High-resolution tracking of single-molecule diffusion in membranes by confocalized and spatially differentiated fluorescence photon stream recording

ChemPhysChem

Volumn 15, Issue 4, 2014, Pages 771-783

  Sahl, Steffen J ^b   Leutenegger, Marcel ^c   Hell, Stefan W ^a   Eggeling, Christian ^d  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b STANFORD UNIVERSITY   (United States)

^c EPFL   (Switzerland)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

confocal microscopy; lipid dynamics; nanoscopy; single molecule microscopy; super resolution

Indexed keywords

PROTON;

ANIMAL; ARTICLE; CONFOCAL MICROSCOPY; DIFFUSION; FLUORESCENCE; FLUORESCENCE MICROSCOPY; LIPID DYNAMICS; NANOSCOPY; SINGLE MOLECULE MICROSCOPY; SUPER-RESOLUTION;

CONFOCAL MICROSCOPY; LIPID DYNAMICS; NANOSCOPY; SINGLE MOLECULE MICROSCOPY; SUPER-RESOLUTION;

ANIMALS; DIFFUSION; FLUORESCENCE; MICROSCOPY, CONFOCAL; MICROSCOPY, FLUORESCENCE; PROTONS;

EID: 84896388110     PISSN: 14394235     EISSN: 14397641     Source Type: Journal    
DOI: 10.1002/cphc.201301090     Document Type: Article

References (50)

1. J. R. Lakowicz, Principles of Fluorescence Spectroscopy, 3rd ed., Springer, New York, 2006.
2. J. Lippincott-Schwartz, E. Snapp, A. Kenworthy, Nat. Rev. Mol. Cell Biol. 2001, 2, 444-456.
3. D. Axelrod, D. Koppel, J. Schlessinger, E. Elson, W. Webb, Biophys. J. 1976, 16, 1055-1069.
4. N. L. Thompson, T. P. Burghardt, D. Axelrod, Biophys. J. 1981, 33, 435-454.
5. C. A. Day, L. J. Kraft, M. Kang, A. K. Kenworthy, Curr. Protein Cytometry 2012, 2-19.
6. D. Magde, E. L. Elson, W. W. Webb, Biopolymers 1974, 13, 29-61.
7. E. Haustein, P. Schwille, Annu. Rev. Biophys. Biomol. Struct. 2007, 36, 151-169.
8. Z. Petrasek, J. Ries, P. Schwille, Methods Enzymol. 2010, 472, 317-343.
9. M. A. Digman, E. Gratton, Annu. Rev. Phys. Chem. 2011, 62, 645-668.
10. P. F. Lenne, L. Wawrezinieck, F. Conchonaud, O. Wurtz, A. Boned, X. J. Guo, H. Rigneault, H. T. He, D. Marguet, EMBO J. 2006, 25, 3245-3256.
11. D. L. Kolin, P. W. Wiseman, Cell Biochem. Biophys. 2007, 49, 141-164.
12. L. Kastrup, H. Blom, C. Eggeling, S. W. Hell, Phys. Rev. Lett. 2005, 94, 178104.
13. C. Eggeling, C. Ringemann, R. Medda, G. Schwarzmann, K. Sandhoff, S. Polyakova, V. N. Belov, B. Hein, C. von Middendorff, A. Schönle, S. W. Hell, Nature 2009, 457, 1159-1163.
14. C. Ringemann, B. Harke, C. von Middendorff, R. Medda, A. Honigmann, R. Wagner, M. Leutenegger, A. Schönle, S. W. Hell, C. Eggeling, New J. Phys. 2009, 11, 103054.
15. V. Mueller, C. Ringemann, A. Honigmann, G. Schwarzmann, R. Medda, M. Leutenegger, S. Polyakova, V. N. Belov, S. W. Hell, C. Eggeling, Biophys. J. 2011, 101, 1651-1660.
16. A. Honigmann, V. Mueller, S. W. Hell, C. Eggeling, Faraday Discuss. 2013, 161, 77-89.
17. F. Göttfert, C. A. Wurm, V. Mueller, S. Berning, V. C. Cordes, A. Honigmann, S. W. Hell, Biophys. J. 2013, 105, L01-L03.
18. K. Simons, M. J. Gerl, Nat. Rev. Mol. Cell Biol. 2010, 11, 688-699.
19. T. Fujiwara, K. Ritchie, H. Murakoshi, K. Jacobson, A. Kusumi, J. Cell Biol. 2002, 157, 1071-1081.
20. A. Kusumi, C. Nakada, K. Ritchie, K. Murase, K. Suzuki, H. Murakoshi, R. S. Kasai, J. Kondo, T. Fujiwara, Annu. Rev. Biophys. Biomol. Struct. 2005, 34, 351-378.
21. M. L. Kraft, Mol. Biol. Cell 2013, 24, 2765-2768.
22. H. Geerts, Biophys. J. 1987, 52, 775-782.
23. M. P. Sheetz, S. Turney, H. Qian, E. L. Elson, Nature 1989, 340, 284-288.
24. A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, P. R. Selvin, Science 2003, 300, 2061-2065.
25. M. Vrljic, S. Y. Nishimura, S. Brasselet, W. E. Moerner, H. M. McConnell, Biophys. J. 2002, 83, 2681-2692.
26. M. Vrljic, S. Y. Nishimura, W. E. Moerner, H. M. McConnell, Biophys. J. 2005, 88, 334-347.
27. S. Wieser, M. Moertelmaier, E. Fuertbauer, H. Stockinger, G. Schütz, Biophys. J. 2007, 92, 3719-3728.
28. K. Jaqaman, H. Kuwata, N. Touret, R. Collins, W. S. Trimble, G. Danuser, S. Grinstein, Cell 2011, 146, 593-606.
29. M. Clausen, B. C. Lagerholm, Curr. Protein Pept. Sci. 2011, 12, 699-713.
30. N. Bobroff, Rev. Sci. Instrum. 1986, 57, 1152-1157.
31. R. E. Thompson, D. R. Larson, W. W. Webb, Biophys. J. 2002, 82, 2775-2783.
32. S. J. Sahl, M. Leutenegger, M. Hilbert, S. W. Hell, C. Eggeling, Proc. Natl. Acad. Sci. USA 2010, 107, 6829-6834.
33. M. Leutenegger, R. Rao, R. A. Leitgeb, T. Lasser, Opt. Express 2006, 14, 11277-11291.
34. D. S. Martin, M. B. Forstner, J. A. Käs, Biophys. J. 2002, 83, 2109-2117.
35. T. Savin, P. S. Doyle, Biophys. J. 2005, 88, 623-638.
36. E. Abbe, Arch. Mikrosk. Anat. 1873, 9, 413-468.
37. S. W. Hell, Nat. Methods 2009, 6, 24-32.
38. S. W. Hell, J. Wichmann, Opt. Lett. 1994, 19, 780-782.
39. T. A. Klar, S. Jakobs, M. Dyba, A. Egner, S. W. Hell, Proc. Natl. Acad. Sci. USA 2000, 97, 8206-8210.
40. E. Betzig, G. H. Patterson, R. Sougrat, O. W. Lindwasser, S. Olenych, J. S. Bonifacino, M. W. Davidson, J. Lippincott-Schwartz, H. F. Hess, Science 2006, 313, 1642-1645.
41. S. T. Hess, T. P. K. Girirajan, M. D. Mason, Biophys. J. 2006, 91, 4258-4272.
42. M. J. Rust, M. Bates, X. Zhuang, Nat. Methods 2006, 3, 793-796.
43. J. Fölling, M. Bossi, H. Bock, R. Medda, C. A. Wurm, B. Hein, S. Jakobs, C. Eggeling, S. W. Hell, Nat. Methods 2008, 5, 943-945.
44. M. Heilemann, S. van de Linde, A. Mukherjee, M. Sauer, Angew. Chem. 2009, 121, 7036-7041
45. Angew. Chem. Int. Ed. 2009, 48, 6903-6908.
46. C. Steinhauer, C. Forthmann, J. Vogelsang, P. Tinnefeld, J. Am. Chem. Soc. 2008, 130, 16840-16841.
47. S. J. Sahl, W. E. Moerner, Curr. Opin. Struct. Biol. 2013, 23, 778-787.
48. R. Zondervan, F. Kulzer, S. B. Orlinskii, M. Orrit, J. Phys. Chem. A 2003, 107, 6770-6776.
49. K. Weber, T. Bibring, M. Osborn, Exp. Cell Res. 1975, 95, 111-120.
50. F. Huang, T. M. P. Hartwich, F. E. Rivera-Molina, Y. Lin, W. C. Duim, J. J. Long, P. D. Uchil, J. R. Myers, M. A. Baird, W. Mothes, M. W. Davidson, D. Toomre, J. Bewersdorf, Nat. Methods 2013, 10, 653-658.