PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30320292-6	2018	Both these nanoparticles show a reduction in dityrosine formation in RNase A caused due to oxidative stress and also prevent RNase A dimer formation to different extents depending on their concentration.	dityrosine	45-55	ribonuclease A family member 1, pancreatic	Homo sapiens	69-76	
31059754-3	2019	Oxidation of RNase A leads to intermolecular dityrosine (DT) bond formation which shows a characteristic fluorescence emission around 405 nm.	dityrosine	45-55	ribonuclease A family member 1, pancreatic	Homo sapiens	13-20	
31059754-3	2019	Oxidation of RNase A leads to intermolecular dityrosine (DT) bond formation which shows a characteristic fluorescence emission around 405 nm.	dityrosine	57-59	ribonuclease A family member 1, pancreatic	Homo sapiens	13-20	
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.	dityrosine	71-73	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.	dityrosine	71-73	ribonuclease A family member 1, pancreatic	Homo sapiens	16-23	
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.	dityrosine	71-73	ribonuclease A family member 1, pancreatic	Homo sapiens	51-58	
27475778-0	2016	DNA melting properties of the dityrosine cross-linked dimer of Ribonuclease A.	dityrosine	30-40	ribonuclease A family member 1, pancreatic	Homo sapiens	63-77	
27475778-3	2016	In the present study, we have compared the DNA binding properties between the RNase A monomer and the dityrosine (DT) cross-linked RNase A dimer, and checked the inhibitory effect of DNA on the ribonucleolytic activity of the dimeric protein.	dityrosine	102-112	ribonuclease A family member 1, pancreatic	Homo sapiens	131-138	
27475778-3	2016	In the present study, we have compared the DNA binding properties between the RNase A monomer and the dityrosine (DT) cross-linked RNase A dimer, and checked the inhibitory effect of DNA on the ribonucleolytic activity of the dimeric protein.	dityrosine	114-116	ribonuclease A family member 1, pancreatic	Homo sapiens	131-138