PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16165096-2	2005	CHO-K1 cells stably express green fluorescent protein-5-lipoxygenase fusion protein (GFP-5LO), which is located predominantly in the nucleus, and is exported by anisomycin, hydrogen peroxide, and sorbitol, with activation of p38 MAPK.	Hydrogen Peroxide	173-190	arachidonate 5-lipoxygenase	Homo sapiens	54-68	
18074773-5	2007	Inhibition of metabolic pathways of 5-lipoxygenase or cyclooxygenase increased the destructive effect of H2O2 on the cells.	Hydrogen Peroxide	105-109	arachidonate 5-lipoxygenase	Homo sapiens	36-50	
11371199-9	2001	Lipid hydroperoxide added to selenide-treated 5LO could not reinstate the signal at g = 6.2, indicating an irreversible change of the coordination of the active site iron.	Hydrogen Peroxide	6-19	arachidonate 5-lipoxygenase	Homo sapiens	46-49	
10698703-6	2000	Addition of 5-lipoxygenase products 5-hydroperoxyeicosatetraenoic acid (5-HPETE) and leukotriene B(4), but not 5-hydroxyeicosatetraenoic acid (5-HETE) and leukotriene C(4), restored LPA-stimulated H(2)O(2) release in cells treated with the lipoxygenase inhibitors nordihydroguaiaretic acid and Zileuton.	Hydrogen Peroxide	197-205	arachidonate 5-lipoxygenase	Homo sapiens	12-26	
10880344-1	2000	In contrast to neutrophils or B-lymphocytes, cells of the monocytic lineage like rat macrophages, human peripheral blood monocytes and Mono Mac 6 cells contain a strong inhibitor of 5-lipoxygenase (5-LO) activity, which scavenges hydroperoxides and inhibits 5-LO activity in broken-cell preparations in the absence of exogenously added thiols.	Hydrogen Peroxide	230-244	arachidonate 5-lipoxygenase	Homo sapiens	182-196	
9375974-16	1997	LTB4 undergoes a H2O2-dependent oxidation that is inhibited by NAC but this is unlikely to account fully for the increased levels of LTB4, suggesting that NAC may increase LTB4 production by blocking the H2O2-dependent inhibition of a synthetic enzyme, such as 5-lipoxygenase.	Hydrogen Peroxide	204-208	arachidonate 5-lipoxygenase	Homo sapiens	261-275	
16465258-1	1997	We investigated the involvement of 5-lipoxygenase activity in the early phases of programmed cell death (PCD) induced by H2O2 or retinoids in different human tumour cells (erythroleukaemia, neuroblastoma, melanoma).	Hydrogen Peroxide	121-125	arachidonate 5-lipoxygenase	Homo sapiens	35-49	
16465258-6	1997	Conversely, the general lipoxygenase inhibitor nordihydroguaiaretic acid and the selective 5-lipoxygenase inhibitor caffeic acid protected the different tumour cells from H2O2-induced PCD to a similar extent.	Hydrogen Peroxide	171-175	arachidonate 5-lipoxygenase	Homo sapiens	91-105	
25912480-12	2015	This was necessary because of a strong impairment of 5-LOX activity by H2O2.	Hydrogen Peroxide	71-75	arachidonate 5-lipoxygenase	Homo sapiens	53-58	
9174105-6	1997	This elevation may be the consequence of an increased cellular hydroperoxide known to activate 5-lipoxygenase (5-LOX) activity and/or an increased arachidonic acid availability, due either to phospholipase A2 (PLA2) activation or inhibition of arachidonate reesterification into phospholipids.	Hydrogen Peroxide	63-76	arachidonate 5-lipoxygenase	Homo sapiens	95-109	
1446663-3	1992	The results of this investigation demonstrate that H2O2 generated during air oxidation of thiols is the main factor in non-turnover-dependent inactivation of purified recombinant human 5-lipoxygenase for the following reasons: catalase protects against oxygen-dependent inactivation of the enzyme in the presence of dithiothreitol; the active, stable enzyme can be prepared under aerobic conditions with the exclusion of dithiothreitol and contaminating metal ions; 10 microM H2O2 causes the rapid inactivation of the enzyme.	Hydrogen Peroxide	51-55	arachidonate 5-lipoxygenase	Homo sapiens	185-199	
1446663-3	1992	The results of this investigation demonstrate that H2O2 generated during air oxidation of thiols is the main factor in non-turnover-dependent inactivation of purified recombinant human 5-lipoxygenase for the following reasons: catalase protects against oxygen-dependent inactivation of the enzyme in the presence of dithiothreitol; the active, stable enzyme can be prepared under aerobic conditions with the exclusion of dithiothreitol and contaminating metal ions; 10 microM H2O2 causes the rapid inactivation of the enzyme.	Hydrogen Peroxide	476-480	arachidonate 5-lipoxygenase	Homo sapiens	185-199	
2018568-10	1991	These data are consistent with the hypothesis that L-656,224 reduces the oxidized form of the 5-lipoxygenase to an inactive form, with degradation of the inhibitor and regeneration of the active enzyme with hydroperoxides.	Hydrogen Peroxide	207-221	arachidonate 5-lipoxygenase	Homo sapiens	94-108	
3089841-0	1986	The importance of hydroperoxide activation for the detection and assay of mammalian 5-lipoxygenase.	Hydrogen Peroxide	18-31	arachidonate 5-lipoxygenase	Homo sapiens	84-98	
24906007-12	2014	Furthermore, our findings indicate that hypoxia-induced increases in cell proliferation and ALOX5 expression are dependent on H2O2 production, as administration of the antioxidant PEG-catalase blocks these effects and addition of H2O2 to HPAEC promotes proliferation.	Hydrogen Peroxide	126-130	arachidonate 5-lipoxygenase	Homo sapiens	92-97	
24906007-12	2014	Furthermore, our findings indicate that hypoxia-induced increases in cell proliferation and ALOX5 expression are dependent on H2O2 production, as administration of the antioxidant PEG-catalase blocks these effects and addition of H2O2 to HPAEC promotes proliferation.	Hydrogen Peroxide	230-234	arachidonate 5-lipoxygenase	Homo sapiens	92-97	
24906007-13	2014	Overall, these studies indicate that hypoxia exposure induces HPAEC proliferation by activating the ALOX5 pathway via the generation of H2O2.	Hydrogen Peroxide	136-140	arachidonate 5-lipoxygenase	Homo sapiens	100-105