ArticleIranian journal of pathology2019
Designing and Analyzing the Structure of DT-STXB Fusion Protein as an Anti-tumor Agent: An
Article in Iranian journal of pathology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Unlocking the potential of tumor-targeting peptides in precision oncology.Oncology research · 2025Review
- AB Toxins as High-Affinity Ligands for Cell Targeting in Cancer Therapy.International journal of molecular sciences · 2023Review
- A comparative study of the arazyme-based fusion proteins with various ligands for more effective targeting cancer therapy: anResearch in pharmaceutical sciences · 2023Article
- Synthetic biology-inspired cell engineering in diagnosis, treatment, and drug development.Signal transduction and targeted therapy · 2023Review
- Design of two immunotoxins based rovalpituzumab antibody against DLL3 receptor; a promising potential opportunity.Research in pharmaceutical sciences · 2022Article
- Comparison of Immune Response in Mice Immunized with Recombinant PreS2/S-C18-27 Protein Derived from Hepatitis B Virus with Commercial Vaccine.Iranian journal of pathology · 2022Article
- Therapeutic Uses of Bacterial Subunit Toxins.Toxins · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BACKGROUND &
objectiveA main contest in chemotherapy is to obtain regulator above the biodistribution of cytotoxic drugs. The utmost promising strategy comprises of drugs coupled with a tumor-targeting bearer that results in wide cytotoxic activity and particular delivery. The B-subunit of Shiga toxin (STxB) is nontoxic and possesses low immunogenicity that exactly binds to the globotriaosylceramide (Gb3/CD77). Gb3/CD77 extremely expresses on a number of human tumors such as pancreatic, colon, and breast cancer and acts as a functional receptor for Shiga toxin (STx). Then, this toxin can be applied to target Gb3-positive human tumors. In this study, we evaluated DT390-STXB chimeric protein as a new anti-tumor candidate via genetically fusing the DT390 fragment of DT538 (Native diphtheria toxin) to STxB.
methodsThis study intended to investigate the DT390- STxB fusion protein structure
resultsThe results demonstrated that codon adaptation index (CAI) of
conclusionOur results showed that DT390-STXB was a stable chimeric protein and it can be recruited as a candidate of novel anti-tumor agents for the development of breast cancer treatment.
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Registered trials
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