메뉴 건너뛰기




Volumn 2, Issue 3, 1998, Pages 320-327

Oligonucleotide libraries - Variatio delectat

Author keywords

[No Author keywords available]

Indexed keywords

DNA; OLIGONUCLEOTIDE; RIBOZYME; RNA;

EID: 0032087815     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80004-5     Document Type: Article
Times cited : (58)

References (69)
  • 1
    • 0031152065 scopus 로고    scopus 로고
    • Aptamers as therapeutic and diagnostic reagents: Problems and prospects
    • Osborne SE, Matsumura I, Ellington AD: Aptamers as therapeutic and diagnostic reagents: problems and prospects. Curr Opin Chem Biol 1997, 1:5-9.
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 5-9
    • Osborne, S.E.1    Matsumura, I.2    Ellington, A.D.3
  • 2
    • 0031151974 scopus 로고    scopus 로고
    • The joys of in vitro selection: Chemically dressing oligonucleotides to satiate protein targets
    • Eaton BE: The joys of in vitro selection: chemically dressing oligonucleotides to satiate protein targets. Curr Opin Chem Biol 1997, 1:10-16.
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 10-16
    • Eaton, B.E.1
  • 3
    • 0031151971 scopus 로고    scopus 로고
    • Novel and variant ribozymes obtained through in vitro selection
    • Pan T: Novel and variant ribozymes obtained through in vitro selection. Curr Opin Chem Biol 1997, 1:17-25.
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 17-25
    • Pan, T.1
  • 4
    • 0031151976 scopus 로고    scopus 로고
    • DNA aptamers and DNA enzymes
    • Breaker RR: DNA aptamers and DNA enzymes. Curr Opin Chem Biol 1997, 1:26-31.
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 26-31
    • Breaker, R.R.1
  • 5
    • 0031152162 scopus 로고    scopus 로고
    • Structural analysis of nucleic acid aptarners
    • Patel D: Structural analysis of nucleic acid aptarners. Curr Opin Chem Biol 1997, 1:32-46.
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 32-46
    • Patel, D.1
  • 6
    • 0031259915 scopus 로고    scopus 로고
    • Accessing rare activities from random RNA sequences: The importance of the length of molecules in the starting pool
    • Sabeti PC, Unrau PJ, Bartel DP: Accessing rare activities from random RNA sequences: the importance of the length of molecules in the starting pool. Chem Biol 1997, 4:767-774.
    • (1997) Chem Biol , vol.4 , pp. 767-774
    • Sabeti, P.C.1    Unrau, P.J.2    Bartel, D.P.3
  • 7
    • 0030799729 scopus 로고    scopus 로고
    • In vitro selection without intervening amplification
    • Smith J, Anslyn EV: In vitro selection without intervening amplification. Angew Chem Int Ed 1997, 36:1879-1881.
    • (1997) Angew Chem Int Ed , vol.36 , pp. 1879-1881
    • Smith, J.1    Anslyn, E.V.2
  • 8
    • 0031102380 scopus 로고    scopus 로고
    • Nucleic acid selection and the challenge of combinatorial chemistry
    • Osborne SE, Ellington AD: Nucleic acid selection and the challenge of combinatorial chemistry. Chem Rev 1997, 97:349-370. One of the most insightful and detailed views of aptamer technology that covers the research in the field up to the end of 1996.
    • (1997) Chem Rev , vol.97 , pp. 349-370
    • Osborne, S.E.1    Ellington, A.D.2
  • 9
    • 0030763907 scopus 로고    scopus 로고
    • RNA aptamers
    • Heus HA: RNA aptamers. Nat Struct Biol 1997, 4:597-600. This is an excellent and very comprehensive review that emphasizes the benefits of aptamer NMR structures for our knowledge of RNA-target recognition.
    • (1997) Nat Struct Biol , vol.4 , pp. 597-600
    • Heus, H.A.1
  • 10
    • 0031563817 scopus 로고    scopus 로고
    • Structure, recognition and adaptive binding in RNA aptamer complexes
    • Patel DJ, Suri AK, Jiang F, Jiang L, Fan P, Kumar RA, Nonin S: Structure, recognition and adaptive binding in RNA aptamer complexes. J Mol Biol 1997, 272:645-664. This well-written review provides an instructive discussion on the structural insights of RNA-aptamer and RNA-peptide complexes.
    • (1997) J Mol Biol , vol.272 , pp. 645-664
    • Patel, D.J.1    Suri, A.K.2    Jiang, F.3    Jiang, L.4    Fan, P.5    Kumar, R.A.6    Nonin, S.7
  • 11
    • 0030752211 scopus 로고    scopus 로고
    • Interlocking structural motifs mediate molecular discrimination by a theophylline-binding RNA
    • Zimmerman GR, Jenison RD, Wick CL, Simorre J-P, Hardi A: Interlocking structural motifs mediate molecular discrimination by a theophylline-binding RNA. Nat Struct Biol 1997, 4:644-649.
    • (1997) Nat Struct Biol , vol.4 , pp. 644-649
    • Zimmerman, G.R.1    Jenison, R.D.2    Wick, C.L.3    Simorre, J.-P.4    Hardi, A.5
  • 12
    • 0031279971 scopus 로고    scopus 로고
    • Structural basis of DNA folding and recognition in an AMP-DNA aptamer complex: Distinct architectures but common recognition motifs for DNA and RNA aptamers complexed to AMP
    • Lin CH, Patel DJ: Structural basis of DNA folding and recognition in an AMP-DNA aptamer complex: distinct architectures but common recognition motifs for DNA and RNA aptamers complexed to AMP. Chem Biol 1997, 4:817-832.
    • (1997) Chem Biol , vol.4 , pp. 817-832
    • Ch, L.1    Patel, D.J.2
  • 16
    • 0031965013 scopus 로고    scopus 로고
    • In vitro selection and characterization of streptomycin-binding RNAs: Recognition discrimination between antibiotics
    • Wallace ST, Schroeder R: In vitro selection and characterization of streptomycin-binding RNAs: Recognition discrimination between antibiotics. RNA 1998, 4:112-123.
    • (1998) RNA , vol.4 , pp. 112-123
    • Wallace, S.T.1    Schroeder, R.2
  • 17
    • 0030970582 scopus 로고    scopus 로고
    • 23S rRNA similarity from selection for peptidyl transferase mimicry
    • Welch M, Majerfeld I, Yarus M: 23S rRNA similarity from selection for peptidyl transferase mimicry. Biochemistry 1997, 36:6614-6623. This is a very interesting study that showed how in vitro selection of combinatorial RNA libraries can be applied to evolutionary questions. The secondary structures of the selected aptamers were carefully determined by lead cleavage and chemical modification/protection assays and sequence comparison, establishing aptamer similarity to the 23S rRNA peptidyl transferase loop.
    • (1997) Biochemistry , vol.36 , pp. 6614-6623
    • Welch, M.1    Majerfeld, I.2    Yarus, M.3
  • 18
    • 0030832285 scopus 로고    scopus 로고
    • In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules
    • Haller AA, Sarnow P: In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules. Proc Natl Acad Sci USA 1997, 94:8521-8526. An impressive example of a small-molecule-binding RNA aptamer that selectively blocks a biological process.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8521-8526
    • Haller, A.A.1    Sarnow, P.2
  • 19
    • 0030992812 scopus 로고    scopus 로고
    • The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo
    • Buckanovich RJ, Darnell RB: The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo. Mol Cell Biol 1997, 17:3194-3201. This beautiful work shows how in vitro selection experiments can be used to identify previously unknown natural nucleic acid binding sites of an RNA-binding protein. This work establishes the usefulness of in vitro selection of combinatorial RNA libraries for the identification of biologically relevant RNA-protein interactions.
    • (1997) Mol Cell Biol , vol.17 , pp. 3194-3201
    • Buckanovich, R.J.1    Darnell, R.B.2
  • 20
    • 0030920331 scopus 로고    scopus 로고
    • RNA recognition by the human polyadenylation factor CstF
    • Takagaki Y, Manley JL: RNA recognition by the human polyadenylation factor CstF. Mol Cell Biol 1997, 17:3907-3914.
    • (1997) Mol Cell Biol , vol.17 , pp. 3907-3914
    • Takagaki, Y.1    Manley, J.L.2
  • 21
    • 0031005029 scopus 로고    scopus 로고
    • Single-stranded RNA recognition by the bacteriophage T4 transitional repressor, regA
    • Brown D, Brown J, Kang C, Gold L, Allen P: Single-stranded RNA recognition by the bacteriophage T4 transitional repressor, regA. J Biol Chem 1997, 272:14969-14974.
    • (1997) J Biol Chem , vol.272 , pp. 14969-14974
    • Brown, D.1    Brown, J.2    Kang, C.3    Gold, L.4    Allen, P.5
  • 22
    • 0030988942 scopus 로고    scopus 로고
    • Identification of a new class of exonic splicing enhancers by in vivo selection
    • Coulter LR, Landree MA, Cooper TA: Identification of a new class of exonic splicing enhancers by in vivo selection. Mol Cell Biol 1997, 17:2143-2150.
    • (1997) Mol Cell Biol , vol.17 , pp. 2143-2150
    • Coulter, L.R.1    Ma, L.2    Cooper, T.A.3
  • 23
    • 0031039644 scopus 로고    scopus 로고
    • In vivo selection of RNAs that localize in the nucleus
    • Grimm C, Lund E, Dahlberg JE: In vivo selection of RNAs that localize in the nucleus. EMBO J 1997, 16:793-806. This paper elegantly shows how selections of combinatorial sequence pools in vivo can be designed and carried out to identify RNA sequences that serve as signals for nuclear localization.
    • (1997) EMBO J , vol.16 , pp. 793-806
    • Grimm, C.1    Lund, E.2    Dahlberg, J.E.3
  • 24
    • 0030984433 scopus 로고    scopus 로고
    • Selecton and nuclear immobilization of exportable RNAs
    • Grimm C, Lund E, Dahlberg JE: Selecton and nuclear immobilization of exportable RNAs. Proc Natl Acad Sci USA 1997, 94:10122-10127.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10122-10127
    • Grimm, C.1    Lund, E.2    Dahlberg, J.E.3
  • 25
    • 0030666827 scopus 로고    scopus 로고
    • Anti-idiotype RNA selected with an anti-nuclear export signal antibody is actively transported in oocytes and inhibits Rev- and cap-dependent RNA export
    • Hamm J, Huber J, Lührmann R: Anti-idiotype RNA selected with an anti-nuclear export signal antibody is actively transported in oocytes and inhibits Rev- and cap-dependent RNA export. Proc Natl Acad Sci USA 1997, 94:12839-12844. This paper describes an anti-idiotype selection approach based on the assumption that an antibody specific for a receptor-binding domain of a ligand could be structurally related to the receptor. The study shows that an aptamer, selected with an anti-ligand antibody, can serve as structural mimic of a receptor-binding domain and is thus a functional substrate for the receptor.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12839-12844
    • Hamm, J.1    Huber, J.2    Lührmann, R.3
  • 26
    • 0029931691 scopus 로고    scopus 로고
    • Characterisation of antibody-binding RNAs selected from structurally constrained libraries
    • Hamm J: Characterisation of antibody-binding RNAs selected from structurally constrained libraries. Nucleic Acids Res 1996, 24:2220-2227.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2220-2227
    • Hamm, J.1
  • 27
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer U, Huber J, Boelens WC, Mattaj IW, Lührmann R: The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 1995, 82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührmann, R.5
  • 28
    • 0031010402 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SeIB
    • Klug SJ, Hüttenhofer A, Kromayer M, Famulok M: In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SeIB. Proc Natl Acad Sci USA 1997, 94:6676-6681. In this paper the biological function of a mRNA element required for selenocysteine incorporation into selenoproteins was dissected from simple binding features by means of in vitro selection of an RNA library.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6676-6681
    • Klug, S.J.1    Hüttenhofer, A.2    Kromayer, M.3    Famulok, M.4
  • 30
    • 0025341614 scopus 로고
    • Features of the formate dehydrogenase mRNA neccessary for decoding of the UGA codon as selenocysteine
    • Zinoni F, Heider J, Böck A: Features of the formate dehydrogenase mRNA neccessary for decoding of the UGA codon as selenocysteine. Proc Natl Acad Sci USA 1990, 87:4660-4664.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4660-4664
    • Zinoni, F.1    Heider, J.2    Böck, A.3
  • 31
    • 1842298127 scopus 로고    scopus 로고
    • Selective targeting and inhibition of yeast RNA polymerase II by RNA aptamers
    • Thomas M, Chédin S, Carles C, Riva M, Famulok M, Sentenac A: Selective targeting and inhibition of yeast RNA polymerase II by RNA aptamers. J Biol Chem 1997, 272:27980-27986.
    • (1997) J Biol Chem , vol.272 , pp. 27980-27986
    • Thomas, M.1    Chédin, S.2    Carles, C.3    Riva, M.4    Famulok, M.5    Sentenac, A.6
  • 32
    • 0031031521 scopus 로고    scopus 로고
    • Isolation of a nuclease-resistant decoy RNA that can protect human acetylcholine receptors from Myasthenic antibodies
    • Lee S-W, Sullenger BA: Isolation of a nuclease-resistant decoy RNA that can protect human acetylcholine receptors from Myasthenic antibodies. Nat Biotechnol 1997, 15:41-45. A nuclease-resistant aptamer is described that binds autoantibodies from patients with Myasthenia gravis. The antibody recognizes the main immunogenic region of the acetylcholine receptor. Thus, the RNA acts as a decoy and protects acetylcholine receptors on human cells from the effects of these autoantibodies.
    • (1997) Nat Biotechnol , vol.15 , pp. 41-45
    • Lee, S.-W.1    Sullenger, B.A.2
  • 33
    • 0031183804 scopus 로고    scopus 로고
    • Isolation and characterization of 2′-fluoro-, 2′-amino-, and 2′-fluoro-/amino-modified RNA ligands to human IFN-γ that inhibit receptor binding
    • Kubik MF, Bell C, Fitzwater T, Watson SR, Tasset DM: Isolation and characterization of 2′-fluoro-, 2′-amino-, and 2′-fluoro-/amino-modified RNA ligands to human IFN-γ that inhibit receptor binding. J Immunol 1997, 159:259-267.
    • (1997) J Immunol , vol.159 , pp. 259-267
    • Kubik, M.F.1    Bell, C.2    Fitzwater, T.3    Watson, S.R.4    Tasset, D.M.5
  • 36
    • 84984776641 scopus 로고    scopus 로고
    • Reflections on mirrors
    • Gold L: Reflections on mirrors. Nat Biotechnol 1996, 14:1080.
    • (1996) Nat Biotechnol , vol.14 , pp. 1080
    • Gold, L.1
  • 37
    • 0030803754 scopus 로고    scopus 로고
    • Bioactive and nuclease-resistant L-DNA ligand of vasopressin
    • Williams KP, Liu XH, Schumacher TN, Lin HY, Ausiello DA, Kim PS, Bartel DP: Bioactive and nuclease-resistant L-DNA ligand of vasopressin. Proc Natl Acad Sci USA 1997, 94:11285-11290. A paper that is somewhat related to the studies described in [34,35]. In contrast to these previous studies, however, an L-DNA ligand which is entirely stable in biological materials is described that recognizes the antidiuretic peptide hormone vasopressin.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11285-11290
    • Kp, W.1    Liu, X.H.2    Schumacher, T.N.3    Lin, H.Y.4    Ausiello, D.A.5    Kim, P.S.6    Bartel, D.P.7
  • 38
    • 0029395440 scopus 로고
    • In vitro selection of RNA-based irreversible inhibitors of human neutrophil elastase
    • Smith D, Kirschenreuter GP, Charlton J, Guidot DM, Repine JE: In vitro selection of RNA-based irreversible inhibitors of human neutrophil elastase. Chem Biol 1995, 2:741-750.
    • (1995) Chem Biol , vol.2 , pp. 741-750
    • Smith, D.1    Kirschenreuter, G.P.2    Charlton, J.3    Guidot, D.M.4    Repine, J.E.5
  • 39
    • 0030889231 scopus 로고    scopus 로고
    • Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library
    • Charlton J, Kirschenheuter GP, Smith D: Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library. Biochemistry 1997, 36:3018-3026.
    • (1997) Biochemistry , vol.36 , pp. 3018-3026
    • Charlton, J.1    Kirschenheuter, G.P.2    Smith, D.3
  • 40
    • 0031282593 scopus 로고    scopus 로고
    • Protective effects of an aptamer inhibitor of neutrophil elastase in lung inflammatory injury
    • Bless NM, Smith D, Charlton J, Czermak BJ, Schmal H, Friedl HP, Ward PA: Protective effects of an aptamer inhibitor of neutrophil elastase in lung inflammatory injury. Curr Biol 1997, 7:877-880. This paper is among the first showing that aptamers can serve as drugs. A previously selected aptamer that strongly binds elastase in vitro, thereby preventing the enzyme from degrading connective tissue, was shown to block swelling and tissue damage in the lungs after injection into rat lungs. In rats that received the highest dose, blood leakage into the lung was 38% less than in control animals that did not receive the aptamer.
    • (1997) Curr Biol , vol.7 , pp. 877-880
    • Bless, N.M.1    Smith, D.2    Charlton, J.3    Czermak, B.J.4    Schmal, H.5    Friedl, H.P.6    Ward, P.A.7
  • 41
    • 0031279943 scopus 로고    scopus 로고
    • In vivo imaging of inflammation using an aptamer inhibitor of human neutrophil elastase
    • Charlton J, Sennello J, Smith D: In vivo imaging of inflammation using an aptamer inhibitor of human neutrophil elastase. Chem Biol 1997, 4:809-816. This is the first example demonstrating that aptamer technology can be used for in vivo diagnostic imaging. In this case, inflammation was visualized in a rat model by using a labeled aptamer in comparison with a clinically used diagnostic antibody. Compared to the antibody, the aptamer achieved a significantly higher target : background ratio, in less time.
    • (1997) Chem Biol , vol.4 , pp. 809-816
    • Charlton, J.1    Sennello, J.2    Smith, D.3
  • 43
    • 0030606308 scopus 로고    scopus 로고
    • Oligonucleotide inhibitors of Taq DNA polymerase facilitate detection of low copy number targets by PCR
    • Dang C, Jayasena SD: Oligonucleotide inhibitors of Taq DNA polymerase facilitate detection of low copy number targets by PCR. J Mol Biol 1996, 264:268-278.
    • (1996) J Mol Biol , vol.264 , pp. 268-278
    • Dang, C.1    Jayasena, S.D.2
  • 44
    • 0031559579 scopus 로고    scopus 로고
    • Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer
    • Lin Y, Jayasena SD: Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. J Mol Biol 1997, 271:100-111.
    • (1997) J Mol Biol , vol.271 , pp. 100-111
    • Lin, Y.1    Jayasena, S.D.2
  • 45
    • 0030996755 scopus 로고    scopus 로고
    • The new world of ribozymes
    • Jaeger L: The new world of ribozymes. Curr Opin Struct Biol 1997, 7:324-335.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 324-335
    • Jaeger, L.1
  • 46
    • 0000917638 scopus 로고    scopus 로고
    • In vitro selection of catalytic polynucleotides
    • Breaker RR: In vitro selection of catalytic polynucleotides. Chem Rev 1997, 97:371-390.
    • (1997) Chem Rev , vol.97 , pp. 371-390
    • Breaker, R.R.1
  • 47
  • 48
    • 0030968710 scopus 로고    scopus 로고
    • Mechanistic aspects of enzymatic catalysis: Lessons from comparison of RNA and protein enzymes
    • Narlikar GJ, Herschlag D: Mechanistic aspects of enzymatic catalysis: lessons from comparison of RNA and protein enzymes. Annu Rev Biochem 1997, 66:19-59. This is an excellent review that gives insight into differences and common features of nucleic acid- and protein-catalyzed reactions.
    • (1997) Annu Rev Biochem , vol.66 , pp. 19-59
    • Narlikar, G.J.1    Herschlag, D.2
  • 49
    • 0346933372 scopus 로고    scopus 로고
    • Synthetic ribozymes and deoxyribozymes
    • Edited by Waldmann H, Mulzer J. Weinheim: Wiley-VCH; in press
    • Burgstaller P, Famulok M: Synthetic ribozymes and deoxyribozymes. In Organic Synthesis Highlights vol 3. Edited by Waldmann H, Mulzer J. Weinheim: Wiley-VCH; 1998:in press.
    • (1998) Organic Synthesis Highlights , vol.3
    • Burgstaller, P.1    Famulok, M.2
  • 50
    • 0030963855 scopus 로고    scopus 로고
    • RNA-catalysed carbon-carbon bond formation
    • Tarasow TM, Tarasow SL, Eaton BE: RNA-catalysed carbon-carbon bond formation. Nature 1997, 389:54-57. This paper describes a ribozyme that expands the scope of RNA catalyzed reactions to C-C bond formation. The ribozyme catalyzes a Diels-Alder reaction and was isolated by a direct selection approach from an RNA library in which every library member was derivatized with the diene at the 5′ end. The dienophile substrate contained a biotin moiety that became covalently linked to any catalylically active RNA in the pool, allowing separation from nonactive RNAs via streptavidin chromatography.
    • (1997) Nature , vol.389 , pp. 54-57
    • Tarasow, T.M.1    Tarasow, S.L.2    Eaton, B.E.3
  • 51
    • 0029956108 scopus 로고    scopus 로고
    • Ribozyme-catalysed amino acid transfer reactions
    • Lohse PA, Szostak JW: Ribozyme-catalysed amino acid transfer reactions. Nature 1996, 381:442-446.
    • (1996) Nature , vol.381 , pp. 442-446
    • Lohse, P.A.1    Szostak, J.W.2
  • 53
    • 0030688863 scopus 로고    scopus 로고
    • Peptide bond formation by in vitro selected ribozyme
    • ■]: a biotinylated methionine, esterified to the 2′/3′-CH of AMP, was substrate for an RNA derivatized at the 5′ end with phenylalanine containing a free α-amino group. In active RNAs, attack of the α-amino group at the biotinyl-methionyl-AMP-ester transferred the biotinylated amino acid onto the 5′ end of the RNA.
    • (1997) Nature , vol.390 , pp. 96-100
    • Zhang, B.1    Cech, T.R.2
  • 54
    • 0031882441 scopus 로고    scopus 로고
    • A novel ribozyme with ester transferase activity
    • Jenne A, Famulok M: A novel ribozyme with ester transferase activity. Chem Biol 1998, 5:23-34.
    • (1998) Chem Biol , vol.5 , pp. 23-34
    • Jenne, A.1    Famulok, M.2
  • 55
    • 0031215080 scopus 로고    scopus 로고
    • Isolation of novel ribozymes that ligate AMP-activated RNA substrates
    • Hager AJ, Szostak JW: Isolation of novel ribozymes that ligate AMP-activated RNA substrates. Chem Biol 1997, 4:607-618.
    • (1997) Chem Biol , vol.4 , pp. 607-618
    • Hager, A.J.1    Szostak, J.W.2
  • 56
    • 0030745635 scopus 로고    scopus 로고
    • Versatile 5′ phosphoryl coupling of small and large molecules to an RNA
    • Huang F, Yarus M: Versatile 5′ phosphoryl coupling of small and large molecules to an RNA. Proc Natl Acad Sci USA 1997, 94:8965-8969.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8965-8969
    • Huang, F.1    Yarus, M.2
  • 57
    • 0030987545 scopus 로고    scopus 로고
    • In vitro selection of self-cleaving RNAs with a low pH optimum
    • Jayasena VK, Gold L: In vitro selection of self-cleaving RNAs with a low pH optimum. Proc Natl Acad Sci USA 1997, 94:10612-10617.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10612-10617
    • Jayasena, V.K.1    Gold, L.2
  • 58
    • 0030976198 scopus 로고    scopus 로고
    • Isolation of hammerhead ribozymes with altered core sequences by in vitro selection
    • Vaish NK, Heaton PA, Eckstein F: Isolation of hammerhead ribozymes with altered core sequences by in vitro selection. Biochemistry 1997, 36:6495-6501.
    • (1997) Biochemistry , vol.36 , pp. 6495-6501
    • Vaish, N.K.1    Heaton, P.A.2    Eckstein, F.3
  • 59
    • 0030901131 scopus 로고    scopus 로고
    • Continuous in vitro evolution of catalytic function
    • Wright MC, Joyce GF: Continuous in vitro evolution of catalytic function. Science 1997, 276:614-617. A continous in vitro evolution scheme similar to the Qβ-replicase system was developed, but the actual catalytic step is carried out by a ribozyme. Continuous evolution was performed by carrying out 100 serial transfers into reaction vessels containing a mix of substrate, 3′ primer, dNTPs, NTPs, reverse transcriptase and T7 RNA polymerase. Approximately 300 cycles of catalysis and amplification were achieved within less than two days. This system might be used to develop a ribozyme with RNA polymerase activity that, perhaps, some day will make the use of a proteinaceous RNA polymerase obsolete.
    • (1997) Science , vol.276 , pp. 614-617
    • Wright, M.C.1    Joyce, G.F.2
  • 60
    • 0342697544 scopus 로고    scopus 로고
    • Libraries of multifunctional RNA conjugates for the selection of new RNA catalysts
    • Hausch F, Jäschke A: Libraries of multifunctional RNA conjugates for the selection of new RNA catalysts. Bioconjugate Chem 1997, 8:885-890.
    • (1997) Bioconjugate Chem , vol.8 , pp. 885-890
    • Hausch, F.1    Jäschke, A.2
  • 61
    • 0030794322 scopus 로고    scopus 로고
    • Cofactor dependent self-cleavage of DNA-libraries with a 3′-5′-phosphoramidate bond
    • Burmeister J, von Kiedrowski G, Ellington AD: Cofactor dependent self-cleavage of DNA-libraries with a 3′-5′-phosphoramidate bond. Angew Chem Int Ed 1997, 36:1321-1324.
    • (1997) Angew Chem Int Ed , vol.36 , pp. 1321-1324
    • Burmeister, J.1    Von Kiedrowski, G.2    Ellington, A.D.3
  • 62
    • 0030954291 scopus 로고    scopus 로고
    • Toward an efficient DNAzyme
    • Li Y, Sen D: Toward an efficient DNAzyme. Biochemistry 1997, 36:5589-5599.
    • (1997) Biochemistry , vol.36 , pp. 5589-5599
    • Li, Y.1    Sen, D.2
  • 63
    • 0031931019 scopus 로고    scopus 로고
    • The modus operandi of a DNA enzyme: Enhancement of substrate basicity
    • Li Y, Sen D: The modus operandi of a DNA enzyme: enhancement of substrate basicity. Chem Biol 1998, 5:1-12.
    • (1998) Chem Biol , vol.5 , pp. 1-12
    • Li, Y.1    Sen, D.2
  • 64
    • 0031556016 scopus 로고    scopus 로고
    • Characterization and divalent metal-ion dependence of in vitro selected deoxyribozymes which cleave DNA/RNA chimeric oligonucleotides
    • Faulhammer D, Famulok M: Characterization and divalent metal-ion dependence of in vitro selected deoxyribozymes which cleave DNA/RNA chimeric oligonucleotides. J Mol Biol 1997, 274:188-201.
    • (1997) J Mol Biol , vol.274 , pp. 188-201
    • Faulhammer, D.1    Famulok, M.2
  • 65
    • 0031215119 scopus 로고    scopus 로고
    • Evidence for the metal-cofactor independence of an RNA phosphodiester-cleaving DNA enzyme
    • Geyer CR, Sen D: Evidence for the metal-cofactor independence of an RNA phosphodiester-cleaving DNA enzyme. Chem Biol 1997, 4:579-594.
    • (1997) Chem Biol , vol.4 , pp. 579-594
    • Geyer, C.R.1    Sen, D.2
  • 66
    • 0030898510 scopus 로고    scopus 로고
    • A general purpose RNA-cleaving DNA enzyme
    • Santoro SW, Joyce GF: A general purpose RNA-cleaving DNA enzyme. Proc Natl Acad Sci USA 1997, 94:4262-4266. A beautiful example of a very short DNAzyme that can cleave any RNA target with multiple turnover and high efficiency. When incorporated into antisense oligonucleotides the 15-mer DNA sequence should lead to active RNA-cleaving oligonucleotides.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4262-4266
    • Santoro, S.W.1    Joyce, G.F.2
  • 67
    • 0031171217 scopus 로고    scopus 로고
    • Rational design of allosteric ribozymes
    • Tang J, Breaker RR: Rational design of allosteric ribozymes. Chem Biol 1997, 4:453-459. A most impressive example of rational ribozyme engineering. The incorporation of aptamer sequences into the hammerhead ribozyme led to ribozyme variants that performed catalytic activity as a function of the presence or absence of aptamer ligand.
    • (1997) Chem Biol , vol.4 , pp. 453-459
    • Tang, J.1    Breaker, R.R.2
  • 68
    • 0030810710 scopus 로고    scopus 로고
    • Examination of the catalytic fitness of the hammerhead ribozyme by in vitro selection
    • Tang J, Breaker RR: Examination of the catalytic fitness of the hammerhead ribozyme by in vitro selection. RNA 1997, 3:914-925.
    • (1997) RNA , vol.3 , pp. 914-925
    • Tang, J.1    Breaker, R.R.2
  • 69
    • 0030250840 scopus 로고    scopus 로고
    • Ribozymes: Aiming at RNA replication and protein synthesis
    • Hager AJ, Pollard JD, Szostak JW: Ribozymes: aiming at RNA replication and protein synthesis. Chem Biol 1996, 3:717-725.
    • (1996) Chem Biol , vol.3 , pp. 717-725
    • Hager, A.J.1    Pollard, J.D.2    Szostak, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.