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• W2890834879 abstract "Abstract Urokinase‐type plasminogen activator (uPA) and tissue‐type plasminogen activator (tPA) are two serine proteases that contribute to initiating fibrinolysis by activating plasminogen. uPA is also an important tumour‐associated protease due to its role in extracellular matrix remodelling. Overexpression of uPA has been identified in several different cancers and uPA inhibition has been reported as a promising therapeutic strategy. Although several peptide‐based uPA inhibitors have been developed, the extent to which uPA tolerates different tetrapeptide sequences that span the P1–P4 positions remains to be thoroughly explored. In this study, we screened a sequence‐defined peptide aldehyde library against uPA and tPA. Preferred sequences from the library screen yielded potent inhibitors for uPA, led by Ac‐GTAR‐H ( K i =18 n m ), but not for tPA. Additionally, synthetic peptide substrates corresponding to preferred inhibitor sequences were cleaved with high catalytic efficiency by uPA but not by tPA. These findings provide new insights into the binding specificity of uPA and tPA and the relative activity of tetrapeptide inhibitors and substrates against these enzymes." @default.
• W2890834879 created "2018-09-27" @default.
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• W2890834879 date "2018-10-24" @default.
• W2890834879 modified "2023-10-15" @default.
• W2890834879 title "Characterising the Subsite Specificity of Urokinase‐Type Plasminogen Activator and Tissue‐Type Plasminogen Activator using a Sequence‐Defined Peptide Aldehyde Library" @default.
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• W2890834879 doi "https://doi.org/10.1002/cbic.201800395" @default.
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• W2890834879 hasPublicationYear "2018" @default.
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