PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9095357-6 1997 Extension of the model study to irradiated BSA and RNase A showed correlation of DOPA formation with Tyr modification up to 120 Gy. Tyrosine 101-104 ribonuclease A family member 1, pancreatic Homo sapiens 51-58 833149-9 1977 The resulting (Tyr-41)- and (Gln 41)-63-residue analogs were also bound by the affinity column and had the same substrate specificity as native RNase A. Tyrosine 15-18 ribonuclease A family member 1, pancreatic Homo sapiens 144-151 293712-3 1979 The U(S) right harpoon over left harpoon U(F) reaction in unfolded RNase A is used both to provide data on the kinetics of proline isomerization in the unfolded protein and as the basis of an assay for measuring proline isomerization during folding.The tyrosine-detected folding kinetics at low temperatures have been compared to those of proline isomerization in unfolded RNase A. Tyrosine 253-261 ribonuclease A family member 1, pancreatic Homo sapiens 67-74 293712-5 1979 At 0 degrees C the tyrosine-detected folding reaction is 100-fold faster than the conversion of U(S) to U(F) in unfolded RNase A. Tyrosine 19-27 ribonuclease A family member 1, pancreatic Homo sapiens 121-128 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. Tyrosine 121-124 ribonuclease A family member 1, pancreatic Homo sapiens 79-86 2252883-4 1990 The concentration of the trans proline species was determined from the integrated intensities of resonance peaks of the C alpha H protons of Tyr-92 and Asn-113, which are well resolved in the 1D proton NMR spectrum of heat-unfolded RNase A. Tyrosine 141-144 ribonuclease A family member 1, pancreatic Homo sapiens 232-239 6253494-5 1980 The CD measurements suggest that one or more tyrosine residues of RNase A may be involved in the interaction with inhibitor. Tyrosine 45-53 ribonuclease A family member 1, pancreatic Homo sapiens 66-73 6928678-1 1980 The three exposed tyrosines of RNase A have been converted to nitrotyrosines by reaction with tetranitromethane, and the changes in the ionization properties of these nitrotyrosines have been used to follow the kinetics of unfolding of the nitrated protein. Tyrosine 18-27 ribonuclease A family member 1, pancreatic Homo sapiens 31-38 25985124-2 2015 In the present study, the influence of SDS and BME on the redox properties of tyrosine and tryptophan for five different globular proteins, BSA, HSA, RNase-A, trypsin and lysozyme were studied using laser induced autofluorescence. Tyrosine 78-86 ribonuclease A family member 1, pancreatic Homo sapiens 150-157 29139109-2 2018 Ribonuclease A (RNase A) has 6 Tyr residues and shows a characteristic DT fluorescence peak upon oxidation in addition to major changes in its secondary structure. Tyrosine 31-34 ribonuclease A family member 1, pancreatic Homo sapiens 0-14 29139109-2 2018 Ribonuclease A (RNase A) has 6 Tyr residues and shows a characteristic DT fluorescence peak upon oxidation in addition to major changes in its secondary structure. Tyrosine 31-34 ribonuclease A family member 1, pancreatic Homo sapiens 16-23 26926397-5 2016 By assessing statistical significance using real-time quantitative PCR (RT-qPCR), the following 4 genes were selected as candidates: cell death-inducing DFFA-like effector c (CIDEC), ribonuclease 1 (RNASE1), solute carrier family 36 member-1 (SLC36A1), and serine/threonine/tyrosine interacting-like 1 (STYXL1). Tyrosine 274-282 ribonuclease A family member 1, pancreatic Homo sapiens 199-205 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. Tyrosine 62-70 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. Tyrosine 113-121 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 28662472-4 2017 These results are subsequently corroborated from the studies of excited-state relaxation dynamics of the intrinsic tyrosine residues of RNase A, and the modulations in fluorescence behavior of an extrinsic probe (ANS) bound to the protein. Tyrosine 115-123 ribonuclease A family member 1, pancreatic Homo sapiens 136-143 25985124-7 2015 The observation was further confirmed with similar proton transfer in absence of tryptophan in RNase-A showing involvement of tyrosine in the process. Tyrosine 126-134 ribonuclease A family member 1, pancreatic Homo sapiens 95-102 19344116-0 2009 Effects of tyrosine mutations on the conformational and oxidative folding of ribonuclease a: a comparative study. Tyrosine 11-19 ribonuclease A family member 1, pancreatic Homo sapiens 77-91 17384067-0 2007 Tracking local conformational changes of ribonuclease A using picosecond time-resolved fluorescence of the six tyrosine residues. Tyrosine 111-119 ribonuclease A family member 1, pancreatic Homo sapiens 41-55 17384067-1 2007 The six tyrosine residues of ribonuclease A (RNase A) are used as individual intrinsic probes for tracking local conformational changes during unfolding. Tyrosine 8-16 ribonuclease A family member 1, pancreatic Homo sapiens 29-43 17384067-1 2007 The six tyrosine residues of ribonuclease A (RNase A) are used as individual intrinsic probes for tracking local conformational changes during unfolding. Tyrosine 8-16 ribonuclease A family member 1, pancreatic Homo sapiens 45-52 17384067-2 2007 The fluorescence decays of RNase A are well described by sums of three exponentials with decay times (tau(1) = 1.7 ns, tau(2) = 180 ps, and tau(3) = 30 ps) and preexponential coefficients (A(1) = 1, A(2) = 1, and A(3) = 4) at pH 7, 25 degrees C. The decay times are controlled by photo-induced electron transfer from individual tyrosine residues to the nearest disulphide (-SS-), bridge, which is distance (R) dependent. Tyrosine 328-336 ribonuclease A family member 1, pancreatic Homo sapiens 27-34 9528688-11 1998 Extension of the model study to irradiated BSA and RNase A also showed DT as the major oxidation product of Tyr under the experimental conditions. Tyrosine 108-111 ribonuclease A family member 1, pancreatic Homo sapiens 51-58