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Volumn 256, Issue 4, 1996, Pages 685-700

Major identity determinants in the "augmented D helix" of tRNAGlu from Escherichia coli

Author keywords

Aminoacyl tRNA synthetase; Footprinting; Steady state kinetics; tRNA identity; tRNA variant

Indexed keywords

BACTERIAL RNA; GLUTAMATE TRANSFER RNA LIGASE; GLUTAMIC ACID TRANSFER RNA;

EID: 0029969359     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0118     Document Type: Article
Times cited : (56)

References (79)
  • 1
    • 0015868989 scopus 로고
    • Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid
    • Agris, P. F., Söll, D. & Seno, T. (1973). Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid. Biochemistry, 12, 4331-4337.
    • (1973) Biochemistry , vol.12 , pp. 4331-4337
    • Agris, P.F.1    Söll, D.2    Seno, T.3
  • 4
    • 0022994045 scopus 로고
    • Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases
    • Breton, R., Sanfacon, H., Papayannopoulos, I., Biemann, K. & Lapointe, J. (1986). Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases. J. Biol. Chem. 261, 10610-10617.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10610-10617
    • Breton, R.1    Sanfacon, H.2    Papayannopoulos, I.3    Biemann, K.4    Lapointe, J.5
  • 5
    • 0025047458 scopus 로고
    • Glutamyl-tRNA synthetases of Bacillus subtilis 168T and of Bacillus stearothermophilus. Cloning and sequencing of the gltX genes and comparison with other aminoacyl-tRNA synthetases
    • Breton, R., Watson, D., Yaguchi, M. & Lapointe, J. (1990). Glutamyl-tRNA synthetases of Bacillus subtilis 168T and of Bacillus stearothermophilus. Cloning and sequencing of the gltX genes and comparison with other aminoacyl-tRNA synthetases. J. Biol. Chem. 265, 18248-18255.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18248-18255
    • Breton, R.1    Watson, D.2    Yaguchi, M.3    Lapointe, J.4
  • 8
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani, G., Delarue, M., Poch, O., Gangloff, J. & Moras, D. (1990). Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature, 347, 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 10
    • 0024959463 scopus 로고
    • Aminoacylation of RNA minihelices with alanine
    • Francklyn, C. & Schimmel, P. (1989). Aminoacylation of RNA minihelices with alanine. Nature, 337, 478-481.
    • (1989) Nature , vol.337 , pp. 478-481
    • Francklyn, C.1    Schimmel, P.2
  • 11
    • 0025114689 scopus 로고
    • Enzymatic aminoacylation of an eight-base-pair microhelix with histidine
    • Francklyn, C. & Schimmel, P. (1990). Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. Proc. Natl Acad. Sci. USA, 87, 8655-8659.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8655-8659
    • Francklyn, C.1    Schimmel, P.2
  • 12
    • 0026561924 scopus 로고
    • Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices
    • Francklyn, C., Shi, J.-P. & Schimmel, P. (1992). Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices. Science, 255, 1121-1125.
    • (1992) Science , vol.255 , pp. 1121-1125
    • Francklyn, C.1    Shi, J.-P.2    Schimmel, P.3
  • 14
    • 0021530217 scopus 로고
    • Purification and characterization of glutamyl-tRNA synthetase from an extreme thermophile, Thermus thermophilus HB8
    • Hara-Yokoyama, M., Yokoyama, S. & Miyazawa, T. (1984). Purification and characterization of glutamyl-tRNA synthetase from an extreme thermophile, Thermus thermophilus HB8. J. Biochem. 96, 1599-1607.
    • (1984) J. Biochem. , vol.96 , pp. 1599-1607
    • Hara-Yokoyama, M.1    Yokoyama, S.2    Miyazawa, T.3
  • 18
    • 0028258296 scopus 로고
    • Structural elements that contribute to an unusual tertiary interaction in a transfer RNA
    • Hou, Y.-M. (1994). Structural elements that contribute to an unusual tertiary interaction in a transfer RNA. Biochemistry, 33, 4677-4681.
    • (1994) Biochemistry , vol.33 , pp. 4677-4681
    • Hou, Y.-M.1
  • 19
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou, Y.-M. & Schimmel, P. (1988). A simple structural feature is a major determinant of the identity of a transfer RNA. Nature, 333, 140-145.
    • (1988) Nature , vol.333 , pp. 140-145
    • Hou, Y.-M.1    Schimmel, P.2
  • 20
    • 0027313443 scopus 로고
    • An unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA
    • Hou, Y.-M., Westhof, E. & Giegé, R. (1993). An unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA. Proc. Natl. Acad. Sci. USA, 90, 6776-6780.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6776-6780
    • Hou, Y.-M.1    Westhof, E.2    Giegé, R.3
  • 21
    • 0025887667 scopus 로고
    • Glnare major recognition elements for E. Coli glutaminyl-tRNA synthetase
    • Glnare major recognition elements for E. coli glutaminyl-tRNA synthetase. Nature, 352, 258-260.
    • (1991) Nature , vol.352 , pp. 258-260
    • Jahn, M.1    Rogers, M.J.2    Söll, D.3
  • 22
    • 0018801590 scopus 로고
    • Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Effect of alteration of the 5-methylaminomethyl-2-thiouridine in the anticodon of glutamic acid transfer ribonucleic acid on the catalytic mechanism
    • Kern, D. & Lapointe, J. (1979). Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Effect of alteration of the 5-methylaminomethyl-2-thiouridine in the anticodon of glutamic acid transfer ribonucleic acid on the catalytic mechanism. Biochemistry, 18, 5819-5826.
    • (1979) Biochemistry , vol.18 , pp. 5819-5826
    • Kern, D.1    Lapointe, J.2
  • 24
    • 0025331936 scopus 로고
    • Construction of Escherichia coli amber suppressor tRNA genes. II. Synthesis of additional tRNA genes and improvement of suppressor efficiency
    • Kleina, L. G., Masson, J.-M., Normanly J., Abelson, J. & Miller, J. H. (1990). Construction of Escherichia coli amber suppressor tRNA genes. II. Synthesis of additional tRNA genes and improvement of suppressor efficiency. J. Mol. Biol. 213, 705-717.
    • (1990) J. Mol. Biol. , vol.213 , pp. 705-717
    • Kleina, L.G.1    Masson, J.-M.2    Normanly, J.3    Abelson, J.4    Miller, J.H.5
  • 26
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA, 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 28
    • 0027992228 scopus 로고
    • Evolution of the Glx-tRNA synthetase family: The glutaminyl enzyme as a case of horizontal gene transfer
    • Lamour, V., Quevillon, S., Diriong, S., N'Guyen, V. C., Lipinski, M. & Mirande, M. (1994). Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad. Sci. USA, 91, 8670-8674.
    • (1994) Proc Natl Acad. Sci. USA , vol.91 , pp. 8670-8674
    • Lamour, V.1    Quevillon, S.2    Diriong, S.3    N'Guyen, V.C.4    Lipinski, M.5    Mirande, M.6
  • 31
    • 0023261832 scopus 로고
    • Differences between transfer RNA molecules
    • McClain, W. H. & Nicolas, H. B., Jr (1987). Differences between transfer RNA molecules. J. Mol. Biol. 194, 635-642.
    • (1987) J. Mol. Biol. , vol.194 , pp. 635-642
    • McClain, W.H.1    Nicolas H.B., Jr.2
  • 32
    • 0024279871 scopus 로고
    • Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end
    • McClain, W. H. & Foss, K. (1988a). Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end. Science, 240, 793-796.
    • (1988) Science , vol.240 , pp. 793-796
    • McClain, W.H.1    Foss, K.2
  • 34
    • 0024300362 scopus 로고
    • Changing the acceptor identity of transfer RNA by altering nucleotides in a "variable pocket"
    • McClain, W. H. & Foss, K. (1988c). Changing the acceptor identity of transfer RNA by altering nucleotides in a "variable pocket". Science, 241, 1804-1807.
    • (1988) Science , vol.241 , pp. 1804-1807
    • McClain, W.H.1    Foss, K.2
  • 35
    • 0024295537 scopus 로고
    • Association of transfer RNA acceptor identity with a helical irregularity
    • McClain, W. H, Chen, Y.-M., Foss, K & Schneider, J. (1988). Association of transfer RNA acceptor identity with a helical irregularity Science, 242, 1681-1684.
    • (1988) Science , vol.242 , pp. 1681-1684
    • McClain, W.H.1    Chen, Y.-M.2    Foss, K.3    Schneider, J.4
  • 38
    • 0023734317 scopus 로고
    • Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification
    • Muramatsu, T., Nishikawa, K., Nemoto, F., Kuchino, Y., Nishimura, S., Miyazawa, T. & Yokoyama, S. (1988). Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification. Nature, 336, 179-181.
    • (1988) Nature , vol.336 , pp. 179-181
    • Muramatsu, T.1    Nishikawa, K.2    Nemoto, F.3    Kuchino, Y.4    Nishimura, S.5    Miyazawa, T.6    Yokoyama, S.7
  • 39
    • 0026766983 scopus 로고
    • Functional contacts of a transfer RNA synthetase with 2′-hydroxyl groups in the RNA minor groove
    • Musier-Forsyth, K. & Schimmel, P. (1992). Functional contacts of a transfer RNA synthetase with 2′-hydroxyl groups in the RNA minor groove. Nature, 357, 513-515.
    • (1992) Nature , vol.357 , pp. 513-515
    • Musier-Forsyth, K.1    Schimmel, P.2
  • 40
    • 0025850420 scopus 로고
    • Specificity for aminoacylation of an RNA helix: An unpaired, exocyclic amino group in the minor groove
    • Musier-Forsyth, K., Usman, N., Scaringe, S., Doudna, J., Green, R. & Schimmel, P. (1991). Specificity for aminoacylation of an RNA helix: an unpaired, exocyclic amino group in the minor groove. Science, 253, 784-786.
    • (1991) Science , vol.253 , pp. 784-786
    • Musier-Forsyth, K.1    Usman, N.2    Scaringe, S.3    Doudna, J.4    Green, R.5    Schimmel, P.6
  • 42
  • 43
    • 0025337664 scopus 로고
    • Construction of Escherichia coli amber suppressor tRNA genes. III. Determination of tRNA specificity
    • Normanly J., Kleina, L. G., Masson, J.-M., Abelson, J. & Miller, J. H. (1990). Construction of Escherichia coli amber suppressor tRNA genes. III. Determination of tRNA specificity J. Mol. Biol. 213, 719-726.
    • (1990) J. Mol. Biol. , vol.213 , pp. 719-726
    • Normanly, J.1    Kleina, L.G.2    Masson, J.-M.3    Abelson, J.4    Miller, J.H.5
  • 44
    • 0002987160 scopus 로고
    • Conformational change of tRNA upon interaction of the identity-determinant set with aminoacyl-tRNA synthetase
    • Nierhaus, K. H., Franceschi, F., Subramanian, A. R., Erdmann, V. A. & Wittmann-Liebold, B., eds, Plenum Press, New York and London
    • Nureki, O., Niimi, T., Muto, Y., Kanno, H., Kohno, T., Muramatsu, T., Kawai, G., Miyazawa, T., Giegé, R., Florentz, C. & Yokoyama, S. (1993). Conformational change of tRNA upon interaction of the identity-determinant set with aminoacyl-tRNA synthetase. In The Translational Apparatus: Structure, Function, Regulation, Evolution (Nierhaus, K. H., Franceschi, F., Subramanian, A. R., Erdmann, V. A. & Wittmann-Liebold, B., eds), pp. 59-66, Plenum Press, New York and London.
    • (1993) The Translational Apparatus: Structure, Function, Regulation, Evolution , pp. 59-66
    • Nureki, O.1    Niimi, T.2    Muto, Y.3    Kanno, H.4    Kohno, T.5    Muramatsu, T.6    Kawai, G.7    Miyazawa, T.8    Giegé, R.9    Florentz, C.10    Yokoyama, S.11
  • 45
    • 0028266202 scopus 로고
    • Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli
    • Nureki, O., Niimi, T., Muramatsu, T., Kanno, H., Kohno, T., Florentz, C., Giegé, R. & Yokoyama, S. (1994). Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli. J. Mol. Biol. 236, 710-724.
    • (1994) J. Mol. Biol. , vol.236 , pp. 710-724
    • Nureki, O.1    Niimi, T.2    Muramatsu, T.3    Kanno, H.4    Kohno, T.5    Florentz, C.6    Giegé, R.7    Yokoyama, S.8
  • 47
    • 0013505610 scopus 로고
    • Primary sequence of glutamic acid tRNA II from Escherichia coli
    • Ohashi, Z., Harada, F. & Nishimura, S. (1972). Primary sequence of glutamic acid tRNA II from Escherichia coli. FEBS Letters, 20, 239-241.
    • (1972) FEBS Letters , vol.20 , pp. 239-241
    • Ohashi, Z.1    Harada, F.2    Nishimura, S.3
  • 48
    • 0026726152 scopus 로고
    • The anticodon and discriminator base are major determinants of cysteine tRNA identity in vivo
    • Pallanck, L., Li, S. & Schulman, L. H. (1992). The anticodon and discriminator base are major determinants of cysteine tRNA identity in vivo. J. Biol. Chem. 267, 7221-7223.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7221-7223
    • Pallanck, L.1    Li, S.2    Schulman, L.H.3
  • 49
    • 0026482716 scopus 로고
    • Determination of recognition nucleotides for Escherichia coli phenylalanyl-tRNA synthetase
    • Peterson, E. T. & Uhlenbeck, O. C. (1992). Determination of recognition nucleotides for Escherichia coli phenylalanyl-tRNA synthetase. Biochemistry, 31, 10380-10389.
    • (1992) Biochemistry , vol.31 , pp. 10380-10389
    • Peterson, E.T.1    Uhlenbeck, O.C.2
  • 50
    • 0027157726 scopus 로고
    • Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase
    • Puglisi, J. D., Pütz, J., Florentz, C. & Giegé, R. (1993). Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase. Nucl. Acids Res. 21, 41-49.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 41-49
    • Puglisi, J.D.1    Pütz, J.2    Florentz, C.3    Giegé, R.4
  • 53
    • 0027764213 scopus 로고
    • Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity
    • Rogers, K. C. & Söll, D. (1993). Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity Biochemistry, 32, 14210-14219.
    • (1993) Biochemistry , vol.32 , pp. 14210-14219
    • Rogers, K.C.1    Söll, D.2
  • 56
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • Rould, M. A., Perona, J. J. & Steitz, T. A. (1991). Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature, 352, 213-218.
    • (1991) Nature , vol.352 , pp. 213-218
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 58
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson, J. R. & Uhlenbeck, O. C. (1988). Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl Acad. Sci. USA, 85, 1033-1037.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 61
    • 0015221041 scopus 로고
    • Selective inactivation of amino acid acceptor and ribosome-binding activities of Escherichia coli tRNA by modification with cyanogen bromide
    • Saneyoshi, M. & Nishimura, S. (1971). Selective inactivation of amino acid acceptor and ribosome-binding activities of Escherichia coli tRNA by modification with cyanogen bromide. Biochim. Biophys. Acta, 246, 123-131.
    • (1971) Biochim. Biophys. Acta , vol.246 , pp. 123-131
    • Saneyoshi, M.1    Nishimura, S.2
  • 62
    • 0024574202 scopus 로고
    • Parameters for the molecular recognition of transfer RNAs
    • Schimmel, P. (1989). Parameters for the molecular recognition of transfer RNAs. Biochemistry, 28, 2747-2759.
    • (1989) Biochemistry , vol.28 , pp. 2747-2759
    • Schimmel, P.1
  • 63
    • 0024285823 scopus 로고
    • Protein biosynthesis in organelles requires misaminoacylation of tRNA
    • Schön, A., Kannangara, G., Gough, S. & Söll, D. (1988). Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature, 31, 187-190.
    • (1988) Nature , vol.31 , pp. 187-190
    • Schön, A.1    Kannangara, G.2    Gough, S.3    Söll, D.4
  • 64
    • 0025932660 scopus 로고
    • Recognition of tRNAs by aminoacyl-tRNA synthetases
    • Schulman, L. H. (1991). Recognition of tRNAs by aminoacyl-tRNA synthetases. Prog. Nucl. Acids Res. Mol. Biol. 41, 23-87.
    • (1991) Prog. Nucl. Acids Res. Mol. Biol. , vol.41 , pp. 23-87
    • Schulman, L.H.1
  • 65
    • 0019230068 scopus 로고
    • 1 gene and the transcription termination signal in the Escherichia coli ribosomal RNA operon rrnF (or G)
    • 1 gene and the transcription termination signal in the Escherichia coli ribosomal RNA operon rrnF (or G). Nucl. Acids Res. 8, 3809-3827.
    • (1980) Nucl. Acids Res. , vol.8 , pp. 3809-3827
    • Sekiya, T.1    Mori, M.2    Takahashi, N.3    Nishimura, S.4
  • 66
    • 0016188393 scopus 로고
    • Glu in the specific interaction with cognate aminoacyl-tRNA synthetase. Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation
    • Glu in the specific interaction with cognate aminoacyl-tRNA synthetase. Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation. Biochim. Biophys. Acta, 349, 328-338.
    • (1974) Biochim. Biophys. Acta , vol.349 , pp. 328-338
    • Seno, T.1    Agris, P.2    Söll, D.3
  • 67
    • 0027074048 scopus 로고
    • Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants
    • Sherman, J. M., Rogers, K., Rogers, M. J. & Söll, D. (1992). Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants. J. Mol. Biol. 228, 1055-1062.
    • (1992) J. Mol. Biol. , vol.228 , pp. 1055-1062
    • Sherman, J.M.1    Rogers, K.2    Rogers, M.J.3    Söll, D.4
  • 68
    • 0026495236 scopus 로고
    • The role of anticodon bases and the discriminator nucleotide in the recognition of some E. coli tRNAs by their aminoacyl-tRNA synthetases
    • Shimizu, M., Asahara, H., Tamura, K., Hasegawa, T. & Himeno, H. (1992). The role of anticodon bases and the discriminator nucleotide in the recognition of some E. coli tRNAs by their aminoacyl-tRNA synthetases. J. Mol. Evol. 35, 436-443.
    • (1992) J. Mol. Evol. , vol.35 , pp. 436-443
    • Shimizu, M.1    Asahara, H.2    Tamura, K.3    Hasegawa, T.4    Himeno, H.5
  • 69
    • 0029976249 scopus 로고    scopus 로고
    • Compilation of tRNA sequences and sequences of tRNA genes
    • in the press
    • Steegborn C. Steinberg, S., Huebel, F. & Sprinzl, M. (1996). Compilation of tRNA sequences and sequences of tRNA genes. Nucl. Acids Res. 24, in the press.
    • (1996) Nucl. Acids Res. , vol.24
    • Steegborn, C.1    Steinberg, S.2    Huebel, F.3    Sprinzl, M.4
  • 70
    • 0028955347 scopus 로고
    • Minor groove recognition of the conserved G·U pair at the Tetrahymena ribozyme reaction site
    • Strobel, S. A. & Cech, T. R. (1995). Minor groove recognition of the conserved G·U pair at the Tetrahymena ribozyme reaction site. Science, 267, 675-679.
    • (1995) Science , vol.267 , pp. 675-679
    • Strobel, S.A.1    Cech, T.R.2
  • 71
    • 0018077590 scopus 로고
    • Crystal structure of yeast phenylalanine transfer RNA. I. Crystallographic refinement
    • Sussman, J. L., Holbrook, S. R., Warrant, R. W., Church, G. M. & Kim, S. H. (1978). Crystal structure of yeast phenylalanine transfer RNA. I. Crystallographic refinement. J. Mol. Biol. 123, 607-630.
    • (1978) J. Mol. Biol. , vol.123 , pp. 607-630
    • Sussman, J.L.1    Holbrook, S.R.2    Warrant, R.W.3    Church, G.M.4    Kim, S.H.5
  • 73
    • 0029562954 scopus 로고
    • A three-dimensional structure model of the complex of glutamyl-tRNA synthetase and its cognate tRNA
    • Tateno, M., Nureki, O., Sekine, S., Kaneda, K., Gō, M. & Yokoyama, S. (1995). A three-dimensional structure model of the complex of glutamyl-tRNA synthetase and its cognate tRNA. FEBS Letters, 377, 77-81.
    • (1995) FEBS Letters , vol.377 , pp. 77-81
    • Tateno, M.1    Nureki, O.2    Sekine, S.3    Kaneda, K.4    Go, M.5    Yokoyama, S.6
  • 75
    • 0019617028 scopus 로고
    • Tertiary structure of tRNAs in solution monitored by phosphodiester modification with ethylnitrosourea
    • Vlassov, V. V., Giegé, R. & Ebel, J. (1981). Tertiary structure of tRNAs in solution monitored by phosphodiester modification with ethylnitrosourea. Eur. J. Biochem. 119, 51-59.
    • (1981) Eur. J. Biochem. , vol.119 , pp. 51-59
    • Vlassov, V.V.1    Giegé, R.2    Ebel, J.3
  • 76
    • 0021879256 scopus 로고
    • Crystallographic refinement of yeast aspartic acid transfer RNA
    • Westhof, E., Dumas, P. & Moras, D. (1985). Crystallographic refinement of yeast aspartic acid transfer RNA. J. Mol. Biol. 184, 119-145.
    • (1985) J. Mol. Biol. , vol.184 , pp. 119-145
    • Westhof, E.1    Dumas, P.2    Moras, D.3
  • 77
    • 0024276561 scopus 로고
    • tRNA identity: A hair of the dogma that bit us
    • Yarus, M. (1988). tRNA identity: a hair of the dogma that bit us. Cell, 55, 739-741.
    • (1988) Cell , vol.55 , pp. 739-741
    • Yarus, M.1
  • 78
    • 0018719498 scopus 로고
    • Three-dimensional structure of hyper-modified nucleoside Q located in the wobbling position of tRNA
    • Yokoyama, S., Miyazawa, T., Iitaka, Y., Yamaizumi, Z., Kasai, H. & Nishimura, S. (1979). Three-dimensional structure of hyper-modified nucleoside Q located in the wobbling position of tRNA. Nature, 282, 107-109.
    • (1979) Nature , vol.282 , pp. 107-109
    • Yokoyama, S.1    Miyazawa, T.2    Iitaka, Y.3    Yamaizumi, Z.4    Kasai, H.5    Nishimura, S.6
  • 79
    • 0025760054 scopus 로고
    • Rapid and simple purification of T7 RNA polymerase
    • Zawadzki, V. & Gross, H. J. (1991). Rapid and simple purification of T7 RNA polymerase. Nucl. Acids Res. 19, 1948.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 1948
    • Zawadzki, V.1    Gross, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.