PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. Phenylalanine 94-97 angiotensinogen Homo sapiens 42-55 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. Phenylalanine 117-120 angiotensinogen Homo sapiens 42-55 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. Phenylalanine 117-120 angiotensinogen Homo sapiens 42-55 25688208-1 2015 Angiotensin converting enzyme 2 (ACE2) is a zinc carboxypeptidase involved in the renin-angiotensin system (RAS) and inactivates the potent vasopressive peptide angiotensin II (Ang II) by removing the C-terminal phenylalanine residue to yield Ang1-7. Phenylalanine 212-225 angiotensinogen Homo sapiens 161-175 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. Phenylalanine 60-63 angiotensinogen Homo sapiens 153-168 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. Phenylalanine 64-67 angiotensinogen Homo sapiens 21-34 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. Phenylalanine 84-97 angiotensinogen Homo sapiens 103-117 27591418-10 2016 Furthermore, the values obtained from the present method were in agreement with the result from isotope dilution quantification using isotopically labeled angiotensin I [Asp-Arg-(Val-d8 )-Tyr-Ile-His-Pro-(Phe-d8 )-His-Leu]. Phenylalanine 205-208 angiotensinogen Homo sapiens 155-168 25688208-1 2015 Angiotensin converting enzyme 2 (ACE2) is a zinc carboxypeptidase involved in the renin-angiotensin system (RAS) and inactivates the potent vasopressive peptide angiotensin II (Ang II) by removing the C-terminal phenylalanine residue to yield Ang1-7. Phenylalanine 212-225 angiotensinogen Homo sapiens 177-183 3143010-1 1988 Dipeptide analogues of angiotensinogen utilizing a structurally modified phenylalanine residue to impart proteolytic stability. Phenylalanine 73-86 angiotensinogen Homo sapiens 23-38 3390186-5 1988 For the proposed His:Phe interaction in angiotensin II, the attraction will be three times greater when the imidazole ring carries a negative charge. Phenylalanine 21-24 angiotensinogen Homo sapiens 40-54 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). Phenylalanine 183-186 angiotensinogen Homo sapiens 139-154 3081342-6 1986 Both major forms have the same amino-terminal sequence, which includes that of ovine angiotensin I: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu. Phenylalanine 128-131 angiotensinogen Homo sapiens 85-98 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. Phenylalanine 115-118 angiotensinogen Homo sapiens 68-83 6743343-0 1984 NMR studies on angiotensin II: histidine and phenylalanine ring stacking and biological activity. Phenylalanine 45-58 angiotensinogen Homo sapiens 15-29 6743343-2 1984 The chemical shifts for the aromatic protons of the phenylalanine residue in angiotensin II are consistent with shielding and restricted rotation for this side-chain. Phenylalanine 52-65 angiotensinogen Homo sapiens 77-91 6743343-4 1984 These findings suggest a stacking interaction for the histidine and phenylalanine side-chains in angiotensin II which is important for activating angiotensin receptors. Phenylalanine 68-81 angiotensinogen Homo sapiens 97-111 6352693-7 1983 The enzyme was found to hydrolyze peptide bonds preferentially at the amino sides of hydrophobic amino acids such as Leu and Phe, when its specificity was studied using insulin B chain and angiotensin I. Phenylalanine 125-128 angiotensinogen Homo sapiens 189-202 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. Phenylalanine 82-85 angiotensinogen Homo sapiens 126-140 24327206-4 2014 Ang II increased ~45 % cell surface area (CSA) and ~37 % [(3)H]-phenylalanine incorporation, effects that were blocked not only by losartan (Los) but also by BQ123 (AT1 and ETA receptor antagonists, respectively). Phenylalanine 64-77 angiotensinogen Homo sapiens 0-6 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. Phenylalanine 245-248 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. Phenylalanine 28-31 angiotensinogen Homo sapiens 94-100 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. Phenylalanine 89-92 angiotensinogen Homo sapiens 16-30 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. Phenylalanine 49-52 angiotensinogen Homo sapiens 7-22 20544751-3 2010 The complex [Ru(eta(6)-C(10)H(8))(Cp)](+) was also used for selective labeling of Tyr and Phe residues of small peptides, namely, angiotensin I and II derivatives. Phenylalanine 90-93 angiotensinogen Homo sapiens 130-150 18656443-5 2008 The main products of Ang III metabolized by rPRCP(40) were Ang 2-7 plus phenylalanine as determined by LC-MS. Angiotensin I (Ang I) blocked the metabolism of Ang III by rPRCP(40). Phenylalanine 72-85 angiotensinogen Homo sapiens 110-123 18656443-5 2008 The main products of Ang III metabolized by rPRCP(40) were Ang 2-7 plus phenylalanine as determined by LC-MS. Angiotensin I (Ang I) blocked the metabolism of Ang III by rPRCP(40). Phenylalanine 72-85 angiotensinogen Homo sapiens 21-26 34758666-7 2022 Four known SNPs as well as a new locus were found associated with PHE, which were rs2493134 (AGT), rs9349379 (PHACTR1), rs1371182 (CYP2C56P-PRPS1P1), rs567481079 (CYP2C56P-PRPS1P1), and chr14:61734822 (HIF1A). Phenylalanine 66-69 angiotensinogen Homo sapiens 93-96 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. Phenylalanine 136-139 angiotensinogen Homo sapiens 149-162 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. Phenylalanine 203-206 angiotensinogen Homo sapiens 159-173 15890659-1 2005 The peptide hormone angiotensin II (AngII) binds to the AT0 (angiotensin type 1) receptor within the transmembrane domains in an extended conformation, and its C-terminal residue interacts with transmembrane domain VII at Phe-293/Asn-294. Phenylalanine 222-225 angiotensinogen Homo sapiens 20-34 15890659-1 2005 The peptide hormone angiotensin II (AngII) binds to the AT0 (angiotensin type 1) receptor within the transmembrane domains in an extended conformation, and its C-terminal residue interacts with transmembrane domain VII at Phe-293/Asn-294. Phenylalanine 222-225 angiotensinogen Homo sapiens 36-41 9892138-15 1999 AngII (1-7) is obtained by deletion of phenylalanine at the C terminus. Phenylalanine 39-52 angiotensinogen Homo sapiens 0-5 8836769-9 1996 By use of a capture competition ELISA, the C-terminal Pro-Phe epitope of photoconjugated AII with the sequence DRVYIHPF was shown to bind specifically to antiAII antibodies (anti-AII abs), although antibodies against both the C- and N-terminal epitopes were present in the assay. Phenylalanine 58-61 angiotensinogen Homo sapiens 89-92 8836769-9 1996 By use of a capture competition ELISA, the C-terminal Pro-Phe epitope of photoconjugated AII with the sequence DRVYIHPF was shown to bind specifically to antiAII antibodies (anti-AII abs), although antibodies against both the C- and N-terminal epitopes were present in the assay. Phenylalanine 58-61 angiotensinogen Homo sapiens 158-161 8106515-3 1994 Irradiation of C alpha H, C2H, and C4H proton resonances in ANG II and [Sar1]ANG II resulted in enhancements of Tyr and Phe ring proton resonances, indicating that the three aromatic rings cluster together. Phenylalanine 120-123 angiotensinogen Homo sapiens 60-66 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. Phenylalanine 86-89 angiotensinogen Homo sapiens 41-56 11901215-6 2002 AngII-induced receptor phosphorylation was significantly inhibited by several substitutions at Phe(8) as well as alanine replacement of Asp(1). Phenylalanine 95-98 angiotensinogen Homo sapiens 0-5 11527428-3 2001 Indeed, the model brings in contact the residues of AII responsible for agonistic activity, Tyr(4), His(6), and Phe(8), with many residues of AT-1 involved in signal transduction according to site-directed mutagenesis. Phenylalanine 112-115 angiotensinogen Homo sapiens 52-55 9843384-7 1998 Both the R state of the receptor and the Tyr4 Ang II dependence of receptor activation can be reinstated by introduction of a larger sized Phe side chain at the 111 position in CR18, suggesting that the CR18 mutation generated an effect similar to the reduction of side chain size in the N111G mutation. Phenylalanine 139-142 angiotensinogen Homo sapiens 46-52 8620603-4 1996 However, 100 nmol/L Ang II did increase [3H]phenylalanine incorporation into neonatal cardiocyte protein over a 24-hour period by 10%, whereas passive load increased [3H]phenylalanine incorporation into protein by 30%, which was not blocked by [Sar1, Ile8]Ang II. Phenylalanine 44-57 angiotensinogen Homo sapiens 20-26 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. Phenylalanine 115-118 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. Phenylalanine 115-118 angiotensinogen Homo sapiens 71-84 1920354-10 1991 Incorporation of the L,L-lactam-Phe modification into [Sar1]ANG II gives a pure ANG II antagonist (pA2 8.3), comparable to saralasin (pA2 8.6). Phenylalanine 32-35 angiotensinogen Homo sapiens 60-66 1920354-10 1991 Incorporation of the L,L-lactam-Phe modification into [Sar1]ANG II gives a pure ANG II antagonist (pA2 8.3), comparable to saralasin (pA2 8.6). Phenylalanine 32-35 angiotensinogen Homo sapiens 80-86