PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17605472-3 2007 On the basis of the recently determined crystal structures of both ACE domains, we have studied their complexes with gonadotropin-releasing hormone (GnRH), which is cleaved releasing both the protected NH2- and COOH-terminal tripeptides. tripeptides 225-236 angiotensin I converting enzyme Homo sapiens 67-70 20721338-1 2010 Tripeptides isoleucyl-prolyl-proline (IPP) and valyl-prolyl-proline (VPP) act as ACE inhibitors in vitro. tripeptides 0-11 angiotensin I converting enzyme Homo sapiens 81-84 19232015-5 2009 Activities of ACE1 and ACE2 and their inhibition by bioactive tripeptides (Ile-Pro-Pro, Val-Pro-Pro, Leu-Pro-Pro) as well as by a standard ACE-inhibitor captopril were assayed in the vitreous body, the retina and the ciliary body using fluorometric detection methods. tripeptides 62-73 angiotensin I converting enzyme Homo sapiens 14-18 19232015-5 2009 Activities of ACE1 and ACE2 and their inhibition by bioactive tripeptides (Ile-Pro-Pro, Val-Pro-Pro, Leu-Pro-Pro) as well as by a standard ACE-inhibitor captopril were assayed in the vitreous body, the retina and the ciliary body using fluorometric detection methods. tripeptides 62-73 angiotensin I converting enzyme Homo sapiens 14-17 19232015-9 2009 The tripeptides inhibited ACE1 at one-thousandth of the concentration needed to inhibit ACE2. tripeptides 4-15 angiotensin I converting enzyme Homo sapiens 26-30 18930012-0 2008 Angiotensin-I converting enzyme (ACE) inhibitory mechanism of tripeptides containing aromatic residues. tripeptides 62-73 angiotensin I converting enzyme Homo sapiens 0-31 18930012-0 2008 Angiotensin-I converting enzyme (ACE) inhibitory mechanism of tripeptides containing aromatic residues. tripeptides 62-73 angiotensin I converting enzyme Homo sapiens 33-36 18930012-2 2008 In this study, the function of amino acids in ACE inhibitory tripeptides was clarified. tripeptides 61-72 angiotensin I converting enzyme Homo sapiens 46-49 11999412-1 2002 Some of the food-derived tripeptides with angiotensin converting enzyme (ACE)-inhibitory activity have been reported to be hypotensive after being orally administered. tripeptides 25-36 angiotensin I converting enzyme Homo sapiens 42-71 17664851-2 2007 Both Val-Pro-Pro (VPP) and Ile-Pro-Pro (IPP), which are tripeptides derived from proteolytic hydrolysate of milk casein, inhibit angiotensin-converting enzyme (ACE), suggesting that both VPP and IPP may improve vascular endothelial function, because many ACE inhibitors are known to improve endothelial function. tripeptides 56-67 angiotensin I converting enzyme Homo sapiens 160-163 17450535-7 2007 We demonstrate the applicability of MC-ACE for the determination of the binding affinities between acid-rich diketopiperazine receptors and basic tripeptides in aqueous solution. tripeptides 146-157 angiotensin I converting enzyme Homo sapiens 39-42 11999412-1 2002 Some of the food-derived tripeptides with angiotensin converting enzyme (ACE)-inhibitory activity have been reported to be hypotensive after being orally administered. tripeptides 25-36 angiotensin I converting enzyme Homo sapiens 73-76 2175927-5 1990 Synthetic acylated tripeptides such as radiolabelled hippuryl-histidyl-leucine and hippuryl-glycyl-glycine have been found to be the most suitable substrates for determining the activity of ACE with radiochemical assays. tripeptides 19-30 angiotensin I converting enzyme Homo sapiens 190-193 2983326-0 1985 Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. tripeptides 95-106 angiotensin I converting enzyme Homo sapiens 24-55 34865771-6 2021 In this context, this work presents a top-down, computer-assisted and hypothesis-driven identification of potent angiotensin I converting enzyme inhibitory tripeptides, as a proof of principle. tripeptides 156-167 angiotensin I converting enzyme Homo sapiens 113-144 34136162-0 2021 Investigation on the characteristics and mechanisms of ACE inhibitory peptides by a thorough analysis of all 8000 tripeptides via binding free energy calculation. tripeptides 114-125 angiotensin I converting enzyme Homo sapiens 55-58 34136162-3 2021 In this study, novel energy calculation and experimentation were combined to elucidate the characteristics and mechanisms of ACE inhibitory tripeptides. tripeptides 140-151 angiotensin I converting enzyme Homo sapiens 125-128 34136162-4 2021 ACE inhibitory activity of all 8,000 tripeptides was investigated by in silico experiments. tripeptides 37-48 angiotensin I converting enzyme Homo sapiens 0-3 34136162-7 2021 By binding free energy analysis of nine representative tripeptides via MM/GBSA, electrostatic energy was found to be the leading energy that contributed to the binding of ACE with its high affinity tripeptides. tripeptides 55-66 angiotensin I converting enzyme Homo sapiens 171-174 34136162-7 2021 By binding free energy analysis of nine representative tripeptides via MM/GBSA, electrostatic energy was found to be the leading energy that contributed to the binding of ACE with its high affinity tripeptides. tripeptides 198-209 angiotensin I converting enzyme Homo sapiens 171-174 34136162-9 2021 Therefore, for tripeptides, their binding pockets in ACE were redefined. tripeptides 15-26 angiotensin I converting enzyme Homo sapiens 53-56 34136162-10 2021 In conclusion, the characteristics of ACE inhibitory peptides were more deeply illustrated by the thorough analysis of all tripeptides. tripeptides 123-134 angiotensin I converting enzyme Homo sapiens 38-41 2485059-4 1987 These and more recently developed ACE inhibitors can be classified according to their structural analogy to dipeptides or tripeptides and according to the nature of their zinc-binding ligands, such as sulfhydryl, ketone, carboxylate, or hydroxyphosphinyl, that contribute greatly to their binding to ACE. tripeptides 122-133 angiotensin I converting enzyme Homo sapiens 34-37 6274413-5 1981 These data indicate that kininase II can release C-terminal tripeptides of substrates having a proline residue in the penultimate position such as des-Arg9-bradykinin and its analogues, and that this enzyme is able not only to act as a dipeptidyl carboxypeptidase but also acts as a tripeptidyl carboxy-peptidase. tripeptides 60-71 angiotensin I converting enzyme Homo sapiens 25-36 6182819-5 1982 Estimation of ACE has greatly benefitted from the use of synthetic tripeptides. tripeptides 67-78 angiotensin I converting enzyme Homo sapiens 14-17 30347317-4 2018 In this work, an 8000 possible tripeptides library was constructed to predict the potential ACE inhibitory peptides by using in silico tools. tripeptides 31-42 angiotensin I converting enzyme Homo sapiens 92-95 31758024-0 2019 Novel ACE inhibitory tripeptides from ovotransferrin using bioinformatics and peptidomics approaches. tripeptides 21-32 angiotensin I converting enzyme Homo sapiens 6-9 31758024-4 2019 Subsequently, in vitro ACE inhibitory activity of potential tripeptides was conducted following the peptide score, toxicity, and water solubility prediction. tripeptides 60-71 angiotensin I converting enzyme Homo sapiens 23-26 31758024-5 2019 Both pharmacophore study and flexible docking were applied to analyze ACE inhibition mechanism of tripeptides. tripeptides 98-109 angiotensin I converting enzyme Homo sapiens 70-73 30347317-6 2018 The first 662 high-ranking tripeptides by ChemScore were chosen to create association rules of tripeptides-ACE complexes. tripeptides 27-38 angiotensin I converting enzyme Homo sapiens 107-110 30347317-6 2018 The first 662 high-ranking tripeptides by ChemScore were chosen to create association rules of tripeptides-ACE complexes. tripeptides 95-106 angiotensin I converting enzyme Homo sapiens 107-110 30347317-8 2018 The association rules (confident values over 90%) illustrated that hydrophobic factor has been displayed as main components in the ACE tripeptides inhibitor from four factors in equation, hydrophobic, aromatic, polar, charged. tripeptides 135-146 angiotensin I converting enzyme Homo sapiens 131-134 22835627-3 2012 The ACE inhibitory tripeptides LKP and IKP differ from each other by one amino acid but their inhibitory potencies for ACE differ significantly. tripeptides 19-30 angiotensin I converting enzyme Homo sapiens 4-7 29086555-4 2017 Moreover, two tripeptides among the chosen six peptides were selected for ACE-I inhibition mechanism analysis which based on Lineweaver-Burk plots indicated that they behave as competitive ACE-I inhibitors. tripeptides 14-25 angiotensin I converting enzyme Homo sapiens 74-77 29086555-4 2017 Moreover, two tripeptides among the chosen six peptides were selected for ACE-I inhibition mechanism analysis which based on Lineweaver-Burk plots indicated that they behave as competitive ACE-I inhibitors. tripeptides 14-25 angiotensin I converting enzyme Homo sapiens 189-192 28452129-3 2017 According to the established models, four novel potent ACE-inhibitory tripeptides GEF, VEF, VRF, and VKF were synthesized. tripeptides 70-81 angiotensin I converting enzyme Homo sapiens 55-58 25181455-2 2014 This study was conducted to identify the most potent ACE-inhibitory tripeptides with a proline C-terminus, using a novel three-step (tautomerization-docking-ADME simulation) virtual screening process and in vitro assays. tripeptides 68-79 angiotensin I converting enzyme Homo sapiens 53-56 25181455-4 2014 ACE inhibition activity for 14 of the 16 tripeptides was reported for the first time. tripeptides 41-52 angiotensin I converting enzyme Homo sapiens 0-3 24596454-0 2014 Does the cis/trans configuration of peptide bonds in bioactive tripeptides play a role in ACE-1 enzyme inhibition? tripeptides 63-74 angiotensin I converting enzyme Homo sapiens 90-95 22918858-9 2012 Thus the inhibition of ACE-1 remains the most plausible mechanism of the antihypertensive effects of the tripeptides. tripeptides 105-116 angiotensin I converting enzyme Homo sapiens 23-28 22835627-3 2012 The ACE inhibitory tripeptides LKP and IKP differ from each other by one amino acid but their inhibitory potencies for ACE differ significantly. tripeptides 19-30 angiotensin I converting enzyme Homo sapiens 119-122 22835627-7 2012 This work presents the molecular mechanism of the interactions between the inhibitory tripeptides and ACE, and deciphers the structural basis for the high affinity LKP inhibition of ACE. tripeptides 86-97 angiotensin I converting enzyme Homo sapiens 102-105 22835627-7 2012 This work presents the molecular mechanism of the interactions between the inhibitory tripeptides and ACE, and deciphers the structural basis for the high affinity LKP inhibition of ACE. tripeptides 86-97 angiotensin I converting enzyme Homo sapiens 182-185 21736845-1 2011 Milk casein-derived angiotensin-converting enzyme (ACE)-inhibitory tripeptides isoleucine-proline-proline (Ile-Pro-Pro) and valine-proline-proline (Val-Pro-Pro) have been shown to have antihypertensive effects in human subjects and to attenuate the development of hypertension in experimental models. tripeptides 67-78 angiotensin I converting enzyme Homo sapiens 20-49 21736845-1 2011 Milk casein-derived angiotensin-converting enzyme (ACE)-inhibitory tripeptides isoleucine-proline-proline (Ile-Pro-Pro) and valine-proline-proline (Val-Pro-Pro) have been shown to have antihypertensive effects in human subjects and to attenuate the development of hypertension in experimental models. tripeptides 67-78 angiotensin I converting enzyme Homo sapiens 51-54 21221598-1 2011 Milk casein-derived tripeptides, valyl prolyl proline (VPP), and isoleucyl prolyl proline (IPP) inhibit angiotensin-converting enzyme (ACE) and both fermented milk and proteolytic hydrolysates of milk casein containing these peptides exert blood pressure-lowering effects in animals and humans. tripeptides 20-31 angiotensin I converting enzyme Homo sapiens 104-133 21221598-1 2011 Milk casein-derived tripeptides, valyl prolyl proline (VPP), and isoleucyl prolyl proline (IPP) inhibit angiotensin-converting enzyme (ACE) and both fermented milk and proteolytic hydrolysates of milk casein containing these peptides exert blood pressure-lowering effects in animals and humans. tripeptides 20-31 angiotensin I converting enzyme Homo sapiens 135-138