PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20158486-4 2010 D-Lys6-GnRH and [Asn1-Val5]-angiotensin II were modified at their histidine side chain within the peptide, whilst IGF-1 (1-3) was modified at the C-terminal glutamic acid residue. Histidine 66-75 angiotensinogen Homo sapiens 28-42 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]. Histidine 196-199 angiotensinogen Homo sapiens 155-168 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]. Histidine 214-217 angiotensinogen Homo sapiens 155-168 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. Histidine 75-78 angiotensinogen Homo sapiens 16-30 28508285-6 2017 Reactions between HNO3 and histidine residues in AI and AII resulted in the formation of dominant [MAI-H+(HNO3)]- and [MAII-H+(HNO3)]- ions. Histidine 27-36 angiotensinogen Homo sapiens 56-59 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. Histidine 237-240 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. Histidine 20-23 angiotensinogen Homo sapiens 94-100 20497104-4 2010 D-Lys6-GnRH and [Asn1-Val5]-angiotensin II were modified at their histidine side chain within the peptide, whilst IGF-1 (1-3) was modified at the C-terminal glutamic acid residue. Histidine 66-75 angiotensinogen Homo sapiens 28-42 19928803-10 2010 Through the detection of a Lim-2-OOH adduct bound at the first histidine (of two) of angiotensin I, it was confirmed that hydroperoxides have the potential to form specific antigens in contact allergy. Histidine 63-72 angiotensinogen Homo sapiens 85-98 17261087-0 2007 The His-Pro-Phe motif of angiotensinogen is a crucial determinant of the substrate specificity of renin. Histidine 4-7 angiotensinogen Homo sapiens 25-40 17261087-1 2007 The amino acid sequence His-Pro-Phe as N-terminal residues 6-8 of the natural renin substrate, angiotensinogen, is conserved among species. Histidine 24-27 angiotensinogen Homo sapiens 95-110 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. Histidine 41-44 angiotensinogen Homo sapiens 7-22 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. Histidine 124-127 angiotensinogen Homo sapiens 149-162 15942685-7 2005 These findings, therefore, indicate that histidine residues at both P2 and P3" positions probably associate with the renin catalytic reaction for angiotensin I generation. Histidine 41-50 angiotensinogen Homo sapiens 146-159 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. Histidine 53-56 angiotensinogen Homo sapiens 7-22 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. Histidine 53-56 angiotensinogen Homo sapiens 7-22 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. Histidine 53-56 angiotensinogen Homo sapiens 7-22 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. Histidine 53-56 angiotensinogen Homo sapiens 7-22 17261087-4 2007 A triple Ala substitution for the His-Pro-Phe motif of angiotensinogen prevented its cleavage by renin. Histidine 34-37 angiotensinogen Homo sapiens 55-70 17261087-7 2007 These results indicate that the His-Pro-Phe motif of angiotensinogen is a crucial determinant of the substrate specificity of renin. Histidine 32-35 angiotensinogen Homo sapiens 53-68 16872275-5 2006 Histidine residues within the unique N-terminal extension of AGT appear to influence polymer formation, although polymer formation can still take place after their removal by renin. Histidine 0-9 angiotensinogen Homo sapiens 61-64 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. Histidine 195-198 angiotensinogen Homo sapiens 159-173 7775978-0 1995 Cu(II) binding by angiotensin II fragments: Asp-Arg-Val-Tyr-Ile-His and Arg-Val-Tyr-Ile-His. Histidine 64-67 angiotensinogen Homo sapiens 18-32 15537355-4 2004 Conformational analysis, using experimental constraints derived from NMR studies, indicated that the Tyr(4) and His(6) residues in one of the angiotensin II analogues were in close proximity to each other. Histidine 112-115 angiotensinogen Homo sapiens 142-156 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. Histidine 100-103 angiotensinogen Homo sapiens 52-55 8817875-1 1996 Angiotensin-converting enzyme (ACE; EN 3.4.15.1) is a peptidyl dipeptide hydrolase that removes the carboxyl terminal His-Leu from angiotensin I to produce the octapeptide angiotensin II. Histidine 118-121 angiotensinogen Homo sapiens 131-144 8817875-1 1996 Angiotensin-converting enzyme (ACE; EN 3.4.15.1) is a peptidyl dipeptide hydrolase that removes the carboxyl terminal His-Leu from angiotensin I to produce the octapeptide angiotensin II. Histidine 118-121 angiotensinogen Homo sapiens 172-186 12729654-4 2003 An example of a novel synthetic non-peptide molecule is given which mimics the His(6)-Pro(7)-Phe(8) part of Ang II and is based on the (S)-pyroglutamic acid. Histidine 79-82 angiotensinogen Homo sapiens 108-114 12036910-5 2002 The facile reaction of this cysteine residue with NO is attributable to its interaction with other residues in hAGT including His-146 and Glu-172 that activate the sulfhydryl group of Cys-145 to allow its nucleophilic attack on DNA adducts. Histidine 126-129 angiotensinogen Homo sapiens 111-115 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Histidine 12-15 angiotensinogen Homo sapiens 46-49 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Histidine 12-15 angiotensinogen Homo sapiens 51-64 8836769-10 1996 A dipeptide His-Leu carboxy-extension form of AII, angiotensin I (AI), only bound to anti-AII abs at 100-200 times higher concentrations, showing that the C-terminal epitope was blocked by the dipeptide. Histidine 12-15 angiotensinogen Homo sapiens 90-93 7775978-2 1995 Potentiometric and spectroscopic (absorption, circular dichroism and electron paramagnetic resonance) study on the coordination of two angiotensin II fragments (Asp-Arg-Val-Tyr-Ile-His and Arg-Val-Tyr-Ile-His) to Cu(II) ions has shown that competition between amino and imidazole nitrogens to anchor metal ions is a complicated process and may lead to formation of macrochelate rings. Histidine 181-184 angiotensinogen Homo sapiens 135-149 7775978-2 1995 Potentiometric and spectroscopic (absorption, circular dichroism and electron paramagnetic resonance) study on the coordination of two angiotensin II fragments (Asp-Arg-Val-Tyr-Ile-His and Arg-Val-Tyr-Ile-His) to Cu(II) ions has shown that competition between amino and imidazole nitrogens to anchor metal ions is a complicated process and may lead to formation of macrochelate rings. Histidine 205-208 angiotensinogen Homo sapiens 135-149 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. Histidine 44-53 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. Histidine 44-53 angiotensinogen Homo sapiens 71-84 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. Histidine 107-110 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. Histidine 107-110 angiotensinogen Homo sapiens 71-84 1499089-2 1992 The reaction products after in vitro incubation of Angiotensin I with styrene oxide, a well known carcinogen, under different conditions, have been characterized: a prominent reactivity of several potential nucleophilic sites of Angiotensin I was shown, including two histidine residues and a tyrosine residue; it is worth noting that it has never been stated that tyrosine is highly reactive with styrene oxide. Histidine 268-277 angiotensinogen Homo sapiens 51-64 1499089-2 1992 The reaction products after in vitro incubation of Angiotensin I with styrene oxide, a well known carcinogen, under different conditions, have been characterized: a prominent reactivity of several potential nucleophilic sites of Angiotensin I was shown, including two histidine residues and a tyrosine residue; it is worth noting that it has never been stated that tyrosine is highly reactive with styrene oxide. Histidine 268-277 angiotensinogen Homo sapiens 229-242 2241171-0 1990 Site-specific oxidation of angiotensin I by copper(II) and L-ascorbate: conversion of histidine residues to 2-imidazolones. Histidine 86-95 angiotensinogen Homo sapiens 27-40 1316850-1 1992 Angiotensin-I-converting enzyme (ACE) is a peptidyl-dipeptide hydrolase which splits off the dipeptide His-Leu from the decapeptide angiotensin I and thus converts it to angiotensin II. Histidine 103-106 angiotensinogen Homo sapiens 132-145 1316850-1 1992 Angiotensin-I-converting enzyme (ACE) is a peptidyl-dipeptide hydrolase which splits off the dipeptide His-Leu from the decapeptide angiotensin I and thus converts it to angiotensin II. Histidine 103-106 angiotensinogen Homo sapiens 170-184 1799223-3 1991 We considered whether a commercially available synthetic tetradecapeptide (TDP), Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, would produce authentic Ang I upon incubation with protease from human immunodeficiency virus type 1 (HIV-1). Histidine 101-104 angiotensinogen Homo sapiens 162-167 1799223-3 1991 We considered whether a commercially available synthetic tetradecapeptide (TDP), Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, would produce authentic Ang I upon incubation with protease from human immunodeficiency virus type 1 (HIV-1). Histidine 113-116 angiotensinogen Homo sapiens 162-167 1894611-1 1991 We have recently identified and characterized a chymotrypsin-like serine proteinase in human heart (human heart chymase) that is the most catalytically efficient enzyme described, thus far, for the cleavage of angiotensin I to yield angiotensin II and the dipeptide His-Leu. Histidine 266-269 angiotensinogen Homo sapiens 210-223 1894611-1 1991 We have recently identified and characterized a chymotrypsin-like serine proteinase in human heart (human heart chymase) that is the most catalytically efficient enzyme described, thus far, for the cleavage of angiotensin I to yield angiotensin II and the dipeptide His-Leu. Histidine 266-269 angiotensinogen Homo sapiens 233-247 2016986-3 1991 This ACP activity co-eluted with activity that cleaved histidine from des-Leu angiotensin I to form angiotensin II and activity that cleaved tyrosine from benzyloxycarbonyl-glutamyl-tyrosine (ZGT). Histidine 55-64 angiotensinogen Homo sapiens 78-91 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. Histidine 22-25 angiotensinogen Homo sapiens 137-152 1918036-1 1991 Human heart chymase, a chymotrypsin-like serine proteinase that hydrolyzes the Phe8-His9 bond in angiotensin I (Ang I) to yield the octapeptide hormone angiotensin II (Ang II) and His-Leu, is the most specific, efficient Ang II-forming enzyme described. Histidine 84-87 angiotensinogen Homo sapiens 97-110 1918036-1 1991 Human heart chymase, a chymotrypsin-like serine proteinase that hydrolyzes the Phe8-His9 bond in angiotensin I (Ang I) to yield the octapeptide hormone angiotensin II (Ang II) and His-Leu, is the most specific, efficient Ang II-forming enzyme described. Histidine 84-87 angiotensinogen Homo sapiens 112-117 1918036-1 1991 Human heart chymase, a chymotrypsin-like serine proteinase that hydrolyzes the Phe8-His9 bond in angiotensin I (Ang I) to yield the octapeptide hormone angiotensin II (Ang II) and His-Leu, is the most specific, efficient Ang II-forming enzyme described. Histidine 84-87 angiotensinogen Homo sapiens 152-166 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. Histidine 78-81 angiotensinogen Homo sapiens 41-56 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. Histidine 90-93 angiotensinogen Homo sapiens 41-56 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. Histidine 90-93 angiotensinogen Homo sapiens 41-56 2241171-1 1990 The reaction of a histidine-containing peptide (angiotensin I) with copper (II)/ascorbate under physiological conditions has been studied chemically. Histidine 18-27 angiotensinogen Homo sapiens 48-61 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. Histidine 17-20 angiotensinogen Homo sapiens 40-54 2356159-6 1990 Connectivities between the His C alpha proton and the two Pro C delta protons illustrated a preferred conformation for angiotensin II in DMSO in which the His-Pro bond exists as the trans isomer. Histidine 27-30 angiotensinogen Homo sapiens 119-133 34356603-1 2021 Angiotensin II (Ang II) may contain a charge relay system (CRS) involving Tyr/His/carboxylate, which creates a tyrosinate anion for receptor activation. Histidine 78-81 angiotensinogen Homo sapiens 0-23 2175370-3 1990 In addition, there is mounting evidence, collected mostly in experiments in vitro, that other enzymes may be able to activate angiotensin I, for example by the stepwise release of the C-terminal His and Leu residues. Histidine 195-198 angiotensinogen Homo sapiens 126-139 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. Histidine 100-103 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. Histidine 100-103 angiotensinogen Homo sapiens 145-159 3351849-0 1988 The importance of residues 2 (arginine) and 6 (histidine) in high-affinity angiotensin II antagonists. Histidine 47-56 angiotensinogen Homo sapiens 75-89 3351849-1 1988 The structure-antagonist activity relationship is described for analogues of [Sar1,Ile8]angiotensin II substituted in position 2 (arginine) and position 6 (histidine). Histidine 156-165 angiotensinogen Homo sapiens 88-102 3351849-3 1988 Evidence is presented suggesting that the position 6 histidine side chain in angiotensin II (AII) is not involved in receptor stimulation. Histidine 53-62 angiotensinogen Homo sapiens 77-91 6743343-0 1984 NMR studies on angiotensin II: histidine and phenylalanine ring stacking and biological activity. Histidine 31-40 angiotensinogen Homo sapiens 15-29 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). Histidine 187-190 angiotensinogen Homo sapiens 139-154 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). Histidine 187-190 angiotensinogen Homo sapiens 139-154 3741422-1 1986 Angiotensin II, the potent hypertensive octapeptide, can be generated by a sequential cleavage of the carboxyl-terminal leucine and histidine from angiotensin I by a human renal extract. Histidine 132-141 angiotensinogen Homo sapiens 0-14 3741422-1 1986 Angiotensin II, the potent hypertensive octapeptide, can be generated by a sequential cleavage of the carboxyl-terminal leucine and histidine from angiotensin I by a human renal extract. Histidine 132-141 angiotensinogen Homo sapiens 147-160 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. Histidine 120-123 angiotensinogen Homo sapiens 85-98 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. Histidine 132-135 angiotensinogen Homo sapiens 85-98 6496943-1 1984 The chemical shifts of the isoleucine and histidine protons of angiotensin I were assigned and the chemical shifts of the protons of the other amino acids in the peptide were confirmed at a field strength of 400 MHz. Histidine 42-51 angiotensinogen Homo sapiens 63-76 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. Histidine 107-110 angiotensinogen Homo sapiens 68-83 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. Histidine 119-122 angiotensinogen Homo sapiens 68-83 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. Histidine 119-122 angiotensinogen Homo sapiens 68-83 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). Histidine 175-178 angiotensinogen Homo sapiens 139-154 4086164-2 1985 The possible existence of intramolecular interactions involving the tyrosine and histidine residues in angiotensin II has been investigated by measuring the reactivities of the functional groups in the molecule. Histidine 81-90 angiotensinogen Homo sapiens 103-117 3911093-4 1985 Cathepsin B hydrolyzed angiotensin I via a dipeptidyl carboxypeptidase mechanism removing His-Leu to form angiotensin II, and it degraded angiotensin II as an endopeptidase at the Val3-Tyr4 bond. Histidine 90-93 angiotensinogen Homo sapiens 23-36 6743343-3 1984 The chemical shifts for the histidine C2 and C4 protons in angiotensin II also indicate shielding, whereas these same protons in the antagonist [Sar1, Ile8]angiotensin II do not demonstrate this shielding influence. Histidine 28-37 angiotensinogen Homo sapiens 59-73 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. Histidine 54-63 angiotensinogen Homo sapiens 97-111 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. Histidine 52-55 angiotensinogen Homo sapiens 153-168 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. Histidine 64-67 angiotensinogen Homo sapiens 153-168 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. Histidine 64-67 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. Histidine 56-59 angiotensinogen Homo sapiens 21-34 6696878-7 1984 The amino-terminal sequence contained the covalent structure of angiotensin I and was Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-X-Glu-Ser-Thr-Cys-Gl u-. Histidine 106-109 angiotensinogen Homo sapiens 64-77 6696878-7 1984 The amino-terminal sequence contained the covalent structure of angiotensin I and was Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-X-Glu-Ser-Thr-Cys-Gl u-. Histidine 118-121 angiotensinogen Homo sapiens 64-77 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. Histidine 62-65 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. Histidine 62-65 angiotensinogen Homo sapiens 141-155 6928653-6 1980 The results indicated that: (i) angiotensin II and [1-sarcosine,8-isoleucine]angiotensin II gave practically identical spectroscopic data; and (ii) N-methylation in either position 4 or position 5 resulted in remarkable changes in the peptide backbone and a severe limitation in rotational freedom of side chains in tyrosine, isoleucine, and histidine residues. Histidine 342-351 angiotensinogen Homo sapiens 32-46 6928653-6 1980 The results indicated that: (i) angiotensin II and [1-sarcosine,8-isoleucine]angiotensin II gave practically identical spectroscopic data; and (ii) N-methylation in either position 4 or position 5 resulted in remarkable changes in the peptide backbone and a severe limitation in rotational freedom of side chains in tyrosine, isoleucine, and histidine residues. Histidine 342-351 angiotensinogen Homo sapiens 77-91