- 1) Hammond, C. and Helenius, A., Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell. Biol., 156, 41-52 (1994).
- 2) Bergeron, J. J., Brenner, M. B., Thomas, D. Y. and Williams, D. B. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends. Biochem. Sci., 19, 124-128 (1994).
- 3) Hammond, C., Braakman, I., and Helenius, A., Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control., Proc. Natl. Acad. Sci. USA, 91, 913-917 (1994).
- 4) Ora, A. and Helenius, A., Calnexin fails to associate with substrate proteins in glucosidase- deficient cell lines. J. Biol. Chem., 270, 26060-26062 (1995).
- 5) Ware, F. E., Vassilakos, A., Peterson, P. A., Jackson, M. R., Lehrman, M. A., and Williams, D. B., The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem., 270, 4697-4704 (1995).
- 6) Wada, I., Rindress, D., Cameron, P. H., Ou, W. J., Doherty, J. J., II, Louvard, D., Bell, A. W., Dignard, D., Thomas, D. Y., and Bergeron, J. J. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol. Chem., 266, 19599-19610 (1991).
- 7) David, V., Hochstenbach, F., Rajagopalan, S., and Brenner, M. B., Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J. Biol. Chem., 268, 9585-9592 (1993).
- 8) Ives, H. E., Yee, V. J., and Warnock, D. G., Asymmetric distribution of the Na+/H+-antiporter in the renal proximal tubule epithelial cell. J. Biol. Chem., 258, 13513-13516 (1983).
- 9) Yamashita, T. and Kawakita, M., Reconstitution of Na+/H+-antiporter of bovine renal brush-border membrane into proteoliposomes and detection of a 110 kDa protein cross-reactive with antibodies against a human Na+/H+-antiporter partial peptide in antiport-active fractions after partial fractionation. J. Biochem., 111, 162-167 (1992).
- 10) Harlow, E. and Lane, D., Antibodies-A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N. Y., pp. 521-523 (1988).
- 11) Ou, W. J., Thomas, D. Y., Bell, A. W., and Bergeron, J. J. Casein kinase II phosphorylation of signal sequence receptor alpha and the associated membrane chaperone calnexin. J. Biol. Chem., 267, 23789-23796 (1992).
- 12) Wong, H. N., Ward, M. A., Bell, A. W., Chevet, E., Bains, S., Blackstock, W. P., Solari, R., Thomas, D. Y., and Bergeron, J. J. Conserved in vivo phosphorylation of calnexin at casein kinase II sites as well as a protein kinase C/proline-directed kinase site. J. Biol. Chem., 273, 17227-17235 (1998).
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Immunoaffinity Purification and Identification of the Molecular Chaperone Calnexin
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