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Volumn 43, Issue 46, 2004, Pages 14624-14636

Dynamics inherent in helix 27 from Escherichia coli 16S ribosomal RNA

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; DNA; ENERGY TRANSFER; ESCHERICHIA COLI; GENETIC ENGINEERING; IONIC STRENGTH; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ULTRAVIOLET RADIATION;

EID: 8744245325     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048533y     Document Type: Article
Times cited : (14)

References (77)
  • 1
    • 0036089703 scopus 로고    scopus 로고
    • Single-particle imaging of macromolecules by cryo-electron microscopy
    • Frank, J. (2002) Single-particle imaging of macromolecules by cryo-electron microscopy, Annu. Rev. Biophys. Biomol. Struct. 31, 303-319.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 303-319
    • Frank, J.1
  • 2
    • 0036703003 scopus 로고    scopus 로고
    • Structural dynamics of ribosomal RNA during decoding on the ribosome
    • Rodnina, M. V., Daviter, T., Gromadski, K., and Wintermeyer, W. (2002) Structural dynamics of ribosomal RNA during decoding on the ribosome, Biochimie 84, 745-754.
    • (2002) Biochimie , vol.84 , pp. 745-754
    • Rodnina, M.V.1    Daviter, T.2    Gromadski, K.3    Wintermeyer, W.4
  • 3
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank, J., and Agrawal, R. K. (2000) A ratchet-like inter-subunit reorganization of the ribosome during translocation, Nature 406, 318-322.
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 6
    • 0042424707 scopus 로고    scopus 로고
    • Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy
    • Tama, F., Valle, M., Frank, J., and Brooks, C. L., III (2003) Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy, Proc. Natl. Acad. Sci. U.S.A. 100, 9319-9323.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9319-9323
    • Tama, F.1    Valle, M.2    Frank, J.3    Brooks III, C.L.4
  • 7
    • 0038433302 scopus 로고    scopus 로고
    • An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation
    • Savelsbergh, A., Katunin, V. I., Mohr, D., Peske, F., Rodnina, M. V., and Wintermeyer, W. (2003) An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation, Mol. Cell 11, 1517-1523.
    • (2003) Mol. Cell , vol.11 , pp. 1517-1523
    • Savelsbergh, A.1    Katunin, V.I.2    Mohr, D.3    Peske, F.4    Rodnina, M.V.5    Wintermeyer, W.6
  • 10
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution, Science 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 11
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle, J. M., Murphy, F. V., Tarry, M. J., and Ramakrishnan, V. (2002) Selection of tRNA by the ribosome requires a transition from an open to a closed form, Cell 111, 721-732.
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 12
    • 0038403669 scopus 로고    scopus 로고
    • Insights into the decoding mechanism from recent ribosome structures
    • Ogle, J. M., Carter, A. P., and Ramakrishnan, V. (2003) Insights into the decoding mechanism from recent ribosome structures, Trends Biochem. Sci. 28, 259-266.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 259-266
    • Ogle, J.M.1    Carter, A.P.2    Ramakrishnan, V.3
  • 14
    • 0021012648 scopus 로고
    • Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids
    • Woese, C. R., Gutell, R., Gupta, R., and Noller, H. F. (1983) Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids, Microbiol. Rev. 47, 621-669.
    • (1983) Microbiol. Rev. , vol.47 , pp. 621-669
    • Woese, C.R.1    Gutell, R.2    Gupta, R.3    Noller, H.F.4
  • 15
    • 0028261409 scopus 로고
    • Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective
    • Gutell, R. R., Larsen, N., and Woese, C. R. (1994) Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective, Microbiol. Rev. 58, 10-26.
    • (1994) Microbiol. Rev. , vol.58 , pp. 10-26
    • Gutell, R.R.1    Larsen, N.2    Woese, C.R.3
  • 16
    • 0023054135 scopus 로고
    • E. coli ribosomes with a C912 to U base change in the 16S rRNA are streptomycin resistant
    • Montandon, P. E., Wagner, R., and Stutz, E. (1986) E. coli ribosomes with a C912 to U base change in the 16S rRNA are streptomycin resistant, EMBO J. 5, 3705-3708.
    • (1986) EMBO J. , vol.5 , pp. 3705-3708
    • Montandon, P.E.1    Wagner, R.2    Stutz, E.3
  • 17
    • 0025125057 scopus 로고
    • Effects of mutagenesis of C912 in the streptomycin binding region of Escherichia coli 16S ribosomal RNA
    • Frattali, A. L., Flynn, M. K., De Stasio, E. A., and Dahlberg, A. E. (1990) Effects of mutagenesis of C912 in the streptomycin binding region of Escherichia coli 16S ribosomal RNA, Biochim. Biophys. Acta 1050, 27-33.
    • (1990) Biochim. Biophys. Acta , vol.1050 , pp. 27-33
    • Frattali, A.L.1    Flynn, M.K.2    De Stasio, E.A.3    Dahlberg, A.E.4
  • 18
    • 0028853679 scopus 로고
    • Genetic and comparative analyses reveal an alternative secondary structure in the region of nt 912 of Escherichia coli 16S rRNA
    • Lodmell, J. S., Gutell, R. R., and Dahlberg, A. E. (1995) Genetic and comparative analyses reveal an alternative secondary structure in the region of nt 912 of Escherichia coli 16S rRNA, Proc. Natl. Acad. Sci. U.S.A. 92, 10555-10559.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10555-10559
    • Lodmell, J.S.1    Gutell, R.R.2    Dahlberg, A.E.3
  • 19
    • 0030806152 scopus 로고    scopus 로고
    • A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA
    • Lodmell, J. S., and Dahlberg, A. E. (1997) A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA, Science 277, 1262-1267.
    • (1997) Science , vol.277 , pp. 1262-1267
    • Lodmell, J.S.1    Dahlberg, A.E.2
  • 20
    • 0033571249 scopus 로고    scopus 로고
    • Major rearrangements in the 70S ribosomal 3D structure caused by a conformational switch in 16S ribosomal RNA
    • Gabashvili, I. S., Agrawal, R. K., Grassucci, R., Squires, C. L., Dahlberg, A. E., and Frank, J. (1999) Major rearrangements in the 70S ribosomal 3D structure caused by a conformational switch in 16S ribosomal RNA, EMBO J. 18, 6501-6507.
    • (1999) EMBO J. , vol.18 , pp. 6501-6507
    • Gabashvili, I.S.1    Agrawal, R.K.2    Grassucci, R.3    Squires, C.L.4    Dahlberg, A.E.5    Frank, J.6
  • 23
    • 0346362326 scopus 로고    scopus 로고
    • Genetic evidence against the 16S ribosomal RNA helix 27 conformational switch model
    • Rodriguez-Correa, D., and Dahlberg, A. E. (2004) Genetic evidence against the 16S ribosomal RNA helix 27 conformational switch model, RNA 10, 28-33.
    • (2004) RNA , vol.10 , pp. 28-33
    • Rodriguez-Correa, D.1    Dahlberg, A.E.2
  • 24
    • 0032582795 scopus 로고    scopus 로고
    • A common motif organizes the structure of multi-helix loops in 16 and 23S ribosomal RNAs
    • Leontis, N. B., and Westhof, E. (1998) A common motif organizes the structure of multi-helix loops in 16 and 23S ribosomal RNAs, J. Mol. Biol. 283, 571-583.
    • (1998) J. Mol. Biol. , vol.283 , pp. 571-583
    • Leontis, N.B.1    Westhof, E.2
  • 25
    • 0035979354 scopus 로고    scopus 로고
    • Imino proton exchange and base-pair kinetics in RNA duplexes
    • Snoussi, K., and Leroy, J. L. (2001) Imino proton exchange and base-pair kinetics in RNA duplexes, Biochemistry 40, 8898-8904.
    • (2001) Biochemistry , vol.40 , pp. 8898-8904
    • Snoussi, K.1    Leroy, J.L.2
  • 26
    • 0346882954 scopus 로고    scopus 로고
    • Altered structural fluctuations in duplex RNA versus DNA: A conformational switch involving base pair opening
    • Pan, Y., and MacKerell, A. D., Jr. (2003) Altered structural fluctuations in duplex RNA versus DNA: a conformational switch involving base pair opening, Nucleic Acids Res. 31, 7131-7140.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 7131-7140
    • Pan, Y.1    MacKerell Jr., A.D.2
  • 27
    • 0842267214 scopus 로고    scopus 로고
    • Reprogrammed genetic decoding in cellular gene expression
    • Namy, O., Rousset, J. P., Naphthine, S., and Brierley, I. (2004) Reprogrammed genetic decoding in cellular gene expression, Mol. Cell 13, 157-168.
    • (2004) Mol. Cell , vol.13 , pp. 157-168
    • Namy, O.1    Rousset, J.P.2    Naphthine, S.3    Brierley, I.4
  • 28
    • 0037073473 scopus 로고    scopus 로고
    • Rearrangement of substrate secondary structure facilitates binding to the Neurospora VS ribozyme
    • Zamel, R., and Collins, R. A. (2002) Rearrangement of substrate secondary structure facilitates binding to the Neurospora VS ribozyme, J. Mol. Biol. 324, 903-915.
    • (2002) J. Mol. Biol. , vol.324 , pp. 903-915
    • Zamel, R.1    Collins, R.A.2
  • 29
    • 0035850733 scopus 로고    scopus 로고
    • Central domain assembly: Thermodynamics and kinetics of S6 and S18 binding to an S15-RNA complex, 3
    • Recht, M. I., and Williamson, J. R. (2001) Central domain assembly: thermodynamics and kinetics of S6 and S18 binding to an S15-RNA complex, 3. Mol. Biol. 313, 35-48.
    • (2001) Mol. Biol. , vol.313 , pp. 35-48
    • Recht, M.I.1    Williamson, J.R.2
  • 30
    • 0037229886 scopus 로고    scopus 로고
    • Comparison of X-ray crystal structure of the 30S subunit-antibiotic complex with NMR structure of decoding site oligonucleotide-paromomycin complex
    • Lynch, S. R., Gonzalez, R. L., and Puglisi, J. D. (2003) Comparison of X-ray crystal structure of the 30S subunit-antibiotic complex with NMR structure of decoding site oligonucleotide-paromomycin complex, Structure 11, 43-53.
    • (2003) Structure , vol.11 , pp. 43-53
    • Lynch, S.R.1    Gonzalez, R.L.2    Puglisi, J.D.3
  • 31
    • 1642458421 scopus 로고    scopus 로고
    • The kink-turn motif in RNA is dimorphic, and metal ion-dependent
    • Goody, T. A., Melcher, S. E., Norman, D. G., and Lilley, D. M. (2004) The kink-turn motif in RNA is dimorphic, and metal ion-dependent, RNA 10, 254-264.
    • (2004) RNA , vol.10 , pp. 254-264
    • Goody, T.A.1    Melcher, S.E.2    Norman, D.G.3    Lilley, D.M.4
  • 33
    • 0034808071 scopus 로고    scopus 로고
    • Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer
    • Walter, N. G. (2001) Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer, Methods 25, 19-30.
    • (2001) Methods , vol.25 , pp. 19-30
    • Walter, N.G.1
  • 35
    • 0025833454 scopus 로고
    • Fluorescence study of the topology of messenger RNA bound to the 30S ribosomal subunit of Escherichia coli
    • Czworkowski, J., Odom, O. W., and Hardesty, B. (1991) Fluorescence study of the topology of messenger RNA bound to the 30S ribosomal subunit of Escherichia coli, Biochemistry 30, 4821-4830.
    • (1991) Biochemistry , vol.30 , pp. 4821-4830
    • Czworkowski, J.1    Odom, O.W.2    Hardesty, B.3
  • 37
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 39
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 40
    • 0038001437 scopus 로고    scopus 로고
    • Trans-acting hepatitis delta virus ribozyme: Catalytic core and global structure are dependent on the 5′ substrate sequence
    • Jeong, S., Sefcikova, J., Tinsley, R. A., Rueda, D., and Walter, N. G. (2003) Trans-acting hepatitis delta virus ribozyme: catalytic core and global structure are dependent on the 5′ substrate sequence, Biochemistry 42, 7727-7740.
    • (2003) Biochemistry , vol.42 , pp. 7727-7740
    • Jeong, S.1    Sefcikova, J.2    Tinsley, R.A.3    Rueda, D.4    Walter, N.G.5
  • 41
    • 0037154091 scopus 로고    scopus 로고
    • The reaction pathway of the trans-acting hepatitis delta virus ribozyme: A conformational change accompanies catalysis
    • Pereira, M. B., Harris, D. A., Rueda, D., and Walter, N. G. (2002)-The reaction pathway of the trans-acting hepatitis delta virus ribozyme: a conformational change accompanies catalysis, Biochemistry 41, 730-740.
    • (2002) Biochemistry , vol.41 , pp. 730-740
    • Pereira, M.B.1    Harris, D.A.2    Rueda, D.3    Walter, N.G.4
  • 42
    • 0026423027 scopus 로고
    • Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops
    • Heus, H. A., and Pardi, A. (1991) Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops, Science 253, 191-194.
    • (1991) Science , vol.253 , pp. 191-194
    • Heus, H.A.1    Pardi, A.2
  • 43
    • 0030596092 scopus 로고    scopus 로고
    • A network of heterogeneous hydrogen bonds in GNRA tetraloops
    • Jucker, F. M., Heus, H. A., Yip, P. F., Moors, E. H., and Pardi, A. (1996) A network of heterogeneous hydrogen bonds in GNRA tetraloops, J. Mol. Biol. 264, 968-980.
    • (1996) J. Mol. Biol. , vol.264 , pp. 968-980
    • Jucker, F.M.1    Heus, H.A.2    Yip, P.F.3    Moors, E.H.4    Pardi, A.5
  • 44
    • 0028953727 scopus 로고
    • The sarcin/ricin loop, a modular RNA
    • Szewczak, A. A., and Moore, P. B. (1995) The sarcin/ricin loop, a modular RNA, J. Mol. Biol. 247, 81-98.
    • (1995) J. Mol. Biol. , vol.247 , pp. 81-98
    • Szewczak, A.A.1    Moore, P.B.2
  • 45
    • 0031668475 scopus 로고    scopus 로고
    • Structure and stability of variants of the sarcin-ricin loop of 28S rRNA: NMR studies of the prokaryotic SRL and a functional mutant
    • Seggerson, K., and Moore, P. B. (1998) Structure and stability of variants of the sarcin-ricin loop of 28S rRNA: NMR studies of the prokaryotic SRL and a functional mutant, RNA 4, 1203-1215.
    • (1998) RNA , vol.4 , pp. 1203-1215
    • Seggerson, K.1    Moore, P.B.2
  • 46
    • 0037225166 scopus 로고    scopus 로고
    • Bistable secondary structures of small RNAs and their structural probing by comparative imino proton NMR spectroscopy
    • Hobartner, C., and Micura, R. (2003) Bistable secondary structures of small RNAs and their structural probing by comparative imino proton NMR spectroscopy, J. Mol. Biol. 325, 421-431.
    • (2003) J. Mol. Biol. , vol.325 , pp. 421-431
    • Hobartner, C.1    Micura, R.2
  • 47
    • 0030974056 scopus 로고    scopus 로고
    • Exact determination of UV-induced crosslinks in 16S ribosomal RNA in 30S ribosomal subunits
    • Wilms, C., Noah, J. W., Zhong, D., and Wollenzien, P. (1997) Exact determination of UV-induced crosslinks in 16S ribosomal RNA in 30S ribosomal subunits, RNA 3, 602-612.
    • (1997) RNA , vol.3 , pp. 602-612
    • Wilms, C.1    Noah, J.W.2    Zhong, D.3    Wollenzien, P.4
  • 48
    • 0034307594 scopus 로고    scopus 로고
    • UV-induced cross-links in the 16S rRNAs of Escherichia coli, Bacillus subtilis and Thermus aquaticus and their implications for ribosome structure and photochemistry
    • Noah, J. W., Shapkina, T., and Wollenzien, P. (2000) UV-induced cross-links in the 16S rRNAs of Escherichia coli, Bacillus subtilis and Thermus aquaticus and their implications for ribosome structure and photochemistry, Nucleic Acids Res. 28, 3785-3792.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3785-3792
    • Noah, J.W.1    Shapkina, T.2    Wollenzien, P.3
  • 49
    • 2542604590 scopus 로고    scopus 로고
    • Efficiency and pattern of UV pulse laser-induced RNA-RNA cross-linking in the ribosome
    • Shapkina, T., Lappi, S., Franzen, S., and Wollenzien, P. (2004) Efficiency and pattern of UV pulse laser-induced RNA-RNA cross-linking in the ribosome, Nucleic Acids Res. 32, 1518-1526.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1518-1526
    • Shapkina, T.1    Lappi, S.2    Franzen, S.3    Wollenzien, P.4
  • 50
    • 0032535207 scopus 로고    scopus 로고
    • Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the a site of the E. coli ribosome
    • Pape, T., Wintermeyer, W., and Rodnina, M. V. (1998) Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome, EMBO J. 17, 7490-7497.
    • (1998) EMBO J. , vol.17 , pp. 7490-7497
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 52
    • 0036786684 scopus 로고    scopus 로고
    • All-atom homology model of the Escherichia coli 30S ribosomal subunit
    • Tung, C. S., Joseph, S., and Sanbonmatsu, K. Y. (2002) All-atom homology model of the Escherichia coli 30S ribosomal subunit, Nat. Struct. Biol. 9, 750-755.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 750-755
    • Tung, C.S.1    Joseph, S.2    Sanbonmatsu, K.Y.3
  • 53
    • 0030969442 scopus 로고    scopus 로고
    • Real-time monitoring of hairpin ribozyme kinetics through base-specific quenching of fluorescein-labeled substrates
    • Walter, N. G., and Burke, J. M. (1997) Real-time monitoring of hairpin ribozyme kinetics through base-specific quenching of fluorescein-labeled substrates, RNA 3, 392-404.
    • (1997) RNA , vol.3 , pp. 392-404
    • Walter, N.G.1    Burke, J.M.2
  • 54
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen, D. E., demons, W. M., Jr., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., and Ramakrishnan, V. (2000) The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit, Cell 103, 1143-1154.
    • (2000) Cell , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Demons Jr., W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 57
    • 0036671344 scopus 로고    scopus 로고
    • Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome
    • Katunin, V. I., Muth, G. W., Strobel, S. A., Wintermeyer, W., and Rodnina, M. V. (2002) Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome, Mol. Cell 10, 339-346.
    • (2002) Mol. Cell , vol.10 , pp. 339-346
    • Katunin, V.I.1    Muth, G.W.2    Strobel, S.A.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 58
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman, E. M., Brunelle, J. L., Kochaniak, A. B., and Green, R. (2004) The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release, Cell 117, 589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 59
    • 0021107155 scopus 로고
    • Nuclear magnetic resonance study on the exchange behavior of the NH-N protons of a ribonucleic acid miniduplex
    • Fritzsche, H., Kan, L. S., and Ts'o, P. O. (1983) Nuclear magnetic resonance study on the exchange behavior of the NH-N protons of a ribonucleic acid miniduplex, Biochemistry 22, 277-280.
    • (1983) Biochemistry , vol.22 , pp. 277-280
    • Fritzsche, H.1    Kan, L.S.2    Ts'o, P.O.3
  • 60
    • 2942630097 scopus 로고    scopus 로고
    • Encoded errors: Mutations and rearrangements mediated by misalignment at repetitive DNA sequences
    • Lovett, S. T. (2004) Encoded errors: mutations and rearrangements mediated by misalignment at repetitive DNA sequences, Mol. Microbiol. 52, 1243-1253.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1243-1253
    • Lovett, S.T.1
  • 62
    • 0029929417 scopus 로고    scopus 로고
    • Preparation of figure 8 and cruciform DNAs and their use in studies of the kinetics of branch migration
    • Mulrooney, S. B., Fishel, R. A., Hejna, J. A., and Warner, R. C. (1996) Preparation of figure 8 and cruciform DNAs and their use in studies of the kinetics of branch migration, J. Biol. Chem. 271, 9648-9659.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9648-9659
    • Mulrooney, S.B.1    Fishel, R.A.2    Hejna, J.A.3    Warner, R.C.4
  • 63
    • 1842861596 scopus 로고    scopus 로고
    • Three-dimensional structural views of branch migration and resolution in DNA homologous recombination
    • Yamada, K., Ariyoshi, M., and Morikawa, K. (2004) Three-dimensional structural views of branch migration and resolution in DNA homologous recombination, Curr. Opin. Struct. Biol. 14, 130-137.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 130-137
    • Yamada, K.1    Ariyoshi, M.2    Morikawa, K.3
  • 65
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D. H., Sabina, J., Zuker, M., and Turner, D. H. (1999) Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure, J. Mol. Biol. 288, 911-940.
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 66
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction, Nucleic Acids Res. 31, 3406-3415.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 67
    • 0030856333 scopus 로고    scopus 로고
    • Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain
    • Correll, C. C., Freeborn, B., Moore, P. B., and Steitz, T. A. (1997)-Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain, Cell 91, 705-712.
    • (1997) Cell , vol.91 , pp. 705-712
    • Correll, C.C.1    Freeborn, B.2    Moore, P.B.3    Steitz, T.A.4
  • 69
    • 0037764044 scopus 로고    scopus 로고
    • Non-Watson-Crick basepairing and hydration in RNA motifs: Molecular dynamics of 5S rRNA loop E
    • Reblova, K., Spackova, N., Stefl, R., Csaszar, K., Koca, J., Leontis, N. B., and Sponer, J. (2003) Non-Watson-Crick basepairing and hydration in RNA motifs: molecular dynamics of 5S rRNA loop E, Biophys. J. 84, 3564-3582.
    • (2003) Biophys. J. , vol.84 , pp. 3564-3582
    • Reblova, K.1    Spackova, N.2    Stefl, R.3    Csaszar, K.4    Koca, J.5    Leontis, N.B.6    Sponer, J.7
  • 70
    • 0346366808 scopus 로고    scopus 로고
    • 2+ ion-binding sites in the 5S rRNA loop E inferred from molecular dynamics simulations
    • 2+ ion-binding sites in the 5S rRNA loop E inferred from molecular dynamics simulations, J. Mol. Biol. 335, 555-571.
    • (2004) J. Mol. Biol. , vol.335 , pp. 555-571
    • Auffinger, P.1    Bielecki, L.2    Westhof, E.3
  • 71
    • 0034624039 scopus 로고    scopus 로고
    • Movement of the decoding region of the 16S ribosomal RNA accompanies tRNA translocation
    • VanLoock, M. S., Agrawal, R. K., Gabashvili, I. S., Qi, L., Frank, J., and Harvey, S. C. (2000) Movement of the decoding region of the 16S ribosomal RNA accompanies tRNA translocation, J. Mol. Biol. 304, 507-515.
    • (2000) J. Mol. Biol. , vol.304 , pp. 507-515
    • Vanloock, M.S.1    Agrawal, R.K.2    Gabashvili, I.S.3    Qi, L.4    Frank, J.5    Harvey, S.C.6
  • 72
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed, D., and Noller, H. F. (1987) Interaction of antibiotics with functional sites in 16S ribosomal RNA, Nature 327, 389-394.
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 74
    • 0030792667 scopus 로고    scopus 로고
    • Interaction of tetracycline with RNA: Photoincorporation into ribosomal RNA of Escherichia coli
    • Oehler, R., Polacek, N., Steiner, G., and Barta, A. (1997) Interaction of tetracycline with RNA: photoincorporation into ribosomal RNA of Escherichia coli, Nucleic Acids Res. 25, 1219-1224.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1219-1224
    • Oehler, R.1    Polacek, N.2    Steiner, G.3    Barta, A.4
  • 75
    • 0029796407 scopus 로고    scopus 로고
    • Antibiotic interactions with the hammerhead ribozyme: Tetracyclines as a new class of hammerhead inhibitor
    • Murray, J. B., and Arnold, J. R. (1996) Antibiotic interactions with the hammerhead ribozyme: tetracyclines as a new class of hammerhead inhibitor, Biochem. J. 317, 855-860.
    • (1996) Biochem. J. , vol.317 , pp. 855-860
    • Murray, J.B.1    Arnold, J.R.2
  • 76
    • 0343799864 scopus 로고    scopus 로고
    • Inhibition of the self-cleavage reaction of the human hepatitis delta virus ribozyme by antibiotics
    • Rogers, J., Chang, A. H., von Ahsen, U., Schroeder, R., and Davies, J. (1996) Inhibition of the self-cleavage reaction of the human hepatitis delta virus ribozyme by antibiotics, J. Mol. Biol. 259, 916-925.
    • (1996) J. Mol. Biol. , vol.259 , pp. 916-925
    • Rogers, J.1    Chang, A.H.2    Von Ahsen, U.3    Schroeder, R.4    Davies, J.5


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