Johan Stenflo
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- 1998
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Mark
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 affinity
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- Contribution to journal › Article
- 1994
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Mark
Baculovirus-mediated expression of the epidermal growth factor-like modules of human factor IX fused to the factor XIIIa transamidation site in fibronectin. Evidence for a direct interaction between the NH2-terminal epidermal growth factor-like module of factor IXa beta and factor X
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- Contribution to journal › Article
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Mark
The gamma-carboxyglutamic acid and epidermal growth factor-like modules of factor IXa beta. Effects on the serine protease module and factor X activation
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- Contribution to journal › Article
- 1993
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Mark
Isolation of intact modules from noncatalytic parts of vitamin K-dependent coagulation factors IX and X and protein C
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- Contribution to journal › Article
- 1992
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Mark
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 IX
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- Contribution to journal › Article
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Mark
Three-Dimensional Structure of the Apo Form of the N-Terminal EGF-like Module of Blood Coagulation Factor X As Determined by NMR Spectroscopy and Simulated Folding
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- Contribution to journal › Article
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Mark
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
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- Contribution to journal › Article
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Mark
Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from cells throughout the male reproductive system
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- Contribution to journal › Article
- 1991
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Mark
The epidermal growth factor-like domains of factor IX. Effect on blood clotting and endothelial cell binding of a fragment containing the epidermal growth factor-like domains linked to the gamma-carboxyglutamic acid region
(
- Contribution to journal › Article
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Mark
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 IX
(
- Contribution to journal › Article