-
1
-
-
0028869690
-
Diversity of oligonucleotide function
-
of special interest. An exhaustive review of RNA aptamers and the techniques used to create them.
-
Gold L, Polisky B, Uhlenbeck O, Yarus M. Diversity of oligonucleotide function. of special interest Annu Rev Biochem. 64:1995;763-797 An exhaustive review of RNA aptamers and the techniques used to create them.
-
(1995)
Annu Rev Biochem
, vol.64
, pp. 763-797
-
-
Gold, L.1
Polisky, B.2
Uhlenbeck, O.3
Yarus, M.4
-
2
-
-
0029031094
-
Oligonucleotides as research, diagnostic, and therapeutic agents
-
Gold L. Oligonucleotides as research, diagnostic, and therapeutic agents. J Biol Chem. 270:1995;13581-13584.
-
(1995)
J Biol Chem
, vol.270
, pp. 13581-13584
-
-
Gold, L.1
-
3
-
-
0029360503
-
Re-creating the RNA World
-
of special interest. A review of the RNA World theory that explains why this theory has fostered efforts to design new functional RNAs via in vitro selection and how these methods are now being employed to test emerging theories of a metabolic state that was maintained in the absence of proteins and DNA.
-
Hirao I, Ellington AD. Re-creating the RNA World. of special interest Curr Biol. 6:1995;1017-1022 A review of the RNA World theory that explains why this theory has fostered efforts to design new functional RNAs via in vitro selection and how these methods are now being employed to test emerging theories of a metabolic state that was maintained in the absence of proteins and DNA.
-
(1995)
Curr Biol
, vol.6
, pp. 1017-1022
-
-
Hirao, I.1
Ellington, A.D.2
-
4
-
-
0028472621
-
Inventing and improving ribozyme function: Rational design versus iterative selection methods
-
Breaker RR, Joyce JF. Inventing and improving ribozyme function: rational design versus iterative selection methods. Trends Biotechnol. 12:1994;268-275.
-
(1994)
Trends Biotechnol
, vol.12
, pp. 268-275
-
-
Breaker, R.R.1
Joyce, J.F.2
-
5
-
-
0028842989
-
Synthetic ribozymes and the first deoxyribozyme
-
Int Ed
-
Burgstaller P, Famulok M. Synthetic ribozymes and the first deoxyribozyme. Int Ed Angew Chem. 34:1995;1189-1192.
-
(1995)
Angew Chem
, vol.34
, pp. 1189-1192
-
-
Burgstaller, P.1
Famulok, M.2
-
6
-
-
0029119820
-
Artificial evolution and natural ribozymes
-
Kumar PKR, Ellington AD. Artificial evolution and natural ribozymes. FASEB J. 9:1995;1183-1195.
-
(1995)
FASEB J
, vol.9
, pp. 1183-1195
-
-
Kumar, P.K.R.1
Ellington, A.D.2
-
7
-
-
0029042615
-
Ribozymes as human therapeutic agents
-
of special interest. An overview of the challenges facing those who are engineering self-cleaving ribozymes to operate as therapeutic agents.
-
Christoffersen RE, Marr JJ. Ribozymes as human therapeutic agents. of special interest J Med Chem. 38:1995;2023-2037 An overview of the challenges facing those who are engineering self-cleaving ribozymes to operate as therapeutic agents.
-
(1995)
J Med Chem
, vol.38
, pp. 2023-2037
-
-
Christoffersen, R.E.1
Marr, J.J.2
-
8
-
-
0029011972
-
A secondary-structure model for the self-cleaving region of Neurospora VS RNA
-
of special interest. A model of the secondary structure for the Neurospora VS self-cleaving RNA is proposed. Site-directed mutagenesis and chemical structure probing data are used to support the presence of six different hairpins and helical regions.
-
Beattie TL, Olive JE, Collins RA. A secondary-structure model for the self-cleaving region of Neurospora VS RNA. of special interest Proc Natl Acad Sci USA. 92:1995;4686-4690 A model of the secondary structure for the Neurospora VS self-cleaving RNA is proposed. Site-directed mutagenesis and chemical structure probing data are used to support the presence of six different hairpins and helical regions.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 4686-4690
-
-
Beattie, T.L.1
Olive, J.E.2
Collins, R.A.3
-
9
-
-
0028855671
-
Efficient trans-cleavage of a stem-loop RNA substrate by a ribozyme derived from Neurospora VS RNA
-
of special interest. The Neurospora VS ribozyme is reformulated into separate `substrate' and `enzyme' domains. Like the group I ribozyme, this enzyme appears not to exclusively rely on base-pairing interactions to bind the substrate domain, but uses sequence-specific tertiary contacts to dock a double-helical substrate, cleaving the target RNA phosphoester residing adjacent to a stem-loop structure.
-
Guo HCT, Collins RA. Efficient trans-cleavage of a stem-loop RNA substrate by a ribozyme derived from Neurospora VS RNA. of special interest EMBO J. 14:1995;363-376 The Neurospora VS ribozyme is reformulated into separate `substrate' and `enzyme' domains. Like the group I ribozyme, this enzyme appears not to exclusively rely on base-pairing interactions to bind the substrate domain, but uses sequence-specific tertiary contacts to dock a double-helical substrate, cleaving the target RNA phosphoester residing adjacent to a stem-loop structure.
-
(1995)
EMBO J
, vol.14
, pp. 363-376
-
-
Guo, H.C.T.1
Collins, R.A.2
-
10
-
-
0028943217
-
Selection of efficient cleavage sites in target RNAs by using a ribozyme expression library
-
Lieber A, Strauss M. Selection of efficient cleavage sites in target RNAs by using a ribozyme expression library. Mol Cell Biol. 15:1995;540-551.
-
(1995)
Mol Cell Biol
, vol.15
, pp. 540-551
-
-
Lieber, A.1
Strauss, M.2
-
11
-
-
0028817431
-
Substrate recognition by human RNase P: Identification of small, model substrates for the enzyme
-
Yuan Y, Altman S. Substrate recognition by human RNase P: identification of small, model substrates for the enzyme. EMBO J. 14:1995;159-168.
-
(1995)
EMBO J
, vol.14
, pp. 159-168
-
-
Yuan, Y.1
Altman, S.2
-
12
-
-
0029025035
-
Novel RNA substrates for the ribozyme from Bacillus subtilis ribonuclease P identified by in vitro selection
-
Pan T. Novel RNA substrates for the ribozyme from Bacillus subtilis ribonuclease P identified by in vitro selection. Biochemistry. 34:1995;8458-8464.
-
(1995)
Biochemistry
, vol.34
, pp. 8458-8464
-
-
Pan, T.1
-
13
-
-
0029143916
-
Isolation of active ribozymes from an RNA pool of random sequences using an anchored substrate RNA
-
Ishizaka M, Ohshima Y, Yani T. Isolation of active ribozymes from an RNA pool of random sequences using an anchored substrate RNA. Biochem Biophys Res Commun. 214:1995;403-409.
-
(1995)
Biochem Biophys Res Commun
, vol.214
, pp. 403-409
-
-
Ishizaka, M.1
Ohshima, Y.2
Yani, T.3
-
15
-
-
0029151591
-
Synthesis, deprotection, analysis and purification of RNA and ribozymes
-
of special interest. A description of methodological improvements for various steps of RNA synthesis, including coupling activation, coupling times, base and 2′-hydorxyl deprotection, and RNA product purification.
-
Wincott F, DiRenzo A, Shaffer C, Grimm S, Tracz D, Workman C, Sweedler D, Gonzalez C, Scaringe S, Usman N. Synthesis, deprotection, analysis and purification of RNA and ribozymes. of special interest Nucleic Acids Res. 23:1995;2677-2684 A description of methodological improvements for various steps of RNA synthesis, including coupling activation, coupling times, base and 2′-hydorxyl deprotection, and RNA product purification.
-
(1995)
Nucleic Acids Res
, vol.23
, pp. 2677-2684
-
-
Wincott, F.1
DiRenzo, A.2
Shaffer, C.3
Grimm, S.4
Tracz, D.5
Workman, C.6
Sweedler, D.7
Gonzalez, C.8
Scaringe, S.9
Usman, N.10
-
16
-
-
0028968617
-
Total chemical synthesis of a ribozyme derived from a group I intron
-
Whoriskey SK, Usman N, Szostak JW. Total chemical synthesis of a ribozyme derived from a group I intron. Proc Natl Acad Sci USA. 92:1995;2465-2469.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 2465-2469
-
-
Whoriskey, S.K.1
Usman, N.2
Szostak, J.W.3
-
17
-
-
0028932288
-
Comparative analysis of cleavage rates after systematic permutation of the NUX consensus target motif for hammerhead ribozymes
-
Zoumadakis M, Tabler M. Comparative analysis of cleavage rates after systematic permutation of the NUX consensus target motif for hammerhead ribozymes. Nucleic Acids Res. 23:1995;1192-1196.
-
(1995)
Nucleic Acids Res
, vol.23
, pp. 1192-1196
-
-
Zoumadakis, M.1
Tabler, M.2
-
18
-
-
0028905538
-
Generality of the NUX rule: Kinetic analysis of the results of systematic mutations in the trinucleotide at the cleavage site of hammerhead ribozymes
-
Shimayama T, Nishikawa S, Taira K. Generality of the NUX rule: kinetic analysis of the results of systematic mutations in the trinucleotide at the cleavage site of hammerhead ribozymes. Biochemistry. 34:1995;3649-3654.
-
(1995)
Biochemistry
, vol.34
, pp. 3649-3654
-
-
Shimayama, T.1
Nishikawa, S.2
Taira, K.3
-
19
-
-
0029041941
-
The effect of base mismatches in the substrate recognition helicies of hammerhead ribozymes on binding and catalysis
-
Werner M, Uhlenbeck OC. The effect of base mismatches in the substrate recognition helicies of hammerhead ribozymes on binding and catalysis. Nucleic Acids Res. 23:1995;2092-2096.
-
(1995)
Nucleic Acids Res
, vol.23
, pp. 2092-2096
-
-
Werner, M.1
Uhlenbeck, O.C.2
-
21
-
-
0028955347
-
Minor groove recognition of the conserved G-U pair at the Tetrahymena ribozyme reaction site
-
of outstanding interest. Functional-group mutagenesis is systematically used to examine the contributions of various functionalities to the recognition of the cleavage site of a group I ribozyme.
-
Strobel SA, Cech TR. Minor groove recognition of the conserved G-U pair at the Tetrahymena ribozyme reaction site. of outstanding interest Science. 267:1995;675-679 Functional-group mutagenesis is systematically used to examine the contributions of various functionalities to the recognition of the cleavage site of a group I ribozyme.
-
(1995)
Science
, vol.267
, pp. 675-679
-
-
Strobel, S.A.1
Cech, T.R.2
-
22
-
-
0028903816
-
Purine functional groups in essential residues of the hairpin ribozyme required for catalytic cleavage on RNA
-
Grasby JA, Mersmann K, Singh M, Gait M. Purine functional groups in essential residues of the hairpin ribozyme required for catalytic cleavage on RNA. Biochemistry. 34:1995;4068-4076.
-
(1995)
Biochemistry
, vol.34
, pp. 4068-4076
-
-
Grasby, J.A.1
Mersmann, K.2
Singh, M.3
Gait, M.4
-
23
-
-
0028858581
-
Chemical modification of hammerhead ribozymes
-
5-fold larger.
-
5-fold larger.
-
(1995)
J Biol Chem
, vol.270
, pp. 25702-25708
-
-
Beigelman, L.1
McSwiggen, J.A.2
Draper, K.G.3
Gonzalez, C.4
Jensen, K.5
Karpeisky, A.M.6
Modak, S.S.7
Matulic-Adamic, J.8
DiRenzo, A.B.9
Haeberli, P.10
-
24
-
-
0028811147
-
Synthesis of 2′-modified nucleotides and their incorporation into hammerhead ribozymes
-
Beigelman L, Karpeisky AM, Matulic-Adamic J, Haeberli P, Sweedler D, Usman N. Synthesis of 2′-modified nucleotides and their incorporation into hammerhead ribozymes. Nucleic Acids Res. 23:1995;4434-4442.
-
(1995)
Nucleic Acids Res
, vol.23
, pp. 4434-4442
-
-
Beigelman, L.1
Karpeisky, A.M.2
Matulic-Adamic, J.3
Haeberli, P.4
Sweedler, D.5
Usman, N.6
-
25
-
-
0028881857
-
An oligodeoxyribonucleotide that supports catalytic activity in the hammerhead ribozyme domain
-
Chartrand R, Harvey SC, Ferbeyre G, Usman N, Cedergren R. An oligodeoxyribonucleotide that supports catalytic activity in the hammerhead ribozyme domain. Nucleic Acids Res. 23:1995;4092-4096.
-
(1995)
Nucleic Acids Res
, vol.23
, pp. 4092-4096
-
-
Chartrand, R.1
Harvey, S.C.2
Ferbeyre, G.3
Usman, N.4
Cedergren, R.5
-
27
-
-
0028875594
-
Kinetic and thermodynamic characterization of the reaction catalyzed by a polynucleotide kinase ribozyme
-
Lorsch JR, Szostak JW. Kinetic and thermodynamic characterization of the reaction catalyzed by a polynucleotide kinase ribozyme. Biochemistry. 34:1995;15315-15327.
-
(1995)
Biochemistry
, vol.34
, pp. 15315-15327
-
-
Lorsch, J.R.1
Szostak, J.W.2
-
28
-
-
0029044353
-
Self-incorporation of coenzymes by ribozymes
-
Breaker RR, Joyce GF. Self-incorporation of coenzymes by ribozymes. J Mol Evol. 40:1995;551-558.
-
(1995)
J Mol Evol
, vol.40
, pp. 551-558
-
-
Breaker, R.R.1
Joyce, G.F.2
-
29
-
-
0029149905
-
RNA folding
-
of special interest. A recent overview of the progress made in understanding RNA folding.
-
Pyle AM, Green JB. RNA folding. of special interest Curr Biol. 5:1995;303-310 A recent overview of the progress made in understanding RNA folding.
-
(1995)
Curr Biol
, vol.5
, pp. 303-310
-
-
Pyle, A.M.1
Green, J.B.2
-
30
-
-
0029100264
-
Relative orientation of RNA helices in a group I ribozyme determined by helix extension electron microscopy
-
of special interest. A unique method of determining RNA tertiary-structure constraints using engineered ribozymes and electron microscopy. Helix orientations determined by this method for the group I ribozyme indicate that the ribozyme maintains significant conformational flexibility, but are consistent with a tertiary-structure model based on phylogenetic analyses.
-
Nakamura TM, Wang Y, Zaug AJ, Griffith JD, Cech TR. Relative orientation of RNA helices in a group I ribozyme determined by helix extension electron microscopy. of special interest EMBO J. 14:1995;4849-4859 A unique method of determining RNA tertiary-structure constraints using engineered ribozymes and electron microscopy. Helix orientations determined by this method for the group I ribozyme indicate that the ribozyme maintains significant conformational flexibility, but are consistent with a tertiary-structure model based on phylogenetic analyses.
-
(1995)
EMBO J
, vol.14
, pp. 4849-4859
-
-
Nakamura, T.M.1
Wang, Y.2
Zaug, A.J.3
Griffith, J.D.4
Cech, T.R.5
-
31
-
-
0029073091
-
The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage
-
2+ binding sites in the RNA structure and implicate one as the catalytic metal ion.
-
2+ binding sites in the RNA structure and implicate one as the catalytic metal ion.
-
(1995)
Cell
, vol.81
, pp. 991-1002
-
-
Scott, W.G.1
Finch, J.T.2
Klug, A.3
-
32
-
-
0028921811
-
Frequent use of the same tertiary motif by self-folding RNAs
-
of outstanding interest. The authors have identified an RNA tertiary-structure motif that occurs with surprising frequency in complex ribozyme structures. This motif, involving the interaction of a GNRA tetraloop with a conserved 11-nucleotide internal bulge, was used to engineer a group I ribozyme that displayed improved kinetic parameters.
-
Costa M, Michel F. Frequent use of the same tertiary motif by self-folding RNAs. of outstanding interest EMBO J. 14:1995;1276-1285 The authors have identified an RNA tertiary-structure motif that occurs with surprising frequency in complex ribozyme structures. This motif, involving the interaction of a GNRA tetraloop with a conserved 11-nucleotide internal bulge, was used to engineer a group I ribozyme that displayed improved kinetic parameters.
-
(1995)
EMBO J
, vol.14
, pp. 1276-1285
-
-
Costa, M.1
Michel, F.2
-
33
-
-
0029670279
-
Catalytic role of 2′-hydroxyl groups within a group II intron active site
-
of special interest. See annotation [34].
-
Abamovitz DL, Friedman RA, Pyle AM. Catalytic role of 2′-hydroxyl groups within a group II intron active site. of special interest Science. 271:1996;1410-1413 See annotation [34].
-
(1996)
Science
, vol.271
, pp. 1410-1413
-
-
Abamovitz, D.L.1
Friedman, R.A.2
Pyle, A.M.3
-
34
-
-
0028904152
-
Conservation of a Group II intron into a new multiple-turnover ribozyme that selectively cleaves oligonucleotides: Elucidation of reaction mechanism and structure/function relationships
-
of special interest. In these papers [33,34], the authors have used an engineered multi-domain ribozyme to facilitate functional-group mutagenesis or to create a new ribozyme with multiple turnover capabilities.
-
Michels WJ Jr, Pyle AM. Conservation of a Group II intron into a new multiple-turnover ribozyme that selectively cleaves oligonucleotides: elucidation of reaction mechanism and structure/function relationships. of special interest Biochemistry. 34:1995;2965-2977 In these papers [33,34], the authors have used an engineered multi-domain ribozyme to facilitate functional-group mutagenesis or to create a new ribozyme with multiple turnover capabilities.
-
(1995)
Biochemistry
, vol.34
, pp. 2965-2977
-
-
Michels W.J., Jr.1
Pyle, A.M.2
-
35
-
-
0029563614
-
Reconstruction of hairpin ribozyme activity following separation of functional domains
-
Butcher SE, Heckman JE, Burke JM. Reconstruction of hairpin ribozyme activity following separation of functional domains. J Biol Chem. 270:1995;29648-29651.
-
(1995)
J Biol Chem
, vol.270
, pp. 29648-29651
-
-
Butcher, S.E.1
Heckman, J.E.2
Burke, J.M.3
-
36
-
-
0028945859
-
Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P
-
Pan T. Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P. Biochemistry. 34:1995;902-909.
-
(1995)
Biochemistry
, vol.34
, pp. 902-909
-
-
Pan, T.1
-
37
-
-
0029258956
-
Self-assembly of a group I intron active site from its components tertiary structural domains
-
Doudna JA, Cech TR. Self-assembly of a group I intron active site from its components tertiary structural domains. RNA. 1:1995;36-45.
-
(1995)
RNA
, vol.1
, pp. 36-45
-
-
Doudna, J.A.1
Cech, T.R.2
-
38
-
-
0028911157
-
Novel system for analysis of group I 3′ splice site reactions based on functional trans-interaction of the P1/P10 reaction helix with the ribozyme's catalytic core
-
Chowrira BM, Berzal-Herranz A, Burke JM. Novel system for analysis of group I 3′ splice site reactions based on functional trans-interaction of the P1/P10 reaction helix with the ribozyme's catalytic core. Nucleic Acids Res. 23:1995;849-855.
-
(1995)
Nucleic Acids Res
, vol.23
, pp. 849-855
-
-
Chowrira, B.M.1
Berzal-Herranz, A.2
Burke, J.M.3
-
39
-
-
0029163563
-
RNA chaperones and the RNA folding problem
-
of special interest. An excellent description of RNA-folding problems and an account of the arguments that implicate the importance and perhaps the common existence of `RNA chaperones' in nature. Unlike specific RNA-binding proteins, RNA chaperones are proteins that bind RNA is a relatively nonspecific fashion and that facilitate correct folding of RNA by reducing kinetic barriers between misfolded and properly folded structures.
-
Herschlag D. RNA chaperones and the RNA folding problem. of special interest J Biol Chem. 270:1995;20871-20874 An excellent description of RNA-folding problems and an account of the arguments that implicate the importance and perhaps the common existence of `RNA chaperones' in nature. Unlike specific RNA-binding proteins, RNA chaperones are proteins that bind RNA is a relatively nonspecific fashion and that facilitate correct folding of RNA by reducing kinetic barriers between misfolded and properly folded structures.
-
(1995)
J Biol Chem
, vol.270
, pp. 20871-20874
-
-
Herschlag, D.1
-
40
-
-
0029050588
-
Efficient protein-facilitated splicing of yeast mitochondrial b15 intron
-
See annotation [41].
-
Weeks KM, Cech TR. Efficient protein-facilitated splicing of yeast mitochondrial b15 intron. Biochemistry. 34:1995;7728-7738 See annotation [41].
-
(1995)
Biochemistry
, vol.34
, pp. 7728-7738
-
-
Weeks, K.M.1
Cech, T.R.2
-
41
-
-
0029155840
-
Protein facilitation of group I intron splicing by assembly of the catalytic core and the 5′ splice site domain
-
of special interest. These papers [40,41] comprise an extensive structural and kinetic analysis of protein-facilitated self-splicing reaction of a group I ribozyme.
-
Weeks KM, Cech TR. Protein facilitation of group I intron splicing by assembly of the catalytic core and the 5′ splice site domain. of special interest Cell. 82:1995;221-230 These papers [40,41] comprise an extensive structural and kinetic analysis of protein-facilitated self-splicing reaction of a group I ribozyme.
-
(1995)
Cell
, vol.82
, pp. 221-230
-
-
Weeks, K.M.1
Cech, T.R.2
-
42
-
-
0029076774
-
An improved version of the hairpin ribozyme functions as a ribonucleoprotein
-
of special interest. The authors have engineered a `hairpin' self-cleaving ribozyme to function unhindered as a ribonucleoprotein complex.
-
Sargueil B, Pecchia DB, Burke JM. An improved version of the hairpin ribozyme functions as a ribonucleoprotein. of special interest Biochemistry. 34:1995;7739-7748 The authors have engineered a `hairpin' self-cleaving ribozyme to function unhindered as a ribonucleoprotein complex.
-
(1995)
Biochemistry
, vol.34
, pp. 7739-7748
-
-
Sargueil, B.1
Pecchia, D.B.2
Burke, J.M.3
-
43
-
-
0030019353
-
Template-directed ligation of peptides to oligonucleotides
-
of special interest. Stable DNA - peptide conjugates are made by transferring a peptide, attached to a donor DNA via a thioester link, to an acceptor DNA that carries a 3′-terminal amine. Acceptor and donor DNAs are aligned on a DNA template to facilitate the formation of a new DNA - peptide conjugate that is linked by an amide bond.
-
Bruick RK, Dawson PE, Kent SBH, Usman N, Joyce GF. Template-directed ligation of peptides to oligonucleotides. of special interest Chem Biol. 3:1996;49-56 Stable DNA - peptide conjugates are made by transferring a peptide, attached to a donor DNA via a thioester link, to an acceptor DNA that carries a 3′-terminal amine. Acceptor and donor DNAs are aligned on a DNA template to facilitate the formation of a new DNA - peptide conjugate that is linked by an amide bond.
-
(1996)
Chem Biol
, vol.3
, pp. 49-56
-
-
Bruick, R.K.1
Dawson, P.E.2
Kent, S.B.H.3
Usman, N.4
Joyce, G.F.5
-
44
-
-
0028826936
-
Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition
-
of special interest. An improved neutrophil elastase inhibitor was made by conjugating a DNA aptamer with a tetrapeptide.
-
Lin Y, Padmapriya A, Morden KM, Jayasena SD. Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition. of special interest Proc Natl Acad Sci USA. 92:1995;11044-11048 An improved neutrophil elastase inhibitor was made by conjugating a DNA aptamer with a tetrapeptide.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 11044-11048
-
-
Lin, Y.1
Padmapriya, A.2
Morden, K.M.3
Jayasena, S.D.4
-
45
-
-
0028859580
-
A group II intron RNA is a catalytic component of a DNA endoribonuclease involved in intron mobility
-
of outstanding interest. A group II ribozyme, operating as a ribonucleoprotein complex with an intron-encoded reverse transcriptase, catalyzes site-specific DNA cleavage to facilitate intron mobility in yeast mitochondria. This example expands the list of catalytic activities for natural ribozymes.
-
Zimmerly S, Guo H, Eskes R, Yang J, Perlman PS, Lambowitz AM. A group II intron RNA is a catalytic component of a DNA endoribonuclease involved in intron mobility. of outstanding interest Cell. 83:1995;529-538 A group II ribozyme, operating as a ribonucleoprotein complex with an intron-encoded reverse transcriptase, catalyzes site-specific DNA cleavage to facilitate intron mobility in yeast mitochondria. This example expands the list of catalytic activities for natural ribozymes.
-
(1995)
Cell
, vol.83
, pp. 529-538
-
-
Zimmerly, S.1
Guo, H.2
Eskes, R.3
Yang, J.4
Perlman, P.S.5
Lambowitz, A.M.6
-
47
-
-
0029093855
-
The secondary structure and sequence optimization of an RNA ligase ribozyme
-
Ekland EH, Bartel DP. The secondary structure and sequence optimization of an RNA ligase ribozyme. Nucleic Acids Res. 23:1995;3231-3238.
-
(1995)
Nucleic Acids Res
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Ekland, E.H.1
Bartel, D.P.2
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48
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0028898110
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Cleavage of an amide bond by a ribozyme
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of outstanding interest. A group I ribozyme variant, enhanced by in vitro selection for DNA-cleaving activity, is also shown to cleave amide bonds with a modest catalytic rate enhancement.
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Dai X, De Mesmaeker AD, Joyce GF. Cleavage of an amide bond by a ribozyme. of outstanding interest Science. 267:1995;237-240 A group I ribozyme variant, enhanced by in vitro selection for DNA-cleaving activity, is also shown to cleave amide bonds with a modest catalytic rate enhancement.
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(1995)
Science
, vol.267
, pp. 237-240
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Dai, X.1
De Mesmaeker, A.D.2
Joyce, G.F.3
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50
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0028911845
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In vitro evolution of a self-alkylating ribozyme
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of outstanding interest. A biotin-binding RNA motif is used to plan an RNA pool that is biased in favor of substrate binding to screen for self-alkylating ribozymes. This strategy can be used to pre-engineer pools that contain substrate- or cofactor-binding sites for the in vitro selection of new ribozymes.
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Wilson C, Szostak JW. In vitro evolution of a self-alkylating ribozyme. of outstanding interest Nature. 374:1995;333-777 A biotin-binding RNA motif is used to plan an RNA pool that is biased in favor of substrate binding to screen for self-alkylating ribozymes. This strategy can be used to pre-engineer pools that contain substrate- or cofactor-binding sites for the in vitro selection of new ribozymes.
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(1995)
Nature
, vol.374
, pp. 333-777
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Wilson, C.1
Szostak, J.W.2
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51
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0029294624
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Isolation of a ribozyme with 5′-5′ ligase activity
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of outstanding interest. A ribozyme is described that condenses an RNA 5′ mono-, di- or triphosphate with an RNA 5′ phosphorimidazolide substrate to produce 5′,5′-pyro-, tri- or tetraphosphate linkages, respectively.
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Chapman KB, Szostak JW. Isolation of a ribozyme with 5′-5′ ligase activity. of outstanding interest Chem Biol. 2:1995;325-333 A ribozyme is described that condenses an RNA 5′ mono-, di- or triphosphate with an RNA 5′ phosphorimidazolide substrate to produce 5′,5′-pyro-, tri- or tetraphosphate linkages, respectively.
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(1995)
Chem Biol
, vol.2
, pp. 325-333
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Chapman, K.B.1
Szostak, J.W.2
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52
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0028675028
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A DNA enzyme that cleaves RNA
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Breaker RR, Joyce GF. A DNA enzyme that cleaves RNA. Chem Biol. 1:1994;223-229.
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(1994)
Chem Biol
, vol.1
, pp. 223-229
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Breaker, R.R.1
Joyce, G.F.2
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53
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0028983570
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2+-dependent RNA phosphoesterase activity
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2+-dependent catalysts can accelerate RNA cleavage by ~100 000-fold and can operate under temperature and ionic strength conditions that exist in vivo.
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2+-dependent catalysts can accelerate RNA cleavage by ~100 000-fold and can operate under temperature and ionic strength conditions that exist in vivo.
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(1995)
Chem Biol
, vol.2
, pp. 660-665
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Breaker, R.R.1
Joyce, G.F.2
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54
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0029037713
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A DNA metalloenzyme with DNA ligase activity
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2+ and accelerates the reaction ~3 400-fold faster that the rate observed using a simple DNA template as a catalyst.
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2+ and accelerates the reaction ~3 400-fold faster that the rate observed using a simple DNA template as a catalyst.
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(1995)
Nature
, vol.375
, pp. 611-614
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Couenoud, B.1
Szostak, J.W.2
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