Binding of vascular anticoagulant alpha (VAC alpha) to planar phospholipid bilayers.

This publication has 42 references indexed in Scilit:

• Vascular anticoagulant β: a novel human Ca²⁺/phospholipid binding protein that inhibits coagulation and phospholipase A₂ activity
  European Journal of Biochemistry, 1989
• Purification and characterization of a novel protein from bovine aorta that inhibits coagulation
  European Journal of Biochemistry, 1988
• Antibodies to the N-terminus of calpactin II (p35) affect calcium binding and phosphorylation by the epidermal growth factor receptor in vitro
  Biochemistry, 1988
• Prothrombin activation on phospholipid membranes with positive electrostatic potential
  Biochemistry, 1988
• Predicted structure for the calcium-dependent membrane-binding proteins p35, p36 and p32
  Protein Engineering, Design and Selection, 1987
• Primary sequence of bovine calpactin I heavy chain (p36), a major cellular substrate for retroviral protein-tyrosine kinases: homology with the human phospholipase A2 inhibitor lipocortin
  Biochemistry, 1986
• Common domain structure of Ca²⁺ and lipid‐binding proteins
  FEBS Letters, 1986
• Blood Coagulation
  Annual Review of Biochemistry, 1980
• Lipid Asymmetry in Membranes
  Annual Review of Biochemistry, 1979
• The enzymatic synthesis of phosphatidylserine and purification by CM-cellulose column chromatography
  Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1977