[1] Farajnia S, Ahmadzadeh V, Tanomand A, Veisi K, Khosroshahi SA, Rahbarnia L. Development trends for generation of single-chain antibody fragments. Immunopharmacol. Immunotoxicol. (2014) 36 (5): 297-308.
[2] Weisser NE, Hall JC. Applications of single-chain variable fragment antibodies in therapeutics and diagnostics. Biotechnol. Adv. (2009) 27 (4): 502-520.
[3] Blažek D, Celer V. The production and application of single-chain antibody fragments. Folia. Microbiol. (Praha) (2003) 48 (5): 687-98.
[4] Ahmad ZA, Yeap SK, Ali AM, Ho WY, Alitheen NB, Hamid M. ScFv antibody: principles and clinical application. Clin. Dev. Immunol. (2012)2012: 980250.
[5] Gopal GJ, Kumar A. Strategies for the production of recombinant protein in Escherichia coli. Protein J. (2013) 32 (6): 419-25.
[6] Zhu YQ, Tong WY, Wei DZ, Zhou F, Zhao JB. Environmental stimuli on the soluble expression of anti-human ovarian carcinoma× anti-human CD3 single-chain bispecific antibody in recombinant Escherichia coli. Biochem. Eng. J. (2007) 37 (2): 184-91.
[7] Terpe K. Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. (2006) 72 (2): 211.
[8] Kamionka M. Engineering of therapeutic proteins production in Escherichia coli. Curr. Pharm. Biotechnol. (2011) 12 (2): 268-74.
[9] Lindner R, Moosmann A, Dietrich A, Böttinger H, Kontermann R, Siemann-Herzberg M. Process development of periplasmatically produced single chain fragment variable against epidermal growth factor receptor in Escherichia coli. J. Biotechnol. (2014) 192: 136-45.
[10] De Marco A. Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. Microb. Cell Fact. (2009) 8 (1): 26.
[11] Mergulhao F, Summers DK, Monteiro GA. Mergulhao F, Summers DK, Monteiro GA. Biotechnol. Adv. (2005) 23 (3): 177-202.
[12] Hajighasemlou et al. Preparation of immunotoxin herceptin-botulinum and killing effects on two breast cancer cell lines. Asian Pac. J. Cancer Prev. (2015) 16: 5977-81.
[13] Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGuire WL. Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGuire WL. Science (1987) 235 (4785): 177-82.
[14] Akbari V, Mir Mohammad Sadeghi H, Jafrian-Dehkordi A, Abedi D, Chou CP. Functional expression of a single-chain antibody fragment against human epidermal growth factor receptor 2 (HER2) in Escherichia coli. J. Ind. Microbiol. Biotechnol. (2014) 41 (6): 947-56.
[15] Cao et al. Single-chain antibody-based immunotoxins targeting Her2/neu: design optimization and impact of affinity on antitumor efficacy and off-target toxicity. Mol. Cancer Ther. (2012) 11(1): 143-53.
[16] Cao Y, Marks JD, Marks JW, Cheung LH, Kim S, Rosenblum MG. Construction and characterization of novel, recombinant immunotoxins targeting the Her2/neu oncogene product: in vitro and in vivo studies. Cancer Res. (2009) 69 (23): 8987-95.
[17] Park et al. Anti-HER2 immunoliposomes enhanced efficacy attributable to targeted delivery. Clin. Cancer Res. (2002) 8 (4): 1172-81.
[18] Park et al. Tumor targeting using anti-her2 immunoliposomes. J. Control Release (2001) 74 (1): 95-113.
[19] Novagen I. pET system manual. Novagen Madison, WI (2002).
[20] Heo MA, Kim SH, Kim SY, Kim YJ, Chung J, Oh MK, Lee SG. Functional expression of single-chain variable fragment antibody against c-Met in the cytoplasm of Escherichia coli. Protein Expr. Purif. (2006) 47 (1): 203-9.
[21] Napathorn SC, Kuroki M. High expression of fusion proteins consisting of a single-chain variable fragment antibody against a tumor-associated antigen and interleukin-2 in Escherichia coli. Anticancer Res. (2014) 34 (8): 3937-46.
[22] Naderi S, Alikhani MY, Karimi J, Shabab N, Mohamadi N, Jaliani HZ, Saidijam M. Cytoplasmic expression, optimization and catalytic activity evaluation of recombinant mature lysostaphin as an anti-staphylococcal therapeutic in Escherichia coli. Acta Med. Int. (2015) 2 (2): 72.
[23] Jaliani HZ, Farajnia S, Safdari Y, Mohammadi SA, Barzegar A, Talebi S. Optimized condition for enhanced soluble-expression of recombinant mutant anabaena variabilis phenylalanine ammonia lyase. Adv. Pharm. Bull. (2014) 4 (3): 261.
[24] Drees JJ, Augustin LB, Mertensotto MJ, Schottel JL, Leonard AS, Saltzman DA. Soluble production of a biologically active single-chain antibody against murine PD-L1 in Escherichia coli. Protein Expr. Purif. (2014) 94: 60-6.
[25] Padiolleau-Lefèvre S, Débat H, Phichith D, Thomas D, Friboulet A, Avalle B. Expression of a functional scFv fragment of an anti-idiotypic antibody with a β-lactam hydrolytic activity. Immunol. Lett. (2006)103(1): 39-44.
[26] Tiwari A, Sankhyan A, Khanna N, Sinha S. Enhanced periplasmic expression of high affinity humanized scFv against Hepatitis B surface antigen by codon optimization. Protein Expr. Purif. (2010) 74 (2): 272-9.
[27] Cronin et al. Annual Report to the Nation on the Status of Cancer, part I. National cancer statistics. Cancer (2018) 124 (13): 2785-2800.
[28] Salamzadeh J, Kamalinejad M, Mofid B, Mortazavi SA, Sheikhlar A, Babaeian M. The Effect of Elaeagnus angustifolia L. Cream on Radiation-Induced Skin Reactions in Women with Breast Cancer; A Preliminary Clinical Trial. Iran. J. Pharm. Sci. (2017) 13 (2): 25-36.
[29] Harrison J, Keshavarz‐Moore E. Production of antibody fragments in Escherichia coli. Ann. N. Y. Acad. Sci. (1996) 782 (1): 143-58.
[30] Ahmadzadeh M, Farshdari F, Nematollahi L, Behdani M, Mohit E. Anti‑HER2 scFv Expression in Escherichia coli SHuffle®T7 Express Cells: Effects on Solubility and Biological Activity. Mol. Biotechnol. (2020) 62: 18–30.