Publications by authors named "Samhitha Urs Ramaraje Urs"
The structure of human coagulation factor XIII (FXIII), a heterotetrameric plasma pro-transglutaminase that covalently crosslinks pre-formed fibrin polymers, remains elusive until today. The heterotetrameric complex is composed of two catalytic FXIII-A and two protective FXIII-B subunits. Structural etiology underlying FXIII deficiency has so far been derived from crystallographic structures, all of which are currently available for the FXIII-A2 homodimer only.
View Article and Find Full Text PDFBackground: Acquired hemophilia A (AHA) is a rare and severe bleeding disorder characterized by autoantibodies inhibiting coagulation factor (F)VIII. Current treatment of AHA involves bypassing agents or FVIII replacement therapy, yet their efficacy is limited in cases of high inhibitor titers. Emicizumab, a humanized bispecific monoclonal antibody, has shown promising hemostatic effectiveness in persons with congenital hemophilia A (HA) and AHA, but a minority of patients developed anti-drug antibodies (ADAs), compromising its efficacy.
View Article and Find Full Text PDFArticle Synopsis
- Coagulation factor XIII (FXIII) is crucial for regulating the blood clotting process by stabilizing fibrin clots, which helps prevent excessive bleeding and thrombosis.
- FXIII exists as a complex made up of two main subunits, FXIII-A and FXIII-B, which are encoded by specific genes and are essential for its function in hemostasis.
- Recent research indicates that FXIII has various roles beyond coagulation, but most studies focus on its connection to bleeding disorders caused by its deficiency.