PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9600911-6 1998 Kinetic analysis indicates that a DNA-histidine complex may perform a reaction that is analogous to the first step of the proposed catalytic mechanism of RNase A, in which the imidazole group of histidine serves as a general base catalyst. Histidine 38-47 ribonuclease A family member 1, pancreatic Homo sapiens 154-161 9600911-6 1998 Kinetic analysis indicates that a DNA-histidine complex may perform a reaction that is analogous to the first step of the proposed catalytic mechanism of RNase A, in which the imidazole group of histidine serves as a general base catalyst. Histidine 195-204 ribonuclease A family member 1, pancreatic Homo sapiens 154-161 9367166-0 1997 Effect of chemical glycosylation of RNase A on the protein stability and surface histidines accessibility in immobilized metal ion affinity electrophoresis (IMAGE) system. Histidine 81-91 ribonuclease A family member 1, pancreatic Homo sapiens 36-43 9367166-1 1997 Immobilized metal ion affinity gel electrophoresis (IMAGE) has been applied to study the change of the surface histidines topography of RNase A when chemically glycosylated on exposed carboxylic groups with glucosamine using carbodiimide as cross-linker, under mild conditions. Histidine 111-121 ribonuclease A family member 1, pancreatic Homo sapiens 136-143 9224937-1 1997 The enzymatic activity of many ribonucleases (RNases) depends on two histidines, as in RNase A, or one histidine and/or glutamate, as in microbial RNases belonging to the T1 family. Histidine 69-79 ribonuclease A family member 1, pancreatic Homo sapiens 87-94 9224937-1 1997 The enzymatic activity of many ribonucleases (RNases) depends on two histidines, as in RNase A, or one histidine and/or glutamate, as in microbial RNases belonging to the T1 family. Histidine 69-78 ribonuclease A family member 1, pancreatic Homo sapiens 87-94 7612603-5 1995 The appearance of a new histidine resonance in the cold-denatured and pressure-denatured RNase A spectra, compared to the absence of this resonance in the heat-denatured state, indicates that the pressure-denatured and cold-denatured states may contain partially folded structures that are similar to that of the early folding intermediate found in the temperature-jump experiment reported by Blum et al. Histidine 24-33 ribonuclease A family member 1, pancreatic Homo sapiens 89-96 7939659-3 1994 Variants of RNase A were produced in which the catalytic histidines at positions 12 and 119 were substituted with the unnatural amino acid 4-fluorohistidine, which has a pKa of 3.5 compared to 6.8 for histidine. Histidine 57-67 ribonuclease A family member 1, pancreatic Homo sapiens 12-19 7939659-3 1994 Variants of RNase A were produced in which the catalytic histidines at positions 12 and 119 were substituted with the unnatural amino acid 4-fluorohistidine, which has a pKa of 3.5 compared to 6.8 for histidine. Histidine 57-66 ribonuclease A family member 1, pancreatic Homo sapiens 12-19 7919003-2 1994 The homonuclear Nuclear Overhauser and exchange spectroscopy spectrum of the uridine vanadate/RNase A complex exhibits cross peaks between both the C5H and C6H protons of uridine vanadate and the H epsilon 1 proton of His-12 of ribonuclease A. Histidine 218-221 ribonuclease A family member 1, pancreatic Homo sapiens 94-101 7919003-3 1994 These cross peaks suggest that the H epsilon 1 proton of His-12 is in the vicinity of the uracil base of uridine vanadate, as observed in the crystallographic structure of the uridine vanadate/RNase A complex. Histidine 57-60 ribonuclease A family member 1, pancreatic Homo sapiens 193-200 1540654-7 1992 The transition observed for loss of alpha-helix coincides with the previously measured transition for His-12 by NMR from a partially folded state to the unfolded state, suggesting that the unfolding of the N-terminal helix in RNase A is lost after unfolding of the core beta-sheet during thermal denaturation. Histidine 102-105 ribonuclease A family member 1, pancreatic Homo sapiens 226-233 3126807-10 1987 We propose a revised reaction mechanism in which two histidine residues play a major role, as they do in the case of RNase A. Histidine 53-62 ribonuclease A family member 1, pancreatic Homo sapiens 117-124 3122207-2 1987 Reagents specific for histidine, lysine, and arginine markedly decrease the ribonucleolytic activity of angiogenin, much as has been observed for RNase A. Histidine 22-31 ribonuclease A family member 1, pancreatic Homo sapiens 146-153 3814749-3 1986 A salt bridge of this type (Glu- 9-His+ 12) was postulated previously to stabilize, to a great extent, the alpha-helical conformation of isolated N-terminal fragments of RNase A: C-peptide and S-peptide (A. Bierzynski, P.S. Histidine 35-38 ribonuclease A family member 1, pancreatic Homo sapiens 170-177 6265917-0 1981 Orientation of histidine residues in RNase A: neutron diffraction study. Histidine 15-24 ribonuclease A family member 1, pancreatic Homo sapiens 37-44 207308-2 1978 3-SLHis-105-RNase A is an active derivative of ribonuclease A (RNase A) spin-labeled at the 3 position of the imidazole ring of histidine-105. Histidine 128-137 ribonuclease A family member 1, pancreatic Homo sapiens 12-19 207308-2 1978 3-SLHis-105-RNase A is an active derivative of ribonuclease A (RNase A) spin-labeled at the 3 position of the imidazole ring of histidine-105. Histidine 128-137 ribonuclease A family member 1, pancreatic Homo sapiens 47-61 207308-2 1978 3-SLHis-105-RNase A is an active derivative of ribonuclease A (RNase A) spin-labeled at the 3 position of the imidazole ring of histidine-105. Histidine 128-137 ribonuclease A family member 1, pancreatic Homo sapiens 63-70 207308-4 1978 The results of these experiments indicate that the spin-label attached to histidine-105 of RNase A is sensitive to modifications affecting the conformational integrity of the molecule and to the reconstituting effects of various active-center ligands. Histidine 74-83 ribonuclease A family member 1, pancreatic Homo sapiens 91-98 23288-1 1977 1H NMR spectroscopy at 100 MHz was used to determine the first-order rate constants for the 1H-2H exchange of the H-2 histidine resonances of RNase-A in 2H2O at 35 degrees C and pH meter readings of 7, 9, 10 and 10.5. Histidine 118-127 ribonuclease A family member 1, pancreatic Homo sapiens 142-149 23288-6 1977 These changes are attributed to a conformational change in the hinge region of RNase-A (probably due to the titration of Tyr-25) which allows His-48 to become accessible to solvent. Histidine 142-145 ribonuclease A family member 1, pancreatic Homo sapiens 79-86 23288-7 1977 1H NMR spectra of S-protein and S-peptide, and of material partially deuterated at the C-2 positions of the histidine residues confirm the reassignment of the histidine resonances of RNase-A [Bradbury, J. H. & Teh, J. S. (1975) Chem. Histidine 108-117 ribonuclease A family member 1, pancreatic Homo sapiens 183-190 23288-7 1977 1H NMR spectra of S-protein and S-peptide, and of material partially deuterated at the C-2 positions of the histidine residues confirm the reassignment of the histidine resonances of RNase-A [Bradbury, J. H. & Teh, J. S. (1975) Chem. Histidine 159-168 ribonuclease A family member 1, pancreatic Homo sapiens 183-190 23288-12 1977 The S-protein is less stable to acid than RNase-A since the former, but not the latter, shows evidence of reversible denaturation at pH 3 and 26 degrees C. His-48 in S-protein titrates normally and has a lower pK than in RN-ase-A probably because of the absence of Asp-14, which in RN-ase-A forms a a hydrogen bond with His-48 and causes it to be inaccessible to solvent, at pH values below 9. Histidine 156-159 ribonuclease A family member 1, pancreatic Homo sapiens 42-49 23288-12 1977 The S-protein is less stable to acid than RNase-A since the former, but not the latter, shows evidence of reversible denaturation at pH 3 and 26 degrees C. His-48 in S-protein titrates normally and has a lower pK than in RN-ase-A probably because of the absence of Asp-14, which in RN-ase-A forms a a hydrogen bond with His-48 and causes it to be inaccessible to solvent, at pH values below 9. Histidine 156-159 ribonuclease A family member 1, pancreatic Homo sapiens 221-229 23288-12 1977 The S-protein is less stable to acid than RNase-A since the former, but not the latter, shows evidence of reversible denaturation at pH 3 and 26 degrees C. His-48 in S-protein titrates normally and has a lower pK than in RN-ase-A probably because of the absence of Asp-14, which in RN-ase-A forms a a hydrogen bond with His-48 and causes it to be inaccessible to solvent, at pH values below 9. Histidine 156-159 ribonuclease A family member 1, pancreatic Homo sapiens 282-290 238843-8 1975 In the presence of phosphate, titration curves for the H-2 proton resonances of histidine-12 and histidine-119 of methylated RNase-A indicate binding of phosphate at the active site, but these curves continue to show deviations from the titration behaviour of native RNase-A. Histidine 80-89 ribonuclease A family member 1, pancreatic Homo sapiens 267-274 238843-7 1975 Titration curves for the H-2 proton resonances of histidine-12 and histidine-119 of methylated RNase-A show deviations from the titration curves for the native enzyme, indicating some alteration of the active-site conformation. Histidine 50-59 ribonuclease A family member 1, pancreatic Homo sapiens 95-102 238843-7 1975 Titration curves for the H-2 proton resonances of histidine-12 and histidine-119 of methylated RNase-A show deviations from the titration curves for the native enzyme, indicating some alteration of the active-site conformation. Histidine 67-76 ribonuclease A family member 1, pancreatic Homo sapiens 95-102 238843-8 1975 In the presence of phosphate, titration curves for the H-2 proton resonances of histidine-12 and histidine-119 of methylated RNase-A indicate binding of phosphate at the active site, but these curves continue to show deviations from the titration behaviour of native RNase-A. Histidine 80-89 ribonuclease A family member 1, pancreatic Homo sapiens 125-132 238843-8 1975 In the presence of phosphate, titration curves for the H-2 proton resonances of histidine-12 and histidine-119 of methylated RNase-A indicate binding of phosphate at the active site, but these curves continue to show deviations from the titration behaviour of native RNase-A. Histidine 97-106 ribonuclease A family member 1, pancreatic Homo sapiens 125-132 238843-8 1975 In the presence of phosphate, titration curves for the H-2 proton resonances of histidine-12 and histidine-119 of methylated RNase-A indicate binding of phosphate at the active site, but these curves continue to show deviations from the titration behaviour of native RNase-A. Histidine 97-106 ribonuclease A family member 1, pancreatic Homo sapiens 267-274 30031072-0 2018 Structural and functional changes in RNAse A originating from tyrosine and histidine cross-linking and oxidation induced by singlet oxygen and peroxyl radicals. Histidine 75-84 ribonuclease A family member 1, pancreatic Homo sapiens 37-44 30031072-5 2018 RNAse A lacks tryptophan and cysteine residues which are major oxidant targets, but contains multiple histidine, tyrosine and methionine residues; these were therefore hypothesized to be the major sites of damage. Histidine 102-111 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 25143596-1 2014 To explore dual-specificity in a small protein interface, we previously generated a "metal switch" anti-RNase A VHH antibody using a combinatorial histidine library approach. Histidine 147-156 ribonuclease A family member 1, pancreatic Homo sapiens 104-111 23381689-2 2013 Based in enzyme kinetics experiments and (1)H NMR spectroscopic analysis we proposed that urea, at low concentrations, directly interacts with the protonated histidines of the active center of RNase A, following a simple model of competitive inhibition. Histidine 158-168 ribonuclease A family member 1, pancreatic Homo sapiens 193-200 21767494-1 2011 Rate-limiting millisecond motions in wild-type (WT) Ribonuclease A (RNase A) are modulated by histidine 48. Histidine 94-103 ribonuclease A family member 1, pancreatic Homo sapiens 52-66 21767494-1 2011 Rate-limiting millisecond motions in wild-type (WT) Ribonuclease A (RNase A) are modulated by histidine 48. Histidine 94-103 ribonuclease A family member 1, pancreatic Homo sapiens 68-75 21568282-3 2011 Using a combinatorial histidine-scanning phage display library, potential metal binding sites were introduced throughout an anti-RNase A antibody interface. Histidine 22-31 ribonuclease A family member 1, pancreatic Homo sapiens 129-136 21250662-0 2011 Alteration of hydrogen bonding in the vicinity of histidine 48 disrupts millisecond motions in RNase A. Histidine 50-59 ribonuclease A family member 1, pancreatic Homo sapiens 95-102 21041096-4 2010 The preferential hydrogen bonding network formation between His-12 and His-119 of RNase A with the polar carboxylic and amino groups of these compounds has been evidenced from the docking studies. Histidine 60-63 ribonuclease A family member 1, pancreatic Homo sapiens 82-89 21041096-4 2010 The preferential hydrogen bonding network formation between His-12 and His-119 of RNase A with the polar carboxylic and amino groups of these compounds has been evidenced from the docking studies. Histidine 71-74 ribonuclease A family member 1, pancreatic Homo sapiens 82-89 19771477-3 2009 Squirrel RNase 1 genes encode typical RNase A ribonucleases, each with eight cysteines, a conserved CKXXNTF signature motif, and a canonical His(12)-Lys(41)-His(119) catalytic triad. Histidine 141-144 ribonuclease A family member 1, pancreatic Homo sapiens 9-16 19771477-3 2009 Squirrel RNase 1 genes encode typical RNase A ribonucleases, each with eight cysteines, a conserved CKXXNTF signature motif, and a canonical His(12)-Lys(41)-His(119) catalytic triad. Histidine 157-160 ribonuclease A family member 1, pancreatic Homo sapiens 9-16 19540766-1 2009 Nucleoside-amino acid conjugates have been employed to inhibit the ribonucleolytic activity of ribonuclease A (RNase A) and affect the protonation/deprotonation equilibrium of its active site histidine residues. Histidine 192-201 ribonuclease A family member 1, pancreatic Homo sapiens 95-109 19540766-1 2009 Nucleoside-amino acid conjugates have been employed to inhibit the ribonucleolytic activity of ribonuclease A (RNase A) and affect the protonation/deprotonation equilibrium of its active site histidine residues. Histidine 192-201 ribonuclease A family member 1, pancreatic Homo sapiens 111-118 19540766-4 2009 The nucleoside-serine conjugate occupies the active site of RNase A and preferential perturbs the pK(a) value of His-119 by its "free amino group" as found from (1)H NMR studies. Histidine 113-116 ribonuclease A family member 1, pancreatic Homo sapiens 60-67 19540766-5 2009 Docking studies revealed that the free amino groups of the most active compounds are within hydrogen bonding distance of His-119 in inhibitor-RNase A complexes. Histidine 121-124 ribonuclease A family member 1, pancreatic Homo sapiens 142-149 18665614-7 2008 The p K a values of three of four histidine residues (His12, -105, and -119) in RNase A were successfully determined by this method and were in good agreement with those determined by (1)H NMR and hydrogen-tritium exchange methods. Histidine 34-43 ribonuclease A family member 1, pancreatic Homo sapiens 80-87 18226913-5 2008 The mode of inhibition has also been confirmed by (1)H NMR studies of the active site histidines of RNase A. Histidine 86-96 ribonuclease A family member 1, pancreatic Homo sapiens 100-107 16862454-2 2006 The changes in the distance between N(epsilon2) of His(12) and N(delta1) of His(119) at the catalytic center of RNase A upon the addition of sodium sulfate, sodium hydrogen sulfate and sodium thiocyanate were evaluated by molecular dynamic methods. Histidine 51-54 ribonuclease A family member 1, pancreatic Homo sapiens 112-119 16862454-2 2006 The changes in the distance between N(epsilon2) of His(12) and N(delta1) of His(119) at the catalytic center of RNase A upon the addition of sodium sulfate, sodium hydrogen sulfate and sodium thiocyanate were evaluated by molecular dynamic methods. Histidine 76-79 ribonuclease A family member 1, pancreatic Homo sapiens 112-119 15713463-11 2005 Since the overall structure of hCNP-CF differs considerably from that of RNase A, it is likely that the similar active sites with two catalytic histidine residues in these enzymes arose through convergent evolution. Histidine 144-153 ribonuclease A family member 1, pancreatic Homo sapiens 73-80 12964199-1 2003 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine 225-228 ribonuclease A family member 1, pancreatic Homo sapiens 74-88 12964199-1 2003 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine 225-228 ribonuclease A family member 1, pancreatic Homo sapiens 90-97 12964199-1 2003 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine 233-236 ribonuclease A family member 1, pancreatic Homo sapiens 74-88 12964199-1 2003 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine 233-236 ribonuclease A family member 1, pancreatic Homo sapiens 90-97 11331007-2 2001 Both catalytic sites are comprised of two histidine side chains acting as a general base-general acid pair and a phosphate-activating residue: an arginine in the case of PI-PLC and a lysine in RNase A. Histidine 42-51 ribonuclease A family member 1, pancreatic Homo sapiens 193-200 11305910-0 2001 Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding. Histidine 32-41 ribonuclease A family member 1, pancreatic Homo sapiens 54-68 10606511-4 1999 It reveals that residues Gln-14, His-15, Lys-38, Thr-42, and His-128 at the active site are conserved as in all other RNase A homologues. Histidine 33-36 ribonuclease A family member 1, pancreatic Homo sapiens 118-125 10606511-4 1999 It reveals that residues Gln-14, His-15, Lys-38, Thr-42, and His-128 at the active site are conserved as in all other RNase A homologues. Histidine 61-64 ribonuclease A family member 1, pancreatic Homo sapiens 118-125 10386039-4 1999 In this work is analysed endonuclease activity of recombinant pancreatic RNase A (K7H), that in position seven instead of a lysine there is a histidine, amino acid residue that participates in main catalytic site p1. Histidine 142-151 ribonuclease A family member 1, pancreatic Homo sapiens 73-80 10386039-6 1999 Results of this investigation have shown that substitution of lysine by histidine in position seven of RNase A has produced total deletion of p2 subsite, and K7H has lost endonuclease activity, and has become exonuclease. Histidine 72-81 ribonuclease A family member 1, pancreatic Homo sapiens 103-110