Davis, G. D., C. Elisee, D. M. Newham and R. G. Harrison. 1999. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol. Bioeng. 65:382-388.
de Gier, J. W. and J. Luirink. 2001. Biogenesis of inner membrane proteins in Escherichia coli. Mol. Microbiol. 40:314-322.
Freedman, R. B. 1992. Protein folding in the cell. In Protein folding (Ed. T. E. Creighton). pp. 455-540. W. H. Freeman and Co., New York.
Grisshammer, R. and C. G. Tate. 1995. Overexpression of integral membrane proteins for structural studies. Q. Rev. Biophys. 28:315-422.
Hoffman, F., J. va den Heuvel, N. Ziddk and U. Rinas. 2004. Minimizing inclusion body formation during recombinant protein production in Escherichia coli at bench and pilot plant scale. Enzyme and Microbial Technology 34:235-241.
Holmgren, A. 1985. Thioredoxin. Ann. Rev. Biochem. 54:237-271.
Katti, S. K., D. M. LeMaster and H. Eklund. 1990. Crystal structure of thioredoxin from Echerichia coli at 1.68 angstrom resolution. J. Mol. Bio. 212:197-184.
Krueger, J. K., A. M. Stock, C. E. Schutt and J. B. Stock. 1990. Inclusion bodies from proteins produced at high levels in Escherichia coli, pp. 136-142. In: (Ed. L. M. Gierasch and J. King), Protein folding, American Association for Advances in Science, Washington DC.
Laemmli, U. K. 1970. Cleavage of structual proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
LaVallie, E. R., E. A. DiBlasio, S. Kovacic, K. L. Grant, P. F. Schendel and J. W. McCoy. 1993. A thioredoxin gene fusion expression system that circumbents inclusion body formation in the E. coli cytoplasm. Biotechnology 11:187-193.
Lunn, C. A., S. Kathju, B. J. Wallace, S. R. Kushner and V. Pigiet. 1984. Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12. J. Biol. Chem. 259:10469-10474.
Lunn, C. A. and V. P. Pigiet. 1982. Localization of thioredoxin from Escherichia coli in an osmotically sensitive compartment. J. Biol. Chem. 257:11424-11430.
Maina, C. V. P. D. Riggs, A. G. Slatko, B. E. Moran, L. S. Tagliamonte, J. A. McReynolds and C. di Guan. 1988. An Escherichia coli vector to express and purify foreign proteins by fusion and separation from maltose-binding protein. Gene 74:365-373.
Nam, E. S., H. J. Jung, J. W. Choi, J. H. Lim, S. K. Hwang, S. K. Kang, K. K. Cho, Y. J. Choi and J. K. Ahn. 2004. $\beta$- galactosidase gene of Thermus thermophilus KNOUC112 isolated from hot spring of volcanic area in New Zealand: Identification of the bacteria, cloning and expression of the gene in Escherichia coli. Asian-Aust. J. Anim. Sci. 17(11):1591-1598.
Nilsson, B., L. Abrahmsen and M. Uhlen. 1985. Immobilization and purification of enzymes with staphyloccocal protein A gene fusion vectors. EMBO J. 4:1075-1080.
Peng, L., Z. Xu, X. Fang, F. Wang and P. Cen. 2004. High level expression of soluble human $\beta$-defensin-2 in Escherichia coli. Biochemistry. In publishing.
SAS. 2004. SAS/STAT software: Changes and Enhancements through Release 8.01. SAS Institute Inc., Cary, NC.
Schein, C. H. 1989. Production of soluble recombinant proteins in bacteria. Biotechnology 7:1141-1147.
Schein, C. H. and M. H. M. Noteborn. 1988. Formation of soluble recombinant proteins in Escherichia coli is favored by lowering growth temperature. Biotechnology 6:291-294.
Seddi, R. J. C. Chaix, A. Puigserver and X. J. Guo. 2003. Expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Protein Expression and Purification. 27:220-228.
Smith, D. B. and K. S. Johnson. 1988. Single step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene. 67:31-40.
Tanaka, T. and R. Y. Yada. 1996. Expression of soluble cloned porcine pepsinogen A in Escherichia coli. Biochem. J. 315:443-446.