results provide novel insights on the adsorption and binding mechanism of the FVIII on cell membrane and will be helpful for the design of anticoagulant materials
Our structure provides insight into many von Willebrand disease mutations including those that diminish factor VIII binding which suggest that factor VIII binds not only to the N-terminal TIL' domain of D' distal from D3 but also extends across 1 side of D3.
Factor VIII 3E6 antibody binding decreases the thermal motion behavior of surface loops in the C2 domain on the opposing face thereby suggesting that cooperative antibody binding is a dynamic effect.
findings provide novel insights into VWFFVIII complex formation leading to a greater understanding of the molecular basis of the bleeding diathesis type 2N VWD.
These results illustrate the potential complexities of the polyclonal anti-factor VIII immune response and further define the "classical" and "nonclassical" types of antibody inhibitors against the factor VIII C2 domain.
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