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Volumn 465, Issue , 2014, Pages 127-133

Cross-platform comparison of nucleic acid hybridization: Toward quantitative reference standards

Author keywords

Biomolecular interaction analysis; Differential scanning calorimetry; DNA; Isothermal titration calorimetry; Oligonucleotides; RNA

Indexed keywords

CALORIMETERS; DNA; ISOTHERMS; MATERIALS HANDLING; OLIGONUCLEOTIDES; RNA; THERMODYNAMIC PROPERTIES; TITRATION;

EID: 84907226932     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2014.08.001     Document Type: Article
Times cited : (3)

References (33)
  • 1
    • 0001160952 scopus 로고    scopus 로고
    • Ligand-receptor interactions
    • P. Bongrand, Ligand-receptor interactions, Rep. Prog. Phys. 62 (1999) 921.
    • (1999) Rep. Prog. Phys. , vol.62 , pp. 921
    • Bongrand, P.1
  • 2
    • 0038387389 scopus 로고    scopus 로고
    • A guide to drug discovery: Hit and lead generation-beyond high-throughput screening
    • K.H. Bleicher, H.-J. Böhm, K. Müller, A.I. Alanine, A guide to drug discovery: hit and lead generation-beyond high-throughput screening, Nat. Rev. Drug Discov. 2 (2003) 369-378.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 369-378
    • Bleicher, K.H.1    Böhm, H.-J.2    Müller, K.3    Alanine, A.I.4
  • 3
    • 0034581194 scopus 로고    scopus 로고
    • Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE
    • D.G. Myszka, Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE, Methods Enzymol. 323 (2000) 325-340.
    • (2000) Methods Enzymol. , vol.323 , pp. 325-340
    • Myszka, D.G.1
  • 4
    • 0037256228 scopus 로고    scopus 로고
    • NMR methods for the determination of protein-ligand dissociation constants
    • L. Fielding, NMR methods for the determination of protein-ligand dissociation constants, Curr. Top. Med. Chem. 3 (2003) 39-53.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 39-53
    • Fielding, L.1
  • 5
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • I. Jelesarov, H.R. Bosshard, Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition, J. Mol. Recognit. 12 (1999) 3-18.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 6
    • 34548169696 scopus 로고    scopus 로고
    • Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions
    • L.M. Hellman, M.G. Fried, Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions, Nat. Protoc. 2 (2007) 1849-1861.
    • (2007) Nat. Protoc. , vol.2 , pp. 1849-1861
    • Hellman, L.M.1    Fried, M.G.2
  • 7
    • 58249085344 scopus 로고    scopus 로고
    • Fluorescence approaches to quantifying biomolecular interactions
    • C.A. Royer, S.F. Scarlata, Fluorescence approaches to quantifying biomolecular interactions, Methods Enzymol. 450 (2008) 79-106.
    • (2008) Methods Enzymol. , vol.450 , pp. 79-106
    • Royer, C.A.1    Scarlata, S.F.2
  • 8
    • 0027138551 scopus 로고
    • Radioligand binding methods: Practical guide and tips
    • D.B. Bylund, M.L. Toews, Radioligand binding methods: practical guide and tips, Am. J. Physiol. 265 (1993) L421-L429.
    • (1993) Am. J. Physiol. , vol.265 , pp. L421-L429
    • Bylund, D.B.1    Toews, M.L.2
  • 9
    • 33845437051 scopus 로고    scopus 로고
    • Calibration in isothermal titration calorimetry: Heat and cell volume from heat of dilution of NaCl(aq)
    • J. Tellinghuisen, Calibration in isothermal titration calorimetry: heat and cell volume from heat of dilution of NaCl(aq), Anal. Biochem. 360 (2007) 47-55.
    • (2007) Anal. Biochem. , vol.360 , pp. 47-55
    • Tellinghuisen, J.1
  • 10
    • 84873739161 scopus 로고    scopus 로고
    • Conditions for calibration of an isothermal titration calorimeter using chemical reactions
    • C. Sgarlata, V. Zito, G. Arena, Conditions for calibration of an isothermal titration calorimeter using chemical reactions, Anal. Bioanal. Chem. 405 (2012) 1085-1094.
    • (2012) Anal. Bioanal. Chem. , vol.405 , pp. 1085-1094
    • Sgarlata, C.1    Zito, V.2    Arena, G.3
  • 11
    • 0029987812 scopus 로고    scopus 로고
    • A comparison of measured and calculated single- and double-stranded oligodeoxynucleotide extinction coefficients
    • G. Kallansrud, B. Ward, A comparison of measured and calculated single- and double-stranded oligodeoxynucleotide extinction coefficients, Anal. Biochem. 236 (1996) 134-138.
    • (1996) Anal. Biochem. , vol.236 , pp. 134-138
    • Kallansrud, G.1    Ward, B.2
  • 12
    • 17444453249 scopus 로고    scopus 로고
    • Revised UV extinction coefficients for nucleoside 5′-monophosphates and unpaired DNA and RNA
    • M.J. Cavaluzzi, Revised UV extinction coefficients for nucleoside 5′-monophosphates and unpaired DNA and RNA, Nucleic Acids Res. 32 (2004) e13.
    • (2004) Nucleic Acids Res. , vol.32 , pp. e13
    • Cavaluzzi, M.J.1
  • 13
    • 80051552234 scopus 로고    scopus 로고
    • Calibration of nanowatt isothermal titration calorimeters with overflow reaction vessels
    • N.A. Demarse, C.F. Quinn, D.L. Eggett, D.J. Russell, L.D. Hansen, Calibration of nanowatt isothermal titration calorimeters with overflow reaction vessels, Anal. Biochem. 417 (2011) 247-255.
    • (2011) Anal. Biochem. , vol.417 , pp. 247-255
    • Demarse, N.A.1    Quinn, C.F.2    Eggett, D.L.3    Russell, D.J.4    Hansen, L.D.5
  • 14
    • 0842303040 scopus 로고    scopus 로고
    • The role of backlash in the "first injection anomaly" in isothermal titration calorimetry
    • L.S. Mizoue, J. Tellinghuisen, The role of backlash in the "first injection anomaly" in isothermal titration calorimetry, Anal. Biochem. 326 (2004) 125-127.
    • (2004) Anal. Biochem. , vol.326 , pp. 125-127
    • Mizoue, L.S.1    Tellinghuisen, J.2
  • 15
  • 16
    • 1542303744 scopus 로고    scopus 로고
    • Analysis of thermal melting curves
    • J.-L. Mergny, L. Lacroix, Analysis of thermal melting curves, Oligonucleotides 13 (2003) 515-537.
    • (2003) Oligonucleotides , vol.13 , pp. 515-537
    • Mergny, J.-L.1    Lacroix, L.2
  • 17
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • H-J. Hinz (Ed.), Springer Verlag, Berlin
    • H. Durchschlag, Specific volumes of biological macromolecules and some other molecules of biological interest, in: H-J. Hinz (Ed.), Thermodynamic Data for Biochemistry and Biotechnology, Springer Verlag, Berlin, 1986, pp. 45-128.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-128
    • Durchschlag, H.1
  • 18
    • 35448961952 scopus 로고    scopus 로고
    • Differential scanning calorimetry
    • J.J. Correia, H.W. Detrich III (Eds.), Elsevier, San Diego
    • C.H. Spink, Differential scanning calorimetry, in: J.J. Correia, H.W. Detrich III (Eds.), Methods in Cell Biology, vol. 84, Elsevier, San Diego, 2008, pp. 115-141.
    • (2008) Methods in Cell Biology , vol.84 , pp. 115-141
    • Spink, C.H.1
  • 21
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • M. Zuker, Mfold web server for nucleic acid folding and hybridization prediction, Nucleic Acids Res. 31 (2003) 3406-3415.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 23
    • 0030669671 scopus 로고    scopus 로고
    • Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity
    • T. Pan, T.R. Sosnick, Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity, Nat. Struct. Biol. 4 (1997) 931-938.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 931-938
    • Pan, T.1    Sosnick, T.R.2
  • 25
    • 37549057040 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry in RNA biochemistry and biophysics
    • A.L. Feig, Applications of isothermal titration calorimetry in RNA biochemistry and biophysics, Biopolymers 87 (2007) 293-301.
    • (2007) Biopolymers , vol.87 , pp. 293-301
    • Feig, A.L.1
  • 26
    • 30744444833 scopus 로고    scopus 로고
    • Heat capacity changes associated with nucleic acid folding
    • P.J. Mikulecky, A.L. Feig, Heat capacity changes associated with nucleic acid folding, Biopolymers 82 (2006) 38-58.
    • (2006) Biopolymers , vol.82 , pp. 38-58
    • Mikulecky, P.J.1    Feig, A.L.2
  • 27
    • 78650110707 scopus 로고    scopus 로고
    • Studying RNA-RNA and RNA-protein interactions by isothermal titration calorimetry
    • D. Herschlag (Ed.), Elsevier, San Diego
    • A.L. Feig, Studying RNA-RNA and RNA-protein interactions by isothermal titration calorimetry, in: D. Herschlag (Ed.), Methods in Enzymology, vol. 468, Elsevier, San Diego, 2009, pp. 409-422.
    • (2009) Methods in Enzymology , vol.468 , pp. 409-422
    • Feig, A.L.1
  • 28
    • 0030026852 scopus 로고    scopus 로고
    • Chain length and oligonucleotide stability at high pressure
    • R.B. Macgregor, Chain length and oligonucleotide stability at high pressure, Biopolymers 38 (1996) 321-328.
    • (1996) Biopolymers , vol.38 , pp. 321-328
    • Macgregor, R.B.1
  • 29
    • 0033614819 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for formation of an oligomeric DNA duplex: Interpretation in terms of coupled processes of formation and association of single-stranded helices
    • J.A. Holbrook, M.W. Capp, R.M. Saecker, M.T. Record, Enthalpy and heat capacity changes for formation of an oligomeric DNA duplex: interpretation in terms of coupled processes of formation and association of single-stranded helices, Biochemistry 38 (1999) 8409-8422.
    • (1999) Biochemistry , vol.38 , pp. 8409-8422
    • Holbrook, J.A.1    Capp, M.W.2    Saecker, R.M.3    Record, M.T.4
  • 30
    • 0030995171 scopus 로고    scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies (part III)
    • Y. Liu, J.M. Sturtevant, Significant discrepancies between van't Hoff and calorimetric enthalpies (part III), Biophys. Chem. 64 (1997) 121-126.
    • (1997) Biophys. Chem. , vol.64 , pp. 121-126
    • Liu, Y.1    Sturtevant, J.M.2
  • 31
    • 0030971891 scopus 로고    scopus 로고
    • Possible origin of differences between van't Hoff and calorimetric enthalpy estimates
    • J.B. Chaires, Possible origin of differences between van't Hoff and calorimetric enthalpy estimates, Biophys. Chem. 64 (1997) 15-23.
    • (1997) Biophys. Chem. , vol.64 , pp. 15-23
    • Chaires, J.B.1
  • 32
    • 0035852865 scopus 로고    scopus 로고
    • Van't Hoff and calorimetric enthalpies from isothermal titration calorimetry: Are there significant discrepancies?
    • J.R. Horn, D. Russell, E.A. Lewis, K.P. Murphy, Van't Hoff and calorimetric enthalpies from isothermal titration calorimetry: Are there significant discrepancies?, Biochemistry 40 (2001) 1774-1778
    • (2001) Biochemistry , vol.40 , pp. 1774-1778
    • Horn, J.R.1    Russell, D.2    Lewis, E.A.3    Murphy, K.P.4
  • 33
    • 0029064484 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies
    • H. Naghibi, A. Tamura, J.M. Sturtevant, Significant discrepancies between van't Hoff and calorimetric enthalpies, Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 5597-5599.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5597-5599
    • Naghibi, H.1    Tamura, A.2    Sturtevant, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.