PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17643133-5 2007 CGS-26303 and phosphoramidon, though not thiorphan, a neutral endopeptidase (NEP) inhibitor, stimulated ECE-1 expression in cells (maximal effect at 16 h, 25 microM). phosphoramidon 14-28 endothelin converting enzyme 1 Homo sapiens 104-109 19151386-6 2009 ET-1 precursor big ET-1 elicited time-dependent vasoconstriction over 20 minutes, which was blocked by the ECE-1 inhibitor phosphoramidon. phosphoramidon 123-137 endothelin converting enzyme 1 Homo sapiens 107-112 18992253-5 2009 Here, we present the crystal structure of the extracellular domain (residues 90-770) of human ECE-1 (C428S) with the generic metalloprotease inhibitor phosphoramidon determined at 2.38 A resolution. phosphoramidon 151-165 endothelin converting enzyme 1 Homo sapiens 94-99 17643133-4 2007 KEY RESULTS: ECE-1 activity was completely inhibited by CGS-26303 25 microM and phosphoramidon 100 microM. phosphoramidon 80-94 endothelin converting enzyme 1 Homo sapiens 13-18 15969636-7 2005 Phosphoramidon, thiorphan, acidification, and phenanthroline inhibited PM ECE activity; the cytosolic ECE activity was not affected by phenanthroline but was inhibited by the others. phosphoramidon 0-14 endothelin converting enzyme 1 Homo sapiens 74-77 15969636-9 2005 Pepstatin, a potent inhibitor of cathepsins, and phosphoramidon, a potent inhibitor of ECE, inhibited the cytosolic conversion of Big ET-1 peptide by 46% and 35%, respectively, whereas the combination of both inhibited the cytosolic activity by 93%. phosphoramidon 49-63 endothelin converting enzyme 1 Homo sapiens 87-90 12827039-0 2003 The effects of phosphoramidon on the expression of human endothelin-converting enzyme-1 (ECE-1) isoforms. phosphoramidon 15-29 endothelin converting enzyme 1 Homo sapiens 57-87 15151517-9 2004 The effects of big ET-1([1-38]) and phosphoramidon suggest the presence of endogenous ECE activity in the skin. phosphoramidon 36-50 endothelin converting enzyme 1 Homo sapiens 86-89 12827039-0 2003 The effects of phosphoramidon on the expression of human endothelin-converting enzyme-1 (ECE-1) isoforms. phosphoramidon 15-29 endothelin converting enzyme 1 Homo sapiens 89-94 12827039-2 2003 This process is inhibited by phosphoramidon through binding to the catalytic domain of ECE-1. phosphoramidon 29-43 endothelin converting enzyme 1 Homo sapiens 87-92 12827039-5 2003 It is not known, however, whether phosphoramidon has similar effects on the expression of other ECE-1 isoforms. phosphoramidon 34-48 endothelin converting enzyme 1 Homo sapiens 96-101 12827039-10 2003 Taken together, our results demonstrate that phosphoramidon differentially affects the expression of three human ECE-1 isoforms. phosphoramidon 45-59 endothelin converting enzyme 1 Homo sapiens 113-118 10352019-5 1999 Northern blot analysis showed that ECE-1 (and not ECE-2) is specifically expressed in Sertoli cells; competitive enzyme immunoassay of ET production showed that Sertoli cell monolayers are capable of cleaving big ET-1, an activity inhibited by the ECE inhibitor phosphoramidon. phosphoramidon 262-276 endothelin converting enzyme 1 Homo sapiens 35-38 11099107-6 2000 PGE2 at 10(-5) M reduced the expression of ET-1 at the mRNA and protein levels but did not exert any significant modification at lower concentrations from 10(-10) to 10(6) M. Phosphoramidon, an endothelin converting enzyme (ECE) inhibitor, drastically decreased the amount of ET-1 accumulating in the culture medium in basal conditions or after UVB irradiation. phosphoramidon 175-189 endothelin converting enzyme 1 Homo sapiens 224-227 11145756-6 2000 Phosphoramidon and a specific ECE-1 inhibitor, FR901533, inhibited ECE-1 activity by over 90%. phosphoramidon 0-14 endothelin converting enzyme 1 Homo sapiens 67-72 11078325-1 2000 Phosphoramidon has been shown to inhibit endothelin-converting enzyme-1 (ECE-1) in a remarkably pH-dependent manner (Ahn et al. phosphoramidon 0-14 endothelin converting enzyme 1 Homo sapiens 41-71 11078325-1 2000 Phosphoramidon has been shown to inhibit endothelin-converting enzyme-1 (ECE-1) in a remarkably pH-dependent manner (Ahn et al. phosphoramidon 0-14 endothelin converting enzyme 1 Homo sapiens 73-78 12477147-10 2002 ECE-1 inhibitors, phosphoramidon and FR-901533, inhibited vascular ECE-1 activity by more than 80%. phosphoramidon 18-32 endothelin converting enzyme 1 Homo sapiens 0-5 12477147-10 2002 ECE-1 inhibitors, phosphoramidon and FR-901533, inhibited vascular ECE-1 activity by more than 80%. phosphoramidon 18-32 endothelin converting enzyme 1 Homo sapiens 67-72 12193062-9 2002 Cleavage of bradykinin by PgPepO occurs at the Pro(7)-Phe(8) bond and is inhibited by the NEP and ECE-1 inhibitor phosphoramidon in a pH-dependent fashion (IC(50) =10 microM at pH 7.0) but not by thiorphan, an NEP-specific inhibitor. phosphoramidon 114-128 endothelin converting enzyme 1 Homo sapiens 98-103 10455291-4 1999 Increases in [Ca2+]i caused by ET-1(1-31), big ET-1 and ET-2(1-31) were completely inhibited by 10(-4)M phosphoramidon, a dual neutral endopeptidase (NEP)/endothelin-converting enzyme (ECE) inhibitor, and 10(-5)M thiorphan, a NEP inhibitor. phosphoramidon 104-118 endothelin converting enzyme 1 Homo sapiens 185-188 10352019-5 1999 Northern blot analysis showed that ECE-1 (and not ECE-2) is specifically expressed in Sertoli cells; competitive enzyme immunoassay of ET production showed that Sertoli cell monolayers are capable of cleaving big ET-1, an activity inhibited by the ECE inhibitor phosphoramidon. phosphoramidon 262-276 endothelin converting enzyme 1 Homo sapiens 35-40 9515580-6 1998 However phosphoramidon (100 microM), an inhibitor of ECE and NEP, almost abolished specific binding, indicating that both NEP and ECE cleave big ET-1 in the kidney. phosphoramidon 8-22 endothelin converting enzyme 1 Homo sapiens 53-56 10217651-7 1999 Phosphoramidon-sensitive ECE activity and immunodetectable amounts of ECE protein in left ventricular membrane preparations did not differ between NF and DCM hearts. phosphoramidon 0-14 endothelin converting enzyme 1 Homo sapiens 25-28 10222335-4 1999 ECE-1 and ECE-2 can be differentiated by pH dependence for optimal activity and by sensitivity to phosphoramidon, which shows selectivity for ECE-2 over ECE-1 and PD159790, a novel ECE-1 selective inhibitor. phosphoramidon 98-112 endothelin converting enzyme 1 Homo sapiens 0-5 10222335-4 1999 ECE-1 and ECE-2 can be differentiated by pH dependence for optimal activity and by sensitivity to phosphoramidon, which shows selectivity for ECE-2 over ECE-1 and PD159790, a novel ECE-1 selective inhibitor. phosphoramidon 98-112 endothelin converting enzyme 1 Homo sapiens 153-158 10222335-4 1999 ECE-1 and ECE-2 can be differentiated by pH dependence for optimal activity and by sensitivity to phosphoramidon, which shows selectivity for ECE-2 over ECE-1 and PD159790, a novel ECE-1 selective inhibitor. phosphoramidon 98-112 endothelin converting enzyme 1 Homo sapiens 153-158 10222335-7 1999 In contrast, ECE activity was unaffected by 30 micromol/L PD159790 but was inhibited markedly by 0.1 and 100 micromol/L phosphoramidon at pH 5. phosphoramidon 120-134 endothelin converting enzyme 1 Homo sapiens 13-16 9515580-6 1998 However phosphoramidon (100 microM), an inhibitor of ECE and NEP, almost abolished specific binding, indicating that both NEP and ECE cleave big ET-1 in the kidney. phosphoramidon 8-22 endothelin converting enzyme 1 Homo sapiens 130-133 9533826-7 1998 Pre-treatment with phosphoramidon (1 micron) an ECE-inhibitor, followed by TNF-alpha stimulation, decreased ir-ET-1 levels. phosphoramidon 19-33 endothelin converting enzyme 1 Homo sapiens 48-51 9595400-9 1998 Such observations, in terms of substrate selectivity and phosphoramidon sensitivity, suggest the presence of distinct ECE activities in human vein and arteries. phosphoramidon 57-71 endothelin converting enzyme 1 Homo sapiens 118-121 9595528-5 1998 Membrane ECE activity was phosphoramidon-sensitive, in contrast to the cytosolic activity capable of producing ET-1 from big ET-1. phosphoramidon 26-40 endothelin converting enzyme 1 Homo sapiens 9-12 9422810-23 1997 To conclude we have demonstrated the presence of a phosphoramidon-sensitive ECE on the smooth muscle layer of the human umbilical vein which can convert big ET-1, big ET-2(1-37), big ET-2(1-38) and big ET-3 to their mature biologically active forms. phosphoramidon 51-65 endothelin converting enzyme 1 Homo sapiens 76-79 8994440-6 1997 The size of the neointima was effectively reduced by phosphoramidon, an inhibitor of neutral metalloproteases, including ECE-1. phosphoramidon 53-67 endothelin converting enzyme 1 Homo sapiens 121-126 8587408-7 1995 These data confirm that exogenous big ET-1 is locally converted to ET-1 and CTF in the human forearm, at least in part by a phosphoramidon-sensitive ECE. phosphoramidon 124-138 endothelin converting enzyme 1 Homo sapiens 149-152 8901663-5 1996 In CHF patients (n = 10), phosphoramidon (a combined ECE and neutral endopeptidase inhibitor) and BQ-123 (an ETA receptor antagonist) increased FBF by 52 +/- 10% (P = .0006) and 31 +/- 6% (P = .002), respectively, and thiorphan (a selective neutral endopeptidase inhibitor) reduced FBF by 15 +/- 5% (P = .0007). phosphoramidon 26-40 endothelin converting enzyme 1 Homo sapiens 53-56 8828809-2 1996 The specific ECE activity was demonstrated by a phosphoramidon dose-dependent decrease in ET-1 level with a concomitant increase in big ET-1 level. phosphoramidon 48-62 endothelin converting enzyme 1 Homo sapiens 13-16 7857289-1 1995 Subcellular fractionation of the phosphoramidon sensitive membrane-bound endothelin converting enzyme (ECE-1) activity from homogenates of bovine aortic endothelial cells and the human endothelial cell line EA.hy 926, combined with studies of intact cells, shows ECE-1 to be localised primarily to the plasma membrane with the topology of an ectoenzyme. phosphoramidon 33-47 endothelin converting enzyme 1 Homo sapiens 263-268 7857289-3 1995 The metallopeptidase ECE-1 obtained displayed a neutral pH optimum, a molecular weight of 250 kDa on gel filtration chromatography and was inhibited by phosphoramidon with an IC50 of 0.8 microM. phosphoramidon 152-166 endothelin converting enzyme 1 Homo sapiens 21-26 8587357-3 1995 Brachial artery infusion of local doses of big ET-1 caused a slow-onset, dose-dependent forearm vasoconstriction that was abolished by co-infusion of the ECE inhibitor phosphoramidon. phosphoramidon 168-182 endothelin converting enzyme 1 Homo sapiens 154-157 7550091-2 1995 Phosphoramidon, at concentrations of 10(-6) to 2 x 10(-4) M, caused a biphasic alteration of the ET-1 release, i.e., at lower concentrations of the drug, there were slight but unexpected increases of the release, whereas higher concentrations led to a decrease which is due to the drug-induced inhibition of ECE. phosphoramidon 0-14 endothelin converting enzyme 1 Homo sapiens 308-311 7550091-5 1995 When high concentrations of phosphoramidon were added, there was a dramatic increase in the release of big ET-1, which cannot be explained only by the drug-induced inhibition of ECE. phosphoramidon 28-42 endothelin converting enzyme 1 Homo sapiens 178-181 7550091-8 1995 In a similar fashion, phosphoramidon markedly inhibited ECE activity of the membrane fraction of cultured cells. phosphoramidon 22-36 endothelin converting enzyme 1 Homo sapiens 56-59 7550091-9 1995 Thus, ET-1 generation from exogenously applied big ET-1 reflects the functional phosphoramidon-sensitive ECE activities in human aortic endothelial cells. phosphoramidon 80-94 endothelin converting enzyme 1 Homo sapiens 105-108 7864859-2 1995 Metalloendoprotease inhibitors (phosphoramidon and DL-thiorphan), but not captopril, inhibited the contractions elicited by human big ET-1 and big ET-2 but DL-thiorphan was less active, suggesting that a non-selective enzymatic process is involved in conversion of big ET-1 and big ET-2 in addition to a phosphoramidon-sensitive ECE. phosphoramidon 32-46 endothelin converting enzyme 1 Homo sapiens 329-332 8587470-1 1995 The structure-activity relationships of phosphoramidon analogues for inhibition of endothelin-converting enzyme (ECE), neutral endopeptidase 24.11 (NEP), and angiotensin-converting enzyme (ACE) were compared. phosphoramidon 40-54 endothelin converting enzyme 1 Homo sapiens 113-116 8587470-2 1995 Phosphoramidon inhibited ECE, NEP, and ACE activities with IC50 values of 3.5, 0.034, and 78 microM, respectively. phosphoramidon 0-14 endothelin converting enzyme 1 Homo sapiens 25-28 8587470-3 1995 Removal of the rhamnose moiety of phosphoramidon (dipeptide 3) reduced the potency for ECE (IC50 = 70 microM), whereas the potencies for NEP (0.003 microM) and ACE (0.20 microM) were increased. phosphoramidon 34-48 endothelin converting enzyme 1 Homo sapiens 87-90 8587470-6 1995 These results suggest that a hydrophobic group in the P1 position of phosphoramidon analogues increases the potency for ECE significantly, whereas compounds containing a free phosphonic acid are optimal for inhibition of NEP and ACE. phosphoramidon 69-83 endothelin converting enzyme 1 Homo sapiens 120-123 8458433-3 1993 The lipoprotein ECE activity, which was optimal at pH 7.0, was inhibited by EDTA, o-phenanthroline, phosphoramidon, thiorphan, phenylmethanesulfonyl fluoride and chymostatin, but not by cysteine or aspartic proteinase inhibitors, suggesting metalloproteinase- and chymotrypsin-like properties. phosphoramidon 100-114 endothelin converting enzyme 1 Homo sapiens 16-19 7949376-6 1994 Both intact cells and membrane preparations used as the enzyme source predict similar IC50 values for phosphoramidon inhibition of ECE (ca 1 microM). phosphoramidon 102-116 endothelin converting enzyme 1 Homo sapiens 131-134 8020872-1 1994 The structure activity relationship of phosphoramidon analogues was studied for their ability to reduce the hypertensive effect of exogenous proET-1, probably via inhibition of an endothelin converting enzyme activity (ECE). phosphoramidon 39-53 endothelin converting enzyme 1 Homo sapiens 219-222 8020872-4 1994 Furthermore, the tryptophan residue of phosphoramidon appeared to be particularly important for the ECE inhibition, whereas thermolysin inhibition seemed to depend greatly on the leucine residue. phosphoramidon 39-53 endothelin converting enzyme 1 Homo sapiens 100-103 8020872-5 1994 It is concluded that in vivo ECE and thermolysin differ in the way they recognise phosphoramidon. phosphoramidon 82-96 endothelin converting enzyme 1 Homo sapiens 29-32 8020872-6 1994 The existence of an hydrophobic pocket, specific for the recognition of the tryptophan residue of phosphoramidon, could be proposed for ECE. phosphoramidon 98-112 endothelin converting enzyme 1 Homo sapiens 136-139 1953706-1 1991 Based on our previous findings that phosphoramidon-sensitive endothelin (ET) converting enzyme (ECE) converts human big ET-1 but does not big ET-3, we investigated structural requirement for substrate peptide. phosphoramidon 36-50 endothelin converting enzyme 1 Homo sapiens 96-99 8431480-3 1993 The metalloproteinase inhibitor phosphoramidon inhibited the conversion of big ET-1 into mature ET-1 both in vivo and in cultured endothelial cells, suggesting that ECE may be a neutral metalloproteinase. phosphoramidon 32-46 endothelin converting enzyme 1 Homo sapiens 165-168 7510007-6 1993 Our results, presented in the above-mentioned models, illustrate the capacity of the phosphoramidon-sensitive endothelin-converting enzyme (ECE) to discriminate between human big ET-1 and big ET-3. phosphoramidon 85-99 endothelin converting enzyme 1 Homo sapiens 140-143 1282965-7 1992 In all tissues studied, the ECE activity was significantly inhibited by phosphoramidon or ethylenediaminetetra-acetate. phosphoramidon 72-86 endothelin converting enzyme 1 Homo sapiens 28-31 7509999-7 1993 A number of studies have reported that the final processing step in ET-1 biosynthesis by the hypothetical endothelin-converting enzyme (ECE) is inhibited by phosphoramidon (PHOS). phosphoramidon 157-171 endothelin converting enzyme 1 Homo sapiens 136-139 7509999-7 1993 A number of studies have reported that the final processing step in ET-1 biosynthesis by the hypothetical endothelin-converting enzyme (ECE) is inhibited by phosphoramidon (PHOS). phosphoramidon 173-177 endothelin converting enzyme 1 Homo sapiens 136-139 1540181-2 1992 ECEs derived from these epithelial cells were very similar to the endothelial ECE in the following biochemical properties: 1) The optimum pH was 7.0; 2) the Km value for big ET-1 was approximately 30 microM; 3) the enzyme was potently inhibited by EDTA, o-phenanthroline and phosphoramidon; and 4) the enzyme did not convert big ET-2 or big ET-3. phosphoramidon 275-289 endothelin converting enzyme 1 Homo sapiens 0-3 1540181-3 1992 These data suggest that phosphoramidon-sensitive ECE is involved in the processing of big ET-1 to ET-1 in the renal tubule. phosphoramidon 24-38 endothelin converting enzyme 1 Homo sapiens 49-52 1725347-10 1991 We further suggest that to induce the release of prostanoids in perfused lungs, human big ET needs to be converted to ET-1 by a phosphoramidon-sensitive endothelin-converting enzyme (ECE). phosphoramidon 128-142 endothelin converting enzyme 1 Homo sapiens 153-181 1725347-10 1991 We further suggest that to induce the release of prostanoids in perfused lungs, human big ET needs to be converted to ET-1 by a phosphoramidon-sensitive endothelin-converting enzyme (ECE). phosphoramidon 128-142 endothelin converting enzyme 1 Homo sapiens 183-186 26996808-6 2016 Modeling was performed using the experimental 3D structure of human endothelin-converting enzyme-1 in the presence of the metabolite phosphoramidon. phosphoramidon 133-147 endothelin converting enzyme 1 Homo sapiens 68-98 33917140-11 2021 The ECE inhibitor phosphoramidon induced autophagy. phosphoramidon 18-32 endothelin converting enzyme 1 Homo sapiens 4-7 24000822-0 2014 Exploring mode of phosphoramidon and Abeta peptide binding to hECE-1 by molecular dynamics and docking studies. phosphoramidon 18-32 endothelin converting enzyme 1 Homo sapiens 62-68 24000822-2 2014 In the present study we have performed molecular dynamics (MD) simulation of crystal structure complex of hECE-1 and its inhibitor phosphoramidon with Zn ion to understand the dynamic behavior of active site residues. phosphoramidon 131-145 endothelin converting enzyme 1 Homo sapiens 106-112 24000822-4 2014 The L-leucyl-L-tryptophan moiety and N-phosphoryl moiety of phosphoramidon was found in the S1 and S2 pockets of hECE-1 respectively. phosphoramidon 60-74 endothelin converting enzyme 1 Homo sapiens 113-119 21174590-3 2011 RESULTS: In human umbilical vein endothelial cells, both phosphoramidon, an inhibitor of ECE-1, and TIMP-2 decreased VEGF-induced ET-1 production. phosphoramidon 57-71 endothelin converting enzyme 1 Homo sapiens 89-94