PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
7856280-4	1994	ACE inhibition with ramiprilat increases kinin concentrations during normoxia, ischemia and reperfusion, whereas deendothelialization markedly reduces kinin and prostacyclin outflow in controls as well as in ACE inhibitor-treated hearts.	ramiprilat	20-30	angiotensin I converting enzyme	Rattus norvegicus	0-3
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
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
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	5'-nucleotidase, cytosolic II	Homo sapiens	104-107
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
8293768-1	1993	The angiotensin converting enzyme (ACE) inhibitors, moexiprilat and ramiprilat, relaxed preconstricted endothelium-intact bovine coronary artery rings and enhanced the relaxant response to bradykinin.	ramiprilat	68-78	angiotensin I converting enzyme	Bos taurus	4-33
8293768-1	1993	The angiotensin converting enzyme (ACE) inhibitors, moexiprilat and ramiprilat, relaxed preconstricted endothelium-intact bovine coronary artery rings and enhanced the relaxant response to bradykinin.	ramiprilat	68-78	angiotensin I converting enzyme	Bos taurus	35-38
8293768-1	1993	The angiotensin converting enzyme (ACE) inhibitors, moexiprilat and ramiprilat, relaxed preconstricted endothelium-intact bovine coronary artery rings and enhanced the relaxant response to bradykinin.	ramiprilat	68-78	kininogen 1	Bos taurus	189-199
8399986-1	1993	In the presence of indomethacin (10 microM) and without previous exposure to bradykinin, two angiotensin-converting enzyme (ACE) inhibitors, moexiprilat and ramiprilat (0.1 microM), elicited distinct relaxation responses from preconstricted endothelium-intact but not from denuded bovine coronary artery rings, and enhanced the relaxation response to bradykinin (3 nM).	ramiprilat	157-167	angiotensin I converting enzyme	Bos taurus	93-122
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	kininogen 1	Homo sapiens	12-22
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
8388656-6	1993	The functional consequence of bradykinin degradation was demonstrated by the potentiating effect of ramiprilat on the generation of endothelium-derived relaxing factors nitric oxide and prostacyclin from endothelial cells.	ramiprilat	100-110	kininogen 1	Homo sapiens	30-40
8448580-2	1993	In addition, we examined the effect on bradykinin outflow of the angiotensin converting enzyme (ACE) inhibitor, ramiprilat.	ramiprilat	112-122	angiotensin I converting enzyme	Rattus norvegicus	65-94
8448580-2	1993	In addition, we examined the effect on bradykinin outflow of the angiotensin converting enzyme (ACE) inhibitor, ramiprilat.	ramiprilat	112-122	angiotensin I converting enzyme	Rattus norvegicus	96-99
1280723-4	1992	The angiotensin converting enzyme (ACE) inhibitor ramiprilat (0.3 microM) selectively enhanced both the 6-keto-PGF1 alpha outflow and the dilator response to Bk.	ramiprilat	50-60	angiotensin-converting enzyme	Oryctolagus cuniculus	4-33
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
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
1335341-6	1992	[3H]-ramiprilat binding to rat (n = 4) and human lung (n = 4) showed a binding site density of 2132 +/- 155 and 1085 +/- 51 fmol mg-1 protein respectively with an affinity of 639 +/- 54 and 325 +/- 22 pM.	ramiprilat	5-15	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	129-133
7508049-2	1993	Incubation of cultured human endothelial cells with moexiprilat or ramiprilat (0.3 microM) caused a maintained increase in resting intracellular calcium [Ca2+]i, which was prevented by the selective B2-receptor antagonist Hoe 140 (0.1 microM).	ramiprilat	67-77	bradykinin receptor B2	Homo sapiens	199-210
1280723-4	1992	The angiotensin converting enzyme (ACE) inhibitor ramiprilat (0.3 microM) selectively enhanced both the 6-keto-PGF1 alpha outflow and the dilator response to Bk.	ramiprilat	50-60	angiotensin-converting enzyme	Oryctolagus cuniculus	35-38
1281378-2	1992	Enalaprilat, moexiprilat and ramiprilat similarly potentiated the increase in [Ca2+]i elicited by bradykinin and caused an increase in resting [Ca2+]i when given alone.	ramiprilat	29-39	kininogen 1	Homo sapiens	98-108
1312513-4	1992	The most potent converting enzyme inhibitors toward aminopeptidase P were the carboxylalkyl compounds, cilazaprilat, enalaprilat, and ramiprilat (I50 values of 3-12 microM).	ramiprilat	134-144	X-prolyl aminopeptidase 2	Sus scrofa	52-68
1282631-4	1992	Ramiprilat also significantly enhanced the increase in intracellular Ca2+ elicited by bradykinin (3 nM).	ramiprilat	0-10	kininogen 1	Bos taurus	86-96
1334350-1	1992	Like bradykinin the converting enzyme inhibitor ramiprilat concentration-dependently enhances the formation of nitric oxide and prostacyclin assessed by intracellular cyclic GMP accumulation and 6-keto prostaglandin F1.	ramiprilat	48-58	kininogen 1	Bos taurus	5-15
1462857-1	1992	In the isolated rabbit thoracic aorta the ACE inhibitor ramiprilat attenuated bradykinin degradation by enzymes localized on vascular endothelial cells as well as on vascular smooth muscle cells by 26% and 32%, respectively.	ramiprilat	56-66	angiotensin-converting enzyme	Oryctolagus cuniculus	42-45
1462888-1	1992	The ACE-inhibitor ramiprilat (40 ng/kg/min) was infused for 6 h into the left coronary artery of anesthetized dogs with ligation of the descending branch of this artery.	ramiprilat	18-28	angiotensin I converting enzyme	Canis lupus familiaris	4-7
1462888-4	1992	The cardioprotective effect of ramiprilat was mimicked by bradykinin and abolished by coadministration of a bradykinin antagonist.	ramiprilat	31-41	kininogen 1	Canis lupus familiaris	58-68
1462888-4	1992	The cardioprotective effect of ramiprilat was mimicked by bradykinin and abolished by coadministration of a bradykinin antagonist.	ramiprilat	31-41	kininogen 1	Canis lupus familiaris	108-118
1462888-5	1992	These results strongly suggest that bradykinin plays a role in the cardioprotective effect of the ACE-inhibitor ramiprilat.	ramiprilat	112-122	kininogen 1	Canis lupus familiaris	36-46
1462888-5	1992	These results strongly suggest that bradykinin plays a role in the cardioprotective effect of the ACE-inhibitor ramiprilat.	ramiprilat	112-122	angiotensin I converting enzyme	Canis lupus familiaris	98-101
1282631-7	1992	In the isolated perfused rabbit heart, ramiprilat (0.3 microM) affected neither resting vascular tone nor endothelial autacoid release; however, the vasodilation and release of PGI2 in response to exogenously applied bradykinin (10 nM) were significantly enhanced by ramiprilat.	ramiprilat	39-49	kininogen 1	Bos taurus	217-227
1282631-7	1992	In the isolated perfused rabbit heart, ramiprilat (0.3 microM) affected neither resting vascular tone nor endothelial autacoid release; however, the vasodilation and release of PGI2 in response to exogenously applied bradykinin (10 nM) were significantly enhanced by ramiprilat.	ramiprilat	267-277	kininogen 1	Bos taurus	217-227
1649762-3	1991	[3H]Ramiprilat binding was completely inhibited by specific inhibitors of ACE: ramiprilat, ramipril, enalaprilat, enalapril and captopril.	ramiprilat	79-89	angiotensin I converting enzyme	Rattus norvegicus	74-77
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
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	kininogen 1	Homo sapiens	104-114
1655653-0	1991	Ramiprilat enhances endothelial autacoid formation by inhibiting breakdown of endothelium-derived bradykinin.	ramiprilat	0-10	kininogen 1	Homo sapiens	98-108
1655653-5	1991	The ramiprilat-induced cyclic GMP increase was completely abolished by the stereospecific inhibitor of nitric oxide synthase, NG-nitro-L-arginine.	ramiprilat	4-14	5'-nucleotidase, cytosolic II	Homo sapiens	30-33
1646621-9	1991	Plasma ACE inhibition by ramiprilat was unaffected by concurrent felodipine.	ramiprilat	25-35	angiotensin I converting enzyme	Homo sapiens	7-10
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	angiotensinogen	Homo sapiens	94-108
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
1650862-9	1991	Ramiprilat-induced contraction of cultured smooth muscle cells may not be relevant in vivo, but the increase of basal [Ca2+]i by ramiprilat may reflect a "reset" of the cellular Ca(2+)-mobilizing mechanism or a depletion of cellular Ca2+ stores and may thus explain the attenuation of the Ca(2+)-mobilizing effect of AII.	ramiprilat	129-139	angiotensinogen	Homo sapiens	317-320
1865630-6	1991	Combined perfusions with threshold concentrations of bradykinin (1 x 10(-12) M) and the ACE inhibitor ramiprilat (2,58 x 10(-9) M), which were ineffective given alone, resulted in a marked cardioprotective effect.	ramiprilat	102-112	angiotensin I converting enzyme	Rattus norvegicus	88-91
1650863-7	1991	It seems possible that ACE (kininase II) inhibitors exert cardioprotection via elevated tissue levels of kinins: bradykinin also improved heart performance after low flow perfusion and bradykinin-induced coronary dilatation was markedly enhanced in the presence of ramiprilate, reflecting attenuated degradation by endothelial kininase II.	ramiprilat	265-276	LOW QUALITY PROTEIN: angiotensin-converting enzyme	Cavia porcellus	23-26
2698963-11	1989	Ramiprilat, a non-SH-containing ACE inhibitor, inhibits free radical-induced damages mainly by stimulation of prostacyclin synthesis and/or release.	ramiprilat	0-10	angiotensin I converting enzyme	Rattus norvegicus	32-35
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
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
1697370-6	1990	Combined perfusions with threshold concentrations of BK (1 X 10(-12) M) and the ACE inhibitor ramiprilat (2.58 X 10(-9) M), which were ineffective given alone, resulted in a marked cardioprotective effect.	ramiprilat	94-104	angiotensin I converting enzyme	Rattus norvegicus	80-83
2483425-6	1989	Comparing ACE activity, measured by fluorimetry, with the amount of [3H]ramiprilat bound shows that the two techniques yield similar results.	ramiprilat	72-82	angiotensin I converting enzyme	Rattus norvegicus	10-13
2792189-8	1989	Likewise, in the presence of angiotensin II (0.1 microM) the effect of ramiprilat was no longer evident.	ramiprilat	71-81	angiotensinogen	Rattus norvegicus	29-43
2792189-10	1989	It is concluded that ramiprilat, at therapeutically relevant concentrations, attenuates the ischemia-induced mobilization of NA via a reduction in local angiotensin II production and/or bradykinin degradation.	ramiprilat	21-31	angiotensinogen	Rattus norvegicus	153-167
2483427-3	1989	ACE activity in pig pulmonary artery endothelial cells is completely inhibited by 100 nM ramiprilat; the IC50 is 2 nM, whatever the form of ACE: soluble ACE released into the culture medium, cellular ACE studied in a cell monolayer homogenate, or tissue ACE purified from pig lung tissue.	ramiprilat	89-99	angiotensin-converting enzyme	Sus scrofa	140-143
2483427-1	1989	Ramiprilat is an angiotensin I-converting enzyme (ACE) inhibitor whose particular lipophilicity may modify its inhibitory activity on the cellular form of this enzyme in comparison to ACE inhibitors that are more hydrophilic.	ramiprilat	0-10	angiotensin-converting enzyme	Sus scrofa	17-48
2483427-4	1989	When added directly to whole living cells in their culture medium, 100 nM ramiprilat inhibits less than 80% of ACE activity in the supernatant while this dose inhibits the cellular form of the enzyme completely, suggesting that ramiprilat reaches and more specifically inhibits membrane-bound ACE rather than ACE secreted by the monolayer of endothelial cells.	ramiprilat	74-84	angiotensin-converting enzyme	Sus scrofa	111-114
2483427-4	1989	When added directly to whole living cells in their culture medium, 100 nM ramiprilat inhibits less than 80% of ACE activity in the supernatant while this dose inhibits the cellular form of the enzyme completely, suggesting that ramiprilat reaches and more specifically inhibits membrane-bound ACE rather than ACE secreted by the monolayer of endothelial cells.	ramiprilat	74-84	angiotensin-converting enzyme	Sus scrofa	293-296
2483427-4	1989	When added directly to whole living cells in their culture medium, 100 nM ramiprilat inhibits less than 80% of ACE activity in the supernatant while this dose inhibits the cellular form of the enzyme completely, suggesting that ramiprilat reaches and more specifically inhibits membrane-bound ACE rather than ACE secreted by the monolayer of endothelial cells.	ramiprilat	74-84	angiotensin-converting enzyme	Sus scrofa	293-296
2483427-4	1989	When added directly to whole living cells in their culture medium, 100 nM ramiprilat inhibits less than 80% of ACE activity in the supernatant while this dose inhibits the cellular form of the enzyme completely, suggesting that ramiprilat reaches and more specifically inhibits membrane-bound ACE rather than ACE secreted by the monolayer of endothelial cells.	ramiprilat	228-238	angiotensin-converting enzyme	Sus scrofa	293-296
2483427-4	1989	When added directly to whole living cells in their culture medium, 100 nM ramiprilat inhibits less than 80% of ACE activity in the supernatant while this dose inhibits the cellular form of the enzyme completely, suggesting that ramiprilat reaches and more specifically inhibits membrane-bound ACE rather than ACE secreted by the monolayer of endothelial cells.	ramiprilat	228-238	angiotensin-converting enzyme	Sus scrofa	293-296
2483427-5	1989	[3H]ramiprilat binds specifically to the membrane of cultured endothelial cells, in a time and dose-dependent manner (Kd = 6 nM; Bmax = 1,600 fmol/mg of protein); specificity is confirmed by the fact that an anti-ACE antibody prevents binding of [3H]ramiprilat and that both cold ramiprilat as well as other synthetic inhibitor compounds (captopril and enalaprilat) displace [3H]ramiprilat in a dose-dependent manner.	ramiprilat	4-14	angiotensin-converting enzyme	Sus scrofa	213-216
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
2483427-1	1989	Ramiprilat is an angiotensin I-converting enzyme (ACE) inhibitor whose particular lipophilicity may modify its inhibitory activity on the cellular form of this enzyme in comparison to ACE inhibitors that are more hydrophilic.	ramiprilat	0-10	angiotensin-converting enzyme	Sus scrofa	50-53
2483427-2	1989	The inhibitory activity of ramiprilat on cellular ACE and its binding to plasma membrane ACE have been studied in cultures of pig vascular endothelial cells.	ramiprilat	27-37	angiotensin-converting enzyme	Sus scrofa	50-53
2483427-2	1989	The inhibitory activity of ramiprilat on cellular ACE and its binding to plasma membrane ACE have been studied in cultures of pig vascular endothelial cells.	ramiprilat	27-37	angiotensin-converting enzyme	Sus scrofa	89-92
2483427-3	1989	ACE activity in pig pulmonary artery endothelial cells is completely inhibited by 100 nM ramiprilat; the IC50 is 2 nM, whatever the form of ACE: soluble ACE released into the culture medium, cellular ACE studied in a cell monolayer homogenate, or tissue ACE purified from pig lung tissue.	ramiprilat	89-99	angiotensin-converting enzyme	Sus scrofa	0-3
2483427-3	1989	ACE activity in pig pulmonary artery endothelial cells is completely inhibited by 100 nM ramiprilat; the IC50 is 2 nM, whatever the form of ACE: soluble ACE released into the culture medium, cellular ACE studied in a cell monolayer homogenate, or tissue ACE purified from pig lung tissue.	ramiprilat	89-99	angiotensin-converting enzyme	Sus scrofa	140-143
2483427-3	1989	ACE activity in pig pulmonary artery endothelial cells is completely inhibited by 100 nM ramiprilat; the IC50 is 2 nM, whatever the form of ACE: soluble ACE released into the culture medium, cellular ACE studied in a cell monolayer homogenate, or tissue ACE purified from pig lung tissue.	ramiprilat	89-99	angiotensin-converting enzyme	Sus scrofa	140-143
2483427-3	1989	ACE activity in pig pulmonary artery endothelial cells is completely inhibited by 100 nM ramiprilat; the IC50 is 2 nM, whatever the form of ACE: soluble ACE released into the culture medium, cellular ACE studied in a cell monolayer homogenate, or tissue ACE purified from pig lung tissue.	ramiprilat	89-99	angiotensin-converting enzyme	Sus scrofa	140-143
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
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
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
33773093-9	2021	Increased exposure of ramipril and less pronounced exposure of ramiprilat were observed in the presence of amlodipine and atorvastatin, with Cmax ratios for ramipril and ramiprilat of 182.6% and 155.9%, and corresponding AUC0-tau ratios of 150.0% and 112.1%, respectively.	ramiprilat	63-73	microtubule associated protein tau	Homo sapiens	226-229
2953225-5	1987	Ramipril diacid given alone produced a small, nonsignificant increase in forearm flow, although the response was significantly related to basal plasma renin.	ramiprilat	0-15	renin	Homo sapiens	151-156
2485046-8	1987	Intravenous injection of ramiprilat (100 micrograms) significantly decreased NA-supported BP in SHRSP and WKY rats for more than 30 min, but did not lower BP in rats supported with ANG II or with NA plus a subpressor dose of ANG II.	ramiprilat	25-35	angiotensinogen	Rattus norvegicus	225-231
2438489-2	1986	Ramiprilat (10 mcg/min for 10 min) produced a 71% mean increase in FBF (n = 8; range, 26-130%; p less than 0.001) in vessels preconstricted with ANG I (64-128 pmol/min), with the effect maximal at the end of ramiprilat infusion and subsiding over 30 min.	ramiprilat	0-10	angiotensinogen	Homo sapiens	145-150
2438489-4	1986	Ramiprilat given alone produced only a small nonsignificant increase in FBF of 7 +/- 4% (n = 12; p = 0.29), though this increase did correlate significantly with plasma renin (r = 0.60; p = 0.04).	ramiprilat	0-10	renin	Homo sapiens	169-174
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
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
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
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
26639833-2	2016	This study was designed to establish PK profiles for ramipril and ramiprilat as well as to determine the effects of ramiprilat on serum angiotensin converting enzyme (ACE) and to select the most appropriate ramipril dose that suppresses ACE activity.	ramiprilat	116-126	angiotensin I converting enzyme	Equus caballus	167-170
26639833-2	2016	This study was designed to establish PK profiles for ramipril and ramiprilat as well as to determine the effects of ramiprilat on serum angiotensin converting enzyme (ACE) and to select the most appropriate ramipril dose that suppresses ACE activity.	ramiprilat	116-126	angiotensin I converting enzyme	Equus caballus	136-165
26639833-9	2016	Although oral availability of ramiprilat was low, ramipril has sufficient enteral absorption and bioconversion to ramiprilat to induce serum ACE inhibitions of almost 85% after a dose of 0.80 mg/kg ramipril.	ramiprilat	114-124	angiotensin I converting enzyme	Equus caballus	141-144
23372044-0	2014	Expressional profile of cardiac uncoupling protein-2 following myocardial ischemia reperfusion in losartan- and ramiprilat-treated rats.	ramiprilat	112-122	uncoupling protein 2	Rattus norvegicus	32-52
23372044-1	2014	BACKGROUND AND AIMS: The aim of this study was to investigate the early changes of cardiac uncoupling protein-2 (UCP2) expression following myocardial ischemia reperfusion in rats chronically treated with ramiprilat and losartan.	ramiprilat	205-215	uncoupling protein 2	Rattus norvegicus	91-111
23372044-1	2014	BACKGROUND AND AIMS: The aim of this study was to investigate the early changes of cardiac uncoupling protein-2 (UCP2) expression following myocardial ischemia reperfusion in rats chronically treated with ramiprilat and losartan.	ramiprilat	205-215	uncoupling protein 2	Rattus norvegicus	113-117
23372044-7	2014	IR-induced overexpression of UCP2 was suppressed by ramiprilat and losartan.	ramiprilat	52-62	uncoupling protein 2	Rattus norvegicus	29-33
23372044-8	2014	CONCLUSION: These findings suggest that losartan and ramiprilat can suppress UCP2 expression following myocardial IR, and by this mechanism may protect the myocardium against IR injury.	ramiprilat	53-63	uncoupling protein 2	Rattus norvegicus	77-81
25143788-11	2014	Ramiprilat or BAY11-7082 inhibited the AGE-induced MMP-2 activation or reactive oxygen species generation in RPTCs.	ramiprilat	0-10	matrix metallopeptidase 2	Rattus norvegicus	51-56
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
17716647-5	2007	The bradykinin/angiotensin I selectivity ratios calculated from double displacement experiments were: perindoprilat, 1.44; ramiprilat, 1.16; quinaprilat, 1.09; trandolaprilat, 1.08; enalaprilat, 1.00.	ramiprilat	123-133	kininogen 1	Homo sapiens	4-14
21535409-11	2011	Ramiprilate significantly decreased the average total MMP activity level by 42% and suppressed the specific MMP-3 activity by 72%, which is comparable to the effect of GM6001 (87%).	ramiprilat	0-11	matrix metallopeptidase 3	Homo sapiens	108-113
21535409-12	2011	Moreover, MMP-9 activity was completely blunted by ramiprilate.	ramiprilat	51-62	matrix metallopeptidase 9	Homo sapiens	10-15
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	matrix metallopeptidase 3	Homo sapiens	43-55
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
20924096-4	2010	Intravenous injection of the active compounds of the 2 ACE inhibitors, zofenoprilat (288 nmol/kg) and ramiprilat (129 nmol/kg), caused similar hypotensive effects in anesthetized rabbits.	ramiprilat	102-112	angiotensin-converting enzyme	Oryctolagus cuniculus	55-58
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
17716647-5	2007	The bradykinin/angiotensin I selectivity ratios calculated from double displacement experiments were: perindoprilat, 1.44; ramiprilat, 1.16; quinaprilat, 1.09; trandolaprilat, 1.08; enalaprilat, 1.00.	ramiprilat	123-133	angiotensinogen	Homo sapiens	15-28
17825088-0	2007	Direct effects of the angiotensin-converting enzyme inhibitor ramiprilat on adult rat ventricular cardiomyocytes.	ramiprilat	62-72	angiotensin I converting enzyme	Rattus norvegicus	22-51
17825088-1	2007	AIM: Angiotensin-converting enzyme (ACE) inhibitors like ramiprilat bind to ACE expressed on the cell surface of endothelial cells and induce cell-specific signalling including the activation of activator protein (AP)-1.	ramiprilat	57-67	angiotensin I converting enzyme	Rattus norvegicus	5-34
17825088-1	2007	AIM: Angiotensin-converting enzyme (ACE) inhibitors like ramiprilat bind to ACE expressed on the cell surface of endothelial cells and induce cell-specific signalling including the activation of activator protein (AP)-1.	ramiprilat	57-67	angiotensin I converting enzyme	Rattus norvegicus	36-39
17825088-1	2007	AIM: Angiotensin-converting enzyme (ACE) inhibitors like ramiprilat bind to ACE expressed on the cell surface of endothelial cells and induce cell-specific signalling including the activation of activator protein (AP)-1.	ramiprilat	57-67	angiotensin I converting enzyme	Rattus norvegicus	76-79
17825088-1	2007	AIM: Angiotensin-converting enzyme (ACE) inhibitors like ramiprilat bind to ACE expressed on the cell surface of endothelial cells and induce cell-specific signalling including the activation of activator protein (AP)-1.	ramiprilat	57-67	Jun proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	195-219
17825088-13	2007	This newly described effect of ramiprilat may contribute to the protective effects seen by application of ACE inhibitors.	ramiprilat	31-41	angiotensin I converting enzyme	Rattus norvegicus	106-109
16088213-4	2005	We analyzed the effect of the ACE inhibitor ramiprilat on AngII-dependent cell adhesion molecule (CAM) expression and adhesion of monocytic THP-1 cells to endothelial cells.	ramiprilat	44-54	angiotensinogen	Homo sapiens	58-63
16734081-1	2006	Ramipril, an angiotensin-converting enzyme (ACE) inhibitor for use in dogs, is converted in vivo to its active form, ramiprilat, which is eliminated in the bile and urine in the dog.	ramiprilat	117-127	angiotensin I converting enzyme	Canis lupus familiaris	13-42
16734081-1	2006	Ramipril, an angiotensin-converting enzyme (ACE) inhibitor for use in dogs, is converted in vivo to its active form, ramiprilat, which is eliminated in the bile and urine in the dog.	ramiprilat	117-127	angiotensin I converting enzyme	Canis lupus familiaris	44-47
16734081-8	2006	The relationship between free plasma ramiprilat concentration and ACE activity was described by using the fractional Hill model.	ramiprilat	37-47	angiotensin I converting enzyme	Canis lupus familiaris	66-69
16408293-11	2006	After 72 h, the expression of CTGF and collagen type IV proteins in high-glucose cultures increased significantly and this increase was effectively attenuated by the candesartan or the ramiprilat.	ramiprilat	185-195	cellular communication network factor 2	Rattus norvegicus	30-34
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
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	dihydropyrimidinase	Homo sapiens	4-7
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	angiotensinogen	Homo sapiens	48-54
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
16088213-7	2005	Ramiprilat reduced AT 1 expression on endothelial cells and decreased the AngII-induced p65 translocation into the nucleus.	ramiprilat	0-10	angiotensin II receptor type 1	Homo sapiens	19-23
16088213-7	2005	Ramiprilat reduced AT 1 expression on endothelial cells and decreased the AngII-induced p65 translocation into the nucleus.	ramiprilat	0-10	angiotensinogen	Homo sapiens	74-79
16088213-7	2005	Ramiprilat reduced AT 1 expression on endothelial cells and decreased the AngII-induced p65 translocation into the nucleus.	ramiprilat	0-10	RELA proto-oncogene, NF-kB subunit	Homo sapiens	88-91
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 II receptor type 1	Homo sapiens	11-15
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	kininogen 1	Homo sapiens	144-154
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	kininogen 1	Homo sapiens	203-213
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	angiotensinogen	Homo sapiens	30-35
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
15569856-10	2005	As a consequence of the ramiprilat-induced increase in COX-2 expression, prostacyclin and prostaglandin E2, but not thromboxane A2, production was increased and was inhibited by the COX-2 inhibitor celecoxib.	ramiprilat	24-34	prostaglandin-endoperoxide synthase 2	Homo sapiens	55-60
15569856-5	2005	A similar (1.5- to 2-fold) increase in COX-2 protein was detected in primary cultures of human endothelial cells treated with ramiprilat.	ramiprilat	126-136	prostaglandin-endoperoxide synthase 2	Homo sapiens	39-44
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
15897362-8	2005	In cell culture, ramiprilat decreased collagen deposition by >50% and increased elastin and fibrillin-1 deposition by >3- and 4-fold respectively (histochemistry and immunohistochemistry).	ramiprilat	17-27	elastin	Homo sapiens	83-90
15897362-8	2005	In cell culture, ramiprilat decreased collagen deposition by >50% and increased elastin and fibrillin-1 deposition by >3- and 4-fold respectively (histochemistry and immunohistochemistry).	ramiprilat	17-27	fibrillin 1	Homo sapiens	95-106
15897362-10	2005	Ramiprilat also reduced gene and protein (Western) expression of both matrix metalloproteinase (MMP)-2 and MMP-3.	ramiprilat	0-10	matrix metallopeptidase 2	Homo sapiens	70-102
15897362-10	2005	Ramiprilat also reduced gene and protein (Western) expression of both matrix metalloproteinase (MMP)-2 and MMP-3.	ramiprilat	0-10	matrix metallopeptidase 3	Homo sapiens	107-112
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	prostaglandin-endoperoxide synthase 2	Homo sapiens	86-91
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
15569856-10	2005	As a consequence of the ramiprilat-induced increase in COX-2 expression, prostacyclin and prostaglandin E2, but not thromboxane A2, production was increased and was inhibited by the COX-2 inhibitor celecoxib.	ramiprilat	24-34	prostaglandin-endoperoxide synthase 2	Homo sapiens	182-187
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	prostaglandin-endoperoxide synthase 2	Homo sapiens	50-55
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	mitogen-activated protein kinase 8	Homo sapiens	167-170
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	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	62-81
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
29887764-9	2003	In both male and female groups, a subject-dependent yield of active metabolite ramiprilat was demonstrated, which was independent of the formulation.There is a large variation in the ramiprilat t1/2beta (50-60% CV).	ramiprilat	79-89	interleukin 1 receptor like 1	Homo sapiens	194-202
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
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	angiotensinogen	Homo sapiens	187-192
15530425-5	2004	Ramiprilat dose-dependently suppressed AngII-induced upregulation of IL-8 and MCP-1.	ramiprilat	0-10	angiotensinogen	Homo sapiens	39-44
15530425-5	2004	Ramiprilat dose-dependently suppressed AngII-induced upregulation of IL-8 and MCP-1.	ramiprilat	0-10	C-X-C motif chemokine ligand 8	Homo sapiens	69-73
15530425-5	2004	Ramiprilat dose-dependently suppressed AngII-induced upregulation of IL-8 and MCP-1.	ramiprilat	0-10	C-C motif chemokine ligand 2	Homo sapiens	78-83
15530425-6	2004	The suppressive effect of ramiprilat on AngII-induced chemokine production and release was in part caused by downregulation of NF-kappaB, but more by a selective and highly significant reduced expression of AT1 receptors as shown in monocytes and endothelial cells.	ramiprilat	26-36	angiotensinogen	Homo sapiens	40-45
15530425-6	2004	The suppressive effect of ramiprilat on AngII-induced chemokine production and release was in part caused by downregulation of NF-kappaB, but more by a selective and highly significant reduced expression of AT1 receptors as shown in monocytes and endothelial cells.	ramiprilat	26-36	nuclear factor kappa B subunit 1	Homo sapiens	127-136
15530425-6	2004	The suppressive effect of ramiprilat on AngII-induced chemokine production and release was in part caused by downregulation of NF-kappaB, but more by a selective and highly significant reduced expression of AT1 receptors as shown in monocytes and endothelial cells.	ramiprilat	26-36	angiotensin II receptor type 1	Homo sapiens	207-210
15530425-7	2004	CONCLUSION: In our study we demonstrated for the first time that ramiprilat reduced expression of AT1R in monocytes and endothelial cells.	ramiprilat	65-75	angiotensin II receptor type 1	Homo sapiens	98-102
15530425-8	2004	In addition, ramiprilat downregulated NF-kappaB activity and thereby reduced the AngII-induced release of IL-8 and MCP-1 in monocytes.	ramiprilat	13-23	nuclear factor kappa B subunit 1	Homo sapiens	38-47
15530425-8	2004	In addition, ramiprilat downregulated NF-kappaB activity and thereby reduced the AngII-induced release of IL-8 and MCP-1 in monocytes.	ramiprilat	13-23	angiotensinogen	Homo sapiens	81-86
15530425-8	2004	In addition, ramiprilat downregulated NF-kappaB activity and thereby reduced the AngII-induced release of IL-8 and MCP-1 in monocytes.	ramiprilat	13-23	C-X-C motif chemokine ligand 8	Homo sapiens	106-110
15530425-8	2004	In addition, ramiprilat downregulated NF-kappaB activity and thereby reduced the AngII-induced release of IL-8 and MCP-1 in monocytes.	ramiprilat	13-23	C-C motif chemokine ligand 2	Homo sapiens	115-120
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
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
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	mitogen-activated protein kinase 8	Mus musculus	184-187
14499867-6	2003	PAB-induced cardiac apoptosis was determined using Western blot analysis by a significantly increased expression of Bax protein and caspase-3 in the hypertrophied RV, which was diminished to almost control levels by chronic ramiprilate treatment.	ramiprilat	224-235	BCL2 associated X, apoptosis regulator	Rattus norvegicus	116-119
14499867-6	2003	PAB-induced cardiac apoptosis was determined using Western blot analysis by a significantly increased expression of Bax protein and caspase-3 in the hypertrophied RV, which was diminished to almost control levels by chronic ramiprilate treatment.	ramiprilat	224-235	caspase 3	Rattus norvegicus	132-141
14728069-4	2003	Moexipril may improve endothelial dysfunction; moexiprilat and ramiprilat have demonstrated greater activity than captopril, enalaprilat and quinaprilat in isolated endothelium-denuded segments of the rabbit jugular vein where bradykinin elicits a constrictor response, mediated by activation of the bradykinin B(2) receptor.	ramiprilat	63-73	B2 bradykinin receptor	Oryctolagus cuniculus	300-324
12717110-0	2003	Mechanisms of myocardial remodeling: ramiprilat blocks the expressional upregulation of protein kinase C-epsilon in the surviving myocardium early after infarction.	ramiprilat	37-47	protein kinase C, epsilon	Rattus norvegicus	88-112
12717110-6	2003	The influence of ACEI on PKC was tested by pretreating the rats with ramiprilat.	ramiprilat	69-79	angiotensin I converting enzyme	Rattus norvegicus	17-21
12717110-6	2003	The influence of ACEI on PKC was tested by pretreating the rats with ramiprilat.	ramiprilat	69-79	protein kinase C, alpha	Rattus norvegicus	25-28
12717110-10	2003	Treatment with ramiprilat could abolish this isoform-specific PKC regulation in both areas.	ramiprilat	15-25	protein kinase C, alpha	Rattus norvegicus	62-65
12941780-6	2003	In hearts from citrate-treated control rats, angiotensin II-stimulated [(3)H]phenylalanine incorporation and atrial natriuretic peptide and beta-myosin heavy chain mRNA expression were prevented by B-type natriuretic peptide (BNP), bradykinin, the ACE inhibitor ramiprilat, and the neutral endopeptidase inhibitor candoxatrilat.	ramiprilat	262-272	angiotensinogen	Rattus norvegicus	45-59
12941780-6	2003	In hearts from citrate-treated control rats, angiotensin II-stimulated [(3)H]phenylalanine incorporation and atrial natriuretic peptide and beta-myosin heavy chain mRNA expression were prevented by B-type natriuretic peptide (BNP), bradykinin, the ACE inhibitor ramiprilat, and the neutral endopeptidase inhibitor candoxatrilat.	ramiprilat	262-272	natriuretic peptide B	Rattus norvegicus	198-224
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	33-44	angiotensin I converting enzyme	Homo sapiens	4-7
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
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	matrix metallopeptidase 2	Homo sapiens	55-60
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	matrix metallopeptidase 9	Homo sapiens	65-70
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	matrix metallopeptidase 2	Homo sapiens	129-134
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	matrix metallopeptidase 9	Homo sapiens	181-186
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
12352328-9	2002	The ACE-inhibitor ramiprilat and AT -receptor antagonist candesartan enhance cardiac norepinephrine release selectively in ischemia by stimulating presynaptic bradykinin B -receptors.	ramiprilat	18-28	angiotensin I converting enzyme	Rattus norvegicus	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
11068029-5	2000	Angiotensin converting enzyme inhibitors, enalaprilat (3 microM), ramiprilat (1 microM) or lisinopril (1 microM), increased the bradykinin-induced renal vasodilation by 40% or more.	ramiprilat	66-76	angiotensin I converting enzyme	Rattus norvegicus	0-29
11121799-1	2001	OBJECTIVES: Our aim was to investigate the potential therapeutic role of endothelial nitric oxide synthase (eNOS) in the modulation of cardiac O(2) consumption induced by the angiotensin converting enzyme (ACE) inhibitor ramiprilat and amlodipine.	ramiprilat	221-231	nitric oxide synthase 3, endothelial cell	Mus musculus	73-106
11121799-1	2001	OBJECTIVES: Our aim was to investigate the potential therapeutic role of endothelial nitric oxide synthase (eNOS) in the modulation of cardiac O(2) consumption induced by the angiotensin converting enzyme (ACE) inhibitor ramiprilat and amlodipine.	ramiprilat	221-231	nitric oxide synthase 3, endothelial cell	Mus musculus	108-112
11121799-1	2001	OBJECTIVES: Our aim was to investigate the potential therapeutic role of endothelial nitric oxide synthase (eNOS) in the modulation of cardiac O(2) consumption induced by the angiotensin converting enzyme (ACE) inhibitor ramiprilat and amlodipine.	ramiprilat	221-231	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	206-209
11358946-5	2001	In this study, we evaluated the participation of endogenous Ang-(1-7) in the improvement of baroreflex sensitivity in spontaneously hypertensive rats after central infusion of ramiprilat, an ACE inhibitor.	ramiprilat	176-186	angiotensin I converting enzyme	Rattus norvegicus	191-194
11145934-6	2001	Moreover, reporter gene analysis with a rat ppET-1 promoter-luciferase construct transiently transfected into porcine aortic cultured endothelial cells revealed that the inhibitory effect of both ramiprilat and irbesartan on deformation-induced ppET-1 expression is species independent and mediated at the level of transcription.	ramiprilat	196-206	endothelin 1	Rattus norvegicus	44-50
11145934-6	2001	Moreover, reporter gene analysis with a rat ppET-1 promoter-luciferase construct transiently transfected into porcine aortic cultured endothelial cells revealed that the inhibitory effect of both ramiprilat and irbesartan on deformation-induced ppET-1 expression is species independent and mediated at the level of transcription.	ramiprilat	196-206	endothelin 1	Rattus norvegicus	245-251
10672850-6	2000	The ACE inhibitor, ramiprilat, potentiated these effects.	ramiprilat	19-29	angiotensin I converting enzyme	Canis lupus familiaris	4-7
11089901-6	2000	SR48968, a selective NK2 receptor antagonist, significantly inhibited the enhancing effect of ramiprilat on BK-induced bronchoconstriction.	ramiprilat	94-104	substance-K receptor	Cavia porcellus	21-33
10942157-11	2000	The enzyme cholinesterase was found to be inhibited by enalaprilat, ramiprilat, and fosinopril.	ramiprilat	68-78	cholinesterase	Oryctolagus cuniculus	11-25
10942157-14	2000	Our data suggest that ACE inhibitors enalaprilat, ramiprilat, and fosinopril produce a significant ocular hypotensive effect in acute and chronic models of ocular hypertension in rabbits.	ramiprilat	50-60	angiotensin-converting enzyme	Oryctolagus cuniculus	22-25
10779122-2	2000	Pretreatment with ramiprilat, an angiotensin-converting enzyme (ACE) inhibitor, induced cardioprotection and its possible mechanism of action was investigated in guinea-pig Langendorff perfused heart.	ramiprilat	18-28	LOW QUALITY PROTEIN: angiotensin-converting enzyme	Cavia porcellus	33-62
10779122-2	2000	Pretreatment with ramiprilat, an angiotensin-converting enzyme (ACE) inhibitor, induced cardioprotection and its possible mechanism of action was investigated in guinea-pig Langendorff perfused heart.	ramiprilat	18-28	LOW QUALITY PROTEIN: angiotensin-converting enzyme	Cavia porcellus	64-67
10779122-13	2000	HOE 140 (a selective bradykinin B2 receptor antagonist), calphostin C (a protein kinase C (PKC) inhibitor) and indomethacin (a cyclo-oxygenase inhibitor) all abolished the cardiac protective effect of ramiprilat.	ramiprilat	201-211	B2 bradykinin receptor	Cavia porcellus	21-43
10737671-8	2000	A combination of experiments with the bradykinin B2 receptor antagonist icatibant, the angiotensin II receptor antagonist losartan, and the converting enzyme inhibitor ramiprilat revealed that NPY-induced natriuresis involves bradykinin while kaliuresis involves angiotensin II.	ramiprilat	168-178	neuropeptide Y	Homo sapiens	193-196
11046097-4	2000	Ramiprilat significantly increased the half-life of BK (P <.01), but the effect was similar for the three kinds of tissues (297 +/- 104, 267 +/- 157, and 407 +/- 146 s, respectively; P = NS).	ramiprilat	0-10	kininogen 1	Homo sapiens	52-54
10900238-9	2000	Protein kinase C or phosphatase inhibitors, however, blocked the effects of BK on the receptor resensitized by enalaprilat or ramiprilat.	ramiprilat	126-136	kininogen 1	Homo sapiens	76-78
10397679-8	1999	This effect was inhibited by captopril and ramiprilat, suggesting conversion of angiotensin I to angiotensin II by angiotensin-converting enzyme in SMCs.	ramiprilat	43-53	angiotensinogen	Homo sapiens	80-93
10961737-3	1999	The effect of bradykinin was enhanced by the ACE inhibitor, ramiprilat.	ramiprilat	60-70	angiotensin I converting enzyme	Rattus norvegicus	45-48
10511138-4	1999	In an isolated perfused rat heart preparation subjected to global ischemia and reperfusion, both apstatin and ramiprilat (an ACE inhibitor) significantly decreased creatine kinase (CK) and lactate dehydrogenase (LDH) release.	ramiprilat	110-120	angiotensin I converting enzyme	Rattus norvegicus	125-128
10397679-8	1999	This effect was inhibited by captopril and ramiprilat, suggesting conversion of angiotensin I to angiotensin II by angiotensin-converting enzyme in SMCs.	ramiprilat	43-53	angiotensinogen	Homo sapiens	97-111
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
10209009-4	1999	Effects of bradykinin and ramiprilat on intracellular signaling were determined by monitoring the activation of the extracellularly regulated kinases Erk1 and Erk2 as well as [Ca2+]i increases in fura 2-loaded endothelial cells.	ramiprilat	26-36	mitogen-activated protein kinase 3	Homo sapiens	150-154
9755121-13	1998	The converting-enzyme inhibitor ramiprilat prevented the decline of the renovascular response with time; concomitantly, it magnified the NPY-induced diuresis, natriuresis, and calciuresis.	ramiprilat	32-42	neuropeptide Y	Rattus norvegicus	137-140
10209009-8	1999	Ramiprilat also decreased [3H]bradykinin binding to CR membranes when applied either before or after bradykinin stimulation.	ramiprilat	0-10	kininogen 1	Homo sapiens	30-40
10209009-8	1999	Ramiprilat also decreased [3H]bradykinin binding to CR membranes when applied either before or after bradykinin stimulation.	ramiprilat	0-10	kininogen 1	Homo sapiens	101-111
10209009-9	1999	Moreover, ramiprilat resulted in reactivation of the B2 receptor in bradykinin-stimulated cells and induced a second peak in [Ca2+]i and reactivation of Erk1/2.	ramiprilat	10-20	bradykinin receptor B2	Homo sapiens	53-64
10209009-9	1999	Moreover, ramiprilat resulted in reactivation of the B2 receptor in bradykinin-stimulated cells and induced a second peak in [Ca2+]i and reactivation of Erk1/2.	ramiprilat	10-20	kininogen 1	Homo sapiens	68-78
10209009-9	1999	Moreover, ramiprilat resulted in reactivation of the B2 receptor in bradykinin-stimulated cells and induced a second peak in [Ca2+]i and reactivation of Erk1/2.	ramiprilat	10-20	mitogen-activated protein kinase 3	Homo sapiens	153-159
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
10082326-3	1999	By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained.	ramiprilat	111-121	angiotensin I converting enzyme	Rattus norvegicus	14-43
10082326-3	1999	By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained.	ramiprilat	111-121	angiotensin I converting enzyme	Rattus norvegicus	45-48
10082326-3	1999	By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained.	ramiprilat	111-121	alanyl aminopeptidase, membrane	Rattus norvegicus	51-67
10082326-3	1999	By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained.	ramiprilat	111-121	membrane metallo-endopeptidase	Rattus norvegicus	78-99
10082326-3	1999	By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained.	ramiprilat	111-121	membrane metallo-endopeptidase	Rattus norvegicus	101-104
9422802-11	1997	The rate of kininogen synthesis was not affected by ramiprilat, bacterial lipopolysaccharide, nerve growth factor or dexamethasone, but was stimulated 1.4 fold when cells were pretreated for 1 day with 1 microM desoxycorticosterone.	ramiprilat	52-62	kininogen 2-like 1	Rattus norvegicus	12-21
9655885-7	1998	Ang 1-7 inhibited purified angiotensin-converting enzyme (ACE) by 30 +/- 3.5% (n = 4) at 10(-6) M. However, in BK-pretreated rings, the ACE inhibitor ramiprilat did not induce relaxation, nor did it affect the relaxant response to Ang 1-7, which suggests that the effect of Ang 1-7 was not caused by ACE inhibition.	ramiprilat	150-160	angiogenin	Sus scrofa	0-7
9655885-7	1998	Ang 1-7 inhibited purified angiotensin-converting enzyme (ACE) by 30 +/- 3.5% (n = 4) at 10(-6) M. However, in BK-pretreated rings, the ACE inhibitor ramiprilat did not induce relaxation, nor did it affect the relaxant response to Ang 1-7, which suggests that the effect of Ang 1-7 was not caused by ACE inhibition.	ramiprilat	150-160	angiotensin-converting enzyme	Sus scrofa	136-139
9655885-7	1998	Ang 1-7 inhibited purified angiotensin-converting enzyme (ACE) by 30 +/- 3.5% (n = 4) at 10(-6) M. However, in BK-pretreated rings, the ACE inhibitor ramiprilat did not induce relaxation, nor did it affect the relaxant response to Ang 1-7, which suggests that the effect of Ang 1-7 was not caused by ACE inhibition.	ramiprilat	150-160	angiotensin-converting enzyme	Sus scrofa	136-139
9446690-10	1998	Studies with the converting enzyme inhibitor ramiprilat and the bradykinin receptor antagonist icatibant indicate that bradykinin mediates, at least partly, diuretic NPY effects.	ramiprilat	45-55	kininogen 1	Homo sapiens	119-129
9446690-10	1998	Studies with the converting enzyme inhibitor ramiprilat and the bradykinin receptor antagonist icatibant indicate that bradykinin mediates, at least partly, diuretic NPY effects.	ramiprilat	45-55	neuropeptide Y	Homo sapiens	166-169
9268227-8	1997	Coperfusion with the angiotensin-converting enzyme inhibitor, ramiprilat (0.5 microM), alone blocked cleavage at the Pro7-Phe8 bond and increased intact [3H]Bk to 75 +/- 3% (p < 0.001 vs. control).	ramiprilat	62-72	angiotensin I converting enzyme	Rattus norvegicus	21-50
9401784-7	1997	Kininases were identified by ramiprilat, phosphoramidon, diprotin A and 2-mercaptoethanol or apstatin as specific inhibitors of ACE, neutral endopeptidase 24.11 (NEP), dipeptidylaminopeptidase IV and aminopeptidase P (APP), respectively.	ramiprilat	29-39	angiotensin I converting enzyme	Rattus norvegicus	128-131
9260992-2	1997	The aim of the present study was to determine the role of ACE in this model and to compare the treatment with the ACE inhibitor ramiprilat with that with the angiotensin II antagonist HR 720.	ramiprilat	128-138	angiotensin I converting enzyme	Rattus norvegicus	114-117
8840953-4	1996	Both ACE inhibitors were associated with an increase in the concentration of whole blood ANG I; however, tissue ANG I levels were significantly increased only following ACE inhibition with ramiprilat but not with enalaprilat.	ramiprilat	189-199	angiotensin I converting enzyme	Rattus norvegicus	5-8
9117086-16	1997	Degradation of [3H]-BK was not influenced by ramiprilat, but was inhibited by 85% in the presence of phosphoramidon.	ramiprilat	45-55	kininogen 1	Bos taurus	20-22
8840953-4	1996	Both ACE inhibitors were associated with an increase in the concentration of whole blood ANG I; however, tissue ANG I levels were significantly increased only following ACE inhibition with ramiprilat but not with enalaprilat.	ramiprilat	189-199	angiotensin I converting enzyme	Rattus norvegicus	169-172
8840953-5	1996	Both plasma and urinary bladder tissue ANG-(1-8) levels decreased significantly following ACE inhibition, but only with ramiprilat.	ramiprilat	120-130	angiogenin	Rattus norvegicus	39-47
8575435-7	1995	In the presence of the inhibitor ramiprilat, the frequencies increase but the spectral broadening is about the same as for ACE without inhibitor.	ramiprilat	33-43	angiotensin-converting enzyme	Oryctolagus cuniculus	123-126
8856122-1	1996	We have recently demonstrated that the angiotensin I-converting enzyme (ACE) inhibitor ramiprilat augments the endothelium-dependent dilator response to bradykinin in the isolated perfused rat heart by an interaction at the B2 receptor level.	ramiprilat	87-97	angiotensin I converting enzyme	Rattus norvegicus	39-70
8856122-1	1996	We have recently demonstrated that the angiotensin I-converting enzyme (ACE) inhibitor ramiprilat augments the endothelium-dependent dilator response to bradykinin in the isolated perfused rat heart by an interaction at the B2 receptor level.	ramiprilat	87-97	angiotensin I converting enzyme	Rattus norvegicus	72-75
8856122-3	1996	Among five different ACE inhibitors, moexiprilat and ramiprilat proved to be the most effective in potentiating the constrictor response to bradykinin.	ramiprilat	53-63	angiotensin-converting enzyme	Oryctolagus cuniculus	21-24
9011643-1	1996	The attenuation of myocardial stunning by the ACE inhibitor ramiprilat is prevented by cyclooxygenase inhibition with indomethacin.	ramiprilat	60-70	angiotensin I converting enzyme	Canis lupus familiaris	46-49
9011643-14	1996	The attenuation of myocardial stunning by the ACE inhibitor ramiprilat is not prevented by aspirin in dosages which are nevertheless sufficient to inhibit platelet aggregation.	ramiprilat	60-70	angiotensin I converting enzyme	Canis lupus familiaris	46-49
9011647-7	1996	Experiments were also performed in the presence of the NO-synthase inhibitor nitro-L-arginine (10 microM) and the ACE-inhibitor ramiprilat (2 microM), the latter known to enhance endogenous nitric oxide formation.	ramiprilat	128-138	LOW QUALITY PROTEIN: angiotensin-converting enzyme	Cavia porcellus	114-117
8575435-12	1995	However, for ACE and its complex with ramiprilat, a significant distortion of the cadmium geometry for carboxypeptidase A had to be adopted in order to calculate NQI"s close to the experimental values.	ramiprilat	38-48	angiotensin-converting enzyme	Oryctolagus cuniculus	13-16
8653880-6	1996	In contrast, pretreatment with the selective bradykinin antagonist HOE 140 (10 micromol/L) attenuated ramiprilat-induced increase in flow velocity (P<.025) and coronary blood flow (P<.05) but not epicardial coronary cross-sectional area.	ramiprilat	102-112	kininogen 1	Canis lupus familiaris	45-55
8653880-9	1996	Ramiprilat-induced vasodilation in resistance arteries is in part mediated by the action of bradykinin.	ramiprilat	0-10	kininogen 1	Canis lupus familiaris	92-102
8591882-2	1996	The blood pressure of rats made hypertensive by coarctation of the aorta between the renal arteries at their origin fell after administration of the angiotensin-converting enzyme inhibitor ramiprilat (2 mg/kg IV; -75 +/- 5 mm Hg) or the angiotensin II antagonist losartan (30 mg/kg IV; -79 +/- 6 mm Hg).	ramiprilat	189-199	angiotensinogen	Rattus norvegicus	237-251
8575435-10	1995	The calculated spectral parameters could be modelled with the measured parameters if the solvent ligand is H2O in free ACE, carboxylate from ramiprilat in the ACE-ramiprilat complex and a mercapto group in the ACE-captopril complex.	ramiprilat	141-151	angiotensin-converting enzyme	Oryctolagus cuniculus	159-162
8575435-10	1995	The calculated spectral parameters could be modelled with the measured parameters if the solvent ligand is H2O in free ACE, carboxylate from ramiprilat in the ACE-ramiprilat complex and a mercapto group in the ACE-captopril complex.	ramiprilat	141-151	angiotensin-converting enzyme	Oryctolagus cuniculus	159-162
8531074-10	1995	In the presence of ramiprilat (0.5 microM), only 22% +/- 6% of the radioactivity in the perfusate was intact [3H]-Bk, and the remaining radioactivity indicated cleavage of the Arg1-Pro2 bond.	ramiprilat	19-29	arginase 1	Rattus norvegicus	176-180
7503796-7	1995	When 125I-Ang I was perfused in the presence of ACE inhibitors (enalaprilat, ramiprilat) in concentrations up to 130 microM, the formation of Ang II was only partially inhibited (approximately 50%).	ramiprilat	77-87	angiotensin I converting enzyme	Rattus norvegicus	48-51
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
7503796-7	1995	When 125I-Ang I was perfused in the presence of ACE inhibitors (enalaprilat, ramiprilat) in concentrations up to 130 microM, the formation of Ang II was only partially inhibited (approximately 50%).	ramiprilat	77-87	angiotensinogen	Rattus norvegicus	142-148
7769810-7	1995	The ACE inhibitor ramiprilat (RT 25 microM) improved postischemic function significantly (55% recovery of EHW vs. 29% for controls).	ramiprilat	18-28	LOW QUALITY PROTEIN: angiotensin-converting enzyme	Cavia porcellus	4-7
7545893-9	1995	CONCLUSIONS: These results indicate that the in vivo cardioprotective effect of ramiprilat can be abolished by antagonizing bradykinin receptors or inhibiting nitric oxide synthase, and that the effect is not related to angiotensin II receptor activity.	ramiprilat	80-90	angiotensinogen	Rattus norvegicus	220-234
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
7646311-4	1995	In the kidney: the affinity of 3H-ramiprilate for the brush borders of the proximal tubular cells was increased by high concentrations of chloride ions as observed in the renal parenchyma, the presence of esterases makes local activation of ramipril (diester) into ramiprilate (active diacid) possible, prolonged treatment with ramipril leads to a lowering of the concentration of ACE in the brush border of the proximal tubular cells, verified after the elimination of the ACE inhibitor fixed on the tissue.	ramiprilat	34-45	angiotensin I converting enzyme	Rattus norvegicus	381-384
7646311-4	1995	In the kidney: the affinity of 3H-ramiprilate for the brush borders of the proximal tubular cells was increased by high concentrations of chloride ions as observed in the renal parenchyma, the presence of esterases makes local activation of ramipril (diester) into ramiprilate (active diacid) possible, prolonged treatment with ramipril leads to a lowering of the concentration of ACE in the brush border of the proximal tubular cells, verified after the elimination of the ACE inhibitor fixed on the tissue.	ramiprilat	34-45	angiotensin I converting enzyme	Rattus norvegicus	474-477
7810335-2	1994	ACE-inhibition by ramiprilat reduced, and subsequent infusion of Ang II (30 ng kg-1 min-1 i.v.)	ramiprilat	18-28	angiotensin I converting enzyme	Canis lupus familiaris	0-3
8071842-1	1994	The purpose of this study was to compare a lipophilic angiotensin-converting enzyme (ACE) inhibitor, ramiprilat, to the hydrophilic agent, captopril, with respect to its efficacy in decreasing blood pressure (BP) and increasing renal blood flow (RBF).	ramiprilat	101-111	angiotensin-converting enzyme	Oryctolagus cuniculus	54-83
7522595-2	1994	Preincubation with captopril, enalaprilat, enalapril, or ramiprilat for 40 min significantly reduced the angiotensin II-induced transplasma membrane calcium influx but did not influence the angiotension II-induced calcium release from internal stores.	ramiprilat	57-67	angiotensinogen	Rattus norvegicus	105-119
7522595-3	1994	Captopril and ramiprilat also inhibited arginine vasopressin, but not the thapsigargin-, norepinephrine-, or the BayK 8644-induced changes in cytosolic calcium.	ramiprilat	14-24	arginine vasopressin	Rattus norvegicus	49-60
8087948-0	1994	Attenuation of myocardial stunning by the ACE inhibitor ramiprilat through a signal cascade of bradykinin and prostaglandins but not nitric oxide.	ramiprilat	56-66	angiotensin I converting enzyme	Canis lupus familiaris	42-45
8087948-0	1994	Attenuation of myocardial stunning by the ACE inhibitor ramiprilat through a signal cascade of bradykinin and prostaglandins but not nitric oxide.	ramiprilat	56-66	kininogen 1	Canis lupus familiaris	95-105
8087948-11	1994	Thus, the beneficial effect of ramiprilat on the functional recovery of stunned myocardium was obviously mediated by bradykinin.	ramiprilat	31-41	kininogen 1	Canis lupus familiaris	117-127
8087948-19	1994	CONCLUSIONS: In summary, the attenuation of stunning by the ACE inhibitor ramiprilat involves a signal cascade of bradykinin and prostaglandins but not nitric oxide.	ramiprilat	74-84	angiotensin I converting enzyme	Canis lupus familiaris	60-63
8087948-19	1994	CONCLUSIONS: In summary, the attenuation of stunning by the ACE inhibitor ramiprilat involves a signal cascade of bradykinin and prostaglandins but not nitric oxide.	ramiprilat	74-84	kininogen 1	Canis lupus familiaris	114-124
8071842-1	1994	The purpose of this study was to compare a lipophilic angiotensin-converting enzyme (ACE) inhibitor, ramiprilat, to the hydrophilic agent, captopril, with respect to its efficacy in decreasing blood pressure (BP) and increasing renal blood flow (RBF).	ramiprilat	101-111	angiotensin-converting enzyme	Oryctolagus cuniculus	85-88
7935859-0	1994	Contribution by bradykinin to the natriuretic response to the angiotensin converting enzyme inhibitor ramiprilat in spontaneously hypertensive rats.	ramiprilat	102-112	angiotensin I converting enzyme	Rattus norvegicus	62-91
7516015-4	1994	Addition of the ACE-inhibitor ramiprilat (RT) to the perfusate throughout the experiment improved postischemic function significantly (55% recovery of EHW for 25 microM RT vs. 30% for controls).	ramiprilat	30-40	LOW QUALITY PROTEIN: angiotensin-converting enzyme	Cavia porcellus	16-19
8157707-8	1994	Angiotensin II incubated with renal tissue from fasted rats suppressed activity to fed levels, but this effect was prevented by the presence of ramiprilat.	ramiprilat	144-154	angiotensinogen	Rattus norvegicus	0-14