PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11809859-1 2002 Agonist activation of endogenous angiotensin II (Ang II) AT(1) receptors expressed in hepatic C9 cells markedly stimulated inositol phosphate production, phosphorylation of the proline-rich tyrosine kinase PyK-2, and ERK activation. Proline 177-184 angiotensinogen Homo sapiens 33-47 12676352-1 2003 The YIPP (tyrosine-isoleucine-proline-proline, amino acids 319-322) motif within the C-terminal part of the human AT(1) receptor is associated with angiotensin II (AII)-induced activation of the Jak-STAT pathway and phospholipase Cgamma1 phosphorylation. Proline 30-37 angiotensinogen Homo sapiens 148-162 12676352-1 2003 The YIPP (tyrosine-isoleucine-proline-proline, amino acids 319-322) motif within the C-terminal part of the human AT(1) receptor is associated with angiotensin II (AII)-induced activation of the Jak-STAT pathway and phospholipase Cgamma1 phosphorylation. Proline 30-37 angiotensinogen Homo sapiens 164-167 12676352-1 2003 The YIPP (tyrosine-isoleucine-proline-proline, amino acids 319-322) motif within the C-terminal part of the human AT(1) receptor is associated with angiotensin II (AII)-induced activation of the Jak-STAT pathway and phospholipase Cgamma1 phosphorylation. Proline 38-45 angiotensinogen Homo sapiens 148-162 12676352-1 2003 The YIPP (tyrosine-isoleucine-proline-proline, amino acids 319-322) motif within the C-terminal part of the human AT(1) receptor is associated with angiotensin II (AII)-induced activation of the Jak-STAT pathway and phospholipase Cgamma1 phosphorylation. Proline 38-45 angiotensinogen Homo sapiens 164-167 11809859-1 2002 Agonist activation of endogenous angiotensin II (Ang II) AT(1) receptors expressed in hepatic C9 cells markedly stimulated inositol phosphate production, phosphorylation of the proline-rich tyrosine kinase PyK-2, and ERK activation. Proline 177-184 angiotensinogen Homo sapiens 49-55 10585456-2 1999 We have identified a natural mutation at the -30 amino acid position of the angiotensinogen signal peptide, in which an arginine is replaced by a proline (R-30P). Proline 146-153 angiotensinogen Homo sapiens 76-91 11262415-0 2001 Down-regulation by antisense oligonucleotides establishes a role for the proline-rich tyrosine kinase PYK2 in angiotensin ii-induced signaling in vascular smooth muscle. Proline 73-80 angiotensinogen Homo sapiens 110-124 24226385-2 1994 The electrospray ionization mass spectra of histidine-containing human angiotensin II (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe) and angiotensin I (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu) in the presence of zinc show abundant multiply charged ions for the zinc-attached peptide [M + aZn(2+) +(c - 2a)H(+)](c+), where a = 1, 2 and c is charge. Proline 111-114 angiotensinogen Homo sapiens 71-85 24226385-2 1994 The electrospray ionization mass spectra of histidine-containing human angiotensin II (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe) and angiotensin I (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu) in the presence of zinc show abundant multiply charged ions for the zinc-attached peptide [M + aZn(2+) +(c - 2a)H(+)](c+), where a = 1, 2 and c is charge. Proline 111-114 angiotensinogen Homo sapiens 71-84 1524216-3 1992 The hydrolysis of Abz-His-Pro-Phe-His-Leu-Val-Ile-His-EDDnp by human renin was inhibited by a highly specific transition-state analog of angiotensinogen (IC50 = 7.8 x 10(-9) M), described by K. Iizuka et al. Proline 26-29 angiotensinogen Homo sapiens 137-152 1335995-0 1992 Bradykinin and angiotensin II analogs containing a conformationally constrained proline analog. Proline 80-87 angiotensinogen Homo sapiens 15-29 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 angiotensinogen Homo sapiens 39-53 8308464-5 1993 The unique and most important substitution in dogfish angiotensin I is a proline residue at position 3 which may cause significant changes in its tertiary structure. Proline 73-80 angiotensinogen Homo sapiens 54-67 8402653-5 1993 The proline at position 140 in mammalian AGTs is replaced by alanine in the Ada and yeast AGTs and by serine in the Ogt AGT. Proline 4-11 angiotensinogen Homo sapiens 41-44 8402653-6 1993 These results suggest that this proline residue affects the configuration of the active site allowing the O6-benzylguanine to enter and react with the mammalian AGT. Proline 32-39 angiotensinogen Homo sapiens 161-164 1797705-1 1991 The N-terminal heptadecapeptide of human angiotensinogen (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Asn-Glu-Ser-Thr-NH2 ), with the C-terminal carboxyl group amidated, was synthesized in order to study the role of Asn-Glu-Ser, a putative carbohydrate binding site, on the hydrolysis by human renin. Proline 82-85 angiotensinogen Homo sapiens 41-56 34853228-9 2021 Furthermore, PTV significantly suppressed the angiotensin-II-induced proline incorporation in primary cultured cardiac fibroblasts. Proline 69-76 angiotensinogen Homo sapiens 46-60 2471521-1 1989 (-)mRNA complementary to human angiotensin II (+)mRNA encodes the "antipeptide" Glu-Gly-Val-Tyr-Val-His-Pro-Val which is structurally related to angiotensin II. Proline 104-107 angiotensinogen Homo sapiens 31-45 2471521-1 1989 (-)mRNA complementary to human angiotensin II (+)mRNA encodes the "antipeptide" Glu-Gly-Val-Tyr-Val-His-Pro-Val which is structurally related to angiotensin II. Proline 104-107 angiotensinogen Homo sapiens 145-159 19034-2 1977 Titration studies of angiotensin I (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu) were also made, whose results indicated a flexible folded conformation similar to that previously proposed for the octapeptide angiotensin II, with a possible additional beta turn at the C terminus. Proline 60-63 angiotensinogen Homo sapiens 21-34 6385771-0 1984 Renin cleavage of a human kidney renin substrate analogous to human angiotensinogen, H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Ser-OH, that is human renin specific and is resistant to cathepsin D. Proline 111-114 angiotensinogen Homo sapiens 68-83 6385771-1 1984 A synthetic tetradecapeptide, H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Ser-OH, which corresponds to the 13 amino terminal residues of human angiotensinogen plus a carboxy terminal serine to replace a suggested site of carbohydrate attachment, has been shown to be a good substrate for human kidney renin. Proline 56-59 angiotensinogen Homo sapiens 153-168 7021592-7 1981 The amino acid sequence of 25 nmol of the peptide was Asp-Arg-Val-Try-Ile-His-Pro-Phe, the same covalent structure as that of angiotensin II. Proline 78-81 angiotensinogen Homo sapiens 126-140 2911013-3 1989 A carboxypeptidase activity that digested angiotensin I to des-Leu-angiotensin I, Ile-His-Pro-Phe to Ile-His-Pro and Phe, and hippuryl-L-phenylalanine to hippuric acid and Phe was detected in the granules of these NK cells. Proline 109-112 angiotensinogen Homo sapiens 42-55 3346064-3 1988 Replacement of the proline residue in position 7 with alanine reduced the pressor and vascular contractile response to less than 1% of Ang II. Proline 19-26 angiotensinogen Homo sapiens 135-141 3346064-5 1988 The results of pharmacological evaluation of various position 7-substituted analogues were as follows: 1) Replacement of proline in position 7 of angiotensin I (Ang I) and Ang II with primary amino acids produced cardiac-specific, positive inotropic properties. Proline 121-128 angiotensinogen Homo sapiens 146-159 3346064-5 1988 The results of pharmacological evaluation of various position 7-substituted analogues were as follows: 1) Replacement of proline in position 7 of angiotensin I (Ang I) and Ang II with primary amino acids produced cardiac-specific, positive inotropic properties. Proline 121-128 angiotensinogen Homo sapiens 161-166 3346064-5 1988 The results of pharmacological evaluation of various position 7-substituted analogues were as follows: 1) Replacement of proline in position 7 of angiotensin I (Ang I) and Ang II with primary amino acids produced cardiac-specific, positive inotropic properties. Proline 121-128 angiotensinogen Homo sapiens 172-178 2485065-3 1987 The minimal length for an effective substrate has been characterised as an octapeptide sequence derived from the amino terminal portion of angiotensinogen (residues 6----13): His-Pro-Phe-His-Leu-Val-Ile-His (Leu-Val is the scissile bond). Proline 179-182 angiotensinogen Homo sapiens 139-154 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 angiotensinogen Homo sapiens 214-228 6928653-1 1980 [1-Sarcosine,8-isoleucine]angiotensin II (Sar-Arg-Val-Tyr-Ile-His-Pro-Ile) has been shown to be a potent antagonist of the pressor action of angiotensin II. Proline 66-69 angiotensinogen Homo sapiens 26-40 6928653-1 1980 [1-Sarcosine,8-isoleucine]angiotensin II (Sar-Arg-Val-Tyr-Ile-His-Pro-Ile) has been shown to be a potent antagonist of the pressor action of angiotensin II. Proline 66-69 angiotensinogen Homo sapiens 141-155 13825-5 1977 The results obtained indicate that substitutions in aspartic acid 1, proline 7, and phenylalanine 8 of angiotensin II entail changes in the backbone conformation. Proline 69-76 angiotensinogen Homo sapiens 103-117 20977208-1 2010 The octapeptide angiotensin II (Ang II; Asp(1)-Arg(2)-Val(3)-Tyr(4)-Ile(5)-His(6)-Pro(7)-Phe(8)) is the primary active hormone of the renin/angiotensin system (RAS) and has been implicated in various cardiovascular diseases. Proline 82-85 angiotensinogen Homo sapiens 16-30 21963180-3 2011 In order to calculate the cis-trans isomerization rate constants of Ang I on the stationary phase"s surface, the first and second moments of the proline peptide elution profiles were determined. Proline 145-152 angiotensinogen Homo sapiens 68-73 21628446-4 2011 Chromatographic purification and structural analysis by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF) revealed an Ang II-like octapeptide, angioprotectin, with the sequence Pro-Glu-Val-Tyr-Ile-His-Pro-Phe, which differs from Ang II in Pro1 and Glu2 instead of Asp1 and Arg2. Proline 217-220 angiotensinogen Homo sapiens 158-164 21628446-5 2011 Pro-Glu-Val-Tyr-Ile-His-Pro-Phe in angioprotectin is most likely generated enzymatically from Ang II. Proline 0-3 angiotensinogen Homo sapiens 94-100 17239455-0 2007 Participation of transmembrane proline 82 in angiotensin II AT1 receptor signal transduction. Proline 31-38 angiotensinogen Homo sapiens 45-59 16220978-1 2005 Two 1,3,5-trisubstituted aromatic scaffolds intended to serve as gamma-turn mimetics have been synthesized and incorporated in five pseudopeptide analogues of angiotensin II (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe), replacing Val-Tyr-Ile, Val-Tyr, or Tyr-Ile. Proline 199-202 angiotensinogen Homo sapiens 159-173 19168184-3 2009 These results have been interpreted in terms of on-column cis-trans isomerization of angiotensin I (a proline containing polypeptide) followed by its "re-conformation" after the interaction with the support. Proline 102-109 angiotensinogen Homo sapiens 85-98 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 angiotensinogen Homo sapiens 167-180 17261087-3 2007 Mutant angiotensinogens in which the Ile-His-Pro-Phe-His-Leu sequence at positions 5-10 of wild-type angiotensinogen was replaced by either His-Pro-Phe-His-Leu-Leu or Ala-Ile-His-Pro-Phe-His were cleaved by renin at the C-terminal side of residues 9 and 11, respectively, while wild-type angiotensinogen was cleaved at residue 10. Proline 45-48 angiotensinogen Homo sapiens 7-22