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Volumn 118, Issue 14, 2014, Pages 3853-3863

Erratum: Single-molecule fluorescence resonance energy transfer studies of the human telomerase RNA pseudoknot: Temperature-/Urea-dependent folding kinetics and thermodynamics (Journal of Physical Chemistry B (2014) 118:14 (3853-3863) DOI: 10.1021/jp501893c);Single-molecule fluorescence resonance energy transfer studies of the human telomerase RNA pseudoknot: Temperature-/urea-dependent folding kinetics and thermodynamics

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENERGY TRANSFER; EQUILIBRIUM CONSTANTS; FORSTER RESONANCE ENERGY TRANSFER; FREE ENERGY; KINETIC ENERGY; METABOLISM; NUCLEIC ACIDS; RNA; UREA;

EID: 84898427603     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp504558u     Document Type: Erratum
Times cited : (20)

References (57)
  • 1
    • 0031561327 scopus 로고    scopus 로고
    • The End-Replication Problem
    • Wynford-Thomas, D.; Kipling, D. The End-Replication Problem Nature 1997, 389, 551-551
    • (1997) Nature , vol.389 , pp. 551-551
    • Wynford-Thomas, D.1    Kipling, D.2
  • 2
    • 0035929353 scopus 로고    scopus 로고
    • Switching and Signaling at the Telomere
    • Blackburn, E. H. Switching and Signaling at the Telomere Cell 2001, 106, 661-673
    • (2001) Cell , vol.106 , pp. 661-673
    • Blackburn, E.H.1
  • 3
    • 0033788565 scopus 로고    scopus 로고
    • The End of the (DNA) Line
    • Blackburn, E. H. The End of the (DNA) Line Nat. Struct. Biol. 2000, 7, 847-850
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 847-850
    • Blackburn, E.H.1
  • 4
    • 2142825133 scopus 로고    scopus 로고
    • Tracking Telomerase
    • Greider, C. W.; Blackburn, E. H. Tracking Telomerase Cell 2004, 116, S83-86
    • (2004) Cell , vol.116 , pp. 83-86
    • Greider, C.W.1    Blackburn, E.H.2
  • 5
    • 0842346436 scopus 로고    scopus 로고
    • Beginning to Understand the End of the Chromosome
    • Cech, T. R. Beginning to Understand the End of the Chromosome Cell 2004, 116, 273-279
    • (2004) Cell , vol.116 , pp. 273-279
    • Cech, T.R.1
  • 6
    • 83055184247 scopus 로고    scopus 로고
    • Single-Molecule Analysis of Telomerase Structure and Function
    • Hengesbach, M.; Akiyama, B. M.; Stone, M. D. Single-Molecule Analysis of Telomerase Structure and Function Curr. Opin. Chem. Biol. 2011, 15, 845-852
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 845-852
    • Hengesbach, M.1    Akiyama, B.M.2    Stone, M.D.3
  • 7
    • 84862907770 scopus 로고    scopus 로고
    • Functional Importance of Telomerase Pseudoknot Revealed by Single-Molecule Analysis
    • Mihalusova, M.; Wu, J. Y.; Zhuang, X. Functional Importance of Telomerase Pseudoknot Revealed by Single-Molecule Analysis Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 20339-20344
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 20339-20344
    • Mihalusova, M.1    Wu, J.Y.2    Zhuang, X.3
  • 9
    • 77951219958 scopus 로고    scopus 로고
    • A Single-Molecule Assay for Telomerase Structure-Function Analysis
    • Wu, J. Y.; Stone, M. D.; Zhuang, X. A Single-Molecule Assay for Telomerase Structure-Function Analysis Nucleic Acids Res. 2010, 38, e16
    • (2010) Nucleic Acids Res. , vol.38 , pp. 16
    • Wu, J.Y.1    Stone, M.D.2    Zhuang, X.3
  • 10
    • 33750695316 scopus 로고    scopus 로고
    • Structural Analysis of the Catalytic Core of Human Telomerase RNA by FRET and Molecular Modeling
    • Gavory, G.; Symmons, M. F.; Krishnan Ghosh, Y.; Klenerman, D.; Balasubramanian, S. Structural Analysis of the Catalytic Core of Human Telomerase RNA by FRET and Molecular Modeling Biochemistry 2006, 45, 13304-13311
    • (2006) Biochemistry , vol.45 , pp. 13304-13311
    • Gavory, G.1    Symmons, M.F.2    Krishnan Ghosh, Y.3    Klenerman, D.4    Balasubramanian, S.5
  • 11
    • 33745862398 scopus 로고    scopus 로고
    • The Biogenesis and Regulation of Telomerase Holoenzymes
    • Collins, K. The Biogenesis and Regulation of Telomerase Holoenzymes Nat. Rev. Mol. Cell Biol. 2006, 7, 484-494
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 484-494
    • Collins, K.1
  • 12
    • 1842813934 scopus 로고    scopus 로고
    • Telomerase RNA Structure and Function: Implications for Dyskeratosis Congenita
    • Chen, J. L.; Greider, C. W. Telomerase RNA Structure and Function: Implications for Dyskeratosis Congenita Trends Biochem. Sci. 2004, 29, 183-192
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 183-192
    • Chen, J.L.1    Greider, C.W.2
  • 13
    • 0034598919 scopus 로고    scopus 로고
    • Secondary Structure of Vertebrate Telomerase RNA
    • Chen, J. L.; Blasco, M. A.; Greider, C. W. Secondary Structure of Vertebrate Telomerase RNA Cell 2000, 100, 503-514
    • (2000) Cell , vol.100 , pp. 503-514
    • Chen, J.L.1    Blasco, M.A.2    Greider, C.W.3
  • 14
    • 0033535962 scopus 로고    scopus 로고
    • The Telomerase RNA Pseudoknot is Critical for the Stable Assembly of a Catalytically Active Ribonucleoprotein
    • Gilley, D.; Blackburn, E. H. The Telomerase RNA Pseudoknot is Critical for the Stable Assembly of a Catalytically Active Ribonucleoprotein Proc. Natl. Acad. Sci. U. S. A. 1999, 96, 6621-6625
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6621-6625
    • Gilley, D.1    Blackburn, E.H.2
  • 15
    • 0037829618 scopus 로고    scopus 로고
    • A Novel Pseudoknot Element is Essential for the Action of a Yeast Telomerase
    • Tzfati, Y.; Knight, Z.; Roy, J.; Blackburn, E. H. A Novel Pseudoknot Element is Essential for the Action of a Yeast Telomerase Genes Dev. 2003, 17, 1779-1788
    • (2003) Genes Dev. , vol.17 , pp. 1779-1788
    • Tzfati, Y.1    Knight, Z.2    Roy, J.3    Blackburn, E.H.4
  • 16
    • 33845871717 scopus 로고    scopus 로고
    • Conformational Analysis of the Telomerase RNA Pseudoknot Hairpin by Raman Spectroscopy
    • Reipa, V.; Niaura, G.; Atha, D. H. Conformational Analysis of the Telomerase RNA Pseudoknot Hairpin by Raman Spectroscopy RNA 2007, 13, 108-115
    • (2007) RNA , vol.13 , pp. 108-115
    • Reipa, V.1    Niaura, G.2    Atha, D.H.3
  • 17
    • 1942453903 scopus 로고    scopus 로고
    • Functional Organization of Repeat Addition Processivity and DNA Synthesis Determinants in the Human Telomerase Multimer
    • Moriarty, T. J.; Marie-Egyptienne, D. T.; Autexier, C. Functional Organization of Repeat Addition Processivity and DNA Synthesis Determinants in the Human Telomerase Multimer Mol. Cell. Biol. 2004, 24, 3720-3733
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3720-3733
    • Moriarty, T.J.1    Marie-Egyptienne, D.T.2    Autexier, C.3
  • 18
    • 0029958047 scopus 로고    scopus 로고
    • Reconstitution of Human Telomerase Activity and Identification of a Minimal Functional Region of the Human Telomerase RNA
    • Autexier, C.; Pruzan, R.; Funk, W. D.; Greider, C. W. Reconstitution of Human Telomerase Activity and Identification of a Minimal Functional Region of the Human Telomerase RNA EMBO. J. 1996, 15, 5928-5935
    • (1996) EMBO. J. , vol.15 , pp. 5928-5935
    • Autexier, C.1    Pruzan, R.2    Funk, W.D.3    Greider, C.W.4
  • 19
    • 0035881160 scopus 로고    scopus 로고
    • Human Telomerase RNA-Protein Interactions
    • Bachand, F.; Triki, I.; Autexier, C. Human Telomerase RNA-Protein Interactions Nucleic Acids Res. 2001, 29, 3385-3393
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3385-3393
    • Bachand, F.1    Triki, I.2    Autexier, C.3
  • 20
    • 56949105325 scopus 로고    scopus 로고
    • Solution Structure and Dynamics of the Wild-Type Pseudoknot of Human Telomerase RNA
    • Kim, N. K.; Zhang, Q.; Zhou, J.; Theimer, C. A.; Peterson, R. D.; Feigon, J. Solution Structure and Dynamics of the Wild-Type Pseudoknot of Human Telomerase RNA J. Mol. Biol. 2008, 384, 1249-1261
    • (2008) J. Mol. Biol. , vol.384 , pp. 1249-1261
    • Kim, N.K.1    Zhang, Q.2    Zhou, J.3    Theimer, C.A.4    Peterson, R.D.5    Feigon, J.6
  • 22
    • 14644435818 scopus 로고    scopus 로고
    • Structure of the Human Telomerase RNA Pseudoknot Reveals Conserved Tertiary Interactions Essential for Function
    • Theimer, C. A.; Blois, C. A.; Feigon, J. Structure of the Human Telomerase RNA Pseudoknot Reveals Conserved Tertiary Interactions Essential for Function Mol. Cell 2005, 17, 671-682
    • (2005) Mol. Cell , vol.17 , pp. 671-682
    • Theimer, C.A.1    Blois, C.A.2    Feigon, J.3
  • 23
    • 0037457985 scopus 로고    scopus 로고
    • Mutations Linked to Dyskeratosis Congenita Cause Changes in the Structural Equilibrium in Telomerase RNA
    • Theimer, C. A.; Finger, L. D.; Trantirek, L.; Feigon, J. Mutations Linked to Dyskeratosis Congenita Cause Changes in the Structural Equilibrium in Telomerase RNA Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 449-454
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 449-454
    • Theimer, C.A.1    Finger, L.D.2    Trantirek, L.3    Feigon, J.4
  • 24
    • 0344874270 scopus 로고    scopus 로고
    • YNMG Tetraloop Formation by a Dyskeratosis Congenita Mutation in Human Telomerase RNA
    • Theimer, C. A.; Finger, L. D.; Feigon, J. YNMG Tetraloop Formation by a Dyskeratosis Congenita Mutation in Human Telomerase RNA RNA 2003, 9, 1446-1455
    • (2003) RNA , vol.9 , pp. 1446-1455
    • Theimer, C.A.1    Finger, L.D.2    Feigon, J.3
  • 25
    • 36248968677 scopus 로고    scopus 로고
    • Single-Molecule Mechanical Unfolding and Folding of a Pseudoknot in Human Telomerase RNA
    • Chen, G.; Wen, J. D.; Tinoco, I., Jr. Single-Molecule Mechanical Unfolding and Folding of a Pseudoknot in Human Telomerase RNA RNA 2007, 13, 2175-2188
    • (2007) RNA , vol.13 , pp. 2175-2188
    • Chen, G.1    Wen, J.D.2    Tinoco Jr., I.3
  • 26
    • 84861860470 scopus 로고    scopus 로고
    • Single-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain
    • Hengesbach, M.; Kim, N. K.; Feigon, J.; Stone, M. D. Single-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain Angew. Chem., Int. Ed. 2012, 51, 5876-5879
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 5876-5879
    • Hengesbach, M.1    Kim, N.K.2    Feigon, J.3    Stone, M.D.4
  • 27
    • 33847280837 scopus 로고    scopus 로고
    • Biphasic Folding Kinetics of RNA Pseudoknots and Telomerase RNA Activity
    • Cao, S.; Chen, S. J. Biphasic Folding Kinetics of RNA Pseudoknots and Telomerase RNA Activity J. Mol. Biol. 2007, 367, 909-924
    • (2007) J. Mol. Biol. , vol.367 , pp. 909-924
    • Cao, S.1    Chen, S.J.2
  • 28
    • 33744547883 scopus 로고    scopus 로고
    • Predicting RNA Pseudoknot Folding Thermodynamics
    • Cao, S.; Chen, S. J. Predicting RNA Pseudoknot Folding Thermodynamics Nucleic Acids Res. 2006, 34, 2634-2652
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2634-2652
    • Cao, S.1    Chen, S.J.2
  • 30
    • 23744470902 scopus 로고    scopus 로고
    • Single-Molecule RNA Folding
    • Bokinsky, G.; Zhuang, X. Single-Molecule RNA Folding Acc. Chem. Res. 2005, 38, 566-573
    • (2005) Acc. Chem. Res. , vol.38 , pp. 566-573
    • Bokinsky, G.1    Zhuang, X.2
  • 31
    • 44449134820 scopus 로고    scopus 로고
    • A Practical Guide to Single-Molecule FRET
    • Roy, R.; Hohng, S.; Ha, T. A Practical Guide to Single-Molecule FRET Nat. Methods 2008, 5, 507-516
    • (2008) Nat. Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 32
    • 70349281455 scopus 로고    scopus 로고
    • RNA Folding Dynamics by Single-Molecule Fluorescence Resonance Energy Transfer
    • Zhao, R.; Rueda, D. RNA Folding Dynamics by Single-Molecule Fluorescence Resonance Energy Transfer Methods 2009, 49, 112-117
    • (2009) Methods , vol.49 , pp. 112-117
    • Zhao, R.1    Rueda, D.2
  • 34
    • 84860768295 scopus 로고    scopus 로고
    • Thermodynamic Origins of Monovalent Facilitated RNA Folding
    • Holmstrom, E. D.; Fiore, J. L.; Nesbitt, D. J. Thermodynamic Origins of Monovalent Facilitated RNA Folding Biochemistry 2012, 51, 3732-3743
    • (2012) Biochemistry , vol.51 , pp. 3732-3743
    • Holmstrom, E.D.1    Fiore, J.L.2    Nesbitt, D.J.3
  • 36
    • 0242500997 scopus 로고    scopus 로고
    • Exploration of the Transition State for Tertiary Structure Formation between an RNA Helix and a Large Structured RNA
    • Bartley, L. E.; Zhuang, X. W.; Das, R.; Chu, S.; Herschlag, D. Exploration of the Transition State for Tertiary Structure Formation Between an RNA Helix and a Large Structured RNA J. Mol. Biol. 2003, 328, 1011-1026
    • (2003) J. Mol. Biol. , vol.328 , pp. 1011-1026
    • Bartley, L.E.1    Zhuang, X.W.2    Das, R.3    Chu, S.4    Herschlag, D.5
  • 37
    • 64849085465 scopus 로고    scopus 로고
    • Enthalpy-Driven RNA Folding: Single-Molecule Thermodynamics of Tetraloop-Receptor Tertiary Interaction
    • Fiore, J. L.; Kraemer, B.; Koberling, F.; Erdmann, R.; Nesbitt, D. J. Enthalpy-Driven RNA Folding: Single-Molecule Thermodynamics of Tetraloop-Receptor Tertiary Interaction Biochemistry 2009, 48, 2550-2558
    • (2009) Biochemistry , vol.48 , pp. 2550-2558
    • Fiore, J.L.1    Kraemer, B.2    Koberling, F.3    Erdmann, R.4    Nesbitt, D.J.5
  • 38
    • 0033592945 scopus 로고    scopus 로고
    • Applicability of Urea in the Thermodynamic Analysis of Secondary and Tertiary RNA Folding
    • Shelton, V. M.; Sosnick, T. R.; Pan, T. Applicability of Urea in the Thermodynamic Analysis of Secondary and Tertiary RNA Folding Biochemistry 1999, 38, 16831-16839
    • (1999) Biochemistry , vol.38 , pp. 16831-16839
    • Shelton, V.M.1    Sosnick, T.R.2    Pan, T.3
  • 39
    • 78651345914 scopus 로고    scopus 로고
    • Assembly of Complex RNAs by Splinted Ligation
    • Akiyama, B. M.; Stone, M. D. Assembly of Complex RNAs by Splinted Ligation Methods Enzymol. 2009, 469, 27-46
    • (2009) Methods Enzymol. , vol.469 , pp. 27-46
    • Akiyama, B.M.1    Stone, M.D.2
  • 40
    • 0034131335 scopus 로고    scopus 로고
    • Joining of RNAs by Splinted Ligation
    • Moore, M. J.; Query, C. C. Joining of RNAs by Splinted Ligation Methods Enzymol. 2000, 317, 109-123
    • (2000) Methods Enzymol. , vol.317 , pp. 109-123
    • Moore, M.J.1    Query, C.C.2
  • 41
    • 33751118289 scopus 로고    scopus 로고
    • An RNA Ligase-Mediated Method for the Efficient Creation of Large, Synthetic RNAs
    • Stark, M. R.; Pleiss, J. A.; Deras, M.; Scaringe, S. A.; Rader, S. D. An RNA Ligase-Mediated Method for the Efficient Creation of Large, Synthetic RNAs RNA 2006, 12, 2014-2019
    • (2006) RNA , vol.12 , pp. 2014-2019
    • Stark, M.R.1    Pleiss, J.A.2    Deras, M.3    Scaringe, S.A.4    Rader, S.D.5
  • 42
    • 0001863161 scopus 로고    scopus 로고
    • Uses of Site-Specifically Modified RNAs Constructed by RNA Ligation
    • Smith, C. W. J. Oxford University Press: New York
    • Moore, M. J.; Query, C. C. Uses of Site-Specifically Modified RNAs Constructed by RNA Ligation. In RNA:Protein Interactions: A Practical Approach; Smith, C. W. J., Ed.; Oxford University Press: New York, 1998; pp 75-140.
    • (1998) RNA:Protein Interactions: A Practical Approach , pp. 75-140
    • Moore, M.J.1    Query, C.C.2
  • 43
    • 20444374113 scopus 로고    scopus 로고
    • Functional Analysis of the Pseudoknot Structure in Human Telomerase RNA
    • Chen, J. L.; Greider, C. W. Functional Analysis of the Pseudoknot Structure in Human Telomerase RNA Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 8080-8085
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8080-8085
    • Chen, J.L.1    Greider, C.W.2
  • 44
  • 46
    • 22144492905 scopus 로고    scopus 로고
    • Accurate FRET Measurements within Single Diffusing Biomolecules Using Alternating-Laser Excitation
    • Lee, N. K.; Kapanidis, A. N.; Wang, Y.; Michalet, X.; Mukhopadhyay, J.; Ebright, R. H.; Weiss, S. Accurate FRET Measurements within Single Diffusing Biomolecules Using Alternating-Laser Excitation Biophys. J. 2005, 88, 2939-2953
    • (2005) Biophys. J. , vol.88 , pp. 2939-2953
    • Lee, N.K.1    Kapanidis, A.N.2    Wang, Y.3    Michalet, X.4    Mukhopadhyay, J.5    Ebright, R.H.6    Weiss, S.7
  • 47
    • 2942650138 scopus 로고    scopus 로고
    • Fluorescence-Aided Molecule Sorting: Analysis of Structure and Interactions by Alternating-Laser Excitation of Single Molecules
    • Kapanidis, A. N.; Lee, N. K.; Laurence, T. A.; Doose, S.; Margeat, E.; Weiss, S. Fluorescence-Aided Molecule Sorting: Analysis of Structure and Interactions by Alternating-Laser Excitation of Single Molecules Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 8936-8941
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8936-8941
    • Kapanidis, A.N.1    Lee, N.K.2    Laurence, T.A.3    Doose, S.4    Margeat, E.5    Weiss, S.6
  • 49
    • 33751204491 scopus 로고    scopus 로고
    • Determination of the Fraction and Stoichiometry of Femtomolar Levels of Biomolecular Complexes in an Excess of Monomer Using Single-Molecule, Two-Color Coincidence Detection
    • Orte, A.; Clarke, R.; Balasubramanian, S.; Klenerman, D. Determination of the Fraction and Stoichiometry of Femtomolar Levels of Biomolecular Complexes in an Excess of Monomer Using Single-Molecule, Two-Color Coincidence Detection Anal. Chem. 2006, 78, 7707-7715
    • (2006) Anal. Chem. , vol.78 , pp. 7707-7715
    • Orte, A.1    Clarke, R.2    Balasubramanian, S.3    Klenerman, D.4
  • 50
    • 56049095755 scopus 로고    scopus 로고
    • Monovalent and Divalent Promoted GAAA-Tetraloop-Receptor Tertiary Interactions from Freely Diffusing Single-Molecule Studies
    • Fiore, J. L.; Hodak, J. H.; Piestert, O.; Downey, C. D.; Nesbitt, D. J. Monovalent and Divalent Promoted GAAA-Tetraloop-Receptor Tertiary Interactions from Freely Diffusing Single-Molecule Studies Biophys. J. 2008, 95, 3892-3905
    • (2008) Biophys. J. , vol.95 , pp. 3892-3905
    • Fiore, J.L.1    Hodak, J.H.2    Piestert, O.3    Downey, C.D.4    Nesbitt, D.J.5
  • 51
    • 41449108157 scopus 로고    scopus 로고
    • An Oxygen Scavenging System for Improvement of Dye Stability in Single-Molecule Fluorescence Experiments
    • Aitken, C. E.; Marshall, R. A.; Puglisi, J. D. An Oxygen Scavenging System for Improvement of Dye Stability in Single-Molecule Fluorescence Experiments Biophys. J. 2008, 94, 1826-1835
    • (2008) Biophys. J. , vol.94 , pp. 1826-1835
    • Aitken, C.E.1    Marshall, R.A.2    Puglisi, J.D.3
  • 53
    • 0026511656 scopus 로고
    • The Folding of an Enzyme. 1. Theory of Protein Engineering Analysis of Stability and Pathway of Protein Folding
    • Fersht, A. R.; Matouschek, A.; Serrano, L. The Folding of an Enzyme. 1. Theory of Protein Engineering Analysis of Stability and Pathway of Protein Folding J. Mol. Biol. 1992, 224, 771-782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 54
    • 71749118806 scopus 로고    scopus 로고
    • Urea Destabilizes RNA by Forming Stacking Interactions and Multiple Hydrogen Bonds with Nucleic Acid Bases
    • Priyakumar, U. D.; Hyeon, C.; Thirumalai, D.; MacKerell, A. D. Urea Destabilizes RNA by Forming Stacking Interactions and Multiple Hydrogen Bonds with Nucleic Acid Bases J. Am. Chem. Soc. 2009, 131, 17759-17761
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17759-17761
    • Priyakumar, U.D.1    Hyeon, C.2    Thirumalai, D.3    Mackerell, A.D.4
  • 55
    • 84868526664 scopus 로고    scopus 로고
    • Denaturation of RNA Secondary and Tertiary Structure by Urea: Simple Unfolded State Models and Free Energy Parameters Account for Measured m -values
    • Lambert, D.; Draper, D. E. Denaturation of RNA Secondary and Tertiary Structure by Urea: Simple Unfolded State Models and Free Energy Parameters Account for Measured m -values Biochemistry 2012, 51, 9014-9026
    • (2012) Biochemistry , vol.51 , pp. 9014-9026
    • Lambert, D.1    Draper, D.E.2
  • 57
    • 33847103691 scopus 로고    scopus 로고
    • The Impact of Dyskeratosis Congenita Mutations on the Structure and Dynamics of the Human Telomerase RNA Pseudoknot Domain
    • Yingling, Y. G.; Shapiro, B. A. The Impact of Dyskeratosis Congenita Mutations on the Structure and Dynamics of the Human Telomerase RNA Pseudoknot Domain J. Biomol. Struct. Dyn. 2007, 24, 303-319
    • (2007) J. Biomol. Struct. Dyn. , vol.24 , pp. 303-319
    • Yingling, Y.G.1    Shapiro, B.A.2


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