Calreticulin endoplasmic reticulum

Comparison of two analytical approaches, atomic force microscopy (AFM) and quartz crystal microbalance, for studying the binding of Con A to glycosylated carboxypeptidase, demonstrated that both could determine the quantitative parameters characterizing the interaction.65 Quantitative analyses of the interaction of Calreticulin (CRT), which is a soluble molecular chaperone of the endoplasmic reticulum, with various... 

Pagny, S., Cabanes-Macheteau, M., Gilikin, J.W., Leborgne-Castel, N., Lerouge, R, Boston, R.S., Faye, L., and Gomord, V. (2000). Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention. Plant Cell 12 739-755. 

R. G., Role of A-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell. Mol. Life Sci. 61,1025-1041, 2004 Bedard, K., Szabo, E., Michalak, M., and Opas, M., Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, andERp57, Int. Rev. Cytol. 245, 91-121, 2005 Ito, Y, Hagihara,... 

I-type CRDs derived from the immunoglobulin fold, (5)calnexin and calreticulin, which bind to N-linked oligosaccharides and retain misfolded glycoproteins in the endoplasmic reticulum, (6) the P-type lectins, which bind mannose-6-phosphate moieties, and (7)the R-type lectins, which contain CRDs similar to those found in ricin. 

Wada, I., Imai, S., Kai, M., Sakane, F., and Kanoh, H. (1995). Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J. Biol. Chem. 270, 20298-20304. 

Patil, A. R., Thomas, C. J., and Surolia, A. (2000). Kinetics and the mechanism of interaction of the endoplasmic reticulum chaperone, calreticulin, with monoglucosylated (GlcjMangGlcNAcg) substrate. J. Biol. Chem. 275, 24348-24356. 

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. 

Fig. 3.3 FVIII biosynthesis. Signal peptide cleavage and asparagine (N)-linked glycosylation of the FVIII occurs after translation and translocation to the lumen of the endoplasmic reticulum (ER). Within the ER, the FVIII is folded, which requires binding to chaperone proteins. FVIII binds immunoglobulin-binding protein (BiP) at the A1 domain, and is released in an ATP-dependent step. Next, FVIII binds calnexin (CNX) and calreticulin (CRT) (not shown) at the B domain. Properly folded FVIII proteins are transported to the Golgi by chaperone proteins, LMANl and MCFD2 (not shown) for further processing LMANl also binds to the FVIII B domain. Incorrectly folded FVIII...

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... 

P27797 Calreticulin precursor + A1807225 KDEL endoplasmic reticulum (ER) protein + ... 

Calnexin, Calreticulin and Glycoprotein Folding Within the Endoplasmic Reticulum... 

Basu, S., and Srivastava, P.K. Calreticulin, a Peptide-binding Chaperone of the Endoplasmic Reticulum, Elicits Tumor- and Peptide-specific Immunity J. Exp. Med. 1999 189, 797-802. 

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