메뉴 건너뛰기




Volumn 46, Issue 9, 2007, Pages 2306-2316

DNA bending by charged peptides: Electrophoretic and spectroscopic analyses

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; BINDING ENERGY; ELECTROPHORESIS; ENERGY TRANSFER; PEPTIDES; SPECTROSCOPIC ANALYSIS;

EID: 33847628327     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061921a     Document Type: Article
Times cited : (8)

References (64)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution, Nature 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
    • 0024424261 scopus 로고
    • Functional replacement of a protein-induced bend in a DNA recombination site
    • Goodman, S. D., and Nash, H. A. (1989) Functional replacement of a protein-induced bend in a DNA recombination site, Nature 341, 251-254.
    • (1989) Nature , vol.341 , pp. 251-254
    • Goodman, S.D.1    Nash, H.A.2
  • 6
    • 0024099904 scopus 로고
    • Three persistence lengths for a stiff polymer with an application to DNA B-Z junctions
    • Manning, G. S. (1988) Three persistence lengths for a stiff polymer with an application to DNA B-Z junctions, Biopolymers 27, 1529-1542.
    • (1988) Biopolymers , vol.27 , pp. 1529-1542
    • Manning, G.S.1
  • 7
    • 0030593510 scopus 로고    scopus 로고
    • Structure of the CAP-DNA complex at 2.5 angstroms resolution: A complete picture of the protein-DNA interface
    • Parkinson, G., Wilson, C., Gunasekera, A., Ebright, Y. W., Ebright, R. E., and Herman, H. M. (1996) Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface, J. Mol. Biol. 260, 395-408.
    • (1996) J. Mol. Biol , vol.260 , pp. 395-408
    • Parkinson, G.1    Wilson, C.2    Gunasekera, A.3    Ebright, Y.W.4    Ebright, R.E.5    Herman, H.M.6
  • 8
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90 degrees
    • Schultz, S. C., Shields, G. C., and Steitz, T. A. (1991) Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees, Science 253, 1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 9
    • 0345097650 scopus 로고    scopus 로고
    • Is a small number of charge neutralizations sufficient to bend nucleosome core DNA onto its superhelical ramp?
    • Manning, G. S. (2003) Is a small number of charge neutralizations sufficient to bend nucleosome core DNA onto its superhelical ramp?, J. Am. Chem. Soc. 125, 15087-15092.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 15087-15092
    • Manning, G.S.1
  • 10
    • 0042166066 scopus 로고    scopus 로고
    • DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution
    • Dragan, A. I., Klass, J., Read, C., Churchill, M. E., Crane-Robinson, C., and Privalov, P. L. (2003) DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution, J. Mol. Biol. 331, 795-813.
    • (2003) J. Mol. Biol , vol.331 , pp. 795-813
    • Dragan, A.I.1    Klass, J.2    Read, C.3    Churchill, M.E.4    Crane-Robinson, C.5    Privalov, P.L.6
  • 13
    • 0037129935 scopus 로고    scopus 로고
    • DNA bending by bZIP charge variants: A unified study using electrophoretic phasing and fluorescence resonance energy transfer
    • Hardwidge, P. R., Wu, J., Williams, S. L., Parkhurst, K. M., Parkhurst, L. J., and Maher, L. J., III (2002) DNA bending by bZIP charge variants: a unified study using electrophoretic phasing and fluorescence resonance energy transfer, Biochemistry 41, 7732-7742.
    • (2002) Biochemistry , vol.41 , pp. 7732-7742
    • Hardwidge, P.R.1    Wu, J.2    Williams, S.L.3    Parkhurst, K.M.4    Parkhurst, L.J.5    Maher III, L.J.6
  • 14
    • 0028597967 scopus 로고
    • DNA bending by asymmetric phosphate neutralization
    • Strauss, J. K., and Maher, L. J., III (1994) DNA bending by asymmetric phosphate neutralization, Science 266, 1829-1834.
    • (1994) Science , vol.266 , pp. 1829-1834
    • Strauss, J.K.1    Maher III, L.J.2
  • 15
    • 0032570251 scopus 로고    scopus 로고
    • Electrostatic effects in DNA bending by GCN4 mutants
    • Strauss-Soukup, J. K., and Maher, L. J., III (1998) Electrostatic effects in DNA bending by GCN4 mutants, Biochemistry 37, 1060-1066.
    • (1998) Biochemistry , vol.37 , pp. 1060-1066
    • Strauss-Soukup, J.K.1    Maher III, L.J.2
  • 17
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning, G. S. (1978) The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides, Q. Rev. Biophys. 11, 179-246.
    • (1978) Q. Rev. Biophys , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 18
    • 0037058905 scopus 로고    scopus 로고
    • Electrostatic free energy of the DNA double helix in counterion condensation theory
    • Manning, G. S. (2002) Electrostatic free energy of the DNA double helix in counterion condensation theory, Biophys. Chem. 101-102, 461-473.
    • (2002) Biophys. Chem , vol.101-102 , pp. 461-473
    • Manning, G.S.1
  • 20
    • 0000562369 scopus 로고    scopus 로고
    • Water and monovalent ions in the minor groove of B-DNA oligonucleotides as seen by NMR
    • Halle, B., and Denisov, V. P. (1998) Water and monovalent ions in the minor groove of B-DNA oligonucleotides as seen by NMR, Biopolymers 48, 210-233.
    • (1998) Biopolymers , vol.48 , pp. 210-233
    • Halle, B.1    Denisov, V.P.2
  • 22
    • 0038713237 scopus 로고    scopus 로고
    • A unified model for the origin of DNA sequence-directed curvature
    • Hud, N. V., and Plavec, J. (2003) A unified model for the origin of DNA sequence-directed curvature, Biopolymers 69, 144-158.
    • (2003) Biopolymers , vol.69 , pp. 144-158
    • Hud, N.V.1    Plavec, J.2
  • 23
    • 0035367927 scopus 로고    scopus 로고
    • DNA-cation interactions: The major and minor grooves are flexible ionophores
    • Hud, N. V., and Polak, M. (2001) DNA-cation interactions: The major and minor grooves are flexible ionophores, Curr. Opin. Struct. Biol. 11, 293-301.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 293-301
    • Hud, N.V.1    Polak, M.2
  • 24
    • 0033605083 scopus 로고    scopus 로고
    • Localization of ammonium ions in the minor groove of DNA duplexes in solution and the origin of DNA A-tract bending
    • Hud, N. V., Sklenar, V., and Feigon, J. (1999) Localization of ammonium ions in the minor groove of DNA duplexes in solution and the origin of DNA A-tract bending, J. Mol. Biol. 286, 651-660.
    • (1999) J. Mol. Biol , vol.286 , pp. 651-660
    • Hud, N.V.1    Sklenar, V.2    Feigon, J.3
  • 26
    • 0024519056 scopus 로고
    • An estimate of the extent of folding of nucleosomal DNA by laterally asymmetric neutralization of phosphate groups
    • Manning, G. S., Ebralidse, K. K., Mirzabekov, A. D., and Rich, A. (1989) An estimate of the extent of folding of nucleosomal DNA by laterally asymmetric neutralization of phosphate groups, J. Biomol. Struct. Dyn. 6, 877-889.
    • (1989) J. Biomol. Struct. Dyn , vol.6 , pp. 877-889
    • Manning, G.S.1    Ebralidse, K.K.2    Mirzabekov, A.D.3    Rich, A.4
  • 27
    • 0001743558 scopus 로고
    • Asymmetric lateral distribution of unshielded phosphate groups in nucleosomal DNA and its role in DNA bending
    • Mirzabekov, A. D., and Rich, A. (1979) Asymmetric lateral distribution of unshielded phosphate groups in nucleosomal DNA and its role in DNA bending, Proc. Natl. Acad. Sci. U.S.A. 76, 1118-1121.
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 1118-1121
    • Mirzabekov, A.D.1    Rich, A.2
  • 28
    • 0008485562 scopus 로고
    • Localized positive charges can bend double helical nucleic acid
    • Rich, A. (1978) Localized positive charges can bend double helical nucleic acid, FEBS Lett. 51, 71-81.
    • (1978) FEBS Lett , vol.51 , pp. 71-81
    • Rich, A.1
  • 29
    • 0009407476 scopus 로고
    • Evidence for translational regulation of the activator of general amino acid control in yeast
    • Hinnebusch, A. G. (1984) Evidence for translational regulation of the activator of general amino acid control in yeast, Proc. Natl. Acad. Sci. U.S.A. 81, 6442-6446.
    • (1984) Proc. Natl. Acad. Sci. U.S.A , vol.81 , pp. 6442-6446
    • Hinnebusch, A.G.1
  • 30
    • 0025349096 scopus 로고
    • Involvement of an initiation factor and protein phosphorylation in translational control of GCN4 mRNA
    • Hinnebusch, A. G. (1990) Involvement of an initiation factor and protein phosphorylation in translational control of GCN4 mRNA, Trends Biochem. Sci. 15, 148-152.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 148-152
    • Hinnebusch, A.G.1
  • 31
    • 0028240180 scopus 로고
    • Creating new DNA binding specificities in the yeast transcriptional activator GCN4 by combining selected amino acid substitutions
    • Suckow, M., Madan, A., Kisters-Woike, B., von Wilcken-Bergmann, B., and Muller-Hill, B. (1994) Creating new DNA binding specificities in the yeast transcriptional activator GCN4 by combining selected amino acid substitutions, Nucleic Acids Res. 22, 2198-2208.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2198-2208
    • Suckow, M.1    Madan, A.2    Kisters-Woike, B.3    von Wilcken-Bergmann, B.4    Muller-Hill, B.5
  • 32
    • 0028852684 scopus 로고
    • Transcription. Zen and the art of Fos and Jun
    • Kerppola, T., and Curran, T. (1995) Transcription. Zen and the art of Fos and Jun, Nature 373, 199-200.
    • (1995) Nature , vol.373 , pp. 199-200
    • Kerppola, T.1    Curran, T.2
  • 33
    • 0025299910 scopus 로고
    • Structural motif of the GCN4 DNA binding domain characterized by affinity cleaving
    • Oakley, M. G., and Dervan, P. B. (1990) Structural motif of the GCN4 DNA binding domain characterized by affinity cleaving, Science 248, 847-850.
    • (1990) Science , vol.248 , pp. 847-850
    • Oakley, M.G.1    Dervan, P.B.2
  • 34
    • 0029790141 scopus 로고    scopus 로고
    • Do basic region-leucine zipper proteins bend their DNA targets...does it matter?
    • Hagerman, P. J. (1996) Do basic region-leucine zipper proteins bend their DNA targets...does it matter?, Proc. Natl. Acad. Sci. U.S.A. 93, 9993-9996.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 9993-9996
    • Hagerman, P.J.1
  • 35
    • 0030876348 scopus 로고    scopus 로고
    • Comparison of DNA bending by Fos-Jun and phased A tracts by multifactorial phasing analysis
    • Kerppola, T. (1997) Comparison of DNA bending by Fos-Jun and phased A tracts by multifactorial phasing analysis, Biochemistry 36, 10872-10884.
    • (1997) Biochemistry , vol.36 , pp. 10872-10884
    • Kerppola, T.1
  • 36
    • 0029789818 scopus 로고    scopus 로고
    • Fos and Jun bend the AP-1 site: Effects of probe geometry on the detection of protein-induced DNA bending
    • Kerppola, T. K. (1996) Fos and Jun bend the AP-1 site: effects of probe geometry on the detection of protein-induced DNA bending, Proc. Natl. Acad. Sci. U.S.A. 93, 10117-10122.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 10117-10122
    • Kerppola, T.K.1
  • 37
    • 0030914369 scopus 로고    scopus 로고
    • The transcription activation domains of Fos and Jun induce DNA bending through electrostatic interactions
    • Kerppola, T. K., and Curran, T. (1997) The transcription activation domains of Fos and Jun induce DNA bending through electrostatic interactions, EMBO J. 16, 2907-2916.
    • (1997) EMBO J , vol.16 , pp. 2907-2916
    • Kerppola, T.K.1    Curran, T.2
  • 38
    • 0030946251 scopus 로고    scopus 로고
    • Structural basis of DNA bending and oriented heterodimer binding by the basic leucine zipper domains of Fos and Jun
    • Leonard, D. A., Rajaram, N., and Kerppola, T. K. (1997) Structural basis of DNA bending and oriented heterodimer binding by the basic leucine zipper domains of Fos and Jun, Proc. Natl. Acad. Sci. U.S.A. 94, 4913-4918.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 4913-4918
    • Leonard, D.A.1    Rajaram, N.2    Kerppola, T.K.3
  • 39
    • 0032539630 scopus 로고    scopus 로고
    • DNA-binding domains of Fos and Jun do not induce DNA curvature: An investigation with solution and gel methods
    • Sitlani, A., and Crothers, D. (1998) DNA-binding domains of Fos and Jun do not induce DNA curvature: an investigation with solution and gel methods, Proc. Natl. Acad. Sci. U.S.A. 95, 1404-1409.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 1404-1409
    • Sitlani, A.1    Crothers, D.2
  • 40
    • 0029866110 scopus 로고    scopus 로고
    • Fos and jun do not bend the AP-1 recognition site
    • Sitlani, A., and Crothers, D. M. (1996) Fos and jun do not bend the AP-1 recognition site, Proc. Natl. Acad. Sci. U.S.A. 93, 3248-3252.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 3248-3252
    • Sitlani, A.1    Crothers, D.M.2
  • 41
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
    • Konig, P., and Richmond, T. J. (1993) The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility, J. Mol. Biol. 233, 139-154.
    • (1993) J. Mol. Biol , vol.233 , pp. 139-154
    • Konig, P.1    Richmond, T.J.2
  • 42
    • 0030803385 scopus 로고    scopus 로고
    • Electrostatic mechanism for DNA bending by bZIP proteins
    • Paolella, D. N., Liu, Y., Fabian, M. A., and Schepartz, A. (1997) Electrostatic mechanism for DNA bending by bZIP proteins, Biochemistry 36, 10033-10038.
    • (1997) Biochemistry , vol.36 , pp. 10033-10038
    • Paolella, D.N.1    Liu, Y.2    Fabian, M.A.3    Schepartz, A.4
  • 43
    • 0028245303 scopus 로고
    • DNA targets for certain bZIP proteins distinguished by an intrinsic bend
    • Paolella, D. N., Palmer, C. R., and Schepartz, A. (1994) DNA targets for certain bZIP proteins distinguished by an intrinsic bend, Science 264, 1130-1133.
    • (1994) Science , vol.264 , pp. 1130-1133
    • Paolella, D.N.1    Palmer, C.R.2    Schepartz, A.3
  • 44
    • 0032546528 scopus 로고    scopus 로고
    • Sequence determinants of the intrinsic bend in the cyclic AMP response element
    • Sloan, L. S., and Schepartz, A. (1998) Sequence determinants of the intrinsic bend in the cyclic AMP response element, Biochemistry 37, 7113-7118.
    • (1998) Biochemistry , vol.37 , pp. 7113-7118
    • Sloan, L.S.1    Schepartz, A.2
  • 45
    • 0026787523 scopus 로고
    • Global features of DNA structure by comparative gel electrophoresis
    • Crothers, D., and Drak, J. (1992) Global features of DNA structure by comparative gel electrophoresis, Methods Enzymol. 212, 46-71.
    • (1992) Methods Enzymol , vol.212 , pp. 46-71
    • Crothers, D.1    Drak, J.2
  • 46
    • 0025228644 scopus 로고
    • Determination of the extent of DNA bending by an adenine-thymine tract
    • Koo, H. S., Drak, J., Rice, J. A., and Crothers, D. M. (1990) Determination of the extent of DNA bending by an adenine-thymine tract, Biochemistry 29, 4227-4234.
    • (1990) Biochemistry , vol.29 , pp. 4227-4234
    • Koo, H.S.1    Drak, J.2    Rice, J.A.3    Crothers, D.M.4
  • 48
    • 0037008044 scopus 로고    scopus 로고
    • Dominant effect of protein charge rather than protein shape in apparent DNA bending by engineered bZIP domains
    • Hardwidge, P. R., Kahn, J. D., and Maher, L. J., III (2002) Dominant effect of protein charge rather than protein shape in apparent DNA bending by engineered bZIP domains, Biochemistry 41, 8277-8288.
    • (2002) Biochemistry , vol.41 , pp. 8277-8288
    • Hardwidge, P.R.1    Kahn, J.D.2    Maher III, L.J.3
  • 49
    • 0035312659 scopus 로고    scopus 로고
    • Recent advances in FRET: Distance determination in protein-DNA complexes
    • Hillisch, A., Lorenz, M., and Diekmann, S. (2001) Recent advances in FRET: distance determination in protein-DNA complexes, Curr. Opin. Struct. Biol. 11, 201-207.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 201-207
    • Hillisch, A.1    Lorenz, M.2    Diekmann, S.3
  • 50
    • 33644855950 scopus 로고    scopus 로고
    • Changes in DNA bending and flexing due to tethered cations detected by fluorescence resonance energy transfer
    • Williams, S. L., Parkhurst, L. K., and Parkhurst, L. J. (2006) Changes in DNA bending and flexing due to tethered cations detected by fluorescence resonance energy transfer, Nucleic Acids Res. 34, 1028-1035.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1028-1035
    • Williams, S.L.1    Parkhurst, L.K.2    Parkhurst, L.J.3
  • 51
    • 0036181263 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer studies of U-shaped DNA molecules
    • Lorenz, M., Hillisch, A., and Diekmann, S. (2002) Fluorescence resonance energy transfer studies of U-shaped DNA molecules, J. Biotechnol. 82, 197-209.
    • (2002) J. Biotechnol , vol.82 , pp. 197-209
    • Lorenz, M.1    Hillisch, A.2    Diekmann, S.3
  • 52
    • 4944226045 scopus 로고    scopus 로고
    • DNA-binding domain of GCN4 induces bending of both the ATF/CREB and AP-1 binding sites of DNA
    • Dragan, A. I., Liu, Y., Makeyeva, E. N., and Privalov, P. L. (2004) DNA-binding domain of GCN4 induces bending of both the ATF/CREB and AP-1 binding sites of DNA, Nucleic Acids Res. 32, 5192-5197.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5192-5197
    • Dragan, A.I.1    Liu, Y.2    Makeyeva, E.N.3    Privalov, P.L.4
  • 53
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: Crystal structure of the protein-DNA complex
    • Ellenberger, T. E., Brandl, C. J., Struhl, K., and Harrison, S. C. (1992) The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex, Cell 71, 1223-1237.
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 54
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen, Y. H., Yang, J. T., and Chau, K. H. (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism, Biochemistry 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 55
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 59
    • 0025155512 scopus 로고
    • Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA
    • Weiss, M. A., Ellenberger, T., Wobbe, C. R., Lee, J. P., Harrison, S. C., and Struhl, K. (1990) Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA, Nature 347, 575-578.
    • (1990) Nature , vol.347 , pp. 575-578
    • Weiss, M.A.1    Ellenberger, T.2    Wobbe, C.R.3    Lee, J.P.4    Harrison, S.C.5    Struhl, K.6
  • 60
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz, V., and Serrano, L. (1995) Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides, J. Mol. Biol. 245, 275-296.
    • (1995) J. Mol. Biol , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 61
    • 0033485813 scopus 로고    scopus 로고
    • Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer
    • Lorenz, M., Hillisch, A., Goodman, S. D., and Diekmann, S. (1999) Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer, Nucleic Acids Res. 27, 4619-4625.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4619-4625
    • Lorenz, M.1    Hillisch, A.2    Goodman, S.D.3    Diekmann, S.4
  • 62
    • 0034612993 scopus 로고    scopus 로고
    • Fluorescence energy transfer analysis of DNA structures containing several bulges and their interaction with CAP
    • Stuhmeier, F., Hillisch, A., Clegg, R. M., and Diekmann, S. (2000) Fluorescence energy transfer analysis of DNA structures containing several bulges and their interaction with CAP, J. Mol. Biol. 302, 1081-1100.
    • (2000) J. Mol. Biol , vol.302 , pp. 1081-1100
    • Stuhmeier, F.1    Hillisch, A.2    Clegg, R.M.3    Diekmann, S.4
  • 63
    • 0026315512 scopus 로고
    • DNA bending by Fos and Jun: The flexible hinge model
    • Kerppola, T. K., and Curran, T. (1991) DNA bending by Fos and Jun: the flexible hinge model, Science 254, 1210-1214.
    • (1991) Science , vol.254 , pp. 1210-1214
    • Kerppola, T.K.1    Curran, T.2
  • 64
    • 0025902328 scopus 로고
    • Fos-Jun heterodimers and Jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity
    • Kerppola, T. K., and Curran, T. (1991) Fos-Jun heterodimers and Jun homodimers bend DNA in opposite orientations: implications for transcription factor cooperativity, Cell 66, 317-326.
    • (1991) Cell , vol.66 , pp. 317-326
    • Kerppola, T.K.1    Curran, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.