PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8195828-2	1993	Inhibition of the enzyme dihydrofolate reductase (DHFR) depletes the available tetrahydrofolate and blocks the formation of thymidylate, purines, the amino acids methionine and glycine, and several other cell constituents.	Purines	137-144	dihydrofolate reductase	Homo sapiens	25-48	
27213086-1	2016	Structural basis for exploration into MDM2 and MDM2-DHFR interaction plays a vital role in analyzing the obstruction in folate metabolism, nonsynthesis of purines, and further epigenetic regulation in Homo sapiens.	Purines	155-162	dihydrofolate reductase	Homo sapiens	52-56	
8195828-2	1993	Inhibition of the enzyme dihydrofolate reductase (DHFR) depletes the available tetrahydrofolate and blocks the formation of thymidylate, purines, the amino acids methionine and glycine, and several other cell constituents.	Purines	137-144	dihydrofolate reductase	Homo sapiens	50-54	
31401334-2	2019	Dihydrofolate reductase (DHFR), an enzyme involved in folate metabolism converts dihydrofolate into tetrahydrofolate, which is required for the de novo synthesis of purines, and certain amino acids.	Purines	165-172	dihydrofolate reductase	Homo sapiens	0-23	
31401334-2	2019	Dihydrofolate reductase (DHFR), an enzyme involved in folate metabolism converts dihydrofolate into tetrahydrofolate, which is required for the de novo synthesis of purines, and certain amino acids.	Purines	165-172	dihydrofolate reductase	Homo sapiens	25-29