Authors: Idinath Badirou, Mohamad Kurdi, Paulette Legendre, Julie Rayes, Marijke Bryckaert, Caterina Casari, Peter J. Lenting, Olivier D. Christophe, Cecile V. Denis
DOI: 10.1371/journal.pone.0037508
Abstract Summary
New research reveals that O-glycosylations in von Willebrand factor (VWF) aren’t needed for normal protein assembly, but specific sites are crucial for function. Mutations at T1255 and T1256 reduced VWF plasma levels and impaired blood clotting in mice, while S1486 proved essential for platelet binding. These findings identify key molecular targets that maintain hemostasis.
Why Brain? ðŸ§
Study reveals specific sugar modifications on von Willebrand factor are crucial for maintaining normal blood clotting, identifying key sites that affect protein stability and platelet binding in bleeding disorders.
The image is AI-generated for illustrative purposes only. Courtesy of Midjourney.
