참고문헌
- Baneyx F, Mujacic M (2004). Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol, 22, 1399-408. https://doi.org/10.1038/nbt1029
- de Marco A, Deuerling E, Mogk A, Tomoyasu T, Bukau B (2007) . Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol, 7, 32. https://doi.org/10.1186/1472-6750-7-32
- Diamant S, Eliahu N, Rosenthal D, Goloubinoff P (2001). Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J Biol Chem, 276, 39586-91. https://doi.org/10.1074/jbc.M103081200
- Frank B, Jennifer M, Petersen R (2010). A cell-based screen for inhibitors of protein folding and degradation. Cell Stress Chaperon, 15, 913-27. https://doi.org/10.1007/s12192-010-0200-3
- Goloubinoff P, Gatenby AA, Lorimer GH (1989). GroE heatshock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature, 337, 44-7. https://doi.org/10.1038/337044a0
- Hoffmann F, Rinas U (2004). Roles of heat-shock chaperones in the production of recombinant proteins in Escherichia coli. Adv Biochem Eng Biotechnol, 89,143-61.
- Huang L, Shakhnovich EI (2012). Is there an en route folding intermediate for Cold shock proteins? Protein Sci, 21, 677-85. https://doi.org/10.1002/pro.2053
- Kiefhaber T, Rudolph R, Kohler HH, Buchner J (1991). Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Biotechnology, 9, 825-9. https://doi.org/10.1038/nbt0991-825
- Moonsuk SC, Saxena AM, Chilukuri NW (2010). A strategy for the production of soluble human senescence marker protein-30 in Escherichia coli. Biochem Bioph Res Co, 393, 509-13. https://doi.org/10.1016/j.bbrc.2010.02.036
- Nishihara K, Kanemori M, Yanagi H (2000). Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl Environ Microbiol, 66, 884-9. https://doi.org/10.1128/AEM.66.3.884-889.2000
- Oyunsuren T, Sanduijav R, Davaadorj D, Nansalmaa D (2006). Hepatocellular carcinoma and its early detection by AFP testing in Mongolia. Asian Pac J Cancer Prev, 7, 460-2.
- Ran F, Gadura N, Michels CA (2010). Hsp90 co-chaperone Aha1 is a negative regulator of the saccharomyces MAL Activator and Acts early in the chaperone activation pathway. J Biol Chem, 285, 13850-62. https://doi.org/10.1074/jbc.M109.040600
- Sambrook J, Russell DW (2001). Molecular cloning: a laboratory manual. Cold Spring Harbor, New York.
- Schrodel A, de Marco A (2005). Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem, 31, 10.
- Timasheff SN (2002). Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry, 41, 13473-82. https://doi.org/10.1021/bi020316e
- Ventura S, Villaverde A (2006). Protein quality in bacterial inclusion bodies. Trends Biotechnol, 24, 179-85. https://doi.org/10.1016/j.tibtech.2006.02.007
- Wilkinson DL, Harrison RG (1991). Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology, 9, 443-8. https://doi.org/10.1038/nbt0591-443
-
Yamaguchi M, Mori S, Kato S (1988). Calcium-binding protein regucalcin is an activator of (
$Ca^{2+}-Mg^{2+}$ )-adenosine triphosphatase in the plasma membranes of rat liver. Chem Pharm Bull, 36, 3532-9. https://doi.org/10.1248/cpb.36.3532 - Zhou SF, Mo FR, Bin YH, et al (2011). Serum immunoreactivity of SMP30 and its tissues expression in hepatocellular carcinoma. Clin Biochem, 44, 331-6. https://doi.org/10.1016/j.clinbiochem.2010.10.008
- Zhou SF, Xie XX, Bin YH (2006). Identification of HCC-22-5 tumor-associated antigen and antibody response in patients. Clinica Chimima Acta, 366, 274-80. https://doi.org/10.1016/j.cca.2005.10.026
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