메뉴 건너뛰기




Volumn 45, Issue 3, 2012, Pages 345-381

Structure and mechanism of purine-binding riboswitches

Author keywords

[No Author keywords available]

Indexed keywords

PURINE DERIVATIVE;

EID: 84865231710     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583512000078     Document Type: Review
Times cited : (62)

References (170)
  • 1
    • 77955437093 scopus 로고    scopus 로고
    • A eubacterial riboswitch class that senses the coenzyme tetrahydrofolate
    • AMES, T. D., RODIONOV, D. A., WEINBERG, Z. & BREAKER, R. R. (2010). A eubacterial riboswitch class that senses the coenzyme tetrahydrofolate. Chemistry and Biology 17, 681-685.
    • (2010) Chemistry and Biology , vol.17 , pp. 681-685
    • Ames, T.D.1    Rodionov, D.A.2    Weinberg, Z.3    Breaker, R.R.4
  • 2
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • AMIKAM, D. & GALPERIN, M. Y. (2006). PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 22, 3-6.
    • (2006) Bioinformatics , vol.22 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 6
    • 46349083026 scopus 로고    scopus 로고
    • The distributions, mechanisms, and structures of metabolite-binding ri-boswitches
    • BARRICK, J. E. & BREAKER, R. R. (2007). The distributions, mechanisms, and structures of metabolite-binding ri-boswitches. Genome Biology 8, R239.
    • (2007) Genome Biology , vol.8
    • Barrick, J.E.1    Breaker, R.R.2
  • 8
    • 84855724406 scopus 로고    scopus 로고
    • Recognition of S-adenosylmethionine by riboswitches
    • BATEY, R. T. (2011). Recognition of S-adenosylmethionine by riboswitches. Wiley Interdisciplinary Reviews: RNA 2, 299-311.
    • (2011) Wiley Interdisciplinary Reviews: RNA , vol.2 , pp. 299-311
    • Batey, R.T.1
  • 9
    • 9244225713 scopus 로고    scopus 로고
    • Structure of a natural guanine-responsive riboswitch complexed with the metabolite hypoxanthine
    • BATEY, R. T., GILBERT, S. D. & MONTANGE, R. K. (2004). Structure of a natural guanine-responsive riboswitch complexed with the metabolite hypoxanthine. Nature 432, 411-415.
    • (2004) Nature , vol.432 , pp. 411-415
    • Batey, R.T.1    Gilbert, S.D.2    Montange, R.K.3
  • 12
    • 78650391868 scopus 로고    scopus 로고
    • Genetics: Revealing the dark matter of the genome
    • BLAXTER, M. (2010). Genetics: revealing the dark matter of the genome. Science 330, 1758-1759.
    • (2010) Science , vol.330 , pp. 1758-1759
    • Blaxter, M.1
  • 14
    • 33845700514 scopus 로고    scopus 로고
    • Riboswitches as antibacterial drug targets
    • BLOUNT, K. F. & BREAKER, R. R. (2006). Riboswitches as antibacterial drug targets. Nature Biotechnology 24, 1558-1564.
    • (2006) Nature Biotechnology , vol.24 , pp. 1558-1564
    • Blount, K.F.1    Breaker, R.R.2
  • 16
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomole-cular recognition
    • BOEHR, D. D., NUSSINOV, R. & WRIGHT, P. E. (2009). The role of dynamic conformational ensembles in biomole-cular recognition. Nature Chemical Biology 5, 789-796.
    • (2009) Nature Chemical Biology , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 17
    • 45849095234 scopus 로고    scopus 로고
    • Biochemistry. How do proteins interact?
    • BOEHR, D. D. & WRIGHT, P. E. (2008). Biochemistry. How do proteins interact? Science 320, 1429-1430.
    • (2008) Science , vol.320 , pp. 1429-1430
    • Boehr, D.D.1    Wright, P.E.2
  • 19
    • 80052973462 scopus 로고    scopus 로고
    • Prospects for riboswitch discovery and analysis
    • BREAKER, R. R. (2011). Prospects for riboswitch discovery and analysis. Molecular Cell 43, 867-879.
    • (2011) Molecular Cell , vol.43 , pp. 867-879
    • Breaker, R.R.1
  • 20
    • 77749304812 scopus 로고    scopus 로고
    • Multivector fluorescence analysis of the xpt guanine riboswitch aptamer domain and the conformational role of guanine
    • BRENNER, M. D., SCANLAN, M. S., NAHAS, M. K., HA, T. & SILVERMAN, S. K. (2010). Multivector fluorescence analysis of the xpt guanine riboswitch aptamer domain and the conformational role of guanine. Biochemistry 49, 1596-1605.
    • (2010) Biochemistry , vol.49 , pp. 1596-1605
    • Brenner, M.D.1    Scanlan, M.S.2    Nahas, M.K.3    Ha, T.4    Silverman, S.K.5
  • 23
    • 77952499429 scopus 로고    scopus 로고
    • Selecting RNA aptamers for synthetic biology: Investigating magnesium dependence and predicting binding affinity
    • CAROTHERS, J. M., GOLER, J. A., KAPOOR, Y., LARA, L. & KEASLING, J. D. (2010). Selecting RNA aptamers for synthetic biology: investigating magnesium dependence and predicting binding affinity. Nucleic Acids Research 38, 2736-2747.
    • (2010) Nucleic Acids Research , vol.38 , pp. 2736-2747
    • Carothers, J.M.1    Goler, J.A.2    Kapoor, Y.3    Lara, L.4    Keasling, J.D.5
  • 26
    • 0030894628 scopus 로고    scopus 로고
    • Xanthine metabolism in Bacillus subtilis: Characterization of the xpt-pbuX operon and evidence for purine-and nitrogen-controlled expression of genes involved in xanthine salvage and catabolism
    • CHRISTIANSEN, L.C., SCHOU, S., NYGAARD, P. & SAXILD, H. H. (1997). Xanthine metabolism in Bacillus subtilis: characterization of the xpt-pbuX operon and evidence for purine-and nitrogen-controlled expression of genes involved in xanthine salvage and catabolism. Journal of Bacteriology 179, 2540-2550.
    • (1997) Journal of Bacteriology , vol.179 , pp. 2540-2550
    • Christiansen, L.C.1    Schou, S.2    Nygaard, P.3    Saxild, H.H.4
  • 27
    • 0037146606 scopus 로고    scopus 로고
    • Breakthrough of the year. Small RNAs make big splash
    • COUZIN, J. (2002). Breakthrough of the year. Small RNAs make big splash. Science 298, 2296-2297.
    • (2002) Science , vol.298 , pp. 2296-2297
    • Couzin, J.1
  • 28
    • 0016169138 scopus 로고
    • The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNA
    • CROTHERS, D. M., COLE, P. E., HILBERS, C. W. & SHULMAN, R. G. (1974). The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNA. Journal of Molecular Biology 87, 63-88.
    • (1974) Journal of Molecular Biology , vol.87 , pp. 63-88
    • Crothers, D.M.1    Cole, P.E.2    Hilbers, C.W.3    Shulman, R.G.4
  • 30
    • 70350107533 scopus 로고    scopus 로고
    • Three-way RNA junctions with remote tertiary contacts: A recurrent and highly versatile fold
    • DE LA PENA, M., DUFOUR, D. & GALLEGO, J. (2009). Three-way RNA junctions with remote tertiary contacts: a recurrent and highly versatile fold. RNA 15, 1949-1964.
    • (2009) RNA , vol.15 , pp. 1949-1964
    • De La Pena, M.1    Dufour, D.2    Gallego, J.3
  • 31
    • 77957935381 scopus 로고    scopus 로고
    • CRISPR/Cas system and its role in phage-bacteria interactions
    • DEVEAU, H., GARNEAU, J. E. & MOINEAU, S. (2010). CRISPR/Cas system and its role in phage-bacteria interactions. Annual Review of Microbiology 64, 475-493.
    • (2010) Annual Review of Microbiology , vol.64 , pp. 475-493
    • Deveau, H.1    Garneau, J.E.2    Moineau, S.3
  • 34
    • 58149138753 scopus 로고    scopus 로고
    • A structural basis for the recognition of 2k-deoxyguanosine by the purine riboswitch
    • EDWARDS, A. L. & BATEY, R. T. (2009). A structural basis for the recognition of 2k-deoxyguanosine by the purine riboswitch. Journal of Molecular Biology 385, 938-948.
    • (2009) Journal of Molecular Biology , vol.385 , pp. 938-948
    • Edwards, A.L.1    Batey, R.T.2
  • 35
    • 84863405959 scopus 로고    scopus 로고
    • Unraveling the structural complexity in a single-stranded RNA tail: Implications for efficient ligand binding in the prequeuosine riboswitch
    • EICHHORN, C.D., FENG, J., SUDDALA, K.C., WALTER, N. G., BROOKS, C. L. III & AL-HASHIMI, H. M. (2012). Unraveling the structural complexity in a single-stranded RNA tail: implications for efficient ligand binding in the prequeuosine riboswitch. Nucleic Acids Research 40, 1345-1355.
    • (2012) Nucleic Acids Research , vol.40 , pp. 1345-1355
    • Eichhorn, C.D.1    Feng, J.2    Suddala, K.C.3    Walter, N.G.4    Brooks III, C.L.5    Al-Hashimi, H.M.6
  • 38
    • 72149126118 scopus 로고    scopus 로고
    • A switch in time: Detailing the life of a riboswitch
    • GARST, A. D. & BATEY, R. T. (2009). A switch in time: detailing the life of a riboswitch. Biochimica et Biophysica Acta 1789, 584-591.
    • (2009) Biochimica et Biophysica Acta , vol.1789 , pp. 584-591
    • Garst, A.D.1    Batey, R.T.2
  • 39
  • 41
    • 58449134534 scopus 로고    scopus 로고
    • Small silencing RNAs: An expanding universe. Nature Reviews
    • GHILDIYAL, M. & ZAMORE, P. D. (2009). Small silencing RNAs: an expanding universe. Nature Reviews. Genetics 10, 94-108.
    • (2009) Genetics , vol.10 , pp. 94-108
    • Ghildiyal, M.1    Zamore, P.D.2
  • 42
    • 36248982074 scopus 로고    scopus 로고
    • Mutational analysis of the purine ribo-switch aptamer domain
    • GILBERT, S.D., LOVE, C.E., EDWARDS, A.L. & BATEY, R. T. (2007). Mutational analysis of the purine ribo-switch aptamer domain. Biochemistry 46, 13297-13309.
    • (2007) Biochemistry , vol.46 , pp. 13297-13309
    • Gilbert, S.D.1    Love, C.E.2    Edwards, A.L.3    Batey, R.T.4
  • 45
    • 66349133602 scopus 로고    scopus 로고
    • Adaptive ligand binding by the purine riboswitch in the recognition of guanine and adenine analogs
    • GILBERT, S.D., REYES, F.E., EDWARDS, A.L. & BATEY, R. T. (2009). Adaptive ligand binding by the purine riboswitch in the recognition of guanine and adenine analogs. Structure 17, 857-868.
    • (2009) Structure , vol.17 , pp. 857-868
    • Gilbert, S.D.1    Reyes, F.E.2    Edwards, A.L.3    Batey, R.T.4
  • 46
    • 33646768226 scopus 로고    scopus 로고
    • Thermodynamic and kinetic characterization of ligand binding to the purine riboswitch apta-mer domain
    • GILBERT, S.D., STODDARD, C. D., WISE, S. J. & BATEY, R. T. (2006b). Thermodynamic and kinetic characterization of ligand binding to the purine riboswitch apta-mer domain. Journal of Molecular Biology 359, 754-768.
    • (2006) Journal of Molecular Biology , vol.359 , pp. 754-768
    • Gilbert, S.D.1    Stoddard, C.D.2    Wise, S.J.3    Batey, R.T.4
  • 47
    • 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. & 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
  • 48
    • 38849204944 scopus 로고    scopus 로고
    • Direct observation of hierarchical folding in single riboswitch aptamers
    • GREENLEAF, W., FRIEDA, K., FOSTER, D., WOODSIDE, M. & BLOCK, S. (2008a). Direct observation of hierarchical folding in single riboswitch aptamers. Science 319, 630.
    • (2008) Science , vol.319 , pp. 630
    • Greenleaf, W.1    Frieda, K.2    Foster, D.3    Woodside, M.4    Block, S.5
  • 49
    • 38849204944 scopus 로고    scopus 로고
    • Direct observation of hierarchical folding in single riboswitch aptamers
    • GREENLEAF, W.J., FRIEDA, K.L., FOSTER, D.A., WOODSIDE, M. T. & BLOCK, S. M. (2008b). Direct observation of hierarchical folding in single riboswitch aptamers. Science 319, 630-633.
    • (2008) Science , vol.319 , pp. 630-633
    • Greenleaf, W.J.1    Frieda, K.L.2    Foster, D.A.3    Woodside, M.T.4    Block, S.M.5
  • 52
    • 80052982281 scopus 로고    scopus 로고
    • The dynamic nature of RNA as key to understanding ribo-switch mechanisms
    • HALLER, A., SOULIERE, M. F. & MICURA, R. (2011b). The dynamic nature of RNA as key to understanding ribo-switch mechanisms. Accounts of Chemical Research 44, 1339-1348.
    • (2011) Accounts of Chemical Research , vol.44 , pp. 1339-1348
    • Haller, A.1    Souliere, M.F.2    Micura, R.3
  • 53
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • HENGGE, R. (2009). Principles of c-di-GMP signalling in bacteria. Nature Reviews Microbiology 7, 263-273.
    • (2009) Nature Reviews Microbiology , vol.7 , pp. 263-273
    • Hengge, R.1
  • 54
    • 38949114262 scopus 로고    scopus 로고
    • Folding of the SAM aptamer is determined by the formation of a K-turn-dependent pseudoknot
    • HEPPELL, B. & LAFONTAINE, D. A. (2008). Folding of the SAM aptamer is determined by the formation of a K-turn-dependent pseudoknot. Biochemistry 47, 1490-1499.
    • (2008) Biochemistry , vol.47 , pp. 1490-1499
    • Heppell, B.1    Lafontaine, D.A.2
  • 55
    • 48249125095 scopus 로고    scopus 로고
    • Structural principles from large RNAs
    • HOLBROOK, S. R. (2008). Structural principles from large RNAs. Annual Review of Biophysics 37, 445-464.
    • (2008) Annual Review of Biophysics , vol.37 , pp. 445-464
    • Holbrook, S.R.1
  • 57
    • 78649970557 scopus 로고    scopus 로고
    • Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch
    • HUANG, L., SERGANOV, A. & PATEL, D. J. (2010). Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch. Molecular Cell 40, 774-786.
    • (2010) Molecular Cell , vol.40 , pp. 774-786
    • Huang, L.1    Serganov, A.2    Patel, D.J.3
  • 58
    • 0344874269 scopus 로고    scopus 로고
    • Evolution of apta-mers with a new specificity and new secondary structures from an ATP aptamer
    • HUANG, Z. & SZOSTAK, J. W. (2003). Evolution of apta-mers with a new specificity and new secondary structures from an ATP aptamer. RNA 9, 1456-1463.
    • (2003) RNA , vol.9 , pp. 1456-1463
    • Huang, Z.1    Szostak, J.W.2
  • 61
    • 77951688391 scopus 로고    scopus 로고
    • Heterogeneity and dynamics of the ligand recognition mode in purine-sensing riboswitches
    • JAIN, N., ZHAO, L., LIU, J.D. & XIA, T. (2010). Heterogeneity and dynamics of the ligand recognition mode in purine-sensing riboswitches. Biochemistry 49, 3703-3714.
    • (2010) Biochemistry , vol.49 , pp. 3703-3714
    • Jain, N.1    Zhao, L.2    Liu, J.D.3    Xia, T.4
  • 62
    • 79960114180 scopus 로고    scopus 로고
    • Comparison of a preQ1 riboswitch aptamer in metabolite-bound and free states with implications for gene regulation
    • JENKINS, J. L., KRUCINSKA, J., MCCARTY, R. M., BANDARIAN, V. & WEDEKIND, J. E. (2011). Comparison of a preQ1 riboswitch aptamer in metabolite-bound and free states with implications for gene regulation. Journal of Biological Chemistry 286, 24626-24637.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 24626-24637
    • Jenkins, J.L.1    Krucinska, J.2    McCarty, R.M.3    Bandarian, V.4    Wedekind, J.E.5
  • 63
    • 0042890402 scopus 로고    scopus 로고
    • Definition of a second Bacillus subtilis pur regulon comprising the pur and xpt-pbuX operons plus pbu G, nupG (yxjA), and pbuE (ydhL)
    • JOHANSEN, L. E., NYGAARD, P., LASSEN, C., AGERSO, Y. & SAXILD, H. H. (2003). Definition of a second Bacillus subtilis pur regulon comprising the pur and xpt-pbuX operons plus pbu G, nupG (yxjA), and pbuE (ydhL). Journal of Bacteriology 185, 5200-5209.
    • (2003) Journal of Bacteriology , vol.185 , pp. 5200-5209
    • Johansen, L.E.1    Nygaard, P.2    Lassen, C.3    Agerso, Y.4    Saxild, H.H.5
  • 64
    • 62549154008 scopus 로고    scopus 로고
    • Structural insights into riboswitch control of the biosynthesis of queuosine, a modified nucleotide found in the antic-odon of tRNA
    • KANG, M., PETERSON, R. & FEIGON, J. (2009). Structural insights into riboswitch control of the biosynthesis of queuosine, a modified nucleotide found in the antic-odon of tRNA. Molecular Cell 33, 784-790.
    • (2009) Molecular Cell , vol.33 , pp. 784-790
    • Kang, M.1    Peterson, R.2    Feigon, J.3
  • 65
    • 73449116019 scopus 로고    scopus 로고
    • Design and antimicrobial action of purine analogues that bind Guanine ri-boswitches
    • KIM, J. N., BLOUNT, K. F., PUSKARZ, I., LIM, J., LINK, K. H. & BREAKER, R. R. (2009). Design and antimicrobial action of purine analogues that bind Guanine ri-boswitches. ACS Chemical Biology 4, 915-927.
    • (2009) ACS Chemical Biology , vol.4 , pp. 915-927
    • Kim, J.N.1    Blount, K.F.2    Puskarz, I.3    Lim, J.4    Link, K.H.5    Breaker, R.R.6
  • 67
    • 62049086072 scopus 로고    scopus 로고
    • Cocrystal structure of a class i preQ1 riboswitch reveals a pseudoknot recognizing an essential hyper-modified nucleobase
    • KLEIN, D.J., EDWARDS, T. E. & FERRE-D'AMARE, A. R. (2009). Cocrystal structure of a class I preQ1 riboswitch reveals a pseudoknot recognizing an essential hyper-modified nucleobase. Nature Structural and Molecular Biology 16, 343-344.
    • (2009) Nature Structural and Molecular Biology , vol.16 , pp. 343-344
    • Klein, D.J.1    Edwards, T.E.2    Ferre-D'Amare, A.R.3
  • 68
    • 33748325570 scopus 로고    scopus 로고
    • Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
    • KLEIN, D. J. & FERRE-D'AMARE, A. R. (2006). Structural basis of glmS ribozyme activation by glucosamine-6-phosphate. Science 313, 1752-1756.
    • (2006) Science , vol.313 , pp. 1752-1756
    • Klein, D.J.1    Ferre-D'Amare, A.R.2
  • 69
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: A new RNA secondary structure motif
    • KLEIN, D. J., SCHMEING, T. M., MOORE, P. B. & STEITZ, T. A. (2001). The kink-turn: a new RNA secondary structure motif. EMBO Journal 20, 4214-4221.
    • (2001) EMBO Journal , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 70
    • 71449123530 scopus 로고    scopus 로고
    • Recognition of the bacterial second messenger cyclic diguanylate by its cognate riboswitch
    • KULSHINA, N., BAIRD, N.J. & FERRE-D'AMARE, A.R. (2009). Recognition of the bacterial second messenger cyclic diguanylate by its cognate riboswitch. Nature Structural and Molecular Biology 16, 1212-1217.
    • (2009) Nature Structural and Molecular Biology , vol.16 , pp. 1212-1217
    • Kulshina, N.1    Baird, N.J.2    Ferre-D'Amare, A.R.3
  • 71
    • 0024041531 scopus 로고
    • Cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon
    • KURODA, M. I., HENNER, D. & YANOFSKY, C. (1988). cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon. Journal of Bacteriology 170, 3080-3088.
    • (1988) Journal of Bacteriology , vol.170 , pp. 3080-3088
    • Kuroda, M.I.1    Henner, D.2    Yanofsky, C.3
  • 72
    • 77955630859 scopus 로고    scopus 로고
    • An allosteric self-splicing ribo-zyme triggered by a bacterial second messenger
    • LEE, E. R., BAKER, J. L., WEINBERG, Z., SUDARSAN, N. & BREAKER, R. R. (2010a). An allosteric self-splicing ribo-zyme triggered by a bacterial second messenger. Science 329, 845-848.
    • (2010) Science , vol.329 , pp. 845-848
    • Lee, E.R.1    Baker, J.L.2    Weinberg, Z.3    Sudarsan, N.4    Breaker, R.R.5
  • 73
    • 85011936077 scopus 로고    scopus 로고
    • Roseoflavin is a natural antibacterial compound that binds to FMN riboswitches and regulates gene expression
    • LEE, E.R., BLOUNT, K. F. & BREAKER, R.R. (2009). Roseoflavin is a natural antibacterial compound that binds to FMN riboswitches and regulates gene expression. RNA Biology 6, 187-194.
    • (2009) RNA Biology , vol.6 , pp. 187-194
    • Lee, E.R.1    Blount, K.F.2    Breaker, R.R.3
  • 75
    • 79851499341 scopus 로고    scopus 로고
    • Comparative study between transcrip-tionally-and translationally-acting adenine riboswitches reveals key differences in riboswitch regulatory mechanisms
    • LEMAY, J.F., DESNOYERS, G., BLOUIN, S., HEPPELL, B., BASTET, L., ST-PIERRE, P., MASSE, E. & LAFONTAINE, D. A. (2011). Comparative study between transcrip-tionally-and translationally-acting adenine riboswitches reveals key differences in riboswitch regulatory mechanisms. PLoS Genetics 7, e1001278.
    • (2011) PLoS Genetics , vol.7
    • Lemay, J.F.1    Desnoyers, G.2    Blouin, S.3    Heppell, B.4    Bastet, L.5    St-Pierre, P.6    Masse, E.7    Lafontaine, D.A.8
  • 76
    • 33847308180 scopus 로고    scopus 로고
    • Core requirements of the adenine riboswitch aptamer for ligand binding
    • LEMAY, J. F. & LAFONTAINE, D. A. (2007). Core requirements of the adenine riboswitch aptamer for ligand binding. RNA 13, 339-350.
    • (2007) RNA , vol.13 , pp. 339-350
    • Lemay, J.F.1    Lafontaine, D.A.2
  • 79
    • 0032300804 scopus 로고    scopus 로고
    • Conserved geometrical base-pairing patterns in RNA
    • LEONTIS, N. B. & WESTHOF, E. (1998). Conserved geometrical base-pairing patterns in RNA. Quarterly Reviews of Biophysics 31, 399-455.
    • (1998) Quarterly Reviews of Biophysics , vol.31 , pp. 399-455
    • Leontis, N.B.1    Westhof, E.2
  • 80
    • 0035010211 scopus 로고    scopus 로고
    • Geometric nomenclature and classification of RNA base pairs
    • LEONTIS, N. B. & WESTHOF, E. (2001). Geometric nomenclature and classification of RNA base pairs. RNA 7, 499-512.
    • (2001) RNA , vol.7 , pp. 499-512
    • Leontis, N.B.1    Westhof, E.2
  • 81
    • 84865243362 scopus 로고    scopus 로고
    • Riboswitch structure in the ligand-free state. Wiley interdisciplinary reviews
    • LIBERMAN, J. A. & WEDEKIND, J. E. (2012). Riboswitch structure in the ligand-free state. Wiley interdisciplinary reviews. RNA 3, 369-384.
    • (2012) RNA , vol.3 , pp. 369-384
    • Liberman, J.A.1    Wedekind, J.E.2
  • 82
    • 44449150695 scopus 로고    scopus 로고
    • The dynamic structural basis of differential enhancement of conforma-tional stability by 5k-and 3k-dangling ends in RNA
    • LIU, J. D., ZHAO, L. & XIA, T. (2008). The dynamic structural basis of differential enhancement of conforma-tional stability by 5k-and 3k-dangling ends in RNA. Biochemistry 47, 5962-5975.
    • (2008) Biochemistry , vol.47 , pp. 5962-5975
    • Liu, J.D.1    Zhao, L.2    Xia, T.3
  • 83
    • 33645999355 scopus 로고    scopus 로고
    • S-adenosylmethionine: Jack of all trades and master of everything?
    • LOENEN, W. A. (2006). S-adenosylmethionine: jack of all trades and master of everything? Biochemical Society Transactions 34, 330-333.
    • (2006) Biochemical Society Transactions , vol.34 , pp. 330-333
    • Loenen, W.A.1
  • 84
    • 79958048297 scopus 로고    scopus 로고
    • Dynamic ensemble view of the con-formational landscape of HIV-1 TAR RNA and allosteric recognition
    • LU, J., KADAKKUZHA, B. M., ZHAO, L., FAN, M., QI, X. & XIA, T. (2011). Dynamic ensemble view of the con-formational landscape of HIV-1 TAR RNA and allosteric recognition. Biochemistry 50, 5042-5057.
    • (2011) Biochemistry , vol.50 , pp. 5042-5057
    • Lu, J.1    Kadakkuzha, B.M.2    Zhao, L.3    Fan, M.4    Qi, X.5    Xia, T.6
  • 85
    • 77649169870 scopus 로고    scopus 로고
    • MRNA secondary structures fold sequentially but exchange rapidly in vivo
    • MAHEN, E. M., WATSON, P. Y., COTTRELL, J. W. & FEDOR, M. J. (2010). mRNA secondary structures fold sequentially but exchange rapidly in vivo. PLoS Biology 8, e1000307.
    • (2010) PLoS Biology , vol.8
    • Mahen, E.M.1    Watson, P.Y.2    Cottrell, J.W.3    Fedor, M.J.4
  • 86
    • 0038210214 scopus 로고    scopus 로고
    • Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria
    • MANDAL, M., BOESE, B., BARRICK, J. E., WINKLER, W. C. & BREAKER, R. R. (2003). Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria. Cell 113, 577-586.
    • (2003) Cell , vol.113 , pp. 577-586
    • Mandal, M.1    Boese, B.2    Barrick, J.E.3    Winkler, W.C.4    Breaker, R.R.5
  • 87
    • 0842334528 scopus 로고    scopus 로고
    • Adenine ri-boswitches and gene activation by disruption of a transcription terminator
    • MANDAL, M. & BREAKER, R. R. (2004a). Adenine ri-boswitches and gene activation by disruption of a transcription terminator. Nature Structural and Molecular Biology 11, 29-35.
    • (2004) Nature Structural and Molecular Biology , vol.11 , pp. 29-35
    • Mandal, M.1    Breaker, R.R.2
  • 90
    • 16244412610 scopus 로고    scopus 로고
    • RNA structure analysis at single nucleotide resolution by selective 2k-hydroxyl acylation and primer extension (SHAPE)
    • MERINO, E.J., WILKINSON, K.A., COUGHLAN, J.L. & WEEKS, K. M. (2005). RNA structure analysis at single nucleotide resolution by selective 2k-hydroxyl acylation and primer extension (SHAPE). Journal of the American Chemical Society 127, 4223-4231.
    • (2005) Journal of the American Chemical Society , vol.127 , pp. 4223-4231
    • Merino, E.J.1    Wilkinson, K.A.2    Coughlan, J.L.3    Weeks, K.M.4
  • 91
    • 41649108068 scopus 로고    scopus 로고
    • Confirmation of a second natural preQ1 aptamer class in Streptococcaceae bacteria
    • MEYER, M. M., ROTH, A., CHERVIN, S. M., GARCIA, G. A. & BREAKER, R. R. (2008). Confirmation of a second natural preQ1 aptamer class in Streptococcaceae bacteria. RNA 14, 685-695.
    • (2008) RNA , vol.14 , pp. 685-695
    • Meyer, M.M.1    Roth, A.2    Chervin, S.M.3    Garcia, G.A.4    Breaker, R.R.5
  • 93
    • 33745628336 scopus 로고    scopus 로고
    • Structure of the S-adenosylmethionine riboswitch regulatory mRNA element
    • MONTANGE, R. K. & BATEY, R. T. (2006). Structure of the S-adenosylmethionine riboswitch regulatory mRNA element. Nature 441, 1172-1175.
    • (2006) Nature , vol.441 , pp. 1172-1175
    • Montange, R.K.1    Batey, R.T.2
  • 94
    • 2342475659 scopus 로고    scopus 로고
    • Molecular basis of box C/D RNA-protein interactions; Cocrystal structure of archaeal L7Ae and a box C/D RNA
    • MOORE, T., ZHANG, Y., FENLEY, M. O. & LI, H. (2004). Molecular basis of box C/D RNA-protein interactions; cocrystal structure of archaeal L7Ae and a box C/D RNA. Structure 12, 807-818.
    • (2004) Structure , vol.12 , pp. 807-818
    • Moore, T.1    Zhang, Y.2    Fenley, M.O.3    Li, H.4
  • 96
    • 34548726217 scopus 로고    scopus 로고
    • Ligand recognition determinants of guanine riboswitches
    • MULHBACHER, J. & LAFONTAINE, D. A. (2007). Ligand recognition determinants of guanine riboswitches. Nucleic Acids Research 35, 5568-5580.
    • (2007) Nucleic Acids Research , vol.35 , pp. 5568-5580
    • Mulhbacher, J.1    Lafontaine, D.A.2
  • 97
    • 0028301674 scopus 로고
    • GAAA tetraloop and conserved bulge stabilize tertiary structure of a group i intron domain
    • MURPHY, F. L. & CECH, T. R. (1994). GAAA tetraloop and conserved bulge stabilize tertiary structure of a group I intron domain. Journal of Molecular Biology 236, 49-63.
    • (1994) Journal of Molecular Biology , vol.236 , pp. 49-63
    • Murphy, F.L.1    Cech, T.R.2
  • 99
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • NEUMAN, K. C. & NAGY, A. (2008). Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nature Methods 5, 491-505.
    • (2008) Nature Methods , vol.5 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 100
    • 80053216036 scopus 로고    scopus 로고
    • Single-molecule force spec-troscopy of the add adenine riboswitch relates folding to regulatory mechanism
    • NEUPANE, K., YU, H., FOSTER, D.A., WANG, F. & WOODSIDE, M. T. (2011). Single-molecule force spec-troscopy of the add adenine riboswitch relates folding to regulatory mechanism. Nucleic Acids Research 39, 7677-7687.
    • (2011) Nucleic Acids Research , vol.39 , pp. 7677-7687
    • Neupane, K.1    Yu, H.2    Foster, D.A.3    Wang, F.4    Woodside, M.T.5
  • 102
    • 33846898497 scopus 로고    scopus 로고
    • Interplay of 'induced fit' and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch
    • NOESKE, J., BUCK, J., FURTIG, B., NASIRI, H. R., SCHWALBE, H. & WOHNERT, J. (2007). Interplay of 'induced fit' and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch. Nucleic Acids Research 35, 572-583.
    • (2007) Nucleic Acids Research , vol.35 , pp. 572-583
    • Noeske, J.1    Buck, J.2    Furtig, B.3    Nasiri, H.R.4    Schwalbe, H.5    Wohnert, J.6
  • 105
    • 67650474303 scopus 로고    scopus 로고
    • The RFN riboswitch of Bacillus subtilis is a target for the antibiotic roseoflavin produced by Streptomyces davawensis
    • OTT, E., STOLZ, J., LEHMANN, M. & MACK, M. (2009). The RFN riboswitch of Bacillus subtilis is a target for the antibiotic roseoflavin produced by Streptomyces davawensis. RNA Biology 6, 276-280.
    • (2009) RNA Biology , vol.6 , pp. 276-280
    • Ott, E.1    Stolz, J.2    Lehmann, M.3    MacK, M.4
  • 106
    • 36248984806 scopus 로고    scopus 로고
    • Ligand-induced folding of the guanine-sensing riboswitch is controlled by a combined predetermined induced fit mechanism
    • OTTINK, O. M., RAMPERSAD, S. M., TESSARI, M., ZAMAN, G. J., HEUS, H. A. & WIJMENGA, S. S. (2007). Ligand-induced folding of the guanine-sensing riboswitch is controlled by a combined predetermined induced fit mechanism. RNA 13, 2202-2212.
    • (2007) RNA , vol.13 , pp. 2202-2212
    • Ottink, O.M.1    Rampersad, S.M.2    Tessari, M.3    Zaman, G.J.4    Heus, H.A.5    Wijmenga, S.S.6
  • 108
    • 79960395328 scopus 로고    scopus 로고
    • Bacterial transcription terminators: The RNA 3k-end chronicles
    • PETERS, J. M., VANGELOFF, A. D. & LANDICK, R. (2011). Bacterial transcription terminators: the RNA 3k-end chronicles. Journal of Molecular Biology 412, 793-813.
    • (2011) Journal of Molecular Biology , vol.412 , pp. 793-813
    • Peters, J.M.1    Vangeloff, A.D.2    Landick, R.3
  • 109
    • 80052967464 scopus 로고    scopus 로고
    • Structural principles of nucleoside selectivity in a 2k-deoxyguanosine riboswitch
    • PIKOVSKAYA, O., POLONSKAIA, A., PATEL, D.J. & SERGANOV, A. (2011). Structural principles of nucleoside selectivity in a 2k-deoxyguanosine riboswitch. Nature Chemical Biology 7, 748-755.
    • (2011) Nature Chemical Biology , vol.7 , pp. 748-755
    • Pikovskaya, O.1    Polonskaia, A.2    Patel, D.J.3    Serganov, A.4
  • 110
    • 77951589688 scopus 로고    scopus 로고
    • Cooperation between translating ribosomes and RNA polymerase in transcription elongation
    • PROSHKIN, S., RAHMOUNI, A. R., MIRONOV, A. & NUDLER, E. (2010). Cooperation between translating ribosomes and RNA polymerase in transcription elongation. Science 328, 504-508.
    • (2010) Science , vol.328 , pp. 504-508
    • Proshkin, S.1    Rahmouni, A.R.2    Mironov, A.3    Nudler, E.4
  • 111
    • 70350149960 scopus 로고    scopus 로고
    • Sequence-dependent folding and unfolding of ligand-bound purine riboswitches
    • PRYCHYNA, O., DAHABIEH, M.S., CHAO, J. & O'NEILL, M. A. (2009). Sequence-dependent folding and unfolding of ligand-bound purine riboswitches. Biopolymers 91, 953-965.
    • (2009) Biopolymers , vol.91 , pp. 953-965
    • Prychyna, O.1    Dahabieh, M.S.2    Chao, J.3    O'Neill, M.A.4
  • 112
    • 60149091561 scopus 로고    scopus 로고
    • A stress-responsive RNA switch regulates VEGFA expression
    • RAY, P. S., JIA, J., YAO, P., MAJUMDER, M., HATZOGLOU, M. & FOX, P. L. (2009). A stress-responsive RNA switch regulates VEGFA expression. Nature 457, 915-919.
    • (2009) Nature , vol.457 , pp. 915-919
    • Ray, P.S.1    Jia, J.2    Yao, P.3    Majumder, M.4    Hatzoglou, M.5    Fox, P.L.6
  • 114
    • 42549108780 scopus 로고    scopus 로고
    • A widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolism
    • REGULSKI, E. E., MOY, R. H., WEINBERG, Z., BARRICK, J. E., YAO, Z., RUZZO, W. L. & BREAKER, R. R. (2008). A widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolism. Molecular Microbiology 68, 918-932.
    • (2008) Molecular Microbiology , vol.68 , pp. 918-932
    • Regulski, E.E.1    Moy, R.H.2    Weinberg, Z.3    Barrick, J.E.4    Yao, Z.5    Ruzzo, W.L.6    Breaker, R.R.7
  • 115
    • 34447548824 scopus 로고    scopus 로고
    • Ligand-induced folding of the adenosine deaminase A-riboswitch and implications on riboswitch translational control. Chembiochem
    • RIEDER, R., LANG, K., GRABER, D. & MICURA, R. (2007). Ligand-induced folding of the adenosine deaminase A-riboswitch and implications on riboswitch translational control. Chembiochem: A European Journal of Chemical Biology 8, 896-902.
    • (2007) A European Journal of Chemical Biology , vol.8 , pp. 896-902
    • Rieder, R.1    Lang, K.2    Graber, D.3    Micura, R.4
  • 119
    • 33750044865 scopus 로고    scopus 로고
    • The PilZ domain is a receptor for the second messenger c-di-GMP: The PilZ domain protein YcgR controls motility in enterobacteria
    • RYJENKOV, D. A., SIMM, R., ROMLING, U. & GOMELSKY, M. (2006). The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ domain protein YcgR controls motility in enterobacteria. Journal of Biological Chemistry 281, 30310-30314.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 30310-30314
    • Ryjenkov, D.A.1    Simm, R.2    Romling, U.3    Gomelsky, M.4
  • 120
    • 2942631408 scopus 로고    scopus 로고
    • The tyranny of adenosine recognition among RNA aptamers to coenzyme A
    • SARAN, D., FRANK, J. & BURKE, D. H. (2003). The tyranny of adenosine recognition among RNA aptamers to coenzyme A. BMC Evolutionary Biology 3, 26.
    • (2003) BMC Evolutionary Biology , vol.3 , pp. 26
    • Saran, D.1    Frank, J.2    Burke, D.H.3
  • 121
    • 0027180473 scopus 로고
    • An RNA motif that binds ATP
    • SASSANFAR, M. & SZOSTAK, J. W. (1993). An RNA motif that binds ATP. Nature 364, 550-553.
    • (1993) Nature , vol.364 , pp. 550-553
    • Sassanfar, M.1    Szostak, J.W.2
  • 122
    • 0035684981 scopus 로고    scopus 로고
    • Definition of the Bacillus subtilis PurR operator using genetic and bioinformatic tools and expansion of the PurR regulon with gly A, gua C, pbu G, xpt-pbu X, yqhZ-fol D, and pbuO
    • SAXILD, H. H., BRUNSTEDT, K., NIELSEN, K. I., JARMER, H. & NYGAARD, P. (2001). Definition of the Bacillus subtilis PurR operator using genetic and bioinformatic tools and expansion of the PurR regulon with gly A, gua C, pbu G, xpt-pbu X, yqhZ-fol D, and pbuO. Journal of Bacteriology 183, 6175-6183.
    • (2001) Journal of Bacteriology , vol.183 , pp. 6175-6183
    • Saxild, H.H.1    Brunstedt, K.2    Nielsen, K.I.3    Jarmer, H.4    Nygaard, P.5
  • 123
    • 3142758746 scopus 로고    scopus 로고
    • A small aptamer with strong and specific recognition of the triphosphate of ATP
    • SAZANI, P. L., LARRALDE, R. & SZOSTAK, J. W. (2004). A small aptamer with strong and specific recognition of the triphosphate of ATP. Journal of the American Chemical Society 126, 8370-8371.
    • (2004) Journal of the American Chemical Society , vol.126 , pp. 8370-8371
    • Sazani, P.L.1    Larralde, R.2    Szostak, J.W.3
  • 124
    • 8444229753 scopus 로고    scopus 로고
    • Strategies for RNA folding and assembly. Nature Reviews
    • SCHROEDER, R., BARTA, A. & SEMRAD, K. (2004). Strategies for RNA folding and assembly. Nature Reviews. Molecular Cell Biology 5, 908-919.
    • (2004) Molecular Cell Biology , vol.5 , pp. 908-919
    • Schroeder, R.1    Barta, A.2    Semrad, K.3
  • 128
    • 0022570121 scopus 로고
    • Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon
    • SHIMOTSU, H., KURODA, M. I., YANOFSKY, C. & HENNER, D. J. (1986). Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon. Journal of Bacteriology 166, 461-471.
    • (1986) Journal of Bacteriology , vol.166 , pp. 461-471
    • Shimotsu, H.1    Kuroda, M.I.2    Yanofsky, C.3    Henner, D.J.4
  • 129
    • 0037377340 scopus 로고    scopus 로고
    • Rube Goldberg goes (ribo)-nuclear? Molecular switches and sensors made from RNA
    • SILVERMAN, S. K. (2003). Rube Goldberg goes (ribo)-nuclear? Molecular switches and sensors made from RNA. RNA 9, 377-383.
    • (2003) RNA , vol.9 , pp. 377-383
    • Silverman, S.K.1
  • 130
    • 77952507419 scopus 로고    scopus 로고
    • Reprogramming bacteria to seek and destroy an herbicide
    • SINHA, J., REYES, S.J. & GALLIVAN, J.P. (2010). Reprogramming bacteria to seek and destroy an herbicide. Nature Chemical Biology 6, 464-470.
    • (2010) Nature Chemical Biology , vol.6 , pp. 464-470
    • Sinha, J.1    Reyes, S.J.2    Gallivan, J.P.3
  • 131
    • 79957467767 scopus 로고    scopus 로고
    • From SELEX to cell dual selections for synthetic riboswitches
    • SINHA, J., TOPP, S. & GALLIVAN, J. P. (2011). From SELEX to cell dual selections for synthetic riboswitches. Methods in Enzymology 497, 207-220.
    • (2011) Methods in Enzymology , vol.497 , pp. 207-220
    • Sinha, J.1    Topp, S.2    Gallivan, J.P.3
  • 133
    • 77956021842 scopus 로고    scopus 로고
    • Structural and biochemical determinants of ligand binding by the c-di-GMP riboswitch
    • SMITH, K.D., LIPCHOCK, S.V., LIVINGSTON, A.L., SHANAHAN, C. A. & STROBEL, S. A. (2010). Structural and biochemical determinants of ligand binding by the c-di-GMP riboswitch. Biochemistry 49, 7351-7359.
    • (2010) Biochemistry , vol.49 , pp. 7351-7359
    • Smith, K.D.1    Lipchock, S.V.2    Livingston, A.L.3    Shanahan, C.A.4    Strobel, S.A.5
  • 135
    • 80053542128 scopus 로고    scopus 로고
    • A powerful approach for the selection of 2-aminopurine substitution sites to investigate RNA folding
    • SOULIERE, M.F., HALLER, A., RIEDER, R. & MICURA, R. (2011). A powerful approach for the selection of 2-aminopurine substitution sites to investigate RNA folding. Journal of the American Chemical Society 133, 16161-16167.
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 16161-16167
    • Souliere, M.F.1    Haller, A.2    Rieder, R.3    Micura, R.4
  • 136
    • 66449089224 scopus 로고    scopus 로고
    • The structural basis for recognition of the PreQ0 metabolite by an unusually small riboswitch aptamer domain
    • SPITALE, R. C., TORELLI, A. T., KRUCINSKA, J., BANDARIAN, V. & WEDEKIND, J. E. (2009). The structural basis for recognition of the PreQ0 metabolite by an unusually small riboswitch aptamer domain. Journal of Biological Chemistry 284, 11012-11016.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 11012-11016
    • Spitale, R.C.1    Torelli, A.T.2    Krucinska, J.3    Bandarian, V.4    Wedekind, J.E.5
  • 137
    • 22744455135 scopus 로고    scopus 로고
    • Pseudoknots: RNA structures with diverse functions
    • STAPLE, D. W. & BUTCHER, S. E. (2005). Pseudoknots: RNA structures with diverse functions. PLoS Biology 3, e213.
    • (2005) PLoS Biology , vol.3
    • Staple, D.W.1    Butcher, S.E.2
  • 139
    • 41649108293 scopus 로고    scopus 로고
    • Ligand-dependent folding of the three-way junction in the purine riboswitch
    • STODDARD, C. D., GILBERT, S. D. & BATEY, R. T. (2008). Ligand-dependent folding of the three-way junction in the purine riboswitch. RNA 14, 675-684.
    • (2008) RNA , vol.14 , pp. 675-684
    • Stoddard, C.D.1    Gilbert, S.D.2    Batey, R.T.3
  • 141
    • 80053019485 scopus 로고    scopus 로고
    • Regulation by small RNAs in bacteria: Expanding frontiers
    • STORZ, G., VOGEL, J. & WASSARMAN, K.M. (2011). Regulation by Small RNAs in Bacteria: expanding Frontiers. Molecular Cell 43, 880-891.
    • (2011) Molecular Cell , vol.43 , pp. 880-891
    • Storz, G.1    Vogel, J.2    Wassarman, K.M.3
  • 144
    • 43149103943 scopus 로고    scopus 로고
    • Targeting RNA with small molecules
    • THOMAS, J. R. & HERGENROTHER, P. J. (2008). Targeting RNA with small molecules. Chemical Reviews 108, 1171-1224.
    • (2008) Chemical Reviews , vol.108 , pp. 1171-1224
    • Thomas, J.R.1    Hergenrother, P.J.2
  • 145
    • 38649086717 scopus 로고    scopus 로고
    • Natural variability in S-adenosylmethio-nine (SAM)-dependent riboswitches: S-box elements in Bacillus subtilis exhibit differential sensitivity to SAM in vivo and in vitro
    • TOMSIC, J., MCDANIEL, B.A., GRUNDY, F. J. & HENKIN, T. M. (2008). Natural variability in S-adenosylmethio-nine (SAM)-dependent riboswitches: S-box elements in Bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro. Journal of Bacteriology 190, 823-833.
    • (2008) Journal of Bacteriology , vol.190 , pp. 823-833
    • Tomsic, J.1    McDaniel, B.A.2    Grundy, F.J.3    Henkin, T.M.4
  • 146
    • 80054074740 scopus 로고    scopus 로고
    • The structure of a tetrahydrofolate-sensing riboswitch reveals two ligand binding sites in a single aptamer
    • TRAUSCH, J.J., CERES, P., REYES, F. E. & BATEY, R. T. (2011). The structure of a tetrahydrofolate-sensing riboswitch reveals two ligand binding sites in a single aptamer. Structure 19, 1413-1423.
    • (2011) Structure , vol.19 , pp. 1413-1423
    • Trausch, J.J.1    Ceres, P.2    Reyes, F.E.3    Batey, R.T.4
  • 147
    • 44949214942 scopus 로고    scopus 로고
    • Regulation of pyrimidine biosynthetic gene expression in bacteria: Repression without repressors
    • TURNBOUGH, C. L., Jr. & SWITZER, R. L. (2008). Regulation of pyrimidine biosynthetic gene expression in bacteria: repression without repressors. Microbiology and Molecular Biology Reviews: MMBR 72, 266-300.
    • (2008) Microbiology and Molecular Biology Reviews: MMBR , vol.72 , pp. 266-300
    • Turnbough, Jr.C.L.1    Switzer, R.L.2
  • 148
    • 30944458838 scopus 로고    scopus 로고
    • Atomic level architecture of group i introns revealed
    • VICENS, Q. & CECH, T. R. (2006). Atomic level architecture of group I introns revealed. Trends in Biochemical Sciences 31, 41-51.
    • (2006) Trends in Biochemical Sciences , vol.31 , pp. 41-51
    • Vicens, Q.1    Cech, T.R.2
  • 149
    • 80455178803 scopus 로고    scopus 로고
    • Molecular sensing by the aptamer domain of the FMN riboswitch: A general model for ligand binding by con-formational selection
    • VICENS, Q., MONDRAGON, E. & BATEY, R.T. (2011). Molecular sensing by the aptamer domain of the FMN riboswitch: a general model for ligand binding by con-formational selection. Nucleic Acids Research.
    • (2011) Nucleic Acids Research
    • Vicens, Q.1    Mondragon, E.2    Batey, R.T.3
  • 150
    • 75649124956 scopus 로고    scopus 로고
    • Queuosine modification of tRNA: Its divergent role in cellular machinery
    • VINAYAK, M. & PATHAK, C. (2010). Queuosine modification of tRNA: its divergent role in cellular machinery. Bioscience Reports 30, 135-148.
    • (2010) Bioscience Reports , vol.30 , pp. 135-148
    • Vinayak, M.1    Pathak, C.2
  • 151
  • 153
    • 80053045739 scopus 로고    scopus 로고
    • Molecular mechanisms of long noncoding RNAs
    • WANG, K. C. & CHANG, H. Y. (2011). Molecular mechanisms of long noncoding RNAs. Molecular cell 43, 904-914.
    • (2011) Molecular Cell , vol.43 , pp. 904-914
    • Wang, K.C.1    Chang, H.Y.2
  • 154
    • 79960611669 scopus 로고    scopus 로고
    • Exploring RNA structural codes with SHAPE chemistry
    • WEEKS, K. M. & MAUGER, D. M. (2011). Exploring RNA Structural Codes with SHAPE Chemistry. Accounts of Chemical Research 44, 1280-1291.
    • (2011) Accounts of Chemical Research , vol.44 , pp. 1280-1291
    • Weeks, K.M.1    Mauger, D.M.2
  • 155
    • 4844227634 scopus 로고    scopus 로고
    • Selection and evolution of NTP-specific aptamers
    • WEILL, L., LOUIS, D. & SARGUEIL, B. (2004). Selection and evolution of NTP-specific aptamers. Nucleic Acids Research 32, 5045-5058.
    • (2004) Nucleic Acids Research , vol.32 , pp. 5045-5058
    • Weill, L.1    Louis, D.2    Sargueil, B.3
  • 157
    • 77951606278 scopus 로고    scopus 로고
    • Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea, and their metagenomes
    • WEINBERG, Z., WANG, J. X., BOGUE, J., YANG, J., CORBINO, K., MOY, R. H. & BREAKER, R. R. (2010). Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea, and their metagenomes. Genome Biology 11, R31.
    • (2010) Genome Biology , vol.11
    • Weinberg, Z.1    Wang, J.X.2    Bogue, J.3    Yang, J.4    Corbino, K.5    Moy, R.H.6    Breaker, R.R.7
  • 158
    • 26444620938 scopus 로고    scopus 로고
    • The kinetics of ligand binding by an adenine-sensing riboswitch
    • WICKISER, J.K., CHEAH, M.T., BREAKER, R.R. & CROTHERS, D. M. (2005a). The kinetics of ligand binding by an adenine-sensing riboswitch. Biochemistry 44, 13404-13414.
    • (2005) Biochemistry , vol.44 , pp. 13404-13414
    • Wickiser, J.K.1    Cheah, M.T.2    Breaker, R.R.3    Crothers, D.M.4
  • 159
    • 15944382675 scopus 로고    scopus 로고
    • The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch
    • WICKISER, J.K., WINKLER, W.C., BREAKER, R.R. & CROTHERS, D. M. (2005b). The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch. Molecular Cell 18, 49-60.
    • (2005) Molecular Cell , vol.18 , pp. 49-60
    • Wickiser, J.K.1    Winkler, W.C.2    Breaker, R.R.3    Crothers, D.M.4
  • 160
    • 16344370497 scopus 로고    scopus 로고
    • RNA SHAPE chemistry reveals nonhierarchical interactions dominate equilibrium structural transitions in tRNA(Asp) transcripts
    • WILKINSON, K. A., MERINO, E. J. & WEEKS, K. M. (2005). RNA SHAPE chemistry reveals nonhierarchical interactions dominate equilibrium structural transitions in tRNA(Asp) transcripts. Journal of the American Chemical Society 127, 4659-4667.
    • (2005) Journal of the American Chemical Society , vol.127 , pp. 4659-4667
    • Wilkinson, K.A.1    Merino, E.J.2    Weeks, K.M.3
  • 161
    • 33947720028 scopus 로고    scopus 로고
    • Selective 2k-hydroxyl acylation analyzed by primer extension (SHAPE): Quantitative RNA structure analysis at single nucleotide resolution
    • WILKINSON, K. A., MERINO, E. J. & WEEKS, K. M. (2006). Selective 2k-hydroxyl acylation analyzed by primer extension (SHAPE): quantitative RNA structure analysis at single nucleotide resolution. Nature Protocols 1, 1610-1616.
    • (2006) Nature Protocols , vol.1 , pp. 1610-1616
    • Wilkinson, K.A.1    Merino, E.J.2    Weeks, K.M.3
  • 162
    • 0142075327 scopus 로고    scopus 로고
    • Genetic control by metabolite-binding riboswitches. Chembiochem
    • WINKLER, W. C. & BREAKER, R. R. (2003). Genetic control by metabolite-binding riboswitches. Chembiochem: A European Journal of Chemical Biology 4, 1024-1032.
    • (2003) A European Journal of Chemical Biology , vol.4 , pp. 1024-1032
    • Winkler, W.C.1    Breaker, R.R.2
  • 163
    • 0034897731 scopus 로고    scopus 로고
    • The GA motif: An RNA element common to bacterial antitermination systems, r RNA, and eu-karyotic RNAs
    • WINKLER, W. C., GRUNDY, F. J., MURPHY, B. A. & HENKIN, T. M. (2001). The GA motif: an RNA element common to bacterial antitermination systems, r RNA, and eu-karyotic RNAs. RNA 7, 1165-1172.
    • (2001) RNA , vol.7 , pp. 1165-1172
    • Winkler, W.C.1    Grundy, F.J.2    Murphy, B.A.3    Henkin, T.M.4
  • 166
    • 79961096926 scopus 로고    scopus 로고
    • Getting past the RNA world: The initial Darwinian ancestor
    • YARUS, M. (2011). Getting past the RNA world: the initial Darwinian ancestor. Cold Spring Harbor Perspectives in Biology 3, a003590.
    • (2011) Cold Spring Harbor Perspectives in Biology , vol.3
    • Yarus, M.1
  • 167
    • 78751662374 scopus 로고    scopus 로고
    • RNA folding in living cells
    • ZEMORA, G. & WALDSICH, C. (2010). RNA folding in living cells. RNA Biology 7, 634-641.
    • (2010) RNA Biology , vol.7 , pp. 634-641
    • Zemora, G.1    Waldsich, C.2
  • 168
    • 78049276834 scopus 로고    scopus 로고
    • Ribozymes and riboswitches: Modulation of RNA function by small molecules
    • ZHANG, J., LAU, M. W. & FERRE-D'AMARE, A. R. (2010). Ribozymes and riboswitches: modulation of RNA function by small molecules. Biochemistry 49, 9123-9131.
    • (2010) Biochemistry , vol.49 , pp. 9123-9131
    • Zhang, J.1    Lau, M.W.2    Ferre-D'Amare, A.R.3
  • 169
    • 34247159140 scopus 로고    scopus 로고
    • Direct revelation of multiple conformations in RNA by femtosecond dynamics
    • ZHAO, L. & XIA, T. (2007). Direct revelation of multiple conformations in RNA by femtosecond dynamics. Journal of the American Chemical Society 129, 4118-4119.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 4118-4119
    • Zhao, L.1    Xia, T.2
  • 170
    • 70349279950 scopus 로고    scopus 로고
    • Probing RNA conformational dynamics and heterogeneity using femtosecond time-resolved fluorescence spectroscopy
    • ZHAO, L. & XIA, T. (2009). Probing RNA conformational dynamics and heterogeneity using femtosecond time-resolved fluorescence spectroscopy. Methods 49, 128-135.
    • (2009) Methods , vol.49 , pp. 128-135
    • Zhao, L.1    Xia, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.