PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15319801-7 2004 However, Hoe 140 D-Arg-[Hyp3, Thi5,D-Tic7, Oic8]-bradykinin, an antagonist of B2 responses, significantly inhibited bradykinin-induced contraction. Arginine 19-22 kininogen 1 Homo sapiens 49-59 15319801-7 2004 However, Hoe 140 D-Arg-[Hyp3, Thi5,D-Tic7, Oic8]-bradykinin, an antagonist of B2 responses, significantly inhibited bradykinin-induced contraction. Arginine 19-22 kininogen 1 Homo sapiens 116-126 12578561-3 2003 Serine and arginine are also the residues at positions P"(1) and P"(2) in human kininogen, from which hK1 releases Lys-bradykinin. Arginine 11-19 kininogen 1 Homo sapiens 119-129 12756290-5 2003 Upon stimulation of NO production by bradykinin, however, recycling is co-stimulated to the extent that more than 80% of the citrulline produced is recycled to arginine. Arginine 160-168 kininogen 1 Homo sapiens 37-47 12392844-4 2002 Nitric oxide (NO) bioactivity was represented by both basal and bradykinin-stimulated cellular cyclic guanosine monophosphate accumulation and L-citrulline conversion from L-arginine. Arginine 172-182 kininogen 1 Homo sapiens 64-74 12645517-3 2003 In addition, TAFIa has been shown to be capable of removing the carboxyl-terminal arginine residues from the anaphylatoxins and bradykinin, thus implying a role for the TAFI pathway in the vascular responses to inflammation. Arginine 82-90 kininogen 1 Homo sapiens 128-138 11500030-6 2001 The sequence of bombinakinin M is preceded by a single basic residue (arginine), which represents the site of cleavage for releasing of mature bombinakinin M. This is the first cDNA cloning of bradykinin-related peptides from amphibian skin. Arginine 70-78 kininogen 1 Homo sapiens 193-203 12372699-5 2002 This effect of BK(1-9) (10(-6) M) was mimicked by the B2 agonist [Phe(8)(CH(2)NH)Arg(9)]-bradykinin (10(-5) M) and blocked by the selective B2-receptor antagonist HOE140 (10(-5) M). Arginine 81-84 kininogen 1 Homo sapiens 89-99 11791011-4 2002 The apoptosis inhibited by bradykinin was reduced by nitric oxide inhibitor N(G)-monomethyl-L-arginine (L-NMMA) and consequently restored by combined treatment with L-NMMA and L-arginine. Arginine 92-102 kininogen 1 Homo sapiens 27-37 11791011-6 2002 Bradykinin increased nitric oxide production, which was inhibited by L-NMMA and restored by combined treatment with L-NMMA and L-arginine. Arginine 127-137 kininogen 1 Homo sapiens 0-10 11744416-6 2001 The inhibitory effect of N(G)-nitro-L-arginine methylester (0.1 mmol/liter) on bradykinin-induced relaxation was lower in UWS- than KHS-incubated segments after U46619 pre-contraction, but similar after KCl pre-contraction; however, the inhibitory effect of 0.5 mmol/liter ouabain was unaffected. Arginine 36-46 kininogen 1 Homo sapiens 79-89 10514288-2 1999 The same modification was performed on the potent bradykinin B(2) receptor antagonist HOE 140 (H-D-Arg-Arg-Pro-Hyp-Gly-Thi-Ser-D-Tic-Oic-Arg-OH), in which the -D-Tic-Oic- moiety was replaced by D-BT to yield H-D-Arg-Arg-Pro-Hyp-Gly-Thi-Ser-D-BT-Arg-OH, 1 (JMV1116). Arginine 99-102 kininogen 1 Homo sapiens 50-60 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. Arginine 33-41 kininogen 1 Homo sapiens 54-64 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). Arginine 72-80 kininogen 1 Homo sapiens 165-175 11292368-3 2001 In this study, we demonstrate that exogenous citrulline was as effective as exogenous arginine in stimulating nitric oxide production and that citrulline in the presence of excess intracellular and extracellular arginine further enhanced bradykinin stimulated endothelial nitric oxide production. Arginine 212-220 kininogen 1 Homo sapiens 238-248 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. Arginine 7-10 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. Arginine 7-10 kininogen 1 Homo sapiens 129-139 9767830-4 1998 NO SYNTHESIS: Nitric oxide is synthesized from L-arginine by NO-synthetase whose activity is regulated by intracellular calcium concentration and modulated by pharmacological compounds such as acetylcholine, 5-hydroxytryptamine, bradykinin and ADP as well as the sheer forces produced by blood flow. Arginine 47-57 kininogen 1 Homo sapiens 229-239 9724311-6 1998 Coinfusion of L-arginine (0.33 mg/min) markedly improved the bradykinin-induced venodilation in smokers (52 +/- 7 to 90 +/- 9%; P < 0.01). Arginine 14-24 kininogen 1 Homo sapiens 61-71 10464023-9 1999 Therefore, we attribute the high B1 receptor selectivity, observed upon removal of Arg(9) from bradykinin, solely to the loss of a charged amino acid and not to altered structural features. Arginine 83-86 kininogen 1 Homo sapiens 95-105 10093213-5 1999 The strongest intramolecular interaction appears to be a proton bridge between the guanidino groups of the N- and C-terminal arginines in bradykinin. Arginine 125-134 kininogen 1 Homo sapiens 138-148 10434255-3 1998 Among these new antagonists, the guanidinium cations, which appear not only in the terminal arginine residues of BK but also in several nonpeptidic antagonists, will be substituted by groups with characteristics similar in terms of electrostatic potential, electron density, shape, etc. Arginine 92-100 kininogen 1 Homo sapiens 113-115 8764214-2 1996 Bradykinin induced a significant increase in [3H]glycoconjugate secretion in a dose-dependent manner from isolated glands, which was significantly inhibited by D-Arg-(Hyp3, Thi5,8, D-Phe7)-bradykinin (the B2-receptor antagonist), whereas Des-Arg9-(Leu8)-bradykinin (B1-receptor antagonist) or indomethacin did not significantly alter it. Arginine 162-165 kininogen 1 Homo sapiens 0-10 9523665-12 1998 The subsequent infusion of L-arginine (300 micromol/L) partially reversed the increased tone and significantly (P < 0.01) restored the relaxation induced by BK, Lys-BK and Met-Lys-BK. Arginine 27-37 kininogen 1 Homo sapiens 160-162 9523665-12 1998 The subsequent infusion of L-arginine (300 micromol/L) partially reversed the increased tone and significantly (P < 0.01) restored the relaxation induced by BK, Lys-BK and Met-Lys-BK. Arginine 27-37 kininogen 1 Homo sapiens 168-170 9523665-12 1998 The subsequent infusion of L-arginine (300 micromol/L) partially reversed the increased tone and significantly (P < 0.01) restored the relaxation induced by BK, Lys-BK and Met-Lys-BK. Arginine 27-37 kininogen 1 Homo sapiens 168-170 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. Arginine 133-136 kininogen 1 Homo sapiens 263-273 16525512-5 1996 For bradykinin and its analogues differing by modification of the residues between the two arginine groups on either end of the molecule, the singly and doubly protonated ions have average activation energies of 1.2 and 0.8 eV, respectively, and average A values of 10(8) and 10(12) s(-1), respectively, i.e., the presence of a second charge reduces the activation energy by 0.4 eV and decreases the A value by a factor of 10(4). Arginine 91-99 kininogen 1 Homo sapiens 4-14 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. Arginine 111-114 kininogen 1 Homo sapiens 294-304 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. Arginine 127-130 kininogen 1 Homo sapiens 294-304 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. Arginine 127-130 kininogen 1 Homo sapiens 294-304 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. Arginine 127-130 kininogen 1 Homo sapiens 294-304 9423284-1 1997 Modification of arginine residues in bradykinin, [1-5]-bradykinin, splenopentin and two synthetic pentapeptides with acetylacetone (pentane-2,4-dione) significantly increases the relative abundance of sequence-specific fragment ions produced by matrix-assisted laser desorption/ionization (MALDI). Arginine 16-24 kininogen 1 Homo sapiens 37-47 9423284-1 1997 Modification of arginine residues in bradykinin, [1-5]-bradykinin, splenopentin and two synthetic pentapeptides with acetylacetone (pentane-2,4-dione) significantly increases the relative abundance of sequence-specific fragment ions produced by matrix-assisted laser desorption/ionization (MALDI). Arginine 16-24 kininogen 1 Homo sapiens 55-65 9056177-5 1997 A comparison with a data base suggested that the sequence is very similar to des-arg9bradykinin (arg-pro-pro-gly-phe-ser-pro-phe). Arginine 81-84 kininogen 1 Homo sapiens 85-95 9056177-10 1997 In conclusion, the existence of des-arg9[hyp3]-bradykinin (arg-pro-hyp-gly-phe-ser-pro-phe) in human plasma is described. Arginine 36-39 kininogen 1 Homo sapiens 47-57 9016333-6 1997 The structures of membrane-bound [Thr6]-bradykinin developed here provide experimental support for the interaction of residues 7 and 8 with the core of the membrane-bound receptor and the N-terminus and C-terminal arginine interacting with the extracellular portion of the receptor. Arginine 214-222 kininogen 1 Homo sapiens 40-50 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. Arginine 133-136 kininogen 1 Homo sapiens 121-131 8759097-9 1996 CONCLUSIONS: These results indicate that bradykinin and its metabolites are selective antithrombins by preventing alpha-thrombin cleavage of the cloned thrombin receptor between arginine-41 and serine-42. Arginine 178-186 kininogen 1 Homo sapiens 41-51 8818341-14 1996 L-Arginine, 30 mumol, reversed the effect of L-NAME, 1 mumol, on the bradykinin- and histamine-induced albumin extravasation into the nasal airway. Arginine 0-10 kininogen 1 Homo sapiens 69-79 8764214-3 1996 Nitric oxide synthase inhibitor (nitro-L-arginine methyl ester) caused a significant inhibition of bradykinin-induced glycoconjugate secretion, which was reversed by the addition of L-arginine. Arginine 39-49 kininogen 1 Homo sapiens 99-109 8764214-2 1996 Bradykinin induced a significant increase in [3H]glycoconjugate secretion in a dose-dependent manner from isolated glands, which was significantly inhibited by D-Arg-(Hyp3, Thi5,8, D-Phe7)-bradykinin (the B2-receptor antagonist), whereas Des-Arg9-(Leu8)-bradykinin (B1-receptor antagonist) or indomethacin did not significantly alter it. Arginine 162-165 kininogen 1 Homo sapiens 189-199 8801862-4 1995 NO-dependent cGMP production in the cells (passage 1; preincubated in L-arginine-free medium for 24 h) was stimulated for 3 min with bradykinin (BK 1 nM) or the calcium-ionophore A23187 (100 nM) or by a 20 min incubation with L-arginine (L-Arg 0.1 mM, 20 min). Arginine 70-80 kininogen 1 Homo sapiens 133-143 8745290-2 1996 We have investigated whether changes in extracellular ion composition and substrate deprivation modulate basal and/or bradykinin-stimulated L-arginine transport and release of nitric oxide (NO) and prostacyclin (PGI2) in porcine aortic endothelial cells cultured and superfused on microcarriers. Arginine 140-150 kininogen 1 Homo sapiens 118-128 8745290-15 1996 Bradykinin-stimulated L-arginine transport was insensitive to removal of Ca2+, whereas agonist-induced NO release was abolished. Arginine 22-32 kininogen 1 Homo sapiens 0-10 8913543-6 1996 Vasodilator responses to bradykinin are antagonized by the B2-receptor icatibant and are blunted (but not abolished) by inhibition of the L-arginine/NO pathway with L-NG-monomethyl arginine. Arginine 138-148 kininogen 1 Homo sapiens 25-35 8801862-4 1995 NO-dependent cGMP production in the cells (passage 1; preincubated in L-arginine-free medium for 24 h) was stimulated for 3 min with bradykinin (BK 1 nM) or the calcium-ionophore A23187 (100 nM) or by a 20 min incubation with L-arginine (L-Arg 0.1 mM, 20 min). Arginine 226-236 kininogen 1 Homo sapiens 133-143 8801862-4 1995 NO-dependent cGMP production in the cells (passage 1; preincubated in L-arginine-free medium for 24 h) was stimulated for 3 min with bradykinin (BK 1 nM) or the calcium-ionophore A23187 (100 nM) or by a 20 min incubation with L-arginine (L-Arg 0.1 mM, 20 min). Arginine 238-243 kininogen 1 Homo sapiens 133-143 8610212-5 1995 The inhibition by L-NAME was reversed by the addition of L-arginine in both MCh- and BK-induced secretions from isolated glands. Arginine 57-67 kininogen 1 Homo sapiens 85-87 15714750-5 1995 Preincubation of endothelial cells with bradykinin and superoxide dismutase (SOD) synergistically potentiated the increase in platelet cGMP, but was attenuated by Nomega-nitro-L-arginine, with partial restoration by L-arginine but not by D-arginine. Arginine 176-186 kininogen 1 Homo sapiens 40-50 8560418-6 1995 These data suggested that LKd had an altered conformation which exposed the amino terminal arginine of bradykinin to antigenic detection. Arginine 91-99 kininogen 1 Homo sapiens 103-113 7530473-13 1994 These results demonstrate that vasodilator responses to both bradykinin and substance P are mediated in part via the L-arginine/NO pathway. Arginine 117-127 kininogen 1 Homo sapiens 61-71 17743549-6 1995 Similar agreement was obtained in initial studies that modeled experimental data for arginine-protonated bradykinin. Arginine 85-93 kininogen 1 Homo sapiens 105-115 7786135-2 1994 Its synthesis from L-arginine is assured by NO-synthase, the activity of which is dependent on intracellular calcium concentrations, which are themselves modulated by pharmacological (acetylcholine, serotonin, bradykinin...) or physical factors (shearing forces exerted by blood flow). Arginine 19-29 kininogen 1 Homo sapiens 210-220 7835634-5 1994 The preincubation with the precursor of NO synthesis, L-arginine (10(-4) M), reduced KCl-induced contraction and increased the BK relaxation. Arginine 54-64 kininogen 1 Homo sapiens 127-129 8012902-5 1994 Paradoxically, L-arginine (10 microM) had an inhibiting rather than an enhancing effect on the bradykinin relaxation. Arginine 15-25 kininogen 1 Homo sapiens 95-105 8048578-6 1994 Endothelium-dependent relaxations to bradykinin and ET-1 were greater in pulmonary veins compared with arteries, inhibited by N omega-nitro-L-arginine, and reversed by L-arginine. Arginine 140-150 kininogen 1 Homo sapiens 37-47 7516884-8 1994 The similarity in the inhibitory effects of N omega-nitro-L-arginine methyl ester and N omega-nitro-L-arginine on responses to acetylcholine, bradykinin, and substance P suggest that the L-arginine analog, N omega-nitro-L-arginine, as well as the methyl ester of N omega-nitro-L-arginine, are useful probes for studying endothelium-dependent vasodilator responses in the mesenteric vascular bed of the cat. Arginine 58-68 kininogen 1 Homo sapiens 142-152 8344795-7 1993 CONCLUSION: These findings demonstrate that in porcine ciliary arteries, local anesthetics impair endothelial formation of nitric oxide from L-arginine after stimulation with bradykinin, which may contribute importantly to the reduction in blood flow to the eye during retrobulbar anesthesia. Arginine 141-151 kininogen 1 Homo sapiens 175-185 8130654-2 1994 The trypsin-generated active form can not only cleave a small synthetic substrate, hippuryl-L-arginine, but can remove terminal arginine from bradykinin. Arginine 94-102 kininogen 1 Homo sapiens 142-152 8357330-5 1993 Bradykinin is a potent activator of the L-arginine nitric oxide system (endothelium-derived relaxing factor). Arginine 40-50 kininogen 1 Homo sapiens 0-10 7680560-6 1993 NOS inhibitor-induced CBF slowing was also observed when cells were pre-stimulated with either bradykinin or substance P and was completely reversed by L-arginine or SNP but not by D-arginine. Arginine 152-162 kininogen 1 Homo sapiens 95-105 1487709-8 1992 Endo-oligopeptidase A cleaved the bonds Phe-Ser of bradykinin, Met-Arg of BAM-12P and Arg-Arg of neurotensin as described for rabbit brain and heart and bovine brain enzymes. Arginine 67-70 kininogen 1 Homo sapiens 51-61 1330642-4 1992 The cyclic GMP responses to bradykinin were suppressed with the same potency by L-arginine analogues in control and in forskolin-treated cells (IC50 of NG-monomethyl-L-arginine 2 microM, of nitro-L-arginine 0.7 microM). Arginine 80-90 kininogen 1 Homo sapiens 28-38 1479739-2 1992 BK, incubated with diluted plasma, was degraded to des-Arg9-BK (des-9-BK), des-Phe8-Arg9-BK (des-8,9-BK) and Arg-Pro-Pro-Gly-Phe ([1-5]BK). Arginine 55-58 kininogen 1 Homo sapiens 0-2 1479739-2 1992 BK, incubated with diluted plasma, was degraded to des-Arg9-BK (des-9-BK), des-Phe8-Arg9-BK (des-8,9-BK) and Arg-Pro-Pro-Gly-Phe ([1-5]BK). Arginine 55-58 kininogen 1 Homo sapiens 60-62 1479739-2 1992 BK, incubated with diluted plasma, was degraded to des-Arg9-BK (des-9-BK), des-Phe8-Arg9-BK (des-8,9-BK) and Arg-Pro-Pro-Gly-Phe ([1-5]BK). Arginine 55-58 kininogen 1 Homo sapiens 60-62 1479739-2 1992 BK, incubated with diluted plasma, was degraded to des-Arg9-BK (des-9-BK), des-Phe8-Arg9-BK (des-8,9-BK) and Arg-Pro-Pro-Gly-Phe ([1-5]BK). Arginine 55-58 kininogen 1 Homo sapiens 60-62 1659406-2 1991 In the presence of nitro-L-arginine (100 microM), an inhibitor of NO synthase, the stimulatory effect of bradykinin on L-arginine uptake was partially inhibited while NO release was completely abolished. Arginine 25-35 kininogen 1 Homo sapiens 105-115 1282939-1 1992 The effect of the arginine analogue, N omega-nitro-L-arginine (L-NNA) was studied on bradykinin-induced relaxation in porcine coronary arteries. Arginine 18-26 kininogen 1 Homo sapiens 85-95 2539165-5 1989 In serum, however, the C-terminal Arg was removed from bradykinin about five times faster than was accounted for by the activity of carboxypeptidase N. The primary substrate of ACE in serum, therefore, was des-Arg9-bradykinin and not bradykinin. Arginine 34-37 kininogen 1 Homo sapiens 215-225 1659406-0 1991 Bradykinin and ATP stimulate L-arginine uptake and nitric oxide release in vascular endothelial cells. Arginine 29-39 kininogen 1 Homo sapiens 0-10 1991651-6 1991 Addition of L-arginine to arginine-deficient but not arginine-containing endothelial cells rapidly restored the capacity of shear stress and bradykinin to generate EDRF. Arginine 12-22 kininogen 1 Homo sapiens 141-151 1991651-6 1991 Addition of L-arginine to arginine-deficient but not arginine-containing endothelial cells rapidly restored the capacity of shear stress and bradykinin to generate EDRF. Arginine 14-22 kininogen 1 Homo sapiens 141-151 1991651-6 1991 Addition of L-arginine to arginine-deficient but not arginine-containing endothelial cells rapidly restored the capacity of shear stress and bradykinin to generate EDRF. Arginine 26-34 kininogen 1 Homo sapiens 141-151 2122744-0 1990 Different activation of L-arginine pathway by bradykinin, serotonin, and clonidine in coronary arteries. Arginine 24-34 kininogen 1 Homo sapiens 46-56 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. Arginine 168-171 kininogen 1 Homo sapiens 134-144 2539165-4 1989 Carboxypeptidase N slowly removed the C-terminal Arg from bradykinin to yield des-Arg9-bradykinin (DBK); the latter was digested by ACE to yield the aforementioned pentapeptide and the tripeptide Ser-Pro-Phe. Arginine 49-52 kininogen 1 Homo sapiens 58-68 2539165-4 1989 Carboxypeptidase N slowly removed the C-terminal Arg from bradykinin to yield des-Arg9-bradykinin (DBK); the latter was digested by ACE to yield the aforementioned pentapeptide and the tripeptide Ser-Pro-Phe. Arginine 49-52 kininogen 1 Homo sapiens 87-97 2539165-5 1989 In serum, however, the C-terminal Arg was removed from bradykinin about five times faster than was accounted for by the activity of carboxypeptidase N. The primary substrate of ACE in serum, therefore, was des-Arg9-bradykinin and not bradykinin. Arginine 34-37 kininogen 1 Homo sapiens 55-65 2539165-5 1989 In serum, however, the C-terminal Arg was removed from bradykinin about five times faster than was accounted for by the activity of carboxypeptidase N. The primary substrate of ACE in serum, therefore, was des-Arg9-bradykinin and not bradykinin. Arginine 34-37 kininogen 1 Homo sapiens 215-225 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. Arginine 91-94 kininogen 1 Homo sapiens 48-58 3395372-3 1988 Purified microvessels contained a membrane-bound carboxypeptidase which hydrolyzed the C-terminal Phe-Arg bond of both kallidin and bradykinin. Arginine 102-105 kininogen 1 Homo sapiens 132-142 2544772-6 1989 The endothelium dependent vasodilator peptides such as bradykinin contain L-arginine in their sequence. Arginine 74-84 kininogen 1 Homo sapiens 55-65 3382440-1 1988 A certain resemblance of three-dimensional molecular organizations of the known peptide bioregulator bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) and the tentative cytophilic centre of the human IgE igercin (Arg-Ala-Val-Ser-Val-Asn-Pro-Gly-Lys) existing along with their pronounced structural similarity was shown by means of energy calculations. Arginine 113-116 kininogen 1 Homo sapiens 101-111 3131684-4 1988 Release of NO from the endothelial cells induced by bradykinin and the calcium ionophore A23187 was reversibly enhanced by infusions of L-arginine and L-citrulline, but not D-arginine or other close structural analogues. Arginine 136-146 kininogen 1 Homo sapiens 52-62 3030335-1 1987 Bradykinin is degraded in human plasma by a carboxypeptidase to yield desArg9-bradykinin (DBK) which is then digested by angiotensin-converting enzyme (ACE) to the pentapeptide Arg-Pro-Pro-Gly-Phe and the tripeptide Ser-Pro-Phe. Arginine 73-76 kininogen 1 Homo sapiens 0-10 3300283-2 1987 Work using classical paper chromatographic techniques for detecting free amino acids indicated that the octapeptide, des-(Arg9)-bradykinin, enters these cells and its amino-terminal arginine residue is released by cytosolic aminopeptidase-P. Arginine 182-190 kininogen 1 Homo sapiens 128-138 3300283-3 1987 We have used 1H NMR to monitor directly the release of arginine from bradykinin. Arginine 55-63 kininogen 1 Homo sapiens 69-79 3643926-2 1987 Sequencing of the NH2-terminal region of the light chain reported herein identified the third kallikrein cleavage site of high molecular weight kininogen as Arg-437. Arginine 157-160 kininogen 1 Homo sapiens 122-153 3030335-1 1987 Bradykinin is degraded in human plasma by a carboxypeptidase to yield desArg9-bradykinin (DBK) which is then digested by angiotensin-converting enzyme (ACE) to the pentapeptide Arg-Pro-Pro-Gly-Phe and the tripeptide Ser-Pro-Phe. Arginine 73-76 kininogen 1 Homo sapiens 78-88 6208535-8 1984 Modification of arginine residues in ACE with cyclohexanedione or butanedione similarly inhibited hydrolysis of SP, bradykinin and Bz-Gly-Phe-Arg (80-93%) indicating an active site arginine is required for hydrolysis of SP. Arginine 16-24 kininogen 1 Homo sapiens 116-126 3633200-4 1986 We hypothesized that modification of arginine residues may prevent cleavage of HMW kininogen, since the initial kallikrein-induced cleavage sites on the HMW kininogen molecule are at the NH2 terminal and the COOH terminal of the bradykinin-containing portion of the molecule, each of which contains arginine. Arginine 37-45 kininogen 1 Homo sapiens 229-239 3633200-5 1986 We found that modification with butanedione of four arginine residues in the HMW kininogen molecule prevented bradykinin release, which results from cleavage of HMW kininogen. Arginine 52-60 kininogen 1 Homo sapiens 110-120 2409028-11 1985 Using high performance liquid chromatography we have separated bradykinin from kallidin, des-Arg9-bradykinin (the degradation product of carboxypeptidase N) as well as the fragments Arg-Pro-Pro-Gly-Phe, Ser-Pro, and Phe-Arg, the degradation products formed by angiotensin-converting enzyme. Arginine 93-96 kininogen 1 Homo sapiens 63-73 2417254-5 1985 Modification of arginine residues in ACE with cylcohexanedione or butanedione inhibited hydrolysis of SP, bradykinin and Bz-Gly-Phe-Arg (80-93%) indicating an active site arginine is required for hydrolysis of SP. Arginine 16-24 kininogen 1 Homo sapiens 106-116 3718539-1 1986 Carboxypeptidase N removed the C-terminal arginine from bradykinin or lysyl bradykinin to leave the des-Arg derivative of each, and no further degradation occurred regardless of enzyme concentration or time of incubation. Arginine 42-50 kininogen 1 Homo sapiens 56-66 3718539-1 1986 Carboxypeptidase N removed the C-terminal arginine from bradykinin or lysyl bradykinin to leave the des-Arg derivative of each, and no further degradation occurred regardless of enzyme concentration or time of incubation. Arginine 42-50 kininogen 1 Homo sapiens 76-86 3718539-4 1986 However, angiotensin converting enzyme degraded des-Arg9-bradykinin in plasma or serum prior to such Phe removal to yield the pentapeptide Arg-Pro-Pro-Gly-Phe and the tripeptide Ser-Pro-Phe. Arginine 52-55 kininogen 1 Homo sapiens 57-67 6437213-2 1984 The purified enzyme cleaved arginine from des-(Arg9)-bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe) had a molecular weight in nondenaturing buffers of 155,000 +/- 6,900 daltons, was not inactivated by chelating agents, had a pH optimum of 7.2, and was stimulated by manganous ions. Arginine 28-36 kininogen 1 Homo sapiens 53-63 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. Arginine 42-50 kininogen 1 Homo sapiens 67-77 6437213-4 1984 Extensively washed and intact human erythrocytes cleaved arginine from exogenously supplied des-(Arg9)-bradykinin; arginine was the earliest-appearing reaction product. Arginine 57-65 kininogen 1 Homo sapiens 103-113 6437213-4 1984 Extensively washed and intact human erythrocytes cleaved arginine from exogenously supplied des-(Arg9)-bradykinin; arginine was the earliest-appearing reaction product. Arginine 115-123 kininogen 1 Homo sapiens 103-113 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. Arginine 28-31 kininogen 1 Homo sapiens 39-49 6556144-2 1983 Bradykinin is destroyed by two enzymes: a plasma carboxypeptidase (anaphylatoxin inactivator) removes the COOH-terminal arginine to yield an inactive octapeptide, and a dipeptidase (identical to the angiotensin-converting enzyme) removes the COOH-terminal Phe-Arg to yield a fragment of seven amino acids that is further fragmented to an end product of five amino acids. Arginine 120-128 kininogen 1 Homo sapiens 0-10 35240-4 1979 It is shown that the two biologically essential arginine residues (Arg1 and Arg9) are important for the specific folded bradykinin conformation. Arginine 48-56 kininogen 1 Homo sapiens 120-130 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. Arginine 51-54 kininogen 1 Homo sapiens 39-49 26068400-4 2015 The Phe(5/8) and Arg(9) residues of BK generally participated in the interactions with colloidal suspended Ag surfaces. Arginine 17-20 kininogen 1 Homo sapiens 36-38 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. Arginine 293-296 kininogen 1 Homo sapiens 128-138 29605732-1 2018 Bradykinin-potentiating peptides (BPPs - 5a, 7a, 9a, 10c, 11e, and 12b) of Bothrops jararaca (Bj) were described as argininosuccinate synthase (AsS) activators, improving l-arginine availability. Arginine 171-181 kininogen 1 Homo sapiens 0-10 562351-0 1977 Synthesis of analogues of bradykinin with replacement of the arginine residues by 4-guanidinophenyl-l-alanine. Arginine 61-69 kininogen 1 Homo sapiens 26-36 26786060-5 2016 TAFI also plays a role in inflammatory processes via the removal of C-terminal arginine or lysine residues from bradykinin, thrombin-cleaved osteopontin, C3a, C5a and chemerin. Arginine 79-87 kininogen 1 Homo sapiens 112-122 22522052-3 2012 We found that replacement of the C-terminal Arg in the natural kB2R activators bradykinin (BK) or kallidin (KD) with Lys (K(9)-BK or K(10)-KD) resulted in agonists that effectively stimulate the downstream signaling of both the kB1R and kB2R as measured by increased inositol turnover, intracellular calcium, ERK1/2 phosphorylation, arachidonic acid release and NO production. Arginine 44-47 kininogen 1 Homo sapiens 79-89 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. Arginine 109-112 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. Arginine 165-168 kininogen 1 Homo sapiens 73-83 22522052-3 2012 We found that replacement of the C-terminal Arg in the natural kB2R activators bradykinin (BK) or kallidin (KD) with Lys (K(9)-BK or K(10)-KD) resulted in agonists that effectively stimulate the downstream signaling of both the kB1R and kB2R as measured by increased inositol turnover, intracellular calcium, ERK1/2 phosphorylation, arachidonic acid release and NO production. Arginine 44-47 kininogen 1 Homo sapiens 91-93 20923691-4 2011 Here, we report the presence of (Arg(0), Trp(5), Leu(8))-bradykinin in the skin secretion of the European edible frog, Pelophylax kl. Arginine 33-36 kininogen 1 Homo sapiens 57-67 21177981-2 2011 Inflammation is accompanied by an increased maturation of DCs and the generation of kinins, particularly Lys-des[Arg(9)]-bradykinin (Lda-BK). Arginine 113-116 kininogen 1 Homo sapiens 121-131 21355573-3 2011 Whereas BK exhibits a stronger interaction with the membrane and prefers to stay on the interface, des-Arg9-BK, with the loss of C-terminal Arg, penetrates further. Arginine 103-106 kininogen 1 Homo sapiens 108-110 20923691-10 2011 Synthetic (Arg(0), Trp(5), Leu(8))-bradykinin was previously reported as having multiphasic effects on arterial blood pressure in conscious trout and here we have demonstrated that it can antagonize the relaxation in rat arterial smooth muscle induced by canonical mammalian bradykinin. Arginine 11-14 kininogen 1 Homo sapiens 35-45 20923691-10 2011 Synthetic (Arg(0), Trp(5), Leu(8))-bradykinin was previously reported as having multiphasic effects on arterial blood pressure in conscious trout and here we have demonstrated that it can antagonize the relaxation in rat arterial smooth muscle induced by canonical mammalian bradykinin. Arginine 11-14 kininogen 1 Homo sapiens 275-285 20923691-11 2011 The discovery of (Arg(0), Trp(5), Leu(8))-bradykinin in the defensive skin secretion of this amphibian completes the spectrum of vertebrate taxon-specific BRPs identified from this source. Arginine 18-21 kininogen 1 Homo sapiens 42-52 18085569-2 2007 We show that bradykinin and three modified peptides containing the basic residue arginine or lysine form stable interactions with single-stranded oligonucleotides. Arginine 81-89 kininogen 1 Homo sapiens 13-23 17327486-1 2007 The kinins, bradykinin (BK) and Lys-des[Arg(9)]-BK, are important inflammatory mediators that act via two specific G protein-coupled kinins, B(1) and B(2) receptors (B(2)R). Arginine 40-43 kininogen 1 Homo sapiens 48-50 17327486-6 2007 The kinin agonists BK and Lys-des[Arg(9)]-BK up-regulated the expression of their respective receptors. Arginine 34-37 kininogen 1 Homo sapiens 42-44 16616057-1 2006 BACKGROUND: Carboxypeptidase N is a plasma zinc metallocarboxypeptidase which is constitutively expressed in the liver and was identified as the enzyme responsible for inactivating bradykinin and kallidin by removing the C-terminal arginine. Arginine 232-240 kininogen 1 Homo sapiens 181-191 17266049-1 2007 High affinity peptide ligands for the bradykinin (BK) B(2) subtype receptor have been shown to adopt a beta-turn conformation of the C-terminal tetrapeptide (H-Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)-OH). Arginine 160-163 kininogen 1 Homo sapiens 38-48 17157876-6 2007 Modeling of the Pro-Phe-Arg C-terminal end of the natural substrate bradykinin into the active site shows that the S1" pocket of CPN1 might better accommodate P1"-Lys than Arg residues, in agreement with CPN"s preference for cleaving off C-terminal Lys residues. Arginine 24-27 kininogen 1 Homo sapiens 68-78 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. Arginine 140-143 kininogen 1 Homo sapiens 167-177 15040788-2 2004 Bradykinin was released from these peptides by the mK1- and rK1-mediated hydrolysis of Arg-Arg and Arg-Ser (or Arg-Ala) peptide bonds. Arginine 87-90 kininogen 1 Homo sapiens 0-10 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. Arginine 99-102 kininogen 1 Homo sapiens 26-36 15040788-2 2004 Bradykinin was released from these peptides by the mK1- and rK1-mediated hydrolysis of Arg-Arg and Arg-Ser (or Arg-Ala) peptide bonds. Arginine 91-94 kininogen 1 Homo sapiens 0-10 15040788-2 2004 Bradykinin was released from these peptides by the mK1- and rK1-mediated hydrolysis of Arg-Arg and Arg-Ser (or Arg-Ala) peptide bonds. Arginine 91-94 kininogen 1 Homo sapiens 0-10 15040788-2 2004 Bradykinin was released from these peptides by the mK1- and rK1-mediated hydrolysis of Arg-Arg and Arg-Ser (or Arg-Ala) peptide bonds. Arginine 91-94 kininogen 1 Homo sapiens 0-10 15040788-5 2004 One of these peptides, Abz-GFSPFRAPRVQ-EDDnp (where EDDnp stands for ethylenediamine 2,4-dinitrophenyl), was preferentially hydrolysed at the Phe-Arg bond, confirming the potential des-[Arg9]bradykinin-releasing activity of hK1 on rat kininogen. Arginine 146-149 kininogen 1 Homo sapiens 191-201 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. Arginine 212-215 kininogen 1 Homo sapiens 53-63