Profibrinolytic Factors and Cancer Progression, Metastasis, and Survival. [PDF]
Hisada Y, Mackman N.
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FabG moonlights as an extracellular adhesin mediates cytoadhesion of Streptococcus suis via interaction with plasminogen. [PDF]
Guo G +5 more
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Global research trends and therapeutic potential of fibrinolytic enzymes. [PDF]
Hazare C, Bhagwat P, Singh S, Pillai S.
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Myocardial Infarction in a Patient With Homozygous Plasminogen Activator Inhibitor-1 (PAI-1) 4G/4G Mutation: A Case Report. [PDF]
Manasrah A +4 more
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Bleeding Complications of Anticoagulation Therapy Used in the Treatment of Acute Coronary Syndromes-Review of the Literature. [PDF]
Kosowski M +9 more
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Bioprinted Micro-Clots for Kinetic Analysis of Endothelial Cell-Mediated Fibrinolysis. [PDF]
Chang JJ +5 more
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TISSUE plasminogen activator (t-PA) is a naturally occurring protein that catalyzes the conversion of the inactive proenzyme plasminogen into the active serine protease plasmin.
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Mechanisms of Plasminogen Activation by Mammalian Plasminogen Activators
Enzyme, 1988Plasminogen activators convert the proenzyme plasminogen to the active serine protease plasmin by hydrolysis of the Arg560-Val561 peptide bond. Physiological plasminogen activation is however regulated by several additional molecular interactions resulting in fibrin-specific clot lysis.
H R, Lijnen, D, Collen
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Plasminogen activator inhibitors
Trends in Cardiovascular Medicine, 1991Plasminogen activator inhibitors (PAIs) regulate plasminogen activation in normal and pathologic processes. Plasminogen activator inhibitor 1 (PAI-1) is the major physiologic inhibitor of both tissue-type and urokinase-type plasminogen activators. It is a highly regulated single-chain glycoprotein, whose overexpression in vivo impairs the fibrinolytic ...
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Glycated Proteins Modulate Tissue–Plasminogen Activator-Catalyzed Plasminogen Activation
Biochemical and Biophysical Research Communications, 1997Plasminogen activation by tissue-plasminogen activator (t-PA) is accelerated by the presence of a macromolecular surface, which acts as a template that brings enzyme and substrate in close proximity. Modification of lysine residues, which are important for this template function, occurs in diabetic patients as a consequence of glycation of proteins. In
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