PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6742738-6 1984 The clearance of radioactive fibrinogen/thrombin clots from the subcutaneous tissues of the rat was found to be delayed if the rats were given epsilon amino caproic acid but it could not be increased with stanozolol. Aminocaproic Acid 143-169 fibrinogen beta chain Homo sapiens 29-39 4773419-0 1973 [Effect of epsilon-aminocaproic acid on the accumulation of labeled fibrinogen I-131 in the transplantable tumor IMP-1]. Aminocaproic Acid 11-36 fibrinogen beta chain Homo sapiens 68-78 6219709-1 1983 The importance of the lysine binding sites of human plasmin for its ability to digest human fibrinogen has been assessed by analyzing the nature and rate of the products formed in the presence of epsilon-aminocaproic acid. Aminocaproic Acid 196-221 fibrinogen beta chain Homo sapiens 92-102 6219709-3 1983 The presence of epsilon-aminocaproic acid, at concentrations ranging from 0.5-5.0 mM, results in progressively stronger inhibition of the digestion of fibrinogen and in appearance of fibrinogen degradation products Y, D and E, for both Lys77-plasmin, and Val442-plasmin, showing the importance of lysine binding regions in this property. Aminocaproic Acid 16-41 fibrinogen beta chain Homo sapiens 151-161 6219709-3 1983 The presence of epsilon-aminocaproic acid, at concentrations ranging from 0.5-5.0 mM, results in progressively stronger inhibition of the digestion of fibrinogen and in appearance of fibrinogen degradation products Y, D and E, for both Lys77-plasmin, and Val442-plasmin, showing the importance of lysine binding regions in this property. Aminocaproic Acid 16-41 fibrinogen beta chain Homo sapiens 183-193 5314853-2 1971 Thrombin clottable fibrinogen estimates in the presence of epsilon amino caproic acid, fibrinogen and fibrin degradation products. Aminocaproic Acid 59-85 fibrinogen beta chain Homo sapiens 19-29 18794767-3 2008 SUMMARY OF BACKGROUND DATA: Preliminary prospective, prospective randomized double-blind, and fibrinogen studies have demonstrated Amicar to be effective in decreasing perioperative blood loss in patients with idiopathic scoliosis undergoing PSF with SSI. Aminocaproic Acid 131-137 fibrinogen beta chain Homo sapiens 94-104 18981961-3 2008 SUMMARY OF BACKGROUND DATA: Previously, a preliminary prospective; prospective randomized double-blind; same-day anterior and posterior spinal fusion; and fibrinogen studies have demonstrated Amicar to be effective in decreasing total perioperative blood loss and transfusion requirements in surgery for idiopathic scoliosis. Aminocaproic Acid 192-198 fibrinogen beta chain Homo sapiens 155-165 14752343-15 2004 This may be due to elevated fibrinogen levels induced by Amicar. Aminocaproic Acid 57-63 fibrinogen beta chain Homo sapiens 28-38 18316072-9 2008 Epsilon-aminocaproic acid limited bead-cell complexation, suggesting fibrinogen degradation products modulate dendritic cell activity. Aminocaproic Acid 0-25 fibrinogen beta chain Homo sapiens 69-79 16138073-3 2005 SUMMARY OF BACKGROUND DATA: Preliminary prospective, randomized double-blind and analysis of same-day anterior spinal fusion (ASF), fibrinogen, and posterior spinal fusion (PSF) studies have demonstrated Amicar to be effective in idiopathic scoliosis surgery. Aminocaproic Acid 204-210 fibrinogen beta chain Homo sapiens 132-142 17268270-1 2007 STUDY DESIGN: Prospective evaluation of fibrinogen levels before surgery and after surgery in patients with idiopathic scoliosis undergoing posterior spinal fusion (PSF) and segmental spinal instrumentation (SSI) who received Amicar to decrease perioperative blood loss. Aminocaproic Acid 226-232 fibrinogen beta chain Homo sapiens 40-50 17268270-3 2007 SUMMARY OF BACKGROUND DATA: Our previous randomized, double-blind (Amicar and control) study demonstrated a rise in fibrinogen levels on the first postoperative day in the Amicar group, but not in the control group. Aminocaproic Acid 67-73 fibrinogen beta chain Homo sapiens 116-126 17268270-7 2007 METHODS: We analyzed fibrinogen levels before surgery and on all postoperative days (4 or 5 days) until discharge in 51 consecutive patients, including our 21 previously reported patients, who received Amicar and underwent a PSF and SSI. Aminocaproic Acid 202-208 fibrinogen beta chain Homo sapiens 21-31 14755788-0 2004 Quantitative assessment of fibrinogen cross-linking by epsilon aminocaproic acid in patients with end-stage liver disease. Aminocaproic Acid 55-80 fibrinogen beta chain Homo sapiens 27-37 14755788-2 2004 We adapted chemical engineering tools used in polymerization studies to quantify fibrinogen cross-linking by plasma from liver transplant patients obtained before and after epsilon aminocaproic acid (EACA) therapy. Aminocaproic Acid 173-198 fibrinogen beta chain Homo sapiens 81-91 14755788-2 2004 We adapted chemical engineering tools used in polymerization studies to quantify fibrinogen cross-linking by plasma from liver transplant patients obtained before and after epsilon aminocaproic acid (EACA) therapy. Aminocaproic Acid 200-204 fibrinogen beta chain Homo sapiens 81-91 7710120-10 1995 Addition of epsilon-aminocaproic acid (epsilon ACA)-plasmin complex to FITC-fibrinogen produced little dequenching, demonstrating a requirement for binding in order to initiate lysis. Aminocaproic Acid 12-37 fibrinogen beta chain Homo sapiens 76-86 2143650-5 1990 Addition of 0.1 mM-6-aminohexanoic acid shifted the non-linear curve obtained in the presence of fibrinogen to a straight line as for controls, indicating that 6-aminohexanoic acid abolishes the fibrinogen-induced inhibition. Aminocaproic Acid 18-39 fibrinogen beta chain Homo sapiens 97-107 2143650-5 1990 Addition of 0.1 mM-6-aminohexanoic acid shifted the non-linear curve obtained in the presence of fibrinogen to a straight line as for controls, indicating that 6-aminohexanoic acid abolishes the fibrinogen-induced inhibition. Aminocaproic Acid 18-39 fibrinogen beta chain Homo sapiens 195-205 2143650-5 1990 Addition of 0.1 mM-6-aminohexanoic acid shifted the non-linear curve obtained in the presence of fibrinogen to a straight line as for controls, indicating that 6-aminohexanoic acid abolishes the fibrinogen-induced inhibition. Aminocaproic Acid 19-39 fibrinogen beta chain Homo sapiens 97-107 2143650-5 1990 Addition of 0.1 mM-6-aminohexanoic acid shifted the non-linear curve obtained in the presence of fibrinogen to a straight line as for controls, indicating that 6-aminohexanoic acid abolishes the fibrinogen-induced inhibition. Aminocaproic Acid 19-39 fibrinogen beta chain Homo sapiens 195-205 3127307-1 1988 The activation of Glu1-plasminogen (Glu-Pg) by streptokinase (SK), urokinase (UK) and tissue plasminogen activator (tPA) is under rigorous control by molecules such as epsilon-aminocaproic acid (EACA), fibrinogen (Fg), fibrin (Fn) and, as we have recently discovered, anions. Aminocaproic Acid 168-193 fibrinogen beta chain Homo sapiens 202-212 3127307-1 1988 The activation of Glu1-plasminogen (Glu-Pg) by streptokinase (SK), urokinase (UK) and tissue plasminogen activator (tPA) is under rigorous control by molecules such as epsilon-aminocaproic acid (EACA), fibrinogen (Fg), fibrin (Fn) and, as we have recently discovered, anions. Aminocaproic Acid 168-193 fibrinogen beta chain Homo sapiens 214-216 3427134-4 1987 After partial hydrolysis of fibrinogen by plasmin, the amount of adsorbed plasminogen increases and the type of binding changes; part of the proenzyme molecules bind in the presence of 0.003 M 6-aminohexanoic acid, i.e., when lysine-binding sites appear to be blocked. Aminocaproic Acid 193-213 fibrinogen beta chain Homo sapiens 28-38 7843797-6 1994 Lysine as well as the lysine analog 6-aminohexanoic acid (AHA) decreased the inhibitory capacity of fibrinogen. Aminocaproic Acid 36-56 fibrinogen beta chain Homo sapiens 100-110 7843797-6 1994 Lysine as well as the lysine analog 6-aminohexanoic acid (AHA) decreased the inhibitory capacity of fibrinogen. Aminocaproic Acid 58-61 fibrinogen beta chain Homo sapiens 100-110 1716481-1 1991 In the present study, we systematically investigated aprotinin, epsilon-aminocaproic acid (EACA) and tranexamic acid as inhibitors of fibrinogen breakdown and of the generation of fibrinogen degradation products (FgDP). Aminocaproic Acid 64-89 fibrinogen beta chain Homo sapiens 134-144 1716481-1 1991 In the present study, we systematically investigated aprotinin, epsilon-aminocaproic acid (EACA) and tranexamic acid as inhibitors of fibrinogen breakdown and of the generation of fibrinogen degradation products (FgDP). Aminocaproic Acid 91-95 fibrinogen beta chain Homo sapiens 134-144 2174048-8 1990 Lysine and epsilon-aminocaproic acid could inhibit the binding of plasminogens and plasminogen derivatives with fibrin and block the enhancement effect of fibrinogen degradation products on plasminogen activation. Aminocaproic Acid 11-36 fibrinogen beta chain Homo sapiens 155-165 3177369-4 1988 Treatment with epsilon-aminocaproic acid to inhibit fibrinolysis and cryoprecipitate to replenish his deficient circulating fibrinogen interrupted the cycle of his systemic coagulopathy and enabled us to transfuse him to a normal hematocrit. Aminocaproic Acid 15-40 fibrinogen beta chain Homo sapiens 124-134