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- W2949242763 abstract "Significance Cardiovascular disease represents a significant health challenge, with towering economic and social costs resulting from the high levels of associated morbidity and mortality. For conditions resulting from undesired blood clotting, treatment options remain limited and are accompanied by significant side effects. Using a rapid chemical ligation platform, 34 homogeneously modified variants of tick anticoagulant proteins were generated. Access to this synthetic protein library enabled key structure–activity relationships to be elucidated and revealed unexpected differences in the mechanism of thrombin inhibition by this group of otherwise closely related molecules. The synthetic platform reported here provides a unique means to expedite the generation and identification of polypeptide and protein therapeutic leads for clotting-associated diseases." @default.
- W2949242763 created "2019-06-27" @default.
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- W2949242763 date "2019-06-20" @default.
- W2949242763 modified "2023-10-02" @default.
- W2949242763 title "Rapid assembly and profiling of an anticoagulant sulfoprotein library" @default.
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- W2949242763 doi "https://doi.org/10.1073/pnas.1905177116" @default.
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