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. Tyrosine 61-64 renin Homo sapiens 134-139 12045255-4 2002 The binding of renin induced a fourfold increase of the catalytic efficiency of angiotensinogen conversion to angiotensin I and induced an intracellular signal with phosphorylation of serine and tyrosine residues associated to an activation of MAP kinases ERK1 and ERK2. Tyrosine 195-203 renin Homo sapiens 15-20 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. Tyrosine 44-47 renin Homo sapiens 231-236 12645296-6 2002 The binding of renin induces an increase of the catalytic efficiency of angiotensinogen conversion into angiotensin I by receptor-bound renin compared to renin in soluble phase, and a rapid phosphorylation of the receptor on serine and tyrosine residues associated with an activation of MAP kinases ERK1/2. Tyrosine 236-244 renin Homo sapiens 15-20 10427707-0 1999 Tyrosine-83 of human renin contributes to biphasic pH dependence of the renin-angiotensinogen reaction. Tyrosine 0-8 renin Homo sapiens 72-77 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). Tyrosine 60-63 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). Tyrosine 64-67 renin Homo sapiens 205-210 10427707-0 1999 Tyrosine-83 of human renin contributes to biphasic pH dependence of the renin-angiotensinogen reaction. Tyrosine 0-8 renin Homo sapiens 21-26 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. Tyrosine 198-201 renin Homo sapiens 121-126 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. Tyrosine 224-227 renin Homo sapiens 121-126 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. Tyrosine 162-165 renin Homo sapiens 0-5 3887901-6 1985 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Tyrosine 78-81 renin Homo sapiens 26-31 3003303-6 1985 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Val-Tyr. Tyrosine 74-77 renin Homo sapiens 26-31 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. Tyrosine 198-201 renin Homo sapiens 0-5 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. Tyrosine 44-47 renin Homo sapiens 311-316 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. Tyrosine 99-102 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. Tyrosine 99-102 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. Tyrosine 99-102 renin Homo sapiens 161-166 6196232-6 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Tyrosine 112-115 renin Homo sapiens 26-31 6099385-6 1984 The minimal substrate for renin has the sequence: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Tyrosine 78-81 renin Homo sapiens 26-31 6347189-0 1983 Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr). Tyrosine 132-135 renin Homo sapiens 22-27 6418650-9 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Tyrosine 112-115 renin Homo sapiens 26-31 6347189-0 1983 Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr). Tyrosine 132-135 renin Homo sapiens 88-93 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. Tyrosine 87-90 renin Homo sapiens 240-245 1009126-2 1976 The amino acid sequence around the renin substrate site is known to be identical to the N-terminal tetradecapeptide: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser. Tyrosine 129-132 renin Homo sapiens 35-40 1009126-2 1976 The amino acid sequence around the renin substrate site is known to be identical to the N-terminal tetradecapeptide: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser. Tyrosine 165-168 renin Homo sapiens 35-40 6357563-6 1983 The minimal substrate for renin is an octapeptide segment of the protein substrate: His-Pro-Phe-His-Leu-Leu-Val-Tyr. Tyrosine 112-115 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. Tyrosine 95-98 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. Tyrosine 131-134 renin Homo sapiens 49-54 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. Tyrosine 350-353 renin Homo sapiens 40-45 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. Tyrosine 313-316 renin Homo sapiens 40-45 13463253-3 1957 The remaining 4 amino acids, leu, val, tyr, ser, apparently link hypertensin I to the protein renin substrate. Tyrosine 39-42 renin Homo sapiens 94-99