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1
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0025061676
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Nucleic acid structures - tetraloops and RNA folding
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Uhlenbeck OC. Nucleic acid structures - tetraloops and RNA folding. Nature. 346:1990;613-614.
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Nature
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Uhlenbeck, O.C.1
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2
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0028063567
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Three-dimensional structure of a hammerhead ribozyme
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Pley HW, Flaherty KM, McKay DB. Three-dimensional structure of a hammerhead ribozyme. Nature. 372:1994;68-74.
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Nature
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Pley, H.W.1
Flaherty, K.M.2
McKay, D.B.3
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3
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0029073091
-
The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage
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Scott WG, Finch JT, Klug A. The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage. Cell. 81:1995;991-1002.
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Cell
, vol.81
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Scott, W.G.1
Finch, J.T.2
Klug, A.3
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4
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0030476765
-
Capturing the structure of a catalytic RNA intermediate: The hammerhead ribozyme
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Scott WG, Murray JB, Arnold JRP, Stoddard BL, Klug A. Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme. Science. 274:1996;2065-2069.
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Science
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Scott, W.G.1
Murray, J.B.2
Arnold, J.R.P.3
Stoddard, B.L.4
Klug, A.5
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5
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-
0029820625
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Crystal structure of a group I ribozyme domain: Principles of RNA packing
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Cate JH, Gooding AR, Podell E, Zhou K, Golden BL, Kundrot CE, Cech TR, Doudna JA. Crystal structure of a group I ribozyme domain: principles of RNA packing. Science. 273:1996;1678-1685.
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Science
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Cate, J.H.1
Gooding, A.R.2
Podell, E.3
Zhou, K.4
Golden, B.L.5
Kundrot, C.E.6
Cech, T.R.7
Doudna, J.A.8
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6
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0028803380
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Preparation of isotopically enriched RNAs for heteronuclear NMR
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Batey RT, Battiste JL, Williamson JR. Preparation of isotopically enriched RNAs for heteronuclear NMR. Methods Enzymol. 261:1995;300-322.
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(1995)
Methods Enzymol
, vol.261
, pp. 300-322
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Batey, R.T.1
Battiste, J.L.2
Williamson, J.R.3
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7
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0028885514
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Multidimensional heteronuclear NMR experiments for structure determination of isotopically labeled RNA
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Pardi A. Multidimensional heteronuclear NMR experiments for structure determination of isotopically labeled RNA. Methods Enzymol. 261:1995;350-380.
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(1995)
Methods Enzymol
, vol.261
, pp. 350-380
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Pardi, A.1
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8
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0028909308
-
Novel techniques in nuclear magnetic resonance for nucleic acids
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Aboul-ela F, Varani G. Novel techniques in nuclear magnetic resonance for nucleic acids. Curr Opin Biotechnol. 6:1995;89-95.
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(1995)
Curr Opin Biotechnol
, vol.6
, pp. 89-95
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Aboul-Ela, F.1
Varani, G.2
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9
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0004093379
-
NMR derived structures of RNA loops: The conformation of eukaryotic 5S ribosomal loop E
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Berkeley: University of California
-
Wimberly BT. NMR derived structures of RNA loops: the conformation of eukaryotic 5S ribosomal loop E. PhD Thesis. 1992;University of California, Berkeley.
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(1992)
PhD Thesis
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-
Wimberly, B.T.1
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10
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-
0029082529
-
Structure of the P1 helix from group I self splicing introns
-
The structure of a hairpin model of the conserved upstream site of cleavage of group I introns represents one of the first examples of RNA structure determined with the aid of isotopically labelled RNA. of special interest
-
Allain FH-T, Varani G. Structure of the P1 helix from group I self splicing introns. J Mol Biol. 250:1995;333-353 The structure of a hairpin model of the conserved upstream site of cleavage of group I introns represents one of the first examples of RNA structure determined with the aid of isotopically labelled RNA. of special interest.
-
(1995)
J Mol Biol
, vol.250
, pp. 333-353
-
-
Allain, F.-T.1
Varani, G.2
-
11
-
-
0031588925
-
How accurately and precisely can RNA structure be determined by NMR?
-
A formal investigation of the quality of NMR-derived RNA structures, obtained by extensive simulations of the crystallographic structure of a ribozyme. of special interest
-
Allain FH-T, Varani G. How accurately and precisely can RNA structure be determined by NMR? J Mol Biol. 267:1997;338-351 A formal investigation of the quality of NMR-derived RNA structures, obtained by extensive simulations of the crystallographic structure of a ribozyme. of special interest.
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(1997)
J Mol Biol
, vol.267
, pp. 338-351
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-
Allain, F.-T.1
Varani, G.2
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14
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0029805937
-
2 by two-dimensional NMR and simulated annealing
-
Biochemical and structural data investigate the stability of tandem G·U mismatches and reveal that stacking interactions may be the major determinants of structure and stability. of special interest
-
2 by two-dimensional NMR and simulated annealing. Biochemistry. 35:1996;14077-14089 Biochemical and structural data investigate the stability of tandem G·U mismatches and reveal that stacking interactions may be the major determinants of structure and stability. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 14077-14089
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-
McDowell, J.A.1
Turner, D.H.2
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15
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-
0029744135
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2 by two-dimensional NMR and the iterative relaxation matrix approach
-
The structure of a symmetric tandem G·A base pair demonstrate that the base-pairing pattern is controlled by the sequence of the flanking base pairs. of special interest
-
2 by two-dimensional NMR and the iterative relaxation matrix approach. Biochemistry. 35:1996;9677-9689 The structure of a symmetric tandem G·A base pair demonstrate that the base-pairing pattern is controlled by the sequence of the flanking base pairs. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 9677-9689
-
-
Wu, M.1
Turner, D.H.2
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16
-
-
0029856954
-
NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP)
-
Schmitz U, Freymann DM, James TL, Keenan RJ, Vinayak R, Walter P. NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP). RNA. 2:1996;1213-1227.
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(1996)
RNA
, vol.2
, pp. 1213-1227
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Schmitz, U.1
Freymann, D.M.2
James, T.L.3
Keenan, R.J.4
Vinayak, R.5
Walter, P.6
-
17
-
-
0029954443
-
Structural features of a six nucleotide RNA hairpin loop found in ribosomal RNA
-
These two papers [17,20] describe the structure of a conserved hairpin loop within the so-called 'GTPase centre' of ribosomal RNA. of special interest
-
Fountain MA, Serra MJ, Krugh TR, Turner DH. Structural features of a six nucleotide RNA hairpin loop found in ribosomal RNA. Biochemistry. 35:1996;6539-6548 These two papers [17,20] describe the structure of a conserved hairpin loop within the so-called 'GTPase centre' of ribosomal RNA. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 6539-6548
-
-
Fountain, M.A.1
Serra, M.J.2
Krugh, T.R.3
Turner, D.H.4
-
18
-
-
0029898708
-
NMR structure of a bacteriophage T4 RNA hairpin involved in translational repression
-
The structures of a wild-type [18] and a mutant [19] hairpin recognized by T4 RNA polymerase reveal that the mutant forms the same structure as the wild-type sequence. Thus, this quadruple mutant was selected by in vitro genetics because of its ability to conserve RNA structure. of special interest
-
Mirmira SR, Tinoco IJ. NMR structure of a bacteriophage T4 RNA hairpin involved in translational repression. Biochemistry. 35:1996;7664-7674 The structures of a wild-type [18] and a mutant [19] hairpin recognized by T4 RNA polymerase reveal that the mutant forms the same structure as the wild-type sequence. Thus, this quadruple mutant was selected by in vitro genetics because of its ability to conserve RNA structure. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 7664-7674
-
-
Mirmira, S.R.1
Tinoco, I.J.2
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19
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-
0029894437
-
A quadruple mutant T4 RNA hairpin with the same structure as the wild-type translational repression
-
See annotation [18]. of special interest
-
Mirmira SR, Tinoco IJ. A quadruple mutant T4 RNA hairpin with the same structure as the wild-type translational repression. Biochemistry. 35:1996;7675-7683 See annotation [18]. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 7675-7683
-
-
Mirmira, S.R.1
Tinoco, I.J.2
-
20
-
-
0029998660
-
Structure of a hexanucleotide RNA hairpin loop conserved in ribosomal RNAs
-
See annotation [17]. of special interest
-
Huang S, Wang Y-X, Draper DE. Structure of a hexanucleotide RNA hairpin loop conserved in ribosomal RNAs. J Mol Biol. 258:1996;308-321 See annotation [17]. of special interest.
-
(1996)
J Mol Biol
, vol.258
, pp. 308-321
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-
Huang, S.1
Wang, Y.-X.2
Draper, D.E.3
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21
-
-
0029894361
-
Structure of a U·U pair within a conserved ribosomal RNA hairpin
-
Wang Y-X, Huang S, Draper DE. Structure of a U·U pair within a conserved ribosomal RNA hairpin. Nucleic Acids Res. 24:1996;2666-2672.
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(1996)
Nucleic Acids Res
, vol.24
, pp. 2666-2672
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-
Wang, Y.-X.1
Huang, S.2
Draper, D.E.3
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22
-
-
0028970660
-
NMR analysis of the trans-activation response (TAR) RNA element of equine infectious anemia virus
-
Hoffman DW, White SW. NMR analysis of the trans-activation response (TAR) RNA element of equine infectious anemia virus. Nucleic Acids Res. 23:1995;4058-4065.
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(1995)
Nucleic Acids Res
, vol.23
, pp. 4058-4065
-
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Hoffman, D.W.1
White, S.W.2
-
23
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-
0029024877
-
Proton NMR and structural features of a 24-nucleotide RNA hairpin
-
Borer PN, Lin Y, Wang S, Roggenbuck MW, Gott JM, Uhlenbeck OC, Pelczer I. Proton NMR and structural features of a 24-nucleotide RNA hairpin. Biochemistry. 34:1995;6488-6503.
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(1995)
Biochemistry
, vol.34
, pp. 6488-6503
-
-
Borer, P.N.1
Lin, Y.2
Wang, S.3
Roggenbuck, M.W.4
Gott, J.M.5
Uhlenbeck, O.C.6
Pelczer, I.7
-
24
-
-
0029852357
-
Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge
-
See annotation [26]. of special interest
-
Aboul-ela F, Karn J, Varani G. Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge. Nucleic Acids Res. 24:1996;3974-3981 See annotation [26]. of special interest.
-
(1996)
Nucleic Acids Res
, vol.24
, pp. 3974-3981
-
-
Aboul-Ela, F.1
Karn, J.2
Varani, G.3
-
25
-
-
0030069826
-
Structure of the polyadenylation regulatory element of the human U1A pre-mRNA 3'-untranslated region and interaction with the U1A protein
-
The structure of the free polyadenylation regulatory element. This study represents a necessary step towards determination of the structure of the U1A - RNA complex (see [58]). of outstanding interest of special interest
-
Gubser CC, Varani G. Structure of the polyadenylation regulatory element of the human U1A pre-mRNA 3'-untranslated region and interaction with the U1A protein. Biochemistry. 35:1996;2253-2267 The structure of the free polyadenylation regulatory element. This study represents a necessary step towards determination of the structure of the U1A - RNA complex (see [58]). of outstanding interest of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 2253-2267
-
-
Gubser, C.C.1
Varani, G.2
-
26
-
-
0028864394
-
The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein
-
The structure of the HIV-1 TAR RNA complexed with a 37-mer peptide from the HIV-1 TAR protein [26] and its comparison with the free form of TAR [24] reveal that protein binding induces a major conformational rearrangement within TAR RNA. A similar conformational change is observed upon binding of a Rev peptide to HIV-1 RRE RNA [38]. of special interest
-
Aboul-ela F, Karn J, Varani G. The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein. J Mol Biol. 253:1995;313-332 The structure of the HIV-1 TAR RNA complexed with a 37-mer peptide from the HIV-1 TAR protein [26] and its comparison with the free form of TAR [24] reveal that protein binding induces a major conformational rearrangement within TAR RNA. A similar conformational change is observed upon binding of a Rev peptide to HIV-1 RRE RNA [38]. of special interest.
-
(1995)
J Mol Biol
, vol.253
, pp. 313-332
-
-
Aboul-Ela, F.1
Karn, J.2
Varani, G.3
-
27
-
-
0030585428
-
Solution structure of the donor site of a trans-splicing RNA
-
A nine-nucleotide hairpin loop from the 5'-splice donor of a trypanosomal splice leader RNA is closed by several unexpected base pairs. An extra helical adenine defines a unique structural feature for intermolecular recognition at the base of the loop. of special interest
-
Greenbaum NL, Radhakrishnan I, Patel DJ, Hirsh D. Solution structure of the donor site of a trans-splicing RNA. Structure. 4:1996;725-733 A nine-nucleotide hairpin loop from the 5'-splice donor of a trypanosomal splice leader RNA is closed by several unexpected base pairs. An extra helical adenine defines a unique structural feature for intermolecular recognition at the base of the loop. of special interest.
-
(1996)
Structure
, vol.4
, pp. 725-733
-
-
Greenbaum, N.L.1
Radhakrishnan, I.2
Patel, D.J.3
Hirsh, D.4
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28
-
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0029861968
-
A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data
-
Laing LG, Hall KB. A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data. Biochemistry. 35:1996;13586-13596.
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(1996)
Biochemistry
, vol.35
, pp. 13586-13596
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-
Laing, L.G.1
Hall, K.B.2
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29
-
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0028866812
-
Solution structure of the CUUG hairpin loop: A novel RNA tetraloop motif
-
Jucker FM, Pardi A. Solution structure of the CUUG hairpin loop: a novel RNA tetraloop motif. Biochemistry. 34:1995;14416-14427.
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(1995)
Biochemistry
, vol.34
, pp. 14416-14427
-
-
Jucker, F.M.1
Pardi, A.2
-
30
-
-
0030011355
-
Conformation of a non-frameshifting RNA pseudoknot from mouse mammary tumor virus
-
See annotation [32]. of special interest
-
Kang H, Hines JV, Tinoco IJ. Conformation of a non-frameshifting RNA pseudoknot from mouse mammary tumor virus. J Mol Biol. 259:1996;135-147 See annotation [32]. of special interest.
-
(1996)
J Mol Biol
, vol.259
, pp. 135-147
-
-
Kang, H.1
Hines, J.V.2
Tinoco, I.J.3
-
31
-
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0030602904
-
A characteristic bent conformation of RNA pseudoknots promotes - 1 frameshift during translation of retroviral RNA
-
See reference [32]. of special interest
-
Chen X, Kang H, Shen LX, Chamorro M, Varmus HE, Tinoco IJ. A characteristic bent conformation of RNA pseudoknots promotes - 1 frameshift during translation of retroviral RNA. J Mol Biol. 260:1996;479-483 See reference [32]. of special interest.
-
(1996)
J Mol Biol
, vol.260
, pp. 479-483
-
-
Chen, X.1
Kang, H.2
Shen, L.X.3
Chamorro, M.4
Varmus, H.E.5
Tinoco, I.J.6
-
32
-
-
0028910590
-
The structure of an RNA pseudoknot that causes efficient frameshifting in mouse mammary tumor virus
-
These three papers [30-32] present the structures of several related RNA pseudoknots, which are either functional or defective in ribosomal frameshifting. The overall shape of the pseudoknot (presence or absence of bending) seems to be important for frameshifting. of special interest
-
Shen LX, Tinoco IJ. The structure of an RNA pseudoknot that causes efficient frameshifting in mouse mammary tumor virus. J Mol Biol. 247:1995;963-978 These three papers [30-32] present the structures of several related RNA pseudoknots, which are either functional or defective in ribosomal frameshifting. The overall shape of the pseudoknot (presence or absence of bending) seems to be important for frameshifting. of special interest.
-
(1995)
J Mol Biol
, vol.247
, pp. 963-978
-
-
Shen, L.X.1
Tinoco, I.J.2
-
33
-
-
0029001288
-
Bent helix formation between RNA hairpins with complementary loops
-
The structures [33,34] of this so-called 'kissing' hairpin motif reveal a dramatic bend created by loop - loop base-pairing interactions. This kink is confirmed by hydrodynamic measurements and may be critical for recognition by the Rop protein. of special interest
-
Marino JP, Gregorian RSJ, Csankovszki G, Crothers DM. Bent helix formation between RNA hairpins with complementary loops. Science. 268:1995;1448-1454 The structures [33,34] of this so-called 'kissing' hairpin motif reveal a dramatic bend created by loop - loop base-pairing interactions. This kink is confirmed by hydrodynamic measurements and may be critical for recognition by the Rop protein. of special interest.
-
(1995)
Science
, vol.268
, pp. 1448-1454
-
-
Marino, J.P.1
Gregorian, R.S.J.2
Csankovszki, G.3
Crothers, D.M.4
-
34
-
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0031591383
-
The structure of an RNA 'kissing' hairpin complex of the BIV TAR hairpin loop and its complement
-
Chang KY, Tinoco U. The structure of an RNA 'kissing' hairpin complex of the BIV TAR hairpin loop and its complement. J Mol Biol. 1997; See annotation [33]. of special interest.
-
(1997)
J Mol Biol
-
-
Chang, K.Y.1
Tinoco, U.2
-
35
-
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0028268016
-
Binding of an HIV Rev peptide to rev responsive element RNA induces formation of purine-purine base pairs
-
Battiste JL, Tan R, Frankel AD, Williamson JR. Binding of an HIV Rev peptide to rev responsive element RNA induces formation of purine-purine base pairs. Biochemistry. 33:1994;2741-2747.
-
(1994)
Biochemistry
, vol.33
, pp. 2741-2747
-
-
Battiste, J.L.1
Tan, R.2
Frankel, A.D.3
Williamson, J.R.4
-
36
-
-
0028175778
-
1H NMR studies of the high-affinity Rev binding site of the Rev responsive element of HIV-1 mRNA: Base pairing in the core binding element
-
Peterson RD, Bartel DP, Szostak JW, Horwath SJ, Feigon J. 1H NMR studies of the high-affinity Rev binding site of the Rev responsive element of HIV-1 mRNA: base pairing in the core binding element. Biochemistry. 33:1994;5357-5366.
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(1994)
Biochemistry
, vol.33
, pp. 5357-5366
-
-
Peterson, R.D.1
Bartel, D.P.2
Szostak, J.W.3
Horwath, S.J.4
Feigon, J.5
-
38
-
-
0030596005
-
Structural change in Rev responsive element RNA of HIV-1 on binding Rev peptide
-
See annotation [26]. of special interest
-
Peterson RD, Feigon J. Structural change in Rev responsive element RNA of HIV-1 on binding Rev peptide. J Mol Biol. 264:1996;863-877 See annotation [26]. of special interest.
-
(1996)
J Mol Biol
, vol.264
, pp. 863-877
-
-
Peterson, R.D.1
Feigon, J.2
-
39
-
-
0029946537
-
Structural basis of RNA folding and recognition in an AMP - RNA aptamer complex
-
See annotation [41]. of outstanding interest
-
Jiang F, Kumar RA, Jones RA, Patel DJ. Structural basis of RNA folding and recognition in an AMP - RNA aptamer complex. Nature. 382:1996;183-186 See annotation [41]. of outstanding interest.
-
(1996)
Nature
, vol.382
, pp. 183-186
-
-
Jiang, F.1
Kumar, R.A.2
Jones, R.A.3
Patel, D.J.4
-
40
-
-
0029847611
-
RNA folding topology and intermolecular contacts in the AMP - RNA aptamer complex
-
See annotation [41]. of outstanding interest of special interest
-
Jiang F, Fiala R, Live D, Kumar RA, Patel DJ. RNA folding topology and intermolecular contacts in the AMP - RNA aptamer complex. Biochemistry. 35:1996;13250-13266 See annotation [41]. of outstanding interest of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 13250-13266
-
-
Jiang, F.1
Fiala, R.2
Live, D.3
Kumar, R.A.4
Patel, D.J.5
-
41
-
-
0029904020
-
Solution structure of an ATP-binding RNA aptamer reveals a novel fold
-
The structure of an RNA aptamer - ATP ligand complex reveals a tight binding pocket formed by the RNA upon ligand binding. The tight binding site is stabilized by intermolecular and intramolecular base-stacking interactions and hydrogen bonds. of outstanding interest
-
Dieckmann T, Suzuki E, Nakamura GK, Feigon J. Solution structure of an ATP-binding RNA aptamer reveals a novel fold. RNA. 2:1996;628-640 The structure of an RNA aptamer - ATP ligand complex reveals a tight binding pocket formed by the RNA upon ligand binding. The tight binding site is stabilized by intermolecular and intramolecular base-stacking interactions and hydrogen bonds. of outstanding interest.
-
(1996)
RNA
, vol.2
, pp. 628-640
-
-
Dieckmann, T.1
Suzuki, E.2
Nakamura, G.K.3
Feigon, J.4
-
42
-
-
0029864853
-
Molecular recognition in the FMN - RNA aptamer complex
-
As in the ATP - RNA aptamer complex [41], the FMN aptamer - RNA complex reveals a tight binding pocket formed by the RNA upon ligand binding. This tight binding site is stabilized by intermolecular and intramolecular base-stacking interactions and hydrogen bonds. of outstanding interest
-
Fan P, Suri AK, Fiala R, Live D, Patel DJ. Molecular recognition in the FMN - RNA aptamer complex. J Mol Biol. 258:1996;480-500 As in the ATP - RNA aptamer complex [41], the FMN aptamer - RNA complex reveals a tight binding pocket formed by the RNA upon ligand binding. This tight binding site is stabilized by intermolecular and intramolecular base-stacking interactions and hydrogen bonds. of outstanding interest.
-
(1996)
J Mol Biol
, vol.258
, pp. 480-500
-
-
Fan, P.1
Suri, A.K.2
Fiala, R.3
Live, D.4
Patel, D.J.5
-
43
-
-
0029972909
-
Structural basis of ligand discrimination by two related RNA aptamers resolved by NMR spectroscopy
-
The structures of the citrulline - RNA aptamer and arginine - RNA aptamer complexes contain internal loops that define the aptamer binding pockets. Differences between these two aptamers are sufficient to discriminate between the two substrates, despite their great similarity. of outstanding interest
-
Yang Y, Kochoyan M, Burgstaller P, Westhof E, Famulok M. Structural basis of ligand discrimination by two related RNA aptamers resolved by NMR spectroscopy. Science. 272:1996;1343-1347 The structures of the citrulline - RNA aptamer and arginine - RNA aptamer complexes contain internal loops that define the aptamer binding pockets. Differences between these two aptamers are sufficient to discriminate between the two substrates, despite their great similarity. of outstanding interest.
-
(1996)
Science
, vol.272
, pp. 1343-1347
-
-
Yang, Y.1
Kochoyan, M.2
Burgstaller, P.3
Westhof, E.4
Famulok, M.5
-
44
-
-
0029825658
-
Structure of the a site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic
-
The structure of an aminoglycoside antibiotic in complex with an oligonucleotide model of the A-site of bacterial 16S ribosomal RNA. This structure (the first of an antibiotic - RNA complex) illustrates many new features of the interactions of drugs in the RNA major groove. Similar features are observed in an aminoglycoside aptamer structure [45]. of outstanding interest
-
Fourmy D, Recht MI, Blanchard SC, Puglisi JD. Structure of the a site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic. Science. 274:1996;1367-1371 The structure of an aminoglycoside antibiotic in complex with an oligonucleotide model of the A-site of bacterial 16S ribosomal RNA. This structure (the first of an antibiotic - RNA complex) illustrates many new features of the interactions of drugs in the RNA major groove. Similar features are observed in an aminoglycoside aptamer structure [45]. of outstanding interest.
-
(1996)
Science
, vol.274
, pp. 1367-1371
-
-
Fourmy, D.1
Recht, M.I.2
Blanchard, S.C.3
Puglisi, J.D.4
-
45
-
-
0030887815
-
Saccharide - RNA recognition in an aminoglycoside antibiotic - RNA aptamer complex
-
Jiang L, Suri AK, Fiala R, Patel DJ. Saccharide - RNA recognition in an aminoglycoside antibiotic - RNA aptamer complex. Chem Biol. 1997; See annotation [44]. of outstanding interest.
-
(1997)
Chem Biol
-
-
Jiang, L.1
Suri, A.K.2
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46
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0030976612
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An inhibitor of the Tat/TAR RNA interaction that effectively suppresses HIV-1 replication
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in press
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Hamy F, Felder ER, Heizmann G, Lazdins J, Aboul-ela F, Varani G, Karn J, Klimkait T. An inhibitor of the Tat/TAR RNA interaction that effectively suppresses HIV-1 replication. Proc Natl Acad Sci USA. 1997;. in press.
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Hamy, F.1
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Varani, G.6
Karn, J.7
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47
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Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif
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0027452957
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High affinity binding of TAR RNA by the human immunodeficiency type-1 tat protein requires base - pairs in the RNA stem and amino acid residues flanking the basic region
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Churcher MJ, Lamont C, Hamy F, Dingwall C, Green SM, Lowe AD, Butler PJG, Gait MJ, Karn J. High affinity binding of TAR RNA by the human immunodeficiency type-1 tat protein requires base - pairs in the RNA stem and amino acid residues flanking the basic region. J Mol Biol. 230:1993;90-110.
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Churcher, M.J.1
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Butler, P.J.G.7
Gait, M.J.8
Karn, J.9
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49
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0028785036
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The amino terminal domain of HIV-1 Rev is required for discrimination of the RRE from nonspecific RNA
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Daly TJ, Doten RC, Rusche JR, Auer M. The amino terminal domain of HIV-1 Rev is required for discrimination of the RRE from nonspecific RNA. J Mol Biol. 253:1995;243-258.
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Daly, T.J.1
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Rusche, J.R.3
Auer, M.4
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50
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0029784592
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α helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex
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In the complex between an HIV Rev-derived peptide and the HIV-1 RRE RNA [50] or an RNA aptamer [51], the peptide assumes an α-helical structure and penetrates deeply into the RNA major groove which is opened up by essential purine - purine base pairs. of outstanding interest
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Battiste JL, Mao H, Rao NS, Tan R, Muhandiram DR, Kay LE, Frankel AD, Williamson JR. α helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex. Science. 273:1996;1547-1551 In the complex between an HIV Rev-derived peptide and the HIV-1 RRE RNA [50] or an RNA aptamer [51], the peptide assumes an α-helical structure and penetrates deeply into the RNA major groove which is opened up by essential purine - purine base pairs. of outstanding interest.
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Science
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Battiste, J.L.1
Mao, H.2
Rao, N.S.3
Tan, R.4
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Kay, L.E.6
Frankel, A.D.7
Williamson, J.R.8
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51
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0030475417
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Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 Rev peptide - RNA aptamer complex
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See annotation [50]. of outstanding interest
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Ye X, Gorin A, Ellington AD, Patel DJ. Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 Rev peptide - RNA aptamer complex. Nat Struct Biol. 3:1996;1026-1033 See annotation [50]. of outstanding interest.
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Nat Struct Biol
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Ye, X.1
Gorin, A.2
Ellington, A.D.3
Patel, D.J.4
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52
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0028858599
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Solution structure of a bovine immunodeficiency virus Tat-TAR peptide - RNA complex
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In the complex between a BIV Tat-derived peptide and its target TAR RNA, the RNA major groove is widened by a bulged-out uracyl and the peptide forms a β hairpin (see also [53]). The comparison with HIV-1 Rev-derived peptides [50,51] reveals that arginine-rich peptides can bind cognate RNAs in very different ways. of outstanding interest
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Puglisi JD, Chen L, Blanchard S, Frankel AD. Solution structure of a bovine immunodeficiency virus Tat-TAR peptide - RNA complex. Science. 270:1995;1200-1203 In the complex between a BIV Tat-derived peptide and its target TAR RNA, the RNA major groove is widened by a bulged-out uracyl and the peptide forms a β hairpin (see also [53]). The comparison with HIV-1 Rev-derived peptides [50,51] reveals that arginine-rich peptides can bind cognate RNAs in very different ways. of outstanding interest.
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(1995)
Science
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Puglisi, J.D.1
Chen, L.2
Blanchard, S.3
Frankel, A.D.4
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53
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0029613238
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Molecular recognition in the bovine immunodeficiency virus Tat peptide - TAR RNA complex
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See reference [52]. of outstanding interest
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Ye X, Kumar RA, Patel DJ. Molecular recognition in the bovine immunodeficiency virus Tat peptide - TAR RNA complex. Chem Biol. 2:1995;827-840 See reference [52]. of outstanding interest.
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Chem Biol
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Ye, X.1
Kumar, R.A.2
Patel, D.J.3
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55
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Conformation of the TAR - arginine complex by NMR
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Puglisi JD, Tan R, Canlan BJ, Frankel AD, Williamson JR. Conformation of the TAR - arginine complex by NMR. Science. 257:1992;76-80.
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56
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Coupling of local folding to site-specific binding of proteins to DNA
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Spolar RS, Record MTJ. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:1994;777-784.
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Science
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Record, M.T.J.2
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0028004607
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Crystal structure at 1.92Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
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Oubridge C, Ito N, Evans PR, Teo C-H, Nagai K. Crystal structure at 1.92Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature. 372:1994;432-438.
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Nagai, K.5
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58
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0029920331
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Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
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The structure of the 22 kDa complex between the human U1A protein and the polyadenylation regulatory element represents the first example of the NMR structure of a protein - RNA complex. The comparison with the structures of free protein and RNA components reveals an unexpected recognition mechanism, which requires both RNA and protein conformational changes. of outstanding interest
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Allain F-HT, Gubser CC, Howe PWA, Nagai K, Neuhaus D, Varani G. Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation. Nature. 380:1996;646-650 The structure of the 22 kDa complex between the human U1A protein and the polyadenylation regulatory element represents the first example of the NMR structure of a protein - RNA complex. The comparison with the structures of free protein and RNA components reveals an unexpected recognition mechanism, which requires both RNA and protein conformational changes. of outstanding interest.
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Nature
, vol.380
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Allain, F.-H.1
Gubser, C.C.2
Howe, P.W.A.3
Nagai, K.4
Neuhaus, D.5
Varani, G.6
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59
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0029978824
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Solution structure of the N-terminal RNP domain of U1A protein: The role of C-terminal residues in structure stability and RNA binding
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Avis J, Allain FH-T, Howe PWA, Varani G, Neuhaus D, Nagai K. Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding. J Mol Biol. 257:1996;398-411.
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Avis, J.1
Allain, F.-T.2
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Varani, G.4
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Nagai, K.6
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