Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Urea-Driven Conformational Changes in Surface-Bound Superoxide Dismutase

  • Kang, Tae-Wook (Department of Chemical and Biomolecular Engineering, Sogang University) ;
  • Hong, Su-Rin (School of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University) ;
  • Choi, In-Hee (School of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University) ;
  • Sung, Jung-Joon (Department of Neurology, Seoul National University Hospital) ;
  • Yi, Jong-Heop (School of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University)
  • Published : 2008.08.20
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References

  1. Phizicky, E.; Bastiaens, P. I.; Zhu, H.; Snyder, M.; Fields, S. Nature 2003, 422, 208 https://doi.org/10.1038/nature01512
  2. Zhang, K.; Diehl, M. R.; Tirrell, D. A. J. Am. Chem. Soc. 2005, 27, 10136
  3. MacBeath, G.; Schreiber, S. L. Science 2000, 289, 1760
  4. Haab, B. B.; Dunham, M. J.; Brown, P. O. Genome Biol. 2001, 2, 1
  5. Nielsen, U. B.; Cardone, M. H.; Sinskey, A. J.; MacBeath, G.; Sorger, P. K. Proc. Natl. Acad. Sci. USA 2003, 100, 9330 https://doi.org/10.1073/pnas.1633513100
  6. Zhu, H.; Snyder, M. Curr. Opin. Chem. Biol. 2003, 7, 55 https://doi.org/10.1016/S1367-5931(02)00005-4
  7. Sadana, A. Chem. Rev. 1992, 92, 1799 https://doi.org/10.1021/cr00016a006
  8. Chah, S.; Kumar, C. V.; Hammond, M. R.; Zare, R. N. Anal. Chem. 2004, 76, 2112 https://doi.org/10.1021/ac035416k
  9. Lindberg, M. J.; Normark, J.; Holmgren, A.; Oliveberg, M. Proc. Natl. Acad. Sci. USA 2004, 101, 15893
  10. Baskakov, I. V.; Legname, G.; Prusiner, S. B.; Cohen, F. E. J. Biol. Chem. 2001, 276, 19687 https://doi.org/10.1074/jbc.C100180200
  11. Gupta, R.; Ahmad, F. Biochemistry 1999, 38, 2471 https://doi.org/10.1021/bi982078m
  12. Harper, S. M.; Neil, L. C.; Gardner, K. H. Science 2003, 301, 1541 https://doi.org/10.1126/science.1086810
  13. Eliezer, D.; Jennings, P. A.; Wright, P. E.; Doniach, S.; Hodgson, K. O.; Tsuruta, H. Science 1995, 270, 487 https://doi.org/10.1126/science.270.5235.487
  14. Ohba, S.; Hosomi, H.; Ito, Y. J. Am. Chem. Soc. 2001, 123, 6349 https://doi.org/10.1021/ja0034287
  15. Rischel, C.; Poulsen, F. M. FEBS Lett. 1995, 374, 105 https://doi.org/10.1016/0014-5793(95)01087-U
  16. Cole, N. B.; Murphy, D. D.; Grider, T.; Rueter, S.; Brasaemle, D.; Nussbaum, R. L. J. Biol. Chem. 2002, 277, 6344 https://doi.org/10.1074/jbc.M108414200
  17. Rosen, D. R.; Siddique, T.; Patterson, D.; Figlewicz, D. A.; Sapp, P.; Hentati, A.; Donaldson, D.; Goto, J. Nature 1993, 362, 59 https://doi.org/10.1038/362059a0
  18. Julien, J. P. Cell 2001, 104, 581 https://doi.org/10.1016/S0092-8674(01)00244-6
  19. Rakhit, R.; Crow, J. P.; Lepock, J. R.; Kondejewski, L. H.; Cashman, N. R.; Chakrabartty, A. J. Biol. Chem. 2004, 279, 15499 https://doi.org/10.1074/jbc.M313295200
  20. Stathopulos, P. B.; Rumfeldt, J. A. O.; Scholz, G. A.; Irani, R. A.; Frey, H. E.; Hallewell, R. A.; Lepock, J. R.; Meiering, E. M. Proc. Natl. Acad. Sci. USA 2003, 100, 7021 https://doi.org/10.1073/pnas.1237797100
  21. Aliyev, E.; Sakall o lu, U.; Eren, Z.; Aç kgoz, G. Biomaterials 2004, 25, 4633
  22. Knoll, W. Annu. Rev. Phys. Chem. 1998, 49, 569 https://doi.org/10.1146/annurev.physchem.49.1.569
  23. Roy, D.; Fendler, J. H. Adv. Mater. 2004, 16, 479 https://doi.org/10.1002/adma.200306195
  24. Chah, S.; Fendler, J. H.; Yi, J. Chem. Commun. 2002, 2094
  25. Kang, T.; Moon, J.; Oh, S.; Hong, S.; Chah, S.; Yi, J. Chem. Commun. 2005, 2360
  26. Chah, S.; Yi, J.; Pettit, C. M.; Roy, D.; Fendler, J. H. Langmuir 2002, 18, 314 https://doi.org/10.1021/la011226y
  27. Kang, T.; Hong, S.; Moon, J.; Oh, S.; Yi, J. Chem. Commun. 2005, 3721
  28. Wischerhoff, E.; Zacher, T.; Laschewsky, A.; Rekai, E. D. Angew. Chem. Int. Ed. 2003, 39, 4602 https://doi.org/10.1002/1521-3773(20001215)39:24<4602::AID-ANIE4602>3.0.CO;2-E
  29. Ekgasit, S.; Thammacharoen, C.; Knoll, W. Anal. Chem. 2004, 76, 561 https://doi.org/10.1021/ac035042v
  30. Sota, H.; Hasegawa, Y. Anal. Chem. 1998, 70, 2019 https://doi.org/10.1021/ac9713666
  31. Kang, T.; Hong, S.; Kim, H. J.; Moon, J.; Oh, S.; Paik, S. R.; Yi, J. Langmuir 2006, 22, 13 https://doi.org/10.1021/la052276w
  32. Zacher, T.; Wischerhoff, E. Langmuir 2002, 18, 1748 https://doi.org/10.1021/la0155707
  33. Boissinot, M.; Karnas, S.; Lepock, J. R.; Cabelli, D. E.; Tainer, J. A.; Getzoff, E. D.; Hallewell, R. A. EMBO J. 1997, 16, 2171 https://doi.org/10.1093/emboj/16.9.2171
  34. Su, X.; Wu, Y. J.; Robelek, R.; Knoll, W. Langmuir 2005, 21, 348 https://doi.org/10.1021/la047997u
  35. Lahiri, J.; Isaacs, L.; Tien, J.; Whitesides, G. M. Anal. Chem. 1999, 71, 777 https://doi.org/10.1021/ac980959t
  36. Tian, Y.; Mao, L.; Okajima, T.; Ohsaka, T. Anal. Chem. 2004, 76, 4162 https://doi.org/10.1021/ac049707k
  37. Tian, Y.; Mao, L.; Okajima, T.; Ohsaka, T. Anal. Chem. 2002, 74, 2428 https://doi.org/10.1021/ac0157270
  38. Sarkar, D.; Somasundara, P. Langmuir 2004, 20, 4657 https://doi.org/10.1021/la035727q
  39. Tainer, J. A.; Getzoff, E. D.; Beem, K. M.; Richardson, D. C. J. Mol. Biol. 1982, 160, 181 https://doi.org/10.1016/0022-2836(82)90174-7
  40. Gehr, R. J.; Boyd, R. W. Chem. Mater. 1996, 8, 1807 https://doi.org/10.1021/cm9600788
  41. Chah, S.; Hammond, M. R.; Zare, R. N. Chem. Biol. 2005, 12, 323 https://doi.org/10.1016/j.chembiol.2005.01.013
  42. Lynch, S. M.; Boswell, S. A.; Colón, W. Biochemistry 2004, 43, 16525 https://doi.org/10.1021/bi048831v
  43. Khare, S. D.; Ding, F.; Dokholyan, N. V. J. Mol. Biol. 2003, 334, 515 https://doi.org/10.1016/j.jmb.2003.09.069

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