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 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 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 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 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 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