W. T. Christiansen

发表

Structure-function assessment of the role of the helical stack domain in the properties of human recombinant protein C and activated protein C.

F. Castellino, J. Geng, W. T. Christiansen, 1995, Biochemistry.

Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid Vesicles.

F. Castellino, M. Prorok, W. T. Christiansen, 1995, Biochemistry.

Properties of recombinant chimeric human protein C and activated protein C containing the gamma-carboxyglutamic acid and trailing helical stack domains of protein C replaced by those of human coagulation factor IX.

F. Castellino, W. T. Christiansen, 1994, Biochemistry.

The activities of recombinant gamma-carboxyglutamic-acid-deficient mutants of activated human protein C toward human coagulation factor Va and factor VIII in purified systems and in plasma.

F. Castellino, L. Zhang, W. T. Christiansen, 1994, Biochemistry.

Functions of individual gamma-carboxyglutamic acid (Gla) residues of human protein c. Determination of functionally nonessential Gla residues and correlations with their mode of binding to calcium.

A. Tulinsky, F. Castellino, W. T. Christiansen, 1994, Biochemistry.

Construction, expression, and properties of a recombinant chimeric human protein C with replacement of its growth factor-like domains by those of human coagulation factor IX.

F. Castellino, L. Zhang, W. T. Christiansen, 1994, Biochemistry.

Transfer of specific endothelial cell-binding properties from the procoagulant protein human factor IX into the anticoagulant protein human protein C.

F. Castellino, E. Plow, J. Geng, 1995, Biochemistry.

The hydrophobic nature of residue-5 of human protein C is a major determinant of its functional interactions with acidic phospholipid vesicles.

F. Castellino, W. T. Christiansen, L. Jalbert, 1996, Biochemistry.