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- W2012328380 endingPage "197" @default.
- W2012328380 startingPage "186" @default.
- W2012328380 abstract "Due to their unlimited chemical diversity, small molecules can rival monoclonal antibodies (mAbs) with respect to specificity and affinity for target molecules. However, key pharmacological properties of mAbs remain unmatched by small molecules. Chemical programming strategies have been developed for site-specific and covalent conjugation of small molecules to mAbs with unique reactivity centers. In addition to blending favorable features of small molecules and mAbs, chemically programmed antibodies (cpAbs) are economically attractive because they utilize the same mAb for an almost unlimited number of target molecule specificities, reducing manufacturing costs and shortening drug discovery and development time. Preclinical studies and clinical trials have begun to demonstrate the broad utility of cpAbs for the treatment and prevention of human diseases." @default.
- W2012328380 created "2016-06-24" @default.
- W2012328380 creator A5065812703 @default.
- W2012328380 date "2014-04-01" @default.
- W2012328380 modified "2023-10-18" @default.
- W2012328380 title "Chemically programmed antibodies" @default.
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- W2012328380 doi "https://doi.org/10.1016/j.tibtech.2014.02.003" @default.
- W2012328380 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3978777" @default.
- W2012328380 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24630478" @default.
- W2012328380 hasPublicationYear "2014" @default.
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