Surface Loop 199–204 in Blood Coagulation Factor IX Is a Cofactor-dependent Site Involved in Macromolecular Substrate Interaction

This publication has 31 references indexed in Scilit:

• Influence of cofactor binding and active site occupancy on the conformation of the macromolecular substrate exosite of factor VIIa
  Journal of Molecular Biology, 1998
• The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa 1 1Edited by T. Richmond
  Journal of Molecular Biology, 1997
• Ca2+ Binding to the First Epidermal Growth Factor-like Domain of Human Blood Coagulation Factor IX Promotes Enzyme Activity and Factor VIII Light Chain Binding
  Published by Elsevier ,1996
• The Sequence Glu1811-Lys1818 of Human Blood Coagulation Factor VIII Comprises a Binding Site for Activated Factor IX
  Published by Elsevier ,1996
• Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin
  Biochemistry, 1994
• Protein engineering of the hydrophobic domain of human factor IX
  Protein Engineering, Design and Selection, 1994
• The coagulation cascade: initiation, maintenance, and regulation
  Biochemistry, 1991
• The molecular basis of blood coagulation
  Cell, 1988
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor
  Journal of Molecular Biology, 1974