartel, D.P.1    Szostak, J.W.2
  • 44
    • 0029147392 scopus 로고
    • Structurally complex and highly active RNA ligases derived from random RNA sequences
    • Ekland E.H., Szostak J.W., Bartel D.P. Structurally complex and highly active RNA ligases derived from random RNA sequences. Science. 269:1995;364-370.
    • (1995) Science , vol.269 , pp. 364-370
    • Ekland, E.H.1    Szostak, J.W.2    Bartel, D.P.3
  • 45
    • 0032955410 scopus 로고    scopus 로고
    • In vitro selection of an allosteric ribozyme that transduces analytes to amplicons
    • Robertson M.P., Ellington A.D. In vitro selection of an allosteric ribozyme that transduces analytes to amplicons. Nat. Biotechnol. 17:1999;62-66.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 62-66
    • Robertson, M.P.1    Ellington, A.D.2
  • 46
    • 0035032445 scopus 로고    scopus 로고
    • The effect of cytidine on the structure and function of an RNA ligase ribozyme
    • Rogers J., Joyce G.F. The effect of cytidine on the structure and function of an RNA ligase ribozyme. RNA. 7:2001;395-404.
    • (2001) RNA , vol.7 , pp. 395-404
    • Rogers, J.1    Joyce, G.F.2
  • 47
    • 0033592981 scopus 로고    scopus 로고
    • A complex ligase ribozyme evolved in vitro from a group I ribozyme domain
    • Jaeger L., Wright M.C., Joyce G.F. A complex ligase ribozyme evolved in vitro from a group I ribozyme domain. Proc. Natl. Acad. Sci. USA. 96:1999;14712-14717.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14712-14717
    • Jaeger, L.1    Wright, M.C.2    Joyce, G.F.3
  • 48
    • 0029832218 scopus 로고    scopus 로고
    • RNA-catalysed RNA polymerization using nucleoside triphosphates
    • Ekland E.H., Bartel D.P. RNA-catalysed RNA polymerization using nucleoside triphosphates. Nature. 382:1996;373-376.
    • (1996) Nature , vol.382 , pp. 373-376
    • Ekland, E.H.1    Bartel, D.P.2
  • 49
    • 0034655587 scopus 로고    scopus 로고
    • Design and optimization of effector-activated ribozyme ligases
    • Robertson M.P., Ellington A.D. Design and optimization of effector-activated ribozyme ligases. Nucleic Acids Res. 28:2000;1751-1759.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1751-1759
    • Robertson, M.P.1    Ellington, A.D.2
  • 50
    • 0034936573 scopus 로고    scopus 로고
    • In vitro selection of nucleoprotein enzymes
    • Robertson M.P., Ellington A.D. In vitro selection of nucleoprotein enzymes. Nat. Biotechnol. 19:2001;650-655.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 650-655
    • Robertson, M.P.1    Ellington, A.D.2
  • 51
    • 0014378880 scopus 로고
    • The origin of the genetic code
    • Crick F.H.C. The origin of the genetic code. J. Mol. Biol. 38:1968;367-379.
    • (1968) J. Mol. Biol. , vol.38 , pp. 367-379
    • Crick, F.H.C.1
  • 52
    • 0014369024 scopus 로고
    • Evolution of the genetic apparatus
    • Orgel L.E. Evolution of the genetic apparatus. J. Mol. Biol. 38:1968;381-393.
    • (1968) J. Mol. Biol. , vol.38 , pp. 381-393
    • Orgel, L.E.1
  • 53
    • 0032549780 scopus 로고    scopus 로고
    • RNA folding at millisecond intervals by synchotron hydroxyl radical footprinting
    • Sclavi B., Sullivan M., Chance M.R., Brenowitz M., Woodson S.A. RNA folding at millisecond intervals by synchotron hydroxyl radical footprinting. Science. 279:1998;1940-1943.
    • (1998) Science , vol.279 , pp. 1940-1943
    • Sclavi, B.1    Sullivan, M.2    Chance, M.R.3    Brenowitz, M.4    Woodson, S.A.5
  • 54
    • 0032549735 scopus 로고    scopus 로고
    • Kinetic intermediates trapped by native interactions in RNA folding
    • Treiber D.K., Rook M.S., Zarrinkar P.P., Williamson J.R. Kinetic intermediates trapped by native interactions in RNA folding. Science. 279:1998;1943-1946.
    • (1998) Science , vol.279 , pp. 1943-1946
    • Treiber, D.K.1    Rook, M.S.2    Zarrinkar, P.P.3    Williamson, J.R.4
  • 55
    • 0034696587 scopus 로고    scopus 로고
    • Kinetic framework for ligation by an efficient RNA ligase ribozyme
    • Bergman N.H., Johnston W.K., Bartel D.P. Kinetic framework for ligation by an efficient RNA ligase ribozyme. Biochemistry. 39:2000;3115-3123.
    • (2000) Biochemistry , vol.39 , pp. 3115-3123
    • Bergman, N.H.1    Johnston, W.K.2    Bartel, D.P.3
  • 56
    • 0034687717 scopus 로고    scopus 로고
    • Recognition of nucleoside triphosphates during RNA-catalyzed primer extension
    • Glasner M.E., Yen C.C., Ekland E.H., Bartel D.P. Recognition of nucleoside triphosphates during RNA-catalyzed primer extension. Biochemistry. 39:2000;15556-15562.
    • (2000) Biochemistry , vol.39 , pp. 15556-15562
    • Glasner, M.E.1    Yen, C.C.2    Ekland, E.H.3    Bartel, D.P.4
  • 57
    • 0036015841 scopus 로고    scopus 로고
    • Continuous in vitro evolution of a ribozyme that catalyzes three successive nucleotidyl addition reactions
    • McGinness K.E., Wright M.C., Joyce G.F. Continuous in vitro evolution of a ribozyme that catalyzes three successive nucleotidyl addition reactions. Chem. Biol. 9:2002;585-596.
    • (2002) Chem. Biol. , vol.9 , pp. 585-596
    • McGinness, K.E.1    Wright, M.C.2    Joyce, G.F.3
  • 58
    • 0030901131 scopus 로고    scopus 로고
    • Continuous in vitro evolution of catalytic function
    • Wright M.C., Joyce G.F. Continuous in vitro evolution of catalytic function. Science. 276:1997;614-617.
    • (1997) Science , vol.276 , pp. 614-617
    • Wright, M.C.1    Joyce, G.F.2
  • 59
    • 0036009338 scopus 로고    scopus 로고
    • RNA-catalyzed RNA ligation on an external RNA template
    • McGinness K.E., Joyce G.F. RNA-catalyzed RNA ligation on an external RNA template. Chem. Biol. 9:2002;297-307.
    • (2002) Chem. Biol. , vol.9 , pp. 297-307
    • McGinness, K.E.1    Joyce, G.F.2
  • 60
    • 0035906978 scopus 로고    scopus 로고
    • RNA-catalyzed RNA polymerization: Accurate and general RNA-templated primer extension
    • Johnston W.K., Unrau P.J., Lawrence M.S., Glasner M.E., Bartel D.P. RNA-catalyzed RNA polymerization. accurate and general RNA-templated primer extension Science. 292:2001;1319-1325.
    • (2001) Science , vol.292 , pp. 1319-1325
    • Johnston, W.K.1    Unrau, P.J.2    Lawrence, M.S.3    Glasner, M.E.4    Bartel, D.P.5
  • 61
    • 0002502220 scopus 로고    scopus 로고
    • Before RNA and after: Geophysical and geochemical constraints on molecular evolution
    • R.F. Gesteland, T.R. Cech, & J.F. Atkins. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 1-47.pp
    • Mojzsis S.J., Krishnamurthy R., Arrhenius G. Before RNA and after. geophysical and geochemical constraints on molecular evolution Gesteland R.F., Cech T.R., Atkins J.F. The RNA World. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 1-47.pp.
    • (1999) The RNA World
    • Mojzsis, S.J.1    Krishnamurthy, R.2    Arrhenius, G.3
  • 62
    • 0002146655 scopus 로고    scopus 로고
    • Re-creating an RNA replicase
    • R.F. Gesteland, T.R. Cech, & J.F. Atkins. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 143-162.pp
    • Bartel D.P. Re-creating an RNA replicase. Gesteland R.F., Cech T.R., Atkins J.F. The RNA World. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 143-162.pp.
    • (1999) The RNA World
    • Bartel, D.P.1
  • 63
    • 0023449816 scopus 로고
    • TRNA-like structures tag the 3′ ends of genomic RNA molecules for replication: Implications for the origin of protein synthesis
    • Weiner A.M., Maizels N. tRNA-like structures tag the 3′ ends of genomic RNA molecules for replication. implications for the origin of protein synthesis Proc. Natl. Acad. Sci. USA. 84:1987;7383-7387.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7383-7387
    • Weiner, A.M.1    Maizels, N.2
  • 64
    • 0002382573 scopus 로고    scopus 로고
    • The genomic tag hypothesis: What molecular fossils tell us about the evolution of tRNA
    • R.F. Gesteland, T.R. Cech, & J.F. Atkins. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 79-111.pp
    • Maizels N., Weiner A.M. The genomic tag hypothesis. what molecular fossils tell us about the evolution of tRNA Gesteland R.F., Cech T.R., Atkins J.F. The RNA World. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 79-111.pp.
    • (1999) The RNA World
    • Maizels, N.1    Weiner, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.