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1
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0030978401
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The conformation of ribosomes and rRNA
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Moore PB. The conformation of ribosomes and rRNA. Curr Opin Struct Biol. 7:1997;343-347.
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Curr Opin Struct Biol
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Moore, P.B.1
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0031253937
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Structural aspects of protein synthesis
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Liljas A, Al-Karadaghi S. Structural aspects of protein synthesis. Nat Struct Biol. 4:1997;767-771.
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Nat Struct Biol
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Liljas, A.1
Al-Karadaghi, S.2
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5
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0032488946
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Molecular movement inside the translational engine
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of special interest. An excellent review of recent progress towards understanding the structural basis of the elongation cycle of the ribosome. Along with [1-4], this is one of a number of recent reviews on the ribosome to have appeared in the past year.
-
Wilson KS, Noller HF. Molecular movement inside the translational engine. of special interest Cell. 92:1998;337-349 An excellent review of recent progress towards understanding the structural basis of the elongation cycle of the ribosome. Along with [1-4], this is one of a number of recent reviews on the ribosome to have appeared in the past year.
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(1998)
Cell
, vol.92
, pp. 337-349
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Wilson, K.S.1
Noller, H.F.2
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6
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0029820625
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Crystal structure of a group 1 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 1 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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7
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0030452773
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New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: A complete 3D model of the Tetrahymena thermophila ribozyme
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Lehnert V, Jaeger L, Michel F, Westhof E. New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: a complete 3D model of the Tetrahymena thermophila ribozyme. Chem Biol. 3:1996;993-1009.
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Chem Biol
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Lehnert, V.1
Jaeger, L.2
Michel, F.3
Westhof, E.4
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8
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0001791833
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Comparative sequence analysis and the structure of 16S and 23S rRNA
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R.A. Zimmerman, Dahlberg A.E. Boca Raton, Florida: CRC Press
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Gutell RR. Comparative sequence analysis and the structure of 16S and 23S rRNA. Zimmerman RA, Dahlberg AE. Ribosomal RNA: Structure, Evolution, Processing, and Function in Protein Biosynthesis. 1996;111-128 CRC Press, Boca Raton, Florida.
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Ribosomal RNA: Structure, Evolution, Processing, and Function in Protein Biosynthesis
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Gutell, R.R.1
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9
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0030941228
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Context dependent RNA-RNA recognition in a three-dimensional model of the 16S rRNA core
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of special interest. The authors used principles abstracted from known RNA structures, along with experimental data, to generate a molecular model of the central region of 16S rRNA.
-
Masquida B, Felden B, Westhof E. Context dependent RNA-RNA recognition in a three-dimensional model of the 16S rRNA core. of special interest Bioorg Med Chem. 5:1997;1021-1035 The authors used principles abstracted from known RNA structures, along with experimental data, to generate a molecular model of the central region of 16S rRNA.
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Bioorg Med Chem
, vol.5
, pp. 1021-1035
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Masquida, B.1
Felden, B.2
Westhof, E.3
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10
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0029286628
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Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA
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Powers T, Noller HF. Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA. RNA. 1:1995;194-209.
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(1995)
RNA
, vol.1
, pp. 194-209
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Powers, T.1
Noller, H.F.2
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11
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0029645318
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The 70S Escherichia coli ribosome at 23 Å resolution: Fitting the ribosomal RNA
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Stark H, Mueller F, Orlova EV, Schatz M, Dube P, Erdemir T, Zemlin F, Brimacombe R, van Heel M. The 70S Escherichia coli ribosome at 23 Å resolution: fitting the ribosomal RNA. Structure. 3:1995;815-821.
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Structure
, vol.3
, pp. 815-821
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Stark, H.1
Mueller, F.2
Orlova, E.V.3
Schatz, M.4
Dube, P.5
Erdemir, T.6
Zemlin, F.7
BriMacOmbe, R.8
Van Heel, M.9
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12
-
-
0029100747
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A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome
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Frank J, Zhu J, Penczek P, Li Y, Srivastava S, Verschoor A, Radermacher M, Grassucci R, Lata RK, Agrawal RK. A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature. 376:1995;441-444.
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Nature
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Frank, J.1
Zhu, J.2
Penczek, P.3
Li, Y.4
Srivastava, S.5
Verschoor, A.6
RaderMacHer, M.7
Grassucci, R.8
Lata, R.K.9
Agrawal, R.K.10
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13
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0030887834
-
Arrangement of tRNAs in pre- and posttrnslocational ribosomes revealed by electron cryomicroscopy
-
of outstanding interest. Together with [14,15], these papers represent a tour de force in ribosome imaging by cryo-electron microscopy. Following up on earlier work [11,12], images of translating ribosomes were compared to empty 70S ribosome complexes in order to reveal the positions of tRNAs. Frank and co-workers [14] used a mixture of translating ribosomes. In this paper from van Heel, experimental tricks were used to obtain homogeneous populations of pre- or post-translocation complexes. Similar principles were used to directly visualize the presence of elongation factor Tu adjacent to the ribosome A-site [15].
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Stark H, Orlova EV, Rinke-Appel J, Junke N, Mueller F, Rodnina M, Wintermeyer W, Brimacombe R, van Heel M, Stark H, et al. Arrangement of tRNAs in pre- and posttrnslocational ribosomes revealed by electron cryomicroscopy. of outstanding interest Cell. 88:1997;19-28 Together with [14,15], these papers represent a tour de force in ribosome imaging by cryo-electron microscopy. Following up on earlier work [11,12], images of translating ribosomes were compared to empty 70S ribosome complexes in order to reveal the positions of tRNAs. Frank and co-workers [14] used a mixture of translating ribosomes. In this paper from van Heel, experimental tricks were used to obtain homogeneous populations of pre- or post-translocation complexes. Similar principles were used to directly visualize the presence of elongation factor Tu adjacent to the ribosome A-site [15].
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(1997)
Cell
, vol.88
, pp. 19-28
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Stark, H.1
Orlova, E.V.2
Rinke-Appel, J.3
Junke, N.4
Mueller, F.5
Rodnina, M.6
Wintermeyer, W.7
BriMacOmbe, R.8
Van Heel, M.9
Stark, H.10
-
14
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0030040661
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Direct visualization of A-, P-, and E-site transfer RNAs in the Escherichia coli ribosome
-
of outstanding interest. See annotation for [13].
-
Agrawal RK, Penczek P, Grassucci RA, Li Y, Leith A, Nierhaus KH, Frank J. Direct visualization of A-, P-, and E-site transfer RNAs in the Escherichia coli ribosome. of outstanding interest Science. 271:1996;1000-1002 See annotation for [13].
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(1996)
Science
, vol.271
, pp. 1000-1002
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Agrawal, R.K.1
Penczek, P.2
Grassucci, R.A.3
Li, Y.4
Leith, A.5
Nierhaus, K.H.6
Frank, J.7
-
15
-
-
0030770467
-
Visualization of elongation factor Tu on the Escherichia coli ribosome
-
of outstanding interest. See annotation for [13].
-
Stark H, Rodnina MV, Rinke-Appel J, Brimacombe R, Wintermeyer W, van Heel M. Visualization of elongation factor Tu on the Escherichia coli ribosome. of outstanding interest Nature. 389:1997;403-406 See annotation for [13].
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(1997)
Nature
, vol.389
, pp. 403-406
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Stark, H.1
Rodnina, M.V.2
Rinke-Appel, J.3
BriMacOmbe, R.4
Wintermeyer, W.5
Van Heel, M.6
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16
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0030871279
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A new technique for the characterization of long-range tertiary contacts in large RNA molecules: Insertion of a photolabel at a selected position in 16S rRNA within the Escherichia coli ribosome
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Baranov PV, Dokudovskaya SS, Oretskaya TS, Dontsova OA, Bogdanov AA, Brimacombe R. A new technique for the characterization of long-range tertiary contacts in large RNA molecules: insertion of a photolabel at a selected position in 16S rRNA within the Escherichia coli ribosome. Nucleic Acids Res. 25:1997;2266-2273.
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Nucleic Acids Res
, vol.25
, pp. 2266-2273
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Baranov, P.V.1
Dokudovskaya, S.S.2
Oretskaya, T.S.3
Dontsova, O.A.4
Bogdanov, A.A.5
BriMacOmbe, R.6
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17
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0030801742
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A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. I. Fitting the RNA to a 3D electron microscopic map at 20 Å
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of special interest. See annotation to [19].
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Mueller F, Brimacombe R. A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. I. Fitting the RNA to a 3D electron microscopic map at 20 Å of special interest J Mol Biol. 271:1997;524-544 See annotation to [19].
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(1997)
J Mol Biol
, vol.271
, pp. 524-544
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Mueller, F.1
BriMacOmbe, R.2
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18
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0030821676
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A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data
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of special interest. See annotation to [19].
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Mueller F, Brimacombe R. A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data. of special interest J Mol Biol. 271:1997;545-565 See annotation to [19].
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J Mol Biol
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, pp. 545-565
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Mueller, F.1
BriMacOmbe, R.2
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19
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0030824580
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A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. III. The topography of the functional centre
-
of outstanding interest. of special interest. In [17-19], the authors attempt to fit a model of the rRNA into the 20 Å electron microscopy contours, integrating extensive chemical modification and cross-linking data. The model differs in a few key respects from those of Noller and co-workers [21], for example, in the placement of residues around the decoding center.
-
of outstanding interest Mueller F, Stark H, van Heel M, Rinke-Appel J, Brimacombe R. A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. III. The topography of the functional centre. of special interest J Mol Biol. 271:1997;566-587 In [17-19], the authors attempt to fit a model of the rRNA into the 20 Å electron microscopy contours, integrating extensive chemical modification and cross-linking data. The model differs in a few key respects from those of Noller and co-workers [21], for example, in the placement of residues around the decoding center.
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(1997)
J Mol Biol
, vol.271
, pp. 566-587
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Mueller, F.1
Stark, H.2
Van Heel, M.3
Rinke-Appel, J.4
BriMacOmbe, R.5
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20
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0029853765
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Directed hydroxyl radical probing of the rRNA neighborhood of ribosomal protein S13 using tethered Fe(II)
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Heilek GM, Noller HF. Directed hydroxyl radical probing of the rRNA neighborhood of ribosomal protein S13 using tethered Fe(II). RNA. 2:1996;597-602.
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(1996)
RNA
, vol.2
, pp. 597-602
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Heilek, G.M.1
Noller, H.F.2
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21
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0030657775
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Mapping the inside of the ribosome with an RNA helical ruler
-
of outstanding interest. As many as 30 stem - loops of differing lengths, which mimic the anticodon stem of tRNA, were found to bind to the ribosome. Radical cleavage of rRNA in the presence of an Fe(II) complex, which is tethered to the end of the tRNA mimics, provides a low resolution (~ 15 Å) map of the nucleotides that are proximal to the tRNA-binding sites in the ribosome.
-
Joseph S, Weiser B, Noller HF. Mapping the inside of the ribosome with an RNA helical ruler. of outstanding interest Science. 278:1997;1093-1098 As many as 30 stem - loops of differing lengths, which mimic the anticodon stem of tRNA, were found to bind to the ribosome. Radical cleavage of rRNA in the presence of an Fe(II) complex, which is tethered to the end of the tRNA mimics, provides a low resolution (~ 15 Å) map of the nucleotides that are proximal to the tRNA-binding sites in the ribosome.
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(1997)
Science
, vol.278
, pp. 1093-1098
-
-
Joseph, S.1
Weiser, B.2
Noller, H.F.3
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22
-
-
0032498266
-
Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing
-
of outstanding interest. A similar approach to that of [21] was used to identify rRNA nucleotides that are near the binding site of elongation factor EF-G. Fe(II) - EDTA complexes were tethered to 18 positions in EF-G. The pattern of hydroxyl radical cleavage of the rRNA resulting from each modified EF-G enabled the authors to place the elongation factor on the low resolution map of the ribosome.
-
Wilson KS, Noller HF. Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing. of outstanding interest Cell. 92:1998;131-139 A similar approach to that of [21] was used to identify rRNA nucleotides that are near the binding site of elongation factor EF-G. Fe(II) - EDTA complexes were tethered to 18 positions in EF-G. The pattern of hydroxyl radical cleavage of the rRNA resulting from each modified EF-G enabled the authors to place the elongation factor on the low resolution map of the ribosome.
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(1998)
Cell
, vol.92
, pp. 131-139
-
-
Wilson, K.S.1
Noller, H.F.2
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23
-
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0030856333
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Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain
-
of outstanding interest. See annotation to [25].
-
Correll CC, Freeborn B, Moore PB, Steitz TA. Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain. of outstanding interest Cell. 91:1997;705-712 See annotation to [25].
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(1997)
Cell
, vol.91
, pp. 705-712
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Correll, C.C.1
Freeborn, B.2
Moore, P.B.3
Steitz, T.A.4
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24
-
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0030781084
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Use of chemically modified nucleotides to determine a 62-nucleotide RNA crystal structure: A survey of phosphorothioates, Br, Pt and Hg
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Correll C, Freeborn B, Moore P, Steitz T. Use of chemically modified nucleotides to determine a 62-nucleotide RNA crystal structure: a survey of phosphorothioates, Br, Pt and Hg. J Biomol Struct Dyn. 15:1997;165-172.
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J Biomol Struct Dyn
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, pp. 165-172
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Correll, C.1
Freeborn, B.2
Moore, P.3
Steitz, T.4
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25
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0031574326
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The loop E loop D region of Escherichia coli 5S rRNA: The solution structure reveals an unusual loop that may be important for binding ribosomal proteins
-
of special interest. Papers [23,24,25] present an atomic resolution picture of a 5S rRNA fragment, made possible by advances in X-ray diffraction techniques. The high resolution structure of the loop E domain reveals in exquisite detail novel base pairs, magnesium-coordination sites, and bound water molecules. The NMR solution structure of the region is essentially similar to that obtained in the crystal.
-
Dallas A, Moore P. The loop E loop D region of Escherichia coli 5S rRNA: the solution structure reveals an unusual loop that may be important for binding ribosomal proteins. of special interest Structure. 5:1997;1639-1653 Papers [23,24,25] present an atomic resolution picture of a 5S rRNA fragment, made possible by advances in X-ray diffraction techniques. The high resolution structure of the loop E domain reveals in exquisite detail novel base pairs, magnesium-coordination sites, and bound water molecules. The NMR solution structure of the region is essentially similar to that obtained in the crystal.
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(1997)
Structure
, vol.5
, pp. 1639-1653
-
-
Dallas, A.1
Moore, P.2
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26
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0031252479
-
Structure of a conserved RNA component of the peptidyl transferase centre
-
of special interest. An unusual C·G pair closes off the base of the three nucleotide loop from the peptidyl transferase centre of 235 rRNA, causing the bases of the loop to splay out into solution. This presumably facilitates base pairing with the acceptor end of tRNA.
-
Puglisi EV, Green R, Noller HF, Puglisi JD. Structure of a conserved RNA component of the peptidyl transferase centre. of special interest Nat Struct Biol. 4:1997;775-778 An unusual C·G pair closes off the base of the three nucleotide loop from the peptidyl transferase centre of 235 rRNA, causing the bases of the loop to splay out into solution. This presumably facilitates base pairing with the acceptor end of tRNA.
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(1997)
Nat Struct Biol
, vol.4
, pp. 775-778
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Puglisi, E.V.1
Green, R.2
Noller, H.F.3
Puglisi, J.D.4
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27
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0029085929
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A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome
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Samaha RR, Green R, Noller HF. A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome. Nature. 377:1995;309-314.
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Nature
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Samaha, R.R.1
Green, R.2
Noller, H.F.3
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28
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0031566952
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Mutations at nucleotides G2251 and U2585 of 23S rRNA perturb the peptidyl transferase center of the ribosome
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Green R, Samaha RR, Noller HF. Mutations at nucleotides G2251 and U2585 of 23S rRNA perturb the peptidyl transferase center of the ribosome. J Mol Biol. 266:1997;40-50.
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J Mol Biol
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Green, R.1
Samaha, R.R.2
Noller, H.F.3
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29
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0018365929
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The structure of the RNA binding site of ribosomal proteins S8 and S15
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Muller R, Garrett RA, Noller HF. The structure of the RNA binding site of ribosomal proteins S8 and S15. J Biol Chem. 254:1979;3873-3878.
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J Biol Chem
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Muller, R.1
Garrett, R.A.2
Noller, H.F.3
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30
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0018360588
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Binding sites for ribosomal proteins S8 and S15 in the 16 s RNA of Escherichia coli
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Zimmermann RA, Singh-Bergmann K. Binding sites for ribosomal proteins S8 and S15 in the 16 s RNA of Escherichia coli. Biochim Biophys Acta. 563:1979;422-431.
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Biochim Biophys Acta
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Zimmermann, R.A.1
Singh-Bergmann, K.2
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31
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0031000077
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The RNA binding site of S8 ribosomal protein of Escherichia coli: Selex and hydroxyl radical probing studies
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Moine H, Cachia C, Westhof E, Ehresmann B, Ehresmann C. The RNA binding site of S8 ribosomal protein of Escherichia coli: selex and hydroxyl radical probing studies. RNA. 3:1997;255-268.
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RNA
, vol.3
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Moine, H.1
Cachia, C.2
Westhof, E.3
Ehresmann, B.4
Ehresmann, C.5
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32
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0030587524
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Structural evidence for specific S8-RNA and S8-protein interactions within the 30S ribosomal subunit: Ribosomal protein S8 from Bacillus stearothermophilus at 1.9 Å resolution
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Davies C, Ramakrishnan V, White SW. Structural evidence for specific S8-RNA and S8-protein interactions within the 30S ribosomal subunit: ribosomal protein S8 from Bacillus stearothermophilus at 1.9 Å resolution. Structure. 4:1996;1093-1104.
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Structure
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Davies, C.1
Ramakrishnan, V.2
White, S.W.3
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33
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0030975691
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Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy
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of special interest. Along with [32], this solution structure of the S8-binding site in 16S rRNA provides a molecular view of a double-stranded RNA protein-binding site.
-
Kalurachchi K, Uma K, Zimmermann RA, Nikonowicz EP. Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy. of special interest Proc Natl Acad Sci USA. 94:1997;2139-2144 Along with [32], this solution structure of the S8-binding site in 16S rRNA provides a molecular view of a double-stranded RNA protein-binding site.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 2139-2144
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Kalurachchi, K.1
Uma, K.2
Zimmermann, R.A.3
Nikonowicz, E.P.4
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34
-
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0030606880
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Interaction of the Bacillus stearothermophilus ribosomal protein S15 with 16 S rRNA: I. Defining the minimal RNA site
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of special interest. See annotation to [35].
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Batey RT, Williamson JR. Interaction of the Bacillus stearothermophilus ribosomal protein S15 with 16 S rRNA: I. Defining the minimal RNA site. of special interest J Mol Biol. 261:1996;536-549 See annotation to [35].
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(1996)
J Mol Biol
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, pp. 536-549
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Batey, R.T.1
Williamson, J.R.2
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35
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0030606876
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Interaction of the Bacillus stearothermophilus ribosomal protein S15 with 16S rRNA: II. Specificity determinants of RNA-protein recognition
-
of special interest. This paper, along with [34], demonstrates that the integrity of a three-way junction in 16S rRNA is required for binding of S15, and suggests that the protein induces a change in the relative orientation of the three double helices.
-
Batey RT, Williamson JR. Interaction of the Bacillus stearothermophilus ribosomal protein S15 with 16S rRNA: II. Specificity determinants of RNA-protein recognition. of special interest J Mol Biol. 261:1996;550-567 This paper, along with [34], demonstrates that the integrity of a three-way junction in 16S rRNA is required for binding of S15, and suggests that the protein induces a change in the relative orientation of the three double helices.
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(1996)
J Mol Biol
, vol.261
, pp. 550-567
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Batey, R.T.1
Williamson, J.R.2
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36
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0032559410
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2+-induced conformational changes in the S15 binding site of a 16S ribosomal RNA
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2+-induced conformational changes in the S15 binding site of a 16S ribosomal RNA. J Mol Biol. 275:1998;453-464.
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(1998)
J Mol Biol
, vol.275
, pp. 453-464
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Orr, J.W.1
Hagerman, P.J.2
Williamson, J.R.3
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37
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0031026421
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Solution structure of the ribosomal RNA binding protein S15 from Thermus thermophilus
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of special interest. The authors show that unlike many of the RNA-binding proteins whose structures have been determined to date, S15 is entirely α helical.
-
Berglund H, Rak A, Serganov A, Garber M, Hard T. Solution structure of the ribosomal RNA binding protein S15 from Thermus thermophilus. of special interest Nat Struct Biol. 4:1997;20-23 The authors show that unlike many of the RNA-binding proteins whose structures have been determined to date, S15 is entirely α helical.
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(1997)
Nat Struct Biol
, vol.4
, pp. 20-23
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Berglund, H.1
Rak, A.2
Serganov, A.3
Garber, M.4
Hard, T.5
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38
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0030774277
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The ribosome-in-pieces: Binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA
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Munishkin A, Wool IG. The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA. Proc Natl Acad Sci USA. 94:1997;12280-12284.
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Proc Natl Acad Sci USA
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, pp. 12280-12284
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Munishkin, A.1
Wool, I.G.2
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39
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0025999688
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Recognition of the highly conserved GTPase center of 23S ribosomal RNA by ribosomal protein L11 and the antibiotic thiostrepton
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Ryan PC, Lu M, Draper DE. Recognition of the highly conserved GTPase center of 23S ribosomal RNA by ribosomal protein L11 and the antibiotic thiostrepton. J Mol Biol. 221:1991;1257-1268.
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J Mol Biol
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Ryan, P.C.1
Lu, M.2
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40
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0029063715
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Stabilization of a ribosomal RNA tertiary structure by ribosomal protein L11
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Xing Y, Draper DE. Stabilization of a ribosomal RNA tertiary structure by ribosomal protein L11. J Mol Biol. 249:1995;319-331.
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J Mol Biol
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Xing, Y.1
Draper, D.E.2
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41
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0030020855
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Cooperative interactions of RNA and thiostrepton antibiotic with two domains of ribosomal protein L11
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Xing Y, Draper DE. Cooperative interactions of RNA and thiostrepton antibiotic with two domains of ribosomal protein L11. Biochemistry. 35:1996;1581-1588.
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Xing, Y.1
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0030948635
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In vitro evolution used to define a protein recognition site within a large RNA domain
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Sapag A, Draper DE. In vitro evolution used to define a protein recognition site within a large RNA domain. Bioorg Med Chem. 5:1997;1097-1105.
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Sapag, A.1
Draper, D.E.2
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43
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0031031915
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High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA
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of outstanding interest. of special interest. See annotation to [44].
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of outstanding interest Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA. High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. of special interest Nat Struct Biol. 4:1997;70-77 See annotation to [44].
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Nat Struct Biol
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Markus, M.A.1
Hinck, A.P.2
Huang, S.3
Draper, D.E.4
Torchia, D.A.5
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44
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0031024655
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The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains
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of outstanding interest. Together with [43], this paper describes the suprising finding that the RNA-binding domain of L11 is structurally homologous with homeodomain transcription factors. This paper provides a nice analysis of the structural and functional similarities between the two.
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Xing Y, Guha Thakurta D, Draper DE. The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains. of outstanding interest Nat Struct Biol. 4:1997;24-27 Together with [43], this paper describes the suprising finding that the RNA-binding domain of L11 is structurally homologous with homeodomain transcription factors. This paper provides a nice analysis of the structural and functional similarities between the two.
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(1997)
Nat Struct Biol
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Xing, Y.1
Guha Thakurta, D.2
Draper, D.E.3
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45
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0030681341
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The RNA binding domain of ribosomal protein L11: Three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA
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of outstanding interest. The NMR solution structure of L11 bound to RNA demonstrates how a flexible loop in the unbound protein becomes ordered in the RNA - protein complex.
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Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA. The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA. of outstanding interest J Mol Biol. 274:1997;101-113 The NMR solution structure of L11 bound to RNA demonstrates how a flexible loop in the unbound protein becomes ordered in the RNA - protein complex.
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(1997)
J Mol Biol
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, pp. 101-113
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Hinck, A.P.1
Markus, M.A.2
Huang, S.3
Grzesiek, S.4
Kustonovich, I.5
Draper, D.E.6
Torchia, D.A.7
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46
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0027270989
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Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
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Clark KL, Halay ED, Lai E, Burley SK. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature. 364:1993;412-420.
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Nature
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Clark, K.L.1
Halay, E.D.2
Lai, E.3
Burley, S.K.4
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47
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0029670530
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A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS- domain-DNA complex
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Kodandapani R, Pio F, Ni CZ, Piccialli G, Klemsz M, McKercher S, Maki RA, Ely KR. A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS- domain-DNA complex. Nature. 380:1996;456-460.
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Nature
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Kodandapani, R.1
Pio, F.2
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Piccialli, G.4
Klemsz, M.5
McKercher, S.6
Maki, R.A.7
Ely, K.R.8
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48
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0029913438
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RNA - Protein complexes
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Nagai K. RNA - protein complexes. Curr Opin Struct Biol. 6:1996;53-61.
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Nagai, K.1
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49
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0028097934
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Crystal structure of prokaryotic ribosomal protein L9: A bi-lobed RNA-binding protein
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Hoffman DW, Davies C, Gerchman SE, Kycia JH, Porter SJ, White SW, Ramakrishnan V. Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein. EMBO J. 13:1994;205-212.
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Hoffman, D.W.1
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Kycia, J.H.4
Porter, S.J.5
White, S.W.6
Ramakrishnan, V.7
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50
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0031471204
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The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
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of special interest. The repeated domain of S1 has a β fold that is highly similar to that of the E. coli cold shock protein. The authors provide a detailed analysis of the phylogenetic and functional relationships among this family of proteins.
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Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. of special interest Cell. 88:1997;235-242 The repeated domain of S1 has a β fold that is highly similar to that of the E. coli cold shock protein. The authors provide a detailed analysis of the phylogenetic and functional relationships among this family of proteins.
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(1997)
Cell
, vol.88
, pp. 235-242
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Bycroft, M.1
Hubbard, T.J.2
Proctor, M.3
Freund, S.M.4
Murzin, A.G.5
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51
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0031572233
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Ribosomal protein S7: A new RNA-binding motif with structural similarities to a DNA architectural factor
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of special interest. See annotation to [52].
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Hosaka H, Nakagawa A, Tanaka I, Harada N, Sano K, Kimura M, Yao M, Wakatsuki S. Ribosomal protein S7: a new RNA-binding motif with structural similarities to a DNA architectural factor. of special interest Structure. 5:1997;1199-1208 See annotation to [52].
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(1997)
Structure
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Hosaka, H.1
Nakagawa, A.2
Tanaka, I.3
Harada, N.4
Sano, K.5
Kimura, M.6
Yao, M.7
Wakatsuki, S.8
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52
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0031572181
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The structure of ribosomal protein S7 at 1.9 Å resolution reveals a beta-hairpin motif that binds double-stranded nucleic acids
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of special interest. Two structures [51,52] of ribosomal protein S7 at 2.5 and 1.9 Å, respectively, reveal an unexpected similarity with the E. coli integration host factor (IHF) and HU DNA-binding proteins. This suggests how the protein may bind to double-stranded RNA.
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Wimberly BT, White SW, Ramakrishnan V. The structure of ribosomal protein S7 at 1.9 Å resolution reveals a beta-hairpin motif that binds double-stranded nucleic acids. of special interest Structure. 5:1997;1187-1198 Two structures [51,52] of ribosomal protein S7 at 2.5 and 1.9 Å, respectively, reveal an unexpected similarity with the E. coli integration host factor (IHF) and HU DNA-binding proteins. This suggests how the protein may bind to double-stranded RNA.
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(1997)
Structure
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Wimberly, B.T.1
White, S.W.2
Ramakrishnan, V.3
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53
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0030806152
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A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA
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of outstanding interest. The authors present extensive genetic and biochemical arguments for a base-pairing switch in 16S rRNA during mRNA decoding. Perturbation of the equilibrium between these base pairings results in either error prone or hyperaccurate phenotypes in protein synthesis.
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Lodmell JS, Dahlberg AE. A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA. of outstanding interest Science. 277:1997;1262-1267 The authors present extensive genetic and biochemical arguments for a base-pairing switch in 16S rRNA during mRNA decoding. Perturbation of the equilibrium between these base pairings results in either error prone or hyperaccurate phenotypes in protein synthesis.
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(1997)
Science
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, pp. 1262-1267
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Lodmell, J.S.1
Dahlberg, A.E.2
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54
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0028090796
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Selective perturbation of G530 of 16S rRNA by translational miscoding agents and a streptomycin-dependence mutation in protein S12
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Powers T, Noller HF. Selective perturbation of G530 of 16S rRNA by translational miscoding agents and a streptomycin-dependence mutation in protein S12. J Mol Biol. 235:1994;156-172.
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J Mol Biol
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Powers, T.1
Noller, H.F.2
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