1[1]Hartl F U, Marin J. Molecular chaperones in cellular protein folding [J]. Curr Opin strcut Biol, 1995, 5:92-102.
2[2]Helenius A, Trombetta E S. Calnexin, calreticulin and the folding of glycoproteins [J] . Trends in Cell Biology, 1997, 7:193-200.
3[3]Maurizio M, Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum [J] . Science, 2000, 288: 331-336.
4[4]Ellgaard L, Helenius A. ER quality control :towards an understanding at the molecular level [J]. Curr Opin Cell Biol, 2001, 13:43-47.
5[5]Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum[J] . Mol Biol Cell, 1994, 5:253-265.
6[6]Merola M, Brazzoli M, Cocchiarella F, et al. Folding of hepatitis C virus E1 glycoprotein in a cell-free system[J].J Virol,2001, 75:11205-11217.
7[7]Dubuisson J, Rice C M. Hepatitis C virus glycoprotein folding:disulfide bond formation and association with Calnexin [J]. J Virol, 1996, 778-786.
8[8]Nakhasi H L, Ramanujam M, Atreya C D, et al. Rubella virus glycoprotein interaction with the endoplasmic reticulum calreticulin and calnexin [J]. Arch Virol, 2001,146:1-14.
9[9]Kim S S, Shin H J, Cho Y H, et al. Expression of stable hepatitis B viral polymerase associated with GRP94 in E.coli[J]. Arch Viro, 2000, 145:1305-1320.
10[10]Cho G, Sub S W, Jung G. HBV polymerase interacts independently with N-terminal and C-terminal fragments of Hsp90beta [J] . Biochem Biophys Res Commun, 2000, 274:203-211.
