PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 renin Homo sapiens 134-139 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 renin Homo sapiens 175-180 17261087-0 2007 The His-Pro-Phe motif of angiotensinogen is a crucial determinant of the substrate specificity of renin. Histidine 4-7 renin Homo sapiens 98-103 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 renin Homo sapiens 78-83 17261087-2 2007 We investigated whether this His-Pro-Phe motif functions as the determinant of the substrate specificity of renin. Histidine 29-32 renin Homo sapiens 108-113 17261087-4 2007 A triple Ala substitution for the His-Pro-Phe motif of angiotensinogen prevented its cleavage by renin. Histidine 34-37 renin Homo sapiens 97-102 17261087-6 2007 Furthermore, the 33-residue C-terminal peptide of human megsin, which carries a naturally occurring His-Pro-Phe sequence, was cleaved by renin at the C-terminal side of the His-Pro-Phe-Leu-Phe sequence. Histidine 100-103 renin Homo sapiens 137-142 17261087-6 2007 Furthermore, the 33-residue C-terminal peptide of human megsin, which carries a naturally occurring His-Pro-Phe sequence, was cleaved by renin at the C-terminal side of the His-Pro-Phe-Leu-Phe sequence. Histidine 173-176 renin Homo sapiens 137-142 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 renin Homo sapiens 126-131 17261087-8 2007 By binding to a corresponding pocket on renin, the His-Pro-Phe motif may act as a molecular anchor to recruit the scissile peptide bond to a favorable site for catalysis. Histidine 51-54 renin Homo sapiens 40-45 8107115-1 1994 The structure of mouse submaxillary renin complexed with a decapeptide inhibitor, CH-66 (Piv-His-Pro-Phe-His-Leu-OH-Leu-Tyr-Tyr-Ser-NH2), where Piv denotes a pivaloyl blocking group, and -OH- denotes a hydroxyethylene (-(S)CHOH-CH2-) transition state isostere as a scissile bond surrogate, has been refined to an agreement factor of 0.18 at 2.0 A resolution. Histidine 93-96 renin Homo sapiens 36-41 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 renin Homo sapiens 117-122 9388263-1 1997 It has been shown that the relative reaction preference of the C4 thiol ester toward oxygen and nitrogen nucleophiles upon activation by proteinase depends on whether residue 1106 is aspartate or histidine (Dodds, A. W., Ren, X.-D., Willis, A. C., and Law, S. K. A. Histidine 196-205 renin Homo sapiens 221-224 9352462-2 1997 In vitro, peptide Piv-His-Pro-Phe-His-Leu-psi[CH(OH)CH2]Leu-Tyr-Tyr-Ser-NH2(XXI) is the most potent inhibitor of rat plasma renin reported having an IC50 of 0.21 nM; it is a much weaker inhibitor of human renin (IC50 45 nM). Histidine 22-25 renin Homo sapiens 205-210 9352462-2 1997 In vitro, peptide Piv-His-Pro-Phe-His-Leu-psi[CH(OH)CH2]Leu-Tyr-Tyr-Ser-NH2(XXI) is the most potent inhibitor of rat plasma renin reported having an IC50 of 0.21 nM; it is a much weaker inhibitor of human renin (IC50 45 nM). Histidine 34-37 renin Homo sapiens 205-210 9273895-4 1997 Peptide Boc-His-Pro-Phe-His-Sta-Val-Ile-His-NH2 (VI) is the best inhibitor of human renin containing Sta at position 10. Histidine 12-15 renin Homo sapiens 84-89 9273895-4 1997 Peptide Boc-His-Pro-Phe-His-Sta-Val-Ile-His-NH2 (VI) is the best inhibitor of human renin containing Sta at position 10. Histidine 24-27 renin Homo sapiens 84-89 9273895-4 1997 Peptide Boc-His-Pro-Phe-His-Sta-Val-Ile-His-NH2 (VI) is the best inhibitor of human renin containing Sta at position 10. Histidine 24-27 renin Homo sapiens 84-89 7493993-3 1995 A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. Histidine 143-146 renin Homo sapiens 128-133 7663352-10 1995 However, it is possible to see that the specific interactions that renin makes with histidine at P2 would not be possible in the case of the other enzymes. Histidine 84-93 renin Homo sapiens 67-72 7678159-8 1993 In addition, structurally related non-histidine containing renin inhibitors showed absolutely no increase in the number of revertant colonies. Histidine 38-47 renin Homo sapiens 59-64 8512070-2 1993 The substrate, DABCYL-gaba-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-EDANS, has been designed to incorporate the renin cleavage site that occurs in the N-terminal peptide of human angiotensinogen. Histidine 31-34 renin Homo sapiens 111-116 8512070-2 1993 The substrate, DABCYL-gaba-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-EDANS, has been designed to incorporate the renin cleavage site that occurs in the N-terminal peptide of human angiotensinogen. Histidine 43-46 renin Homo sapiens 111-116 7678159-10 1993 A second line of evidence showing parallelism to growth enhancing compounds concerns the comutagenicity of histidine containing renin inhibitors. Histidine 107-116 renin Homo sapiens 128-133 1443599-1 1992 The angiotensin I-based peptide Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Glu-Glu-Ser yields angiotensin I (Ang I) and Leu-Glu-Glu-Ser upon hydrolysis by the human immunodeficiency virus type 1 (HIV-1) protease, but not by human renin. Histidine 52-55 renin Homo sapiens 231-236 1812733-0 1991 Substrate analogue renin inhibitors containing replacements of histidine in P2 or isosteres of the amide bond between P3 and P2 sites. Histidine 63-72 renin Homo sapiens 19-24 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 renin Homo sapiens 69-74 1524216-7 1992 Therefore, specific and sensitive substrates for the continuous assay of human renin in which as little as 70 microGU of human renin could be detected by Abz-Phe-His-Leu-Val-Ile-His-EDDnp were described. Histidine 162-165 renin Homo sapiens 79-84 1524216-7 1992 Therefore, specific and sensitive substrates for the continuous assay of human renin in which as little as 70 microGU of human renin could be detected by Abz-Phe-His-Leu-Val-Ile-His-EDDnp were described. Histidine 162-165 renin Homo sapiens 127-132 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 renin Homo sapiens 302-307 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 renin Homo sapiens 302-307 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 renin Homo sapiens 302-307 1799412-6 1991 A novel derivative of the fluorogenic substrate, containing a 3-methyl histidine substitution at the P2 site, was used to test the recent hypothesis that renin functions by virtue of substrate-directed catalysis. Histidine 71-80 renin Homo sapiens 154-159 1716913-1 1991 A metal binding peptide, hexahistidine, preceding a renin cleavage sequence (Pro-Phe-His-Leu-Val-Ile-His-) was engineered on to the N-terminus of HIV-1 reverse transcriptase (RT). Histidine 85-88 renin Homo sapiens 52-57 2520246-1 1989 Fast-atom bombardment mass spectrometry of a synthetic renin substrate decapeptide (Pro-His-Pro-Phe-His-Leu-Val-Ile-His-D-Lys) indicated the presence of several side-products, including a component 12 Da higher in mass. Histidine 88-91 renin Homo sapiens 55-60 2266553-2 1990 The aspartic proteinase, endothiapepsin (EC 3.4.23.6), was complexed with a highly potent renin inhibitor, H-261 (t-Boc-His-Pro-Phe-His-LeuOHVal-Ile-His), where OH denotes a hydroxyethylene (-(S) CHOH-CH2-) transition-state isostere in the scissile bond surrogate. Histidine 120-123 renin Homo sapiens 90-95 2266553-2 1990 The aspartic proteinase, endothiapepsin (EC 3.4.23.6), was complexed with a highly potent renin inhibitor, H-261 (t-Boc-His-Pro-Phe-His-LeuOHVal-Ile-His), where OH denotes a hydroxyethylene (-(S) CHOH-CH2-) transition-state isostere in the scissile bond surrogate. Histidine 132-135 renin Homo sapiens 90-95 2184838-3 1990 Finally, the results using the above plasma ANGs extend previous studies showing that the substrate specificity of human renin may be influenced by the amino acid residues at P2 (i.e., Ile, Val, or Tyr) and P3 (i.e., His or Tyr) sites. Histidine 217-220 renin Homo sapiens 121-126 2186807-1 1990 Steady-state kinetic analysis of human renin demonstrates the histidine proximal to the substrate scissile peptide bond contributes to the unique specificity and pH dependence of this aspartyl protease. Histidine 62-71 renin Homo sapiens 39-44 2186807-4 1990 Renin pH dependence was evaluated between pH 4.0 and 8.0 by using a synthetic substrate identical with the amino terminus of porcine angiotensinogen (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu*Leu-Val-Tyr-Ser, where the asterisk indicates the scissile peptide bond and the proximal histidine is in italics) and an analogous tetradecapeptide where the proximal histidine was substituted with glutamine. Histidine 170-173 renin Homo sapiens 0-5 2186807-4 1990 Renin pH dependence was evaluated between pH 4.0 and 8.0 by using a synthetic substrate identical with the amino terminus of porcine angiotensinogen (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu*Leu-Val-Tyr-Ser, where the asterisk indicates the scissile peptide bond and the proximal histidine is in italics) and an analogous tetradecapeptide where the proximal histidine was substituted with glutamine. Histidine 182-185 renin Homo sapiens 0-5 2186807-4 1990 Renin pH dependence was evaluated between pH 4.0 and 8.0 by using a synthetic substrate identical with the amino terminus of porcine angiotensinogen (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu*Leu-Val-Tyr-Ser, where the asterisk indicates the scissile peptide bond and the proximal histidine is in italics) and an analogous tetradecapeptide where the proximal histidine was substituted with glutamine. Histidine 279-288 renin Homo sapiens 0-5 2186807-4 1990 Renin pH dependence was evaluated between pH 4.0 and 8.0 by using a synthetic substrate identical with the amino terminus of porcine angiotensinogen (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu*Leu-Val-Tyr-Ser, where the asterisk indicates the scissile peptide bond and the proximal histidine is in italics) and an analogous tetradecapeptide where the proximal histidine was substituted with glutamine. Histidine 357-366 renin Homo sapiens 0-5 2186807-5 1990 Comparison of the pH profiles shows the catalytic efficiency (V/Km) and maximal velocity (V) of renin are greater above pH 6.5 with the substrate containing histidine proximal to the scissile peptide bond, but below pH 5.0 these parameters are greater with the glutamine substrate analogue. Histidine 157-166 renin Homo sapiens 96-101 2186807-7 1990 Molecular modeling indicates the substrate histidine could hydrogen bond to Asp-226 of the enzyme (renin numbering), thus perturbing the ionization of the catalytic aspartyl groups (Asp-38 and Asp-226). Histidine 43-52 renin Homo sapiens 99-104 2100004-1 1990 Conformation of the renin inhibitor peptide, Pro-His-Pro-Phe-His-Phe-Phe-Val-Tyr-Lys (RIP) has been studied in aqueous solution and in lipid bilayers using 500 MHz 1H NMR spectroscopy. Histidine 49-52 renin Homo sapiens 20-25 2520246-1 1989 Fast-atom bombardment mass spectrometry of a synthetic renin substrate decapeptide (Pro-His-Pro-Phe-His-Leu-Val-Ile-His-D-Lys) indicated the presence of several side-products, including a component 12 Da higher in mass. Histidine 100-103 renin Homo sapiens 55-60 3543358-5 1986 The analogues having a Phe residue in place of Val1 (X) and His or amino acid with an aliphatic side chain such as norleucine or norvaline in the Y position showed the highest inhibition of human plasma renin activity with IC50 values of about 10(-8)M. Esterification or amidification of the carboxyl group of the C-terminal statine did not change the inhibitory potency. Histidine 60-63 renin Homo sapiens 203-208 3126296-10 1988 We further suggest that the high selectivity of potent renin inhibitors known to be only weak pepsin and cathepsin D inhibitors is due in part to the extent of histidine protonation at P2 arising from pH differences in the inhibition kinetics assay of renin (neutral conditions) compared to other aspartic proteinases (acid pH 2-4). Histidine 160-169 renin Homo sapiens 55-60 3126296-10 1988 We further suggest that the high selectivity of potent renin inhibitors known to be only weak pepsin and cathepsin D inhibitors is due in part to the extent of histidine protonation at P2 arising from pH differences in the inhibition kinetics assay of renin (neutral conditions) compared to other aspartic proteinases (acid pH 2-4). Histidine 160-169 renin Homo sapiens 252-257 3275777-7 1988 10-fold) in renin inhibitory activity as exemplified by the pentapeptide Ac-Ftr-Pro-Phe-His-Sta-NH2 (12; IC50 = 3.8 X 10(-9) M). Histidine 88-91 renin Homo sapiens 12-17 3305946-8 1987 Of these, the inhibitors that contain histidine show marked selectivity toward renin over a related aspartic proteinase, pepsin. Histidine 38-47 renin Homo sapiens 79-84 2485065-5 1987 The homologous fungal aspartic proteinase, endothiapepsin, has been cocrystallised with human renin inhibitors of the type His-Pro-Phe-His-Leu-R-Val-Ile-His, where R indicates a reduced carbonyl analogue of the scissile peptide bond. Histidine 123-126 renin Homo sapiens 94-99 2485065-5 1987 The homologous fungal aspartic proteinase, endothiapepsin, has been cocrystallised with human renin inhibitors of the type His-Pro-Phe-His-Leu-R-Val-Ile-His, where R indicates a reduced carbonyl analogue of the scissile peptide bond. Histidine 135-138 renin Homo sapiens 94-99 2485065-5 1987 The homologous fungal aspartic proteinase, endothiapepsin, has been cocrystallised with human renin inhibitors of the type His-Pro-Phe-His-Leu-R-Val-Ile-His, where R indicates a reduced carbonyl analogue of the scissile peptide bond. Histidine 135-138 renin Homo sapiens 94-99 3003303-6 1985 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Val-Tyr. Histidine 50-53 renin Homo sapiens 26-31 3003303-6 1985 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Val-Tyr. Histidine 62-65 renin Homo sapiens 26-31 3887901-6 1985 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 50-53 renin Homo sapiens 26-31 3887901-6 1985 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 62-65 renin Homo sapiens 26-31 6099385-6 1984 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 50-53 renin Homo sapiens 26-31 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 renin Homo sapiens 0-5 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 renin Homo sapiens 33-38 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 renin Homo sapiens 161-166 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 renin Homo sapiens 0-5 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 renin Homo sapiens 33-38 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 renin Homo sapiens 161-166 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 renin Homo sapiens 0-5 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 renin Homo sapiens 33-38 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 renin Homo sapiens 161-166 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 renin Homo sapiens 311-316 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 renin Homo sapiens 311-316 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 renin Homo sapiens 311-316 6380499-2 1984 Calculations and comparison of low energy structures for these peptides give support to the existence of a beta-turn-like structure involving the His-Pro-Phe-His region of the renin substrate and of the competitive inhibitors containing that sequence. Histidine 146-149 renin Homo sapiens 176-181 6380499-2 1984 Calculations and comparison of low energy structures for these peptides give support to the existence of a beta-turn-like structure involving the His-Pro-Phe-His region of the renin substrate and of the competitive inhibitors containing that sequence. Histidine 158-161 renin Homo sapiens 176-181 6099385-6 1984 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 62-65 renin Homo sapiens 26-31 6418650-9 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 84-87 renin Homo sapiens 26-31 6418650-9 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 96-99 renin Homo sapiens 26-31 13463253-1 1957 A purified preparation of a polypeptide renin substrate prepared by tryptic degradation of the protein renin substrate has been analyzed by the fluorodinitrobenzene method and after degradation with renin, carboxypeptidase, and phenylisothiocyanate, has been found to possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser. Histidine 334-337 renin Homo sapiens 40-45 6196232-6 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 84-87 renin Homo sapiens 26-31 6196232-6 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 96-99 renin Homo sapiens 26-31 6357563-6 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 84-87 renin Homo sapiens 26-31 6357563-6 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Histidine 96-99 renin Homo sapiens 26-31 19034-1 1977 The properties of aqueous solutions of synthetic renin substrate tetradecapeptide (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser) were examined through electrometric titrations, infrared and circular dichroism spectroscopy, and spectrofluorometry. Histidine 103-106 renin Homo sapiens 49-54 19034-1 1977 The properties of aqueous solutions of synthetic renin substrate tetradecapeptide (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser) were examined through electrometric titrations, infrared and circular dichroism spectroscopy, and spectrofluorometry. Histidine 115-118 renin Homo sapiens 49-54 19034-3 1977 The experimental results of the tetradecapeptide study, associated with Chou and Fasman calculations and with an analysis of structure-activity relationships in renin substrates and competitive inhibitors, led to the proposal of a beta turn involving the His-Pro-Phe-His sequence of the tetradecapeptide. Histidine 255-258 renin Homo sapiens 161-166 1009126-4 1976 Several analogs of the octapeptide segment: His-Pro-Phe-His-Leu-Leu-Val-Tyr of this tetradecapeptide act as competitive inhibitors for human renin with inhibition constants down to 1 muM. Histidine 44-47 renin Homo sapiens 141-146 5662012-10 1968 It is suggested that the compounds his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13)-ser(14) or his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13) might be used as substrates for the chemical assay and standardization of renin. Histidine 35-38 renin Homo sapiens 240-245 5662012-10 1968 It is suggested that the compounds his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13)-ser(14) or his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13) might be used as substrates for the chemical assay and standardization of renin. Histidine 56-59 renin Homo sapiens 240-245 5662012-10 1968 It is suggested that the compounds his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13)-ser(14) or his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13) might be used as substrates for the chemical assay and standardization of renin. Histidine 56-59 renin Homo sapiens 240-245 5662012-10 1968 It is suggested that the compounds his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13)-ser(14) or his(6)-pro(7)-phe(8)-his(9)-leu(10)-leu(11)-val(12)-tyr(13) might be used as substrates for the chemical assay and standardization of renin. Histidine 56-59 renin Homo sapiens 240-245 13463253-1 1957 A purified preparation of a polypeptide renin substrate prepared by tryptic degradation of the protein renin substrate has been analyzed by the fluorodinitrobenzene method and after degradation with renin, carboxypeptidase, and phenylisothiocyanate, has been found to possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser. Histidine 322-325 renin Homo sapiens 40-45