Chaperone calnexin

Hasenfratz, M.P., Jeltsch, J.M., Michalak, M., and Durst, F., Cloning and characterization of a wounding-induced analog of the chaperone calnexin from Helianthus tuberosus, Plant Physiol. Biochem., 35, 553-564, 1997. 

Another chaperone, calnexin, is a 90 kDa Ca +-binding protein and is an integral membrane phosphoprotein of ER. Calnexin monitors the export of newly synthesized glycoproteins by complexing with misfolded glycoproteins that have undergone glycosylation (Chapter 16). If a protein... 

Beauregard PB, Guerin R, Turcotte C, Lindquist S, Rokeach LA (2009) A nucleolar protein allows viability in the absence of the essential ER-residing molecular chaperone calnexin. J Cell Sci 122 1342-1351... 

Collin P, Beauregard PB, Elagoz A, Rokeach LA (2004) A non-chromosomal factor allows viability of Schizosaccharomyces pombe lacking the essential chaperone calnexin. J Cell Sci 117 907-918... 

Vassilakos, A., Michalak, M., Lehrman, M. A., and Williams, D. B. (1998). Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37, 3480-3490. 

Bass, J., Chiu, G., Argon, Y., and Steiner, D. R (1998). Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin andcalreticulin and impaired by rapid dimerization. J. Cell Biol. 141, 637-646. 

Pipe, S. W., Morris, J. A., Shah, J., and Kaufman, R. J. (1998). Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin./. Biol. Chem. 273, 8537-8544. 

Van Leeuwen, J. E. M., and Kearse, K. P. (1996). The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum. J. Biol. Chem. 271, 25345-25349. 

Rabbit polyclonal anti-calnexin CT (Stressgen Bioreagents), which recognizes the cytoplasmic tail of the ER chaperone calnexin. 

Pilon M, Schekman R, Romisch K (1997) Sec6lp mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J 16 4540-4548 Pipe SW, Morris JA, Shah J, Kaufman RJ (1998) Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem 273 8537 8544 Plemper RK, Bohmler S, Bordallo J, Sommer T, Wolf DH (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388 891 895 Plemper RK, Deak PM, Otto RT, Wolf DH (1999) Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. FEBS Lett 443 241-245... 

Ware, F.E., Vassilakos, A., Peterson, P.A., Jackson, M.R., Lehrman, M.A., and Williams, D.B. The Molecular Chaperone Calnexin Binds GlciMangGlcNAci Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins J. Biol. Chem. 19 270, 4697-4704. 

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