Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity

Biochemical Journal

Volumn 328, Issue 3, 1997, Pages 841-846

  Song, Jiu Li ^a   Quan, Hui ^a   Wang, Chih Chen ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; LYSOZYME; PROTEIN DISULFIDE ISOMERASE;

ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; IONIC STRENGTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION;

ANIMALIA;

EID: 0031438770     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3280841     Document Type: Article

References (29)

1. Freedman, R. B., Hirst, T. R. and Tuite, M. F. (1994) Trends Biochem. Sci. 19, 331-336
2. Gething, M. J. and Sambrook, J. (1992) Nature (London) 355, 33-45
3. Noiva, R. (1994) Protein Expression Purif. 5, 1-13
4. Noiva, R. and Lennarz, W. J. (1992) J. Biol. Chem. 267, 3553-3556
5. Koivu, J., Myllyla, R., Hellakoski, T., Pihlajaniemi, T., Tasanen, K. and Kivirikko, K. I. (1987) J. Biol. Chem. 262, 6447-6449
6. Wetterau, J. R., Combs, J. R., Spinner, S. N. and Joiner, B. J. (1990) J. Biol. Chem. 265, 9800-9807
7. Noiva, R., Kimura, H., Roos, J. and Lennarz, W. J. (1991) J. Biol. Chem. 266, 19645-19649
8. Hayano, T., Hirose, M. and Kikuchi, M. (1995) FEBS Lett. 377, 505-511
9. Otsu, M., Omura, F., Yoshimori, T. and Kikuchi, M. (1994) J. Biol. Chem. 269, 6874-6877
10. Vuori, K., Pihlajaniemi, T., Myllyla, R. and Kivirikko, K. I. (1992) EMBO J. 11, 4213-4217
11. Lamberg, A., Jauhiainen, M., Metso, J., Ehnholm, C., Shoulders, C., Scott, J., Pihlajaniemi, T. and Kivirikko, K. I. (1996) Biochem. J. 315, 533-536
12. Ellis, R. J. (1993) Philos. Trans. R. Soc. London Ser. B Biol. Sci. 339, 257-261
13. Wang, C. C. and Tsou, C. L. (1993) FASEB J. 7, 1515-1517
14. Wang, C. C. (1997) Prolyl Hydroxylase, Protein Disulfide Isomerase, and Other Structurally Related Proteins (Guzman, N. A., ed,), pp. 315-359, Marcel Dekker, New York
15. Cai, H., Wang, C. C. and Tsou, C. L. (1994) J. Biol. Chem. 269, 24550-24552
16. Song, J. L. and Wang, C. C. (1995) Eur. J. Biochem. 231, 312-316
17. Puig, A. and Gilbert, H. F. (1994) J. Biol. Chem. 269, 7764-7771
18. Yao, Y., Zhou, Y. C. and Wang, C. C. (1997) EMBO J. 16, 651-658
19. Lilie, H., McLaughlin, S., Freedman, R. B. and Buchner, J. (1994) J. Biol. Chem. 269, 14290-14296
20. Puig, A., Lyles, M. M., Noiva, R. and Gilbert, H. F. (1994) J. Biol. Chem. 269, 19128-19135
21. Primm, T. P., Walker, K. W. and Gilbert, H. F. (1996) J. Biol. Chem. 271, 33664-33669
22. Quan, H., Fan, G. B. and Wang, C. C. (1995) J. Biol. Chem. 270, 17077-17079
23. Lambert, N. and Freedman, R. B. (1983) Biochem. J. 213, 225-234
24. Hwang, C., Sinskey, A. J. and Lodish, H. F. (1992) Science 257, 1496-1502
25. Goldberg, M., Rudolph, R. and Jaenicke, R. (1991) Biochemistry 30, 2790-2797
26. Noiva, R., Freedman, R. B. and Lennarz, W. J. (1993) J. Biol. Chem. 268, 19210-19217
27. Dai, Y. and Wang, C.-c. (1997) J. Biol. Chem. 272, in the press
28. Raman, B., Ramakrishna, T. and Rao, Ch. M. (1996) J. Biol. Chem. 271, 17067-17072
29. Rothwarf, D. M. and Scheraga, H. A. (1993) Biochemistry 32, 2690-2697