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Biochemical and Biophysical Research Communications|May 1, 2001
Synthesis of gamma-carboxylated polypeptides by alpha-cells of the pancreatic isletsL M Stenberg, E Nilsson, O Ljungberg, et al.
Protein Science : a Publication of the Protein Society|October 23, 1997
Calcium binding to tandem repeats of EGF-like modules. Expression and characterization of the EGF-like modules of human Notch-1 implicated in receptor-ligand interactionsM D Rand, A Lindblom, J Carlson, et al.
Journal of Molecular Biology|November 2, 1999
EGF-like module pair 3-4 in vitamin K-dependent protein S: modulation of calcium affinity of module 4 by module 3, and interaction with factor XY Stenberg, A Muranyi, C Steen, et al.
Biochemical and Biophysical Research Communications|February 13, 2001
A functional prothrombin gene product is synthesized by human kidney cellsL M Stenberg, M A Brown, E Nilsson, et al.
Thrombosis and Haemostasis|January 5, 2002
Complexes between activated protein C and protein C inhibitor measured with a new method: comparison of performance with other markers of hypercoagulability in the diagnosis of deep vein thrombosisK Strandberg, J Astermark, O Björgell, et al.
The Journal of Biological Chemistry|October 5, 1989
Calcium binding to the isolated beta-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor XE Persson, M Selander, S Linse, et al.
The Journal of Biological Chemistry|December 15, 1988
Beta-hydroxyaspartic acid in the first epidermal growth factor-like domain of protein C. Its role in Ca2+ binding and biological activityA K Ohlin, G Landes, P Bourdon, et al.
Nature Structural Biology|June 1, 1995
Structure of the Ca(2+)-free Gla domain sheds light on membrane binding of blood coagulation proteinsM Sunnerhagen, S Forsén, A M Hoffrén, et al.
The Journal of Biological Chemistry|June 15, 1988
Relationship between anticoagulant activities and polyanionic properties of rabbit thrombomodulinM C Bourin, A K Ohlin, D A Lane, et al.
Biochemistry|September 10, 1996
The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering studyM Sunnerhagen, G A Olah, J Stenflo, et al.
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