1. Levi‐Montalcini, R. (1987) the nerve growth factor: 35 years later (Nobel lecture). Angewandte Chemie. 26 (8), 707-716.
2. Alzheimer, C. (2012) (Ed.). Molecular and Cellular Biology of Neuroprotection in the CNS. Springer Science & Business Media.
3. Snider, W. D. (1994) Functions of the neurotrophins during nervous system development: What the knockouts are teaching us. Cell. 77 (5), 627.
4. Wang, W., Chen, J., Guo., X. (2014) The role of nerve growth factor and its receptors in tumorigenesis and cancer pain. Biosci Trends. 8, 68-74.
5. Althaus, H. H. (2004) Remyelination in multiple sclerosis: a new role for neurotrophins?. Prog Brain Res.146, 415-432.
6. Zhou, H., Gong, Y., Liu, Y., Huang, A., Zhu, X., Liu, J., Liu, J. (2020). Intelligently thermoresponsive flower-like hollow nano-ruthenium system for sustained release of nerve growth factor to inhibit hyperphosphorylation of tau and neuronal damage for the treatment of Alzheimer's disease. Biomaterials. 237, 119822.
7. Kawamoto, K., Matsuda, H. (2004) Nerve growth factor and wound healing. Prog Brain Res. 146, 369-384.
8. Lambiase, A., Sacchetti, M., and Bonini, B. (2012) Nerve growth factor therapy for corneal disease. Curr Opin Ophthalmol. 23, 296-302.
9. Paoletti, F., Malerba, F., Ercole, B. B., Lamba, D., and Cattaneo, A (2015) A comparative analysis of the structural, functional and biological differences between Mouse and Human Nerve Growth Factor. Biochim. Biophys. Acta. 1854, 187-197.
10. Hajihassan, Z., Tilko, P. G., Sadat, S. M. (2018). Improved Production of Recombinant Human β-NGF in Escherichia coli–a Bioreactor Scale Study. Pol j of microbiol. 67(3), 355.
11. Edwards, R. H., Selby, M. J., Mobley, W. C., Weinrich, S. L., Hruby, D. E., Rutter, W. J. (1988). Processing and secretion of nerve growth factor: expression in mammalian cells with a vaccinia virus vector. Mol cell biol. 8(6), 2456-2464.
12. Dong, W., Li, C., Yang, Y., Wang, T. Wang, F. (2019). Increasing transgenic expression in recombinant Chinese hamster ovary cells using introns in different directions. Chin j biotechnol. 35(6), 1071-1078.
13. Sezonov, G., Joseleau-Petit, D., D'Ari, R. (2007) Escherichia coli physiology in Luria-Bertani broth. J. bacteriol.Res. 189, 8746-8749.
14. Burgess, R. R. (2009) Refolding solubilized inclusion body proteins. Methods in enzymology. 463, 259-282.
15. Maksum, I. P., Lestari, A., Fauzia, R. P., Rachman, S. D., Soedjanaatmadja, U. M. (2019) Escherichia coli BL21 (DE3) expression system using TorA signal peptide for Recombinant Human Albumin (rHA) secretion. Int. J. Res. 10(4), 3319-3324.
16. Rosano, G. L., Ceccarelli, E. A. (2014) Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol. 5, 172.
17. De Marco, A., De Marco, V. (2004) Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning. J. Biotechnol. 109, 45-52.
18. Hartl, F. U., Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295, 1852-1858.
19. Vabulas, R. M., Raychaudhuri, S., Hayer-Hartl, M., X Hartl, R. M. (2010) Protein folding in the cytoplasm and the heat shock response. Csh Perspect Biol. 2, a004390.
20. Hartl, F. U., Martin, J. (1995) Molecular chaperones in cellular protein folding. Curr Opin Struct Biol. 5, 92-102.
21. Sonoda, H., Kumada, H., Katsuda, T., Yamaji, H. (2011) Effects of cytoplasmic and periplasmic chaperones on secretory production of single-chain Fv antibody in Escherichia coli. J Biosci Bioeng. 111, 465-470.
22. Baneyx, F. Palumbo, J. L. (2003) Improving heterologous protein folding via molecular chaperone and foldase co-expression in E. coli. Gene Expression Protocols, ed: Springer. 171-197.
23. Saibil, H. (2013) Chaperone machines for protein folding, unfolding and disaggregation. Nature reviews Molecular cell biology. 14, 630-642.
24. Sambrook, J., Russelt, D.W. (2001). Molecular cloning: A laboratory manual. Fourth edition. New York: Cold spring harbor laboratory press.
25. Libby, R. T., Braedt, G., Kronheim, S. R., March, C. J., Urdal, D. L., Chiaverotti, T. A. (1987) Expression and purification of native human granulocyte-macrophage colony-stimulating factor from an Escherichia coli secretion vector. DNA. 6, 221.
26. U. K. Laemmli, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680-685.
27. De Maio, A. (1994) Protein blotting and immunoblotting using nitrocellulose membranes, in Protein Blotting. A Practical Approach, ed: IRL Press New York. 11-32.
28. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
29. Sadat, S. M., Z. Hajihassan, Z., Barshan-tashnizi, M., Abdi. M. (2018) Co-expression of recombinant human nerve growth factor with trigger factor chaperone in E. coli. Nova Biol. Reperta. 5, 221-228.
30. Hajihassan, Z., Abdi, M., Roshani Yasaghi, E., Rabbani-Chadegani, A. (2017) Optimization of recombinant beta-NGF purification using immobilized metal affinity chromatography. Minerva Biotecnol. 29, 126-132.
31. McGuire, J. C., Greene, L. A. (1979) Rapid stimulation by nerve growth factor of amino acid uptake by clonal PC12 pheochromocytoma cells. J. Biol. Chem. 254, 3362-3367.
32. Derman, A. I., Prinz, W. A., Belin, D., Beckwith, J. (1993) Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science. 262, 1744-1747.
33. Huang, C. J., Lin, H., Yang, X. (2012) Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements. J Ind Microbiol Biotechnol. 39, 383-399.
34. Puertas, J. M., Nannenga, B. L., Dornfeld, K. T., Betton, J. M., Baneyx, F. (2010) Enhancing the secretory yields of leech carboxypeptidase inhibitor in Escherichia coli: influence of trigger factor and signal recognition particle. Protein Expr Purif. 74, 122-128.
35. Jia, Q., Fan, D., Ma, P., Ma, X., 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.
36. Tong, Y., Feng, S., Xin, Y., Yang, H., Zhang, L., Wang, 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.