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Biochemical and Biophysical Research Communications
|
February 13, 2001
A functional prothrombin gene product is synthesized by human kidney cells
L 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 thrombosis
K 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 X
E 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 activity
A 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 proteins
M 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 thrombomodulin
M 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 study
M Sunnerhagen, G A Olah, J Stenflo, et al.
The Journal of Biological Chemistry
|
June 25, 1979
Multiple modes of association in bovine prothrombin and its proteolysis products
C M Jackson, C W Peng, G M Brenckle, et al.
The Journal of Biological Chemistry
|
September 25, 1992
How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X
M Selander-Sunnerhagen, M Ullner, E Persson, et al.
Blood Cells, Molecules & Diseases
|
February 10, 2006
The complex between activated protein C and protein C inhibitor: A clinically useful indicator of aortic aneurysms?
J Stenflo, M Kjellberg, K Strandberg, et al.
Page
of 13
Search research articles
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Showing results (101-110 of 124) with videos related to
Sort By:
Page
of 13
Biochemical and Biophysical Research Communications
|
February 13, 2001
A functional prothrombin gene product is synthesized by human kidney cells
L 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 thrombosis
K 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 X
E 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 activity
A 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 proteins
M 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 thrombomodulin
M 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 study
M Sunnerhagen, G A Olah, J Stenflo, et al.
The Journal of Biological Chemistry
|
June 25, 1979
Multiple modes of association in bovine prothrombin and its proteolysis products
C M Jackson, C W Peng, G M Brenckle, et al.
The Journal of Biological Chemistry
|
September 25, 1992
How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X
M Selander-Sunnerhagen, M Ullner, E Persson, et al.
Blood Cells, Molecules & Diseases
|
February 10, 2006
The complex between activated protein C and protein C inhibitor: A clinically useful indicator of aortic aneurysms?
J Stenflo, M Kjellberg, K Strandberg, et al.
Page
of 13