D W Stafford - JoVE Visualize

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The Journal of Biological Chemistry|May 2, 1997

The propeptide binding site of the bovine gamma-glutamyl carboxylaseS M Wu, V P Mutucumarana, S Geromanos, et al.

Blood|February 1, 1989

Identification of a F.VIII epitope recognized by a human hemophilic inhibitorB C Lubahn, J Ware, D W Stafford, et al.

Science (New York, N.Y.)|December 13, 1991

Cloning and expression of the cDNA for human gamma-glutamyl carboxylaseS M Wu, W F Cheung, D Frazier, et al.

Blood|September 15, 1994

The role of amino-terminal residues of the heavy chain of factor IXa in the binding of its cofactor, factor VIIIaN Hamaguchi, S P Bajaj, K J Smith, et al.

Proceedings of the National Academy of Sciences of the United States of America|December 14, 2006

Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2Pei-Hsuan Chu, Teng-Yi Huang, Jason Williams, et al.

Biochemistry|November 26, 1999

Amino acids responsible for reduced affinities of vitamin K-dependent propeptides for the carboxylaseT B Stanley, J Humphries, K A High, et al.

The Journal of Biological Chemistry|April 25, 1993

Characterization of the purified vitamin K-dependent gamma-glutamyl carboxylaseD P Morris, B A Soute, C Vermeer, et al.

The Journal of Biological Chemistry|October 15, 1992

The binding of human factor IX to endothelial cells is mediated by residues 3-11W F Cheung, N Hamaguchi, K J Smith, et al.

Journal of Thrombosis and Haemostasis : JTH|May 29, 2013

Evaluation of warfarin resistance using transcription activator-like effector nucleases-mediated vitamin K epoxide reductase knockout HEK293 cellsJ-K Tie, D-Y Jin, K Tie, et al.

The Journal of Biological Chemistry|August 5, 1990

In vitro gamma-carboxylation of a 59-residue recombinant peptide including the propeptide and the gamma-carboxyglutamic acid domain of coagulation factor IX. Effect of mutations near the propeptide cleavage siteS M Wu, B A Soute, C Vermeer, et al.

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Showing results (31-40 of 92) with videos related to

Sort By:

Pageof 10

The Journal of Biological Chemistry|May 2, 1997

The propeptide binding site of the bovine gamma-glutamyl carboxylaseS M Wu, V P Mutucumarana, S Geromanos, et al.

Blood|February 1, 1989

Identification of a F.VIII epitope recognized by a human hemophilic inhibitorB C Lubahn, J Ware, D W Stafford, et al.

Science (New York, N.Y.)|December 13, 1991

Cloning and expression of the cDNA for human gamma-glutamyl carboxylaseS M Wu, W F Cheung, D Frazier, et al.

Blood|September 15, 1994

The role of amino-terminal residues of the heavy chain of factor IXa in the binding of its cofactor, factor VIIIaN Hamaguchi, S P Bajaj, K J Smith, et al.

Proceedings of the National Academy of Sciences of the United States of America|December 14, 2006

Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2Pei-Hsuan Chu, Teng-Yi Huang, Jason Williams, et al.

Biochemistry|November 26, 1999

Amino acids responsible for reduced affinities of vitamin K-dependent propeptides for the carboxylaseT B Stanley, J Humphries, K A High, et al.

The Journal of Biological Chemistry|April 25, 1993

Characterization of the purified vitamin K-dependent gamma-glutamyl carboxylaseD P Morris, B A Soute, C Vermeer, et al.

The Journal of Biological Chemistry|October 15, 1992

The binding of human factor IX to endothelial cells is mediated by residues 3-11W F Cheung, N Hamaguchi, K J Smith, et al.

Journal of Thrombosis and Haemostasis : JTH|May 29, 2013

Evaluation of warfarin resistance using transcription activator-like effector nucleases-mediated vitamin K epoxide reductase knockout HEK293 cellsJ-K Tie, D-Y Jin, K Tie, et al.

The Journal of Biological Chemistry|August 5, 1990

In vitro gamma-carboxylation of a 59-residue recombinant peptide including the propeptide and the gamma-carboxyglutamic acid domain of coagulation factor IX. Effect of mutations near the propeptide cleavage siteS M Wu, B A Soute, C Vermeer, et al.

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