1- Florio, P., Luisi, S., Marchetti, P., Lupi, R., Cobellis, L., Falaschi, C., Sugino, H., Navalesi, R., Genazzani, A.R., and Petraglia, F. (2000) Activin A stimulates insulin secretion in cultured human pancreatic islets. J. Endocrinol. Invest. 23, 231-234.
2- Mason, A.J., Farnworth, P.G., and Sullivan, J. (1996) Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. J. Mol. Endocrinol. 10, 1055-1065.
3- Paulsson, K., Heidenblad, M., Strombeck, B., Staaf, J., Jonsson, G., Borg, A., Fioretos, T., and Johansson, B. (2006) High-resolution genome-wide array-based comparative genome hybridization reveals cryptic chromosome changes in AML and MDS cases with trisomy 8 as the sole cytogenetic aberration. J. Leuk. 20, 840-846.
4- Tanimoto, K., Yoshida, E., Mita, S., Nibu, Y., Murakami, K., and Fukamizu, A. (1996) Human activin βA gene Identification of novel 5′ exon, functional promoter, and enhancers. J. Biol. Chem. 271, 32760-32769.
5- Mason, A.J. (1994) Functional analysis of the cysteine residues of activin A. J. Mol. Endocrinol. 8, 325-332.
6- Phillips, D.J., de Kretser, D.M., and Hedger, M.P. (2009) Activin and related proteins in inflammation: not just interested bystanders. Cytokine. growth. Factor. Rev. 20, 153-164.
7- Pauklin, S., and Vallier, L. (2015) Activin/Nodal signalling in stem cells. J. Dev. 142, 607-619.
8- Sozzani, S., and Musso, T. (2011) The yin and yang of Activin A. Blood. 117, 5013-5015.
9- Papakonstantinou, T., Harris, S.J., Fredericks, D., Harrison, C., Wallace, E.M., and Hearn, M.T. (2009) Synthesis, purification and bioactivity of recombinant human activin A expressed in the yeast Pichia pastoris. Protein. Expr. Purif. 64: 131-138.
10- Hoffmann, A., Bukau, B., and Kramer, G. (2010) Structure and function of the molecular chaperone Trigger Factor. Biochim. Biophys. Acta. Mol. Cell. Res. 1803, 650-661.
11- Saibil, H. (2013) Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Mol. Cell. Biol. 14, 630-642.
12- Bertelsen, E.B., Chang, L., Gestwicki, J.E., and Zuiderweg, E.R. (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc. Natl. Acad. Sci. 106, 8471-8476.
13- Hartl, F.U., and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. J. Sci. 295, 1852-1858.
14- Sharma, S.K., De Los Rios, P., Christen, P., Lustig, A., and Goloubinoff, P. (2010) The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat. Chem. Biol. 6, p.914.
15- Green, M.R., and Sambrook, J. (2012) Working with synthetic oligonucleotide probes, Molecular cloning: a laboratory manual. 10.11–10.16.
16- Hajihassan, Z., Sohrabi, M., Rajabi Bazl, M., and Eftekhary, H.S. (2016) Expression of human nerve growth factor beta and bacterial protein disulfide isomerase (DsbA) as a fusion protein (DsbA:: hNGF) significantly enhances periplasmic production of hNGF beta in Escherichia coli. Rom. Biotech. Lett. 21, 11850-6.
17- Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680-685.
18- Demaio, A. (1996) Protein blotting and immunoblotting using nitrocellulose membranes. Protein blotting. Oxford University Press, Oxford, PP 11-32.
19- Hajihassan, Z., Abdi, M., Roshani Yasaghi, E., and Rabbani-Chadegani, A. (2017) Optimization of recombinant beta-NGF purification using immobilized metal affinity chromatography. Minerva Biotecnol, 29, 126-132.
20- Chen, Y., Phillips, D.J., McMillan, J., Bedford, P., Goldstein, J., Wu, H., Hedger, M.P., and Smith, J.A. (2011) Pattern of activin A and follistatin release in a sheep model of cardiopulmonary bypass. Cytokine. 54, 154-160.
21- Huang, C.J., Lin, H., and Yang, X. (2012) Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements. J. Ind. Microbiol. Biotechnol. 39, 383-399.
22- Cao, W., Li, H., Zhang, J., Li, D., Acheampong, D.O., Chen, Z., and Wang, M. (2013) Periplasmic expression optimization of VEGFR2 D3 adopting response surface methodology: Antiangiogenic activity study. Protein. Expr. Purif. 90, 55-66.
23- Papaneophytou, C.P., Rinotas, V., Douni, E., and Kontopidis, G. (2013) A statistical approach for optimization of RANKL overexpression in Escherichia coli: purification and characterization of the protein. Protein. Expr. Purif. 90, 9-19.
24- Baneyx, F. and Palumbo, J. L. (2003) Improving heterologous protein folding via molecular chaperone and foldase co-expression. E. coli Gene Expression Protocols, Springer, Humana Press, PP 171-197.
25- Yao, D., Fan, J., Han, R., Xiao, J., Li, Q., Xu, G., Dong, J., and Ni, Y. (2020) Enhancing soluble expression of sucrose phosphorylase in Escherichia coli by molecular chaperones. Protein. Expr. Purif. 169, 105571.
26- Fang, Y., Fu, X., Xie, W., Li, L., Liu, Z., Zhu, C., and Mou, H. (2019) Expression, purification and characterisation of chondroitinase AC II with glyceraldehyde-3-phosphate dehydrogenase tag and chaperone (GroEs-GroEL) from Arthrobacter sp. CS01. Int. J. Biol. Macromol. 129, 471-476.
27- Summpunn, P., Jomrit, J., and Panbangred, W. (2018) Improvement of extracellular bacterial protein production in Pichia pastoris by co-expression of endoplasmic reticulum residing GroEL–GroES. J. Biosci. Bioeng. 125, 268-274.
28- Tong, Y., Feng, S., Xin, Y., Yang, H., Zhang, L., Wang, W., and Chen, W. (2016) Enhancement of soluble expression of codon-optimized Thermomicrobium roseum sarcosine oxidase in Escherichia coli via chaperone co-expression. J. Biotechnol. 218, 75-84.
29- Jia, Q., Fan, D., Ma, P., Ma, X., and Xue, W. (2014) The different roles of chaperone teams on over-expression of human-like collagen in recombinant Escherichia coli. J. Taiwan. Inst. Chem. Eng. 45, 2843-2850.