Bulletin of the Korean Chemical Society

  • 제32권2호
  • /
  • Pages.731-734
  • /
  • 2011
  • /
  • 0253-2964(pISSN)
  • /
  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
권호 표지
DOI QR코드

DOI QR Code

Molecular Dynamics Simulations of Prion Peptides: Effect of Glycosylation

  • Choi, Young-Jin (BioChip Research Center, Hoseo University) ;
  • Kim, Hyun-Myung (Department of Advanced Technology Fusion, Konkuk University) ;
  • Hwang, Sun-Tae (Department of Computer Science, Kookmin University) ;
  • Jeong, Karp-Joo (Department of Advanced Technology Fusion, Konkuk University) ;
  • Jung, Seun-Ho (Research Institute for Ubiquitous Information Technologies and Applications (UBITA), Konkuk University)
  • 투고 : 2010.11.16
  • 심사 : 2010.12.14
  • 발행 : 2011.02.20
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

키워드

참고문헌

  1. Wang, C.; Eufemi, M.; Turano, C.; Giartosio, A. Biochemistry 1996, 35, 7299. https://doi.org/10.1021/bi9517704
  2. Liang, F.; Chen, R.; Lin, C.; Huang, K.; Chan, S. Biochem. Biophys. Res. Commun. 2006, 342, 482. https://doi.org/10.1016/j.bbrc.2006.01.168
  3. Spiriti, J.; Bogani, F.; van der Vaart, A.; Ghirlanda, G. Biophys. Chem. 2008, 134, 157. https://doi.org/10.1016/j.bpc.2008.02.005
  4. Westermark, G. T.; Westermark, P. Trend. Mol. Med. 2010, 16, 501. https://doi.org/10.1016/j.molmed.2010.08.004
  5. Chen, P.; Lin, C.; Chang, Y.; Lin, S.; Chan, S. Proc. Natl. Acad. Sci. USA 2002, 99, 12633. https://doi.org/10.1073/pnas.192137799
  6. Ho, C.; Lee, L.; Huang, K.; Lin, C.; Ku, M.; Yang, C.; Chan, S.; Hsu, R.; Chen, R. Proteins 2009, 76, 213. https://doi.org/10.1002/prot.22341
  7. Prusiner, S. B. Science 1982, 216, 136. https://doi.org/10.1126/science.6801762
  8. Caughey, B. W.; Dong, A.; Bhat, K. S.; Ernst, D.; Hayes, S. F.; Caughey, W. S. Biochemistry 1991, 30, 7672. https://doi.org/10.1021/bi00245a003
  9. Kaneko, K.; Ball, H. L.; Wille, H.; Zhang, H.; Groth, D.; Torchia, M.; Tremblay, P.; Safar, J.; Prusiner, S. B.; DeArmond, S. J.; Baldwin, M. A.; Cohen, F. E. J. Mol. Biol. 2000, 295, 997. https://doi.org/10.1006/jmbi.1999.3386
  10. Kaneko, K.; Peretz, D.; Pan, K. M.; Blochberger, T. C.; Wille, H.; Gabizon, R.; Griffith, O. H.; Cohen, F. E.; Baldwin, M. A.; Prusiner, S. B. Proc. Natl. Acad. Sci. USA 1995, 92, 11160. https://doi.org/10.1073/pnas.92.24.11160
  11. Zhang, H.; Kaneko, K.; Nguyen, J. T.; Livshits, T. L.; Baldwin, M. A.; Cohen, F. E.; James, T. L.; Prusiner, S. B. J. Mol. Biol. 1995, 250, 514. https://doi.org/10.1006/jmbi.1995.0395
  12. James, T. L.; Liu, H.; Ulyanov, N. B.; Farr-Jones, S.; Zhang, H.; Donne, D. G.; Kaneko, K.; Groth, D.; Mehlhorn, I.; Prusiner, S. B.; Cohen, F. E. Proc. Natl. Acad. Sci. USA 1997, 94, 10086. https://doi.org/10.1073/pnas.94.19.10086
  13. Lipfert, J.; Franklin, J.; Wu, F.; Doniach, S. J. Mol. Biol. 2005, 349, 648. https://doi.org/10.1016/j.jmb.2005.03.083
  14. Jang, S.; Shin, S. J. Phys. Chem. B Lett. 2006, 110, 1955. https://doi.org/10.1021/jp055568e
  15. Simone, A. D.; Esposito, L.; Pedone, C.; Vitagliano, L. Biophys. J. 2008, 95, 1965. https://doi.org/10.1529/biophysj.108.129213
  16. Zhuang, W.; Sgourakis, N. G.; Li, Z.; Garcia, A. E.; Mukamel, S. Proc. Natl. Acad. Sci. USA 2010, 107, 15687. https://doi.org/10.1073/pnas.1002131107
  17. Kannan, S.; Zacharias, M. J. Struct. Biol. 2009, 166, 288. https://doi.org/10.1016/j.jsb.2009.02.015
  18. Sanchez, N.; Pallarés, I.; Aviles, F.; Vendrell, J.; Ventura, S. BMC Struct Biol. 2005, 5, 18. https://doi.org/10.1186/1472-6807-5-18
  19. Case, D. A.; Cheatham, T. E., III.; Darden, T.; Gohlke, H.; Luo, R.; Merz, K. M., Jr.; Onufriev, A.; Simmerling, C.; Wang, B.; Woods, R. J. Computat. Chem. 2005, 26, 1668. https://doi.org/10.1002/jcc.20290
  20. Kirschner, K. N.; Yongye, A. B.; Tschampel, S. M.; Daniels, C. R.; Foley, B. L.; Woods, R. J. J. Comput. Chem. 2008, 29, 622. https://doi.org/10.1002/jcc.20820
  21. Pitera, J. D.; Swope, W. Proc. Natl. Acad. Sci. USA 2003, 100, 7587. https://doi.org/10.1073/pnas.1330954100
  22. Jorgensen, W. L. J. Chem. Phys. 1982, 77, 4156. https://doi.org/10.1063/1.444325
  23. Darden, T.; York, D.; Pedersen, L. J. Chem. Phys. 1993, 98, 10089. https://doi.org/10.1063/1.464397
  24. Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. J. Comput. Phys. 1977, 23, 327. https://doi.org/10.1016/0021-9991(77)90098-5

피인용 문헌

  1. A Structural Model of Glycosylated Neuraminidase Based on Molecular Dynamics Simulations for Virtual Inhibitor Screening Against Influenza Virus vol.33, pp.3, 2011, https://doi.org/10.5012/bkcs.2012.33.3.1059