PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2501113-2	1989	NADPH-dependent iron and drug redox cycling, as well as lipid peroxidation process were investigated in microsomes isolated from human term placenta.	Iron	16-20	2,4-dienoyl-CoA reductase 1	Homo sapiens	0-5	
2556968-14	1989	Since the cytosol normally maintains a highly oxidized NAD+/NADH redox ratio, it is interesting to speculate that increased availability of NADH from the oxidation of ethanol may support microsomal reduction of iron complexes, with the subsequent generation of reactive oxygen intermediates.	Iron	211-215	2,4-dienoyl-CoA reductase 1	Homo sapiens	140-144	
2501113-10	1989	Drastic peroxidative conditions involving superoxide and prolonged incubation in the presence of iron were found to destroy flavin nucleotides, inhibit NADPH:cytochrome P-450 reductase and inhibit propagation step of lipid peroxidation.	Iron	97-101	2,4-dienoyl-CoA reductase 1	Homo sapiens	152-157	
2501113-12	1989	Reactive oxo-complex formed between iron and superoxide is proposed as an ultimate species for the initiation of lipid peroxidation in microsomes from human term placenta as well as for the destruction of flavin nucleotides and inhibition of NADPH:cytochrome P-450 reductase as well as for impairment of promotion of lipid peroxidation under drastic peroxidative conditions.	Iron	36-40	2,4-dienoyl-CoA reductase 1	Homo sapiens	242-247	
7150343-0	1982	Adriamycin stimulates only the iron ion-induced, NADPH-dependent microsomal alkane formation.	Iron	31-35	2,4-dienoyl-CoA reductase 1	Homo sapiens	49-54	
16663575-0	1984	Cytosolic NADPH is the electron donor for extracellular fe reduction in iron-deficient bean roots.	Iron	56-58	2,4-dienoyl-CoA reductase 1	Homo sapiens	10-15	
16663575-0	1984	Cytosolic NADPH is the electron donor for extracellular fe reduction in iron-deficient bean roots.	Iron	72-76	2,4-dienoyl-CoA reductase 1	Homo sapiens	10-15	
16663575-2	1984	In iron-deficient plants, total NADP per gram fresh weight and the NADPH/NADP(+) ratio were twice the values found in iron-sufficient plants.	Iron	3-7	2,4-dienoyl-CoA reductase 1	Homo sapiens	67-72	
16663575-3	1984	The NADPH/NADP(+) ratio in iron-deficient plants was considerably lowered after a 2 minute incubation in 1 millimolar ferricyanide.	Iron	27-31	2,4-dienoyl-CoA reductase 1	Homo sapiens	4-9	
16663575-4	1984	Total NAD was not influenced by growth conditions and was mainly present in oxidized form.These results indicate that NADPH is the electron donor for the high Fe(III) reduction activity found in iron-deficient roots, a process that is part of the Fe-uptake mechanism.	Iron	195-199	2,4-dienoyl-CoA reductase 1	Homo sapiens	118-123	
16663575-4	1984	Total NAD was not influenced by growth conditions and was mainly present in oxidized form.These results indicate that NADPH is the electron donor for the high Fe(III) reduction activity found in iron-deficient roots, a process that is part of the Fe-uptake mechanism.	Iron	159-161	2,4-dienoyl-CoA reductase 1	Homo sapiens	118-123	
32409586-2	2020	It shares sequence homology with three enzymes (STEAP2-STEAP4) that catalyze the NADPH-dependent reduction of iron(III).	Iron	110-114	2,4-dienoyl-CoA reductase 1	Homo sapiens	81-86	
32409586-7	2020	Enzymatic assays in human cells revealed that STEAP1 promotes iron(III) reduction when fused to the intracellular NADPH-binding domain of its family member STEAP4, suggesting that STEAP1 functions as a ferric reductase in STEAP heterotrimers.	Iron	62-66	2,4-dienoyl-CoA reductase 1	Homo sapiens	114-119	
25688831-0	2015	Ferredoxin, in conjunction with NADPH and ferredoxin-NADP reductase, transfers electrons to the IscS/IscU complex to promote iron-sulfur cluster assembly.	Iron	125-129	2,4-dienoyl-CoA reductase 1	Homo sapiens	32-37	
11796730-5	2002	The structures provide a complete picture of the electron transfer chain from NADPH to the substrate, 5-iodouracil, spanning a distance of 56 A and involving FAD, four [Fe-S] clusters, and FMN as cofactors.	Iron	169-173	2,4-dienoyl-CoA reductase 1	Homo sapiens	78-83	
7548161-4	1995	NADPH would then donate two electrons, one to compound II for reduction of the iron and the other to the protein free radical.	Iron	79-83	2,4-dienoyl-CoA reductase 1	Homo sapiens	0-5	
7548161-5	1995	In this paper, we report calculations to find the dominant electron tunneling pathways between NADPH and the heme iron in the catalase from the peroxide-resistant mutant of Proteus mirabilis.	Iron	114-118	2,4-dienoyl-CoA reductase 1	Homo sapiens	95-100	
8083224-7	1994	A sequence encompassing a peptide corresponding to the uracil binding site was found between the NADPH/FAD-containing NH2-terminal portion of the protein and the iron-sulfur binding sites near to the COOH terminus.	Iron	162-166	2,4-dienoyl-CoA reductase 1	Homo sapiens	97-102	
2310194-0	1990	NADPH- and adriamycin-dependent microsomal release of iron and lipid peroxidation.	Iron	54-58	2,4-dienoyl-CoA reductase 1	Homo sapiens	0-5	
2154337-5	1990	In fact, lipid peroxidation initiated by a ferrous-oxygen complex (as in iron/NADPH-dependent peroxidation) was inhibited by AD 5 in a range of concentration of 2-4 mM.	Iron	73-77	2,4-dienoyl-CoA reductase 1	Homo sapiens	78-83	
2154337-6	1990	On the contrary, iron/NADPH-independent lipid peroxidation, where alkoxy radicals (RO.)	Iron	17-21	2,4-dienoyl-CoA reductase 1	Homo sapiens	22-27