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Protein Expression and Purification|January 13, 1998
An efficient system for production of recombinant urokinase-type plasminogen activatorW Tang, Z Y Sun, R Pannell, et al.Thrombosis Research|January 11, 2001
Catalytic and fibrinolytic properties of recombinant urokinase plasminogen activator from E. coli, mammalian, and yeast cellsP Wang, J Zhang, Z Sun, et al.Thrombosis Research|October 24, 2001
Urokinase-type plasminogen activator up-regulates its own expression by endothelial cells and monocytes via the u-PAR pathwayC Li, J Zhang, Y Jiang, et al.The Journal of Clinical Investigation|June 1, 1984
Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-urokinase). A study in vitro and in two animal speciesV Gurewich, R Pannell, S Louie, et al.British Medical Journal|July 10, 1971
Passive flexion and femoral vein flow: a study using a motorized foot moverV C Roberts, S Sabri, M C Pietroni, et al.The Journal of Biological Chemistry|July 5, 1990
Thrombospondin forms complexes with single-chain and two-chain forms of urokinaseR L Silverstein, R L Nachman, R Pannell, et al.Biochemistry|April 16, 1998
Analysis of the forces which stabilize the active conformation of urokinase-type plasminogen activatorZ Sun, B F Liu, Y Chen, et al.Journal of Thrombosis and Haemostasis : JTH|July 15, 2006
Thrombolysis vs. bleeding from hemostatic sites by a prourokinase mutant compared with tissue plasminogen activatorV Gurewich, R Pannell, A Simmons-Byrd, et al.Artery|January 1, 1987
Lipids, lipoproteins, fibrinogen and fibrinolytic activity in angiographically assessed coronary heart diseaseI Lipinska, V Gurewich, C M Meriam, et al.Biochemistry|November 12, 1996
A site-directed mutagenesis of pro-urokinase which substantially reduces its intrinsic activityJ N Liu, W Tang, Z Y Sun, et al.Pageof 20