메뉴 건너뛰기




Volumn 3, Issue 3, 1996, Pages 173-184

Crystal structures of an A-form duplex with single-adenosine bulges and a conformational basis for site-specific RNA self-cleavage

Author keywords

Base triples; Bending; Major and minor groove widths; Transesterification; X ray crystallography

Indexed keywords

RNA; RNA BINDING PROTEIN;

EID: 0030090986     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90260-4     Document Type: Article
Times cited : (68)

References (76)
  • 1
    • 0002176755 scopus 로고
    • RNA structural elements and RNA function
    • Gesteland, R.F. & Atkins, J.F., eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Wyatt J.R. & Tinoco Jr, I. (1993). RNA structural elements and RNA function. In The RNA World (Gesteland, R.F. & Atkins, J.F., eds), pp. 465-496, Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1993) The RNA World , pp. 465-496
    • Wyatt, J.R.1    Tinoco Jr., I.2
  • 3
    • 0024577464 scopus 로고
    • A difference in the importance of bulged nucleotides and their parent base pairs in the binding of transcription factor IIIA to Xenopus 5S RNA and 5S RNA genes
    • Baudin, F. & Romaniuk, P.J. (1989). A difference in the importance of bulged nucleotides and their parent base pairs in the binding of transcription factor IIIA to Xenopus 5S RNA and 5S RNA genes. Nucleic Acids Res. 17, 2043-2056.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 2043-2056
    • Baudin, F.1    Romaniuk, P.J.2
  • 4
    • 0025039326 scopus 로고
    • HIV-1 Tat protein stimulates transcription by binding to a U-rich bulge in the stem of the TAR RNA structure
    • Dingwall, C., et al., & Skinner, M.A. (1990). HIV-1 Tat protein stimulates transcription by binding to a U-rich bulge in the stem of the TAR RNA structure. EMBO J. 9, 4145-4153.
    • (1990) EMBO J. , vol.9 , pp. 4145-4153
    • Dingwall, C.1    Skinner, M.A.2
  • 5
    • 0025162336 scopus 로고
    • A bulge structure in HIV-1 TAR RNA is required for Tat binding and Tat-mediated trans-activation
    • Roy, S., Delling, U., Chen, C.-H., Rosen, C. A. & Sonenberg, N. (1990). A bulge structure in HIV-1 TAR RNA is required for Tat binding and Tat-mediated trans-activation. Genes Dev. 4, 1365-1373.
    • (1990) Genes Dev. , vol.4 , pp. 1365-1373
    • Roy, S.1    Delling, U.2    Chen, C.-H.3    Rosen, C.A.4    Sonenberg, N.5
  • 6
    • 0025871656 scopus 로고
    • Refolded HIV-1 Tat protein protects both bulge and loop nucleotides in TAR RNA from ribonucleolytic cleavage
    • Harper, J.W. & Logsdon, N.J. (1991). Refolded HIV-1 Tat protein protects both bulge and loop nucleotides in TAR RNA from ribonucleolytic cleavage. Biochemistry 30, 8060-8066.
    • (1991) Biochemistry , vol.30 , pp. 8060-8066
    • Harper, J.W.1    Logsdon, N.J.2
  • 7
    • 0343007324 scopus 로고
    • Evidence for several higher order structural elements in ribosomal RNA
    • Woese C.R. & Gutell, R.R. (1989). Evidence for several higher order structural elements in ribosomal RNA. Proc. Natl. Acad. Sci. USA 86, 3119-3122.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3119-3122
    • Woese, C.R.1    Gutell, R.R.2
  • 8
    • 0023657074 scopus 로고
    • Role of a bulged A residue in a specific RNA-protein interaction
    • Wu, H.-N. & Uhlenbeck, O.C. (1987). Role of a bulged A residue in a specific RNA-protein interaction. Biochemistry 26, 8221-8227.
    • (1987) Biochemistry , vol.26 , pp. 8221-8227
    • Wu, H.-N.1    Uhlenbeck, O.C.2
  • 9
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Valegård, K., Murray, J.B., Stockley, P.G, Stonehouse, N.J. & Liljas, L. (1994). Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371, 623-626.
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegård, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouse, N.J.4    Liljas, L.5
  • 10
    • 0024431086 scopus 로고
    • Physical studies of 5S RNA variants at position 66
    • Zhang, P., Popienick, P. & Moore, P.B. (1989). Physical studies of 5S RNA variants at position 66. Nucleic Acids Res. 17, 8645-8656.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8645-8656
    • Zhang, P.1    Popienick, P.2    Moore, P.B.3
  • 11
    • 0024427177 scopus 로고
    • The guanosine-binding site of the Tetrahymena ribozyme
    • Michel, F., Hanna, M., Green, R., Bartel, D.P. & Szostak, J.W. (1989). The guanosine-binding site of the Tetrahymena ribozyme. Nature 342, 391-395.
    • (1989) Nature , vol.342 , pp. 391-395
    • Michel, F.1    Hanna, M.2    Green, R.3    Bartel, D.P.4    Szostak, J.W.5
  • 12
    • 0025367254 scopus 로고
    • Self-splicing of group I introns
    • Cech, T.R. (1990). Self-splicing of group I introns. Annu. Rev. Biochem. 59, 543-568.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 543-568
    • Cech, T.R.1
  • 13
    • 0024995219 scopus 로고
    • Self-splicing group II and nuclear pre-mRNA introns: How similar are they?
    • Jacquier, A. (1990). Self-splicing group II and nuclear pre-mRNA introns: how similar are they? Trends Biochem. Sci. 15, 351-354.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 351-354
    • Jacquier, A.1
  • 14
    • 0025828645 scopus 로고
    • Effects of mutations of the bulged nucleotide in the conserved P7 pairing element of the phage T4 td intron on ribozyme function
    • Schroeder, R., von Ahsen, U. & Belfort, M. (1991). Effects of mutations of the bulged nucleotide in the conserved P7 pairing element of the phage T4 td intron on ribozyme function. Biochemistry 30, 3295-3303.
    • (1991) Biochemistry , vol.30 , pp. 3295-3303
    • Schroeder, R.1    Von Ahsen, U.2    Belfort, M.3
  • 15
    • 0026486884 scopus 로고
    • Mutational analysis of the yeast U2 snRNA suggests a structural similarity to the catalytic core of group I introns
    • McPheeters, D.S. & Abelson, J. (1992). Mutational analysis of the yeast U2 snRNA suggests a structural similarity to the catalytic core of group I introns. Cell 71, 819-831.
    • (1992) Cell , vol.71 , pp. 819-831
    • McPheeters, D.S.1    Abelson, J.2
  • 16
    • 0001877802 scopus 로고
    • Splicing of precursors to mRNA by the spliceosome
    • Gesteland, R.F. & Atkins, J.F., eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Moore, M.J., Query, C.C. & Sharp, P.A. (1993). Splicing of precursors to mRNA by the spliceosome. In The RNA World (Gesteland, R.F. & Atkins, J.F., eds), pp. 303-357, Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1993) The RNA World , pp. 303-357
    • Moore, M.J.1    Query, C.C.2    Sharp, P.A.3
  • 17
    • 0028089094 scopus 로고
    • RNAs and ribonucleoproteins in recognition and catalysis
    • Wittop Koning T. H. & Schümperli, D. (1994). RNAs and ribonucleoproteins in recognition and catalysis. Eur. J. Biochem. 219, 25-42.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 25-42
    • Wittop Koning, T.H.1    Schümperli, D.2
  • 18
    • 0028205987 scopus 로고
    • Branch nucleophile selection in pre-mRNA splicing: Evidence for the bulged duplex model
    • Query, C.C., Moore, M.J. & Sharp, P.A. (1994). Branch nucleophile selection in pre-mRNA splicing: evidence for the bulged duplex model. Genes Dev. 8, 587-597.
    • (1994) Genes Dev. , vol.8 , pp. 587-597
    • Query, C.C.1    Moore, M.J.2    Sharp, P.A.3
  • 19
    • 0024564403 scopus 로고
    • Use of lead(II) to probe the structure of large RNAs. Conformation of the 3′ terminal domain of E coli 16S rRNA and its involvement in building the tRNA binding sites
    • Gornicki, P., et al., & Ehresmann, B. (1989). Use of lead(II) to probe the structure of large RNAs. Conformation of the 3′ terminal domain of E coli 16S rRNA and its involvement in building the tRNA binding sites. J. Biomol. Struct. Dyn. 6, 971-984.
    • (1989) J. Biomol. Struct. Dyn. , vol.6 , pp. 971-984
    • Gornicki, P.1    Ehresmann, B.2
  • 20
    • 0027318824 scopus 로고
    • Lead cleavage sites in the core structure of group I intron-RNA
    • Streicher, B., von Ahsen, U. & Schroeder, R. (1993). Lead cleavage sites in the core structure of group I intron-RNA. Nucleic Acids Res. 21, 311-317.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 311-317
    • Streicher, B.1    Von Ahsen, U.2    Schroeder, R.3
  • 21
    • 0025186882 scopus 로고
    • Thermodynamic and spectroscopic study of bulge loops in oligoribonucleotides
    • Longfellow, C.E., Kierzek, R. & Turner, D.H. (1990). Thermodynamic and spectroscopic study of bulge loops in oligoribonucleotides. Biochemistry 29, 278-285.
    • (1990) Biochemistry , vol.29 , pp. 278-285
    • Longfellow, C.E.1    Kierzek, R.2    Turner, D.H.3
  • 22
    • 0024580995 scopus 로고
    • Effects of single-base bulges on intercalator binding to small RNA and DNA hairpins and a ribosomal RNA fragment
    • White, S.A. & Draper, D.E. (1989). Effects of single-base bulges on intercalator binding to small RNA and DNA hairpins and a ribosomal RNA fragment. Biochemistry 28, 1892-1897.
    • (1989) Biochemistry , vol.28 , pp. 1892-1897
    • White, S.A.1    Draper, D.E.2
  • 23
    • 0025729926 scopus 로고
    • Thermodynamic characterization of deoxyribonucleotide duplexes containing bulges
    • LeBlanc, D.A. & Morden, K.M. (1991). Thermodynamic characterization of deoxyribonucleotide duplexes containing bulges. Biochemistry 30, 4042-4047.
    • (1991) Biochemistry , vol.30 , pp. 4042-4047
    • LeBlanc, D.A.1    Morden, K.M.2
  • 24
    • 0024579255 scopus 로고
    • Thermal stability of RNA hairpins containing a four-membered loop and a bulge nucleotide
    • Groebe, D.R. & Uhlenbeck, O.C. (1989). Thermal stability of RNA hairpins containing a four-membered loop and a bulge nucleotide. Biochemistry 28, 742-747.
    • (1989) Biochemistry , vol.28 , pp. 742-747
    • Groebe, D.R.1    Uhlenbeck, O.C.2
  • 25
    • 0001690587 scopus 로고
    • Deletions of bases in one strand of duplex DNA, in contrast to single-base mismatches, produce highly kinked molecules: Possible relevance to the folding of single-stranded nucleic acids
    • Hsieh, C.-H. & Griffith, J.D. (1989). Deletions of bases in one strand of duplex DNA, in contrast to single-base mismatches, produce highly kinked molecules: possible relevance to the folding of single-stranded nucleic acids. Proc. Natl. Acad. Sci. USA 86, 4833-4837.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4833-4837
    • Hsieh, C.-H.1    Griffith, J.D.2
  • 26
    • 0024375698 scopus 로고
    • DNA bending by the bulge defect
    • Rice, J.A. & Crothers, D.E. (1989). DNA bending by the bulge defect. Biochemistry 28, 4512-4516.
    • (1989) Biochemistry , vol.28 , pp. 4512-4516
    • Rice, J.A.1    Crothers, D.E.2
  • 27
    • 0025336457 scopus 로고
    • Bulge loops used to measure the helical twist of RNA in solution
    • Tang, R.S. & Draper, D.E. (1990). Bulge loops used to measure the helical twist of RNA in solution. Biochemistry 29, 5232-5237.
    • (1990) Biochemistry , vol.29 , pp. 5232-5237
    • Tang, R.S.1    Draper, D.E.2
  • 28
    • 0025171938 scopus 로고
    • RNA bulges and the helical periodicity of double-stranded RNA
    • Bhattacharyya, A., Murchie, A.I.H. & Lilley, D.M.J. (1990). RNA bulges and the helical periodicity of double-stranded RNA. Nature 343, 484-487.
    • (1990) Nature , vol.343 , pp. 484-487
    • Bhattacharyya, A.1    Murchie, A.I.H.2    Lilley, D.M.J.3
  • 29
    • 0026694960 scopus 로고
    • Kinking of RNA helices by bulged bases, and the structure of the human immunodeficiency virus transactivator response element
    • Riordan, F.A., Bhattacharyya, A., McAteer, S. & Lilley, D.M.J. (1992). Kinking of RNA helices by bulged bases, and the structure of the human immunodeficiency virus transactivator response element. J. Mol. Biol. 226, 305-310.
    • (1992) J. Mol. Biol. , vol.226 , pp. 305-310
    • Riordan, F.A.1    Bhattacharyya, A.2    McAteer, S.3    Lilley, D.M.J.4
  • 30
    • 0029111762 scopus 로고
    • Kinking of DNA and RNA by base bulges
    • Lilley, D.M.J. (1995). Kinking of DNA and RNA by base bulges. Proc. Natl. Acad. Sci. USA 92, 7140-7142.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7140-7142
    • Lilley, D.M.J.1
  • 31
    • 0027370486 scopus 로고
    • Major groove accessibility of RNA
    • Weeks, K.M. & Crothers, D.M. (1993). Major groove accessibility of RNA. Science 261, 1574-1577.
    • (1993) Science , vol.261 , pp. 1574-1577
    • Weeks, K.M.1    Crothers, D.M.2
  • 32
    • 0026651395 scopus 로고
    • Conformation of the TAR RNA-arginine complex by NMR spectroscopy
    • Puglisi, J.D., Tan, R., Calnan, B.J., Frankel, A.D. & Williamson, J.R. (1992). Conformation of the TAR RNA-arginine complex by NMR spectroscopy. Science 257, 76-80.
    • (1992) Science , vol.257 , pp. 76-80
    • Puglisi, J.D.1    Tan, R.2    Calnan, B.J.3    Frankel, A.D.4    Williamson, J.R.5
  • 33
    • 0028858599 scopus 로고
    • Solution structure of a bovine immunodeficiency virus Tat-TAR peptide RNA complex
    • Puglisi, J.D., Chen, L., Blanchard, S. & Frankel, A.D. (1995). Solution structure of a bovine immunodeficiency virus Tat-TAR peptide RNA complex. Science 270, 1200-1203.
    • (1995) Science , vol.270 , pp. 1200-1203
    • Puglisi, J.D.1    Chen, L.2    Blanchard, S.3    Frankel, A.D.4
  • 34
    • 0029613238 scopus 로고
    • Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex
    • Ye, X., Kumar, A. & Patel, D.J. (1995). Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex. Chemistry & Biology 2, 827-840.
    • (1995) Chemistry & Biology , vol.2 , pp. 827-840
    • Ye, X.1    Kumar, A.2    Patel, D.J.3
  • 35
    • 0020473228 scopus 로고
    • Extra adenosine stacks into the self-complementary d(CGCAGAATTCGCG) duplex in solution
    • Patel, D.J., et al., & Breslauer, K.J. (1982). Extra adenosine stacks into the self-complementary d(CGCAGAATTCGCG) duplex in solution. Biochemistry 21, 445-451.
    • (1982) Biochemistry , vol.21 , pp. 445-451
    • Patel, D.J.1    Breslauer, K.J.2
  • 36
    • 0023052458 scopus 로고
    • Extrahelical adenosine stacks into right-handed DNA: Solution conformation of the d(C-G-C-A-G-A-G-C-T-C-G-C-G) duplex deduced from distance geometry analysis of nuclear Overhauser effect spectra
    • Hare, D., Shapiro, L. & Patel, D. J. (1986). Extrahelical adenosine stacks into right-handed DNA: solution conformation of the d(C-G-C-A-G-A-G-C-T-C-G-C-G) duplex deduced from distance geometry analysis of nuclear Overhauser effect spectra. Biochemistry 25, 7456-7464.
    • (1986) Biochemistry , vol.25 , pp. 7456-7464
    • Hare, D.1    Shapiro, L.2    Patel, D.J.3
  • 37
    • 10444284813 scopus 로고
    • 32P NMR and two-dimensional NMR spectra of nucleic acids and 2D NOESY-constrained molecular mechanics calculations for structural solution of duplex oligonucleotides
    • 32P NMR and two-dimensional NMR spectra of nucleic acids and 2D NOESY-constrained molecular mechanics calculations for structural solution of duplex oligonucleotides. Bull. Magn. Reson. 8, 137-146.
    • (1987) Bull. Magn. Reson. , vol.8 , pp. 137-146
    • Gorenstein, D.G.1    Jones, C.R.2
  • 38
    • 0023473652 scopus 로고
    • Conformational perturbation due to an extra adenosine base in a self-complementary oligodeoxynucleotide duplex
    • Roy, S., Sklenar, V., Appella, E. & Cohen, J. S. (1987). Conformational perturbation due to an extra adenosine base in a self-complementary oligodeoxynucleotide duplex. Biochemistry 26, 2041-2052.
    • (1987) Biochemistry , vol.26 , pp. 2041-2052
    • Roy, S.1    Sklenar, V.2    Appella, E.3    Cohen, J.S.4
  • 40
    • 0024206235 scopus 로고
    • Binding of a 9-amino-acridine to bulged-base DNA oligomers from a frameshift hot spot
    • Woodson, S. A. & Crothers, D. M. (1988). Binding of a 9-amino-acridine to bulged-base DNA oligomers from a frameshift hot spot. Biochemistry 27, 8904-8914.
    • (1988) Biochemistry , vol.27 , pp. 8904-8914
    • Woodson, S.A.1    Crothers, D.M.2
  • 41
    • 0024516799 scopus 로고
    • Conformation of adenosine bulge-containing deoxytridecanucleotide duplexes in solution: Extra adenosine stacks into duplex independent of flanking sequence and temperature
    • Kalnik, M. W., Norman, D. G., Swann, P. F. & Patel, D. J. (1989). Conformation of adenosine bulge-containing deoxytridecanucleotide duplexes in solution: extra adenosine stacks into duplex independent of flanking sequence and temperature. J. Biol. Chem. 264, 3702-3712.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3702-3712
    • Kalnik, M.W.1    Norman, D.G.2    Swann, P.F.3    Patel, D.J.4
  • 42
    • 0024686721 scopus 로고
    • Conformation of a bulge-containing oligomer from a hot spot sequence by NMR and energy minimization
    • Woodson, S. A. & Crothers, D. M. (1989). Conformation of a bulge-containing oligomer from a hot spot sequence by NMR and energy minimization. Biopolymers 28, 1149-1177.
    • (1989) Biopolymers , vol.28 , pp. 1149-1177
    • Woodson, S.A.1    Crothers, D.M.2
  • 43
    • 0024471947 scopus 로고
    • 31P NMR spectra and restrained molecular dynamics structure of an extrahelical adenosine base tridecamer oligodeoxyribonucleotide duplex
    • 31P NMR spectra and restrained molecular dynamics structure of an extrahelical adenosine base tridecamer oligodeoxyribonucleotide duplex. Biochemistry 28, 8714-8725.
    • (1989) Biochemistry , vol.28 , pp. 8714-8725
    • Nikonowicz, E.P.1    Roongta, V.2    Jones, C.R.3    Gorenstein, D.G.4
  • 47
    • 0025037779 scopus 로고
    • Conformational transitions in thymidine bulge-containing deoxytridecanucleotide duplexes
    • Kalnik, M. W., Norman, D. G., Li, B. F., Swann, P. F. & Patel, D. J. (1990). Conformational transitions in thymidine bulge-containing deoxytridecanucleotide duplexes. J. Biol. Chem. 265, 636-647.
    • (1990) J. Biol. Chem. , vol.265 , pp. 636-647
    • Kalnik, M.W.1    Norman, D.G.2    Li, B.F.3    Swann, P.F.4    Patel, D.J.5
  • 48
    • 0024965969 scopus 로고
    • Conformational transitions in cytidine bulge-containing deoxytrideca-nucleotide duplexes: Extra cytidine equilibrates between looped out (low temperature) and stacked (elevated temperature) conformations in solution
    • Kalnik, M. W., Norman, D. G., Zagorski, M. G., Swann, P. F. & Patel, D. J. (1989). Conformational transitions in cytidine bulge-containing deoxytrideca-nucleotide duplexes: extra cytidine equilibrates between looped out (low temperature) and stacked (elevated temperature) conformations in solution. Biochemistry 28, 294-303.
    • (1989) Biochemistry , vol.28 , pp. 294-303
    • Kalnik, M.W.1    Norman, D.G.2    Zagorski, M.G.3    Swann, P.F.4    Patel, D.J.5
  • 49
    • 0023893160 scopus 로고
    • Bulge-out structures in the single-stranded trimer AUA and in the duplex (CUGGUGCGG)·(CCGCCCAG). A model-building and NMR study
    • van den Hoogen, Y. T., van Beuzekom, A. A., de Vroom, E., van der Marel, G. A., van Boom, J. H. & Altona, C. (1988). Bulge-out structures in the single-stranded trimer AUA and in the duplex (CUGGUGCGG)·(CCGCCCAG). A model-building and NMR study. Nucleic Acids Res. 16, 5013-5030.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5013-5030
    • Van Den Hoogen, Y.T.1    Van Beuzekom, A.A.2    De Vroom, E.3    Van Der Marel, G.A.4    Van Boom, J.H.5    Altona, C.6
  • 51
    • 0028063567 scopus 로고
    • Three-dimensional structure of a hammerhead ribozyme
    • Pley, H. W., Flaherty, K. M. & McKay, D. B. (1994). Three-dimensional structure of a hammerhead ribozyme. Nature 372, 68-74.
    • (1994) Nature , vol.372 , pp. 68-74
    • Pley, H.W.1    Flaherty, K.M.2    McKay, D.B.3
  • 52
    • 0026556769 scopus 로고
    • Crystal structure of an Okazaki fragment at 2 Å resolution
    • Egli, M., Usman, N., Zhang, S. & Rich, A. (1992). Crystal structure of an Okazaki fragment at 2 Å resolution. Proc. Natl. Acad. Sci. USA 89, 534-538.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 534-538
    • Egli, M.1    Usman, N.2    Zhang, S.3    Rich, A.4
  • 53
    • 0027299690 scopus 로고
    • Conformational influence of the ribose 2′-hydroxyl group: Crystal structures of DNA-RNA chimeric duplexes
    • Egli, M., Usman, N. & Rich A. (1993). Conformational influence of the ribose 2′-hydroxyl group: crystal structures of DNA-RNA chimeric duplexes. Biochemistry 32, 3221-3237.
    • (1993) Biochemistry , vol.32 , pp. 3221-3237
    • Egli, M.1    Usman, N.2    Rich, A.3
  • 54
    • 0028350664 scopus 로고
    • A single 2′-hydroxyl group converts B-DNA to A-DNA. Crystal structure of the DNA-RNA chimeric decamer duplex d(CCGGC)r(G)d(CCGG) with a novel intermolecular G·C base-paired quadruplet
    • Ban, C., Ramakrishnan, B. & Sundaralingam, M. (1994). A single 2′-hydroxyl group converts B-DNA to A-DNA. Crystal structure of the DNA-RNA chimeric decamer duplex d(CCGGC)r(G)d(CCGG) with a novel intermolecular G·C base-paired quadruplet. J. Mol. Biol. 236, 275-285.
    • (1994) J. Mol. Biol. , vol.236 , pp. 275-285
    • Ban, C.1    Ramakrishnan, B.2    Sundaralingam, M.3
  • 55
    • 0025071240 scopus 로고
    • Solution structure of an unusually stable RNA hairpin, 5′GGAC(UUCG)GUCC
    • Cheong, C., Varani, G. & Tinoco Jr., I. (1990). Solution structure of an unusually stable RNA hairpin, 5′GGAC(UUCG)GUCC. Nature 346, 680-682.
    • (1990) Nature , vol.346 , pp. 680-682
    • Cheong, C.1    Varani, G.2    Tinoco Jr., I.3
  • 56
    • 0023423118 scopus 로고
    • The crystal structure of d(CCCCGGGG): A new A-form variant with an extended backbone conformation
    • Haran, T. E., Shakked, Z., Wang, A. H.-J. & Rich, A. (1987). The crystal structure of d(CCCCGGGG): a new A-form variant with an extended backbone conformation. J. Biomol. Struct. Dyn. 5, 199-217.
    • (1987) J. Biomol. Struct. Dyn. , vol.5 , pp. 199-217
    • Haran, T.E.1    Shakked, Z.2    Wang, A.H.-J.3    Rich, A.4
  • 57
    • 0029051383 scopus 로고
    • The crystal structure of r(CCCCGGGG) in two distinct lattices
    • Portmann, S., Usman, N. & Egli, M. (1995). The crystal structure of r(CCCCGGGG) in two distinct lattices. Biochemistry 34, 7569-7575.
    • (1995) Biochemistry , vol.34 , pp. 7569-7575
    • Portmann, S.1    Usman, N.2    Egli, M.3
  • 58
    • 0028072693 scopus 로고
    • Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence energy transfer
    • Gohlke, C., Murchie, A.I.H., Lilley, D.M.J. & Clegg, R.M. (1994). Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence energy transfer. Proc. Natl. Acad. Sci. USA 91, 11660-11664.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11660-11664
    • Gohlke, C.1    Murchie, A.I.H.2    Lilley, D.M.J.3    Clegg, R.M.4
  • 59
    • 0028969693 scopus 로고
    • Bulge-induced bends in RNA: Quantification by transient electric birefringence
    • Zacharias, M. & Hagerman, P.J. (1995). Bulge-induced bends in RNA: quantification by transient electric birefringence. J. Mol. Biol. 247, 486-500.
    • (1995) J. Mol. Biol. , vol.247 , pp. 486-500
    • Zacharias, M.1    Hagerman, P.J.2
  • 60
    • 0028000994 scopus 로고
    • Coaxial stacking of helixes enhances binding of oligoribonucleotides and improves predictions of RNA folding
    • Walter, A.E., et al., & Zuker, M. (1994). Coaxial stacking of helixes enhances binding of oligoribonucleotides and improves predictions of RNA folding. Proc. Natl. Acad. Sci. USA 91, 9218-9222.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9218-9222
    • Walter, A.E.1    Zuker, M.2
  • 61
    • 0016146021 scopus 로고
    • Three-dimensional tertiary structure of yeast phenylalanine transfer RNA
    • Kim, S.-H., et al., & Rich, A. (1974). Three-dimensional tertiary structure of yeast phenylalanine transfer RNA. Science 185, 435-440.
    • (1974) Science , vol.185 , pp. 435-440
    • Kim, S.-H.1    Rich, A.2
  • 62
    • 0016354122 scopus 로고
    • Structure of yeast phenylalanine tRNA at 3 Å resolution
    • Robertus, J.D., et al., & Klug, A. (1974). Structure of yeast phenylalanine tRNA at 3 Å resolution. Nature 250, 546-551.
    • (1974) Nature , vol.250 , pp. 546-551
    • Robertus, J.D.1    Klug, A.2
  • 63
    • 0029073091 scopus 로고
    • The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA cleavage
    • Scott, W.G., Finch, J.T. & Klug, A. (1995). The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA cleavage. Cell 81, 991-1002.
    • (1995) Cell , vol.81 , pp. 991-1002
    • Scott, W.G.1    Finch, J.T.2    Klug, A.3
  • 64
    • 0343387237 scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of double-helical RNA octamers
    • Egli, M., Portmann, S., Tracz, D., Workman, C. & Usman, N. (1995). Crystallization and preliminary X-ray diffraction analysis of double-helical RNA octamers. Acta Cryst. D 51, 1065-1070.
    • (1995) Acta Cryst. D , vol.51 , pp. 1065-1070
    • Egli, M.1    Portmann, S.2    Tracz, D.3    Workman, C.4    Usman, N.5
  • 65
    • 0002920388 scopus 로고
    • Pseudo-rotation in the hydrolysis of phosphate esters
    • Westheimer, F.H. (1968). Pseudo-rotation in the hydrolysis of phosphate esters. Accounts Chem. Res. 1, 70-78.
    • (1968) Accounts Chem. Res. , vol.1 , pp. 70-78
    • Westheimer, F.H.1
  • 66
    • 0022433369 scopus 로고
    • Crystallographic and biochemical investigation of the lead(II)-catalyzed hydrolysis of yeast phenylalanine tRNA
    • Brown, R.S., Dewan, J.C. & Klug, A. (1985). Crystallographic and biochemical investigation of the lead(II)-catalyzed hydrolysis of yeast phenylalanine tRNA. Biochemistry 24, 4785-4801.
    • (1985) Biochemistry , vol.24 , pp. 4785-4801
    • Brown, R.S.1    Dewan, J.C.2    Klug, A.3
  • 67
    • 0000806492 scopus 로고
    • Hydrolytic stability of helical RNA: A selective advantage for the natural 3′,5′-bond
    • Usher, D.A. & McHale, A.H. (1976). Hydrolytic stability of helical RNA: a selective advantage for the natural 3′,5′-bond. Proc. Natl. Acad. Sci. USA 73, 1149-1153.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1149-1153
    • Usher, D.A.1    McHale, A.H.2
  • 68
    • 0023498849 scopus 로고
    • Conformational changes and dynamics of tRNAs: Evidence from hydrolysis patterns
    • Dock-Bregeon, A.C. & Moras, D. (1987). Conformational changes and dynamics of tRNAs: evidence from hydrolysis patterns. Cold Spring Harb. Symp. Quant. Biol. 52, 113-121.
    • (1987) Cold Spring Harb. Symp. Quant. Biol. , vol.52 , pp. 113-121
    • Dock-Bregeon, A.C.1    Moras, D.2
  • 69
    • 0027930396 scopus 로고
    • Sequence-specific cleavage of oligoribonucleotide capable of forming a stem and loop structure
    • Hosaka, H., Sakabe, I., Sakamoto, K., Yokoyama, S. & Takaku, H. (1994). Sequence-specific cleavage of oligoribonucleotide capable of forming a stem and loop structure. J. Biol. Chem. 269, 20090-20094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20090-20094
    • Hosaka, H.1    Sakabe, I.2    Sakamoto, K.3    Yokoyama, S.4    Takaku, H.5
  • 70
    • 0027105233 scopus 로고
    • Large scale chemical synthesis, purification and crystallization of RNA-DNA chimeras
    • Usman, N., Egli, M. & Rich, A. (1992). Large scale chemical synthesis, purification and crystallization of RNA-DNA chimeras. Nucleic Acids Res. 20, 6695-6699.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6695-6699
    • Usman, N.1    Egli, M.2    Rich, A.3
  • 71
    • 0029151591 scopus 로고
    • Synthesis, deprotection, analysis and purification of RNA and ribozymes
    • Wincott, F., et al., & Usman, N. (1995). Synthesis, deprotection, analysis and purification of RNA and ribozymes. Nucleic Acids Res. 23, 2677-2684.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2677-2684
    • Wincott, F.1    Usman, N.2
  • 72
    • 0025234477 scopus 로고
    • Atomic-resolution structure of the cellulose synthase regulator cyclic diguanylic acid
    • Egli, M., et al., & Frederick, C. A. (1990). Atomic-resolution structure of the cellulose synthase regulator cyclic diguanylic acid. Proc. Natl. Acad. Sci. USA 87, 3235-3239.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3235-3239
    • Egli, M.1    Frederick, C.A.2
  • 74
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 75
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 76
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.