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Volumn 45, Issue 19, 2006, Pages 6075-6084

Reversible photocontrol of DNA binding by a designed GCN4-bZIP protein

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE; CHROMOPHORES; ISOMERIZATION; MOLECULES; PROTEINS;

EID: 33646557708     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060142r     Document Type: Article
Times cited : (84)

References (59)
  • 1
    • 0027480532 scopus 로고
    • Controlling cell chemistry with caged compounds
    • Adams, S. R., and Tsien, R. Y. (1993) Controlling cell chemistry with caged compounds, Annu. Rev. Physiol. 55, 755-784.
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 755-784
    • Adams, S.R.1    Tsien, R.Y.2
  • 4
    • 0035206072 scopus 로고    scopus 로고
    • Synthesis and application of caged peptides and proteins
    • Shigeri, Y., Tatsu, Y., and Yumoto, N. (2001) Synthesis and application of caged peptides and proteins, Pharmacol. Ther. 91, 85-92.
    • (2001) Pharmacol. Ther. , vol.91 , pp. 85-92
    • Shigeri, Y.1    Tatsu, Y.2    Yumoto, N.3
  • 5
    • 0036866562 scopus 로고    scopus 로고
    • Phytochrome-mediated photoperception and signal transduction in higher plants
    • Schafer, E., and Bowle, C. (2002) Phytochrome-mediated photoperception and signal transduction in higher plants, EMBO Rep. 3, 1042-1048.
    • (2002) EMBO Rep. , vol.3 , pp. 1042-1048
    • Schafer, E.1    Bowle, C.2
  • 6
    • 0032510475 scopus 로고    scopus 로고
    • Structure at 0.85 Å resolution of an early protein photocycle intermediate
    • Genick, U. K., Soltis, S. M., Kuhn, P., Canestrelli, I. L., and Getzoff, E. D. (1998) Structure at 0.85 Å resolution of an early protein photocycle intermediate, Nature 392, 206-209.
    • (1998) Nature , vol.392 , pp. 206-209
    • Genick, U.K.1    Soltis, S.M.2    Kuhn, P.3    Canestrelli, I.L.4    Getzoff, E.D.5
  • 7
    • 0024515763 scopus 로고
    • Protein design, a minimalist approach
    • DeGrado, W. F., Wasserman, Z. R., and Lear, J. D. (1989) Protein design, a minimalist approach, Science 243, 622-628.
    • (1989) Science , vol.243 , pp. 622-628
    • DeGrado, W.F.1    Wasserman, Z.R.2    Lear, J.D.3
  • 8
    • 22244487296 scopus 로고    scopus 로고
    • Photocontrolling peptide alpha helices
    • Woolley, G. A. (2005) Photocontrolling peptide alpha helices, Acc. Chem. Res. 38, 486-493.
    • (2005) Acc. Chem. Res. , vol.38 , pp. 486-493
    • Woolley, G.A.1
  • 10
    • 0036009333 scopus 로고    scopus 로고
    • Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization
    • Flint, D. G., Kumita, J. R., Smart, O. S., and Woolley, G. A. (2002) Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization, Chem. Biol. 9, 391-397.
    • (2002) Chem. Biol. , vol.9 , pp. 391-397
    • Flint, D.G.1    Kumita, J.R.2    Smart, O.S.3    Woolley, G.A.4
  • 11
    • 20444371915 scopus 로고    scopus 로고
    • Reversibility of conformational switching in light-sensitive peptides
    • Borisenko, V., and Woolley, G. A. (2005) Reversibility of conformational switching in light-sensitive peptides, J. Photochem. Photobiol., A. 173, 21-28.
    • (2005) J. Photochem. Photobiol., A , vol.173 , pp. 21-28
    • Borisenko, V.1    Woolley, G.A.2
  • 12
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E. K., Rutkowski, R., and Kim, P. S. (1989) Evidence that the leucine zipper is a coiled coil, Science 243, 538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 13
    • 0022981167 scopus 로고
    • Saturation mutagenesis of the yeast his3 regulatory site: Requirements for transcriptional induction and for binding by GCN4 activator protein
    • Hill, D. E., Hope, I. A., Macke, J. P., and Struhl, K. (1986) Saturation mutagenesis of the yeast his3 regulatory site: requirements for transcriptional induction and for binding by GCN4 activator protein, Science 234, 451-457.
    • (1986) Science , vol.234 , pp. 451-457
    • Hill, D.E.1    Hope, I.A.2    Macke, J.P.3    Struhl, K.4
  • 14
    • 0004131634 scopus 로고
    • GCN4 protein, a positive transcription factor in yeast, binds general control promoters at all 5′ TGACTC 3′ sequences
    • Arndt, K., and Fink, G. R. (1986) GCN4 protein, a positive transcription factor in yeast, binds general control promoters at all 5′ TGACTC 3′ sequences, Proc. Natl. Acad. Sci. U.S.A. 83, 8516-8520.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8516-8520
    • Arndt, K.1    Fink, G.R.2
  • 15
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E. K., Klemm, J. D., Kim, P. S., and Alber, T. (1991) X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil, Science 254, 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 16
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Landschulz, W. H., Johnson, P. F., and McKnight, S. L. (1988) The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins, Science 240.
    • (1988) Science , pp. 240
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 17
    • 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
  • 18
    • 0033525126 scopus 로고    scopus 로고
    • Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: Implications for the entropy of association with DNA
    • Bracken, C., Carr, P. A., Cavanagh, J., and Palmer, A. G., III (1999) Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA, J. Mol. Biol. 285, 2133-2146.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2133-2146
    • Bracken, C.1    Carr, P.A.2    Cavanagh, J.3    Palmer III, A.G.4
  • 19
    • 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
  • 21
    • 0027458868 scopus 로고
    • Design of a metallo-bZIP protein that discriminates between CRE and API target sites: Selection against AP1
    • Cuenoud, B., and Schepartz, A. (1993) Design of a metallo-bZIP protein that discriminates between CRE and API target sites: selection against AP1, Proc. Natl. Acad. Sci. U.S.A 90, 1154-1159.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 1154-1159
    • Cuenoud, B.1    Schepartz, A.2
  • 22
    • 0033616697 scopus 로고    scopus 로고
    • Stability of the dimerization domain effects the cooperative DNA binding of short peptides
    • Aizawa, Y., Sugiura, Y., Ueno, M., Mori, Y., Imoto, K., Makino, K., and Morii, T. (1999) Stability of the dimerization domain effects the cooperative DNA binding of short peptides, Biochemistry 38, 4008-4017.
    • (1999) Biochemistry , vol.38 , pp. 4008-4017
    • Aizawa, Y.1    Sugiura, Y.2    Ueno, M.3    Mori, Y.4    Imoto, K.5    Makino, K.6    Morii, T.7
  • 23
    • 0034732899 scopus 로고    scopus 로고
    • GCN4 binds with high affinity to DNA sequences containing a single consensus half-site
    • Hollenbeck, J. J., and Oakley, M. G. (2000) GCN4 binds with high affinity to DNA sequences containing a single consensus half-site, Biochemistry 39, 6380-6389.
    • (2000) Biochemistry , vol.39 , pp. 6380-6389
    • Hollenbeck, J.J.1    Oakley, M.G.2
  • 24
    • 0037026871 scopus 로고    scopus 로고
    • Sequence-specific recognition of DNA by hydrophobic, alanine-rich mutants of the basic region/leucine zipper motif investigated by fluorescence anisotropy
    • Bird, G. H., Lajmi, A. R., and Shin, J. A. (2002) Sequence-specific recognition of DNA by hydrophobic, alanine-rich mutants of the basic region/leucine zipper motif investigated by fluorescence anisotropy, Biopolymers 65, 10-20.
    • (2002) Biopolymers , vol.65 , pp. 10-20
    • Bird, G.H.1    Lajmi, A.R.2    Shin, J.A.3
  • 25
    • 0036655377 scopus 로고    scopus 로고
    • Photo-control of peptide helix content by an azobenzene cross-linker: Steric interactions with underlying residues are not critical
    • Kumita, J. R., Flint, D. G., Smart, O. S., and Woolley, G. A. (2002) Photo-control of peptide helix content by an azobenzene cross-linker: steric interactions with underlying residues are not critical, Protein Eng. 15, 561-569.
    • (2002) Protein Eng. , vol.15 , pp. 561-569
    • Kumita, J.R.1    Flint, D.G.2    Smart, O.S.3    Woolley, G.A.4
  • 26
    • 0001444863 scopus 로고
    • A refinement of the crystal structure of azobenzene
    • Brown, C. J. (1966) A refinement of the crystal structure of azobenzene, Acta Crystallogr. 21, 146-152.
    • (1966) Acta Crystallogr. , vol.21 , pp. 146-152
    • Brown, C.J.1
  • 27
    • 37049158574 scopus 로고
    • Crystal structure and configuration of the isomeric azobenzenes
    • Robertson, J. M. (1939) Crystal structure and configuration of the isomeric azobenzenes, J. Chem. Soc., 232-236.
    • (1939) J. Chem. Soc. , pp. 232-236
    • Robertson, J.M.1
  • 28
    • 0043076202 scopus 로고    scopus 로고
    • Ab initio calculation of the vibrational and electronic spectra of trans- and cis-azobenzene
    • Fliegl, H., Kohn, A., Hattig, C., and Ahlrichs, R. (2003) Ab initio calculation of the vibrational and electronic spectra of trans- and cis-azobenzene, J. Am. Chem. Soc. 125, 9821-9827.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9821-9827
    • Fliegl, H.1    Kohn, A.2    Hattig, C.3    Ahlrichs, R.4
  • 29
    • 0038384656 scopus 로고    scopus 로고
    • Mechanism of cis-to-trans isomerization of azobenzene: A direct MD study
    • Ikegami, T., Kurita, N., Sekino, H., and Ishikawa, Y. (2003) Mechanism of cis-to-trans isomerization of azobenzene: A direct MD study, J. Phys. Chem. A 107, 4555-4562.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 4555-4562
    • Ikegami, T.1    Kurita, N.2    Sekino, H.3    Ishikawa, Y.4
  • 30
    • 0036140263 scopus 로고    scopus 로고
    • Calculation of protein ionization equilibria with conformational sampling: PK(a) of a model leucine zipper, GCN4 and barnase
    • Gorfe, A. A., Ferrara, P., Caflisch, A., Marti, D. N., Bosshard, H. R., and Jelesarov, I. (2002) Calculation of protein ionization equilibria with conformational sampling: pK(a) of a model leucine zipper, GCN4 and barnase, Proteins 46, 41-60.
    • (2002) Proteins , vol.46 , pp. 41-60
    • Gorfe, A.A.1    Ferrara, P.2    Caflisch, A.3    Marti, D.N.4    Bosshard, H.R.5    Jelesarov, I.6
  • 31
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch, A., and Apweiler, R. (2000) The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000, Nucleic Acids Res. 28, 45-48.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 32
    • 0037795660 scopus 로고    scopus 로고
    • Achieving photo-control of protein conformation and activity: Producing a photo-controlled leucine zipper
    • discussion 171-190
    • Kumita, J. R., Flint, D. G., Woolley, G. A., and Smart, O. S. (2003) Achieving photo-control of protein conformation and activity: producing a photo-controlled leucine zipper, Faraday Discuss. 122, 89-103 (discussion 171-190).
    • (2003) Faraday Discuss. , vol.122 , pp. 89-103
    • Kumita, J.R.1    Flint, D.G.2    Woolley, G.A.3    Smart, O.S.4
  • 34
    • 0037778822 scopus 로고    scopus 로고
    • A water-soluble azobenzene cross-linker for photocontrol of peptide conformation
    • Zhang, Z., Burns, D. C., Kumita, J. R., Smart, O. S., and Woolley, G. A. (2003) A water-soluble azobenzene cross-linker for photocontrol of peptide conformation, Bioconjugate Chem. 14, 824-829.
    • (2003) Bioconjugate Chem. , vol.14 , pp. 824-829
    • Zhang, Z.1    Burns, D.C.2    Kumita, J.R.3    Smart, O.S.4    Woolley, G.A.5
  • 35
    • 1242317050 scopus 로고    scopus 로고
    • Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1
    • Ibarra-Molero, B., Zitzewitz, J. A., and Matthews, C. R. (2004) Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1, J. Mol. Biol. 336, 989-996.
    • (2004) J. Mol. Biol. , vol.336 , pp. 989-996
    • Ibarra-Molero, B.1    Zitzewitz, J.A.2    Matthews, C.R.3
  • 36
    • 0025045635 scopus 로고
    • Thermal unfolding studies of a leucine zipper domain and its specific DNA complex: Implications for scissor's grip recognition
    • Weiss, M. A. (1990) Thermal unfolding studies of a leucine zipper domain and its specific DNA complex: implications for scissor's grip recognition, Biochemistry 29, 8020-8024.
    • (1990) Biochemistry , vol.29 , pp. 8020-8024
    • Weiss, M.A.1
  • 37
    • 0035210771 scopus 로고    scopus 로고
    • Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate
    • Meng, F. G., Zeng, X., Hong, Y. K., and Zhou, H. M. (2001) Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate, Biochimie 83, 953-956.
    • (2001) Biochimie , vol.83 , pp. 953-956
    • Meng, F.G.1    Zeng, X.2    Hong, Y.K.3    Zhou, H.M.4
  • 38
    • 28844436330 scopus 로고    scopus 로고
    • Kinetic capillary electrophoresis (KCE): A conceptual platform for kinetic homogeneous affinity methods
    • Petrov, A., Okhonin, V., Berezovski, M., and Krylov, S. N. (2005) Kinetic capillary electrophoresis (KCE): a conceptual platform for kinetic homogeneous affinity methods, J. Am. Chem. Soc. 127, 17104-17110.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17104-17110
    • Petrov, A.1    Okhonin, V.2    Berezovski, M.3    Krylov, S.N.4
  • 39
    • 14744278465 scopus 로고    scopus 로고
    • Thermochemistry of protein-DNA interaction studied with temperature-controlled non-equilibrium capillary electrophoresis of equilibrium mixtures
    • Berezovski, M., and Krylov, S. N. (2005) Thermochemistry of protein-DNA interaction studied with temperature-controlled non-equilibrium capillary electrophoresis of equilibrium mixtures, Anal. Chem. 77, 1526-1529.
    • (2005) Anal. Chem. , vol.77 , pp. 1526-1529
    • Berezovski, M.1    Krylov, S.N.2
  • 40
    • 0032549490 scopus 로고    scopus 로고
    • Diffusion-controlled DNA recognition by an unfolded, monomeric bZIP transcription factor
    • Berger, C., Piubelli, L., Haditsch, U., and Bosshard, H. R. (1998) Diffusion-controlled DNA recognition by an unfolded, monomeric bZIP transcription factor, FEBS Lett. 425, 14-18.
    • (1998) FEBS Lett. , vol.425 , pp. 14-18
    • Berger, C.1    Piubelli, L.2    Haditsch, U.3    Bosshard, H.R.4
  • 42
    • 0030996370 scopus 로고    scopus 로고
    • -1 by phosphorylation of a serine in the e position
    • -1 by phosphorylation of a serine in the e position, Protein Sci. 6, 1273-1283.
    • (1997) Protein Sci. , vol.6 , pp. 1273-1283
    • Szilák, L.1    Moitra, J.2    Vinson, C.3
  • 43
    • 27644522929 scopus 로고    scopus 로고
    • Photocontrol of DNA binding specificity of a miniature engrailed homeodomain
    • Guerrero, L., Smart, O. S., Woolley, G. A., and Allemann, R. K. (2005) Photocontrol of DNA binding specificity of a miniature engrailed homeodomain, J. Am. Chem. Soc. 127, 15624-15629.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15624-15629
    • Guerrero, L.1    Smart, O.S.2    Woolley, G.A.3    Allemann, R.K.4
  • 45
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T., and DeGrado, W. F. (1990) A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids, Science 250, 646-651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 46
    • 0026434114 scopus 로고
    • erratum
    • [erratum: (1991) Science 253, 952].
    • (1991) Science , vol.253 , pp. 952
  • 47
    • 9444298521 scopus 로고    scopus 로고
    • Photochemical regulation of the activity of an endonuclease BamHI using an azobenzene moiety incorporated site-selectively into the dimer interface
    • Nakayama, K., Endo, M., and Majima, T. (2004) Photochemical regulation of the activity of an endonuclease BamHI using an azobenzene moiety incorporated site-selectively into the dimer interface, Chem. Commun., 2386-2387.
    • (2004) Chem. Commun. , pp. 2386-2387
    • Nakayama, K.1    Endo, M.2    Majima, T.3
  • 48
    • 0001157823 scopus 로고
    • Functionalization of crown ethers and calixarenes: New applications as ligands, carriers, and host molecules
    • (Dugas, H., Ed.), Springer-Verlag, Berlin
    • Shinkai, S. (1990) Functionalization of crown ethers and calixarenes: New applications as ligands, carriers, and host molecules, in Bioorganic Chemistry Frontiers (Dugas, H., Ed.) pp 161-195, Springer-Verlag, Berlin.
    • (1990) Bioorganic Chemistry Frontiers , pp. 161-195
    • Shinkai, S.1
  • 49
    • 0346550511 scopus 로고
    • Photoresponsive crown ethers. 16. Photoregulated ion-binding to azobenzene-linked ethylenediamines and iminodiacetic acids
    • Shinkai, S., Nakamura, S., Nakashima, M., Manabe, O., and Iwamoto, M. (1985) Photoresponsive crown ethers. 16. Photoregulated ion-binding to azobenzene-linked ethylenediamines and iminodiacetic acids, Bull. Chem. Soc. Jpn. 58, 2340-2347.
    • (1985) Bull. Chem. Soc. Jpn. , vol.58 , pp. 2340-2347
    • Shinkai, S.1    Nakamura, S.2    Nakashima, M.3    Manabe, O.4    Iwamoto, M.5
  • 50
    • 33646596848 scopus 로고    scopus 로고
    • Effect of packing on orientation and cis-trans isomerization of azobenzene chromophore in Langmuir-Blodgett film
    • in press
    • Takahashi, M., Okuhara, T., Yokohari, T., and Kobayashi, K. (2005) Effect of packing on orientation and cis-trans isomerization of azobenzene chromophore in Langmuir-Blodgett film, J. Colloid Interface Sci. (in press).
    • (2005) J. Colloid Interface Sci.
    • Takahashi, M.1    Okuhara, T.2    Yokohari, T.3    Kobayashi, K.4
  • 51
    • 22944471420 scopus 로고    scopus 로고
    • Photoisomerization of azobenzene from first-principles constrained density-functional calculations
    • Tiago, M. L., Ismail-Beigi, S., and Louie, S. G. (2005) Photoisomerization of azobenzene from first-principles constrained density-functional calculations, J. Chem. Phys. 122, 094311.
    • (2005) J. Chem. Phys. , vol.122 , pp. 094311
    • Tiago, M.L.1    Ismail-Beigi, S.2    Louie, S.G.3
  • 53
    • 28544431572 scopus 로고    scopus 로고
    • T-jump infrared study of the folding mechanism of coiled-coil GCN4-p1
    • Wang, T., Lau, W. L., DeGrado, W. F., and Gai, F. (2005) T-jump infrared study of the folding mechanism of coiled-coil GCN4-p1, Biophys. J. 89, 4180-4187.
    • (2005) Biophys. J. , vol.89 , pp. 4180-4187
    • Wang, T.1    Lau, W.L.2    DeGrado, W.F.3    Gai, F.4
  • 55
    • 13844272399 scopus 로고    scopus 로고
    • Membrane-permeable arginine-rich peptides and the translocation mechanisms
    • Futaki, S. (2005) Membrane-permeable arginine-rich peptides and the translocation mechanisms, Adv. Drug Deliv. Rev. 57, 547-558.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 547-558
    • Futaki, S.1
  • 56
    • 31544435747 scopus 로고    scopus 로고
    • Probing the impact of valency on the routing of arginine-rich peptides into eukaryotic cells
    • Kawamura, K. S., Sung, M., Bolewska-Pedyczak, E., and Gariepy, J. (2006) Probing the impact of valency on the routing of arginine-rich peptides into eukaryotic cells, Biochemistry 45, 1116-1127.
    • (2006) Biochemistry , vol.45 , pp. 1116-1127
    • Kawamura, K.S.1    Sung, M.2    Bolewska-Pedyczak, E.3    Gariepy, J.4
  • 58
    • 0036788581 scopus 로고    scopus 로고
    • An enlightened genetic switch
    • Mendelsohn, A. R. (2002) An enlightened genetic switch, Nat. Biotechnol. 20, 985-987.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 985-987
    • Mendelsohn, A.R.1
  • 59
    • 0036902245 scopus 로고    scopus 로고
    • Photoregulation of the transcription reaction of T7 RNA polymerase by tethering an azobenzene to the promoter
    • Asanuma, H., Tamaru, D., Yamazawa, A., Liu, M., and Komiyama, M. (2002) Photoregulation of the transcription reaction of T7 RNA polymerase by tethering an azobenzene to the promoter, ChemBioChem 3, 786-789.
    • (2002) ChemBioChem , vol.3 , pp. 786-789
    • Asanuma, H.1    Tamaru, D.2    Yamazawa, A.3    Liu, M.4    Komiyama, M.5


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