Histone h1 structural changes and its interaction with dna in the presence of high glucose concentration in vivo and in vitro

Journal of Biomolecular Structure and Dynamics

Volumn 28, Issue 4, 2011, Pages 575-586

  Rahmanpour, Rahman ^a   Bathaie, S Zahra ^a  

^a TARBIAT MODARES UNIVERSITY   (Iran)

Author keywords

Chemical chaperone; Diabetes complication; DNA protein interaction; Protein misfolding; Small molecules

Indexed keywords

CHAPERONE; DNA; GLUCOSE; HISTONE; SPERMINE;

ANIMAL EXPERIMENT; ARTICLE; IN VITRO STUDY; IN VIVO STUDY; INCUBATION TIME; MALE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; RAT;

RATTUS;

EID: 78650941502     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2011.10508596     Document Type: Article

References (68)

1. Ahmed, N., 2005. Clin Practice, 67:3–21.
2. Brownlee, M., 1995. Clin Invest Med, 18:275–281.
3. Travers, A., Hiriart, E., Churcher, M., Caserta, M., and Di Mauro, E., 2010. J Biomol Struct Dyn, 27:713–724.
4. Xu, F., and Olson, W. K., 2010. J Biomol Struct Dyn, 27:725–739.
5. Trifonov, E. N., 2010. J Biomol Struct Dyn, 27:741–746.
6. De Santis, P., Morosetti, S., and Scipioni, A., 2010. J Biomol Struct Dyn, 27:747–764.
7. Babbitt, G. A., Tolstorukov, M. Y., and Kim, Y., 2010. J Biomol Struct Dyn, 27:765–780.
8. Clark, D. J., 2010. J Biomol Struct Dyn, 27:781–793.
9. Johnson, S. M., 2010. J Biomol Struct Dyn, 27:795–802.
10. Arya, G., Maitra, A., and Grigoryev, S. A., 2010. J Biomol Struct Dyn, 27:803–820.
11. Cui, F., and Zhurkin, V. B., 2010. J Biomol Struct Dyn, 27:821–841.
12. Wang, D., Ulyanov, N. B., and Zhurkin, V. B., 2010. J Biomol Struct Dyn, 27:843–859.
13. West, S. M., Rohs, R., Mann, R. S., and Honig, B., 2010. J Biomol Struct Dyn, 27:861–866.
14. Sereda, Y. V., and Bishop, T. C., 2010. J Biomol Struct Dyn, 27:867–887.
15. Gabdank, I., Barash, D., and Trifonov, E. N., 2009. J Biomol Struct Dyn, 26:403–411.
16. Hartman, P. G., Chapman, G. E., Moss, T., and Bradbury, E. M., 1977. Eur J Biochem, 77:45–51.
17. Chapman, G. E., Hartman, P. G., Cary, P. D., Bradbury, E. M., and Lee, D. R., 1978. Eur J Biochem, 86:35–44.
18. Ramakrishnan, V., Finch, J. T., Graziano, V., Lee, P. L., and Sweet, R. M., 1993. Nature, 362:219–223.
19. Cerf, C., Lippens, G., Ramakrishnan, V., Muyldermans, S., Segers, A., Wyns, L., Wodak, S. J., and Hallenga, K., 1994. Biochemistry, 33:11079–11086.
20. Vila, R., Ponte, I., Jiménez, M. A., Rico, M., and Suau, P., 2002. Protein Sci, 11:214–220.
21. Bathaie, S. Z., Moosavi-Movahedi, A. A., Ranjbar, B., and Saboury, A. A., 2003. Colloid Surf B:Biointer, 28:17–25.
22. Allan, J., Mitchell, T., Harborne, N., Bohm, L., and Crane-Robinson, C., 1986. J Mol Biol, 187:591–601.
23. Zlatanova, J., and van Hold, K., 1992. J Cell Sci, 103:889–895.
24. Wolffe, A. P., Khochbin, P. S., and Dimitrov, S., 1997. BioEssays, 19:249–255.
25. Bouvet, P., Dimitrov, S., and Wolffe, A. P., 1994. Genes Devel, 8:1147–1159.
26. Shen, X., and Gorovsky, M. A., 1996. Cell, 86:475–483.
27. Lee, H. L., and Archer, T. K., 1998. EMBO J, 17:1454–1466.
28. Vermaak, D., Steinbach, O. C., Dimitrov, S., Rupp, R. A. W., and Wolffe, A. P., 1998. Curr Biol, 8:533–536.
29. Dou, Y., Mizzen, C. A., Abrams, M., Allis, C. D., and Gorovsky, M. A., 1999. Mol Cell, 4:641–647.
30. Agardh, C. D., Stenram, U., Torffvit, O., and Agardh, E., 2002. J Diabetes Complicat, 16:395–400.
31. Jafarnejad, A., Bathaie, S. Z., Nakhjavani, M., Hassan, M. Z., and Banasadegh, S., 2008. Diabetes Metab Res Rev, 24:64–73.
32. Jafarnejad, A., Bathaie, S. Z., Nakhjavani, M., and Hassan, M. Z., 2008. Life Sci, 82:301–307.
33. Jafarnejad, A., Bathaie, S. Z., Nakhjavani, M., and Hassan, M. Z., 2008. J Pharm Exp Therap, 324:850–857.
34. Bai, C., Biwersi, J., Verkman, A. S., and Matthay, M. A., 1998. J Pharm Toxicol Methods, 40:39–45.
35. Perlmutter, D. H., 2002. Pediat Res, 52:832–836.
36. Harding, J. J., and Ganea, E., 2006. Biochim Biophys Acta, 1764:1436–1446.
37. Gugliucci, A., and Menini, T., 2003. Life Sci, 72:2603–2616.
38. Leal, L. I., 2004. Biomed Pharmacother, 58:598–604.
39. Mendez, J. D., and Balderas, F. L., 2006. Biomed Pharmacother, 60:26–31.
40. Welch, W. J., and Brown, C. R., 1996. Cell Stress & Chaperones, 1:109–15.
41. Mendez, J. D., and Ramos, G. H. B., 1994. Arch Med Res, 25:367–375.
42. Til, H. P., Falke, H. E., Prinsen, M. K., and Willems, M. I., 1997. Food Chem Toxicol, 35:337–48.
43. Ramirez, M. G., Leuba, S. H., and Ausio, J., 1990. Protein Express Purif, 1:40–44.
44. Laemmeli, U. K., 1970. Nature, 227:680–685.
45. Yanevat, J., Schroth, G. P., Van holde, K. E., and Zlatanova, J., 1995. Pro Natl Acad Sci USA, 92:7060–7064.
46. Bathaie, S. Z., Moosavi-movahedi, A. A., and Saboury, A. A., 1999. Nuc Acids Res, 27:1001–1005.
47. McFadyen, W. D., Sotirellis, N., Denny, W. A., and Wakelin, L. P. G., 1990. Biochim Biophys Acta, 1048:50–58.
48. Lane, D., Prentki, P., and Chandleri, M., 1992. Microbiol Rev, 56:509–528.
49. Gavilanes, J. G., Lizarbe, M. A., Munico, A. M., and Onadera, M., 1985. Int J Pept Prot Res, 26:187–194.
50. Clark, D. J., and Thomas, J., 1988. Eur J Biochem, 178:225–233.
51. Gugliucci, A., and Bendayan, M., 1995. Biochem Biophys Res Commun, 212:56–62.
52. Buche, A., Colson, P., and Houssier, C., 1993. J Biomol Struct Dyn, 11:95–119.
53. Fasman, G. D., Schaffhausen, B., Goldsmith, L., and Adler, A., 1970. Circular Dichroism studies. Biochemistry, 9:2814–2822.
54. Oque, A., Orrego, M., Ponte, I., and Suau, P., 2004. Nucl Acids Res, 32:6111–6119.
55. Nasiri, R., Bahrami, H., Zahedi, M., Moosavi-Movahedi, A. A., and Sattarahmady, N., 2010. J Biomol Struct Dyn, 28:211–226.
56. Talasz, H., Wasserer, S., and Puschendorf, B., 2002. J Cell Biochem, 85:24–34.
57. Ashrafi, M., Bathaie, S. Z., Taghikhani, M., and Moosavi-Movahedi, A. A., 2005. Int J Biol Macromol, 36:246–252.
58. Bathaie, S. Z., Sedghgoo, F., Jafarnejad, A., Farzami, B., and Khayatian, M., 2008. Spectrochim Acta A:Mol Biomol Spect, 71:803–808.
59. Hoshyar, R., Bathaie, S. Z., and Ashrafi, M., 2008. DNA and Cell Biology, 27:1–9.
60. Motamedi, M., Bathaie, S. Z., and Hemmateenejad, B., 2007. J Mol Struct (THEOCHEM), 806:205–211.
61. Jobst, K., and Lakatos, Á. 1996. Clin Chim Acta, 245:203–204.
62. Giardino, I., Edelstein, D., and Brownlee, M., 1994. J Clin Invest, 94:110–117.
63. Mendez, D. L., Jensen, R. A., McElroy, L. A., Pena, J. M., and Esquerra, R. M., 2005. Arch Biochem Biophys, 444:92–99.
64. Sattarahmady, N., Moosavi-Movahedi, A. A., Ahmad, F., and Hakimelahi, G. H., 2007. Biochim Biophys Acta, 1770:932–942.
65. Jordano, J., Barbero, J. L., Montero, F., and Franco, L., 1983. J Biol Chem, 258:315–320.
66. Barbero, J. L., Montero, F., and Franco, L., 1984. J Prot Chem, 3:455–463.
67. Zlatanova, J., and van Hola, K., 1996. Prog Nucl Acids Res, 52:217–259.
68. Watanabe, H., 1986. Nucl Acids Res, 14:3573–3585.