메뉴 건너뛰기




Volumn 17, Issue 8, 2011, Pages 1589-1603

RNA molecules with conserved catalytic cores but variable peripheries fold along unique energetically optimized pathways

Author keywords

Group I introns; Kinetic intermediates; Ribozymes; RNA folding; Structural homology

Indexed keywords

HYDROXYL GROUP; RIBOZYME; RNA;

EID: 79960466968     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2694811     Document Type: Article
Times cited : (19)

References (75)
  • 1
    • 3042848954 scopus 로고    scopus 로고
    • Crystal structure of a self-splicing group I intron with both exons
    • DOI 10.1038/nature02642
    • Adams P, Stahley M, Kosek A, Wang J, Strobel S. 2004. Crystal structure of a self-splicing group I intron with both exons. Nature 430: 45-50. (Pubitemid 38915218)
    • (2004) Nature , vol.430 , Issue.6995 , pp. 45-50
    • Adams, P.L.1    Stahley, M.R.2    Kosek, A.B.3    Wang, J.4    Strobel, S.A.5
  • 2
    • 0027434244 scopus 로고
    • Thermal unfolding of a group I ribozyme: The low-temperature transition is primarily disruption of tertiary structure
    • DOI 10.1021/bi00052a021
    • Banerjee AR, Jaeger JA, Turner DH. 1993. Thermal unfolding of a group I ribozyme: the low-temperature transition is primarily disruption of tertiary structure. Biochemistry 32: 153-163. (Pubitemid 23033332)
    • (1993) Biochemistry , vol.32 , Issue.1 , pp. 153-163
    • Banerjee, A.R.1    Jaeger, J.A.2    Turner, D.H.3
  • 4
    • 0032991584 scopus 로고    scopus 로고
    • Influence of specific mutations on the thermal stability of the td group I intron in vitro and on its splicing efficiency in vivo: A comparative study
    • DOI 10.1017/S1355838299990477
    • Brion P, Schroeder R, Michel F, Westhof E. 1999. Influence of specific mutations on the thermal stability of the td group I intron in vitro and on its splicing efficiency in vivo: a comparative study. RNA 5: 947-958. (Pubitemid 29321074)
    • (1999) RNA , vol.5 , Issue.7 , pp. 947-958
    • Brion, P.1    Schroeder, R.2    Michel, F.3    Westhof, E.4
  • 7
    • 2942571539 scopus 로고    scopus 로고
    • The comparative RNA web (CRW) site: An online database of comparative sequence and structure information for ribosomal, intron, and other RNAs
    • doi: 10.1186/1471-2105-3-2
    • Cannone JJ, Subramanian S, Schnare MN, Collett JR, D'Souza LM, Du Y, Feng B, Lin N, Madabusi LV, Muller KM, et al. 2002. The comparative RNA web (CRW) site: an online database of comparative sequence and structure information for ribosomal, intron, and other RNAs. BMC Bioinformatics 3: 2. doi: 10.1186/1471-2105-3-2.
    • (2002) BMC Bioinformatics , vol.3 , pp. 2
    • Cannone, J.J.1    Subramanian, S.2    Schnare, M.N.3    Collett, J.R.4    D'Souza, L.M.5    Du, Y.6    Feng, B.7    Lin, N.8    Madabusi, L.V.9    Muller, K.M.10
  • 9
    • 0026409841 scopus 로고
    • Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity: Implications for protein-DNA interactions in vivo
    • Cayley S, Lewis BA, Guttman HJ, Record MT Jr. 1991. Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo. J Mol Biol 222: 281-300. (Pubitemid 121004007)
    • (1991) Journal of Molecular Biology , vol.222 , Issue.2 , pp. 281-300
    • Cayley, S.1    Lewis, B.A.2    Guttman, H.J.3    Record Jr., M.T.4
  • 10
    • 0025367254 scopus 로고
    • Self-splicing of group I introns
    • Cech TR. 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
  • 11
    • 38649085954 scopus 로고    scopus 로고
    • Tertiary interactions determine the accuracy of RNA folding
    • DOI 10.1021/ja076166i
    • Chauhan S, Woodson SA. 2008. Tertiary interactions determine the accuracy of RNA folding. J Am Chem Soc 130: 1296-1303. (Pubitemid 351171008)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.4 , pp. 1296-1303
    • Chauhan, S.1    Woodson, S.A.2
  • 12
    • 60149088502 scopus 로고    scopus 로고
    • Structural rearrangements linked to global folding pathways of the Azoarcus group I ribozyme
    • Chauhan S, Behrouzi R, Rangan P, Woodson SA. 2009. Structural rearrangements linked to global folding pathways of the Azoarcus group I ribozyme. J Mol Biol 386: 1167-1178.
    • (2009) J Mol Biol , vol.386 , pp. 1167-1178
    • Chauhan, S.1    Behrouzi, R.2    Rangan, P.3    Woodson, S.A.4
  • 13
    • 0028921811 scopus 로고
    • Frequent use of the same tertiary motif by self-folding RNAs
    • Costa M, Michel F. 1995. Frequent use of the same tertiary motif by self-folding RNAs. EMBO J 14: 1276-1285.
    • (1995) EMBO J , vol.14 , pp. 1276-1285
    • Costa, M.1    Michel, F.2
  • 14
    • 0030959348 scopus 로고    scopus 로고
    • Rules for RNA recognition of GNRA tetraloops deduced by vitro selection: Comparison with in vivo evolution
    • DOI 10.1093/emboj/16.11.3289
    • Costa M, Michel F. 1997. Rules for RNA recognition of GNRA tetraloops deduced by in vitro selection: comparison with in vivo evolution. EMBO J 16: 3289-3302. (Pubitemid 27234966)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3289-3302
    • Costa, M.1    Michel, F.2
  • 15
    • 13944278373 scopus 로고    scopus 로고
    • SAFA: Semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experiments
    • DOI 10.1261/rna.7214405
    • Das R, Laederach A, Pearlman SM, Herschlag D, Altman RB. 2005. SAFA: semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experiments. RNA 11: 344-354. (Pubitemid 40270826)
    • (2005) RNA , vol.11 , Issue.3 , pp. 344-354
    • Das, R.1    Laederach, A.2    Pearlman, S.M.3    Herschlag, D.4    Altman, R.B.5
  • 18
    • 0034646209 scopus 로고    scopus 로고
    • The P5abc peripheral element facilitates preorganization of the Tetrahymena group I ribozyme for catalysis
    • DOI 10.1021/bi992313g
    • Engelhardt MA, Doherty EA, Knitt DS, Doudna JA, Herschlag D. 2000. The P5abc peripheral element facilitates preorganization of the Tetrahymena group I ribozyme for catalysis. Biochemistry 39: 2639-2651. (Pubitemid 30148917)
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2639-2651
    • Engelhardt, M.A.1    Doherty, E.A.2    Knitt, D.S.3    Doudna, J.A.4    Herschlag, D.5
  • 19
    • 0032590020 scopus 로고    scopus 로고
    • Mg2+-dependent folding of a large ribozyme without kinetic traps
    • Fang XW, Pan T, Sosnick TR. 1999. Mg2+-dependent folding of a large ribozyme without kinetic traps. Nat Struct Biol 6: 1091-1095.
    • (1999) Nat Struct Biol , vol.6 , pp. 1091-1095
    • Fang, X.W.1    Pan, T.2    Sosnick, T.R.3
  • 20
    • 40249103230 scopus 로고    scopus 로고
    • Comprehensive features of natural and in vitro selected GNRA tetraloop-binding receptors
    • DOI 10.1093/nar/gkm1048
    • Geary C, Baudrey S, Jaeger L. 2008. Comprehensive features of natural and in vitro selected GNRA tetraloop-binding receptors. Nucleic Acids Res 36: 1138-1152. (Pubitemid 351330932)
    • (2008) Nucleic Acids Research , vol.36 , Issue.4 , pp. 1138-1152
    • Geary, C.1    Baudrey, S.2    Jaeger, L.3
  • 21
    • 11444263264 scopus 로고    scopus 로고
    • Crystal structure of a phage Twort group I ribozyme-product complex
    • DOI 10.1038/nsmb868
    • Golden BL, Kim H, Chase E. 2005. Crystal structure of a phage Twort group I ribozyme-product complex. Nat Struct Mol Biol 12: 82-89. (Pubitemid 40082921)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.1 , pp. 82-89
    • Golden, B.L.1    Kim, H.2    Chase, E.3
  • 22
    • 8644229237 scopus 로고    scopus 로고
    • Structure of the tetrahymena ribozyme: Base triple sandwich and metal ion at the active site
    • DOI 10.1016/j.molcel.2004.10.003, PII S1097276504005921
    • Guo F, Gooding AR, Cech TR. 2004. Structure of the Tetrahymena ribozyme: base triple sandwich and metal ion at the active site. Mol Cell 16: 351-362. (Pubitemid 39504790)
    • (2004) Molecular Cell , vol.16 , Issue.3 , pp. 351-362
    • Guo, F.1    Gooding, A.R.2    Cech, T.R.3
  • 23
    • 0022719007 scopus 로고
    • Higher order structure in ribosomal RNA
    • Gutell RR, Noller HF, Woese CR. 1986. Higher order structure in ribosomal RNA. EMBO J 5: 1111-1113.
    • (1986) EMBO J , vol.5 , pp. 1111-1113
    • Gutell, R.R.1    Noller, H.F.2    Woese, C.R.3
  • 25
    • 0033570893 scopus 로고    scopus 로고
    • Self-splicing of the Tetrahymena intron from mRNA in mammalian cells
    • DOI 10.1093/emboj/18.22.6491
    • Hagen M, Cech TR. 1999. Self-splicing of the Tetrahymena intron from mRNA in mammalian cells. EMBO J 18: 6491-6500. (Pubitemid 29533253)
    • (1999) EMBO Journal , vol.18 , Issue.22 , pp. 6491-6500
    • Hagen, M.1    Cech, T.R.2
  • 26
    • 0025085590 scopus 로고
    • Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active site
    • Herschlag D, Cech TR. 1990a. Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active site. Biochemistry 29: 10159-10171.
    • (1990) Biochemistry , vol.29 , pp. 10159-10171
    • Herschlag, D.1    Cech, T.R.2
  • 27
    • 0025149015 scopus 로고
    • Catalysis of RNA cleavage by the Tetrahymena thermaphila ribozyme. 2. Kinetic description of the reaction of an RNA substrate that forms a mismatch at the active site
    • Herschlag D, Cech TR. 1990b. Catalysis of RNA cleavage by the Tetrahymena thermaphila ribozyme. 2. Kinetic description of the reaction of an RNA substrate that forms a mismatch at the active site. Biochemistry 29: 10172-10180.
    • (1990) Biochemistry , vol.29 , pp. 10172-10180
    • Herschlag, D.1    Cech, T.R.2
  • 29
    • 0029963656 scopus 로고    scopus 로고
    • A simple method for 39-labeling of RNA
    • Huang Z, Szostak JW. 1996. A simple method for 39-labeling of RNA. Nucleic Acids Res 24: 4360-4361.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4360-4361
    • Huang, Z.1    Szostak, J.W.2
  • 30
    • 0034859319 scopus 로고    scopus 로고
    • A comparative study on two GNRA-tetraloop receptors: 11-nt and IC3 motifs
    • Ikawa Y, Nohmi K, Atsumi S, Shiraishi H, Inoue T. 2001. A comparative study on two GNRA-tetraloop receptors: 11-nt and IC3 motifs. J Biochem 130: 251-255. (Pubitemid 32785872)
    • (2001) Journal of Biochemistry , vol.130 , Issue.2 , pp. 251-255
    • Ikawa, Y.1    Nohmi, K.2    Atsumi, S.3    Shiraishi, H.4    Inoue, T.5
  • 33
    • 33646089899 scopus 로고    scopus 로고
    • Local kinetic measures of macromolecular structure reveal partitioning among multiple parallel pathways from the earliest steps in the folding of a large RNA molecule
    • Laederach A, Shcherbakova I, Liang MP, Brenowitz M, Altman RB. 2006. Local kinetic measures of macromolecular structure reveal partitioning among multiple parallel pathways from the earliest steps in the folding of a large RNA molecule. J Mol Biol 358: 1179-1190.
    • (2006) J Mol Biol , vol.358 , pp. 1179-1190
    • Laederach, A.1    Shcherbakova, I.2    Liang, M.P.3    Brenowitz, M.4    Altman, R.B.5
  • 35
    • 0033536050 scopus 로고    scopus 로고
    • Unexpected abundance of self-splicing introns in the genome of bacteriophage Twort: Introns in multiple genes, a single gene with three introns, and exon skipping by group I ribozymes
    • DOI 10.1073/pnas.96.12.7005
    • Landthaler M, Shub DA. 1999. Unexpected abundance of self-splicing introns in the genome of bacteriophage Twort: introns in multiple genes, a single gene with three introns, and exon skipping by group I ribozymes. Proc Natl Acad Sci 96: 7005-7010. (Pubitemid 29275000)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.12 , pp. 7005-7010
    • Landthaler, M.1    Shub, D.A.2
  • 36
    • 33745951899 scopus 로고    scopus 로고
    • The UAA/GAN Internal Loop Motif: A New RNA Structural Element that Forms a Cross-strand AAA Stack and Long-range Tertiary Interactions
    • DOI 10.1016/j.jmb.2006.05.066, PII S0022283606006838
    • Lee JC, Gutell RR, Russell R. 2006. The UAA/GAN internal loop motif: a new RNA structural element that forms a cross-strand AAA stack and long-range tertiary interactions. J Mol Biol 360: 978-988. (Pubitemid 44062516)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.5 , pp. 978-988
    • Lee, J.C.1    Gutell, R.R.2    Russell, R.3
  • 37
    • 0030452773 scopus 로고    scopus 로고
    • New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: A complete 3d model of the Tetrahymena thermophila ribozyme
    • Lehnert V, Jaeger L, Michel F, Westhof E. 1996. New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: a complete 3D model of the Tetrahymena thermophila ribozyme. Chem Biol 3: 993-1009. (Pubitemid 27058823)
    • (1996) Chemistry and Biology , vol.3 , Issue.12 , pp. 993-1009
    • Lehnert, V.1    Jaeger, L.2    Michel, F.3    Westhof, E.4
  • 38
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • DOI 10.1126/science.286.5438.295
    • Lockless SW, Ranganathan R. 1999. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286: 295-299. (Pubitemid 29484693)
    • (1999) Science , vol.286 , Issue.5438 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 39
    • 79960444497 scopus 로고    scopus 로고
    • Exhaustive enumeration of kinetic model topologies for the analysis of time-resolved RNA folding
    • Martin JS, Simmons K, Laederach A. 2009. Exhaustive enumeration of kinetic model topologies for the analysis of time-resolved RNA folding. Algorithms Mol Biol 2: 200-214.
    • (2009) Algorithms Mol Biol , vol.2 , pp. 200-214
    • Martin, J.S.1    Simmons, K.2    Laederach, A.3
  • 40
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • DOI 10.1038/340122a0
    • Matouschek A, Kellis JJ, Serrano L, Fersht A. 1989. Mapping the transition state and pathway of protein folding by protein engineering. Nature 340: 122-126. (Pubitemid 19175363)
    • (1989) Nature , vol.340 , Issue.6229 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 42
    • 0025678737 scopus 로고
    • Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis
    • Michel F, Westhof E. 1990. Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis. J Mol Biol 216: 585-610. (Pubitemid 120037393)
    • (1990) Journal of Molecular Biology , vol.216 , Issue.3 , pp. 585-610
    • Michel, F.1    Westhof, E.2
  • 43
    • 33745216899 scopus 로고    scopus 로고
    • Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques
    • Philo JS. 2006. Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. Anal Biochem 354: 238-246.
    • (2006) Anal Biochem , vol.354 , pp. 238-246
    • Philo, J.S.1
  • 44
    • 44049104652 scopus 로고    scopus 로고
    • Group I introns and GNRA tetraloops: Remnants of 'The RNA world'?
    • Prathiba J, Malathi R. 2008. Group I introns and GNRA tetraloops: remnants of 'The RNA world'? Mol Biol Rep 35: 239-249.
    • (2008) Mol Biol Rep , vol.35 , pp. 239-249
    • Prathiba, J.1    Malathi, R.2
  • 45
    • 0038737980 scopus 로고    scopus 로고
    • 2+ binding in the group I intron core
    • DOI 10.1016/S0022-2836(03)00430-3
    • Rangan P, Woodson SA. 2003. Structural requirement for Mg2+ binding in the group I intron core. J Mol Biol 329: 229-238. (Pubitemid 36561580)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.2 , pp. 229-238
    • Rangan, P.1    Woodson, S.A.2
  • 47
    • 0026599998 scopus 로고
    • Self-splicing introns in tRNA genes of widely divergent bacteria
    • Reinhold-Hurek B, Shub DA. 1992. Self-splicing introns in tRNA genes of widely divergent bacteria. Nature 357: 173-176.
    • (1992) Nature , vol.357 , pp. 173-176
    • Reinhold-Hurek, B.1    Shub, D.A.2
  • 49
    • 0033520410 scopus 로고    scopus 로고
    • New pathways in folding of the Tetrahymena group I RNA enzyme
    • DOI 10.1006/jmbi.1999.3026
    • Russell R, Herschlag D. 1999. New pathways in folding of the Tetrahymena group I RNA enzyme. J Mol Biol 291: 1155-1167. (Pubitemid 29423778)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.5 , pp. 1155-1167
    • Russell, R.1    Herschlag, D.2
  • 50
    • 0035906731 scopus 로고    scopus 로고
    • Probing the folding landscape of the Tetrahymena ribozyme: Commitment to form the native conformation is late in the folding pathway
    • DOI 10.1006/jmbi.2001.4751
    • Russell R, Herschlag D. 2001. Probing the folding landscape of the Tetrahymena ribozyme: commitment to form the native conformation is late in the folding pathway. J Mol Biol 308: 839-851. (Pubitemid 32574363)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.5 , pp. 839-851
    • Russell, R.1    Herschlag, D.2
  • 51
    • 0034100560 scopus 로고    scopus 로고
    • Small angle X-ray scattering reveals a compact intermediate in RNA folding
    • DOI 10.1038/75132
    • Russell R, Millett IS, Doniach S, Herschlag D. 2000. Small angle X-ray scattering reveals a compact intermediate in RNA folding. Nat Struct Biol 7: 367-370. (Pubitemid 30249997)
    • (2000) Nature Structural Biology , vol.7 , Issue.5 , pp. 367-370
    • Russell, R.1    Millett, I.S.2    Doniach, S.3    Herschlag, D.4
  • 54
    • 34247606396 scopus 로고    scopus 로고
    • Deletion of the P5abc peripheral element accelerates early and late folding steps of the Tetrahymena group I ribozyme
    • DOI 10.1021/bi0620149
    • Russell R, Tijerina P, Chadee AB, Bhaskaran H. 2007. Deletion of the P5abc peripheral element accelerates early and late folding steps of the Tetrahymena group I ribozyme. Biochemistry 46: 4951-4961. (Pubitemid 46682994)
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 4951-4961
    • Russell, R.1    Tijerina, P.2    Chadee, A.B.3    Bhaskaran, H.4
  • 55
    • 33846573286 scopus 로고    scopus 로고
    • Self-splicing of the bacteriophage T4 group I introns requires efficient translation of the pre-mRNA in vivo and correlates with the growth state of the infected bacterium
    • DOI 10.1128/JB.01287-06
    • Sandegren L, Sjoberg BM. 2007. Self-splicing of the bacteriophage T4 group I introns requires efficient translation of the pre-mRNA in vivo and correlates with the growth state of the infected bacterium. J Bacteriol 189: 980-990. (Pubitemid 46183873)
    • (2007) Journal of Bacteriology , vol.189 , Issue.3 , pp. 980-990
    • Sandegren, L.1    Sjoberg, B.-M.2
  • 57
    • 0032549780 scopus 로고    scopus 로고
    • RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting
    • DOI 10.1126/science.279.5358.1940
    • Sclavi B, Sullivan M, Chance MR, Brenowitz M, Woodson SA. 1998. RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting. Science 279: 1940-1943. (Pubitemid 28168649)
    • (1998) Science , vol.279 , Issue.5358 , pp. 1940-1943
    • Sclavi, B.1    Sullivan, M.2    Chance, M.R.3    Brenowitz, M.4    Woodson, S.A.5
  • 58
    • 27644457113 scopus 로고    scopus 로고
    • Perturbation of the hierarchical folding of a large RNA by the destabilization of its scaffold's tertiary structure
    • DOI 10.1016/j.jmb.2005.09.032, PII S0022283605010971
    • Shcherbakova I, Brenowitz M. 2005. Perturbation of the hierarchical folding of a large RNA by the destabilization of its Scaffold's tertiary structure. J Mol Biol 354: 483-496. (Pubitemid 41579860)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.2 , pp. 483-496
    • Shcherbakova, I.1    Brenowitz, M.2
  • 59
    • 39449112406 scopus 로고    scopus 로고
    • Monitoring structural changes in nucleic acids with single residue spatial and millisecond time resolution by quantitative hydroxyl radical footprinting
    • DOI 10.1038/nprot.2007.533, PII NPROT.2007.533
    • Shcherbakova I, Brenowitz M. 2008. Monitoring structural changes in nucleic acids with single residue spatial and millisecond time resolution by quantitative hydroxyl radical footprinting. Nat Protoc 3: 288-302. (Pubitemid 351266513)
    • (2008) Nature Protocols , vol.3 , Issue.2 , pp. 288-302
    • Shcherbakova, I.1    Brenowitz, M.2
  • 60
    • 33645819791 scopus 로고    scopus 로고
    • Fast Fenton footprinting: A laboratory-based method for the time-resolved analysis of DNA, RNA and proteins
    • doi: 10.1093/nar/gkl055
    • Shcherbakova I, Mitra S, Beer R, Brenowitz M. 2006. Fast Fenton footprinting: a laboratory-based method for the time-resolved analysis of DNA, RNA and proteins. Nucleic Acids Res 34: e48. doi: 10.1093/nar/gkl055.
    • (2006) Nucleic Acids Res , vol.34
    • Shcherbakova, I.1    Mitra, S.2    Beer, R.3    Brenowitz, M.4
  • 61
    • 25644452032 scopus 로고    scopus 로고
    • Evolutionary information for specifying a protein fold
    • DOI 10.1038/nature03991, PII N03991
    • Socolich M, Lockless SW, Russ WP, Lee H, Gardner KH, Ranganathan R. 2005. Evolutionary information for specifying a protein fold. Nature 437: 512-518. (Pubitemid 41613543)
    • (2005) Nature , vol.437 , Issue.7058 , pp. 512-518
    • Socolich, M.1    Lockless, S.W.2    Russ, W.P.3    Lee, H.4    Gardner, K.H.5    Ranganathan, R.6
  • 62
    • 48249086517 scopus 로고    scopus 로고
    • Kinetic barriers and the role of topology in protein and RNA folding
    • Sosnick TR. 2008. Kinetic barriers and the role of topology in protein and RNA folding. Protein Sci 17: 1308-1318.
    • (2008) Protein Sci , vol.17 , pp. 1308-1318
    • Sosnick, T.R.1
  • 63
    • 4444363049 scopus 로고    scopus 로고
    • Reduced contact order and RNA folding rates
    • DOI 10.1016/j.jmb.2004.08.002, PII S0022283604009684
    • Sosnick TR, Pan T. 2004. Reduced contact order and RNA folding rates. J Mol Biol 342: 1359-1365. (Pubitemid 39208664)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.5 , pp. 1359-1365
    • Sosnick, T.R.1    Pan, T.2
  • 64
    • 34547654293 scopus 로고    scopus 로고
    • Structural Metals in the Group I Intron: A Ribozyme with a Multiple Metal Ion Core
    • DOI 10.1016/j.jmb.2007.06.026, PII S0022283607008212
    • Stahley MR, Adams PL, Wang J, Strobel SA. 2007. Structural metals in the group I intron: a ribozyme with a multiple metal ion core. J Mol Biol 372: 89-102. (Pubitemid 47223219)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.1 , pp. 89-102
    • Stahley, M.R.1    Adams, P.L.2    Wang, J.3    Strobel, S.A.4
  • 65
    • 6344242969 scopus 로고    scopus 로고
    • Principles of RNA compaction: Insights from the equilibrium folding pathway of the P4-P6 RNA domain in monovalent cations
    • DOI 10.1016/j.jmb.2004.08.080, PII S0022283604010800
    • Takamoto K, Das R, He Q, Doniach S, Brenowitz M, Herschlag D, Chance M. 2004. Principles of RNA compaction: insights from the equilibrium folding pathway of the P4-P6 RNA domain in monovalent cations. J Mol Biol 343: 1195-1206. (Pubitemid 39387820)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1195-1206
    • Takamoto, K.1    Das, R.2    He, Q.3    Doniach, S.4    Brenowitz, M.5    Herschlag, D.6    Chance, M.R.7
  • 66
    • 0029805902 scopus 로고    scopus 로고
    • Activity and thermostability of the small self-splicing group I intron in the pre-tRNA(Ile) of the purple bacterium Azoarcus
    • Tanner M, Cech T. 1996. Activity and thermostability of the small self-splicing group I intron in the pre-tRNA(lle) of the purple bacterium Azoarcus. RNA 2: 74-83. (Pubitemid 26371313)
    • (1996) RNA , vol.2 , Issue.1 , pp. 74-83
    • Tanner, M.A.1    Cech, T.R.2
  • 68
    • 0035808384 scopus 로고    scopus 로고
    • Concerted kinetic folding of a multidomain ribozyme with a disrupted loop-receptor interaction
    • DOI 10.1006/jmbi.2000.4253
    • Treiber DK, Williamson JR. 2001b. Concerted kinetic folding of a multidomain ribozyme with a disrupted loop-receptor interaction. J Mol Biol 305: 11-21. (Pubitemid 32039741)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.1 , pp. 11-21
    • Treiber, D.K.1    Williamson, J.R.2
  • 69
    • 0037466333 scopus 로고    scopus 로고
    • Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme
    • DOI 10.1016/S0022-2836(03)00247-X
    • Uchida T, Takamoto K, He Q, Chance M, Brenowitz M. 2003. Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme. J Mol Biol 328: 463-478. (Pubitemid 36407588)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.2 , pp. 463-478
    • Uchida, T.1    Takamoto, K.2    He, Q.3    Chance, M.R.4    Brenowitz, M.5
  • 70
    • 30944458838 scopus 로고    scopus 로고
    • Atomic level architecture of group I introns revealed
    • DOI 10.1016/j.tibs.2005.11.008, PII S0968000405003403
    • Vicens Q, Cech TR. 2006. Atomic level architecture of group I introns revealed. Trends Biochem Sci 31: 41-51. (Pubitemid 43117542)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.1 , pp. 41-51
    • Vicens, Q.1    Cech, T.R.2
  • 71
    • 52949123649 scopus 로고    scopus 로고
    • Toward predicting self-splicing and protein-facilitated splicing of group I introns
    • Vicens Q, Paukstelis PJ, Westhof E, Lambowitz AM, Cech TR. 2008. Toward predicting self-splicing and protein-facilitated splicing of group I introns. RNA 14: 2013-2029.
    • (2008) RNA , vol.14 , pp. 2013-2029
    • Vicens, Q.1    Paukstelis, P.J.2    Westhof, E.3    Lambowitz, A.M.4    Cech, T.R.5
  • 72
    • 6044241907 scopus 로고    scopus 로고
    • Structural biology. Evolution of RNA architecture
    • Westhof E, Massire C. 2004. Structural biology. Evolution of RNA architecture. Science 306: 62-63.
    • (2004) Science , vol.306 , pp. 62-63
    • Westhof, E.1    Massire, C.2
  • 73
    • 20444496805 scopus 로고    scopus 로고
    • Structure and assembly of group I introns
    • DOI 10.1016/j.sbi.2005.05.007, PII S0959440X05000916
    • Woodson SA. 2005. Structure and assembly of group I introns. Curr Opin Struct Biol 15: 324-330. (Pubitemid 40826452)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.3 SPEC. ISS , pp. 324-330
    • Woodson, S.A.1
  • 74
    • 0027991626 scopus 로고
    • Kinetic intermediates in RNA folding
    • Zarrinkar P, Williamson J. 1994. Kinetic intermediates in RNA folding. Science 265: 918-924. (Pubitemid 24281488)
    • (1994) Science , vol.265 , Issue.5174 , pp. 918-924
    • Zarrinkar, P.P.1    Williamson, J.R.2
  • 75
    • 0024285808 scopus 로고
    • Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: Enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes
    • Zaug AJ, Grosshans CA, Cech TR. 1988. Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes. Biochemistry 27: 8924-8931.
    • (1988) Biochemistry , vol.27 , pp. 8924-8931
    • Zaug, A.J.1    Grosshans, C.A.2    Cech, T.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.