PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
33180478-0	2020	The Protective Effects of Tripeptides VPP and IPP against Small Extracellular Vesicles from Angiotensin II-Induced Vascular Smooth Muscle Cells Mediating Endothelial Dysfunction in Human Umbilical Vein Endothelial Cells.	valyl-prolyl-proline	38-41	angiotensinogen	Homo sapiens	92-106
34082361-3	2021	Val-Pro-Pro (VPP) is a milk-derived tripeptide with assumed mild inhibitory activity against angiotensin-converting enzyme (ACE).	valyl-prolyl-proline	0-11	angiotensin I converting enzyme	Homo sapiens	93-122
34082361-3	2021	Val-Pro-Pro (VPP) is a milk-derived tripeptide with assumed mild inhibitory activity against angiotensin-converting enzyme (ACE).	valyl-prolyl-proline	0-11	angiotensin I converting enzyme	Homo sapiens	124-127
34082361-3	2021	Val-Pro-Pro (VPP) is a milk-derived tripeptide with assumed mild inhibitory activity against angiotensin-converting enzyme (ACE).	valyl-prolyl-proline	13-16	angiotensin I converting enzyme	Homo sapiens	93-122
34082361-3	2021	Val-Pro-Pro (VPP) is a milk-derived tripeptide with assumed mild inhibitory activity against angiotensin-converting enzyme (ACE).	valyl-prolyl-proline	13-16	angiotensin I converting enzyme	Homo sapiens	124-127
34082361-4	2021	Computational (DFT) methods are applied on simplified models of Zn2+-HEXXH binding motif without/with bound inhibitors in order to assess the ability of two pharmaceutical drugs (Captopril and Lisinopril) and Val-Pro-Pro to coordinate with Zn2+-HEXXH binding motif of ACE.	valyl-prolyl-proline	209-220	angiotensin I converting enzyme	Homo sapiens	268-271
9001375-7	1996	These data suggest that L-valyl-L-prolyl-L-proline and L-isoleucyl-L-prolyl-L-proline in the Calpis sour milk are absorbed directly without being decomposed by digestive enzymes, reach the abdominal aorta, inhibit the angiotensin I-converting enzyme, and show antihypertensive effects in spontaneously hypertensive rats.	valyl-prolyl-proline	24-50	angiotensin I converting enzyme	Rattus norvegicus	218-249
33180478-6	2020	VPP and IPP treatment reduced the level of reactive oxygen species and EV-induced expression of adhesion molecules and restored the ability of tube formation by upregulating endothelial nitric oxide synthase expression.	valyl-prolyl-proline	0-3	nitric oxide synthase 3	Homo sapiens	174-207
33180478-7	2020	VPP and IPP reduced the protein levels of IL-6 to 227.34 +- 10.56 and 273.84 +- 22.28 pg/mL, of IL-1beta protein to 131.56 +- 23.18 and 221.14 +- 13.8 pg/mL, and of MCP-1 to 301.48 +- 19.75 and 428.68 +- 9.59 pg/mL.	valyl-prolyl-proline	0-3	interleukin 6	Homo sapiens	42-46
33180478-7	2020	VPP and IPP reduced the protein levels of IL-6 to 227.34 +- 10.56 and 273.84 +- 22.28 pg/mL, of IL-1beta protein to 131.56 +- 23.18 and 221.14 +- 13.8 pg/mL, and of MCP-1 to 301.48 +- 19.75 and 428.68 +- 9.59 pg/mL.	valyl-prolyl-proline	0-3	interleukin 1 alpha	Homo sapiens	96-104
33180478-7	2020	VPP and IPP reduced the protein levels of IL-6 to 227.34 +- 10.56 and 273.84 +- 22.28 pg/mL, of IL-1beta protein to 131.56 +- 23.18 and 221.14 +- 13.8 pg/mL, and of MCP-1 to 301.48 +- 19.75 and 428.68 +- 9.59 pg/mL.	valyl-prolyl-proline	0-3	C-C motif chemokine ligand 2	Homo sapiens	165-170
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.	valyl-prolyl-proline	25-36	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.	valyl-prolyl-proline	25-36	angiotensin I converting enzyme	Homo sapiens	68-71
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.	valyl-prolyl-proline	25-36	interleukin 10	Homo sapiens	178-183
31822614-5	2019	To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1.	valyl-prolyl-proline	49-63	cryptochrome 2	Arabidopsis thaliana	103-107
31822614-5	2019	To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1.	valyl-prolyl-proline	49-63	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	109-113
31822614-5	2019	To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1.	valyl-prolyl-proline	65-67	cryptochrome 2	Arabidopsis thaliana	103-107
31822614-5	2019	To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1.	valyl-prolyl-proline	65-67	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	109-113
31822614-5	2019	To this end, we analyzed the role of a conserved valine-proline (VP) motif in the C-terminal domain of CRY2 (CCT2), which resembles the core COP1-WD40-binding sequences present in the substrates of COP1.	valyl-prolyl-proline	65-67	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	141-145
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	17-19	cryptochrome 2	Arabidopsis thaliana	29-33
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	17-19	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	17-19	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	80-84
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	17-19	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	17-19	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	29-33
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	80-84
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	29-33
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	80-84
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-6	2019	We show that the VP motif in CRY2 is essential for the interaction of CRY2 with COP1 in yeast two-hybrid assays and in planta Mutations in the VP motif of CRY2 abolished the CRY2 activity in photomorphogenesis, indicating the importance of VP.	valyl-prolyl-proline	143-145	cryptochrome 2	Arabidopsis thaliana	70-74
31822614-7	2019	The interaction between COP1 and its VP-containing substrate PAP2 was prevented in the presence of coexpressed CRY2, but not in the presence of CRY2 carrying a VP mutation.	valyl-prolyl-proline	37-39	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	24-28
31822614-7	2019	The interaction between COP1 and its VP-containing substrate PAP2 was prevented in the presence of coexpressed CRY2, but not in the presence of CRY2 carrying a VP mutation.	valyl-prolyl-proline	37-39	Purple acid phosphatases superfamily protein	Arabidopsis thaliana	61-65
31822614-8	2019	Thus, since both PAP2 and CRY2 engage VP motifs to bind to COP1, these results demonstrate that CRY2 outcompetes PAP2 for binding to COP1.	valyl-prolyl-proline	38-40	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	133-137
31822614-7	2019	The interaction between COP1 and its VP-containing substrate PAP2 was prevented in the presence of coexpressed CRY2, but not in the presence of CRY2 carrying a VP mutation.	valyl-prolyl-proline	37-39	cryptochrome 2	Arabidopsis thaliana	111-115
31822614-7	2019	The interaction between COP1 and its VP-containing substrate PAP2 was prevented in the presence of coexpressed CRY2, but not in the presence of CRY2 carrying a VP mutation.	valyl-prolyl-proline	160-162	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	24-28
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	97-99	SPA (suppressor of phyA-105) protein family	Arabidopsis thaliana	65-69
31822614-7	2019	The interaction between COP1 and its VP-containing substrate PAP2 was prevented in the presence of coexpressed CRY2, but not in the presence of CRY2 carrying a VP mutation.	valyl-prolyl-proline	160-162	Purple acid phosphatases superfamily protein	Arabidopsis thaliana	61-65
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	97-99	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	77-81
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	97-99	cryptochrome 2	Arabidopsis thaliana	109-113
31822614-8	2019	Thus, since both PAP2 and CRY2 engage VP motifs to bind to COP1, these results demonstrate that CRY2 outcompetes PAP2 for binding to COP1.	valyl-prolyl-proline	38-40	Purple acid phosphatases superfamily protein	Arabidopsis thaliana	17-21
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	97-99	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	179-183
31822614-8	2019	Thus, since both PAP2 and CRY2 engage VP motifs to bind to COP1, these results demonstrate that CRY2 outcompetes PAP2 for binding to COP1.	valyl-prolyl-proline	38-40	cryptochrome 2	Arabidopsis thaliana	26-30
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	97-99	SPA (suppressor of phyA-105) protein family	Arabidopsis thaliana	193-197
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	157-159	SPA (suppressor of phyA-105) protein family	Arabidopsis thaliana	65-69
31822614-8	2019	Thus, since both PAP2 and CRY2 engage VP motifs to bind to COP1, these results demonstrate that CRY2 outcompetes PAP2 for binding to COP1.	valyl-prolyl-proline	38-40	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	59-63
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	157-159	phosphorylcholine cytidylyltransferase2	Arabidopsis thaliana	77-81
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	157-159	cryptochrome 2	Arabidopsis thaliana	109-113
31822614-8	2019	Thus, since both PAP2 and CRY2 engage VP motifs to bind to COP1, these results demonstrate that CRY2 outcompetes PAP2 for binding to COP1.	valyl-prolyl-proline	38-40	cryptochrome 2	Arabidopsis thaliana	96-100
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	157-159	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	179-183
22972320-0	2012	Accumulation of ACE inhibitory tripeptides, Val-Pro-Pro and Ile-Pro-Pro, in vascular endothelial cells.	valyl-prolyl-proline	44-55	angiotensin I converting enzyme	Rattus norvegicus	16-19
31822614-9	2019	We further found that the previously unknown interaction between SPA1-WD and CCT2 occurs via the VP motif in CRY2, suggesting structural similarities in the VP-binding pockets of COP1-WD40 and SPA1-WD40 domains.	valyl-prolyl-proline	157-159	SPA (suppressor of phyA-105) protein family	Arabidopsis thaliana	193-197
31822614-10	2019	A VP motif present in CRY1 is also essential for binding to COP1.	valyl-prolyl-proline	2-4	cryptochrome 1	Arabidopsis thaliana	22-26
31822614-10	2019	A VP motif present in CRY1 is also essential for binding to COP1.	valyl-prolyl-proline	2-4	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	60-64
30160110-0	2018	Milk-Derived Tripeptides IPP (Ile-Pro-Pro) and VPP (Val-Pro-Pro) Enhance Insulin Sensitivity and Prevent Insulin Resistance in 3T3-F442A Preadipocytes.	valyl-prolyl-proline	52-63	insulin	Homo sapiens	73-80
30160110-0	2018	Milk-Derived Tripeptides IPP (Ile-Pro-Pro) and VPP (Val-Pro-Pro) Enhance Insulin Sensitivity and Prevent Insulin Resistance in 3T3-F442A Preadipocytes.	valyl-prolyl-proline	52-63	insulin	Homo sapiens	105-112
30160110-2	2018	Previously, we showed adipogenic and insulin mimetic actions of IPP (Ile-Pro-Pro) and VPP (Val-Pro-Pro), the milk-derived tripeptides on cultured preadipocytes, in addition to their previously characterized antihypertensive and anti-inflammatory functions.	valyl-prolyl-proline	91-102	insulin	Homo sapiens	37-44
27435541-3	2016	Both L. helveticus strains produced bioactive tripeptides, isoleucylprolyl-proline and valyl-prolyl-proline, during fermentation of milk.	valyl-prolyl-proline	87-107	Weaning weight-maternal milk	Bos taurus	132-136
25714093-1	2015	Milk derived tripeptides IPP (Ile-Pro-Pro) and VPP (Val-Pro-Pro) have shown promise as anti-hypertensive agents due to their inhibitory effects on angiotensin converting enzyme (ACE).	valyl-prolyl-proline	52-63	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	147-176
25714093-1	2015	Milk derived tripeptides IPP (Ile-Pro-Pro) and VPP (Val-Pro-Pro) have shown promise as anti-hypertensive agents due to their inhibitory effects on angiotensin converting enzyme (ACE).	valyl-prolyl-proline	52-63	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	178-181
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.	valyl-prolyl-proline	16-27	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.	valyl-prolyl-proline	16-27	angiotensin I converting enzyme	Homo sapiens	156-159
26346532-1	2015	SCOPE: This study aimed to examine the effects of Val-Pro-Pro (VPP), a food-derived peptide with an angiotensin-converting enzyme (ACE) inhibitory property, on obesity-linked insulin resistance, and adipose inflammation in vivo and in vitro.	valyl-prolyl-proline	50-61	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	131-134
23631494-0	2013	Milk-derived peptides, Val-Pro-Pro and Ile-Pro-Pro, attenuate atherosclerosis development in apolipoprotein e-deficient mice: a preliminary study.	valyl-prolyl-proline	23-34	apolipoprotein E	Mus musculus	93-109
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.	valyl-prolyl-proline	124-146	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.	valyl-prolyl-proline	124-146	angiotensin I converting enzyme	Homo sapiens	51-54
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.	valyl-prolyl-proline	148-159	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.	valyl-prolyl-proline	148-159	angiotensin I converting enzyme	Homo sapiens	51-54
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.	valyl-prolyl-proline	31-42	angiotensin I converting enzyme	Homo sapiens	63-66
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.	valyl-prolyl-proline	33-53	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.	valyl-prolyl-proline	33-53	angiotensin I converting enzyme	Homo sapiens	135-138
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.	valyl-prolyl-proline	55-58	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.	valyl-prolyl-proline	55-58	angiotensin I converting enzyme	Homo sapiens	135-138
18604316-3	2008	The sequences Val-Pro-Pro (VPP) and Ile-Pro-Pro (IPP), with angiotensin-converting enzyme (ACE) inhibitory activity, have been isolated from these fermented products.	valyl-prolyl-proline	14-25	angiotensin I converting enzyme	Homo sapiens	60-89
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.	valyl-prolyl-proline	89-100	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.	valyl-prolyl-proline	54-65	angiotensin I converting enzyme	Homo sapiens	149-153
20721338-1	2010	Tripeptides isoleucyl-prolyl-proline (IPP) and valyl-prolyl-proline (VPP) act as ACE inhibitors in vitro.	valyl-prolyl-proline	47-67	angiotensin I converting enzyme	Homo sapiens	81-84
20721338-1	2010	Tripeptides isoleucyl-prolyl-proline (IPP) and valyl-prolyl-proline (VPP) act as ACE inhibitors in vitro.	valyl-prolyl-proline	69-72	angiotensin I converting enzyme	Homo sapiens	81-84
19907102-1	2009	AIM: A food-derived bioactive tripeptide, Val-Pro-Pro (VPP), has been shown to possess angiotensin I-converting enzyme (ACE) inhibitory activity and foods containing such peptides exhibit an anti-hypertensive effect in clinical settings.	valyl-prolyl-proline	42-53	angiotensin I converting enzyme	Homo sapiens	87-118
19907102-1	2009	AIM: A food-derived bioactive tripeptide, Val-Pro-Pro (VPP), has been shown to possess angiotensin I-converting enzyme (ACE) inhibitory activity and foods containing such peptides exhibit an anti-hypertensive effect in clinical settings.	valyl-prolyl-proline	42-53	angiotensin I converting enzyme	Homo sapiens	120-123
19907102-1	2009	AIM: A food-derived bioactive tripeptide, Val-Pro-Pro (VPP), has been shown to possess angiotensin I-converting enzyme (ACE) inhibitory activity and foods containing such peptides exhibit an anti-hypertensive effect in clinical settings.	valyl-prolyl-proline	55-58	angiotensin I converting enzyme	Homo sapiens	87-118
19907102-1	2009	AIM: A food-derived bioactive tripeptide, Val-Pro-Pro (VPP), has been shown to possess angiotensin I-converting enzyme (ACE) inhibitory activity and foods containing such peptides exhibit an anti-hypertensive effect in clinical settings.	valyl-prolyl-proline	55-58	angiotensin I converting enzyme	Homo sapiens	120-123
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.	valyl-prolyl-proline	39-50	angiotensin I converting enzyme	Homo sapiens	14-17
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).	valyl-prolyl-proline	244-266	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).	valyl-prolyl-proline	244-266	angiotensin I converting enzyme	Homo sapiens	132-135
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).	valyl-prolyl-proline	268-271	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).	valyl-prolyl-proline	268-271	angiotensin I converting enzyme	Homo sapiens	132-135
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.	valyl-prolyl-proline	88-99	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.	valyl-prolyl-proline	88-99	angiotensin converting enzyme 2	Homo sapiens	23-27
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.	valyl-prolyl-proline	88-99	angiotensin I converting enzyme	Homo sapiens	14-17
19884823-2	2010	Research has mainly focused on isoleucine-proline-proline and valine-proline-proline (IPP + VPP), two lactotripeptides that can inhibit the angiotensin-converting enzyme (ACE) in vitro.	valyl-prolyl-proline	62-84	angiotensin I converting enzyme	Homo sapiens	140-169
19884823-2	2010	Research has mainly focused on isoleucine-proline-proline and valine-proline-proline (IPP + VPP), two lactotripeptides that can inhibit the angiotensin-converting enzyme (ACE) in vitro.	valyl-prolyl-proline	62-84	angiotensin I converting enzyme	Homo sapiens	171-174
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.	valyl-prolyl-proline	87-98	angiotensin I converting enzyme	Homo sapiens	47-50
18604316-3	2008	The sequences Val-Pro-Pro (VPP) and Ile-Pro-Pro (IPP), with angiotensin-converting enzyme (ACE) inhibitory activity, have been isolated from these fermented products.	valyl-prolyl-proline	14-25	angiotensin I converting enzyme	Homo sapiens	91-94
11999412-3	2002	Val-Pro-Pro, an ACE-inhibitory peptide from fermented milk, was used as a model tripeptide.	valyl-prolyl-proline	0-11	angiotensin I converting enzyme	Homo sapiens	16-19
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).	valyl-prolyl-proline	131-134	angiotensin I converting enzyme	Homo sapiens	78-81
17383063-2	2007	The tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), isolated from hydrolysed casein have been shown to lower blood pressure by inhibiting angiotensin I-converting enzyme (ACE).	valyl-prolyl-proline	53-75	angiotensin I converting enzyme	Rattus norvegicus	169-200
17383063-2	2007	The tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), isolated from hydrolysed casein have been shown to lower blood pressure by inhibiting angiotensin I-converting enzyme (ACE).	valyl-prolyl-proline	53-75	angiotensin I converting enzyme	Rattus norvegicus	202-205
17383063-2	2007	The tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), isolated from hydrolysed casein have been shown to lower blood pressure by inhibiting angiotensin I-converting enzyme (ACE).	valyl-prolyl-proline	77-80	angiotensin I converting enzyme	Rattus norvegicus	169-200
17383063-2	2007	The tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), isolated from hydrolysed casein have been shown to lower blood pressure by inhibiting angiotensin I-converting enzyme (ACE).	valyl-prolyl-proline	77-80	angiotensin I converting enzyme	Rattus norvegicus	202-205
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.	valyl-prolyl-proline	5-16	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.	valyl-prolyl-proline	5-16	angiotensin I converting enzyme	Homo sapiens	255-258
11999412-6	2002	Since no intact Val-Pro-Pro was detected in the cells, Val-Pro-Pro apically taken by Caco-2 cells via PepT1 was likely to have been quickly hydrolyzed by intracellular peptidases, producing free Val and Pro.	valyl-prolyl-proline	55-66	solute carrier family 15 member 1	Homo sapiens	102-107
12047101-2	2002	The products contained tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), which have been shown to possess angiotensin converting enzyme (ACE) inhibitory activity.	valyl-prolyl-proline	72-94	angiotensin I converting enzyme	Rattus norvegicus	135-164
12047101-2	2002	The products contained tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), which have been shown to possess angiotensin converting enzyme (ACE) inhibitory activity.	valyl-prolyl-proline	72-94	angiotensin I converting enzyme	Rattus norvegicus	166-169
12047101-2	2002	The products contained tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), which have been shown to possess angiotensin converting enzyme (ACE) inhibitory activity.	valyl-prolyl-proline	96-99	angiotensin I converting enzyme	Rattus norvegicus	135-164
12047101-2	2002	The products contained tripeptides isoleucine-proline-proline (IPP) and valine-proline-proline (VPP), which have been shown to possess angiotensin converting enzyme (ACE) inhibitory activity.	valyl-prolyl-proline	96-99	angiotensin I converting enzyme	Rattus norvegicus	166-169