Identification of Functionally Important Amino Acid Residues within the C2-Domain of Human Factor V Using Alanine-Scanning Mutagenesis
- 1 February 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 39 (8) , 1951-1958
- https://doi.org/10.1021/bi992256r
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micellesBiochemical Journal, 1998
- Roles of factor Va heavy and light chains in protein and lipid rearrangements associated with the formation of a bovine factor Va-membrane complexBiophysical Journal, 1997
- Cleavage Requirements for Activation of Factor V by Factor XaEuropean Journal of Biochemistry, 1997
- The X-ray structure of human serum ceruloplasmin at 3.1 Å: nature of the copper centresJBIC Journal of Biological Inorganic Chemistry, 1996
- Interactions of protein antigens with antibodies.Proceedings of the National Academy of Sciences, 1996
- Characterization of an acquired inhibitor to coagulation factor V. Antibody binding to the second C-type domain of factor V inhibits the binding of factor V to phosphatidylserine and neutralizes procoagulant activity.Journal of Clinical Investigation, 1992
- Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins.Proceedings of the National Academy of Sciences, 1984
- Human coagluation factor V purification and thrombin-catalyzed activation.Journal of Clinical Investigation, 1980
- Hemorrhagic death associated with a high titer factor V inhibitorAmerican Journal of Hematology, 1978