메뉴 건너뛰기




Volumn 102, Issue 3, 2012, Pages

Chain length determines the folding rates of RNA

Author keywords

[No Author keywords available]

Indexed keywords

RNA;

EID: 84856710189     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.01.003     Document Type: Article
Times cited : (40)

References (29)
  • 1
    • 16344371778 scopus 로고    scopus 로고
    • RNA and protein folding: Common themes and variations
    • DOI 10.1021/bi047314+
    • D. Thirumalai, and C. Hyeon RNA and protein folding: common themes and variations Biochemistry 44 2005 4957 4970 (Pubitemid 40471212)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 4957-4970
    • Thirumalai, D.1    Hyeon, C.2
  • 3
    • 77952896659 scopus 로고    scopus 로고
    • Compact intermediates in RNA folding
    • S.A. Woodson Compact intermediates in RNA folding Annu. Rev. Biophys. 39 2010 61 77
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 61-77
    • Woodson, S.A.1
  • 4
    • 33845328453 scopus 로고    scopus 로고
    • Size, shape, and flexibility of RNA structures
    • C. Hyeon, R.I. Dima, and D. Thirumalai Size, shape, and flexibility of RNA structures J. Chem. Phys. 125 2006 194905
    • (2006) J. Chem. Phys. , vol.125 , pp. 194905
    • Hyeon, C.1    Dima, R.I.2    Thirumalai, D.3
  • 6
    • 77953648210 scopus 로고    scopus 로고
    • On the significance of an RNA tertiary structure prediction
    • C.E. Hajdin, and F. Ding K.M. Weeks On the significance of an RNA tertiary structure prediction RNA 16 2010 1340 1349
    • (2010) RNA , vol.16 , pp. 1340-1349
    • Hajdin, C.E.1    Ding, F.2    Weeks, K.M.3
  • 7
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding kinetics
    • D. Thirumalai From minimal models to real proteins: time scales for protein folding kinetics J. Phys. 5 1995 1457 1467
    • (1995) J. Phys. , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 8
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
    • Z. Guo, and D. Thirumalai Kinetics of protein folding: nucleation mechanism, time scales, and pathways Biopolymers 36 1995 83 102
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 9
    • 0031576334 scopus 로고    scopus 로고
    • Folding of RNA involves parallel pathways
    • DOI 10.1006/jmbi.1997.1311
    • J. Pan, D. Thirumalai, and S.A. Woodson Folding of RNA involves parallel pathways J. Mol. Biol. 273 1997 7 13 (Pubitemid 27460208)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 7-13
    • Pan, J.1    Thirumalai, D.2    Woodson, S.A.3
  • 11
    • 0015846852 scopus 로고
    • Thermodynamics and kinetics of the helix-coil transition of oligomers containing GC base pairs
    • D. Pörschke, O. Uhlenbeck, and F. Martin Thermodynamics and kinetics of the helix-coil transition of oligomers containing GC base pairs Biopolymers 12 1973 1313 1335
    • (1973) Biopolymers , vol.12 , pp. 1313-1335
    • Pörschke, D.1    Uhlenbeck, O.2    Martin, F.3
  • 13
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • DOI 10.1038/nature01609
    • W.Y. Yang, and M. Gruebele Folding at the speed limit Nature 423 2003 193 197 (Pubitemid 36569545)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 16
    • 8344253719 scopus 로고    scopus 로고
    • Folding thermodynamics and kinetics of YNMG RNA hairpins: Specific incorporation of 8-bromoguanosine leads to stabilization by enhancement of the folding rate
    • DOI 10.1021/bi048213e
    • D.J. Proctor, and H. Ma P.C. Bevilacqua Folding thermodynamics and kinetics of YNMG RNA hairpins: specific incorporation of 8-bromoguanosine leads to stabilization by enhancement of the folding rate Biochemistry 43 2004 14004 14014 (Pubitemid 39482750)
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14004-14014
    • Proctor, D.J.1    Ma, H.2    Kierzek, E.3    Kierzek, R.4    Gruebele, M.5    Bevilacqua, P.C.6
  • 17
    • 0016257808 scopus 로고
    • Thermodynamic and kinetic parameters of an oligonucleotide hairpin helix
    • D. Porschke Thermodynamic and kinetic parameters of an oligonucleotide hairpin helix Biophys. Chem. 1 1974 381 386
    • (1974) Biophys. Chem. , vol.1 , pp. 381-386
    • Porschke, D.1
  • 18
    • 0000977766 scopus 로고
    • Thermodynamics and kinetics of conformational transitions in oligonucleotides and tRNA
    • J. Duchesne, Academic Press London
    • D. Riesner, and R. Römer Thermodynamics and kinetics of conformational transitions in oligonucleotides and tRNA J. Duchesne, Physico-Chemical Properties of Nucleic Acids Vol. 2 1973 Academic Press London 237 318
    • (1973) Physico-Chemical Properties of Nucleic Acids , vol.2 , pp. 237-318
    • Riesner, D.1    Römer, R.2
  • 20
    • 40249094662 scopus 로고    scopus 로고
    • Loop dependence of the stability and dynamics of nucleic acid hairpins
    • DOI 10.1093/nar/gkm1083
    • S.V. Kuznetsov, and C.C. Ren A. Ansari Loop dependence of the stability and dynamics of nucleic acid hairpins Nucleic Acids Res. 36 2008 1098 1112 (Pubitemid 351330928)
    • (2008) Nucleic Acids Research , vol.36 , Issue.4 , pp. 1098-1112
    • Kuznetsov, S.V.1    Ren, C.-C.2    Woodson, S.A.3    Ansari, A.4
  • 21
    • 83055179382 scopus 로고    scopus 로고
    • Fast folding of RNA pseudoknots initiated by laser temperature-jump
    • R. Narayanan, and Y. Velmurugu A. Ansari Fast folding of RNA pseudoknots initiated by laser temperature-jump J. Am. Chem. Soc. 133 2011 18767 18774
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18767-18774
    • Narayanan, R.1    Velmurugu, Y.2    Ansari, A.3
  • 23
    • 4444363049 scopus 로고    scopus 로고
    • Reduced contact order and RNA folding rates
    • DOI 10.1016/j.jmb.2004.08.002, PII S0022283604009684
    • T.R. Sosnick, and T. Pan Reduced contact order and RNA folding rates J. Mol. Biol. 342 2004 1359 1365 (Pubitemid 39208664)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.5 , pp. 1359-1365
    • Sosnick, T.R.1    Pan, T.2
  • 24
    • 0034641668 scopus 로고    scopus 로고
    • Folding mechanism of the Tetrahymena ribozyme P4-P6 domain
    • M.L. Deras, and M. Brenowitz S.A. Woodson Folding mechanism of the Tetrahymena ribozyme P4-P6 domain Biochemistry 39 2000 10975 10985
    • (2000) Biochemistry , vol.39 , pp. 10975-10985
    • Deras, M.L.1    Brenowitz, M.2    Woodson, S.A.3
  • 26
    • 0032590020 scopus 로고    scopus 로고
    • Mg-dependent folding of a large ribozyme without kinetic traps
    • X. Fang, T. Pan, and T.R. Sosnick Mg-dependent folding of a large ribozyme without kinetic traps Nat. Struct. Biol. 12 1999 1091 1095
    • (1999) Nat. Struct. Biol. , vol.12 , pp. 1091-1095
    • Fang, X.1    Pan, T.2    Sosnick, T.R.3
  • 27
    • 0242317691 scopus 로고    scopus 로고
    • Concerted folding of a Candida ribozyme into the catalytically active structure posterior to a rapid RNA compaction
    • DOI 10.1093/nar/gkg455
    • M. Xiao, M.J. Leibowitz, and Y. Zhang Concerted folding of a Candida ribozyme into the catalytically active structure posterior to a rapid RNA compaction Nucleic Acids Res. 31 2003 3901 3908 (Pubitemid 37442269)
    • (2003) Nucleic Acids Research , vol.31 , Issue.14 , pp. 3901-3908
    • Xiao, M.1    Leibowitz, M.J.2    Zhang, Y.3
  • 28
    • 0029958503 scopus 로고    scopus 로고
    • Slow folding kinetics of RNase P RNA
    • P.P. Zarrinkar, J. Wang, and J.R. Williamson Slow folding kinetics of RNase P RNA RNA 2 1996 564 573 (Pubitemid 26374228)
    • (1996) RNA , vol.2 , Issue.6 , pp. 564-573
    • Zarrinkar, P.P.1    Wang, J.2    Williamson, J.R.3
  • 29
    • 0032549780 scopus 로고    scopus 로고
    • RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting
    • DOI 10.1126/science.279.5358.1940
    • B. Sclavi, and M. Sullivan S.A. Woodson RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting Science 279 1998 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.