PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2483429-4 1989 It is a nonsulfhydryl ACE inhibitor, and after oral absorption it is transformed in the liver into its active metabolite ramiprilat, which is at least 23 times more lipophilic than enalaprilat. ramiprilat 121-131 angiotensin I converting enzyme Homo sapiens 22-25 2474098-1 1989 Evidence for effects of angiotensin converting enzyme (ACE) on isolated human glomeruli was provided using specific binding of tritium-labeled ramiprilat, a potent inhibitor of ACE. ramiprilat 143-153 angiotensin I converting enzyme Homo sapiens 24-53 2474098-1 1989 Evidence for effects of angiotensin converting enzyme (ACE) on isolated human glomeruli was provided using specific binding of tritium-labeled ramiprilat, a potent inhibitor of ACE. ramiprilat 143-153 angiotensin I converting enzyme Homo sapiens 55-58 2474098-1 1989 Evidence for effects of angiotensin converting enzyme (ACE) on isolated human glomeruli was provided using specific binding of tritium-labeled ramiprilat, a potent inhibitor of ACE. ramiprilat 143-153 angiotensin I converting enzyme Homo sapiens 177-180 2474102-4 1989 The maximal plasma level of ramipril was 57.0 +/- 26.8 ng/ml after 1.4 h; t1/2 was 2.4 +/- 1.2 h. The peak level of ramiprilat was 27.9 +/- 24 ng/ml after 4.6 h; t1/2 for the active compound was 6 +/- 4.2 h. The total recovery of ramipril and metabolites in urine was on average 39 +/- 17.5% within 96 h. Ninety-five percent inhibition of ACE activity was observed in all patients and 80% inhibition lasted 24 h. Systolic and diastolic blood pressure decreased without changes in heart rate. ramiprilat 116-126 angiotensin I converting enzyme Homo sapiens 339-342 2474105-9 1989 A strong correlation between the plasma ramiprilat levels and the inhibition of plasma ACE activity was noted for all groups. ramiprilat 40-50 angiotensin I converting enzyme Homo sapiens 87-90 2849453-1 1988 Evidence for angiotensin-converting enzyme (ACE) on isolated human glomeruli was furnished by specific binding of tritium-labeled ramiprilat, a potent inhibitor of ACE. ramiprilat 130-140 angiotensin I converting enzyme Homo sapiens 13-42 2849453-1 1988 Evidence for angiotensin-converting enzyme (ACE) on isolated human glomeruli was furnished by specific binding of tritium-labeled ramiprilat, a potent inhibitor of ACE. ramiprilat 130-140 angiotensin I converting enzyme Homo sapiens 44-47 2849453-1 1988 Evidence for angiotensin-converting enzyme (ACE) on isolated human glomeruli was furnished by specific binding of tritium-labeled ramiprilat, a potent inhibitor of ACE. ramiprilat 130-140 angiotensin I converting enzyme Homo sapiens 164-167 3034032-8 1987 A correlation was found between the log of plasma concentrations of ramipril diacid metabolite and the drug-induced plasma ACE activity inhibition and increase in brachial artery blood flow. ramiprilat 68-83 angiotensin I converting enzyme Homo sapiens 123-126 2831105-6 1988 We determined the brush border ACE value of IC50 = 3 X 10(-9) M Ramipril-diacid, which is the same value for serum and lung ACE. ramiprilat 64-79 angiotensin I converting enzyme Homo sapiens 31-34 2831105-6 1988 We determined the brush border ACE value of IC50 = 3 X 10(-9) M Ramipril-diacid, which is the same value for serum and lung ACE. ramiprilat 64-79 angiotensin I converting enzyme Homo sapiens 124-127 21535409-14 2011 Increased functional MMP activity, notably MMP-3 and -9, is present in Crohn"s fistulas and may be inhibited by ramiprilate, a widely available ACE inhibitor. ramiprilat 112-123 angiotensin I converting enzyme Homo sapiens 144-147 2485060-0 1987 Kinetic properties of the angiotensin converting enzyme inhibitor ramiprilat. ramiprilat 66-76 angiotensin I converting enzyme Homo sapiens 26-55 2485060-1 1987 The interaction of angiotensin converting enzyme (ACE) with ramiprilat was studied at pH 7.5 in the presence of 300 mmol/l sodium chloride with furanacryloyl-Phe-Gly-Gly as substrate. ramiprilat 60-70 angiotensin I converting enzyme Homo sapiens 19-48 2485060-1 1987 The interaction of angiotensin converting enzyme (ACE) with ramiprilat was studied at pH 7.5 in the presence of 300 mmol/l sodium chloride with furanacryloyl-Phe-Gly-Gly as substrate. ramiprilat 60-70 angiotensin I converting enzyme Homo sapiens 50-53 2485060-2 1987 Ramiprilat inhibits ACE with a Ki value of 7 pmol/l. ramiprilat 0-10 angiotensin I converting enzyme Homo sapiens 20-23 2485060-4 1987 Binding of ramiprilat to ACE proceeds by a two-step mechanism E + I in equilibrium EI in equilibrium EI* in which the inhibitor rapidly binds to enzyme to form an initial enzyme-inhibitor complex, which then undergoes a slow isomerization. ramiprilat 11-21 angiotensin I converting enzyme Homo sapiens 25-28 2485060-5 1987 The interaction of ramiprilat with ACE is compared to that of two other potent inhibitors, captopril and enalaprilat. ramiprilat 19-29 angiotensin I converting enzyme Homo sapiens 35-38 23087017-10 2013 ACE inhibition with ramiprilat, ET-1 receptor inhibition with bosentan, and treatment with the vasodilator bradykinin prevented flow-induced, EC-dependent SMC changes. ramiprilat 20-30 angiotensin I converting enzyme Homo sapiens 0-3 16398929-0 2006 Human physiologically based pharmacokinetic model for ACE inhibitors: ramipril and ramiprilat. ramiprilat 83-93 angiotensin I converting enzyme Homo sapiens 54-57 18399693-1 2008 Studies that allow computing values of aqueous proton dissociation constants (pKa), gas phase proton affinities, and the free energy of solvation have been performed for six members of angiotensin-I-converting enzyme (ACE) inhibitor family (captopril, enalaprilat, imidaprilat, ramiprilat, perindoprilat, and spiraprilat). ramiprilat 278-288 angiotensin I converting enzyme Homo sapiens 218-221 12361743-1 2002 A fast and robust liquid chromatography-mass spectrometry (LC-MS-MS) method has been developed for simultaneous quantitation of the angiotensin-converting enzyme (ACE) inhibitor, ramipril and its metabolite ramiprilat in human plasma. ramiprilat 207-217 angiotensin I converting enzyme Homo sapiens 132-161 16220025-8 2006 The DHP Ca2+-channel agonist BayK8644 and ACE inhibitors captopril and ramiprilat led extracellular superoxide concentration to control level. ramiprilat 71-81 angiotensin I converting enzyme Homo sapiens 42-45 16220025-12 2006 Suppression of substance P-evoked NO release by Ang II (>70%, n = 6) was reversed by the PKC inhibitor chelerythrine, the DHP amlodipine and nisoldipine and the ACE inhibitor ramiprilat. ramiprilat 178-188 angiotensin I converting enzyme Homo sapiens 164-167 16088213-8 2005 Diminished AT 1 expression and adhesion molecule expression in response to ramiprilat treatment were partially reversed after incubation with a bradykinin 2 receptor antagonist, suggesting that elevated bradykinin levels under ACE inhibition may be involved in the beneficial effect of ACE inhibitors. ramiprilat 75-85 angiotensin I converting enzyme Homo sapiens 227-230 16088213-8 2005 Diminished AT 1 expression and adhesion molecule expression in response to ramiprilat treatment were partially reversed after incubation with a bradykinin 2 receptor antagonist, suggesting that elevated bradykinin levels under ACE inhibition may be involved in the beneficial effect of ACE inhibitors. ramiprilat 75-85 angiotensin I converting enzyme Homo sapiens 286-289 16088213-9 2005 Thus, modulation of the local AngII system by ramiprilat may at least in part contribute to the benefits of ACE inhibition in the treatment of atherosclerotic diseases. ramiprilat 46-56 angiotensin I converting enzyme Homo sapiens 108-111 15569856-6 2005 In an endothelial cell line stably expressing human somatic ACE, ramiprilat increased COX-2 promoter activity, an effect not observed in ACE-deficient cells or cells expressing a nonphosphorylatable ACE mutant (S1270A). ramiprilat 65-75 angiotensin I converting enzyme Homo sapiens 60-63 15569856-7 2005 The ramiprilat-induced, ACE-dependent increase in COX-2 expression and promoter activity (both 1.5- to 2-fold greater than control) was prevented by the inhibition of JNK. ramiprilat 4-14 angiotensin I converting enzyme Homo sapiens 24-27 15569856-8 2005 Ramiprilat significantly enhanced the DNA binding activity of activator protein-1 in cells expressing ACE but not S1270A ACE. ramiprilat 0-10 angiotensin I converting enzyme Homo sapiens 102-105 15530425-3 2004 Therefore, our study concentrates on the effect of the ACE-inhibitor ramiprilat on chemokine release, AngII receptor (ATR) expression, and NF-kappaB activity in monocytes stimulated with AngII. ramiprilat 69-79 angiotensin I converting enzyme Homo sapiens 55-58 14615289-3 2004 The ACE inhibitors ramiprilat and perindoprilat, and the substrate bradykinin (but not angiotensin I), enhanced the activity of ACE-associated CK2 and the phosphorylation of ACE Ser1270 in cultured endothelial cells. ramiprilat 19-29 angiotensin I converting enzyme Homo sapiens 4-7 14615289-3 2004 The ACE inhibitors ramiprilat and perindoprilat, and the substrate bradykinin (but not angiotensin I), enhanced the activity of ACE-associated CK2 and the phosphorylation of ACE Ser1270 in cultured endothelial cells. ramiprilat 19-29 angiotensin I converting enzyme Homo sapiens 128-131 14615289-3 2004 The ACE inhibitors ramiprilat and perindoprilat, and the substrate bradykinin (but not angiotensin I), enhanced the activity of ACE-associated CK2 and the phosphorylation of ACE Ser1270 in cultured endothelial cells. ramiprilat 19-29 angiotensin I converting enzyme Homo sapiens 128-131 14615289-7 2004 Prolonged ramiprilat treatment increased ACE expression in primary cultures of human endothelial cells and in vivo (mouse lung), a response that was prevented by pretreatment with the JNK inhibitor SP600125. ramiprilat 10-20 angiotensin I converting enzyme Homo sapiens 41-44 15601445-1 2004 The pharmacokinetic (PK) properties and the pharmacokinetic/pharmacodynamic (PK/PD) relationships for the angiotensin-converting enzyme (ACE) inhibitors (ACEIs), such as enalaprilat, benazeprilat, imidaprilat and ramiprilat, differ from those of conventional drugs. ramiprilat 213-223 angiotensin I converting enzyme Homo sapiens 106-135 15601445-1 2004 The pharmacokinetic (PK) properties and the pharmacokinetic/pharmacodynamic (PK/PD) relationships for the angiotensin-converting enzyme (ACE) inhibitors (ACEIs), such as enalaprilat, benazeprilat, imidaprilat and ramiprilat, differ from those of conventional drugs. ramiprilat 213-223 angiotensin I converting enzyme Homo sapiens 137-140 14727938-2 2003 ), an angiotensin-converting enzyme (ACE) inhibitor, is a prodrug which is rapidly hydrolyzed after absorption to the active metabolite ramiprilat. ramiprilat 136-146 angiotensin I converting enzyme Homo sapiens 6-35 14727938-2 2003 ), an angiotensin-converting enzyme (ACE) inhibitor, is a prodrug which is rapidly hydrolyzed after absorption to the active metabolite ramiprilat. ramiprilat 136-146 angiotensin I converting enzyme Homo sapiens 37-40 12381651-7 2002 The ACE inhibitors captopril and ramiprilate inhibited MMP-2 and MMP-9 activity in vitro (inhibitory capacity (IC50), in mmol/l: MMP-2: captopril 2.0 (0.16), ramiprilate 2.1 (0.3); MMP-9: captopril 1.65 (0.18), ramiprilate 2.0 (0.3)). ramiprilat 158-169 angiotensin I converting enzyme Homo sapiens 4-7 12381651-7 2002 The ACE inhibitors captopril and ramiprilate inhibited MMP-2 and MMP-9 activity in vitro (inhibitory capacity (IC50), in mmol/l: MMP-2: captopril 2.0 (0.16), ramiprilate 2.1 (0.3); MMP-9: captopril 1.65 (0.18), ramiprilate 2.0 (0.3)). ramiprilat 33-44 angiotensin I converting enzyme Homo sapiens 4-7 12381651-7 2002 The ACE inhibitors captopril and ramiprilate inhibited MMP-2 and MMP-9 activity in vitro (inhibitory capacity (IC50), in mmol/l: MMP-2: captopril 2.0 (0.16), ramiprilate 2.1 (0.3); MMP-9: captopril 1.65 (0.18), ramiprilate 2.0 (0.3)). ramiprilat 158-169 angiotensin I converting enzyme Homo sapiens 4-7 12076194-1 2002 UNLABELLED: Ramipril, an angiotensin-converting enzyme (ACE) inhibitor, is a prodrug which is rapidly hydrolysed after absorption to the active metabolite ramiprilat. ramiprilat 155-165 angiotensin I converting enzyme Homo sapiens 25-54 12076194-1 2002 UNLABELLED: Ramipril, an angiotensin-converting enzyme (ACE) inhibitor, is a prodrug which is rapidly hydrolysed after absorption to the active metabolite ramiprilat. ramiprilat 155-165 angiotensin I converting enzyme Homo sapiens 56-59 10209009-10 1999 CONCLUSIONS: The ACE inhibitor ramiprilat interferes with the targeting of the B2 kinin receptor to CR membrane domains in native endothelial cells. ramiprilat 31-41 angiotensin I converting enzyme Homo sapiens 17-20 10209009-0 1999 Angiotensin-converting enzyme inhibitor ramiprilat interferes with the sequestration of the B2 kinin receptor within the plasma membrane of native endothelial cells. ramiprilat 40-50 angiotensin I converting enzyme Homo sapiens 0-29 8963479-0 1995 Tight binding of ramiprilat to ACE: consequences for pharmacokinetic and pharmacodynamic measurements. ramiprilat 17-27 angiotensin I converting enzyme Homo sapiens 31-34 8963479-3 1995 The present paper discusses how tight binding of ramiprilat to ACE affects the pharmacokinetic characteristics and in vitro measurement of ACE inhibition. ramiprilat 49-59 angiotensin I converting enzyme Homo sapiens 63-66 8963479-3 1995 The present paper discusses how tight binding of ramiprilat to ACE affects the pharmacokinetic characteristics and in vitro measurement of ACE inhibition. ramiprilat 49-59 angiotensin I converting enzyme Homo sapiens 139-142 8963479-7 1995 With respect to pharmacodynamics, free ramiprilat depletion due to tight binding is the reason for the steep nature of concentration-effect curves often observed for ACE inhibition. ramiprilat 39-49 angiotensin I converting enzyme Homo sapiens 166-169 7515323-0 1994 Enhancement of cytosolic calcium, prostacyclin and nitric oxide by bradykinin and the ACE inhibitor ramiprilat in porcine brain capillary endothelial cells. ramiprilat 100-110 angiotensin I converting enzyme Homo sapiens 86-89 7768254-1 1995 The pharmacokinetics and pharmacodynamics of the prodrug ramipril and its active ACE-inhibiting metabolite ramiprilat were investigated in an open, randomised, three-way cross-over study in 12 healthy male volunteers. ramiprilat 107-117 angiotensin I converting enzyme Homo sapiens 81-84 7515323-4 1994 Bradykinin and the ACE inhibitor ramiprilat concentration-dependently increased the formation of cyclic GMP which was completely prevented by the stereospecific inhibitor of NO synthase, NG-nitro-L-arginine. ramiprilat 33-43 angiotensin I converting enzyme Homo sapiens 19-22 1663586-2 1991 The ACE inhibitors ramiprilat and enalaprilat (0.3 microM) enhanced the increase in [Ca2+]i elicited by bradykinin (3 nM) and also caused an increase in resting [Ca2+]i when given alone. ramiprilat 19-29 angiotensin I converting enzyme Homo sapiens 4-7 1335341-3 1992 In this work we identified ACE binding sites in human left ventricle and lung by radioligand binding using the ACE inhibitor [3H]-ramiprilat in all tissues tested was saturable, temperature and zinc-dependent, and inhibited by EDTA. ramiprilat 130-140 angiotensin I converting enzyme Homo sapiens 27-30 1335341-3 1992 In this work we identified ACE binding sites in human left ventricle and lung by radioligand binding using the ACE inhibitor [3H]-ramiprilat in all tissues tested was saturable, temperature and zinc-dependent, and inhibited by EDTA. ramiprilat 130-140 angiotensin I converting enzyme Homo sapiens 111-114 8137599-6 1994 Ramiprilat binds to ACE with high affinity at concentrations similar to that of the enzyme and establishes equilibrium slowly. ramiprilat 0-10 angiotensin I converting enzyme Homo sapiens 20-23 8388656-3 1993 Most of the bradykinin-degrading activity in cell monolayers could be inhibited in a concentration-dependent manner by the ACE inhibitors lisinopril, ramiprilat, and captopril. ramiprilat 150-160 angiotensin I converting enzyme Homo sapiens 123-126 8276048-2 1993 The aim of the present study was primarily to evaluate the haemodynamic effects of the ACE-inhibitor ramipril which is active via its metabolite ramiprilat. ramiprilat 145-155 angiotensin I converting enzyme Homo sapiens 87-90 8276048-9 1993 Complete inhibition of ACE-activity was seen at a mean plasma concentration of ramiprilat of 4.7 ng.ml-1. ramiprilat 79-89 angiotensin I converting enzyme Homo sapiens 23-26 2147879-1 1990 After oral administration, ramipril, a nonsulfhydryl angiotensin-converting enzyme (ACE) inhibitor, is transformed in the liver into its active metabolite ramiprilat. ramiprilat 155-165 angiotensin I converting enzyme Homo sapiens 53-82 1650862-4 1991 While ramiprilat itself induced an increase of basal [Ca2+]i, the Ca(2+)-mobilizing effect of angiotensin II (AII) was blunted in the presence of the ACE inhibitor (659 +/- 38 nM vs 360 +/- 45 nM, p less than .001). ramiprilat 6-16 angiotensin I converting enzyme Homo sapiens 150-153 1646621-9 1991 Plasma ACE inhibition by ramiprilat was unaffected by concurrent felodipine. ramiprilat 25-35 angiotensin I converting enzyme Homo sapiens 7-10 2147879-1 1990 After oral administration, ramipril, a nonsulfhydryl angiotensin-converting enzyme (ACE) inhibitor, is transformed in the liver into its active metabolite ramiprilat. ramiprilat 155-165 angiotensin I converting enzyme Homo sapiens 84-87