PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34641326-4	2021	Our laboratory has previously examined this hypothesis in tumor cells and has demonstrated that dinitrosyl-dithiol-iron-complexes are transported and stored by multi-drug resistance-related protein 1 and glutathione-S-transferase P1.	Iron	115-119	glutathione S-transferase pi 1	Homo sapiens	204-232	
34641326-5	2021	A crystal structure of a dinitrosyl-dithiol-iron complex with glutathione-S-transferase P1 has been solved that demonstrates that a tyrosine residue in glutathione-S-transferase P1 is responsible for binding dinitrosyl-dithiol-iron-complexes.	Iron	44-48	glutathione S-transferase pi 1	Homo sapiens	62-90	
34641326-5	2021	A crystal structure of a dinitrosyl-dithiol-iron complex with glutathione-S-transferase P1 has been solved that demonstrates that a tyrosine residue in glutathione-S-transferase P1 is responsible for binding dinitrosyl-dithiol-iron-complexes.	Iron	44-48	glutathione S-transferase pi 1	Homo sapiens	152-180	
34641326-5	2021	A crystal structure of a dinitrosyl-dithiol-iron complex with glutathione-S-transferase P1 has been solved that demonstrates that a tyrosine residue in glutathione-S-transferase P1 is responsible for binding dinitrosyl-dithiol-iron-complexes.	Iron	227-231	glutathione S-transferase pi 1	Homo sapiens	62-90	
34641326-5	2021	A crystal structure of a dinitrosyl-dithiol-iron complex with glutathione-S-transferase P1 has been solved that demonstrates that a tyrosine residue in glutathione-S-transferase P1 is responsible for binding dinitrosyl-dithiol-iron-complexes.	Iron	227-231	glutathione S-transferase pi 1	Homo sapiens	152-180	
34121709-5	2021	Aim: This study aimed to investigate the relationship between GSTP1 polymorphism and early complications of allo-HSCT, iron parameters, overall survival (OS), and transplantation-related mortality (TRM).	Iron	119-123	glutathione S-transferase pi 1	Homo sapiens	62-67	
30623722-7	2019	In patients with tubular dysfunction, enhanced urinary iron and transferrin excretion were associated with distal tubular injury as indicated by increased urinary glutathione S-transferase pi 1-1 (GSTP1-1) excretion.	Iron	55-59	glutathione S-transferase pi 1	Homo sapiens	163-195	
30623722-7	2019	In patients with tubular dysfunction, enhanced urinary iron and transferrin excretion were associated with distal tubular injury as indicated by increased urinary glutathione S-transferase pi 1-1 (GSTP1-1) excretion.	Iron	55-59	glutathione S-transferase pi 1	Homo sapiens	197-204	
27866158-3	2016	We previously demonstrated by using tumor cells that glutathione S-transferase P1 (GSTP1) sequesters NO as dinitrosyl-dithiol iron complexes (DNICs) and inhibits NO-mediated iron release from cells via the transporter multidrug resistance protein 1 (MRP1/ABCC1).	Iron	126-130	glutathione S-transferase pi 1	Homo sapiens	53-81	
27866158-3	2016	We previously demonstrated by using tumor cells that glutathione S-transferase P1 (GSTP1) sequesters NO as dinitrosyl-dithiol iron complexes (DNICs) and inhibits NO-mediated iron release from cells via the transporter multidrug resistance protein 1 (MRP1/ABCC1).	Iron	126-130	glutathione S-transferase pi 1	Homo sapiens	83-88	
27866158-3	2016	We previously demonstrated by using tumor cells that glutathione S-transferase P1 (GSTP1) sequesters NO as dinitrosyl-dithiol iron complexes (DNICs) and inhibits NO-mediated iron release from cells via the transporter multidrug resistance protein 1 (MRP1/ABCC1).	Iron	174-178	glutathione S-transferase pi 1	Homo sapiens	53-81	
27866158-3	2016	We previously demonstrated by using tumor cells that glutathione S-transferase P1 (GSTP1) sequesters NO as dinitrosyl-dithiol iron complexes (DNICs) and inhibits NO-mediated iron release from cells via the transporter multidrug resistance protein 1 (MRP1/ABCC1).	Iron	174-178	glutathione S-transferase pi 1	Homo sapiens	83-88	
22262835-10	2012	The generation of dinitrosyl-dithiol-iron complexes acts as a common currency for NO transport and storage by MRP1 and GST P1-1, respectively.	Iron	37-41	glutathione S-transferase pi 1	Homo sapiens	119-127	
16195232-1	2005	We have recently shown that dinitrosyl diglutathionyl iron complex, a possible in vivo nitric oxide (NO) donor, binds with extraordinary affinity to one of the active sites of human glutathione transferase (GST) P1-1 and triggers negative cooperativity in the neighboring subunit of the dimer.	Iron	54-58	glutathione S-transferase pi 1	Homo sapiens	182-216	
16195232-7	2005	Electron paramagnetic resonance spectroscopy studies on intact Escherichia coli cells expressing the recombinant GST P1-1 enzyme indicate that bacterial cells, in response to NO treatment, are able to form the dinitrosyl diglutathionyl iron complex using intracellular iron and GSH.	Iron	236-240	glutathione S-transferase pi 1	Homo sapiens	113-121