Academic literature on the topic 'Therapeutic potential of anticancer immunotoxins'

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Journal articles on the topic "Therapeutic potential of anticancer immunotoxins"

1

Choudhary, Swati, Mrudula Mathew, and Rama S. Verma. "Therapeutic potential of anticancer immunotoxins." Drug Discovery Today 16, no. 11-12 (2011): 495–503. http://dx.doi.org/10.1016/j.drudis.2011.04.003.

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2

Ahmad, Zuhaida Asra, Swee Keong Yeap, Abdul Manaf Ali, Wan Yong Ho, Noorjahan Banu Mohamed Alitheen, and Muhajir Hamid. "scFv Antibody: Principles and Clinical Application." Clinical and Developmental Immunology 2012 (2012): 1–15. http://dx.doi.org/10.1155/2012/980250.

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To date, generation of single-chain fragment variable (scFv) has become an established technique used to produce a completely functional antigen-binding fragment in bacterial systems. The advances in antibody engineering have now facilitated a more efficient and generally applicable method to produce Fv fragments. Basically, scFv antibodies produced from phage display can be genetically fused to the marker proteins, such as fluorescent proteins or alkaline phosphatase. These bifunctional proteins having both antigen-binding capacity and marker activity can be obtained from transformed bacteria
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3

Oszajca, Katarzyna, Łukasz Wieteska, Magdalena Cybula, and Janusz Szemraj. "The assessment of prokaryotic addictive modules’ activity in the context of seeking novel immunotoxins." Postępy Polskiej Medycyny i Farmacji 5 (June 26, 2017): 59–63. http://dx.doi.org/10.5604/01.3001.0011.6195.

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Despite of the fact that current anticancer chemotherapeutics have many beneficial achievements, there is an urgent need for new efficient therapies. A new type of drugs which are extensively investigated are immunotoxinshybrid proteins that consist of cytotoxic component and second part which is responsible for selective binding to the receptors on tumor cells. Unfortunately, this group of therapeutics still has many drawbacks. There is a strong demand for research on a new substances and develo-ping targeted therapy strategies. In the present study we tested VapC toxin derived from prokaryot
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4

Stone, Marvin J. "Immunotoxins as Potential Anticancer Agents." Baylor University Medical Center Proceedings 3, no. 4 (1990): 35–37. http://dx.doi.org/10.1080/08998280.1990.11929736.

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5

Pincus, Seth H. "Therapeutic potential of anti-HIV immunotoxins." Antiviral Research 33, no. 1 (1996): 1–9. http://dx.doi.org/10.1016/s0166-3542(96)00995-3.

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Kawakami, Koji, Oumi Nakajima, Ryuichi Morishita, and Ryozo Nagai. "Targeted Anticancer Immunotoxins and Cytotoxic Agents with Direct Killing Moieties." Scientific World JOURNAL 6 (2006): 781–90. http://dx.doi.org/10.1100/tsw.2006.162.

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Despite the progress of the bioinformatics approach to characterize cell-surface antigens and receptors on tumor cells, it remains difficult to generate novel cancer vaccines or neutralizing monoclonal antibody therapeutics. Among targeted cancer therapeutics, biologicals with targetable antibodies or ligands conjugated or fused to toxins or chemicals for direct cell-killing ability have been developed over the last 2 decades. These conjugated or fused chimeric proteins are termed immunotoxins or cytotoxic agents. Two agents, DAB389IL-2 (ONTAKTM) targeting the interleukin-2 receptor and CD33-c
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Weldon, John E., Laiman Xiang, Oleg Chertov, et al. "A protease-resistant immunotoxin against CD22 with greatly increased activity against CLL and diminished animal toxicity." Blood 113, no. 16 (2009): 3792–800. http://dx.doi.org/10.1182/blood-2008-08-173195.

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Abstract Immunotoxins based on Pseudomonas exotoxin A (PE) are promising anticancer agents that combine a variable fragment (Fv) from an antibody to a tumor-associated antigen with a 38-kDa fragment of PE (PE38). The intoxication pathway of PE immunotoxins involves receptor-mediated internalization and trafficking through endosomes/lysosomes, during which the immunotoxin undergoes important proteolytic processing steps but must otherwise remain intact for eventual transport to the cytosol. We have investigated the proteolytic susceptibility of PE38 immunotoxins to lysosomal proteases and found
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Narbona, Javier, Rubén G. Gordo, Jaime Tomé-Amat та Javier Lacadena. "A New Optimized Version of a Colorectal Cancer-Targeted Immunotoxin Based on a Non-Immunogenic Variant of the Ribotoxin α-Sarcin". Cancers 15, № 4 (2023): 1114. http://dx.doi.org/10.3390/cancers15041114.

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Due to its incidence and mortality, cancer remains one of the main risks to human health and lifespans. In order to overcome this worldwide disease, immunotherapy and the therapeutic use of immunotoxins have arisen as promising approaches. However, the immunogenicity of foreign proteins limits the dose of immunotoxins administered, thereby leading to a decrease in its therapeutic benefit. In this study, we designed two different variants of non-immunogenic immunotoxins (IMTXA33αSDI and IMTXA33furαSDI) based on a deimmunized variant of the ribotoxin α-sarcin. The inclusion of a furin cleavage s
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Balalaeva, I. V., E. A. Sokolova, A. D. Puzhikhina, A. A. Brilkina, and S. M. Deyev. "Spheroids of HER2-Positive Breast Adenocarcinoma for Studying Anticancer Immunotoxins In Vitro." Acta Naturae 9, no. 1 (2017): 38–44. http://dx.doi.org/10.32607/20758251-2017-9-1-38-44.

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Tumor response to therapeutic treatment is largely determined by its heterogeneity and the presence of intercellular junctions, hindering the penetration of large molecules deep into the three-dimensional structure of the tumor. In that context, 3D in vitro tumor models such as cancer cell spheroids are becoming increasingly popular. We obtained spheroids of human breast adenocarcinoma SKBR-3 overexpressing the HER2 cancer marker. The toxicity of HER2-targeted immunotoxin 4D5scFv-PE40 against spheroids was shown to be several orders of magnitude lower compared to a monolayer cell culture. The
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10

Ruiz-de-la-Herrán, Javier, Jaime Tomé-Amat, Rodrigo Lázaro-Gorines, José G. Gavilanes та Javier Lacadena. "Inclusion of a Furin Cleavage Site Enhances Antitumor Efficacy against Colorectal Cancer Cells of Ribotoxin α-Sarcin- or RNase T1-Based Immunotoxins". Toxins 11, № 10 (2019): 593. http://dx.doi.org/10.3390/toxins11100593.

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Immunotoxins are chimeric molecules that combine the specificity of an antibody to recognize and bind tumor antigens with the potency of the enzymatic activity of a toxin, thus, promoting the death of target cells. Among them, RNases-based immunotoxins have arisen as promising antitumor therapeutic agents. In this work, we describe the production and purification of two new immunoconjugates, based on RNase T1 and the fungal ribotoxin α-sarcin, with optimized properties for tumor treatment due to the inclusion of a furin cleavage site. Circular dichroism spectroscopy, ribonucleolytic activity s
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