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The Journal of Biological Chemistry|September 5, 1985
Protein C in bovine plasma after warfarin treatment. Purification, partial characterization, and beta-hydroxyaspartic acid contentT Sugo, U Persson, J StenfloThe Journal of Biological Chemistry|June 10, 1982
Thrombin-catalyzed activation of human coagulation factor VK Suzuki, B Dahlbäck, J StenfloPhysical Review Letters|November 13, 2003
Electromagnetic wave collapse in a radiation backgroundMattias Marklund, Gert Brodin, Lennart StenfloEuropean Journal of Biochemistry|March 26, 1999
The epidermal growth factor precursor. A calcium-binding, beta-hydroxyasparagine containing modular protein present on the surface of plateletsC Valcarce, I Björk, J StenfloJournal of Thrombosis and Haemostasis : JTH|January 18, 2006
The cleaved and latent forms of antithrombin are normal constituents of blood plasma: a quantitative method to measure cleaved antithrombinM Kjellberg, T Ikonomou, J StenfloThe Journal of Biological Chemistry|October 21, 1994
Calcium-dependent interaction between gamma-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor XC Valcarce, A Holmgren, J StenfloThe Journal of Biological Chemistry|February 5, 1991
The gamma-carboxyglutamic acid and epidermal growth factor-like domains of factor X. Effect of isolated domains on prothrombin activation and endothelial cell binding of factor XE Persson, C Valcarce, J StenfloFEBS Letters|January 2, 1984
erythro-beta-Hydroxyaspartic acid in bovine factor IX and factor XT Sugo, P Fernlund, J StenfloProceedings of the National Academy of Sciences of the United States of America|January 1, 1987
beta-Hydroxyasparagine in domains homologous to the epidermal growth factor precursor in vitamin K-dependent protein SJ Stenflo, A Lundwall, B DahlbäckJournal of Thrombosis and Haemostasis : JTH|October 25, 2006
An immunochemical method for quantitative determination of latent antithrombin, the reactive center loop-inserted uncleaved form of antithrombinM Kjellberg, B Rimac, J StenfloPageof 87,334