PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
25985124-2	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	
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