PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22467199-8 2012 In this hydrolysate we identified the well-known potent ACE-inhibitor and antihypertensive tripeptide Ile-Pro-Pro (IPP) and another novel octapeptide Gln-Asp-Lys-Thr-Glu-Ile-Pro-Thr (QDKTEIPT). isoleucyl-prolyl-proline 102-113 angiotensin I converting enzyme Homo sapiens 56-59 32448573-9 2020 The known ACE inhibitors Val-Pro-Pro and Ile-Pro-Pro showed similar ACE inhibition to previously published results, while also inducing the production of the regulatory cytokine IL-10 by monocytes in the presence and absence of a proinflammatory stimulant. isoleucyl-prolyl-proline 41-52 angiotensin I converting enzyme Homo sapiens 10-13 32448573-9 2020 The known ACE inhibitors Val-Pro-Pro and Ile-Pro-Pro showed similar ACE inhibition to previously published results, while also inducing the production of the regulatory cytokine IL-10 by monocytes in the presence and absence of a proinflammatory stimulant. isoleucyl-prolyl-proline 41-52 angiotensin I converting enzyme Homo sapiens 68-71 33337010-1 2019 Ile-Pro-Pro and Val-Pro-Pro are two most well-known food-derived bioactive peptides, initially identified as inhibitors of angiotensin I-converting enzyme (ACE) from a sample of sour milk. isoleucyl-prolyl-proline 0-11 angiotensin I converting enzyme Homo sapiens 123-154 33337010-1 2019 Ile-Pro-Pro and Val-Pro-Pro are two most well-known food-derived bioactive peptides, initially identified as inhibitors of angiotensin I-converting enzyme (ACE) from a sample of sour milk. isoleucyl-prolyl-proline 0-11 angiotensin I converting enzyme Homo sapiens 156-159 22467199-8 2012 In this hydrolysate we identified the well-known potent ACE-inhibitor and antihypertensive tripeptide Ile-Pro-Pro (IPP) and another novel octapeptide Gln-Asp-Lys-Thr-Glu-Ile-Pro-Thr (QDKTEIPT). isoleucyl-prolyl-proline 115-118 angiotensin I converting enzyme Homo sapiens 56-59 21779574-6 2011 In particular, Ile-Pro-Pro and Val-Pro-Pro are fore runners in ACE inhibition, and have been incorporated into commercial products. isoleucyl-prolyl-proline 15-26 angiotensin I converting enzyme Homo sapiens 63-66 21864683-5 2011 Mutant recombinant ACE constructions revealed that affinity gap between BK and Met-Lys-BK-Ser-Ser is larger for the N-terminal catalytic site than for the C-terminal one, based on competition for the substrate Abz-Phe-Arg-Lys(Dnp)-Pro-OH in an enzymatic assay. isoleucyl-prolyl-proline 231-237 angiotensin I converting enzyme Homo sapiens 19-22 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. isoleucyl-prolyl-proline 107-118 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. isoleucyl-prolyl-proline 107-118 angiotensin I converting enzyme Homo sapiens 51-54 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. isoleucyl-prolyl-proline 27-38 angiotensin I converting enzyme Homo sapiens 160-163 20721338-1 2010 Tripeptides isoleucyl-prolyl-proline (IPP) and valyl-prolyl-proline (VPP) act as ACE inhibitors in vitro. isoleucyl-prolyl-proline 38-41 angiotensin I converting enzyme Homo sapiens 81-84 19619856-5 2009 The levels of ACE inhibitory peptides, Val-Pro-Pro and Ile-Pro-Pro, were increased in the casein miso paste during the fermentation. isoleucyl-prolyl-proline 55-66 angiotensin I converting enzyme Homo sapiens 14-17 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. isoleucyl-prolyl-proline 75-86 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. isoleucyl-prolyl-proline 75-86 angiotensin I converting enzyme Homo sapiens 14-17 20486467-6 2010 It was shown, apparently for the first time, that the inhibitory effects of Ile-Pro-Pro, Val-Pro-Pro and Leu-Pro-Pro on ACE1 at micromolar concentrations are competitive in nature. isoleucyl-prolyl-proline 76-87 angiotensin I converting enzyme Homo sapiens 120-124 20486467-10 2010 The findings support the hypothesis that Ile-Pro-Pro, Val-Pro-Pro and Leu-Pro-Pro act favourably on blood pressure mainly by selective inhibition of ACE1. isoleucyl-prolyl-proline 41-52 angiotensin I converting enzyme Homo sapiens 149-153 19506528-1 2009 BACKGROUND: The potential blood pressure lowering effect of fermented milk may involve inhibition of angiotensin-converting enzyme (ACE) by dairy lactotripeptides generated during milk fermentation, such as isoleucine-proline-proline (IPP) and valine-proline-proline (VPP). isoleucyl-prolyl-proline 235-238 angiotensin I converting enzyme Homo sapiens 101-130 19506528-1 2009 BACKGROUND: The potential blood pressure lowering effect of fermented milk may involve inhibition of angiotensin-converting enzyme (ACE) by dairy lactotripeptides generated during milk fermentation, such as isoleucine-proline-proline (IPP) and valine-proline-proline (VPP). isoleucyl-prolyl-proline 235-238 angiotensin I converting enzyme Homo sapiens 132-135 18490081-10 2008 The results of this study demonstrate that the ACE inhibitory peptides Ile-Pro-Pro and Val-Pro-Pro are absorbed partially undegraded. isoleucyl-prolyl-proline 71-82 angiotensin I converting enzyme Homo sapiens 47-50 19109662-10 2008 A high proportion of the reported trials was carried out using the well-known ACE inhibiting tripeptides - Valine-Proline-Proline (VPP) and Isoleucine-Proline-Proline (IPP). isoleucyl-prolyl-proline 168-171 angiotensin I converting enzyme Homo sapiens 78-81 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. isoleucyl-prolyl-proline 27-38 angiotensin I converting enzyme Homo sapiens 255-258 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. isoleucyl-prolyl-proline 40-43 angiotensin I converting enzyme Homo sapiens 160-163 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. isoleucyl-prolyl-proline 40-43 angiotensin I converting enzyme Homo sapiens 255-258