PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31520592-5	2019	Furthermore, the tetrahydrofolate- and time-dependent, covalent binding by thymidylate synthase of each 5-fluoro-dUMP and N4-hydroxy-dCMP was shown to be accompanied by the enzyme inactivation, as well as spectrophotometrically confirmed dihydrofolate production, the latter demonstrated to depend on the reaction time, thymidylate synthase activity and temperature of the incubation mixture, further documenting its catalytic character.	N-4-hydroxy-2'-deoxycytidylic acid	122-137	thymidylate synthase	Mus musculus	75-95	
33800923-8	2021	This difference may be crucial for the explanation of the "abortive reaction" inhibitory mechanism of N4OH-dCMP towards TS.	N-4-hydroxy-2'-deoxycytidylic acid	102-111	thymidylate synthase	Mus musculus	120-122	
31520592-1	2019	In view of previous crystallographic studies, N4-hydroxy-dCMP, a slow-binding thymidylate synthase inhibitor apparently caused "uncoupling" of the two thymidylate synthase-catalyzed reactions, including the N5,10-methylenetetrahydrofolate one-carbon group transfer and reduction, suggesting the enzyme"s capacity to use tetrahydrofolate as a cofactor reducing the pyrimidine ring C(5) in the absence of the 5-methylene group.	N-4-hydroxy-2'-deoxycytidylic acid	46-61	thymidylate synthase	Mus musculus	78-98	
31520592-1	2019	In view of previous crystallographic studies, N4-hydroxy-dCMP, a slow-binding thymidylate synthase inhibitor apparently caused "uncoupling" of the two thymidylate synthase-catalyzed reactions, including the N5,10-methylenetetrahydrofolate one-carbon group transfer and reduction, suggesting the enzyme"s capacity to use tetrahydrofolate as a cofactor reducing the pyrimidine ring C(5) in the absence of the 5-methylene group.	N-4-hydroxy-2'-deoxycytidylic acid	46-61	thymidylate synthase	Mus musculus	151-171	
31520592-4	2019	Further studies of the mouse enzyme binding with 5-fluoro-dUMP/N4-hydroxy-dCMP by TCA precipitation of the complex on filter paper showed it to be tetrahydrofolate-promoted, as well as to depend on both time in the range of minutes and the enzyme molecular activity, indicating thymidylate synthase-catalyzed reaction to be responsible for it.	N-4-hydroxy-2'-deoxycytidylic acid	63-78	thymidylate synthase	Mus musculus	278-298	
33946210-0	2021	Molecular Mechanism of Thymidylate Synthase Inhibition by N4-Hydroxy-dCMP in View of Spectrophotometric and Crystallographic Studies.	N-4-hydroxy-2'-deoxycytidylic acid	58-73	thymidylate synthase	Mus musculus	23-43	
33946210-1	2021	Novel evidence is presented allowing further clarification of the mechanism of the slow-binding thymidylate synthase (TS) inhibition by N4-hydroxy-dCMP (N4-OH-dCMP).	N-4-hydroxy-2'-deoxycytidylic acid	136-151	thymidylate synthase	Mus musculus	96-116	
33946210-1	2021	Novel evidence is presented allowing further clarification of the mechanism of the slow-binding thymidylate synthase (TS) inhibition by N4-hydroxy-dCMP (N4-OH-dCMP).	N-4-hydroxy-2'-deoxycytidylic acid	153-163	thymidylate synthase	Mus musculus	96-116	
31520592-5	2019	Furthermore, the tetrahydrofolate- and time-dependent, covalent binding by thymidylate synthase of each 5-fluoro-dUMP and N4-hydroxy-dCMP was shown to be accompanied by the enzyme inactivation, as well as spectrophotometrically confirmed dihydrofolate production, the latter demonstrated to depend on the reaction time, thymidylate synthase activity and temperature of the incubation mixture, further documenting its catalytic character.	N-4-hydroxy-2'-deoxycytidylic acid	122-137	thymidylate synthase	Mus musculus	320-340	
26916840-0	2016	Phosphorylation of thymidylate synthase affects slow-binding inhibition by 5-fluoro-dUMP and N(4)-hydroxy-dCMP.	N-4-hydroxy-2'-deoxycytidylic acid	93-110	thymidylate synthase	Mus musculus	19-39