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Volumn 25, Issue 2, 1996, Pages 237-252

Protein structure and the sequential structure of mRNA: α-Helix and β- sheet signals at the nucleotide level

Author keywords

computer prediction; cotranslational folding; neural network; protein secondary structure; reading frame; ribosome

Indexed keywords

MESSENGER RNA;

EID: 0029902243     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199606)25:2<237::AID-PROT9>3.3.CO;2-Y     Document Type: Article
Times cited : (59)

References (73)
  • 1
    • 0023046874 scopus 로고
    • Codon usage in yeast: Cluster analysis clearly differentiates highly and lowly expressed genes
    • Sharp, P.M., Tuohy, T.M.F., Mosurski, K.R. Codon usage in yeast: Cluster analysis clearly differentiates highly and lowly expressed genes. Nucleic Acids Res. 14:5125-5143, 1986.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 5125-5143
    • Sharp, P.M.1    Tuohy, T.M.F.2    Mosurski, K.R.3
  • 2
    • 0023115826 scopus 로고
    • Occurrence of nucleotide triplets in genes and secondary structure of the coded proteins
    • Kypr, J., Mràzek, J. Occurrence of nucleotide triplets in genes and secondary structure of the coded proteins. Int. J. Biol. Macromol. 9:49-53, 1987.
    • (1987) Int. J. Biol. Macromol. , vol.9 , pp. 49-53
    • Kypr, J.1    Mràzek, J.2
  • 3
    • 0023134450 scopus 로고
    • Translation rate modification by preferential codon usage: Intragenic position effects
    • Liljenström, H., Heijne, von G. Translation rate modification by preferential codon usage: Intragenic position effects. J. Theor. Biol. 124:43-55, 1987.
    • (1987) J. Theor. Biol. , vol.124 , pp. 43-55
    • Liljenström, H.1    Von Heijne, G.2
  • 4
    • 0024619015 scopus 로고
    • Features of the cell-free translation of a spider fibrion mRNA
    • Candelas, G.C., Ortiz, A., Ortiz, N. Features of the cell-free translation of a spider fibrion mRNA. Biochem. Cell Biol. 67:173-176, 1989.
    • (1989) Biochem. Cell Biol. , vol.67 , pp. 173-176
    • Candelas, G.C.1    Ortiz, A.2    Ortiz, N.3
  • 5
    • 0024405193 scopus 로고
    • Codon usage determines translation rate in Escherichia coli
    • Sørensen, M.A., Kurland, C.G., Pedersen, S. Codon usage determines translation rate in Escherichia coli. J. Mol. Biol. 207:365-377, 1989.
    • (1989) J. Mol. Biol. , vol.207 , pp. 365-377
    • Sørensen, M.A.1    Kurland, C.G.2    Pedersen, S.3
  • 6
    • 0026584271 scopus 로고
    • Protein folding within the cell
    • Gething, M., Sambrook, J. Protein folding within the cell. Nature 355:33-45, 1992.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.1    Sambrook, J.2
  • 7
    • 0027189824 scopus 로고
    • Discrete nascent chain lengths are required for the insertionof presecretory proteins into microsomal membranes
    • Wolin, S.L., Walter, P. Discrete nascent chain lengths are required for the insertionof presecretory proteins into microsomal membranes. J. Cell. Biol. 121:1211-1219, 1993.
    • (1993) J. Cell. Biol. , vol.121 , pp. 1211-1219
    • Wolin, S.L.1    Walter, P.2
  • 8
    • 0023659927 scopus 로고
    • The efficiency of folding of some proteins is increased by controlled rates of translation in vivo - A hypothesis
    • Purvis, I.J., Bettany, A.J., Santiago, T.C., Coggins, J.R., Duncan, K., Eason, R., Brown, A.J. The efficiency of folding of some proteins is increased by controlled rates of translation in vivo - a hypothesis. J. Mol. Biol. 193:413-417, 1987.
    • (1987) J. Mol. Biol. , vol.193 , pp. 413-417
    • Purvis, I.J.1    Bettany, A.J.2    Santiago, T.C.3    Coggins, J.R.4    Duncan, K.5    Eason, R.6    Brown, A.J.7
  • 9
    • 0026459383 scopus 로고
    • Protein folding within the cell is influenced by controlled rates of polypeptide elongation
    • Crombie, T., Swaffield, J., Brown, A.J.P. Protein folding within the cell is influenced by controlled rates of polypeptide elongation. J. Mol. Biol. 228:7-12, 1992.
    • (1992) J. Mol. Biol. , vol.228 , pp. 7-12
    • Crombie, T.1    Swaffield, J.2    Brown, A.J.P.3
  • 10
    • 0027218791 scopus 로고
    • Folding of the MS2 coat protein in Escherichia coli is modulated by translational pauses resulting from mRNA secondary structure and codon usage: A hypothesis
    • Guisez, Y., Robbins, J., Remaut, E., Fiers, W. Folding of the MS2 coat protein in Escherichia coli is modulated by translational pauses resulting from mRNA secondary structure and codon usage: A hypothesis. J. Theor. Biol. 162:243-252, 1993.
    • (1993) J. Theor. Biol. , vol.162 , pp. 243-252
    • Guisez, Y.1    Robbins, J.2    Remaut, E.3    Fiers, W.4
  • 11
    • 0024257727 scopus 로고
    • The role of clusters of rare codons in determining the bound-aries of portions of the polypeptide chain with a monotypic secondary structure in the process of co-translational folding of the protein
    • Krasheninnikov, I.A., Komar, A.A., Adzhubei, I.A. The role of clusters of rare codons in determining the bound-aries of portions of the polypeptide chain with a monotypic secondary structure in the process of co-translational folding of the protein. Dokl. Akad., Nauk. S.S.S.R. 303:995-999, 1988.
    • (1988) Dokl. Akad., Nauk. S.S.S.R. , vol.303 , pp. 995-999
    • Krasheninnikov, I.A.1    Komar, A.A.2    Adzhubei, I.A.3
  • 12
    • 0026047846 scopus 로고
    • Non-uniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational folding model
    • Krasheninnikov, I.A., Komar, A.A., Adzhubei, I.A. Non-uniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational folding model. J. Prot. Chem. 10:445-453, 1991.
    • (1991) J. Prot. Chem. , vol.10 , pp. 445-453
    • Krasheninnikov, I.A.1    Komar, A.A.2    Adzhubei, I.A.3
  • 13
    • 0016209912 scopus 로고
    • Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure
    • Lim, V.I. Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure. J. Mol. Biol. 88:857-872, 1974.
    • (1974) J. Mol. Biol. , vol.88 , pp. 857-872
    • Lim, V.I.1
  • 14
    • 0016162558 scopus 로고
    • Algorithms for prediction of alpha-helical and beta-structural regions in globular proteins
    • Lim, V.I. Algorithms for prediction of alpha-helical and beta-structural regions in globular proteins. J. Mol. Biol. 88:873-894, 1974.
    • (1974) J. Mol. Biol. , vol.88 , pp. 873-894
    • Lim, V.I.1
  • 15
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformations
    • Chou, P.Y., Fasman, G.D. Empirical predictions of protein conformations. Annu. Rev. Biochem. 47:251-276, 1978.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 16
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P.Y., Fasman, G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 47:45-48, 1978.
    • (1978) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-48
    • Chou, P.Y.1    Fasman, G.D.2
  • 17
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Gamier, J., Osguthorpe, D.J., Robson, B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120, 1978.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Gamier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 18
    • 0021097529 scopus 로고
    • How good are predictions of protein secondary structure?
    • Kabsch, W., Sander, C. How good are predictions of protein secondary structure? FEBS Lett. 155:179-182, 1983.
    • (1983) FEBS Lett. , vol.155 , pp. 179-182
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0023803244 scopus 로고
    • Predicting the secondary structure of globular proteins using neural network models
    • Qian, N., Sejnowski, T.J. Predicting the secondary structure of globular proteins using neural network models. J. Mol. Biol. 202:865-884, 1988.
    • (1988) J. Mol. Biol. , vol.202 , pp. 865-884
    • Qian, N.1    Sejnowski, T.J.2
  • 22
    • 0000268209 scopus 로고
    • Protein secondary structure prediction with a neural network
    • Holley, L.H., Karplus, M. Protein secondary structure prediction with a neural network. Proc. Natl. Acad. Sci., U.S.A. 86:152-156, 1989.
    • (1989) Proc. Natl. Acad. Sci., U.S.A. , vol.86 , pp. 152-156
    • Holley, L.H.1    Karplus, M.2
  • 23
    • 0024412170 scopus 로고
    • Prediction of beta-turns in proteins using neural networks
    • MacGregor, M.J., Flores, T.P., Sternberg, M.J.E. Prediction of beta-turns in proteins using neural networks. Protein Eng, 2:521-526, 1989.
    • (1989) Protein Eng , vol.2 , pp. 521-526
    • MacGregor, M.J.1    Flores, T.P.2    Sternberg, M.J.E.3
  • 24
    • 0025334980 scopus 로고
    • Improvements in protein secondary prediction by an enhanced neural network
    • Kneller, D.G., Cohen, F.E., Langridge, R. Improvements in protein secondary prediction by an enhanced neural network. J. Mol. Biol. 214:171-182, 1990.
    • (1990) J. Mol. Biol. , vol.214 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 25
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., Sander, C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584-599, 1993.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 26
    • 0344397947 scopus 로고
    • Correlation between protein secondary structure and the mRNA nucleotide sequence
    • Bohr, H., Brunak, S., (eds.). Amsterdam: IOS Press
    • Brunak, S., Engelbrecht, J., Kesmir, C. Correlation between protein secondary structure and the mRNA nucleotide sequence. In: "Protein Structure by Distance Analysis." Bohr, H., Brunak, S., (eds.). Amsterdam: IOS Press, 1994:327-334.
    • (1994) Protein Structure by Distance Analysis , pp. 327-334
    • Brunak, S.1    Engelbrecht, J.2    Kesmir, C.3
  • 27
    • 0025036111 scopus 로고
    • Ribosome gymnastics - degree of difficulty 9.5, style 10.0
    • Atkins, J.F., Weiss, R.B., Gesteland, R.F. Ribosome gymnastics - degree of difficulty 9.5, style 10.0. Cell 62:413-423, 1990.
    • (1990) Cell , vol.62 , pp. 413-423
    • Atkins, J.F.1    Weiss, R.B.2    Gesteland, R.F.3
  • 28
    • 0026317770 scopus 로고
    • Towards a genetic dissection of the basis of triplet decoding, and its natural subversion: Programmed reading frame shifts and hops
    • Atkins, J.F., Weiss, R.B., Thompson, S., Gesteland, R.F. Towards a genetic dissection of the basis of triplet decoding, and its natural subversion: Programmed reading frame shifts and hops. Annu. Rev. Genet. 25:201-228, 1991.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 201-228
    • Atkins, J.F.1    Weiss, R.B.2    Thompson, S.3    Gesteland, R.F.4
  • 29
    • 0023194889 scopus 로고
    • Translation framing code and frame-monitoring mechanism as suggested by the analysis of mRNA and 16S rRNA nucleotide sequences
    • Trifonov, E.N. Translation framing code and frame-monitoring mechanism as suggested by the analysis of mRNA and 16S rRNA nucleotide sequences. J. Mol. Biol. 194: 643-652, 1987.
    • (1987) J. Mol. Biol. , vol.194 , pp. 643-652
    • Trifonov, E.N.1
  • 30
    • 0026778490 scopus 로고
    • Recognition of correct reading frame by the ribosome
    • Trifonov, E.N. Recognition of correct reading frame by the ribosome. Biochimie 74:357-362, 1992.
    • (1992) Biochimie , vol.74 , pp. 357-362
    • Trifonov, E.N.1
  • 31
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical feature
    • Kabsch, W., Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical feature. Biopolymers 22:2577-2637, 1983.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 32
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • Pearson, R. Rapid and sensitive sequence comparison with FASTP and FASTA. Methods Enzymol. 183:63-98, 1990.
    • (1990) Methods Enzymol. , vol.183 , pp. 63-98
    • Pearson, R.1
  • 33
    • 0025765686 scopus 로고
    • The protein structure code: What is its present status?
    • Garnier, J., Levin, J.M. The protein structure code: What is its present status? CABIOS 7:133-142, 1991.
    • (1991) CABIOS , vol.7 , pp. 133-142
    • Garnier, J.1    Levin, J.M.2
  • 38
    • 0025744474 scopus 로고
    • Prediction of human mRNA donor and acceptor sites from the DNA sequence
    • Brunak, S., Engelbrecht, J., Knudsen, S. Prediction of human mRNA donor and acceptor sites from the DNA sequence. J. Mol. Biol. 220:49-65, 1991.
    • (1991) J. Mol. Biol. , vol.220 , pp. 49-65
    • Brunak, S.1    Engelbrecht, J.2    Knudsen, S.3
  • 40
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon, C.E. A mathematical theory of communication. Bell System Tech. J. 27:379-423/623-656, 1948.
    • (1948) Bell System Tech. J. , vol.27 , pp. 379-423
    • Shannon, C.E.1
  • 41
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider, T.D., Stephens, R.M. Sequence logos: A new way to display consensus sequences. Nucleic Acids Res. 18:6097-6100, 1990.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 42
    • 0028237028 scopus 로고
    • A graphic approach to analyzing codon usage in 1563 Escherichia coli protein coding sequences
    • Zhang, C.-T., Chou, K.-C. A graphic approach to analyzing codon usage in 1563 Escherichia coli protein coding sequences. J. Mol. Biol. 238:1-8, 1994.
    • (1994) J. Mol. Biol. , vol.238 , pp. 1-8
    • Zhang, C.-T.1    Chou, K.-C.2
  • 43
    • 0016772212 scopus 로고
    • Comparison of the predicted and observed secondary structure of T4 phage lysozyme
    • Mathews, B.W. Comparison of the predicted and observed secondary structure of T4 phage lysozyme. Biochim. Biophys. Acta, 405:442-451, 1975.
    • (1975) Biochim. Biophys. Acta , vol.405 , pp. 442-451
    • Mathews, B.W.1
  • 44
    • 0023046211 scopus 로고
    • Codon usage in regulatory genes in Escherichia coli does not reflect selection for 'TOTe' codons
    • Sharp, P.M., Li, W.H. Codon usage in regulatory genes in Escherichia coli does not reflect selection for 'TOTe' codons. Nucleic Acids Res. 10:7737-7749, 1986.
    • (1986) Nucleic Acids Res. , vol.10 , pp. 7737-7749
    • Sharp, P.M.1    Li, W.H.2
  • 46
    • 0020655246 scopus 로고
    • Structural domains in proteins and their role in the dynamics of protein function
    • Janin, J., Wodak, S. Structural domains in proteins and their role in the dynamics of protein function. Prog. Biophys. Mol. Biol. 42:21-78, 1983.
    • (1983) Prog. Biophys. Mol. Biol. , vol.42 , pp. 21-78
    • Janin, J.1    Wodak, S.2
  • 47
    • 0001848681 scopus 로고
    • Large multidomain and multisubunit proteins
    • Creighton, T.E. (ed.). New York: W.H. Freeman
    • Garel, J.-R. Large multidomain and multisubunit proteins. In: "Protein Folding." Creighton, T.E. (ed.). New York: W.H. Freeman, 1992:405-454.
    • (1992) Protein Folding , pp. 405-454
    • Garel, J.-R.1
  • 52
    • 0020580026 scopus 로고
    • The isolation, characterisation, and sequence of the pyruvate kinase gene of saccharomyces cerevisiae
    • Burke, R.L., Tekamp-Olsen, P., Najarian, R. The isolation, characterisation, and sequence of the pyruvate kinase gene of saccharomyces cerevisiae. J. Biol. Chem. 258: 2193-2202, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2193-2202
    • Burke, R.L.1    Tekamp-Olsen, P.2    Najarian, R.3
  • 53
    • 40649119845 scopus 로고
    • Chicago, The University of Chicago Press
    • Bickerton, D. "Language & Species." Chicago, The University of Chicago Press, 1990.
    • (1990) Language & Species
    • Bickerton, D.1
  • 56
    • 0028081516 scopus 로고
    • Neural network model of the genetic code is strongly correlated to the GES scale of amino acid transfer free energies
    • Tolstrup, N., Toftgaard, J., Engelbrecht, J., Brunak, S. Neural network model of the genetic code is strongly correlated to the GES scale of amino acid transfer free energies. J. Mol. Biol. 243:816-820, 1994.
    • (1994) J. Mol. Biol. , vol.243 , pp. 816-820
    • Tolstrup, N.1    Toftgaard, J.2    Engelbrecht, J.3    Brunak, S.4
  • 57
    • 0026743157 scopus 로고
    • Limits on α-helix prediction with neural network models
    • Hayward, S., Collins, J.F. Limits on α-helix prediction with neural network models. Proteins 14:372-381, 1992.
    • (1992) Proteins , vol.14 , pp. 372-381
    • Hayward, S.1    Collins, J.F.2
  • 58
    • 0345558291 scopus 로고
    • Doing sequence analysis by inspecting the order in which neural networks learn
    • Soumpasis, D.M., Jovin, T.M. (eds.). Berlin: Springer-Verlag
    • Brunak, S. Doing sequence analysis by inspecting the order in which neural networks learn. In: "Computation of Biomolecular Structures - Achievements, Problems and Perspectives." Soumpasis, D.M., Jovin, T.M. (eds.). Berlin: Springer-Verlag, 1993:43-54.
    • (1993) Computation of Biomolecular Structures - Achievements, Problems and Perspectives , pp. 43-54
    • Brunak, S.1
  • 59
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta, L.G., Rose, G.D. Helix signals in proteins. Science 240:1632-1641, 1988.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 60
    • 0027256739 scopus 로고
    • Hydrogen bonding, hydrophobicity, packing and protein folding
    • Rose, G.D., Wolfenden, R. Hydrogen bonding, hydrophobicity, packing and protein folding. Annu. Rev. Biophys. Biomol. Struct. 22:381-415, 1993.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 381-415
    • Rose, G.D.1    Wolfenden, R.2
  • 61
    • 0025767350 scopus 로고
    • Beta-breakers: An aperiodic secondary structure
    • Colloc'h, N., Cohen, F.E. Beta-breakers: An aperiodic secondary structure. J. Mol. Biol. 221:603-613, 1991.
    • (1991) J. Mol. Biol. , vol.221 , pp. 603-613
    • Colloc'h, N.1    Cohen, F.E.2
  • 62
    • 0025733603 scopus 로고
    • Ribosomal RNA and translation
    • Noller, H.F. Ribosomal RNA and translation. Annu. Rev. Biochem. 60:191-227, 1991.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 191-227
    • Noller, H.F.1
  • 63
    • 0021012648 scopus 로고
    • Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids
    • Woese, C.R., Gutell, R.R., Gupta, R., Noller, H.F. Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids. Microbiol. Rev. 47:621-669, 1983.
    • (1983) Microbiol. Rev. , vol.47 , pp. 621-669
    • Woese, C.R.1    Gutell, R.R.2    Gupta, R.3    Noller, H.F.4
  • 65
    • 0016291570 scopus 로고
    • Topography of 16S RNA in 3OS ribosomal subunits. Nucleotide sequences and location of sites of reaction with kethoxal
    • Noller, H.F. Topography of 16S RNA in 3OS ribosomal subunits. Nucleotide sequences and location of sites of reaction with kethoxal. Biochemistry 13:4694-4703, 1974.
    • (1974) Biochemistry , vol.13 , pp. 4694-4703
    • Noller, H.F.1
  • 67
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribisome binding sites
    • Shine, J., Dalgarno, L. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribisome binding sites. Proc. Natl. Acad. Sci. U.S.A. 71:1342-1346, 1974.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 69
    • 0025322342 scopus 로고
    • DNA-hydridixation electron microscopy. Localization of five regions of 16S rRNA on the surface of 30S ribosomal subunits
    • Oakes, M.I., Lake, J.A. DNA-hydridixation electron microscopy. Localization of five regions of 16S rRNA on the surface of 30S ribosomal subunits. J. Mol. Biol. 221:897-906, 1990.
    • (1990) J. Mol. Biol. , vol.221 , pp. 897-906
    • Oakes, M.I.1    Lake, J.A.2
  • 70
    • 0025829049 scopus 로고
    • Sites of contact with 16S rRNA and 23S rRNA in the Escherichia coli ribosome
    • Wollenzien, P., Expert-Bezancon, A., Fauvre, A. Sites of contact with 16S rRNA and 23S rRNA in the Escherichia coli ribosome. Biochemistry 30:1788-1795, 1991.
    • (1991) Biochemistry , vol.30 , pp. 1788-1795
    • Wollenzien, P.1    Expert-Bezancon, A.2    Fauvre, A.3
  • 71
    • 0028196987 scopus 로고
    • Arrangement of messenger RNA on Escherichia coli ribosomes with respect to 10 16S rRNA cross-linking sites
    • Bhangu, R., Juzumiene, D., Wollenzien, P. Arrangement of messenger RNA on Escherichia coli ribosomes with respect to 10 16S rRNA cross-linking sites. Biochemistry 33:3063-3070, 1994.
    • (1994) Biochemistry , vol.33 , pp. 3063-3070
    • Bhangu, R.1    Juzumiene, D.2    Wollenzien, P.3
  • 72
    • 0024966993 scopus 로고
    • Codon usage and secondary structure of MS2 phage RNA
    • Bulmer, M. Codon usage and secondary structure of MS2 phage RNA. Nucleic Acids Res. 17:1839-1843, 1989.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1839-1843
    • Bulmer, M.1
  • 73
    • 0027407856 scopus 로고
    • Identification of unusual RNA folding patterns encoded by bacteriophage T4 gene 60
    • Le, S.Y., Chen, J.H., Maizel, J.V. Identification of unusual RNA folding patterns encoded by bacteriophage T4 gene 60. Gene 124:21-28, 1993.
    • (1993) Gene , vol.124 , pp. 21-28
    • Le, S.Y.1    Chen, J.H.2    Maizel, J.V.3


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