PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6358755-3 1983 This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. Proline 67-74 kininogen 1 Homo sapiens 199-209 6274413-5 1981 These data indicate that kininase II can release C-terminal tripeptides of substrates having a proline residue in the penultimate position such as des-Arg9-bradykinin and its analogues, and that this enzyme is able not only to act as a dipeptidyl carboxypeptidase but also acts as a tripeptidyl carboxy-peptidase. Proline 95-102 kininogen 1 Homo sapiens 156-166 6124421-4 1982 This enzyme cleaves N-terminal arginyl residues unless the adjacent penultimate residue is proline as is the case for bradykinin. Proline 91-98 kininogen 1 Homo sapiens 118-128 687639-3 1978 In contrast, the N-terminal Arg-Pro of bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) was not cleaved by the enzyme. Proline 32-35 kininogen 1 Homo sapiens 39-49 5822045-0 1969 Substrate specificity of collagen proline hydroxylase: hydroxylation of a specific proline residue in bradykinin. Proline 34-41 kininogen 1 Homo sapiens 102-112 3198-2 1976 N-acetyl-L-phenylalaninamide, support our previous conclusion (Biochemistry 12, 3780, 1973) that the positive 221-nm CD band of bradykinin is a composite of bands due to two chromophores, the 217-nm band characteristic of the Phe residues overlying the 223-nm band of the N-terminal sequence, Arg-Pro-Pro. Proline 297-300 kininogen 1 Homo sapiens 128-138 3198-2 1976 N-acetyl-L-phenylalaninamide, support our previous conclusion (Biochemistry 12, 3780, 1973) that the positive 221-nm CD band of bradykinin is a composite of bands due to two chromophores, the 217-nm band characteristic of the Phe residues overlying the 223-nm band of the N-terminal sequence, Arg-Pro-Pro. Proline 301-304 kininogen 1 Homo sapiens 128-138 26957155-6 2016 We further applied it to examine the design of template molecules for aromatic meta-C-H activation in solutions and investigate solution conformations of the nonapeptide Bradykinin involving slow cis-trans isomerizations of three proline residues. Proline 230-237 kininogen 1 Homo sapiens 170-180 22488046-7 2012 The proline residue, in position 4 of the bradykinin sequence promotes a turn in the longer peptide chain, shortening its end-to-end distance. Proline 4-11 kininogen 1 Homo sapiens 42-52 25838788-0 2015 An IMS-IMS threshold method for semi-quantitative determination of activation barriers: Interconversion of proline cis trans forms in triply protonated bradykinin. Proline 107-114 kininogen 1 Homo sapiens 152-162 23373819-0 2013 Cis-trans isomerizations of proline residues are key to bradykinin conformations. Proline 28-35 kininogen 1 Homo sapiens 56-66 23373819-1 2013 A recent ion mobility-mass spectrometry (IM-MS) study of the nonapeptide bradykinin (BK, amino acid sequence Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)) found evidence for 10 populations of conformations that depend upon the solution composition [J. Proline 116-119 kininogen 1 Homo sapiens 73-83 23373819-1 2013 A recent ion mobility-mass spectrometry (IM-MS) study of the nonapeptide bradykinin (BK, amino acid sequence Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)) found evidence for 10 populations of conformations that depend upon the solution composition [J. Proline 123-126 kininogen 1 Homo sapiens 73-83 23373819-7 2013 IM-MS distributions of the analogue peptides, when compared to the distribution for BK, indicate the multiple structures are associated with different combinations of cis and trans forms of the three proline residues. Proline 200-207 kininogen 1 Homo sapiens 84-86 24516103-2 2014 Dipeptidyl peptidase-4 degrades other peptides with a penultimate proline or alanine, including bradykinin and substance P, which are also substrates of angiotensin-converting enzyme (ACE). Proline 66-73 kininogen 1 Homo sapiens 96-106 17297930-8 2007 In certain configurations, cleavage products are produced in less than 10 s. Reproducible product patterns consistent with cleavage of the peptide bond at proline for angiotensin I, Lys-bradykinin, and myoglobin are demonstrated using capillary electrophoresis. Proline 155-162 kininogen 1 Homo sapiens 186-196 18986166-5 2008 IDE specifically degrades bradykinin and kallidin at the Pro/Phe site. Proline 57-60 kininogen 1 Homo sapiens 26-36 21835190-4 2012 The aim of the present article is to reveal that the snake proline-rich oligopeptides, known as bradykinin-potentiating peptides, are still a source of surprising scientific discoveries, some of them useful not only to reveal potential new targets but also to introduce prospective lead molecules for drug development. Proline 59-66 kininogen 1 Homo sapiens 96-106 18598727-1 2008 The first naturally occurring angiotensin-converting enzyme (ACE) inhibitors described are pyroglutamyl proline-rich oligopeptides, found in the venom of the viper Bothrops jararaca, and named as bradykinin-potentiating peptides (BPPs). Proline 104-111 kininogen 1 Homo sapiens 196-206 15040788-6 2004 The proline residue that is two residues upstream of bradykinin in rat kininogen is, in part, responsible for this pattern of hydrolysis, since the peptide Abz-GFSPFRASRVQ-EDDnp was preferentially cleaved at the Arg-Ala bond by hK1. Proline 4-11 kininogen 1 Homo sapiens 53-63 16599534-1 2006 The conformers of gaseous bradykinin, BK, (Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)) and its protonated forms, [BK + H](+), [BK + 2H](2+), and [BK + 3H](3+), were examined theoretically using a combination of the Merck molecular force field, Hartree-Fock, and density functional theory. Proline 50-53 kininogen 1 Homo sapiens 26-36 16599534-1 2006 The conformers of gaseous bradykinin, BK, (Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)) and its protonated forms, [BK + H](+), [BK + 2H](2+), and [BK + 3H](3+), were examined theoretically using a combination of the Merck molecular force field, Hartree-Fock, and density functional theory. Proline 57-60 kininogen 1 Homo sapiens 26-36 15134872-3 2004 The key to conversion of bradykinin into an antagonist was replacement of the proline residue at position 7 with a D-aromatic amino acid. Proline 78-85 kininogen 1 Homo sapiens 25-35 12049789-4 2002 To investigate the interaction, an NMR study was carried out on the binding of a representative polyphenol, penta-O-galloyl-D-glucopyranose, to a nonapeptide hormone, bradykinin (BDK), where proline accounts for 30% of residues. Proline 191-198 kininogen 1 Homo sapiens 167-177 10871321-7 2000 BK1-5 (Arg-Pro-Pro-Gly-Phe), the 1-to-5 amino acid fragment of bradykinin, was identified as a major stable plasma metabolite of bradykinin. Proline 11-14 kininogen 1 Homo sapiens 63-73 11523086-10 2001 The presence of two highly basic arginine residues on bradykinin results in its high GB(app), while the basicity of des-Arg1-bradykinin ions is increased by the presence of two proline residues at the N-terminus. Proline 177-184 kininogen 1 Homo sapiens 54-64 11523086-10 2001 The presence of two highly basic arginine residues on bradykinin results in its high GB(app), while the basicity of des-Arg1-bradykinin ions is increased by the presence of two proline residues at the N-terminus. Proline 177-184 kininogen 1 Homo sapiens 125-135 10871321-7 2000 BK1-5 (Arg-Pro-Pro-Gly-Phe), the 1-to-5 amino acid fragment of bradykinin, was identified as a major stable plasma metabolite of bradykinin. Proline 11-14 kininogen 1 Homo sapiens 129-139 10871321-7 2000 BK1-5 (Arg-Pro-Pro-Gly-Phe), the 1-to-5 amino acid fragment of bradykinin, was identified as a major stable plasma metabolite of bradykinin. Proline 15-18 kininogen 1 Homo sapiens 63-73 10871321-7 2000 BK1-5 (Arg-Pro-Pro-Gly-Phe), the 1-to-5 amino acid fragment of bradykinin, was identified as a major stable plasma metabolite of bradykinin. Proline 15-18 kininogen 1 Homo sapiens 129-139 7523301-4 1994 The enzyme hydrolyzed (optimum pH 6.5) the Pro-pNA bond in carbobenzoxy-Gly-Pro-p-nitroanilide (Z-Gly-Pro-pNA) and bonds at the carboxyl side of proline in several human bioactive peptides, such as bradykinin, substance P, neurotensin, angiotensins, oxytocin, vasopressin, and human endothelin fragment 22-38. Proline 145-152 kininogen 1 Homo sapiens 198-208 10742606-9 2000 We also studied several peptides related to bradykinin, and the results emphasized the formation of turns involving the proline residues and the decrease of conformational flexibility induced by using TFE as the solvent. Proline 120-127 kininogen 1 Homo sapiens 44-54 10749777-3 2000 Moreover, a proportion of kinin peptides is hydroxylated on proline(3) of the bradykinin sequence. Proline 60-67 kininogen 1 Homo sapiens 78-88 9461491-7 1998 The low Km and high kcat values (Km 7.3 and 5.0 microM, kcat 226 and 207 s-1 for the hydrolysis of Phe-Ser-Pro-Arg-Leu-Gly-Lys-Arg and Phe-Ser-Pro-Arg-Leu-Gly-Arg-Arg, respectively) obtained for the hydrolysis of these two peptides by insect ACE means that these peptides, along with mammalian bradykinin, are the most favoured in vitro ACE substrates so far identified. Proline 107-110 kininogen 1 Homo sapiens 294-304 9606729-1 1997 NMR spectroscopy has been used to obtain structural information on the bioactive conformation of the nonapeptide hormone bradykinin (Arg-Pro-Pro-Gly-Ser-Pro-Phe-Arg, BK) bound to the Fab-fragment of an antibody that mimics the hormone binding site of the natural bradykinin B2-receptor. Proline 137-140 kininogen 1 Homo sapiens 121-131 9606729-1 1997 NMR spectroscopy has been used to obtain structural information on the bioactive conformation of the nonapeptide hormone bradykinin (Arg-Pro-Pro-Gly-Ser-Pro-Phe-Arg, BK) bound to the Fab-fragment of an antibody that mimics the hormone binding site of the natural bradykinin B2-receptor. Proline 137-140 kininogen 1 Homo sapiens 263-273 9606729-1 1997 NMR spectroscopy has been used to obtain structural information on the bioactive conformation of the nonapeptide hormone bradykinin (Arg-Pro-Pro-Gly-Ser-Pro-Phe-Arg, BK) bound to the Fab-fragment of an antibody that mimics the hormone binding site of the natural bradykinin B2-receptor. Proline 141-144 kininogen 1 Homo sapiens 121-131 9606729-1 1997 NMR spectroscopy has been used to obtain structural information on the bioactive conformation of the nonapeptide hormone bradykinin (Arg-Pro-Pro-Gly-Ser-Pro-Phe-Arg, BK) bound to the Fab-fragment of an antibody that mimics the hormone binding site of the natural bradykinin B2-receptor. Proline 141-144 kininogen 1 Homo sapiens 263-273 1361094-0 1992 Proline-specific aminopeptidases: potential role in bradykinin degradation. Proline 0-7 kininogen 1 Homo sapiens 52-62 1335995-0 1992 Bradykinin and angiotensin II analogs containing a conformationally constrained proline analog. Proline 80-87 kininogen 1 Homo sapiens 0-10 1335995-1 1992 Three analogs of bradykinin and one of angiotensin II have been prepared in which the naturally occurring proline residues have been replaced by the bicyclic amino acid, 2,4-methanoproline (2,4-MePro). Proline 106-113 kininogen 1 Homo sapiens 17-27 1540646-8 1992 Hydrolysis of the substrate was strongly inhibited by bradykinin and those of its lower homologs that contain two adjacent proline residues. Proline 123-130 kininogen 1 Homo sapiens 54-64 8344943-2 1993 Prolylcarboxypeptidase, a lysosomal serine carboxypeptidase, cleaves COOH-terminal amino acids linked to proline, as in angiotensin II and III and [des-Arg9] bradykinin. Proline 105-112 kininogen 1 Homo sapiens 158-168 1361094-1 1992 The N-terminus of bradykinin is shown to be sequentially degraded by the human proline-specific aminopeptidases aminopeptidase P (EC 3.4.11.9) and dipeptidyl peptidase IV (EC 3.4.14.5). Proline 79-86 kininogen 1 Homo sapiens 18-28 2539165-8 1989 Our studies indicate that the final products of bradykinin degradation were the tripeptide Arg-Pro-Pro, one mole each of Ser, Pro, Gly, and Arg, and two moles of phenylalanine. Proline 95-98 kininogen 1 Homo sapiens 48-58 2372310-2 1990 The use of NMR methods to study conformational and dynamic aspects of the proline residues in the nonapeptide bradykinin is reviewed. Proline 74-81 kininogen 1 Homo sapiens 110-120 2640567-8 1989 Sequence analysis of peak A showed that the proline at the third amino acid residue of bradykinin was replaced by hydroxyproline. Proline 44-51 kininogen 1 Homo sapiens 87-97 3182782-5 1988 Sequence analysis of fraction I showed that the proline at the third amino acid residue of bradykinin was replaced by hydroxyproline. Proline 48-55 kininogen 1 Homo sapiens 91-101 2423824-4 1986 Comparing the structure-activity relationships of the peptides, the amino acid sequence Arg-Pro at the N-terminal region of bradykinin and substance P or Pro-Arg at the C-terminal part of tuftsin and rigin appear to be responsible for the lymphokine secretion. Proline 92-95 kininogen 1 Homo sapiens 124-134 3366244-1 1988 Hydroxyproline (Hyp) analogues of bradykinin and lysyl-bradykinin, in which the third residue of bradykinin, proline, is replaced by hydroxyproline, were isolated from human urine. Proline 7-14 kininogen 1 Homo sapiens 34-44 3366244-1 1988 Hydroxyproline (Hyp) analogues of bradykinin and lysyl-bradykinin, in which the third residue of bradykinin, proline, is replaced by hydroxyproline, were isolated from human urine. Proline 7-14 kininogen 1 Homo sapiens 55-65 3366244-1 1988 Hydroxyproline (Hyp) analogues of bradykinin and lysyl-bradykinin, in which the third residue of bradykinin, proline, is replaced by hydroxyproline, were isolated from human urine. Proline 7-14 kininogen 1 Homo sapiens 55-65