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- W2153309584 abstract "Ideally, an immunotoxin should be inactive 'en route', acquire activity only after tumor cell surface binding and have no off-target effects towards normal cells. In this respect, antibody-based fusion proteins that exploit the tumor-selective pro-apoptotic death ligands sFasL and sTRAIL appear promising. Soluble FasL largely lacks receptor-activating potential, whereas sTRAIL is inactive towards normal cells. Fusion proteins in which an anti-tumor antibody fragment (scFv) is fused to sFasL or sTRAIL prove to be essentially inactive when soluble, while gaining potent anti-tumor activity after selective binding to a predefined tumor-associated cell surface antigen. Importantly, off-target binding by scFv:sTRAIL to normal cells showed no signs of toxicity. In this review, we highlight the rationale and perspectives of scFv:TRAIL/scFv:sFasL based fusion proteins for cancer therapy." @default.
- W2153309584 created "2016-06-24" @default.
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- W2153309584 date "2013-05-01" @default.
- W2153309584 modified "2023-10-14" @default.
- W2153309584 title "Antibody-based fusion proteins to target death receptors in cancer" @default.
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- W2153309584 doi "https://doi.org/10.1016/j.canlet.2010.11.006" @default.
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