D. Straight

发表

Binding of alpha 2-macroglobulin-thrombin complexes and methylamine-treated alpha 2-macroglobulin to human blood monocytes.

R. Snyderman, P. McKee, L. Jakoi, 1988, Biochemistry.

A coagulation factor IX-deficient mouse model for human hemophilia B.

N. Maeda, O. Smithies, D. Stafford, 1997, Blood.

Gla domain mutants in vivo Circulating and binding characteristics of wild-type factor IX and certain

H. Roberts, D. Stafford, Hui-feng Lin, 2013 .

Changing Residue 338 in Human Factor IX from Arginine to Alanine Causes an Increase in Catalytic Activity*

W. Bode, H. Brandstetter, Jianping Jin, 1998, The Journal of Biological Chemistry.

A Conserved Region of Human Vitamin K-dependent Carboxylase between Residues 393 and 404 Is Important for Its Interaction with the Glutamate Substrate*

F. Acher, D. Stafford, V. Mutucumarana, 2003, Journal of Biological Chemistry.

The effects of fibrinogen and its cleavage products on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity.

P. McKee, L. Fretto, M. A. Lucas, 1983, The Journal of biological chemistry.

Binding of the Factor IX γ-Carboxyglutamic Acid Domain to the Vitamin K-dependent γ-Glutamyl Carboxylase Active Site Induces an Allosteric Effect That May Ensure Processive Carboxylation and Regulate the Release of Carboxylated Product*

D. Stafford, P. Lin, D. Straight, 2004, Journal of Biological Chemistry.

The Putative Vitamin K-dependent γ-Glutamyl Carboxylase Internal Propeptide Appears to Be the Propeptide Binding Site*

D. Stafford, J. Tie, D. Jin, 2002, The Journal of Biological Chemistry.

Effect of protease binding by alpha 2-macroglobulin on intrinsic fluorescence.

P. McKee, D. Straight, 1982, Biochemistry.

The roles of factor VII's structural domains in tissue factor binding.

D. Stafford, J. Chang, D. Stafford, 1995, Biochemistry.

Circulating and binding characteristics of wild-type factor IX and certain Gla domain mutants in vivo.

Tong Gui, H. Roberts, D. Stafford, 2002, Blood.

Functional study of the vitamin K cycle in mammalian cells.

D. Stafford, J. Tie, D. Jin, 2011, Blood.

Structural and functional characterization of the inhibition of urokinase by alpha 2-macroglobulin.

P. McKee, D. Straight, M. A. Hassett, 1985, Biochemistry.

Activation of normal and abnormal human factor IX with trypsin.

M. Griffith, D. Monroe, C. Noyes, 1985, Archives of biochemistry and biophysics.

Bovine alpha- and beta-thrombin. Reduced fibrinogen-clotting activity of beta-thrombin is not a consequence of reduced affinity for fibrinogen.

K. Mann, R. Lundblad, J. Jenzano, 1984, The Journal of biological chemistry.

Determination of Disulfide Bond Assignment of Human Vitamin K-dependent γ-Glutamyl Carboxylase by Matrix-assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry*

D. Stafford, R. Pope, J. Tie, 2003, Journal of Biological Chemistry.

Identification of the N-linked glycosylation sites of vitamin K-dependent carboxylase and effect of glycosylation on carboxylase function.

D. Stafford, R. Pope, J. Tie, 2006, Biochemistry.

Effect of Vitamin K-dependent Protein Precursor Propeptide, Vitamin K Hydroquinone, and Glutamate Substrate Binding on the Structure and Function of γ-Glutamyl Carboxylase*

J. Jorgenson, D. Stafford, V. Mutucumarana, 2010, The Journal of Biological Chemistry.

Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation, in the human vitamin K-dependent gamma-glutamyl carboxylase.

L. Perera, D. Stafford, J. Tie, 2008, Biochemistry.

INTRINSIC FLUORESCENCE ANALYSES OF STRUCTURE‐FUNCTION: RELATIONSHIPS DURING α2‐MACROGLOBULIN‐PROTEASE REACTIONS a

P. McKee, D. Straight, 1983 .

Characterization of thrombin binding to alpha 2-macroglobulin.

P. McKee, D. Straight, 1984, The Journal of biological chemistry.

The role of the epidermal growth factor-1 and hydrophobic stack domains of human factor IX in binding to endothelial cells.

W. Cheung, D. Straight, D. Stafford, 1991, The Journal of biological chemistry.

Structural and functional characteristics of activated human factor IX after chemical modification of gamma-carboxyglutamic acid residues.

R. Hiskey, M. Griffith, C. Noyes, 1985, The Journal of biological chemistry.

Inactivation of human blood coagulation factor X by chemical modification of gamma-carboxyglutamic acid residues.

R. Hiskey, M. Griffith, H. Roberts, 1984, Biochemical and biophysical research communications.