PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 angiotensinogen Homo sapiens 4-17 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 angiotensinogen Homo sapiens 82-87 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 angiotensinogen Homo sapiens 94-108 17145192-5 2007 gACE was potently inhibited by EDTA, 1,10-phenanthroline, captopril and lisinopril, and it promptly released the dipeptides His-Leu and Phe-Arg from angiotensin I and bradykinin. Dipeptides 113-123 angiotensinogen Homo sapiens 149-162 14609329-7 2003 The dipeptide, Pro-Phe, completely inhibits ACE2 activity at 180 microM with angiotensin II as the substrate. Dipeptides 4-13 angiotensinogen Homo sapiens 77-91 15537355-0 2004 AT2-selective angiotensin II analogues containing tyrosine-functionalized 5,5-bicyclic thiazabicycloalkane dipeptide mimetics. Dipeptides 107-116 angiotensinogen Homo sapiens 14-28 15537355-1 2004 This paper reports the synthesis of two angiotensin II analogues with tyrosine-functionalized 5,5-bicyclic thiazabicycloalkane dipeptide mimetics replacing the Tyr(4)-Ile(5) residues. Dipeptides 127-136 angiotensinogen Homo sapiens 40-54 12680844-2 2003 In the present study, the depressor action of the dipeptide Val-Tyr, with an in vivo antihypertensive effect, was investigated in transgenic mice carrying the human renin gene cross-mated with mice bearing the human angiotensinogen gene (Tsukuba Hypertensive Mouse; THM). Dipeptides 50-59 angiotensinogen Homo sapiens 216-231 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 angiotensinogen Homo sapiens 139-152 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 angiotensinogen Homo sapiens 198-212 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 angiotensinogen Homo sapiens 132-145 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 angiotensinogen Homo sapiens 178-191 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 angiotensinogen Homo sapiens 211-225 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Dipeptides 2-11 angiotensinogen Homo sapiens 46-49 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Dipeptides 2-11 angiotensinogen Homo sapiens 51-64 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Dipeptides 2-11 angiotensinogen Homo sapiens 90-93 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Dipeptides 193-202 angiotensinogen Homo sapiens 46-49 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Dipeptides 193-202 angiotensinogen Homo sapiens 51-64 9273895-7 1997 Although Sta has come to be accepted as an isosteric replacement for a dipeptide unit rather than for a single amino acid residue, in our series of inhibitors Sta is more effective when replacing only the amino acid at position 10 in the natural angiotensinogen sequence. Dipeptides 71-80 angiotensinogen Homo sapiens 246-261 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 angiotensinogen Homo sapiens 170-184 1894611-1 1991 We have recently identified and characterized a chymotrypsin-like serine proteinase in human heart (human heart chymase) that is the most catalytically efficient enzyme described, thus far, for the cleavage of angiotensin I to yield angiotensin II and the dipeptide His-Leu. Dipeptides 256-265 angiotensinogen Homo sapiens 210-223 1894611-1 1991 We have recently identified and characterized a chymotrypsin-like serine proteinase in human heart (human heart chymase) that is the most catalytically efficient enzyme described, thus far, for the cleavage of angiotensin I to yield angiotensin II and the dipeptide His-Leu. Dipeptides 256-265 angiotensinogen Homo sapiens 233-247 34770898-1 2021 Human dipeptidyl-peptidase III (hDPP III) is capable of specifically cleaving dipeptides from the N-terminal of small peptides with biological activity such as angiotensin II (Ang II, DRVYIHPF), and participates in blood pressure regulation, pain modulation, and the development of cancers in human biological activities. Dipeptides 78-88 angiotensinogen Homo sapiens 160-174 1851160-4 1991 Both domains are enzymatically active and cleave the C-terminal dipeptide of hippuryl-His-Leu or angiotensin I. Dipeptides 64-73 angiotensinogen Homo sapiens 97-110 1705633-1 1990 Enalkiren (A-64662), a potent, dipeptide renin inhibitor, mimics the transition state of the human renin substrate, angiotensinogen. Dipeptides 31-40 angiotensinogen Homo sapiens 116-131 34389655-6 2021 Both dipeptides also enhanced hydrolysis of Nln endogenous substrates neurotensin, angiotensin I and bradykinin, and increased efficiency of the synthetic substrate hydrolysis (Vmax/Km ratio) in a concentration-dependent manner. Dipeptides 5-15 angiotensinogen Homo sapiens 83-96 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 angiotensinogen Homo sapiens 143-156 34770898-1 2021 Human dipeptidyl-peptidase III (hDPP III) is capable of specifically cleaving dipeptides from the N-terminal of small peptides with biological activity such as angiotensin II (Ang II, DRVYIHPF), and participates in blood pressure regulation, pain modulation, and the development of cancers in human biological activities. Dipeptides 78-88 angiotensinogen Homo sapiens 176-182 3741422-3 1986 The more widely recognized biosynthetic pathway is by the extracellular dipeptide cleavage of angiotensin I by an enzyme which also degrades bradykinin, i.e., angiotensin converting enzyme. Dipeptides 72-81 angiotensinogen Homo sapiens 94-107 3295239-5 1987 Angiotensinogen analogues such as peptides IX and X that contain the dipeptide isostere (2R,3R,4R,5S)-5-amino-3,4-dihydroxy-2-isopropyl-7-methyloctanoic acid residue at the scissile site are shown to be potent inhibitors of human plasma renin. Dipeptides 69-78 angiotensinogen Homo sapiens 0-15 3143009-1 1988 Dipeptide analogues of angiotensinogen utilizing a dihydroxyethylene transition-state mimic at the scissile bond to impart greater inhibitory potency. Dipeptides 0-9 angiotensinogen Homo sapiens 23-38 3143010-1 1988 Dipeptide analogues of angiotensinogen utilizing a structurally modified phenylalanine residue to impart proteolytic stability. Dipeptides 0-9 angiotensinogen Homo sapiens 23-38 3309313-1 1987 Dipeptide analogues of angiotensinogen incorporating transition-state, nonpeptidic replacements at the scissile bond. Dipeptides 0-9 angiotensinogen Homo sapiens 23-38 3309313-2 1987 A series of dipeptide analogues of angiotensinogen have been prepared and evaluated for their ability to inhibit the aspartic proteinase renin. Dipeptides 12-21 angiotensinogen Homo sapiens 35-50 3305946-3 1987 The coupling of these fragments to protected dipeptides that mimic positions 8 and 9 in angiotensinogen produces inhibitors of human renin even though the molecules contain no functionality beyond what is formally the Val11 side chain of angiotensinogen. Dipeptides 45-55 angiotensinogen Homo sapiens 88-103 3305946-3 1987 The coupling of these fragments to protected dipeptides that mimic positions 8 and 9 in angiotensinogen produces inhibitors of human renin even though the molecules contain no functionality beyond what is formally the Val11 side chain of angiotensinogen. Dipeptides 45-55 angiotensinogen Homo sapiens 238-253 3027262-3 1987 The purified protein, like the mammalian enzyme, acted as a peptidyl dipeptidase in cleaving dipeptides from the C-terminus of a variety of peptide substrates, including angiotensin I, bradykinin, [Met5]enkephalin, [Leu5]enkephalin, and the model substrate hippuryl (benzoylglycyl; BzGly)-His-Leu. Dipeptides 93-103 angiotensinogen Homo sapiens 170-183 28321-6 1978 The rate of hydrolysis increased when phenylalanine in the N-protected dipeptide was replaced with alanine, valine, or leucine or when the octapeptide angiotensin II or the heptapeptide angiotensin III were the substrates. Dipeptides 71-80 angiotensinogen Homo sapiens 151-165 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 angiotensinogen Homo sapiens 147-160 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 angiotensinogen Homo sapiens 180-194