PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2168898-6	1990	In an effort to establish that phosphate turnover was occurring on the cellular dUTPase protein, cells were prelabeled with 32P-orthophosphate and then infected with HSV in the absence of label.	Phosphates	31-40	Deoxyuridine triphosphatase	Drosophila melanogaster	80-87	
8631817-13	1996	[32P]Orthophosphate-labeled dUTPase was purified from HeLa cells, revealing that only the nuclear form of dUTPase is phosphorylated.	Phosphates	5-19	Deoxyuridine triphosphatase	Drosophila melanogaster	28-35	
8631817-13	1996	[32P]Orthophosphate-labeled dUTPase was purified from HeLa cells, revealing that only the nuclear form of dUTPase is phosphorylated.	Phosphates	5-19	Deoxyuridine triphosphatase	Drosophila melanogaster	106-113	
21831832-3	2011	Our spectroscopy and transient kinetics results on human dUTPase mutants combined with previous structural studies indicate that (i) H-bond interactions between the gamma-phosphate and the P-loop-like motif V promote the catalytically competent conformation of the reaction center at the alpha-phosphate group; (ii) these interactions accelerate the chemical step of the kinetic cycle and that (iii) hydrolysis occurs very slowly or not at all in the absence of the gamma-phosphate--motif V interactions, i.e., in dUDP, dUDP.BeFx, or in the motif V-deleted mutant.	Phosphates	171-180	Deoxyuridine triphosphatase	Drosophila melanogaster	57-64	
2168898-7	1990	Evidence from this experiment indicates that the phosphate moiety is removed from the cellular dUTPase protein during the infection.	Phosphates	49-58	Deoxyuridine triphosphatase	Drosophila melanogaster	95-102	
23982515-4	2013	Combining mass spectrometry analysis of the dUTPase-catalyzed reaction carried out in and quantum mechanics/molecular mechanics (QM/MM) simulation, we show that the nucleophilic attack occurs at the alpha-phosphate site.	Phosphates	205-214	Deoxyuridine triphosphatase	Drosophila melanogaster	44-51	
23982515-0	2013	Catalytic mechanism of alpha-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.	Phosphates	29-38	Deoxyuridine triphosphatase	Drosophila melanogaster	49-56