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Biochemical and Biophysical Research Communications|August 31, 2001
An anti-EGF monoclonal antibody that detects intramolecular communication in factor IXK E Persson, K E Knobe, J Stenflo
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1974
Vitamin K dependent modifications of glutamic acid residues in prothrombinJ Stenflo, P Fernlund, W Egan, et al.
The Journal of Biological Chemistry|August 10, 1975
Vitamin K and the biosynthesis of prothrombin. V. Gamma-carboxyglutamic acids, the vitamin K-dependent structures in prothrombinP Fernlund, J Stenflo, P Roepstorff, et al.
Haemophilia : the Official Journal of the World Federation of Hemophilia|January 30, 2009
The plasma concentration of activated protein C appears normal in patients with haemophiliaS Schulman, A Eelde, M Blombäck, et al.
The Journal of Biological Chemistry|February 15, 1992
Effects of gamma-carboxyglutamic acid and epidermal growth factor-like modules of factor IX on factor X activation. Studies using proteolytic fragments of bovine factor IXJ Astermark, P J Hogg, I Björk, et al.
Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics|September 4, 2008
Superluminal tunneling of microwaves in smoothly varying transmission linesA B Shvartsburg, M Marklund, G Brodin, et al.
Biochemistry|August 28, 1990
Molecular analysis of the gene for vitamin K dependent protein S and its pseudogene. Cloning and partial gene organizationC M Edenbrandt, A Lundwall, R Wydro, et al.
FEBS Letters|February 19, 1998
Calcium binding to the first EGF-like module of human factor IX in a recombinant fragment containing residues 1-85. Mutations V46E and Q50E each manifest a negligible increase in calcium affinityK E Persson, J Astermark, I Björk, et al.
Biochemical and Biophysical Research Communications|June 15, 2004
Isolation and characterization of three novel Gla-containing Conus marmoreus venom peptides, one with a novel cysteine patternKarin Hansson, Bruce Furie, Barbara C Furie, et al.
The Journal of Biological Chemistry|February 5, 1991
Structural requirements for Ca2+ binding to the gamma-carboxyglutamic acid and epidermal growth factor-like regions of factor IX. Studies using intact domains isolated from controlled proteolytic digests of bovine factor IXJ Astermark, I Björk, A K Ohlin, et al.
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