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Volumn 153, Issue 6, 2013, Pages 1408-1408.e1

XSnapShot: Single-molecule fluorescence

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; IMMOBILIZED PROTEIN;

EID: 84878866504     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2013.05.024     Document Type: Short Survey
Times cited : (6)

References (10)
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    • Axelrod, D.1
  • 2
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    • Nanovesicle trapping for studying weak protein interactions by single-molecule FRET
    • Benítez, J.J., Keller, A.M., and Chen, P. (2010). Nanovesicle trapping for studying weak protein interactions by single-molecule FRET. Methods Enzymol. 472, 41-60.
    • (2010) Methods Enzymol , vol.472 , pp. 41-60
    • Benítez, J.J.1
  • 3
    • 84875733923 scopus 로고    scopus 로고
    • Ultrahigh accuracy imaging modality for super-localization microscopy
    • Chao, J., Ram, S., Ward, E.S., and Ober, R.J. (2013). Ultrahigh accuracy imaging modality for super-localization microscopy. Nat. Methods 10, 335-338.
    • (2013) Nat. Methods , vol.10 , pp. 335-338
    • Chao, J.1    Ram, S.2    Ward, E.S.3    Ober, R.J.4
  • 4
    • 0034536115 scopus 로고    scopus 로고
    • Protein structural dynamics by single-molecule fluorescence polarization
    • S.H. Leuba and J. Zlatanova, eds . Schliwa, ed. (Kidlington, Oxford, United Kingdom: Elsevier Science Ltd.)
    • Forkey, J.N., Quinlan, M.E., and Goldman, Y.E. (2001). Protein structural dynamics by single-molecule fluorescence polarization. In Biology at the Single Molecule Level, S.H. Leuba and J. Zlatanova, eds . Schliwa, ed. (Kidlington, Oxford, United Kingdom: Elsevier Science Ltd.), pp. 1 -36.
    • (2001) Biology at the Single Molecule Level , pp. 1-36
    • Forkey, J.N.1    Quinlan, M.E.2    Goldman, Y.E.3
  • 5
    • 0037154114 scopus 로고    scopus 로고
    • Biological and chemical applications of fluorescence correlation spectroscopy
    • Hess, S.T., Huang, S., Heikal, A.A., and Webb, W.W. (2002). Biological and chemical applications of fluorescence correlation spectroscopy. Biochemistry 41, 697-705.
    • (2002) Biochemistry , vol.41 , pp. 697-705
    • Hess, S.T.1    Huang, S.2    Heikal, A.A.3    Webb, W.W.4
  • 6
    • 84871337430 scopus 로고    scopus 로고
    • Single-molecule nanometry for biological physics
    • Kim, H., and Ha, T. (2013). Single-molecule nanometry for biological physics. Rep. Prog. Phys. 76, 016601.
    • (2013) Rep. Prog. Phys. , vol.76 , pp. 016601
    • Kim, H.1    Ha, T.2
  • 7
    • 53349152992 scopus 로고    scopus 로고
    • Zero-mode waveguides: Sub-wavelength nanostructures for single molecule studies at high concentrations
    • Moran-Mirabal, J.M., and Craighead, H.G. (2008). Zero-mode waveguides: sub-wavelength nanostructures for single molecule studies at high concentrations. Methods 46, 11-17.
    • (2008) Methods , vol.46 , pp. 11-17
    • Moran-Mirabal, J.M.1    Craighead, H.G.2
  • 8
    • 84862638904 scopus 로고    scopus 로고
    • Single-molecule tracking of collagenase on native type i collagen fibrils reveals degradation mechanism
    • Sarkar, S.K., Marmer, B., Goldberg, G., and Neuman, K.C. (2012). Single-molecule tracking of collagenase on native type I collagen fibrils reveals degradation mechanism. Curr. Biol. 22, 1047-1056.
    • (2012) Curr. Biol. , vol.22 , pp. 1047-1056
    • Sarkar, S.K.1    Marmer, B.2    Goldberg, G.3    Neuman, K.C.4
  • 9
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    • Do-it-yourself guide: How to use the modern single-molecule toolkit
    • Walter, N.G., Huang, C.-Y., Manzo, A.J., and Sobhy, M.A. (2008). Do-it-yourself guide: how to use the modern single-molecule toolkit. Nat. Methods 5, 475-489.
    • (2008) Nat. Methods , vol.5 , pp. 475-489
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  • 10
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    • Single-molecule fluorescence imaging in living cells
    • Xia, T., Li, N., and Fang, X. (2013). Single-molecule fluorescence imaging in living cells. Annu. Rev. Phys. Chem. 64, 459-480.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.