Bulletin of the Korean Chemical Society

  • 제35권11호
  • /
  • Pages.3369-3372
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  • 2014
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  • 0253-2964(pISSN)
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  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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Studies of Small Molecule Dyes that Interact with Pyrene-labeled Amyloid Fragments

  • Lee, Hyemin (Department of Chemistry and Nanoscience Global Top 5 Research Program, Ewha Womans University) ;
  • Lee, Hwiin (Department of Chemistry and Nanoscience Global Top 5 Research Program, Ewha Womans University) ;
  • Lee, Minyung (Department of Chemistry and Nanoscience Global Top 5 Research Program, Ewha Womans University)
  • 투고 : 2014.04.29
  • 심사 : 2014.07.26
  • 발행 : 2014.11.20
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참고문헌

  1. Sigurdsoon, E. M.; Calero, M.; Gasset, M. Amyloid Proteins: Methods and Protocols, 2nd ed.; Springer: 2012.
  2. Hamley, I. W. Chem. Rev. 2012, 112, 5147. https://doi.org/10.1021/cr3000994
  3. Otzen, D. E. Amyloid Fibrils and Perfibrillar Aggregates: Molecular and Biological Properties; Wiley-VCH: Germany, 2013; p 102.
  4. Sikorski, P.; Atkins, E. D.; Serpell, L. C. Structure 2003, 11, 915. https://doi.org/10.1016/S0969-2126(03)00149-7
  5. Petkova, A. T.; Buntkowsky, G.; Dyda, F.; Leapman, R. D.; Yau, W. M.; Tycko, R. J. Mol. Biol. 2004, 335, 247. https://doi.org/10.1016/j.jmb.2003.10.044
  6. Kim, J.; Lee, M. Biochem. Biophys. Res. Commun. 2004, 316, 393. https://doi.org/10.1016/j.bbrc.2004.02.059
  7. Boucher, G.; Mousseau, N.; Derreumaux, P. Proteins 2006, 65, 877. https://doi.org/10.1002/prot.21134
  8. Negureanu, L.; Baumketner, A. J. Mol. Biol. 2009, 389, 921. https://doi.org/10.1016/j.jmb.2009.04.058
  9. Lehrer, S. S. Biochem. 1995, 24, 115.
  10. Bains, G.; Patel, A. B.; Narayanawami, V. Molecules 2011, 16, 7909. https://doi.org/10.3390/molecules16097909
  11. Lakowicz, J. R. Principles of Fluorescence Spectroscopy, 3rd ed.; Springer: 2006.
  12. Yang, F.; Lim, G. P.; Begum, A. N.; Ubeda, O. J.; Simmons, M. R.; Ambeqaokar, S. S.; Chen, P. P.; Kayed, R.; Glabe, C. G.; Frautschy, S. A.; Cole, G. M. J. Biol. Chem. 2005, 280, 5892. https://doi.org/10.1074/jbc.M404751200
  13. Anand, P.; Kunnumakkara, A. B.; Newman, R. A.; Aggarwal, B. B. Mol. Pharmaceutics 2007, 4, 807. https://doi.org/10.1021/mp700113r
  14. Priyadarsini, K. I. J. Photochem. Photobiol. C 2009, 10, 81. https://doi.org/10.1016/j.jphotochemrev.2009.05.001
  15. Howlett, D.; Cutler, P.; Heales, S.; Camilleri, P. FEBS Lett. 1997, 417, 249. https://doi.org/10.1016/S0014-5793(97)01290-8
  16. Li, B.; Qin, C.; Wang, L.; Dong, S. Anal. Chem. 2009, 81, 3544. https://doi.org/10.1021/ac900110a
  17. Chuang, J. Y.; Lee, C. W.; Shih, Y. H.; Yang, T.; Yu, L.; Kuo, Y. M. PLoS One 2012, 7, e33120. https://doi.org/10.1371/journal.pone.0033120
  18. Bandara, H. M.; Burdette, S. C. Chem. Soc. Rev. 2012, 41, 1809. https://doi.org/10.1039/c1cs15179g
  19. Matveeva, E. G.; Rudolph, A.; Moll, J. R.; Thompson, R. B. ACS Chem. Neurosci. 2012, 3, 982. https://doi.org/10.1021/cn3001262
  20. Duhamel, J. Langmuir 2012, 28, 6527. https://doi.org/10.1021/la2047646
  21. Khurana, R.; Coleman, C.; Ionescu-Zanetti, C.; Carter, S. A.; Krishna, V.; Grover, R. K.; Roy, R.; Singh, S. J. Struct. Biol. 2005, 151, 229. https://doi.org/10.1016/j.jsb.2005.06.006
  22. Krebs, M. R. H. J. Struct. Biol. 2005, 149, 30. https://doi.org/10.1016/j.jsb.2004.08.002
  23. Levine, H. Amyloid 2007, 14, 185. https://doi.org/10.1080/13506120701461020
  24. Maezawa, I.; Hong, H.; Liu, R.; Chun, W.; Cheng, R. H.; Kung, M.; Kung, H.; Lam, K.; Oddo, S.; La, F. M.; Lee, J. J. Neurochem. 2008, 104, 458.
  25. Hamaguchi, T.; Ono, K.; Yamada, M. Cell Mol. Life Sci. 2006, 63, 1538. https://doi.org/10.1007/s00018-005-5599-9
  26. Necula, M.; Kayed, R.; Milton, S.; Glabe, C. G. J. Biol. Chem. 2007, 282, 10311. https://doi.org/10.1074/jbc.M608207200