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Volumn 40, Issue 14, 2012, Pages

DNA origami as biocompatible surface to match single-molecule and ensemble experiments

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; MOLECULAR SCAFFOLD; SINGLE STRANDED DNA; TATA BINDING PROTEIN;

EID: 84864919485     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks326     Document Type: Article
Times cited : (48)

References (47)
  • 1
    • 33645990641 scopus 로고    scopus 로고
    • Bridging conformational dynamics and function using single-molecule spectroscopy
    • Myong, S., Stevens, B.C. and Ha, T. (2006) Bridging conformational dynamics and function using single-molecule spectroscopy. Structure, 14, 633-643.
    • (2006) Structure , vol.14 , pp. 633-643
    • Myong, S.1    Stevens, B.C.2    Ha, T.3
  • 2
    • 18844423055 scopus 로고    scopus 로고
    • Branching out of single-molecule fluorescence spectroscopy: Challenges for chemistry and influence on biology
    • DOI 10.1002/anie.200300647
    • Tinnefeld, P. and Sauer, M. (2005) Branching out of single-molecule fluorescence spectroscopy: challenges for chemistry and influence on biology. Angew. Chem. Int. Ed. Engl., 44, 2642-2671. (Pubitemid 40689566)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.18 , pp. 2642-2671
    • Tinnefeld, P.1    Sauer, M.2
  • 4
    • 0032828419 scopus 로고    scopus 로고
    • Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation
    • Schwille, P., Haupts, U., Maiti, S. and Webb, W.W. (1999) Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one-and two-photon excitation. Biophys. J., 77, 2251-2265. (Pubitemid 29463185)
    • (1999) Biophysical Journal , vol.77 , Issue.4 , pp. 2251-2265
    • Schwille, P.1    Haupts, U.2    Maiti, S.3    Webb, W.W.4
  • 6
    • 1842607369 scopus 로고    scopus 로고
    • Biofunctionalized, Ultrathin Coatings of Cross-Linked Star-Shaped Poly(ethylene oxide) Allow Reversible Folding of Immobilized Proteins
    • DOI 10.1021/ja0318028
    • Groll, J., Amirgoulova, E.V., Ameringer, T., Heyes, C.D., Rocker, C., Nienhaus, G.U. and Moller, M. (2004) Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allow reversible folding of immobilized proteins. J. Am. Chem. Soc., 126, 4234-4239. (Pubitemid 38453882)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.13 , pp. 4234-4239
    • Groll, J.1    Amirgoulova, E.V.2    Ameringer, T.3    Heyes, C.D.4    Rocker, C.5    Nienhaus, G.U.6    Moller, M.7
  • 7
    • 7544225920 scopus 로고    scopus 로고
    • Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic
    • Okumus, B., Wilson, T.J., Lilley, D.M. and Ha, T. (2004) Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic. Biophys. J., 87, 2798-2806.
    • (2004) Biophys. J. , vol.87 , pp. 2798-2806
    • Okumus, B.1    Wilson, T.J.2    Lilley, D.M.3    Ha, T.4
  • 8
    • 23744433971 scopus 로고    scopus 로고
    • Surfaces and Orientations: Much to FRET about?
    • DOI 10.1021/ar040138c
    • Rasnik, I., McKinney, S.A. and Ha, T. (2005) Surfaces and orientations: much to FRET about? Acc. Chem. Res., 38, 542-548. (Pubitemid 41128406)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.7 , pp. 542-548
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 9
    • 70350052649 scopus 로고    scopus 로고
    • Single molecule nanocontainers made porous using a bacterial toxin
    • Okumus, B., Arslan, S., Fengler, S.M., Myong, S. and Ha, T. (2009) Single molecule nanocontainers made porous using a bacterial toxin. J. Am. Chem. Soc., 131, 14844-14849.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14844-14849
    • Okumus, B.1    Arslan, S.2    Fengler, S.M.3    Myong, S.4    Ha, T.5
  • 10
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • Talaga, D.S., Lau, W.L., Roder, H., Tang, J., Jia, Y., DeGrado, W.F. and Hochstrasser, R.M. (2000) Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc. Natl Acad. Sci. USA, 97, 13021-13026.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13021-13026
    • Talaga, D.S.1    Lau, W.L.2    Roder, H.3    Tang, J.4    Jia, Y.5    Degrado, W.F.6    Hochstrasser, R.M.7
  • 12
    • 0030575902 scopus 로고    scopus 로고
    • Three-dimensional imaging of single molecules solvated in pores of poly(acrylamide) gels
    • DOI 10.1126/science.274.5289.966
    • Dickson, R.M., Norris, D.J., Tzeng, Y.L. and Moerner, W.E. (1996) Three-dimensional imaging of single molecules solvated in pores of poly(acrylamide) gels. Science, 274, 966-969. (Pubitemid 26398415)
    • (1996) Science , vol.274 , Issue.5289 , pp. 966-969
    • Dickson, R.M.1    Norris, D.J.2    Tzeng, Y.-L.3    Moerner, W.E.4
  • 13
    • 78649704916 scopus 로고    scopus 로고
    • Temperature-independent porous nanocontainers for single-molecule fluorescence studies
    • Ishitsuka, Y., Okumus, B., Arslan, S., Chen, K.H. and Ha, T. (2010) Temperature-independent porous nanocontainers for single-molecule fluorescence studies. Anal. Chem., 82, 9694-9701.
    • (2010) Anal. Chem. , vol.82 , pp. 9694-9701
    • Ishitsuka, Y.1    Okumus, B.2    Arslan, S.3    Chen, K.H.4    Ha, T.5
  • 14
    • 54349103761 scopus 로고    scopus 로고
    • Nucleosome immobilization strategies for single-pair FRET microscopy
    • Koopmans, W.J., Schmidt, T. and van Noort, J. (2008) Nucleosome immobilization strategies for single-pair FRET microscopy. Chemphyschem., 9, 2002-2009.
    • (2008) Chemphyschem. , vol.9 , pp. 2002-2009
    • Koopmans, W.J.1    Schmidt, T.2    Van Noort, J.3
  • 15
    • 27944496013 scopus 로고    scopus 로고
    • Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy
    • DOI 10.1007/s00249-005-0010-1
    • Kufer, S.K., Dietz, H., Albrecht, C., Blank, K., Kardinal, A., Rief, M. and Gaub, H.E. (2005) Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy. Eur Biophys. J., 35, 72-78. (Pubitemid 41667027)
    • (2005) European Biophysics Journal , vol.35 , Issue.1 , pp. 72-78
    • Kufer, S.K.1    Dietz, H.2    Albrecht, C.3    Blank, K.4    Kardinal, A.5    Rief, M.6    Gaub, H.E.7
  • 18
    • 77953645331 scopus 로고    scopus 로고
    • Nanomaterials based on DNA
    • Seeman, N.C. (2010) Nanomaterials based on DNA. Annu. Rev. Biochem., 79, 65-87.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 65-87
    • Seeman, N.C.1
  • 19
    • 80052929444 scopus 로고    scopus 로고
    • DNA origami: A quantum leap for self-assembly of complex structures
    • Torring, T., Voigt, N.V., Nangreave, J., Yan, H. and Gothelf, K.V. (2011) DNA origami: a quantum leap for self-assembly of complex structures. Chem. Soc. Rev., 40, 5636-5646.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 5636-5646
    • Torring, T.1    Voigt, N.V.2    Nangreave, J.3    Yan, H.4    Gothelf, K.V.5
  • 20
    • 83555174809 scopus 로고    scopus 로고
    • Challenges and opportunities for structural DNA nanotechnology
    • Pinheiro, A.V., Han, D., Shih, W.M. and Yan, H. (2011) Challenges and opportunities for structural DNA nanotechnology. Nat. Nanotechnol., 6, 763-772.
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 763-772
    • Pinheiro, A.V.1    Han, D.2    Shih, W.M.3    Yan, H.4
  • 24
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • Rothemund, P.W. (2006) Folding DNA to create nanoscale shapes and patterns. Nature, 440, 297-302.
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.1
  • 25
    • 79551488258 scopus 로고    scopus 로고
    • FRET (fluorescence resonance energy transfer) sheds light on transcription
    • Grohmann, D., Klose, D., Fielden, D. and Werner, F. (2011) FRET (fluorescence resonance energy transfer) sheds light on transcription. Biochem. Soc. Trans., 39, 122-127.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 122-127
    • Grohmann, D.1    Klose, D.2    Fielden, D.3    Werner, F.4
  • 26
    • 67749103813 scopus 로고    scopus 로고
    • On the mechanism of Trolox as antiblinking and antibleaching reagent
    • Cordes, T., Vogelsang, J. and Tinnefeld, P. (2009) On the mechanism of Trolox as antiblinking and antibleaching reagent. J. Am. Chem. Soc., 131, 5018-5019.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5018-5019
    • Cordes, T.1    Vogelsang, J.2    Tinnefeld, P.3
  • 27
    • 33750295496 scopus 로고    scopus 로고
    • Nonblinking and long-lasting single-molecule fluorescence imaging
    • DOI 10.1038/nmeth934, PII NMETH934
    • Rasnik, I., McKinney, S.A. and Ha, T. (2006) Nonblinking and long-lasting single-molecule fluorescence imaging. Nat. Methods, 3, 891-893. (Pubitemid 44614723)
    • (2006) Nature Methods , vol.3 , Issue.11 , pp. 891-893
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 28
    • 66249137759 scopus 로고    scopus 로고
    • Self-assembly of DNA into nanoscale three-dimensional shapes
    • Douglas, S.M., Dietz, H., Liedl, T., Hogberg, B., Graf, F. and Shih, W.M. (2009) Self-assembly of DNA into nanoscale three-dimensional shapes. Nature, 459, 414-418.
    • (2009) Nature , vol.459 , pp. 414-418
    • Douglas, S.M.1    Dietz, H.2    Liedl, T.3    Hogberg, B.4    Graf, F.5    Shih, W.M.6
  • 30
    • 0036753399 scopus 로고    scopus 로고
    • A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription
    • DOI 10.1016/S1097-2765(02)00629-9
    • Werner, F. and Weinzierl, R.O. (2002) A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription. Mol. Cell, 10, 635-646. (Pubitemid 35284179)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 635-646
    • Werner, F.1    Weinzierl, R.O.J.2
  • 31
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • DOI 10.1038/nmeth.1208, PII NMETH.1208
    • Roy, R., Hohng, S. and Ha, T. (2008) A practical guide to single-molecule FRET. Nat. Methods, 5, 507-516. (Pubitemid 351761757)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 34
    • 83555174809 scopus 로고    scopus 로고
    • Challenges and opportunities for structural DNA nanotechnology
    • Pinheiro, A.V., Han, D., Shih, W.M. and Yan, H. (2011) Challenges and opportunities for structural DNA nanotechnology. Nat. Nanotechnol., 6, 763-772.
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 763-772
    • Pinheiro, A.V.1    Han, D.2    Shih, W.M.3    Yan, H.4
  • 35
    • 79953050409 scopus 로고    scopus 로고
    • Single-molecule four-color FRET visualizes energy-transfer paths on DNA origami
    • Stein, I.H., Steinhauer, C. and Tinnefeld, P. (2011) Single-molecule four-color FRET visualizes energy-transfer paths on DNA origami. J. Am. Chem. Soc., 133, 4193-4195.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4193-4195
    • Stein, I.H.1    Steinhauer, C.2    Tinnefeld, P.3
  • 36
    • 79961168437 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching
    • Berardi, M.J., Shih, W.M., Harrison, S.C. and Chou, J.J. (2011) Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching. Nature, 476, 109-113.
    • (2011) Nature , vol.476 , pp. 109-113
    • Berardi, M.J.1    Shih, W.M.2    Harrison, S.C.3    Chou, J.J.4
  • 37
    • 78649282278 scopus 로고    scopus 로고
    • Visualization of dynamic conformational switching of the G-quadruplex in a DNA nanostructure
    • Sannohe, Y., Endo, M., Katsuda, Y., Hidaka, K. and Sugiyama, H. (2010) Visualization of dynamic conformational switching of the G-quadruplex in a DNA nanostructure. J. Am. Chem. Soc., 132, 16311-16313.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 16311-16313
    • Sannohe, Y.1    Endo, M.2    Katsuda, Y.3    Hidaka, K.4    Sugiyama, H.5
  • 40
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • DOI 10.1529/biophysj.106.082487
    • McKinney, S.A., Joo, C. and Ha, T. (2006) Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys. J., 91, 1941-1951. (Pubitemid 44352455)
    • (2006) Biophysical Journal , vol.91 , Issue.5 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 41
    • 4143055013 scopus 로고    scopus 로고
    • Exploring rare conformational species and ionic effects in DNA Holliday junctions using single-molecule spectroscopy
    • DOI 10.1016/j.jmb.2004.06.024, PII S0022283604006941
    • Joo, C., McKinney, S.A., Lilley, D.M. and Ha, T. (2004) Exploring rare conformational species and ionic effects in DNA Holliday junctions using single-molecule spectroscopy. J. Mol. Biol., 341, 739-751. (Pubitemid 39118408)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.3 , pp. 739-751
    • Joo, C.1    McKinney, S.A.2    Lilley, D.M.J.3    Ha, T.4
  • 42
  • 43
    • 78651504121 scopus 로고    scopus 로고
    • Evolution of multisubunit RNA polymerases in the three domains of life
    • Werner, F. and Grohmann, D. (2011) Evolution of multisubunit RNA polymerases in the three domains of life. Nat. Rev. Microbiol, 9, 85-98.
    • (2011) Nat. Rev. Microbiol , vol.9 , pp. 85-98
    • Werner, F.1    Grohmann, D.2
  • 44
    • 0041856190 scopus 로고    scopus 로고
    • Native human TATA-binding protein simultaneously binds and bends promoter DNA without a slow isomerization step or TFIIB requirement
    • DOI 10.1074/jbc.M305201200
    • Masters, K.M., Parkhurst, K.M., Daugherty, M.A. and Parkhurst, L.J. (2003) Native human TATA-binding protein simultaneously binds and bends promoter DNA without a slow isomerization step or TFIIB requirement. J. Biol. Chem., 278, 31685-31690. (Pubitemid 37048347)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 31685-31690
    • Masters, K.M.1    Parkhurst, K.M.2    Daugherty, M.A.3    Parkhurst, L.J.4
  • 46
    • 77952404245 scopus 로고    scopus 로고
    • A proximity-based programmable DNA nanoscale assembly line
    • Gu, H., Chao, J., Xiao, S.-J. and Seeman, N.C. (2010) A proximity-based programmable DNA nanoscale assembly line. Nature, 465, 202-205.
    • (2010) Nature , vol.465 , pp. 202-205
    • Gu, H.1    Chao, J.2    Xiao, S.-J.3    Seeman, N.C.4
  • 47
    • 78449290663 scopus 로고    scopus 로고
    • Single-molecule kinetics and super-resolution microscopy by fluorescence imaging of transient binding on DNA origami
    • Jungmann, R., Steinhauer, C., Scheible, M., Kuzyk, A., Tinnefeld, P. and Simmel, F.C. (2010) Single-molecule kinetics and super-resolution microscopy by fluorescence imaging of transient binding on DNA origami. Nano Lett., 10, 4756-4761.
    • (2010) Nano Lett. , vol.10 , pp. 4756-4761
    • Jungmann, R.1    Steinhauer, C.2    Scheible, M.3    Kuzyk, A.4    Tinnefeld, P.5    Simmel, F.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.