PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28035004-6	2017	These structures based on high quality data showed that the base moieties of two substrates are located on the similar but not the same position in the substrate binding pocket and adopt a different hydrogen-bonding pattern, and both triphosphate moieties bind to the hMTH1 Nudix motif (i.e. the hydrolase motif) similarly and align for the hydrolysis reaction.	triphosphoric acid	234-246	nudix hydrolase 1	Homo sapiens	268-273	
10938385-3	2000	hMTH1 protein reduces spontaneous mutations by removing 8-oxo-dGTP from the triphosphate pool.	triphosphoric acid	76-88	nudix hydrolase 1	Homo sapiens	0-5	
26879218-3	2016	Interestingly, these triphosphates were poor substrates for hMTH1, but exhibited strong competitive inhibition against hMTH1 at nanomolar levels.	triphosphoric acid	21-34	nudix hydrolase 1	Homo sapiens	60-65	
26879218-3	2016	Interestingly, these triphosphates were poor substrates for hMTH1, but exhibited strong competitive inhibition against hMTH1 at nanomolar levels.	triphosphoric acid	21-34	nudix hydrolase 1	Homo sapiens	119-124