Results 41 to 50 of about 12,705,637 (166)
Molecular models of the procoagulant Factor VIIIa–Factor IXa complex
Formation of the intrinsic tenase complex is an essential event in the procoagulant reactions that lead to clot formation. The tenase complex is formed when the activated serine protease, Factor IXa (FIXa), and its cofactor Factor VIIIa (FVIIIa) assemble on a phospholipid surface to proteolytically convert the zymogen Factor X (FX) into its active form
L. Autin +5 more
semanticscholar +3 more sources
Recombinant Factor IX Fc Fusion Protein Maintains Full Procoagulant Properties and Exhibits Prolonged Efficacy in Hemophilia B Mice. [PDF]
INTRODUCTION:Hemophilia B is an inherited X chromosome-linked disorder characterized by impaired blood clotting owing to the absence of functional coagulation factor IX.
Garabet G Toby +8 more
doaj +1 more source
Periocular subcutaneous granuloma annulare in a child: A case report
Purpose: We describe a rare case of annular granuloma involving the eyelid of a child, a 6-year-old male, who presented with multiple subcutaneous nodular lesions involving the upper eyelid of the right eye. Observations: The slit-lamp examination of the
Aysha Waheed AlOqab +2 more
doaj +1 more source
Localization of a Factor X Interactive Site in the A1 Subunit of Factor VIIIa [PDF]
The protein cofactor, factor (F) VIIIa, is required for the efficient conversion of the substrate FX to FXa by the serine protease FIXa. The interaction between human FVIII (and its constituent subunits) and FX was characterized using a solid phase binding assay performed in the absence of phospholipid and FIXa. Saturable binding of FX to heterodimeric
Kirsty A. Lapan, Philip J. Fay
openalex +4 more sources
Introduction Despite decades of brain MRI research demonstrating atypical neuroanatomical substrate in patients with autism spectrum disorder (ASD), it remains unclear whether and to what extent disorder-selective neuroanatomical abnormalities occur in ...
D. Liloia +6 more
doaj +1 more source
Phosphorylation of factor Va and factor VIIIa by activated platelets [PDF]
Platelet activation leads to the incorporation of 32[PO4(2-)] into bovine coagulation factor Va and recombinant human factor VIII. In the presence of the soluble fraction from thrombin-activated platelets and (gamma-32P) adenosine triphosphate, radioactivity is incorporated exclusively into the M(r) = 94,000 heavy chain (H94) of factor Va and into the ...
M, Kalafatis +4 more
openaire +3 more sources
A3 domain residue Glu1829 contributes to A2 subunit retention in factor VIIIa [PDF]
Abstract Factor VIII circulates as a heterodimer composed of a heavy chain (HC) and light chain (LC). Thrombin converts factor VIII into the active cofactor, factor VIIIa, by cleaving HC into A1 and A2 subunits. While the A1 subunit maintains a stable interaction with the LC-derived A3C1C2 subunit, the A2 subunit is weakly associated in ...
Hironao Wakabayashi +3 more
openalex +4 more sources
Cleavage of Factor VIII Light Chain Is Required for Maximal Generation of Factor VIIIa Activity [PDF]
Thrombin-catalyzed activation of heterodimeric factor VIII occurs by limited proteolysis, yielding subunits A1 and A2 derived from the heavy chain (HC) and A3-C1-C2 derived from the light chain (LC). The roles of these cleavages in the function of procoagulant activity are poorly understood.
Lisa M. Regan, Philip J. Fay
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Background The yellow scorpion Tityus serrulatus (Ts) is responsible for the highest number of accidents and the most severe scorpion envenoming in Brazil. Although its venom has been studied since the 1950s, it presents a number of orphan peptides that
Priscila C. Lima +6 more
doaj +1 more source
Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa [PDF]
Individuals with hemophilia A require frequent infusion of preparations of coagulation factor VIII. The activity of factor VIII (FVIII) as a cofactor for factor IXa in the coagulation cascade is limited by its instability after activation by thrombin.
S W, Pipe, R J, Kaufman
openaire +2 more sources

