Ahmadi S., Ghafouri H., Tarazi S., Sarikhan S. and Saberi K.O. 2020. Cloning, purification and biochemical characterization of two glutathione S-transferase isoforms from Rutilus frisii kutum. Protein Expression and Purification, 179: 1–9 (105800).
Amado L.L., Rosa C.E. Da Leite A. M., Moraes L., Pires W.V., Pinho G.L.L., Martins C.M.G., Robaldo R.B., Nery L.E.M., Monserrat J.M., Bianchini A., Martinez P.E. and Geracitano L.A. 2006. Biomarkers in croakers Micropogonias furnieri (Teleostei: Sciaenidae) from polluted and non-polluted areas from the Patos Lagoon estuary (Southern Brazil): Evidences of genotoxic and immunological effects. Marine Pollution Bulletin, 52(2): 199–206.
Bhandari B.K., Gardner P.P. and Lim C.S. 2020. Solubility-weighted index: Fast and accurate prediction of protein solubility. Bioinformatics, 36(18): 4691–4698.
Castineiras T.S., Williams S.G., Hitchcock A.G. and Smith D.C. 2018. E. coli strain engineering for the production of advanced biopharmaceutical products. FEMS Microbiology Letters, 365(15): 1–10.
Coles B., Ketterer B. and Hinson J.A. 1990. The role of glutathione and glutathione transferases in chemical cardnogenesi. Critical Reviews in Biochemistry and Molecular Biology, 25(1): 47–70.
Dadar M., Adel M., Saravi H. N. and Dadar M. 2016. A comparative study of trace metals in male and female Caspian kutum (Rutilus frisii kutum) from the southern basin of Caspian Sea. Environmental Science and Pollution Research, 23(24): 24540–24546.
Doyen P., Vasseur P. and Rodius F. 2005. cDNA cloning and expression pattern of pi-class glutathione S-transferase in the freshwater bivalves Unio tumidus and Corbicula fluminea. Comparative Biochemistry and Physiology (C), 140(3-4): 300–308.
Esposito D. and Chatterjee D.K. 2006. Enhancement of soluble protein expression through the use of fusion tags. Current Opinion in Biotechnology, 17(4): 353–358.
Evans C.G., Chang L. and Gestwicki J.E. 2010. Heat shock protein 70 (Hsp70) as an emerging drug target. Journal of Medicinal Chemistry, 53(12): 4585–4602.
Gallagher S.R. 2006. One-dimensional SDS gel electrophoresis of proteins. Current Protocols in Molecular Biology, 75(1): 1–38 (10.2A).
Garcia-Fruitos E., Sabate R., De Groot N.S., Villaverde A., and Ventura S. 2011. Biological role of bacterial inclusion bodies: A model for amyloid aggregation. FEBS Journal, 278(14): 2419–2427.
Ghazaei C. 2017. Role and mechanism of the Hsp70 molecular chaperone machines in bacterial pathogens. Journal of Medical Microbiology, 66(3): 259–265.
Harlow E. and Lane D. 2006. Bradford assay. Cold Spring Harbor Protocols, 6: 4644.
Hayes J.D., Flanagan J.U. and Jowsey I.R. 2005. Glutathione transferases. Annual Review of Pharmacology and Toxicology, 45: 51–88.
Hoffmann F., Van Den Heuvel J., Zidek N. and Rinas U. 2004. Minimizing inclusion body formation during recombinant protein production in Escherichia coli at bench and pilot plant scale. Enzyme and Microbial Technology, 34(3–4): 235–241.
Idalia V.M.N. and Bernardo F. 2017. Escherichia coli as a model organism and its application in biotechnology. P: 253–274. In: Samie A. (Ed.). Escherichia coli- Recent Advances on Physiology, Pathogenesis and Biotechnological Applications. IntechOpen, England.
Ikura K., Kokubu T., Natsuka S., Ichikawa A., Adachi M., Nishihara K., Yanagi H. and Utsumi S. 2002. Co-overexpression of folding modulators improves the solubility of the recombinant guinea pig liver transglutaminase expressed in Escherichia coli. Preparative Biochemistry and Biotechnology, 32(2): 189–205.
Iwama G.K., Thomas P.T., Forsyth R.B. and Vijayan M.M. 1998. Heat shock protein expression in fish. Reviews in Fish Biology and Fisheries, 8(1): 35–56.
Jakobsson P.J., Morgenstern R., Mancini J., Ford-Hutchinson A. and Persson B. 2008. Common structural features of mapeg-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Science, 8(3): 689–692.
Kalita J., Shukla R. and Tripathi T. 2019. Structural basis of urea-induced unfolding of Fasciola gigantica glutathione S-transferase. Journal of Cellular Physiology, 234(4): 4491–4503.
Kim K.J., Kim H.E., Lee K.H., Han W., Yi M.J., Jeong J. and Oh B.H. 2004. Two-promoter vector is highly efficient for overproduction of protein complexes. Protein Science, 13(6): 1698–1703.
Kopito R.R. 2000. Aggresomes, inclusion bodies and protein aggregation. Trends in Cell Biology, 10(12): 524–530.
Lund P.A. 2001. Microbial molecular chaperones. Advances in Microbial Physiology, 44: 93–140.
Ojopagogo Y.A., Adewale I.O., Adeyemi J.A. and Afolayan A. 2015. Some novel features of glutathione transferase from juvenile catfish (Clarias gariepinus) exposed to lindane-contaminated water. Perspectives in Science, 4: 62–65.
Ozaslan M. S., Demir Y., Aksoy M., Kufrevioglu O. I. and Beydemir S. 2018. Inhibition effects of pesticides on glutathione-S-transferase enzyme activity of Van Lake fish liver. Journal of Biochemical and Molecular Toxicology, 32(9): 1–5 (e22196).
Peng S., Chu Z., Lu J., Li D., Wang Y., Yang S. and Zhang Y. 2016. Co-expression of chaperones from P. furiosus enhanced the soluble expression of the recombinant hyperthermophilic α-amylase in E. coli. Cell Stress and Chaperones, 21(3): 477–484.
Postlethwait J., Amores A., Cresko W., Singer A. and Yan Y.L. 2004. Subfunction partitioning, the teleost radiation and the annotation of the human genome. Trends in Genetics, 20(10): 481–490.
Rinas U., Hoffmann F., Betiku E., Estape D. and Marten S. 2007. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli. Journal of Biotechnology, 127(2), 244–257.
Romier C., Ben Jelloul M., Albeck S., Buchwald G., Busso D., Celie P.H.N., Christodoulou E., De Marco V., Van Gerwen S., Knipscheer P., Lebbink J.H., Notenboom V., Poterszman A., Rochel N., Cohen S.X., Unger T., Sussman J.L., Moras D., Sixma T.K. and Perrakis A. 2006. Co-expression of protein complexes in prokaryotic and eukaryotic hosts: Experimental procedures, database tracking and case studies. Acta Crystallographica Section (D), 62(10): 1232–1242.
Rudiger S., Buchberger A. and Bukau B. 1997. Interaction of Hsp70 chaperones with substrates. Nature Structural Biology, 4(5): 342–349.
Rudneva I.I., Kuzminova N.S. and Skuratovskaya E.N. 2010. Glutathione-S-transferase activity in tissues of Black Sea fish species. Asian Journal of Experimental Biological Sciences, 1(1): 141–150.
Sakamaki K. and Satou Y. 2009. Caspases: Evolutionary aspects of their functions in vertebrates. Journal of Fish Biology, 74(4): 727–753.
Singh A., Upadhyay V., Upadhyay A.K., Singh S.M. and Panda A.K. 2015. Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process. Microbial Cell Factories, 14(1): 1–10.
Speed M.A., Wang D.I.C. and King J. 1996. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nature Biotechnology, 14(10): 1283–1287.
Townsend D.M. and Tew K.D. 2003. The role of glutathione-S-transferase in anti-cancer drug resistance. Oncogene, 22(47): 7369–7375.
Tsuchida S. and Sato K. 1992. Glutathione transferases and cancer. Critical Reviews in Biochemistry and Molecular Biology, 27(4–5): 337–384.
Upadhyay V., Singh A., Jha D., Singh A. and Panda A.K. 2016. Recovery of bioactive protein from bacterial inclusion bodies using trifluoroethanol as solubilization agent. Microbial Cell Factories, 15(1): 1–13.
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