Conformers, dimers, and anticodon complexes of tRNAGlu2 (Escherichia coli)

Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity

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Structure of yeast phenylalanine tRNA at 3 Å resolution

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Three-Dimensional Tertiary Structure of Yeast Phenylalanine Transfer RNA

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Stability of ribonucleic acid double-stranded helices

Borer, P. N., Dengler, B., Tinoco, I., & Uhlenbeck, O. C. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90357-x · Cited by 762

The General Structure of Transfer RNA Molecules

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Conformational changes of transfer ribonucleic acid. Equilibrium phase diagrams

Cole, P. E., Yang, S. K., & Crothers, D. M. (1972) · Biochemistry · doi:10.1021/bi00773a024 · Cited by 232

Renaturation of transfer ribonucleic acids through site binding of magnesium.

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Molecular Mechanics of Translation : a Reciprocating Ratchet Mechanism

Woese, C. R. (1970) · Nature · doi:10.1038/226817a0 · Cited by 194

Three-dimensional structure of yeast phenylalanine transfer RNA at 3. 0Å resolution

Suddath, F. L., Quigley, G. J., McPherson, A., Sneden, D., Kim, J. J., Kim, S., & Rich, A. (1974) · Nature · doi:10.1038/248020a0 · Cited by 157

Complementary oligonucleotide binding to transfer RNA

Uhlenbeck, O. C. (1972) · Journal of Molecular Biology · doi:10.1016/0022-2836(72)90489-5 · Cited by 128

Studies of the complex between transfer RNAs with complementary anticodons

Grosjean, H., Söll, D. G., & Crothers, D. M. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90214-x · Cited by 234

Ribozyme-catalysed RNA synthesis using triplet building blocks

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Structure of an unmodified tRNA molecule

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Effect of modified nucleotides on Escherichia coli tRNAGlu structure and on its aminoacylation by glutamyl‐tRNA synthetase

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Conformational changes of yeast tRNAPhe and E. coli tRNA2Glu as indicated by different nuclease digestion patterns.

Wrede, P., Wurst, R. M., Vournakis, J. N., & Rich, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83559-7 · Cited by 82

A study of the interaction of Escherichia coli elongation factor-Tu with aminoacyl-tRNAs by partial digestion with cobra venom ribonuclease

Boutorin, A. S., Clark, B. F. C., Ebel, J. P., Kruse, T. A., Petersen, H. U., Rémy, P., & Vassilenko, S. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90271-0 · Cited by 71

Proton nuclear magnetic resonance of minor nucleosides in yeast phenylalanine transfer ribonucleic acid. Conformational changes as a consquence of aminoacylation, removal of the Y base, and codon-anticodon interaction

Davanloo, P., Sprinzl, M., & Cramer, F. (1979) · Biochemistry · doi:10.1021/bi00582a001 · Cited by 61

Allosteric interpretation of Mg2+ ion binding to the denaturable Escherichia coli tRNAGlu2

Bina-Stein, M., & Stein, A. (1976) · Biochemistry · doi:10.1021/bi00663a002 · Cited by 54

Purification and properties of tRNA(adenine-1)-methyltransferase from rat liver.

Glick, J. M., & Leboy, P. S. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40125-6 · Cited by 44

RNA structure

Kallenbach, N. R., & Berman, H. M. (1977) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500000202 · Cited by 44

Kinetics of tRNA folding monitored by aminoacylation

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Correlation between chemical modification and surface accessibility in yeast phenylalanine transfer RNA

Holbrook, S. R., & Kim, S. (1983) · Biopolymers · doi:10.1002/bip.360220410 · Cited by 40

Magnesium-dependent alternative foldings of active and inactive Escherichia coli tRNAGIU revealed by chemical probing

Madore, É., Florentz, C., Giegé, R., & Lapointe, J. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.17.3583 · Cited by 39

Role of Divalent Ions in Folding of tRNA

Leroy, J., Guéron, M., Thomas, G. D., & Favre, A. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11426.x · Cited by 37

Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Study of the interactions with its substrates

Kern, D., & Lapointe, J. (1979) · Biochemistry · doi:10.1021/bi00593a010 · Cited by 35

Structure of the ribotrinucleoside diphosphate codon UpUpC bound to tRNAPhe from yeast

Clore, G. M., Gronenborn, A. M., & McLaughlin, L. W. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90370-x · Cited by 35

The Solution Structure of Yeast tRNAPheas Studied by Nuclear Overhauser Effects in NMR

Hilbers, C. W., Heerschap, A., HAASNOOT, C. A. G., & Walters, J. A. L. I. (1983) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1983.10507434 · Cited by 35

The Modified Nucleosides in Transfer RNA

AGRIS, P. F., & Söll, D. G. (1977) · Elsevier eBooks · doi:10.1016/b978-0-12-722560-9.50024-x · Cited by 33

The structure of yeast tRNAAsp. A model for tRNA interacting with messenger RNA

Moras, D., Dock‐Brégeon, A., Dumas, P., Westhof, É., Romby, P., Ebel, J., & Giegé, R. (1985) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1985.10508436 · Cited by 30

On Codon-Anticodon Interactions

Grosjean, H., & Chantrenne, H. (1980) · Molecular biology, biochemistry, and biophysics · doi:10.1007/978-3-642-81503-4_27 · Cited by 29

A 13C NMR study of [5,8-13C2]spermidine binding to tRNA and to Escherichia coli macromolecules.

Frydman, B., Santos, C. D. L., & Frydman, R. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45297-5 · Cited by 26

Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction

Grosjean, H., Houssier, C., Romby, P., & Marquet, R. (2014) · ASM Press eBooks · doi:10.1128/9781555818296.ch7 · Cited by 25

Nuclear magnetic resonance studies of codon-anticodon interaction in tRNAPhe

Geerdes, H. A. M., BOOM, J. H. V., & Hilbers, C. W. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90045-5 · Cited by 25

Binding of spermidine to transfer ribonucleic acid

McMahon, M. E., & Erdmann, V. A. (1982) · Biochemistry · doi:10.1021/bi00264a025 · Cited by 20

High-resolution phosphorus nuclear magnetic resonance spectroscopy of transfer ribonucleic acids: multiple conformations in the anticodon loop

Gorenstein, D. G., & Goldfield, E. M. (1982) · Biochemistry · doi:10.1021/bi00266a018 · Cited by 19

Improved procedure for the isolation of a double-strand-specific ribonuclease and its application to structural analysis of various 5S rRNAs and tRNAs

Digweed, M., Pieler, T., KLUWE, D., SCHUSTER, L., Walker, R. T., & Erdmann, V. A. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09355.x · Cited by 18

tRNA and Aminoacyl-tRNA Synthetases

Ofengand, J. (1977) · Elsevier eBooks · doi:10.1016/b978-0-12-744250-1.50007-x · Cited by 16

Kinetics of the renaturation of yeast tRNA3Leu

Hawkins, E. R., Chang, S. H., & Mattice, W. L. (1977) · Biopolymers · doi:10.1002/bip.1977.360160714 · Cited by 15

Chapter 7 Codon Recognition: Evaluation of the Effects of Modified Bases in the Anticodon Loop of Trna Using the Temperature-Jump Relaxation Method

Grosjean, H., & Houssier, C. (1990) · Journal of chromatography library · doi:10.1016/s0301-4770(08)61473-6 · Cited by 13

Interaction of elongation factor Tu with the aminoacyl transfer ribonucleic acid dimer Phe-tRNA-Glu-tRNA

Yamane, T., Miller, D. L., & Hopfield, J. J. (1981) · Biochemistry · doi:10.1021/bi00505a034 · Cited by 13

Theoretical study of hydration of RNA

Kim, K., & John, M. S. (1979) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(79)90089-3 · Cited by 9

Laser light‐scattering analysis of the dimerization of transfer ribonucleic acids with complementary anticodons

Wang, C., Ford, N. C., & Fournier, M. J. (1981) · Biopolymers · doi:10.1002/bip.1981.360200111 · Cited by 7

High resolution phosphorus NMR spectroscopy of transfer ribonucleic acids

Gorenstein, D. G., & Goldfield, E. M. (1982) · Molecular and Cellular Biochemistry · doi:10.1007/bf00236777 · Cited by 7

PMR Studies of Secondary and Tertiary Structure of Transfer RNA in Solution

Bolton, P. H., & Kearns, D. R. (1978) · Biological magnetic resonance · doi:10.1007/978-1-4615-6534-5_3 · Cited by 6

Conformational Change of the L-Shaped tRNAPheMolecule

Nagamatsu, K. (1989) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1989.10507733 · Cited by 4

Conformational transition required for efficient splicing of transcripts from hybrid .lambda.-promoter yeast tRNA gene fusion

Shapero, M. H., & Greer, C. L. (1991) · Biochemistry · doi:10.1021/bi00240a017 · Cited by 3

Reactive Sites and the Evolution of Transfer RNAs

Dillon, L. S. (1978) · Springer eBooks · doi:10.1007/978-1-4684-2436-2_8

Société Belge De Biochimie Belgische Vereniging Voor Biochemie95: e Réunion, GAND, 13 décembre 1975 1. — Conférence

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Properties of a dimer of tRNATyr (Escherichia coli)

Yang, S. K., Soell, D., & Crothers, D. M. (1972) · Biochemistry · doi:10.1021/bi00762a016 · Cited by 33

tRNA-guanine transglycosylase from Escherichia coli: Recognition of dimeric, unmodified tRNATyr

Curnow, A. W., & Garcia, G. A. (1994) · Biochimie · doi:10.1016/0300-9084(94)90048-5 · Cited by 25

The so-called of Escherichia coli is a stable denatured conformer of the major isoacceptor

Tremblay, T.-L., & Lapointe, J. (1986) · Biochemistry and Cell Biology · doi:10.1139/o86-044 · Cited by 14

Magnesium-dependent alternative foldings of active and inactive Escherichia coli tRNAGIU revealed by chemical probing

Madore, É., Florentz, C., Giegé, R., & Lapointe, J. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.17.3583 · Cited by 39

The Solution Structure of the Escherichia coli Initiator tRNA and Its Interactions with Initiation Factor 2 and the Ribosomal 30 S Subunit

Wakao, H., Romby, P., Westhof, É., Laalami, S., GRUNBERG‐MANAGO, M., Ebel, J., Ehresmann, C., & Ehresmann, B. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47072-5 · Cited by 51