PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19895477-0 2009 Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity. Dipeptides 37-46 angiotensin I converting enzyme Homo sapiens 100-103 20929253-6 2010 The three dipeptides showed weak inhibitory properties toward CaMPDE but strong inhibitions (IC50 values <25 mM) of ACE and renin. Dipeptides 10-20 angiotensin I converting enzyme Homo sapiens 119-122 19895477-15 2009 However, postabsorptive ACE inhibitory activities of dipeptides in vivo are most likely limited due to the very low intestinal permeability of dipeptides. Dipeptides 53-63 angiotensin I converting enzyme Homo sapiens 24-27 19895477-15 2009 However, postabsorptive ACE inhibitory activities of dipeptides in vivo are most likely limited due to the very low intestinal permeability of dipeptides. Dipeptides 143-153 angiotensin I converting enzyme Homo sapiens 24-27 19895477-3 2009 The purpose of this study was to identify descriptors of intestinal stability, permeability, and ACE inhibitory activity of dipeptides. Dipeptides 124-134 angiotensin I converting enzyme Homo sapiens 97-100 19895477-11 2009 2D-fingerprint models were identified describing ACE inhibitory activity of dipeptides. Dipeptides 76-86 angiotensin I converting enzyme Homo sapiens 49-52 19267429-3 2009 We studied the cis-trans isomerization of the proline dipeptide (Ace-Pro-NMe) in explicit water by molecular dynamics simulations using a combined potential derived from ab initio quantum mechanics and empirical molecular mechanics. Dipeptides 54-63 angiotensin I converting enzyme Homo sapiens 65-68 16165357-2 2005 This compound was conjugated to H2N-Ala-Pro dipeptide to give a prodrug to be activated by intestinal ACE and to be used in the treatment of different forms of colon cancer. Dipeptides 44-53 angiotensin I converting enzyme Homo sapiens 102-105 17485083-1 2007 The angiotensin I-converting enzyme (ACE) converts the decapeptide angiotensin I (Ang I) into angiotensin II by releasing the C-terminal dipeptide. Dipeptides 137-146 angiotensin I converting enzyme Homo sapiens 4-35 17485083-1 2007 The angiotensin I-converting enzyme (ACE) converts the decapeptide angiotensin I (Ang I) into angiotensin II by releasing the C-terminal dipeptide. Dipeptides 137-146 angiotensin I converting enzyme Homo sapiens 37-40 16857833-0 2006 The ACE inhibitory dipeptide Met-Tyr diminishes free radical formation in human endothelial cells via induction of heme oxygenase-1 and ferritin. Dipeptides 19-28 angiotensin I converting enzyme Homo sapiens 4-7 16857833-2 2006 Methionine-tyrosine (Met-Tyr) is an ACE inhibitory dipeptide derived from sardine muscle. Dipeptides 51-60 angiotensin I converting enzyme Homo sapiens 36-39 19273273-2 2009 A dipeptide YY derived from RJ proteins is known to inhibit angiotensin converting enzyme (ACE) activity. Dipeptides 2-11 angiotensin I converting enzyme Homo sapiens 60-89 19273273-2 2009 A dipeptide YY derived from RJ proteins is known to inhibit angiotensin converting enzyme (ACE) activity. Dipeptides 2-11 angiotensin I converting enzyme Homo sapiens 91-94 18669035-0 2008 Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides. Dipeptides 101-111 angiotensin I converting enzyme Homo sapiens 58-89 18669035-1 2008 The dipeptides Ala-Trp, Val-Phe, and Val-Tyr inhibit the angiotensin-I-converting enzyme. Dipeptides 4-14 angiotensin I converting enzyme Homo sapiens 57-88 18669035-3 2008 The angiotensin-I-converting enzyme inhibitory potency of these synthetic dipeptides was quantified using a spectrophotometric assay. Dipeptides 74-84 angiotensin I converting enzyme Homo sapiens 4-35 18027352-0 2007 Modeling dipeptides as ACE inhibitors and bitter-tasting compounds by means of E-state structure-information representation. Dipeptides 9-19 angiotensin I converting enzyme Homo sapiens 23-26 17879071-12 2007 Several quantitative structure activity relationship (QSAR) models were developed for various oligopeptides and polypeptides including 58 dipeptides and 31 pentapeptides with angiotensin converting enzyme (ACE) inhibition by multiple linear regression (MLR) method. Dipeptides 138-148 angiotensin I converting enzyme Homo sapiens 206-209 17654623-8 2007 In addition, the relationship of ACE-inhibiting activities with bitter-tasting thresholds has been investigated by applying the above-constructed models to predictions on 400 theoretically possible dipeptides. Dipeptides 198-208 angiotensin I converting enzyme Homo sapiens 33-36 17605472-6 2007 In support of this, the protected NH2-terminal dipeptide of GnRH exhibits stronger interactions than the protected COOH-terminal dipeptide with the N-domain of ACE. Dipeptides 47-56 angiotensin I converting enzyme Homo sapiens 160-163 17605472-6 2007 In support of this, the protected NH2-terminal dipeptide of GnRH exhibits stronger interactions than the protected COOH-terminal dipeptide with the N-domain of ACE. Dipeptides 129-138 angiotensin I converting enzyme Homo sapiens 160-163 17157962-1 2007 Insect angiotensin converting enzyme (ACE) is a zinc metallopeptidase capable of inactivating a variety of small to medium size peptide hormones by cleavage of C-terminal dipeptides and dipeptideamides. Dipeptides 171-181 angiotensin I converting enzyme Homo sapiens 7-36 17157962-1 2007 Insect angiotensin converting enzyme (ACE) is a zinc metallopeptidase capable of inactivating a variety of small to medium size peptide hormones by cleavage of C-terminal dipeptides and dipeptideamides. Dipeptides 171-181 angiotensin I converting enzyme Homo sapiens 38-41 14692507-3 2003 In vitro, 8 of 9 dipeptides were found to be competitive inhibitors of ACE. Dipeptides 17-27 angiotensin I converting enzyme Homo sapiens 71-74 15134871-7 2004 HPLC analysis showed that ACE cleaved SP at Phe(8)-Gly(9) and Gly(9)-Leu(10) to release C-terminal tri- and dipeptide (ratio = 4:1). Dipeptides 108-117 angiotensin I converting enzyme Homo sapiens 26-29 15134871-9 2004 ACE released only dipeptide from SP free acid. Dipeptides 18-27 angiotensin I converting enzyme Homo sapiens 0-3 12086537-9 2002 For 58 dipeptides inhibiting angiotensin-converting enzyme (ACE), a 5-variable QSAR model (M2) between the pIC(50) of peptides and 5-descriptor subset is derived. Dipeptides 7-17 angiotensin I converting enzyme Homo sapiens 29-58 12914653-1 2003 SUMMARY: Angiotensin-I-converting enzyme (ACE) is a monomeric, membrane-bound, zinc- and chloride-dependent peptidyl dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the octapeptide angiotensin II, by removing a carboxy-terminal dipeptide. Dipeptides 258-267 angiotensin I converting enzyme Homo sapiens 9-40 12914653-1 2003 SUMMARY: Angiotensin-I-converting enzyme (ACE) is a monomeric, membrane-bound, zinc- and chloride-dependent peptidyl dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the octapeptide angiotensin II, by removing a carboxy-terminal dipeptide. Dipeptides 258-267 angiotensin I converting enzyme Homo sapiens 42-45 12540854-1 2003 Angiotensin-converting enzyme (ACE) has a critical role in cardiovascular function by cleaving the carboxy terminal His-Leu dipeptide from angiotensin I to produce a potent vasopressor octapeptide, angiotensin II. Dipeptides 124-133 angiotensin I converting enzyme Homo sapiens 0-29 12540854-1 2003 Angiotensin-converting enzyme (ACE) has a critical role in cardiovascular function by cleaving the carboxy terminal His-Leu dipeptide from angiotensin I to produce a potent vasopressor octapeptide, angiotensin II. Dipeptides 124-133 angiotensin I converting enzyme Homo sapiens 31-34 12383874-6 2002 Both insect and human ACE hydrolyze Neb-ODAIF by sequentially cleaving off two C-terminal dipeptides. Dipeptides 90-100 angiotensin I converting enzyme Homo sapiens 22-25 12230125-1 2002 The change in plasma level of dipeptide, Val-Tyr (VY), with in vitro angiotensin I-converting enzyme inhibitory activity was investigated after a single oral administration of a VY-drink at doses of 0, 6 or 12 mg given to mild hypertensive subjects. Dipeptides 30-39 angiotensin I converting enzyme Homo sapiens 69-100 12086537-9 2002 For 58 dipeptides inhibiting angiotensin-converting enzyme (ACE), a 5-variable QSAR model (M2) between the pIC(50) of peptides and 5-descriptor subset is derived. Dipeptides 7-17 angiotensin I converting enzyme Homo sapiens 60-63 11885929-2 2001 Further studies have indicated that a more active form of the peptide is generated by removal of the C-terminal dipeptide by angiotensin-I-converting enzyme (ACE), and additional detailed studies have shown that the actual immunodominant peptide is a decamer P18-I10 (RGPGRAFVTI) (Kozlowski et al., 1993). Dipeptides 112-121 angiotensin I converting enzyme Homo sapiens 125-156 11277718-5 2001 The MEDV-13 is used to study the QSAR of the corticosteroid-binding globulin (CBG) binding affinity of the steroids and the activity inhibiting angiotensin-converting enzyme (ACE) of dipeptides, and resulting models have a comparable quality to the current three-dimensional (3D) methods such as CoMFA though the MEDV-13 is a descriptor based on two-dimensional topological information. Dipeptides 183-193 angiotensin I converting enzyme Homo sapiens 144-173 11277718-5 2001 The MEDV-13 is used to study the QSAR of the corticosteroid-binding globulin (CBG) binding affinity of the steroids and the activity inhibiting angiotensin-converting enzyme (ACE) of dipeptides, and resulting models have a comparable quality to the current three-dimensional (3D) methods such as CoMFA though the MEDV-13 is a descriptor based on two-dimensional topological information. Dipeptides 183-193 angiotensin I converting enzyme Homo sapiens 175-178 11885929-2 2001 Further studies have indicated that a more active form of the peptide is generated by removal of the C-terminal dipeptide by angiotensin-I-converting enzyme (ACE), and additional detailed studies have shown that the actual immunodominant peptide is a decamer P18-I10 (RGPGRAFVTI) (Kozlowski et al., 1993). Dipeptides 112-121 angiotensin I converting enzyme Homo sapiens 158-161 11697054-1 2001 The novel Cluj property indices are used for modeling the biological properties of dipeptides: the ACE inhibition activity of a set of 58 dipeptides and the bitter tasting activity of a set of 48 dipeptides, taken from the literature. Dipeptides 83-93 angiotensin I converting enzyme Homo sapiens 99-102 8968386-5 1996 The hematopoietic system regulatory peptide acetyl-Ser-Asp-Lys-Pro was split to two dipeptides by N-ACE, depending on the chloride concentration, 8 to 24 times faster than by germinal ACE; at 100 mM Cl-, the Kcat with N-ACE was eight times higher. Dipeptides 84-94 angiotensin I converting enzyme Homo sapiens 100-103 11163985-7 2000 A series of dipeptide-like compounds varying within specific domains were selected from a large number of commercially available ACE inhibitors and SQ-29852 analogues. Dipeptides 12-21 angiotensin I converting enzyme Homo sapiens 129-132 10336644-4 1999 ACE activity removes C-terminal dipeptides to generate the Gly-extended peptides, whereas CP hydrolysis gives rise to CCK5-GR and LH-RH-GK, both of which are susceptible to the dipeptidyl carboxypeptidase activity of ACE. Dipeptides 32-42 angiotensin I converting enzyme Homo sapiens 0-3 10919370-6 2000 The dipeptide and nonapeptide showed dose-dependent inhibition of ACE, with IC50 values of 12 and 1.7 micromol/l, respectively. Dipeptides 4-13 angiotensin I converting enzyme Homo sapiens 66-69 8737991-3 1996 Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an IC50 value of 122.1 microM. Dipeptides 8-18 angiotensin I converting enzyme Homo sapiens 34-37 8558518-2 1996 Incorporation of bicyclic and substituted monocyclic azepinones as dipeptide surrogates in angiotensin-converting enzyme/neutral endopeptidase inhibitors. Dipeptides 67-76 angiotensin I converting enzyme Homo sapiens 91-120 8558518-3 1996 A series of substituted monocyclic and bicyclic azepinones were incorporated as dipeptide surrogates in mercaptoacetyl dipeptides with the desire to generate a single compound which would potently inhibit both angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP). Dipeptides 80-89 angiotensin I converting enzyme Homo sapiens 210-239 8360888-0 1993 Application of a conformationally restricted Phe-Leu dipeptide mimetic to the design of a combined inhibitor of angiotensin I-converting enzyme and neutral endopeptidase 24.11. Dipeptides 53-62 angiotensin I converting enzyme Homo sapiens 112-143 7780654-15 1995 The effects of enalapril maleate and captopril on [14C]-Gly-Sar transport and pHi suggest that these two ACE inhibitors share the H(+)-coupled mechanism involved in dipeptide transport. Dipeptides 165-174 angiotensin I converting enzyme Homo sapiens 105-108 8052664-8 1994 In agreement with the results reported with recombinant variants of ACE, the ileal enzyme is less Cl(-)-dependent than somatic ACE; release of the C-terminal dipeptide from a peptide substrate was optimal in only 10 mM Cl-. Dipeptides 158-167 angiotensin I converting enzyme Homo sapiens 68-71 8052664-8 1994 In agreement with the results reported with recombinant variants of ACE, the ileal enzyme is less Cl(-)-dependent than somatic ACE; release of the C-terminal dipeptide from a peptide substrate was optimal in only 10 mM Cl-. Dipeptides 158-167 angiotensin I converting enzyme Homo sapiens 127-130 2175927-3 1990 The ACE is a glycoprotein with a molecular weight of 150,000 daltons and it cleaves C-terminal dipeptides of several oligo-peptides, including angiotensin I and bradykinin. Dipeptides 95-105 angiotensin I converting enzyme Homo sapiens 4-7 1316850-1 1992 Angiotensin-I-converting enzyme (ACE) is a peptidyl-dipeptide hydrolase which splits off the dipeptide His-Leu from the decapeptide angiotensin I and thus converts it to angiotensin II. Dipeptides 52-61 angiotensin I converting enzyme Homo sapiens 0-31 1316850-1 1992 Angiotensin-I-converting enzyme (ACE) is a peptidyl-dipeptide hydrolase which splits off the dipeptide His-Leu from the decapeptide angiotensin I and thus converts it to angiotensin II. Dipeptides 52-61 angiotensin I converting enzyme Homo sapiens 33-36 1697356-5 1990 Kininase II enzymes release the C-terminal dipeptide Phe-Arg; angiotensin I-converting enzyme and neutral endopeptidase 24.11 (enkephalinase) are prominent members of this subgroup of proteins. Dipeptides 43-52 angiotensin I converting enzyme Homo sapiens 0-11 2162675-1 1990 The synthesis of a series of novel, potent angiotensin converting enzyme (ACE) inhibitors containing 1(S)-carboxy-omega-(4-piperidyl)alkyl group at the N-terminal of the dipeptide is described. Dipeptides 170-179 angiotensin I converting enzyme Homo sapiens 43-72 2162675-1 1990 The synthesis of a series of novel, potent angiotensin converting enzyme (ACE) inhibitors containing 1(S)-carboxy-omega-(4-piperidyl)alkyl group at the N-terminal of the dipeptide is described. Dipeptides 170-179 angiotensin I converting enzyme Homo sapiens 74-77 34060658-0 2021 Study on the domain selective inhibition of angiotensin-converting enzyme (ACE) by food-derived tyrosine-containing dipeptides. Dipeptides 116-126 angiotensin I converting enzyme Homo sapiens 44-73 34060658-0 2021 Study on the domain selective inhibition of angiotensin-converting enzyme (ACE) by food-derived tyrosine-containing dipeptides. Dipeptides 116-126 angiotensin I converting enzyme Homo sapiens 75-78 34060658-1 2021 In this article, the selective inhibition of several tyrosine-containing dipeptides on N and C domain of ACE (angiotensin-converting enzyme) was studied, and the interaction mode of ACE and inhibitors was simulated by molecular docking. Dipeptides 73-83 angiotensin I converting enzyme Homo sapiens 105-108 34060658-1 2021 In this article, the selective inhibition of several tyrosine-containing dipeptides on N and C domain of ACE (angiotensin-converting enzyme) was studied, and the interaction mode of ACE and inhibitors was simulated by molecular docking. Dipeptides 73-83 angiotensin I converting enzyme Homo sapiens 110-139 34060658-3 2021 The results showed that the food-derived dipeptides AY (Ala-Tyr), LY (Leu-Tyr), and IY (Ile-Tyr) containing tyrosine at the C-terminal were favorable structures for selective inhibition of ACE C-domain. Dipeptides 41-51 angiotensin I converting enzyme Homo sapiens 189-192 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. Dipeptides 108-118 angiotensin I converting enzyme Homo sapiens 34-37 2539165-3 1989 Angiotensin-converting enzyme was an effective kininase in mixtures with carboxypeptidase N at physiologic concentration and digested bradykinin to the dipeptides Phe- Arg and Ser-Pro plus the pentapeptide Arg-Pro-Pro-Gly-Phe. Dipeptides 152-162 angiotensin I converting enzyme Homo sapiens 0-29 2983326-1 1985 Angiotensin I converting enzyme (ACE; kininase II; peptidyldipeptide hydrolase, EC 3.4.15.1) cleaves COOH-terminal dipeptides from active peptides containing a free COOH terminus. Dipeptides 115-125 angiotensin I converting enzyme Homo sapiens 0-31 2983326-5 1985 ACE also released the COOH-terminal tripeptide, Arg-Pro-Gly-NH2, and then sequentially the dipeptides Gly-Leu and Ser-Try, leaving less than Glu-His-Trp intact. Dipeptides 91-101 angiotensin I converting enzyme Homo sapiens 0-3 2983326-1 1985 Angiotensin I converting enzyme (ACE; kininase II; peptidyldipeptide hydrolase, EC 3.4.15.1) cleaves COOH-terminal dipeptides from active peptides containing a free COOH terminus. Dipeptides 115-125 angiotensin I converting enzyme Homo sapiens 33-36 2983326-1 1985 Angiotensin I converting enzyme (ACE; kininase II; peptidyldipeptide hydrolase, EC 3.4.15.1) cleaves COOH-terminal dipeptides from active peptides containing a free COOH terminus. Dipeptides 115-125 angiotensin I converting enzyme Homo sapiens 38-49 6097262-2 1984 A second enzyme, angiotensin converting enzyme (CE), releases the strong vasoconstricting octapeptide ANG II via degradation of a C-terminal dipeptide. Dipeptides 141-150 angiotensin I converting enzyme Homo sapiens 17-46 2417254-3 1985 ACE cleaved SP at Phe8-Gly9 and Gly9-Leu10 to release C-terminal tri- and dipeptide (ratio = 4:1). Dipeptides 74-83 angiotensin I converting enzyme Homo sapiens 0-3 6095846-3 1984 Significant increases in ACE inhibitory activity were observed by introduction of conformation constraint into acyclic acyl dipeptides, thus further defining the three dimensional structure of the ACE active site. Dipeptides 124-134 angiotensin I converting enzyme Homo sapiens 25-28 6095846-3 1984 Significant increases in ACE inhibitory activity were observed by introduction of conformation constraint into acyclic acyl dipeptides, thus further defining the three dimensional structure of the ACE active site. Dipeptides 124-134 angiotensin I converting enzyme Homo sapiens 197-200 6208535-5 1984 HPLC analysis showed that ACE cleaved SP at Phe8-Gly9 and Gly9-Leu10 to release C-terminal tri- and dipeptide (ratio = 4:1). Dipeptides 100-109 angiotensin I converting enzyme Homo sapiens 26-29 6180780-3 1982 The C-terminal heptapeptide and the dipeptide Arg-Pro negligibly inhibited ACE activity. Dipeptides 36-45 angiotensin I converting enzyme Homo sapiens 75-78 6301459-1 1983 Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. Dipeptides 69-79 angiotensin I converting enzyme Homo sapiens 17-46 164083-3 1975 In normal human blood serum the carboxycathepsin activity varied from 7.5 to 18 nmoles of the dipeptide, liberated per mg of protein per hr. Dipeptides 94-103 angiotensin I converting enzyme Homo sapiens 32-48 6255989-1 1980 A method for sequence analysis of polypeptides starting at the carboxyl terminus is described that utilizes degradation of the polypeptide into dipeptides with angiotensin I converting enzyme. Dipeptides 144-154 angiotensin I converting enzyme Homo sapiens 160-191 30857128-0 2019 Structure-Activity Prediction of ACE Inhibitory/Bitter Dipeptides-A Chemometric Approach Based on Stepwise Regression. Dipeptides 55-65 angiotensin I converting enzyme Homo sapiens 33-36 31655961-0 2020 Insight into structural requirements of ACE inhibitory dipeptides: QSAR and molecular docking studies. Dipeptides 55-65 angiotensin I converting enzyme Homo sapiens 40-43 31655961-8 2020 Moreover, molecular docking studies were employed to predict the binding mode between dipeptides and ACE receptor. Dipeptides 86-96 angiotensin I converting enzyme Homo sapiens 101-104 32915574-6 2020 14 new dipeptides predicted to lower blood pressure by inhibiting ACE were selected. Dipeptides 7-17 angiotensin I converting enzyme Homo sapiens 66-69 32915574-7 2020 Molecular docking indicated that these dipeptides formed hydrogen bonds with ACE. Dipeptides 39-49 angiotensin I converting enzyme Homo sapiens 77-80 31889785-4 2019 GO analysis showed that the main biological processes involved in ACE include: the process of transforming angiotensinogen into mature angiotensin; angiotensin"s mediation of the brain"s response to alcohol consumption and thirst control; any chemical reaction involving the regulation of angiotensin; and the process of catalyzing the release of a C-terminal dipeptide from a polypeptide chain. Dipeptides 360-369 angiotensin I converting enzyme Homo sapiens 66-69 31028832-1 2019 Sequences of one-symbol abbreviations of amino acids are applied as the basis to build up predictive model of Angiotensin converting enzyme (ACE) inhibitory activity of dipeptides and antibacterial activity of group of polypeptides. Dipeptides 169-179 angiotensin I converting enzyme Homo sapiens 110-139 31028832-1 2019 Sequences of one-symbol abbreviations of amino acids are applied as the basis to build up predictive model of Angiotensin converting enzyme (ACE) inhibitory activity of dipeptides and antibacterial activity of group of polypeptides. Dipeptides 169-179 angiotensin I converting enzyme Homo sapiens 141-144 31028832-5 2019 The obtained results confirm that IIC can be applied to improve predictive potential of models for ACE inhibitor activity of dipeptides and antibacterial activity of polypeptides. Dipeptides 125-135 angiotensin I converting enzyme Homo sapiens 99-102 30857128-1 2019 Forward and backward stepwise regression (FR and BR, respectively) was applied for the structure-bioactivity prediction of angiotensin converting enzyme (ACE)-inhibitory/bitter-tasting dipeptides. Dipeptides 185-195 angiotensin I converting enzyme Homo sapiens 123-152 30857128-1 2019 Forward and backward stepwise regression (FR and BR, respectively) was applied for the structure-bioactivity prediction of angiotensin converting enzyme (ACE)-inhibitory/bitter-tasting dipeptides. Dipeptides 185-195 angiotensin I converting enzyme Homo sapiens 154-157 28626916-3 2017 We showed that ACE could hydrolyse gastrin, a neuropeptide from the gastrointestinal tract, releasing the C-terminal amidated dipeptide H-Asp-Phe-NH2 . Dipeptides 126-135 angiotensin I converting enzyme Homo sapiens 15-18 29303958-7 2018 The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE. Dipeptides 28-37 angiotensin I converting enzyme Homo sapiens 190-193 28984136-0 2017 New Quantitative Structure-Activity Relationship Model for Angiotensin-Converting Enzyme Inhibitory Dipeptides Based on Integrated Descriptors. Dipeptides 100-110 angiotensin I converting enzyme Homo sapiens 59-88 28984136-2 2017 In this paper, a benchmark data set containing 141 unique ACE inhibitory dipeptides was constructed through database mining, and a quantitative structure-activity relationships (QSAR) study was carried out to predict half-inhibitory concentration (IC50) of ACE activity. Dipeptides 73-83 angiotensin I converting enzyme Homo sapiens 58-61 28984136-2 2017 In this paper, a benchmark data set containing 141 unique ACE inhibitory dipeptides was constructed through database mining, and a quantitative structure-activity relationships (QSAR) study was carried out to predict half-inhibitory concentration (IC50) of ACE activity. Dipeptides 73-83 angiotensin I converting enzyme Homo sapiens 257-260 27535479-2 2016 A comprehensive conformational analysis of dipeptide model Ace-Gly-NMe (1) has been carried out by using a combination of theoretical calculations and experimental ((1) H and (13) C NMR and NOESY) spectroscopic measurements to assess the relevance of cis-peptide conformers. Dipeptides 43-52 angiotensin I converting enzyme Homo sapiens 59-62 29173648-8 2017 Furthermore, predicted values of ACE inhibitory activity of dipeptides obtained by peptide cutter are relatively high, which recommend them for application as functional food supplements and natural alternatives to ACE inhibitory drugs. Dipeptides 60-70 angiotensin I converting enzyme Homo sapiens 33-36 29173648-8 2017 Furthermore, predicted values of ACE inhibitory activity of dipeptides obtained by peptide cutter are relatively high, which recommend them for application as functional food supplements and natural alternatives to ACE inhibitory drugs. Dipeptides 60-70 angiotensin I converting enzyme Homo sapiens 215-218 20941517-2 2011 The descriptors were then applied to study on quantitative structure-activity relationships (QSARs) of nine peptide datasets of angiotensin-converting enzyme inhibitor (ACE-inhibitor) oligopeptides (between dipeptides and decapeptides) by using partial least square (PLS) regression. Dipeptides 207-217 angiotensin I converting enzyme Homo sapiens 169-172 27120469-9 2016 Since so far ACE activity measurement is substrate specific due to the usage of only one oligopeptide, taking several dipeptides as potential products of ACE into account may provide a broader picture of the ACE activity. Dipeptides 118-128 angiotensin I converting enzyme Homo sapiens 154-157 27120469-9 2016 Since so far ACE activity measurement is substrate specific due to the usage of only one oligopeptide, taking several dipeptides as potential products of ACE into account may provide a broader picture of the ACE activity. Dipeptides 118-128 angiotensin I converting enzyme Homo sapiens 154-157 26403559-4 2015 The high resolution crystal structures of N-domain ACE in complex with the dipeptide products of Ac-SDKP cleavage were obtained and offered a template to model the mechanism of substrate recognition of the enzyme. Dipeptides 75-84 angiotensin I converting enzyme Homo sapiens 51-54 23082758-1 2012 UNLABELLED: Human somatic angiotensin-1 converting enzyme (ACE) is a zinc-dependent exopeptidase, that catalyses the conversion of the decapeptide angiotensin I to the octapeptide angiotensin II, by removing a C-terminal dipeptide. Dipeptides 221-230 angiotensin I converting enzyme Homo sapiens 26-57 23082758-1 2012 UNLABELLED: Human somatic angiotensin-1 converting enzyme (ACE) is a zinc-dependent exopeptidase, that catalyses the conversion of the decapeptide angiotensin I to the octapeptide angiotensin II, by removing a C-terminal dipeptide. Dipeptides 221-230 angiotensin I converting enzyme Homo sapiens 59-62 27120469-2 2016 Although it is known that ACE especially cleaves COOH-terminal dipeptides from active polypeptides, the whole range of substrates and products is still unknown. Dipeptides 63-73 angiotensin I converting enzyme Homo sapiens 26-29 27120469-8 2016 Two of these resulting dipeptides, namely aspartylphenylalanine and phenylalanylserine, showed significant associations with blood pressure which qualifies them-and perhaps also the other dipeptides-as readouts of ACE-activity. Dipeptides 23-33 angiotensin I converting enzyme Homo sapiens 214-217 23871047-5 2013 As might be expected, quantitative structure-activity relationship modeling reveals a significant positive correlation between the ACE inhibition and bitterness of dipeptides, but this correlation is quite modest for tripeptides and, particularly, tetrapeptides. Dipeptides 164-174 angiotensin I converting enzyme Homo sapiens 131-134 24215325-14 2013 The pentapeptide, GPSMR, was hydrolysed after digestion and it was predicted to release a dipeptide ACE inhibitor, GP, from its precursor. Dipeptides 90-99 angiotensin I converting enzyme Homo sapiens 100-103 23030610-0 2012 Dipeptide inhibitors of thermolysin and angiotensin I-converting enzyme. Dipeptides 0-9 angiotensin I converting enzyme Homo sapiens 40-71 21186397-2 2011 ACE also cleaves the terminal dipeptide of vasodilating hormone bradykinin (a nonapeptide) to inactivate this hormone. Dipeptides 30-39 angiotensin I converting enzyme Homo sapiens 0-3