Continuous throughput and long-term observation of single-molecule FRET without immobilization

Nature Methods

Volumn 11, Issue 3, 2014, Pages 297-300

  Tyagi, Swati ^a   Vandelinder, Virginia ^a,b   Banterle, Niccolò ^a   Fuertes, Gustavo ^a   Milles, Sigrid ^a   Agez, Morgane ^a   Lemke, Edward A ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b SANDIA NATIONAL LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; NANOCHANNEL; NUCLEIC ACID; PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2;

ARTICLE; EXCITATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HOLLIDAY JUNCTION; MICROFLUIDICS; MOLECULE; NANODEVICE; NANOFABRICATION; NUCLEOSOME; OBSERVATION; PRIORITY JOURNAL; SINGLE MOLECULE WITHOUT IMMOBILIZATION;

AUTOMATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; GTP-BINDING PROTEINS; HUMANS; MICROFLUIDICS; MODELS, MOLECULAR; TRANSGLUTAMINASES;

EID: 84895555644     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.2809     Document Type: Article

References (27)

1. Ha, T. Cell 154, 723-726 (2013).
2. Roy, R., Hohng, S. & Ha, T. Nat. Methods 5, 507-516 (2008).
3. Milles, S. & Lemke, E.A. Bioessays 35, 65-74 (2013).
4. Schuler, B. & Eaton, W.A. Curr. Opin. Struct. Biol. 18, 16-26 (2008).
5. Wang, Y.M. et al. Proc. Natl. Acad. Sci. USA 102, 9796-9801 (2005).
6. Quake, S.R. & Scherer, A. Science 290, 1536-1540 (2000).
7. Sui, G. et al. Anal. Chem. 78, 5543-5551 (2006).
8. Gambin, Y. et al. Nat. Methods 8, 239-241 (2011).
9. Shi, X., Lim, J. & Ha, T. Anal. Chem. 82, 6132-6138 (2010).
10. Lemke, E.A. et al. J. Am. Chem. Soc. 131, 13610-13612 (2009).
11. Müller, J.D., Chen, Y. & Gratton, E. Methods Enzymol. 361, 69-92 (2003).
12. Holden, S.J. et al. Biophys. J. 99, 3102-3111 (2010).
13. Kapanidis, A.N. et al. Proc. Natl. Acad. Sci. USA 101, 8936-8941 (2004).
14. Gansen, A. et al. Proc. Natl. Acad. Sci. USA 106, 15308-15313 (2009).
15. Milles, S. et al. EMBO Rep. 14, 178-183 (2013).
16. Clouthier, C.M., Mironov, G.G., Okhonin, V., Berezovski, M.V. & Keillor, J.W. Angew. Chem. Int. Ed. Engl. 51, 12464-12468 (2012).
17. Siegel, M. et al. PLoS One 3, e1861 (2008).
18. Keppler, A., Pick, H., Arrivoli, C., Vogel, H. & Johnsson, K. Proc. Natl. Acad. Sci. USA 101, 9955-9959 (2004).
19. Chung, H.S., McHale, K., Louis, J.M. & Eaton, W.A. Science 335, 981-984 (2012).
20. McKinney, S.A., Déclais, A.C., Lilley, D.M. & Ha, T. Nat. Struct. Biol. 10, 93-97 (2003).
21. Milles, S. & Lemke, E.A. Biophys. J. 101, 1710-1719 (2011).
22. Lowary, P.T. & Widom, J. J. Mol. Biol. 276, 19-42 (1998).
23. Lee, K.-M. & Narlikar, G. Curr. Protoc. Mol. Biol. 54, 21.6 (2001).
24. Roy, I., Smith, O., Clouthier, C.M. & Keillor, J.W. Protein Expr. Purif. 87, 41-46 (2013).
25. Gopich, I.V. & Szabo, A. J. Phys. Chem. B 111, 12925-12932 (2007).
26. Vogelsang, J. et al. Angew. Chem. Int. Ed. Engl. 47, 5465-5469 (2008).
27. Qian, H., Sheetz, M.P. & Elson, E.L. Biophys. J. 60, 910-921 (1991).