PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16011263-5 2005 RESULTS: Using the established method, we developed accordingly QSAR models of Bitter tasting dipeptide, ACE inhibitors and bradykinin-potentiating pentapeptides and their r2 and XV-r2 were more than 0.70. Dipeptides 94-103 kininogen 1 Homo sapiens 124-134 21186397-2 2011 ACE also cleaves the terminal dipeptide of vasodilating hormone bradykinin (a nonapeptide) to inactivate this hormone. Dipeptides 30-39 kininogen 1 Homo sapiens 64-74 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 kininogen 1 Homo sapiens 167-177 24639651-4 2014 Of three BK sequences extended by a C-terminal dipeptide, BK-His-Leu had the most desirable profile, exhibiting little direct affinity for the receptor but a significant one for ACE (as shown by competition of [(3)H]BK binding to B2R-GFP or of [(3)H]enalaprilat to recombinant ACE, respectively). Dipeptides 47-56 kininogen 1 Homo sapiens 58-60 24639651-4 2014 Of three BK sequences extended by a C-terminal dipeptide, BK-His-Leu had the most desirable profile, exhibiting little direct affinity for the receptor but a significant one for ACE (as shown by competition of [(3)H]BK binding to B2R-GFP or of [(3)H]enalaprilat to recombinant ACE, respectively). Dipeptides 47-56 kininogen 1 Homo sapiens 58-60 16504505-0 2006 Bradykinin antagonists modified with dipeptide mimetic beta-turn inducers. Dipeptides 37-46 kininogen 1 Homo sapiens 0-10 10882364-1 2000 We recently described a potent bradykinin B(2) receptor agonist (JMV1116) obtained by replacing the D-Tic-Oic dipeptide moiety of HOE140 by a (3S)-amino-5-(carbonylmethyl)-2,3-dihydro-1, 5-benzothiazepin-4(5H)-one (D-BT) moiety. Dipeptides 110-119 kininogen 1 Homo sapiens 31-41 10888199-1 2000 Different types of dipeptide building units containing N- or C-terminal arginine were prepared for synthesis of the backbone cyclic analogues of the peptide hormone bradykinin (BK: Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg). Dipeptides 19-28 kininogen 1 Homo sapiens 165-175 10514288-7 1999 These data provide evidence for a bioactive conformation of bradykinin constrained at the dipeptide Pro-Phe. Dipeptides 90-99 kininogen 1 Homo sapiens 60-70 10514289-0 1999 Synthesis and characterization of bradykinin B(2) receptor agonists containing constrained dipeptide mimics. Dipeptides 91-100 kininogen 1 Homo sapiens 34-44 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 kininogen 1 Homo sapiens 161-171 2274475-1 1990 The analgesic potency of the C-terminal dipeptide of tuftsin (Pro-Arg) was found to be much stronger than that of the C-terminal of bradykinin dipeptide Phe-Arg. Dipeptides 143-152 kininogen 1 Homo sapiens 132-142 2612455-5 1989 Catalytic actions of NME-I and NME-II upon bradykinin were identical; the Gly4-Phe5 and Pro7-Phe8 bonds of bradykinin were cleaved with the final hydrolytic products for each enzyme being the tetrapeptide, Arg-Pro-Pro-Gly, the tripeptide, Phe-Ser-Pro, and the dipeptide, Phe-Arg. Dipeptides 260-269 kininogen 1 Homo sapiens 107-117 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 kininogen 1 Homo sapiens 101-111 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 kininogen 1 Homo sapiens 134-144 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 kininogen 1 Homo sapiens 141-151 3013204-2 1986 Bradykinin was cleaved at two sites to produce the pentapeptide Arg-Pro-Pro-Gly-Phe plus dipeptides Ser-Pro and Phe-Arg. Dipeptides 89-99 kininogen 1 Homo sapiens 0-10 3013204-3 1986 Lysyl bradykinin was cleaved similarly to release the same dipeptides plus the hexapeptide Lys-Arg-Pro-Pro-Gly-Phe. Dipeptides 59-69 kininogen 1 Homo sapiens 6-16 6349683-8 1983 Both enzymes inactivated bradykinin by release of the C-terminal dipeptide but were inhibited differentially by specific inhibitors. Dipeptides 65-74 kininogen 1 Homo sapiens 25-35 6709646-2 1984 The enzyme also catalyzes the cleavage of arginine from des-[Arg9]-bradykinin and the hydrolysis of several X-proline dipeptides including L-arginyl-L-proline, L-leucyl-L-proline, and L-alanyl-L-proline. Dipeptides 118-128 kininogen 1 Homo sapiens 67-77 1184280-3 1975 Two tripeptides and one dipeptide, protected except at the carboxyl ends, have been prepared in solution and used as intermediates in a new synthesis of bradykinin on a solid support. Dipeptides 24-33 kininogen 1 Homo sapiens 153-163