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- W3196571805 abstract "Objective Recent studies indicate that binding of coagulation factor IX (FIX) to extracellular matrix (ECM) contributes to its extravascular (EV) storage and its hemostatic efficacy. It is postulated that the binding affinity of FIX to ECM, more specifically to Collagen IV (Col-IV), increases when Lysine at position 5 is mutated to Arginine (K5R) and decreases when Lysine is mutated to Alanine (K5A). To understand the physiological role of FIX in EV space we aimed to characterize recombinantly generated K5 variants in comparison to wildtype rFIX molecules. We used albumin fused (FP) rFIX variants (rFIX-FP, K5A-FP, K5R-FP) for this purpose." @default.
- W3196571805 created "2021-09-13" @default.
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- W3196571805 date "2021-06-01" @default.
- W3196571805 modified "2023-09-27" @default.
- W3196571805 title "In vitro characterization of K5A and K5R variants of Factor IX" @default.
- W3196571805 doi "https://doi.org/10.1055/s-0041-1728194" @default.
- W3196571805 hasPublicationYear "2021" @default.
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