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• W2021067723 endingPage "608" @default.
• W2021067723 startingPage "600" @default.
• W2021067723 abstract "Antibodies are large and complex molecules, with two identical parts that bind independently of each other onto the antigen and the third part of the molecule that dictates the effector function(s). To improve the therapeutic value of antibodies, protein-engineering endeavors reduced the size of the antigen-binding moiety to a single-domain unit. Occasionally, it was demonstrated that the single-domain antigen-binding derivatives of antibodies can have--on their own--an agonistic (or antagonistic) effect on their target. The small size and strict monomeric behavior, in combination with other biochemical properties such as high solubility and high specificity and affinity for the cognate antigen, make single-domain antibodies ideal to design novel man-made conjugates harnessed with innovative effector functions outside the reach of classical antibodies." @default.
• W2021067723 created "2016-06-24" @default.
• W2021067723 creator A5023971009 @default.
• W2021067723 creator A5049845759 @default.
• W2021067723 creator A5070576417 @default.
• W2021067723 date "2008-10-01" @default.
• W2021067723 modified "2023-10-17" @default.
• W2021067723 title "Single-domain antibodies as building blocks for novel therapeutics" @default.
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• W2021067723 doi "https://doi.org/10.1016/j.coph.2008.07.006" @default.
• W2021067723 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18691671" @default.
• W2021067723 hasPublicationYear "2008" @default.
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