Homology models of the yersinia pseudotuberculosis and yersinia pestis general porins and comparative analysis of their functional and antigenic regions

Journal of Biomolecular Structure and Dynamics

Volumn 23, Issue 2, 2005, Pages 163-174

  Likhatskaya, G N ^a   Solov'eva, T F ^a   Novikova, O D ^a   Issaeva, M P ^a   Gusev, K V ^a   Kryzhko, I B ^b   Trifonov, E V ^b   Nurminski, E A ^b  

^a RUSSIAN ACADEMY OF SCIENCES   (Russian Federation)

^b INSTITUTE OF AUTOMATION AND CONTROL PROCESSES   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; GLUTAMIC ACID; PENTAPEPTIDE; PORIN; PROLYLGLUTAMYLPHENYLALANYLGLYCYLGLYCYLASPARTIC ACID; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SEQUENCE; ANTIGENICITY; ARTICLE; COMPARATIVE STUDY; CROSS REACTION; ESCHERICHIA COLI; MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SEQUENCE ANALYSIS; STRUCTURAL HOMOLOGY; YERSINIA PESTIS; YERSINIA PSEUDOTUBERCULOSIS;

ENTEROBACTERIACEAE; YERSINIA; YERSINIA PESTIS; YERSINIA PSEUDOTUBERCULOSIS;

EID: 25144499658     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2005.10507056     Document Type: Article

References (52)

1. Nikaido, H., 2003. Microbiol. Mol. Biol. Rev., 67:593–656.
2. Jap, B. K., and Walian, P. J., 1996. Physiol. Rev., 76:1073–1088.
3. Galdiero, M., Vitiello, M., and Galdiero, S., 2003. FEMS Microbiol. Letters, 226:57–64.
4. Cowan, S. W., Schrimer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., Jansonius, J. N., and Rosenbusch, J. P., 1992. Nature, 358:727–733.
5. Arockiasamy, A., and Krishnaswamy, S., 2000. J. Biomolec. Struct. Dyn., 18:261–271.
6. Alberti, S., Rodriquez-Quinones, F., Schirmer, T., Rummel, G., Tomas, J. M., and Rosenbusch, J. P., 1995. Infect. Immun., 63:903–910.
7. Brubaker, R. R., 1972. Curr. Top. Microbiol. Immunol., 57:111–158.
8. Parkhill, J., Wren, B. W., Thomson, N. R., Titball, R. W., and et al. 2001. Nature, 413:523–527.
9. Likhatskaya, G. N., Novikova, O. D., Solovjeva, T. F., and Ovodov, Yu. S., 1985. Biol. Membrany (Russian), 2:1218–1224.
10. Novikova, O. D., Frolova, G. M., Vakorina, T. I., Tarankova, Z. A., Glasunov, V. P., Solovjeva, T. F., and Yu, S., 1989. Ovodov, Bioorg. Khim. (Russian), 15:763–772.
11. Isaeva, M. P., Novikova, O. D., Solov'eva, T. F., Rasskasov, V. A., and Degtyarev, S. Kh., 2003. Adv. Exp. Med. Biol., 529:257–260.
12. Chains, P. S. G., Carniel, E., Larimer, F. W., Lamerdin, J., Stoutland, P. O., Regala, W. M., Georgescu, A. M., Vergez, L. M., Land, M. L., Motin, V. L., Brubacker, R. R., Fowler, J., Hinnebusch, J., Marceau, M., Medigue, C., Simonet, M., Chenal-Francisque, V., Souza, B., Dacheux, D., Elliott, J. M., Derbise, A., Hauser, L. J., and Garcia, E., 2004. Proc. Natl. Acad. Sci. USA, 103:13826–13831.
13. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., and Bourne, P. E., 2000. Nucleic Acids Research., 28:235–242.
14. Kelley, L. A., MacCallum, R. M., and Sternberg, M. J. E., 2000. J. Mol. Biol., 299:499–520.
15. Guex, N., and Peitsch, M. C., 1997. Electrophoresis, 18:2714–2723.
16. Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C., 2003. Nucleic Acids Research, 31:3381–3385.
17. Peitsch, M. C., 1995. Bio/Technology, 13:658–660.
18. Hooft, R. W. W., Vriend, G., Sander, C., and Abola, E. E., 1996. Nature, 381:272
19. Koradi, R., Billeter, M., and Wethrich, K., 1996. J. Mol. Graphics, 14:51–55.
20. van Gunsteren, W. F., Billeter, S. R., Eising, A. A., Hünenberger, P. H., Krüger, P., Mark, A. E., Scott, W. R. P., and Tironi, I. G., 1996. Biomolecular Simulation:The GROMOS96 Manual and User Guide. Zürich, Groningen:VdF:Hochschulverlag AG an der ETH Zürich and BIOMOS b.v.
21. Lindahl, E., Hess, B., and van der Spoel, D., 2001. J. Mol. Mod., 7:306–317.
22. Sayle, R. A., and Milner, E. J., 1995. White Trends in Biochemical Sciences, 20:374–376.
23. Smart, O. S., Goodfellow, J. M., and Wallace, B. A., 1993. Biophys. J., 65:2455–2460.
24. Smart, O. S., Breed, J., Smith, G. R., and Sansom, M. S.P., 1997. Biophys. J., 72:1109–1126.
25. Tommassen, J., 1988. Membrane Biogenesis. 351–373. Heidelberg, Germany:Springer-Verlag.
26. Tieleman, D. P., and Berendsen, H. J. C., 1998. Biophysical J., 74:2786–2801.
27. Muller, D. J., and Engel, A., 1999. J. Mol. Biol., 285:92–94.
28. Novikova, O. D., Likhatskaya, G. N., Frolova, G. M., Vostrikova, O. P., Khomenko, V. A., Timchenko, N. F., and Solov'eva, T. F., 1990. Ovodov, Biol. Membrany (Russian)., 7:453–461. Yu. S
29. Provencher, C. W., and Glöcker, J., 1981. Biochemistry, 20:33–37.
30. Jeanteur, D., Lakey, J. H., and Pattus, F., 1991. Mol. Microbiol., 5:2153–2164.
31. Phale, P. S., Philippsen, A., Widmer, C., Phale, V. P., Rosenbusch, J. P., and Schirmer, T., 2001. Biochemistry, 40:6319–6325.
32. Phale, P. S., Schirmer, T., Prilipov, A., Lou, K.-L., Hardmeyer, A., and Rosenbusch, J. P., 1997. Proc. Natl. Acad. Sci. USA, 94:6741–6745.
33. Karshikoff, A., Spassov, V., Cowan, S. W., Ladenstein, R., and Schirmer, T., 1994. J. Mol. Biol., 240:372–384.
34. Liu, N., and Delcour, A. H., 1998. Protein Engineering, 9:797–802.
35. Samartzidou, H., and Delcour, A. H., 1999. J. Bacteriol., 181:791–798.
36. Todt, J. C., Rocque, W. J., and McGroarty, E. J., 1992. Biochemistry, 31:10471–10478.
37. Iyer, R., Wu, Z., Woster, P. M., and Delcour, A. H., 2000. J. Mol. Biol., 297:933–945.
38. Liu, N., and Delcour, A. H., 1998. FEBS Lett., 434:160–164.
39. Lugtenberg, B., and Van Alphen, L., 1983. Biochim. Biophys. Acta, 737:51–115.
40. Vostrikova, O. P., Novikova, O. D., Kim, N. Yu., Likhatskaya, G. N., and Solov'eva, T. F., 2003. Adv. Exp. Med. Biol., 529:261–263.
41. Fourel, D., Mizushima, S., Bernadac, A., and Pages, J.-M., 1993. J. Bacteriol., 175:2754–2757.
42. Van Gelder, P., and Tommassen, J., 1996. J. Bacteriol., 178:5320–5322.
43. Struyve, M., Moons, M., and Tomassen, C., 1991. J. Molec. Biol., 218:141–148.
44. Bosch, D., Scholten, M., and Tomassen, C., 1989. J. Molec. Genet., 216:144–148.
45. Fourel, D., Mizushima, S., Bernadac, A., and Pages, J.-M., 1993. J. Bacteriol., 175:2754–2757.
46. Benson, S. A., Occi, J. L. L., and Sampson, B. A., 1988. J. Molec. Biol., 203:960–971.
47. Rocque, W. J., and McGroarty, E. J., 1990. Biochemistry, 29:5344–5351.
48. Phale, R. S., Phillpsen, A., Keifhaber, T., Koebnik, R., Phale, V. P., Schirmer, T., and Rosenbusch, J. P., 1998. Biochemistry, 37:15663–15670.
49. Karle, I. L., 1999. J. Mol. Struct., 474:103–112.
50. Portnyagina, O. Yu., Novikova, O. D., Vostrikova, O. P., and Solovjeva, T. F., 1999. Byul. Eksp. Biol. Med. (Russian), 128:437–440.
51. Darmov, I. V., Marakulin, I. V., Pogorelsky, I. P., Novikova, O. D., Portnyagina, O. Yu., and Solovjeva, T. F., 1999. Byul. Eksp. Biol. Med. (Russian), 127:221–223.
52. Williams, K. M., Bigley, E. C., and Raybourne, R. B., 2000. Infect. Immun., 68:2535–2545. J. Paniagua-Solis, V. Sanchez, V. Oritz-Navarrete, C. R. Gonzalez, and A. Isibasi. FEMS Microbiol. Lett. 141, 31–36 (1996)