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Volumn 351, Issue 4, 2005, Pages 731-748

Structural dynamics of precursor and product of the RNA enzyme from the hepatitis delta virus as revealed by molecular dynamics simulations

Author keywords

Cytidine protonation; HDV ribozyme; Hydration site; Metal ion binding; RNA folding

Indexed keywords

CYTIDINE; METAL ION; RIBOZYME; SODIUM ION;

EID: 23444456517     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.06.016     Document Type: Article
Times cited : (59)

References (78)
  • 1
    • 0029071510 scopus 로고
    • The molecular biology of hepatitis delta virus
    • M.M. Lai The molecular biology of hepatitis delta virus Annu. Rev. Biochem. 64 1995 259 286
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 259-286
    • Lai, M.M.1
  • 2
    • 0035997396 scopus 로고    scopus 로고
    • Catalytic strategies of the hepatitis delta virus ribozymes
    • I.H. Shih, and M.D. Been Catalytic strategies of the hepatitis delta virus ribozymes Annu. Rev. Biochem. 71 2002 887 917
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 887-917
    • Shih, I.H.1    Been, M.D.2
  • 3
    • 0033215448 scopus 로고    scopus 로고
    • Imidazole rescue of a cytosine mutation in a self-cleaving ribozyme
    • A.T. Perrotta, I. Shih, and M.D. Been Imidazole rescue of a cytosine mutation in a self-cleaving ribozyme Science 286 1999 123 126
    • (1999) Science , vol.286 , pp. 123-126
    • Perrotta, A.T.1    Shih, I.2    Been, M.D.3
  • 4
    • 0034712097 scopus 로고    scopus 로고
    • General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme
    • S. Nakano, D.M. Chadalavada, and P.C. Bevilacqua General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme Science 287 2000 1493 1497
    • (2000) Science , vol.287 , pp. 1493-1497
    • Nakano, S.1    Chadalavada, D.M.2    Bevilacqua, P.C.3
  • 5
    • 0026663180 scopus 로고
    • Random mutations to evaluate the role of bases at two important single-stranded regions of genomic HDV ribozyme
    • P.K. Kumar, Y.A. Suh, H. Miyashiro, F. Nishikawa, J. Kawakami, K. Taira, and S. Nishikawa Random mutations to evaluate the role of bases at two important single-stranded regions of genomic HDV ribozyme Nucl. Acids Res. 20 1992 3919 3924
    • (1992) Nucl. Acids Res. , vol.20 , pp. 3919-3924
    • Kumar, P.K.1    Suh, Y.A.2    Miyashiro, H.3    Nishikawa, F.4    Kawakami, J.5    Taira, K.6    Nishikawa, S.7
  • 6
    • 0028446537 scopus 로고
    • A three-dimensional model of hepatitis delta virus ribozyme based on biochemical and mutational analyses
    • N.K. Tanner, S. Schaff, G. Thill, E. Petit-Koskas, A.M. Crain-Denoyelle, and E. Westhof A three-dimensional model of hepatitis delta virus ribozyme based on biochemical and mutational analyses Curr. Biol. 4 1994 488 498
    • (1994) Curr. Biol. , vol.4 , pp. 488-498
    • Tanner, N.K.1    Schaff, S.2    Thill, G.3    Petit-Koskas, E.4    Crain-Denoyelle, A.M.5    Westhof, E.6
  • 7
    • 0029964591 scopus 로고    scopus 로고
    • Core sequences and a cleavage site wobble pair required for HDV antigenomic ribozyme self-cleavage
    • A.T. Perrotta, and M.D. Been Core sequences and a cleavage site wobble pair required for HDV antigenomic ribozyme self-cleavage Nucl. Acids Res. 24 1996 1314 1321
    • (1996) Nucl. Acids Res. , vol.24 , pp. 1314-1321
    • Perrotta, A.T.1    Been, M.D.2
  • 8
    • 0032497521 scopus 로고    scopus 로고
    • Crystal structure of a hepatitis delta virus ribozyme
    • A.R. Ferre-D'Amare, K. Zhou, and J.A. Doudna Crystal structure of a hepatitis delta virus ribozyme Nature 395 1998 567 574
    • (1998) Nature , vol.395 , pp. 567-574
    • Ferre-D'Amare, A.R.1    Zhou, K.2    Doudna, J.A.3
  • 9
    • 0034695419 scopus 로고    scopus 로고
    • Crystallization and structure determination of a hepatitis delta virus ribozyme: Use of the RNA-binding protein U1A as a crystallization module
    • A.R. Ferre-D'Amare, and J.A. Doudna Crystallization and structure determination of a hepatitis delta virus ribozyme: use of the RNA-binding protein U1A as a crystallization module J. Mol. Biol. 295 2000 541 556
    • (2000) J. Mol. Biol. , vol.295 , pp. 541-556
    • Ferre-D'Amare, A.R.1    Doudna, J.A.2
  • 10
    • 2442641641 scopus 로고    scopus 로고
    • A conformational switch controls hepatitis delta virus ribozyme catalysis
    • A. Ke, K. Zhou, F. Ding, J.H. Cate, and J.A. Doudna A conformational switch controls hepatitis delta virus ribozyme catalysis Nature 429 2004 201 205
    • (2004) Nature , vol.429 , pp. 201-205
    • Ke, A.1    Zhou, K.2    Ding, F.3    Cate, J.H.4    Doudna, J.A.5
  • 11
    • 0035793217 scopus 로고    scopus 로고
    • A pH-sensitive RNA tertiary interaction affects self-cleavage activity of the HDV ribozymes in the absence of added divalent metal ion
    • T.S. Wadkins, I. Shih, A.T. Perrotta, and M.D. Been A pH-sensitive RNA tertiary interaction affects self-cleavage activity of the HDV ribozymes in the absence of added divalent metal ion J. Mol. Biol. 305 2001 1045 1055
    • (2001) J. Mol. Biol. , vol.305 , pp. 1045-1055
    • Wadkins, T.S.1    Shih, I.2    Perrotta, A.T.3    Been, M.D.4
  • 12
    • 0035852640 scopus 로고    scopus 로고
    • Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage
    • I.H. Shih, and M.D. Been Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage Proc. Natl Acad. Sci. USA 98 2001 1489 1494
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1489-1494
    • Shih, I.H.1    Been, M.D.2
  • 13
    • 0035861073 scopus 로고    scopus 로고
    • Proton inventory of the genomic HDV ribozyme in Mg(2+)-containing solutions
    • S. Nakano, and P.C. Bevilacqua Proton inventory of the genomic HDV ribozyme in Mg(2+)-containing solutions J. Am. Chem. Soc. 123 2001 11333 11334
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11333-11334
    • Nakano, S.1    Bevilacqua, P.C.2
  • 14
    • 0037133526 scopus 로고    scopus 로고
    • PK(a) perturbation in genomic Hepatitis Delta Virus ribozyme catalysis evidenced by nucleotide analogue interference mapping
    • A.K. Oyelere, J.R. Kardon, and S.A. Strobel pK(a) perturbation in genomic Hepatitis Delta Virus ribozyme catalysis evidenced by nucleotide analogue interference mapping Biochemistry 41 2002 3667 3675
    • (2002) Biochemistry , vol.41 , pp. 3667-3675
    • Oyelere, A.K.1    Kardon, J.R.2    Strobel, S.A.3
  • 15
    • 0035812381 scopus 로고    scopus 로고
    • Direct pK(a) measurement of the active-site cytosine in a genomic hepatitis delta virus ribozyme
    • A. Luptak, A.R. Ferre-D'Amare, K. Zhou, K.W. Zilm, and J.A. Doudna Direct pK(a) measurement of the active-site cytosine in a genomic hepatitis delta virus ribozyme J. Am. Chem. Soc. 123 2001 8447 8452
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8447-8452
    • Luptak, A.1    Ferre-D'Amare, A.R.2    Zhou, K.3    Zilm, K.W.4    Doudna, J.A.5
  • 16
    • 0037154091 scopus 로고    scopus 로고
    • Reaction pathway of the trans-acting hepatitis delta virus ribozyme: A conformational change accompanies catalysis
    • M.J. Pereira, D.A. Harris, D. Rueda, and N.G. Walter Reaction pathway of the trans-acting hepatitis delta virus ribozyme: a conformational change accompanies catalysis Biochemistry 41 2002 730 740
    • (2002) Biochemistry , vol.41 , pp. 730-740
    • Pereira, M.J.1    Harris, D.A.2    Rueda, D.3    Walter, N.G.4
  • 17
    • 0037044320 scopus 로고    scopus 로고
    • Local conformational changes in the catalytic core of the trans-acting hepatitis delta virus ribozyme accompany catalysis
    • D.A. Harris, D. Rueda, and N.G. Walter Local conformational changes in the catalytic core of the trans-acting hepatitis delta virus ribozyme accompany catalysis Biochemistry 41 2002 12051 12061
    • (2002) Biochemistry , vol.41 , pp. 12051-12061
    • Harris, D.A.1    Rueda, D.2    Walter, N.G.3
  • 18
    • 0038001437 scopus 로고    scopus 로고
    • Trans-acting hepatitis delta virus ribozyme: Catalytic core and global structure are dependent on the 5′ substrate sequence
    • S. Jeong, J. Sefcikova, R.A. Tinsley, D. Rueda, and N.G. Walter Trans-acting hepatitis delta virus ribozyme: catalytic core and global structure are dependent on the 5′ substrate sequence Biochemistry 42 2003 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
  • 19
    • 0242666821 scopus 로고    scopus 로고
    • Significant kinetic solvent isotope effects in folding of the catalytic RNA from the hepatitis delta virus
    • R.A. Tinsley, D.A. Harris, and N.G. Walter Significant kinetic solvent isotope effects in folding of the catalytic RNA from the hepatitis delta virus J. Am. Chem. Soc. 125 2003 13972 13973
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13972-13973
    • Tinsley, R.A.1    Harris, D.A.2    Walter, N.G.3
  • 20
    • 3142746008 scopus 로고    scopus 로고
    • Magnesium dependence of the amplified conformational switch in the trans-acting hepatitis delta virus ribozyme
    • R.A. Tinsley, D.A. Harris, and N.G. Walter Magnesium dependence of the amplified conformational switch in the trans-acting hepatitis delta virus ribozyme Biochemistry 43 2004 8935 8945
    • (2004) Biochemistry , vol.43 , pp. 8935-8945
    • Tinsley, R.A.1    Harris, D.A.2    Walter, N.G.3
  • 21
    • 3342915806 scopus 로고    scopus 로고
    • Terbium-mediated footprinting probes a catalytic conformational switch in the antigenomic hepatitis delta virus ribozyme
    • D.A. Harris, R.A. Tinsley, and N.G. Walter Terbium-mediated footprinting probes a catalytic conformational switch in the antigenomic hepatitis delta virus ribozyme J. Mol. Biol. 341 2004 389 403
    • (2004) J. Mol. Biol. , vol.341 , pp. 389-403
    • Harris, D.A.1    Tinsley, R.A.2    Walter, N.G.3
  • 23
    • 0025597973 scopus 로고
    • The self-cleaving domain from the genomic RNA of hepatitis delta virus: Sequence requirements and the effects of denaturant
    • A.T. Perrotta, and M.D. Been The self-cleaving domain from the genomic RNA of hepatitis delta virus: sequence requirements and the effects of denaturant Nucl. Acids Res. 18 1990 6821 6827
    • (1990) Nucl. Acids Res. , vol.18 , pp. 6821-6827
    • Perrotta, A.T.1    Been, M.D.2
  • 24
    • 0032054952 scopus 로고    scopus 로고
    • Simulations of the molecular dynamics of nucleic acids
    • P. Auffinger, and E. Westhof Simulations of the molecular dynamics of nucleic acids Curr. Opin. Struct. Biol. 8 1998 227 236
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 227-236
    • Auffinger, P.1    Westhof, E.2
  • 25
    • 0032907143 scopus 로고    scopus 로고
    • Molecular dynamics simulations of solvated yeast tRNA(Asp)
    • P. Auffinger, S. Louise-May, and E. Westhof Molecular dynamics simulations of solvated yeast tRNA(Asp) Biophys. J. 76 1999 50 64
    • (1999) Biophys. J. , vol.76 , pp. 50-64
    • Auffinger, P.1    Louise-May, S.2    Westhof, E.3
  • 26
    • 0034235396 scopus 로고    scopus 로고
    • Importance of discriminator base stacking interactions: Molecular dynamics analysis of A73 microhelix(Ala) variants
    • M.C. Nagan, P. Beuning, K. Musier-Forsyth, and C.J. Cramer Importance of discriminator base stacking interactions: molecular dynamics analysis of A73 microhelix(Ala) variants Nucl. Acids Res. 28 2000 2527 2534
    • (2000) Nucl. Acids Res. , vol.28 , pp. 2527-2534
    • Nagan, M.C.1    Beuning, P.2    Musier-Forsyth, K.3    Cramer, C.J.4
  • 27
    • 0033855843 scopus 로고    scopus 로고
    • Conformational dynamics of a 5S rRNA hairpin domain containing loop D and a single nucleotide bulge
    • J. Sarzynska, T. Kulinski, and L. Nilsson Conformational dynamics of a 5S rRNA hairpin domain containing loop D and a single nucleotide bulge Biophys. J. 79 2000 1213 1227
    • (2000) Biophys. J. , vol.79 , pp. 1213-1227
    • Sarzynska, J.1    Kulinski, T.2    Nilsson, L.3
  • 28
    • 14244271476 scopus 로고    scopus 로고
    • Molecular dynamics simulation of nucleic acids: Successes, limitations, and promise
    • T.E. Cheatham 3rd, and M.A. Young Molecular dynamics simulation of nucleic acids: successes, limitations, and promise Biopolymers 56 2000 232 256
    • (2000) Biopolymers , vol.56 , pp. 232-256
    • Cheatham III, T.E.1    Young, M.A.2
  • 29
    • 0034837523 scopus 로고    scopus 로고
    • Molecular dynamics and thermodynamics of protein-RNA interactions: Mutation of a conserved aromatic residue modifies stacking interactions and structural adaptation in the U1A-stem loop 2 RNA complex
    • D.M. Blakaj, K.J. McConnell, D.L. Beveridge, and A.M. Baranger Molecular dynamics and thermodynamics of protein-RNA interactions: mutation of a conserved aromatic residue modifies stacking interactions and structural adaptation in the U1A-stem loop 2 RNA complex J. Am. Chem. Soc. 123 2001 2548 2551
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2548-2551
    • Blakaj, D.M.1    McConnell, K.J.2    Beveridge, D.L.3    Baranger, A.M.4
  • 30
    • 0035834495 scopus 로고    scopus 로고
    • Molecular dynamics of the frame-shifting pseudoknot from beet western yellows virus: The role of non-Watson-Crick base-pairing, ordered hydration, cation binding and base mutations on stability and unfolding
    • K. Csaszar, N. Spackova, R. Stefl, J. Sponer, and N.B. Leontis Molecular dynamics of the frame-shifting pseudoknot from beet western yellows virus: the role of non-Watson-Crick base-pairing, ordered hydration, cation binding and base mutations on stability and unfolding J. Mol. Biol. 313 2001 1073 1091
    • (2001) J. Mol. Biol. , vol.313 , pp. 1073-1091
    • Csaszar, K.1    Spackova, N.2    Stefl, R.3    Sponer, J.4    Leontis, N.B.5
  • 31
    • 0035951296 scopus 로고    scopus 로고
    • Molecular dynamics simulation reveals conformational switching of water-mediated uracil-cytosine base-pairs in an RNA duplex
    • C. Schneider, M. Brandl, and J. Suhnel Molecular dynamics simulation reveals conformational switching of water-mediated uracil-cytosine base-pairs in an RNA duplex J. Mol. Biol. 305 2001 659 667
    • (2001) J. Mol. Biol. , vol.305 , pp. 659-667
    • Schneider, C.1    Brandl, M.2    Suhnel, J.3
  • 32
    • 0037114646 scopus 로고    scopus 로고
    • Molecular dynamics simulation studies of induced fit and conformational capture in U1A-RNA binding: Do molecular substates code for specificity?
    • F. Pitici, D.L. Beveridge, and A.M. Baranger Molecular dynamics simulation studies of induced fit and conformational capture in U1A-RNA binding: do molecular substates code for specificity? Biopolymers 65 2002 424 435
    • (2002) Biopolymers , vol.65 , pp. 424-435
    • Pitici, F.1    Beveridge, D.L.2    Baranger, A.M.3
  • 33
    • 0037764044 scopus 로고    scopus 로고
    • Non-Watson-Crick base-pairing and hydration in RNA motifs: Molecular dynamics of 5S rRNA loop e
    • K. Reblova, N. Spackova, R. Stefl, K. Csaszar, J. Koca, N.B. Leontis, and J. Sponer Non-Watson-Crick base-pairing and hydration in RNA motifs: molecular dynamics of 5S rRNA loop E Biophys. J. 84 2003 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
  • 34
    • 17944388579 scopus 로고    scopus 로고
    • Molecular dynamics simulations of RNA kissing-loop motifs reveal structural dynamics and formation of cation-binding pockets
    • K. Reblova, N. Spackova, J.E. Sponer, J. Koca, and J. Sponer Molecular dynamics simulations of RNA kissing-loop motifs reveal structural dynamics and formation of cation-binding pockets Nucl. Acids Res. 31 2003 6942 6952
    • (2003) Nucl. Acids Res. , vol.31 , pp. 6942-6952
    • Reblova, K.1    Spackova, N.2    Sponer, J.E.3    Koca, J.4    Sponer, J.5
  • 35
    • 0038539610 scopus 로고    scopus 로고
    • 2+ binding sites of the 5S rRNA loop e motif as investigated by molecular dynamics simulations
    • 2+ binding sites of the 5S rRNA loop E motif as investigated by molecular dynamics simulations Chem. Biol. 10 2003 551 561
    • (2003) Chem. Biol. , vol.10 , pp. 551-561
    • Auffinger, P.1    Bielecki, L.2    Westhof, E.3
  • 36
    • 0037453255 scopus 로고    scopus 로고
    • Understanding discrimination by the ribosome: Stability testing and groove measurement of codon-anticodon pairs
    • K.Y. Sanbonmatsu, and S. Joseph Understanding discrimination by the ribosome: stability testing and groove measurement of codon-anticodon pairs J. Mol. Biol. 328 2003 33 47
    • (2003) J. Mol. Biol. , vol.328 , pp. 33-47
    • Sanbonmatsu, K.Y.1    Joseph, S.2
  • 37
    • 0242317674 scopus 로고    scopus 로고
    • Molecular dynamics reveals the stabilizing role of loop closing residues in kissing interactions: Comparison between TAR-TAR* and TAR-aptamer
    • F. Beaurain, C. Di Primo, J.J. Toulme, and M. Laguerre Molecular dynamics reveals the stabilizing role of loop closing residues in kissing interactions: comparison between TAR-TAR* and TAR-aptamer Nucl. Acids Res. 31 2003 4275 4284
    • (2003) Nucl. Acids Res. , vol.31 , pp. 4275-4284
    • Beaurain, F.1    Di Primo, C.2    Toulme, J.J.3    Laguerre, M.4
  • 38
    • 1242347628 scopus 로고    scopus 로고
    • Theoretical methods for the simulation of nucleic acids
    • M. Orozco, A. Perez, A. Noy, and F.J. Luque Theoretical methods for the simulation of nucleic acids Chem. Soc. Rev. 32 2003 350 364
    • (2003) Chem. Soc. Rev. , vol.32 , pp. 350-364
    • Orozco, M.1    Perez, A.2    Noy, A.3    Luque, F.J.4
  • 39
    • 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 2004 555 571
    • (2004) J. Mol. Biol. , vol.335 , pp. 555-571
    • Auffinger, P.1    Bielecki, L.2    Westhof, E.3
  • 40
    • 17844375121 scopus 로고    scopus 로고
    • Hinge-like motions in RNA kink-turns: The role of the second A-minor motif and nominally unpaired bases
    • F. Razga, J. Koca, J. Sponer, and N.B. Leontis Hinge-like motions in RNA kink-turns: the role of the second A-minor motif and nominally unpaired bases Biophys. J. 88 2005 3466 3485
    • (2005) Biophys. J. , vol.88 , pp. 3466-3485
    • Razga, F.1    Koca, J.2    Sponer, J.3    Leontis, N.B.4
  • 41
    • 0030849184 scopus 로고    scopus 로고
    • Evidence for a hydroxide ion bridging two magnesium ions at the active site of the hammerhead ribozyme
    • T. Hermann, P. Auffinger, W.G. Scott, and E. Westhof Evidence for a hydroxide ion bridging two magnesium ions at the active site of the hammerhead ribozyme Nucl. Acids Res. 25 1997 3421 3427
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3421-3427
    • Hermann, T.1    Auffinger, P.2    Scott, W.G.3    Westhof, E.4
  • 42
    • 0031915278 scopus 로고    scopus 로고
    • Molecular dynamics investigations of hammerhead ribozyme RNA
    • T. Hermann, P. Auffinger, and E. Westhof Molecular dynamics investigations of hammerhead ribozyme RNA Eur. Biophys. J. 27 1998 153 165
    • (1998) Eur. Biophys. J. , vol.27 , pp. 153-165
    • Hermann, T.1    Auffinger, P.2    Westhof, E.3
  • 43
    • 0032530132 scopus 로고    scopus 로고
    • Molecular dynamics study displays near in-line attack conformations in the hammerhead ribozyme self-cleavage reaction
    • R.A. Torres, and T.C. Bruice Molecular dynamics study displays near in-line attack conformations in the hammerhead ribozyme self-cleavage reaction Proc. Natl Acad. Sci. USA 95 1998 11077 11082
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11077-11082
    • Torres, R.A.1    Bruice, T.C.2
  • 44
    • 0034624405 scopus 로고    scopus 로고
    • The mechanism of phosphodiester hydrolysis: Near in-line attack conformations in the hammerhead ribozyme
    • R.A. Torres, and T.C. Bruice The mechanism of phosphodiester hydrolysis: near in-line attack conformations in the hammerhead ribozyme J. Am. Chem. Soc. 122 2000 781 791
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 781-791
    • Torres, R.A.1    Bruice, T.C.2
  • 45
    • 0037205883 scopus 로고    scopus 로고
    • Catalytic role of metal ion in the selection of competing reaction paths: A first principles molecular dynamics study of the enzymatic reaction in ribozyme
    • M. Boero, K. Terakura, and M. Tateno Catalytic role of metal ion in the selection of competing reaction paths: A first principles molecular dynamics study of the enzymatic reaction in ribozyme J. Am. Chem. Soc. 124 2002 8949 8957
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8949-8957
    • Boero, M.1    Terakura, K.2    Tateno, M.3
  • 46
    • 4043179941 scopus 로고    scopus 로고
    • DNA and its counterions: A molecular dynamics study
    • P. Varnai, and K. Zakrzewska DNA and its counterions: a molecular dynamics study Nucl. Acids Res. 32 2004 4269 4280
    • (2004) Nucl. Acids Res. , vol.32 , pp. 4269-4280
    • Varnai, P.1    Zakrzewska, K.2
  • 47
    • 4143138536 scopus 로고    scopus 로고
    • Exploring the counterion atmosphere around DNA: What can be learned from molecular dynamics simulations?
    • M. Rueda, E. Cubero, C.A. Laughton, and M. Orozco Exploring the counterion atmosphere around DNA: what can be learned from molecular dynamics simulations? Biophys. J. 87 2004 800 811
    • (2004) Biophys. J. , vol.87 , pp. 800-811
    • Rueda, M.1    Cubero, E.2    Laughton, C.A.3    Orozco, M.4
  • 49
    • 0037102491 scopus 로고    scopus 로고
    • The non-Watson-Crick base-pairs and their associated isostericity matrices
    • N.B. Leontis, J. Stombaugh, and E. Westhof The non-Watson-Crick base-pairs and their associated isostericity matrices Nucl. Acids Res. 30 2002 3497 3531
    • (2002) Nucl. Acids Res. , vol.30 , pp. 3497-3531
    • Leontis, N.B.1    Stombaugh, J.2    Westhof, E.3
  • 50
    • 0347763707 scopus 로고    scopus 로고
    • Catalytic roles for proton transfer and protonation in ribozymes
    • P.C. Bevilacqua, T.S. Brown, S. Nakano, and R. Yajima Catalytic roles for proton transfer and protonation in ribozymes Biopolymers 73 2004 90 109
    • (2004) Biopolymers , vol.73 , pp. 90-109
    • Bevilacqua, P.C.1    Brown, T.S.2    Nakano, S.3    Yajima, R.4
  • 52
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • P. Nissen, J. Hansen, N. Ban, P.B. Moore, and T.A. Steitz The structural basis of ribosome activity in peptide bond synthesis Science 289 2000 920 930
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 53
    • 0034637102 scopus 로고    scopus 로고
    • A single adenosine with a neutral pKa in the ribosomal peptidyl transferase center
    • G.W. Muth, L. Ortoleva-Donnelly, and S.A. Strobel A single adenosine with a neutral pKa in the ribosomal peptidyl transferase center Science 289 2000 947 950
    • (2000) Science , vol.289 , pp. 947-950
    • Muth, G.W.1    Ortoleva-Donnelly, L.2    Strobel, S.A.3
  • 54
    • 0035848837 scopus 로고    scopus 로고
    • Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis
    • P.B. Rupert, and A.R. Ferre-D'Amare Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis Nature 410 2001 780 786
    • (2001) Nature , vol.410 , pp. 780-786
    • Rupert, P.B.1    Ferre-D'Amare, A.R.2
  • 56
    • 0034757629 scopus 로고    scopus 로고
    • PH-dependent conformational flexibility within the ribosomal peptidyl transferase center
    • G.W. Muth, L. Chen, A.B. Kosek, and S.A. Strobel pH-dependent conformational flexibility within the ribosomal peptidyl transferase center RNA 7 2001 1403 1415
    • (2001) RNA , vol.7 , pp. 1403-1415
    • Muth, G.W.1    Chen, L.2    Kosek, A.B.3    Strobel, S.A.4
  • 57
    • 0035942753 scopus 로고    scopus 로고
    • Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide
    • N. Polacek, M. Gaynor, A. Yassin, and A.S. Mankin Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide Nature 411 2001 498 501
    • (2001) Nature , vol.411 , pp. 498-501
    • Polacek, N.1    Gaynor, M.2    Yassin, A.3    Mankin, A.S.4
  • 58
    • 0036671344 scopus 로고    scopus 로고
    • Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome
    • V.I. Katunin, G.W. Muth, S.A. Strobel, W. Wintermeyer, and M.V. Rodnina Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome Mol. Cell 10 2002 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
  • 59
    • 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
    • E.M. Youngman, J.L. Brunelle, A.B. Kochaniak, and R. Green 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 2004 589 599
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 63
    • 2942577491 scopus 로고    scopus 로고
    • Role of an active site guanine in hairpin ribozyme catalysis probed by exogenous nucleobase rescue
    • Y.I. Kuzmin, C.P. Da Costa, and M.J. Fedor Role of an active site guanine in hairpin ribozyme catalysis probed by exogenous nucleobase rescue J. Mol. Biol. 340 2004 233 251
    • (2004) J. Mol. Biol. , vol.340 , pp. 233-251
    • Kuzmin, Y.I.1    Da Costa, C.P.2    Fedor, M.J.3
  • 64
    • 0343213055 scopus 로고    scopus 로고
    • Performance of empirical potentials (AMBER, CFF95, CVFF, CHARMM, OPLS, POLTEV), semi-empirical quantum chemical methods (AM1, MNDO/M, PM3), and ab initio Hartree-Fock method for interaction of DNA bases: Comparison with non-empirical beyond Hartree-Fock results
    • P. Hobza, M. Kabelac, J. Sponer, P. Mejzlik, and J. Vondrasek Performance of empirical potentials (AMBER, CFF95, CVFF, CHARMM, OPLS, POLTEV), semi-empirical quantum chemical methods (AM1, MNDO/M, PM3), and ab initio Hartree-Fock method for interaction of DNA bases: comparison with non-empirical beyond Hartree-Fock results J. Comput. Chem. 18 1997 1136 1150
    • (1997) J. Comput. Chem. , vol.18 , pp. 1136-1150
    • Hobza, P.1    Kabelac, M.2    Sponer, J.3    Mejzlik, P.4    Vondrasek, J.5
  • 65
    • 12844258405 scopus 로고    scopus 로고
    • Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex
    • K. Reblova, N. Spackova, J. Koca, N.B. Leontis, and J. Sponer Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex Biophys. J. 87 2004 3397 3412
    • (2004) Biophys. J. , vol.87 , pp. 3397-3412
    • Reblova, K.1    Spackova, N.2    Koca, J.3    Leontis, N.B.4    Sponer, J.5
  • 68
    • 0029011701 scopus 로고
    • A 2nd generation force-field for the simulation of proteins, nucleic-acids, and organic-molecules
    • W.D. Cornell, P. Cieplak, C.I. Bayly, I.R. Gould, K.M. Merz, and D.M. Ferguson A 2nd generation force-field for the simulation of proteins, nucleic-acids, and organic-molecules J. Am. Chem. Soc. 117 1995 5179 5197
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3    Gould, I.R.4    Merz, K.M.5    Ferguson, D.M.6
  • 69
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • J.M. Wang, P. Cieplak, and P.A. Kollman How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21 2000 1049 1074
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.M.1    Cieplak, P.2    Kollman, P.A.3
  • 70
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • T.E. Cheatham, P. Cieplak, and P.A. Kollman A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat J. Biomol. Struct. Dynam. 16 1999 845 862
    • (1999) J. Biomol. Struct. Dynam. , vol.16 , pp. 845-862
    • Cheatham, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 72
    • 0344796204 scopus 로고
    • Ion water interaction potentials derived from free-energy perturbation simulations
    • J. Aqvist Ion water interaction potentials derived from free-energy perturbation simulations J. Phys. Chem. 94 1990 8021 8024
    • (1990) J. Phys. Chem. , vol.94 , pp. 8021-8024
    • Aqvist, J.1
  • 73
    • 0034836422 scopus 로고    scopus 로고
    • Structural dynamics and cation interactions of DNA quadruplex molecules containing mixed guanine/cytosine quartets revealed by large-scale MD simulations
    • N. Spackova, I. Berger, and J. Sponer Structural dynamics and cation interactions of DNA quadruplex molecules containing mixed guanine/cytosine quartets revealed by large-scale MD simulations J. Am. Chem. Soc. 123 2001 3295 3307
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3295-3307
    • Spackova, N.1    Berger, I.2    Sponer, J.3
  • 76
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Chem. 23 1977 327 341
    • (1977) J. Comput. Chem. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3


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