Results 191 to 200 of about 54,262 (254)

Global research trends and therapeutic potential of fibrinolytic enzymes. [PDF]

open access: yesJ Genet Eng Biotechnol
Hazare C, Bhagwat P, Singh S, Pillai S.
europepmc   +1 more source

Bleeding Complications of Anticoagulation Therapy Used in the Treatment of Acute Coronary Syndromes-Review of the Literature. [PDF]

open access: yesJ Clin Med
Kosowski M   +9 more
europepmc   +1 more source

Bioprinted Micro-Clots for Kinetic Analysis of Endothelial Cell-Mediated Fibrinolysis. [PDF]

open access: yesAdv Healthc Mater
Chang JJ   +5 more
europepmc   +1 more source

Tissue Plasminogen Activator

New England Journal of Medicine, 1988
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.
John A. Oates   +3 more
openaire   +2 more sources

Mechanisms of Plasminogen Activation by Mammalian Plasminogen Activators

Enzyme, 1988
Plasminogen 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
openaire   +2 more sources

Plasminogen activator inhibitors

Trends in Cardiovascular Medicine, 1991
Plasminogen 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 ...
J, Schneiderman, D J, Loskutoff
openaire   +2 more sources

Glycated Proteins Modulate Tissue–Plasminogen Activator-Catalyzed Plasminogen Activation

Biochemical and Biophysical Research Communications, 1997
Plasminogen 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
I W, Bobbink   +5 more
openaire   +2 more sources

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