Wei et al. “Oxidative refolding of recombinant prochymosin”, Biochem J. vol. 340, pp. 345-351, May 10, 1999.* |
Chen, “Recombinant rhizopuspepsingen,” J Biol Chem 266(18):11718-11725 (1991). |
Cheng, et al., “High-level synthesis of recombinant HIV-1 protease and the recovery of active enzyme from inclusion bodies,” Gene 87:243-248 (1990). |
Ermolieff, et al., “Kinetic properties of saquinavir-resistant mutants of human immunodeficiency virus type 1 protease and their implications in drug resistance in vivo,” Biochemistry 36(40):12364-12370 (1997). |
Fusek, et al., “Enzymic pproperties of thermopsin,” J Biol Chem 265(3):1496-1501 (1990). |
Ghosh, et al., “Design of potent inhibitors for human brain memapsin 2(β-secretase),” J Am Chem Soc 122:3522-3523 (2000). |
Huxtable, et al., “Renaturation of 1-aminocyclopropane-1-carboxylate synthesis expressed in E. coli. in the form of inclusion bodies into a dimeric and catalytically active enzyme,” Protein Expression and Purification 12(3):305-314 (1998). |
Kelley & Winkler, “Folding of eukaryotic proteins produced in E. coli,” Genetic Engineering 12:1-19 (1990). |
Koelsch, et al., “Enzymic characteristics of secreted aspartic proteases of Candida albicans,” Biochemica et Biophysica Acta 1480:117-131 (2000). |
Lin & Tang, “Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius,” J Biol Chem 265(3):1490-1495 (1990). |
Lin, “Construction of new retroviral producer cells from adenoviral and retroviral vectors,” Gene Therapy 5:1251-1258 (1998). |
Lin, et al., “Conformational instability of the N-and C-terminal lobes of porcine pepsin in neutral and alkaline solutions,” Protein Science 2:1383-1390 (1993). |
Lin, et al., “Effect of point mutations on the kinetics and the inhibition of human immunodefiency virus type 1 protease: Relationship to drug resistance,” Biochemistry 34(4):1143-1152 (1995). |
Lin, et al., “Enzymatic activities ot two-chain pepsinogen, two-chain pepsin, and the amino-terminal lobe of pepsinogen,” J Biol Chem 267(24):17257-17263 (1992). |
Lin, et al., “Heterologous expression of thermopsin, a heat-stable acid proteinase,” Enzyme Microb Technol 14:696-701 (1992). |
Lin, et al., “Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein,” Proc. Natl. Acad. Sci. USA 97(4):1456-1460 (2000). |
Lin, et al., “Intracellular diversion of glycoprotein GP160 of human immunodeficiency virus to lysosomes as a strategy of AIDS gene therapy,” FASEB Journal 7:1070-1080 (1993). |
Lin, et al., “pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants,” J Biol Chem 267(26):18413-18418 (1992). |
Lin, et al., “Recombinant canditropsin, an extracellular aspartic protease from yeast Candida tropicals,” J Biol Chem 268(27):20143-20147 (1993). |
Lin, et al., “Relationships of human immunodeficiency virus protease with eukaryotic aspartic protease,” Methods in Enzymology 241:195-224 (1994). |
Lin, et al., “Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen,” J Biol Chem 264(8):4482-4489 (1989). |
Reed, et al., “Alteration of glycosylation renders HIV sensitive to inactivation by normal human serum,” J Immunology 159:4359-4361 (1997). |
Roswell, “Lysosome-associated membrane protein-1-mediated targeting of the HIV-1 envelope protein to an endosomal/lysosomal compartment enhances its presentation to MHC Class II-restricted T cells,” J Immunology 155:1818-1828 (1995). |
Tang & Lin, “A new anti-HIV gene therapy strategy—Diversion of gp160 to lysosomes,” International Antiviral News 2(2):19-20 (1994). |
Tang & Lin, “Engineering aspartic proteases to probe structure and function relationships,” Current Opinion in Biotechnology 5:422-427 (1994). |
Tang, et al., “Understanding HIV protease: Can it be translated into effective therapy against AIDS?” Scand J Clin Lab Invest Suppl 210:127-35 (1992). |
Tichy, et al., “Improved procedure for high-yield recovery of enzymatically active recombinant calf chymosin from E. coli inclusion bodies,” Protein Expression and Purification 4(1):59-63 (1993). |
Wang, et al., “Crystal structure of the catalytic domain of human plasmin complexed with streptokinase,” Science 281:1662-1665 (1998). |
Wang, et al., “Human plasminogen catalytic domain undergoes an unusual conformational change upon activation,” J Mol. Biol 295:903-914 (2000). |