Direct characterization of factor VIII in plasma: detection of a mutation altering a thrombin cleavage site (arginine-372----histidine).

Gelijkaardige items

• Cysteamine enhances the procoagulant activity of Factor VIII-East Hartford, a dysfunctional protein due to a light chain thrombin cleavage site mutation (arginine-1689 to cysteine).
  door: Aly, A M, et al.
  Gepubliceerd in: (1992)
• Partial correction of a severe molecular defect in hemophilia A, because of errors during expression of the factor VIII gene.
  door: Young, M, et al.
  Gepubliceerd in: (1997)
• Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P(1) site
  door: Nogami, Keiji, et al.
  Gepubliceerd in: (2005)
• Molecular basis of factor VIII inhibition by human antibodies. Antibodies that bind to the factor VIII light chain prevent the interaction of factor VIII with phospholipid.
  door: Arai, M, et al.
  Gepubliceerd in: (1989)
• Cleavage at Arg-1689 Influences Heavy Chain Cleavages during Thrombin-catalyzed Activation of Factor VIII
  door: Newell, Jennifer L., et al.
  Gepubliceerd in: (2009)