PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	Selenium	87-95	glutathione peroxidase 2	Homo sapiens	20-26
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	Selenium	166-174	glutathione peroxidase 2	Homo sapiens	20-26
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	Selenium	166-174	glutathione peroxidase 2	Homo sapiens	148-154
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	Selenium	166-174	glutathione peroxidase 2	Homo sapiens	148-154
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	cgpx	192-196	glutathione peroxidase 2	Homo sapiens	20-26
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	Selenium	166-174	glutathione peroxidase 2	Homo sapiens	20-26
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	Selenium	166-174	glutathione peroxidase 2	Homo sapiens	148-154
10609889-4	1999	A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein.	Selenium	166-174	glutathione peroxidase 2	Homo sapiens	148-154
9914487-4	1999	The selenium-dependent expression of GI-GPx was analyzed in comparison with that of other GPx types at the level of mRNA and protein in HepG2 and CaCo-2 cells.	Selenium	4-12	glutathione peroxidase 2	Homo sapiens	37-43
9914487-5	1999	Furthermore, the selenocysteine insertion sequence (SECIS) efficiencies of GI-GPx, phospholipid hydroperoxide glutathione peroxidase (PHGPx) and cGPx in response to selenium were determined by a reporter-gene assay in human hepatoma cells and baby hamster kidney cells.	Selenocysteine	17-31	glutathione peroxidase 2	Homo sapiens	75-81
9914487-5	1999	Furthermore, the selenocysteine insertion sequence (SECIS) efficiencies of GI-GPx, phospholipid hydroperoxide glutathione peroxidase (PHGPx) and cGPx in response to selenium were determined by a reporter-gene assay in human hepatoma cells and baby hamster kidney cells.	Selenium	165-173	glutathione peroxidase 2	Homo sapiens	75-81
9914487-6	1999	GI-GPx mRNA levels increased during selenium deficiency, whereas cGPx mRNA levels decreased and PHGPx mRNA levels remained almost unaffected.	Selenium	36-44	glutathione peroxidase 2	Homo sapiens	0-6
9914487-8	1999	Upon selenium repletion immunoreactive GI-GPx protein reached a plateau after 10 h, whereas cGPx started to be expressed at 24 h and did not reach its maximum level before 3 days.	Selenium	5-13	glutathione peroxidase 2	Homo sapiens	39-45
9914487-11	1999	The high mRNA stability under selenium restriction, the speed of biosynthesis upon selenium repletion and the marginal effect of selenium on the SECIS efficiency indicate that of the GPx isotypes, GI-GPx ranks highest in the hierarchy of selenoproteins and point to a vital role of GI-GPx in the gastrointestinal tract.	Selenium	30-38	glutathione peroxidase 2	Homo sapiens	197-203
9914487-11	1999	The high mRNA stability under selenium restriction, the speed of biosynthesis upon selenium repletion and the marginal effect of selenium on the SECIS efficiency indicate that of the GPx isotypes, GI-GPx ranks highest in the hierarchy of selenoproteins and point to a vital role of GI-GPx in the gastrointestinal tract.	Selenium	83-91	glutathione peroxidase 2	Homo sapiens	197-203
9914487-11	1999	The high mRNA stability under selenium restriction, the speed of biosynthesis upon selenium repletion and the marginal effect of selenium on the SECIS efficiency indicate that of the GPx isotypes, GI-GPx ranks highest in the hierarchy of selenoproteins and point to a vital role of GI-GPx in the gastrointestinal tract.	Selenium	83-91	glutathione peroxidase 2	Homo sapiens	197-203
9433474-7	1997	The applicability of monofunctional peptide-dextran conjugates was demonstrated by investigating the titer and specificity of a polyclonal anti-peptide serum developed against human gastrointestinal glutathione peroxidase.	Peptides	36-43	glutathione peroxidase 2	Homo sapiens	182-221
9783826-8	1998	Deglycosylation of a GPRP also led to a dramatic increase in tannin-binding ability, showing that the carbohydrate side-chains prevent binding of tannin.	Tannins	61-67	glutathione peroxidase 2	Homo sapiens	21-25
9783826-8	1998	Deglycosylation of a GPRP also led to a dramatic increase in tannin-binding ability, showing that the carbohydrate side-chains prevent binding of tannin.	Carbohydrates	102-114	glutathione peroxidase 2	Homo sapiens	21-25
9783826-8	1998	Deglycosylation of a GPRP also led to a dramatic increase in tannin-binding ability, showing that the carbohydrate side-chains prevent binding of tannin.	Tannins	146-152	glutathione peroxidase 2	Homo sapiens	21-25
9433474-7	1997	The applicability of monofunctional peptide-dextran conjugates was demonstrated by investigating the titer and specificity of a polyclonal anti-peptide serum developed against human gastrointestinal glutathione peroxidase.	Dextrans	44-51	glutathione peroxidase 2	Homo sapiens	182-221
8428933-6	1993	Similar substrate specificities are found for GSHPx-1 and GSHPx-GI; they both catalyze the reduction of H2O2, tert-butyl hydroperoxide, cumene hydroperoxide, and linoleic acid hydroperoxide with glutathione, but not of phosphatidylcholine hydroperoxide.	Glutathione	195-206	glutathione peroxidase 2	Homo sapiens	58-66
9235981-9	1997	Structure-activity correlation showed that fibrinogen-like acyl-GPRP and acyl-GHRP could inhibit D. E association at the millimolar range, but in a manner different from fibrin-related GPR peptides did, which required the NH2 as well as Arg presence.	Arginine	237-240	glutathione peroxidase 2	Homo sapiens	64-68
8562283-7	1995	Also, selenium (Se) is a trace element essential for the activity of glutathione peroxidase (2) and type I iodothyronine 5-deiodinase (3).	Selenium	6-14	glutathione peroxidase 2	Homo sapiens	69-133
8562283-7	1995	Also, selenium (Se) is a trace element essential for the activity of glutathione peroxidase (2) and type I iodothyronine 5-deiodinase (3).	Selenium	16-18	glutathione peroxidase 2	Homo sapiens	69-133
7663337-4	1995	Fragment D was also co-crystallized with the ligand GPRP-amide, in which case the space group is consistent with P212121, unit cell dimensions a = 476 A, b = 82 A, c = 432 A.	Amides	57-62	glutathione peroxidase 2	Homo sapiens	52-56
8428933-6	1993	Similar substrate specificities are found for GSHPx-1 and GSHPx-GI; they both catalyze the reduction of H2O2, tert-butyl hydroperoxide, cumene hydroperoxide, and linoleic acid hydroperoxide with glutathione, but not of phosphatidylcholine hydroperoxide.	Hydrogen Peroxide	104-108	glutathione peroxidase 2	Homo sapiens	58-66
8428933-6	1993	Similar substrate specificities are found for GSHPx-1 and GSHPx-GI; they both catalyze the reduction of H2O2, tert-butyl hydroperoxide, cumene hydroperoxide, and linoleic acid hydroperoxide with glutathione, but not of phosphatidylcholine hydroperoxide.	tert-Butylhydroperoxide	110-134	glutathione peroxidase 2	Homo sapiens	58-66
8428933-6	1993	Similar substrate specificities are found for GSHPx-1 and GSHPx-GI; they both catalyze the reduction of H2O2, tert-butyl hydroperoxide, cumene hydroperoxide, and linoleic acid hydroperoxide with glutathione, but not of phosphatidylcholine hydroperoxide.	cumene hydroperoxide	136-156	glutathione peroxidase 2	Homo sapiens	58-66
8428933-6	1993	Similar substrate specificities are found for GSHPx-1 and GSHPx-GI; they both catalyze the reduction of H2O2, tert-butyl hydroperoxide, cumene hydroperoxide, and linoleic acid hydroperoxide with glutathione, but not of phosphatidylcholine hydroperoxide.	linoleic acid hydroperoxide	162-189	glutathione peroxidase 2	Homo sapiens	58-66
8428933-6	1993	Similar substrate specificities are found for GSHPx-1 and GSHPx-GI; they both catalyze the reduction of H2O2, tert-butyl hydroperoxide, cumene hydroperoxide, and linoleic acid hydroperoxide with glutathione, but not of phosphatidylcholine hydroperoxide.	phosphatidylcholine hydroperoxide	219-252	glutathione peroxidase 2	Homo sapiens	58-66
8428933-9	1993	In fact, GSHPx-GI appears to be the major glutathione-dependent peroxidase activity in rodent GI tract.	Glutathione	42-53	glutathione peroxidase 2	Homo sapiens	9-17
8428933-10	1993	This finding suggests that GSHPx-GI could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides.	Lipid Peroxides	112-132	glutathione peroxidase 2	Homo sapiens	27-35
8428933-11	1993	In conclusion, we have demonstrated that GSHPx-GI is the fourth member in the selenium-dependent glutathione peroxidase family, in addition to GSHPx-1, GSHPx-P, and phospholipid hydroperoxide glutathione peroxidase (PHGPX).	Selenium	78-86	glutathione peroxidase 2	Homo sapiens	41-49
35398749-0	2022	Regulatory mechanism of alpha-hederin upon cisplatin sensibility in NSCLC at safe dose by destroying GSS/GSH/GPX2 axis-mediated glutathione oxidation-reduction system.	beta-hederin	24-37	glutathione peroxidase 2	Homo sapiens	109-113
34678723-6	2021	Furthermore, we found that corosolic acid destabilized the glutathione peroxidase 2-mediated redox system, which increased mitochondrial and liposomal oxidative stress.	corosolic acid	27-41	glutathione peroxidase 2	Homo sapiens	59-83
34307361-17	2021	In addition, silencing GPX2 or DDIT4 could partially reverse the erastin-induced ferroptosis.	erastin	65-72	glutathione peroxidase 2	Homo sapiens	23-27
1397508-4	1992	The purified GPRP had a molecular weight of 78 kDa as analyzed by SDS-PAGE.	Sodium Dodecyl Sulfate	66-69	glutathione peroxidase 2	Homo sapiens	13-17
1397508-16	1992	The GPRP bound to hydroxyapatite and this binding could be partially inhibited by preincubation of the hydroxyapatite with parotid or submandibular saliva.	Durapatite	18-32	glutathione peroxidase 2	Homo sapiens	4-8
1397508-16	1992	The GPRP bound to hydroxyapatite and this binding could be partially inhibited by preincubation of the hydroxyapatite with parotid or submandibular saliva.	Durapatite	103-117	glutathione peroxidase 2	Homo sapiens	4-8
34954079-10	2022	Furthermore, significant correlations were found between NQO1 and GPX2 demethylation and human intestinal tissue iron-status, thus suggesting that these iron-mediated epigenetic modifications are likely in iron-replete enterocytes.	Iron	153-157	glutathione peroxidase 2	Homo sapiens	66-70
35398749-6	2022	Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system.	beta-hederin	82-95	glutathione peroxidase 2	Homo sapiens	146-150
35398749-8	2022	Taken together, the study provided molecular data to confirm that alpha-hederin induced ferroptosis, apoptosis, and membrane permeabilization in NSCLC by destroying the GSS/GSH/GPX2 axis-mediated GSH oxidation-reduction system at a safe and low-toxicity dose.	beta-hederin	66-79	glutathione peroxidase 2	Homo sapiens	177-181
35398749-0	2022	Regulatory mechanism of alpha-hederin upon cisplatin sensibility in NSCLC at safe dose by destroying GSS/GSH/GPX2 axis-mediated glutathione oxidation-reduction system.	Cisplatin	43-52	glutathione peroxidase 2	Homo sapiens	109-113
35398749-8	2022	Taken together, the study provided molecular data to confirm that alpha-hederin induced ferroptosis, apoptosis, and membrane permeabilization in NSCLC by destroying the GSS/GSH/GPX2 axis-mediated GSH oxidation-reduction system at a safe and low-toxicity dose.	Glutathione	173-176	glutathione peroxidase 2	Homo sapiens	177-181
35398749-8	2022	Taken together, the study provided molecular data to confirm that alpha-hederin induced ferroptosis, apoptosis, and membrane permeabilization in NSCLC by destroying the GSS/GSH/GPX2 axis-mediated GSH oxidation-reduction system at a safe and low-toxicity dose.	Glutathione	196-199	glutathione peroxidase 2	Homo sapiens	177-181
35398749-0	2022	Regulatory mechanism of alpha-hederin upon cisplatin sensibility in NSCLC at safe dose by destroying GSS/GSH/GPX2 axis-mediated glutathione oxidation-reduction system.	Glutathione	105-108	glutathione peroxidase 2	Homo sapiens	109-113
35398749-0	2022	Regulatory mechanism of alpha-hederin upon cisplatin sensibility in NSCLC at safe dose by destroying GSS/GSH/GPX2 axis-mediated glutathione oxidation-reduction system.	Glutathione	128-139	glutathione peroxidase 2	Homo sapiens	109-113
35398749-6	2022	Proteomics, metabolomics, and high-throughput sequencing detection confirmed that alpha-hederin treatment downregulated glutathione peroxidase 2 (GPX2), and glutathione synthase (GSS) expression suppressed the synthesis of glutathione (GSH), which destroyed the GSH redox system.	beta-hederin	82-95	glutathione peroxidase 2	Homo sapiens	120-144
35104504-9	2022	Using exclusion-based techniques, we show that for the RBP IGF2BP1 in cultured mammary epithelial cells, mRNA binding partners are enriched in mRNAs important for de-toxifying superoxides (specifically GPX-1 and GPX-2) and other mRNAs encoding mitochondrial proteins.	Superoxides	176-187	glutathione peroxidase 2	Homo sapiens	212-217
34045966-4	2021	Meanwhile, CD13 can activate NRF1 and up-regulate ROS scavenging genes transcription, such as SOD1, GPX1, GPX2 and GPX3, leading to down-regulation of intracellular ROS level and reducing the sensitivity of cells to chemotherapy agent.	ros	50-53	glutathione peroxidase 2	Homo sapiens	106-110
35204227-8	2022	Moreover, ATRA treatment prevented TGEV-induced ROS and MDA production and the upregulation of P38MAPK phosphorylation level, which is related to the increase in the activities of antioxidant enzymes (SOD, CAT, and T-AOC) and the mRNA abundance of antioxidant-related genes (GPX1, GPX2, SOD1, CAT, GCLC, and GCLM).	Tretinoin	10-14	glutathione peroxidase 2	Homo sapiens	281-285
35162241-8	2022	A low dose of SWCNTs-COOH induced ROS generation and increased the expression of catalase, MnSOD, CuZnSOD, and SOD-2 mRNA but decreased the expression of GPX-2 and GPX-3 mRNA in human monocytes.	Carbonic Acid	21-25	glutathione peroxidase 2	Homo sapiens	154-159
35193955-2	2022	GPx2 loss stimulates malignant progression due to reactive oxygen species/hypoxia inducible factor-alpha (HIF1alpha)/VEGFA (vascular endothelial growth factor A) signaling, causing poor perfusion and hypoxia, which were reversed by GPx2 reexpression or HIF1alpha inhibition.	Oxygen	59-65	glutathione peroxidase 2	Homo sapiens	0-4
35193955-2	2022	GPx2 loss stimulates malignant progression due to reactive oxygen species/hypoxia inducible factor-alpha (HIF1alpha)/VEGFA (vascular endothelial growth factor A) signaling, causing poor perfusion and hypoxia, which were reversed by GPx2 reexpression or HIF1alpha inhibition.	Oxygen	59-65	glutathione peroxidase 2	Homo sapiens	232-236
2827786-9	1988	Binding of GPRP-fibrin (soluble fibrin oligomers formed in the presence of 1 mM Gly-Pro-Arg-Pro) to ADP-stimulated platelets was also inhibited by a monoclonal antibody directed against the GPIIb-IIIa complex.	glycyl-prolyl-arginyl-proline	80-95	glutathione peroxidase 2	Homo sapiens	11-15
2827786-9	1988	Binding of GPRP-fibrin (soluble fibrin oligomers formed in the presence of 1 mM Gly-Pro-Arg-Pro) to ADP-stimulated platelets was also inhibited by a monoclonal antibody directed against the GPIIb-IIIa complex.	Adenosine Diphosphate	100-103	glutathione peroxidase 2	Homo sapiens	11-15
2827787-3	1988	Synthetic GPRP and GHRP, corresponding to the N-terminal tripeptide sequence of the fibrin alpha-chains and the tetrapeptide sequence of the beta-chains, respectively, were minimally effective in blocking soluble fibrin polymer binding to ADP-stimulated platelets.	tripeptide K-26	57-67	glutathione peroxidase 2	Homo sapiens	10-14
29662611-9	2018	Our findings demonstrated that GPX2 plays an important role in bladder carcinogenesis through the regulation of apoptosis against intracellular ROS, and may be considered as a novel biomarker or therapeutic target in bladder cancer.	Reactive Oxygen Species	144-147	glutathione peroxidase 2	Homo sapiens	31-35
32215178-3	2020	The knockdown of GPX2 expression in A549/DDP cells inhibited cell proliferation in vitro and in vivo, decreased the IC50 values of DDP, induced apoptosis, inhibited the activities of GSH-Px and superoxide dismutase (SOD), inhibited ATP production and glucose uptake, and increased malondialdehyde (MDA) and reactive oxygen species (ROS) production; while GPX2 overexpression in A549 cells resulted in the opposite effects.	Reactive Oxygen Species	307-330	glutathione peroxidase 2	Homo sapiens	17-21
32215178-3	2020	The knockdown of GPX2 expression in A549/DDP cells inhibited cell proliferation in vitro and in vivo, decreased the IC50 values of DDP, induced apoptosis, inhibited the activities of GSH-Px and superoxide dismutase (SOD), inhibited ATP production and glucose uptake, and increased malondialdehyde (MDA) and reactive oxygen species (ROS) production; while GPX2 overexpression in A549 cells resulted in the opposite effects.	Reactive Oxygen Species	332-335	glutathione peroxidase 2	Homo sapiens	17-21
32215178-4	2020	Using gene set enrichment analysis (GSEA), we found that GPX2 may be involved in DDP resistance through mediating drug metabolism, the cell cycle, DNA repair and energy metabolism, and the regulation of an ATP-binding cassette (ABC) transporters member ABCB6, which is one of the hallmark genes in glycolysis.	gsea	36-40	glutathione peroxidase 2	Homo sapiens	57-61
32215178-5	2020	Moreover, immunohistochemistry revealed that GPX2 was upregulated in 58.6% (89/152) of LUAD cases, and elevated GPX2 expression was correlated with high expression of ABCB6, high 18-fluorodeoxyglucose (18F-FDG) uptake, and adverse disease-free survival (DFS) in our cohort.	18-fluorodeoxyglucose	179-200	glutathione peroxidase 2	Homo sapiens	112-116
32215178-5	2020	Moreover, immunohistochemistry revealed that GPX2 was upregulated in 58.6% (89/152) of LUAD cases, and elevated GPX2 expression was correlated with high expression of ABCB6, high 18-fluorodeoxyglucose (18F-FDG) uptake, and adverse disease-free survival (DFS) in our cohort.	Fluorodeoxyglucose F18	202-209	glutathione peroxidase 2	Homo sapiens	112-116
32009948-6	2019	Oxidative stress induced by pimozide caused changes in the expression of antioxidant enzymes (SOD1, peroxiredoxin 6, and glutathione peroxidase 2) and CISD2.	Pimozide	28-36	glutathione peroxidase 2	Homo sapiens	121-145
31765890-1	2020	Glutathione peroxidase 2 (GPx2) is one of the five selenoprotein GPxs having a selenocysteine in the active center.	Selenocysteine	79-93	glutathione peroxidase 2	Homo sapiens	0-24
31765890-1	2020	Glutathione peroxidase 2 (GPx2) is one of the five selenoprotein GPxs having a selenocysteine in the active center.	Selenocysteine	79-93	glutathione peroxidase 2	Homo sapiens	26-30
31765890-9	2020	Under unstimulated conditions, the levels of the COX-derived prostaglandins PGE2 and PGD2 were enhanced in GPx2 as well as in GPx1 kd compared to control cells.	Dinoprostone	61-80	glutathione peroxidase 2	Homo sapiens	107-111
31765890-11	2020	Taken together, GPx2 and GPx1 have overlapping functions in controlling inflammatory lipid mediator synthesis and, most probably, exert their anti-inflammatory effects by preventing excessive PGE2 production.	Dinoprostone	192-196	glutathione peroxidase 2	Homo sapiens	16-20
31695405-0	2019	GPX2 suppression of H2O2 stress regulates cervical cancer metastasis and apoptosis via activation of the beta-catenin-WNT pathway.	Water	20-24	glutathione peroxidase 2	Homo sapiens	0-4
31695405-8	2019	GPX2 was determined to reduce apoptotic damage by reducing hydroperoxides.	Hydrogen Peroxide	59-73	glutathione peroxidase 2	Homo sapiens	0-4
30212802-6	2018	TXNRD1 and GPX2 protein expression and enzymatic activity were significantly greater upon Se supplementation (p < 0.05).	Selenium	90-92	glutathione peroxidase 2	Homo sapiens	11-15
30208132-6	2018	CONCLUSION: Cultured fibroblasts obtained from burn patients and treated with vitamin C resulted in 10 differentially expressed genes, all overexpressed, with DUOX1, GPX5, GPX2 and PTGS1 being of most interest.	Ascorbic Acid	78-87	glutathione peroxidase 2	Homo sapiens	172-176
33963958-1	2021	BACKGROUND: CD44 variant 9 (CD44v9) has been reported to suppress reactive oxygen spices (ROS) in association with antioxidant factors such as glutathione (GSH) and glutathione peroxidase 2 (GPx2), resulting in promoted tumor growth.	reactive oxygen spices	66-88	glutathione peroxidase 2	Homo sapiens	165-189
33963958-1	2021	BACKGROUND: CD44 variant 9 (CD44v9) has been reported to suppress reactive oxygen spices (ROS) in association with antioxidant factors such as glutathione (GSH) and glutathione peroxidase 2 (GPx2), resulting in promoted tumor growth.	reactive oxygen spices	66-88	glutathione peroxidase 2	Homo sapiens	191-195
33963958-1	2021	BACKGROUND: CD44 variant 9 (CD44v9) has been reported to suppress reactive oxygen spices (ROS) in association with antioxidant factors such as glutathione (GSH) and glutathione peroxidase 2 (GPx2), resulting in promoted tumor growth.	Glutathione	143-154	glutathione peroxidase 2	Homo sapiens	191-195
33963958-1	2021	BACKGROUND: CD44 variant 9 (CD44v9) has been reported to suppress reactive oxygen spices (ROS) in association with antioxidant factors such as glutathione (GSH) and glutathione peroxidase 2 (GPx2), resulting in promoted tumor growth.	Glutathione	156-159	glutathione peroxidase 2	Homo sapiens	191-195
31774184-4	2020	The regulatory function of GPX2 in PC was explored by treatment with short hairpin RNA against GPX2 or LiCl (activator of wingless-type MMTV integration site [Wnt] pathway) in PC cells.	Lithium Chloride	103-107	glutathione peroxidase 2	Homo sapiens	27-31
31774184-11	2020	Furthermore, the trend of EMT and invasion and metastasis of PC induced by the LiCl-activated Wnt pathway was reversed when the GPX2 was silenced.	Lithium Chloride	79-83	glutathione peroxidase 2	Homo sapiens	128-132
32215178-0	2020	Elevated Glutathione Peroxidase 2 Expression Promotes Cisplatin Resistance in Lung Adenocarcinoma.	Cisplatin	54-63	glutathione peroxidase 2	Homo sapiens	9-33
32215178-1	2020	The aim of this study was to explore the roles of GPX2, a member of the glutathione peroxidase family (GPXs, GSH-Px), in cisplatin (DDP) resistance in lung adenocarcinoma (LUAD).	gsh-px	109-115	glutathione peroxidase 2	Homo sapiens	50-54
32215178-1	2020	The aim of this study was to explore the roles of GPX2, a member of the glutathione peroxidase family (GPXs, GSH-Px), in cisplatin (DDP) resistance in lung adenocarcinoma (LUAD).	Cisplatin	121-130	glutathione peroxidase 2	Homo sapiens	50-54
32215178-1	2020	The aim of this study was to explore the roles of GPX2, a member of the glutathione peroxidase family (GPXs, GSH-Px), in cisplatin (DDP) resistance in lung adenocarcinoma (LUAD).	Cisplatin	132-135	glutathione peroxidase 2	Homo sapiens	50-54
32215178-3	2020	The knockdown of GPX2 expression in A549/DDP cells inhibited cell proliferation in vitro and in vivo, decreased the IC50 values of DDP, induced apoptosis, inhibited the activities of GSH-Px and superoxide dismutase (SOD), inhibited ATP production and glucose uptake, and increased malondialdehyde (MDA) and reactive oxygen species (ROS) production; while GPX2 overexpression in A549 cells resulted in the opposite effects.	gsh-px	183-189	glutathione peroxidase 2	Homo sapiens	17-21
32215178-3	2020	The knockdown of GPX2 expression in A549/DDP cells inhibited cell proliferation in vitro and in vivo, decreased the IC50 values of DDP, induced apoptosis, inhibited the activities of GSH-Px and superoxide dismutase (SOD), inhibited ATP production and glucose uptake, and increased malondialdehyde (MDA) and reactive oxygen species (ROS) production; while GPX2 overexpression in A549 cells resulted in the opposite effects.	Adenosine Triphosphate	232-235	glutathione peroxidase 2	Homo sapiens	17-21
32215178-3	2020	The knockdown of GPX2 expression in A549/DDP cells inhibited cell proliferation in vitro and in vivo, decreased the IC50 values of DDP, induced apoptosis, inhibited the activities of GSH-Px and superoxide dismutase (SOD), inhibited ATP production and glucose uptake, and increased malondialdehyde (MDA) and reactive oxygen species (ROS) production; while GPX2 overexpression in A549 cells resulted in the opposite effects.	Glucose	251-258	glutathione peroxidase 2	Homo sapiens	17-21
32215178-3	2020	The knockdown of GPX2 expression in A549/DDP cells inhibited cell proliferation in vitro and in vivo, decreased the IC50 values of DDP, induced apoptosis, inhibited the activities of GSH-Px and superoxide dismutase (SOD), inhibited ATP production and glucose uptake, and increased malondialdehyde (MDA) and reactive oxygen species (ROS) production; while GPX2 overexpression in A549 cells resulted in the opposite effects.	Malondialdehyde	281-296	glutathione peroxidase 2	Homo sapiens	17-21
32215178-3	2020	The knockdown of GPX2 expression in A549/DDP cells inhibited cell proliferation in vitro and in vivo, decreased the IC50 values of DDP, induced apoptosis, inhibited the activities of GSH-Px and superoxide dismutase (SOD), inhibited ATP production and glucose uptake, and increased malondialdehyde (MDA) and reactive oxygen species (ROS) production; while GPX2 overexpression in A549 cells resulted in the opposite effects.	Malondialdehyde	298-301	glutathione peroxidase 2	Homo sapiens	17-21
31417181-9	2019	We demonstrated that the concomitant knockdown of four of these genes products, GPX2, GLRX, ALDH3A1, and PDK4, significantly increased ROS-dependent caspase activation, thus partially mimicking the consequences of NLUCAT1 inactivation in LUAD cells.	ros	135-138	glutathione peroxidase 2	Homo sapiens	80-84
27922182-0	2017	Retinoid derivative Tp80 exhibits anti-hepatitis C virus activity through restoration of GI-GPx expression.	Retinoids	0-8	glutathione peroxidase 2	Homo sapiens	89-95
28916653-3	2017	YAP activation led to excessive accumulation of reactive oxygen species (ROS) by downregulating the antioxidant enzyme GPX2 in a manner related to p63 blockade.	Reactive Oxygen Species	48-71	glutathione peroxidase 2	Homo sapiens	119-123
28916653-3	2017	YAP activation led to excessive accumulation of reactive oxygen species (ROS) by downregulating the antioxidant enzyme GPX2 in a manner related to p63 blockade.	Reactive Oxygen Species	73-76	glutathione peroxidase 2	Homo sapiens	119-123
29020613-4	2017	Excess GPX2 leads to excess glutathione-mediated reactive oxygen species scavenging activity that blunts the DNA damage response and apoptosis.	Glutathione	28-39	glutathione peroxidase 2	Homo sapiens	7-11
29020613-4	2017	Excess GPX2 leads to excess glutathione-mediated reactive oxygen species scavenging activity that blunts the DNA damage response and apoptosis.	Reactive Oxygen Species	49-72	glutathione peroxidase 2	Homo sapiens	7-11
29156796-9	2017	Hypoxia-induced DNA damage was prevented by expressing the hydroperoxide-scavenging enzyme glutathione peroxidase-2 (GPx2), indicating that reactive oxygen species mediate hypoxia-induced DNA damage.	Hydrogen Peroxide	59-72	glutathione peroxidase 2	Homo sapiens	91-115
29156796-9	2017	Hypoxia-induced DNA damage was prevented by expressing the hydroperoxide-scavenging enzyme glutathione peroxidase-2 (GPx2), indicating that reactive oxygen species mediate hypoxia-induced DNA damage.	Hydrogen Peroxide	59-72	glutathione peroxidase 2	Homo sapiens	117-121
29156796-9	2017	Hypoxia-induced DNA damage was prevented by expressing the hydroperoxide-scavenging enzyme glutathione peroxidase-2 (GPx2), indicating that reactive oxygen species mediate hypoxia-induced DNA damage.	Reactive Oxygen Species	140-163	glutathione peroxidase 2	Homo sapiens	91-115
29156796-9	2017	Hypoxia-induced DNA damage was prevented by expressing the hydroperoxide-scavenging enzyme glutathione peroxidase-2 (GPx2), indicating that reactive oxygen species mediate hypoxia-induced DNA damage.	Reactive Oxygen Species	140-163	glutathione peroxidase 2	Homo sapiens	117-121
27922182-6	2017	Furthermore, comparison of Tp80 with other retinoid derivatives revealed Tp80 shows best potency in both GI-GPx restoration and anti-HCV activity among compounds we examined.	Retinoids	43-51	glutathione peroxidase 2	Homo sapiens	105-111
28558074-0	2017	Individual expression features of GPX2, NQO1 and SQSTM1 transcript variants induced by hydrogen peroxide treatment in HeLa cells.	Hydrogen Peroxide	87-104	glutathione peroxidase 2	Homo sapiens	34-38
28558074-7	2017	In the present paper we analyzed whether transcript variants of GPX2, NQO1 and SQSTM1 were characterized by individual features of expression when HeLa cells were exposed to pro-oxidative stimulation with hydrogen peroxide.	Hydrogen Peroxide	205-222	glutathione peroxidase 2	Homo sapiens	64-68
26599691-6	2016	The result indicated that the expression of glutathione-dependent enzymes (GSTA, M, P, and GPX2) was sensitive to oxygen and medium type.	Glutathione	44-55	glutathione peroxidase 2	Homo sapiens	91-95
26599691-6	2016	The result indicated that the expression of glutathione-dependent enzymes (GSTA, M, P, and GPX2) was sensitive to oxygen and medium type.	Oxygen	114-120	glutathione peroxidase 2	Homo sapiens	91-95
25488369-1	2015	Gastrointestinal glutathione peroxidase (GI-GPx, GPx2) is a selenium-dependent enzyme and regarded as the first line of defense against oxidative stress caused by ingested pro-oxidants or gut microbes.	Selenium	60-68	glutathione peroxidase 2	Homo sapiens	0-39
25488369-1	2015	Gastrointestinal glutathione peroxidase (GI-GPx, GPx2) is a selenium-dependent enzyme and regarded as the first line of defense against oxidative stress caused by ingested pro-oxidants or gut microbes.	Selenium	60-68	glutathione peroxidase 2	Homo sapiens	41-47
25488369-1	2015	Gastrointestinal glutathione peroxidase (GI-GPx, GPx2) is a selenium-dependent enzyme and regarded as the first line of defense against oxidative stress caused by ingested pro-oxidants or gut microbes.	Selenium	60-68	glutathione peroxidase 2	Homo sapiens	49-53
25488369-2	2015	As the essential part of the catalytic site of GPx2, selenocysteine (Sec) is encoded by an in-frame UGA stop codon, which makes the expression of human GPx2 (hGPx2) using traditional recombinant DNA technology difficult.	Selenocysteine	53-67	glutathione peroxidase 2	Homo sapiens	47-51
25488369-2	2015	As the essential part of the catalytic site of GPx2, selenocysteine (Sec) is encoded by an in-frame UGA stop codon, which makes the expression of human GPx2 (hGPx2) using traditional recombinant DNA technology difficult.	Selenocysteine	53-67	glutathione peroxidase 2	Homo sapiens	152-156
25488369-2	2015	As the essential part of the catalytic site of GPx2, selenocysteine (Sec) is encoded by an in-frame UGA stop codon, which makes the expression of human GPx2 (hGPx2) using traditional recombinant DNA technology difficult.	Selenocysteine	53-67	glutathione peroxidase 2	Homo sapiens	158-163
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Cysteine	123-131	glutathione peroxidase 2	Homo sapiens	42-47
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Cysteine	123-131	glutathione peroxidase 2	Homo sapiens	61-66
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Cysteine	133-136	glutathione peroxidase 2	Homo sapiens	42-47
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Cysteine	133-136	glutathione peroxidase 2	Homo sapiens	61-66
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Serine	165-171	glutathione peroxidase 2	Homo sapiens	42-47
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Serine	165-171	glutathione peroxidase 2	Homo sapiens	61-66
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Serine	173-176	glutathione peroxidase 2	Homo sapiens	42-47
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Serine	173-176	glutathione peroxidase 2	Homo sapiens	61-66
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Cysteine	241-244	glutathione peroxidase 2	Homo sapiens	42-47
25488369-3	2015	In order to produce bioactive recombinant hGPx2, the gene of hGPx2 was designed with the conversion of the codons for four cysteine (Cys) residues to the codons for serine (Ser) residues and the codon for Sec-40 was changed to the codon for Cys.	Cysteine	241-244	glutathione peroxidase 2	Homo sapiens	61-66
25488369-4	2015	This recombinant seleno-hGPx2 mutant was obtained using a single protein production system in a cysteine (Cys) auxotrophic strain, in which Sec was introduced into the protein via tRNA(Cys) misleading.	Cysteine	96-104	glutathione peroxidase 2	Homo sapiens	24-29
25488369-4	2015	This recombinant seleno-hGPx2 mutant was obtained using a single protein production system in a cysteine (Cys) auxotrophic strain, in which Sec was introduced into the protein via tRNA(Cys) misleading.	Cysteine	106-109	glutathione peroxidase 2	Homo sapiens	24-29
23151063-5	2013	The dissociation constant of the complex formed from the D-dimer and 4-D15L8-GPRP labeled with fluorescein was determined by fluorescense titration and found to be 3 nM, an affinity 4 orders of magnitude higher than that of free GPRP.	Fluorescein	95-106	glutathione peroxidase 2	Homo sapiens	77-81
24562575-4	2014	Next, we determined the proliferation rate and level of reactive oxygen species (ROS) in GPX2-small interfering RNA (siRNA)-transfected CRPC cells.	Reactive Oxygen Species	56-79	glutathione peroxidase 2	Homo sapiens	89-93
24562575-4	2014	Next, we determined the proliferation rate and level of reactive oxygen species (ROS) in GPX2-small interfering RNA (siRNA)-transfected CRPC cells.	Reactive Oxygen Species	81-84	glutathione peroxidase 2	Homo sapiens	89-93
24562575-12	2014	These findings suggest that GPX2 is a prognostic marker in CRPC and affects proliferation of prostate cancer under androgen depletion partially through protection against ROS signaling.	Reactive Oxygen Species	171-174	glutathione peroxidase 2	Homo sapiens	28-32
24561720-6	2014	We also observed that treatment with NG in PQ-exposed BEAS-2B cells can significantly induce the expression of antioxidant-related genes, including GPX2, GPX3, GPX5, and GPX7.	naringenin	37-39	glutathione peroxidase 2	Homo sapiens	148-152
24561720-6	2014	We also observed that treatment with NG in PQ-exposed BEAS-2B cells can significantly induce the expression of antioxidant-related genes, including GPX2, GPX3, GPX5, and GPX7.	Paraquat	43-45	glutathione peroxidase 2	Homo sapiens	148-152
23201771-4	2013	MAJOR CONCLUSIONS: GPxs are involved in balancing the H2O2 homeostasis in signalling cascades, e.g. in the insulin signalling pathway by GPx1; GPx2 plays a dual role in carcinogenesis depending on the mode of initiation and cancer stage; GPx3 is membrane associated possibly explaining a peroxidatic function despite low plasma concentrations of GSH; GPx4 has novel roles in the regulation of apoptosis and, together with GPx5, in male fertility.	Hydrogen Peroxide	54-58	glutathione peroxidase 2	Homo sapiens	143-147
23201771-4	2013	MAJOR CONCLUSIONS: GPxs are involved in balancing the H2O2 homeostasis in signalling cascades, e.g. in the insulin signalling pathway by GPx1; GPx2 plays a dual role in carcinogenesis depending on the mode of initiation and cancer stage; GPx3 is membrane associated possibly explaining a peroxidatic function despite low plasma concentrations of GSH; GPx4 has novel roles in the regulation of apoptosis and, together with GPx5, in male fertility.	Glutathione	346-349	glutathione peroxidase 2	Homo sapiens	143-147
22894151-1	2013	A series of shorter peptide analogues of Bactenecin7 (RP, PRP, GPRP and RPRP) were synthesized and conjugated to 3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid to study the effect of conjugation.	bactenecin7	41-52	glutathione peroxidase 2	Homo sapiens	63-67
25261240-0	2014	GPx2 suppression of H2O2 stress links the formation of differentiated tumor mass to metastatic capacity in colorectal cancer.	Hydrogen Peroxide	20-24	glutathione peroxidase 2	Homo sapiens	0-4
25261240-2	2014	Here, we studied how the H2O2-reducing enzyme glutathione peroxidase 2 (GPx2) regulates H2O2 stress and differentiation in patient-derived "colonosphere" cultures.	Hydrogen Peroxide	25-29	glutathione peroxidase 2	Homo sapiens	46-70
25261240-2	2014	Here, we studied how the H2O2-reducing enzyme glutathione peroxidase 2 (GPx2) regulates H2O2 stress and differentiation in patient-derived "colonosphere" cultures.	Hydrogen Peroxide	25-29	glutathione peroxidase 2	Homo sapiens	72-76
25261240-2	2014	Here, we studied how the H2O2-reducing enzyme glutathione peroxidase 2 (GPx2) regulates H2O2 stress and differentiation in patient-derived "colonosphere" cultures.	Hydrogen Peroxide	88-92	glutathione peroxidase 2	Homo sapiens	46-70
25261240-2	2014	Here, we studied how the H2O2-reducing enzyme glutathione peroxidase 2 (GPx2) regulates H2O2 stress and differentiation in patient-derived "colonosphere" cultures.	Hydrogen Peroxide	88-92	glutathione peroxidase 2	Homo sapiens	72-76
25261240-3	2014	GPx2 silencing caused accumulation of radical oxygen species, sensitization to H2O2-induced apoptosis, and strongly reduced clone- and metastasis-forming capacity.	Oxygen	46-52	glutathione peroxidase 2	Homo sapiens	0-4
25261240-3	2014	GPx2 silencing caused accumulation of radical oxygen species, sensitization to H2O2-induced apoptosis, and strongly reduced clone- and metastasis-forming capacity.	Hydrogen Peroxide	79-83	glutathione peroxidase 2	Homo sapiens	0-4
25261240-7	2014	Finally, GPx2 expression was inversely correlated with H2O2-stress signatures in human colon tumor cohorts, but positively correlated with differentiation and proliferation.	Hydrogen Peroxide	55-59	glutathione peroxidase 2	Homo sapiens	9-13
25261240-9	2014	We conclude that H2O2 neutralization by GPx2 is essential for maintaining clonogenic and metastatic capacity, but also for the generation of differentiated proliferating tumor mass.	Hydrogen Peroxide	17-21	glutathione peroxidase 2	Homo sapiens	40-44
23934683-0	2013	Selenium alters miRNA profile in an intestinal cell line: evidence that miR-185 regulates expression of GPX2 and SEPSH2.	Selenium	0-8	glutathione peroxidase 2	Homo sapiens	104-108
23151063-5	2013	The dissociation constant of the complex formed from the D-dimer and 4-D15L8-GPRP labeled with fluorescein was determined by fluorescense titration and found to be 3 nM, an affinity 4 orders of magnitude higher than that of free GPRP.	Fluorescein	95-106	glutathione peroxidase 2	Homo sapiens	229-233
22758632-6	2012	The model further revealed a GPx2-independent decrease in tumor development by selenium (Se) and detrimental effects of the Nrf2-activator sulforaphane in moderate Se deficiency.	Selenium	79-87	glutathione peroxidase 2	Homo sapiens	29-33
22820176-0	2012	TrxR1 and GPx2 are potently induced by isothiocyanates and selenium, and mutually cooperate to protect Caco-2 cells against free radical-mediated cell death.	Isothiocyanates	39-54	glutathione peroxidase 2	Homo sapiens	10-14
22820176-0	2012	TrxR1 and GPx2 are potently induced by isothiocyanates and selenium, and mutually cooperate to protect Caco-2 cells against free radical-mediated cell death.	Selenium	59-67	glutathione peroxidase 2	Homo sapiens	10-14
22820176-0	2012	TrxR1 and GPx2 are potently induced by isothiocyanates and selenium, and mutually cooperate to protect Caco-2 cells against free radical-mediated cell death.	Free Radicals	124-136	glutathione peroxidase 2	Homo sapiens	10-14
22820176-4	2012	Therefore, this investigation examined the effect of two forms of selenium, selenium-methylselenocysteine and sodium selenite, both individually and in combination with two ITCs, sulforaphane or iberin, on the expression of the two selenoenzymes, thioredoxin reductase 1 (TrxR1) and gastrointestinal glutathione peroxidase (GPx2), which are targets of ITCs, in Caco-2 cells.	Selenium	66-74	glutathione peroxidase 2	Homo sapiens	283-322
22820176-4	2012	Therefore, this investigation examined the effect of two forms of selenium, selenium-methylselenocysteine and sodium selenite, both individually and in combination with two ITCs, sulforaphane or iberin, on the expression of the two selenoenzymes, thioredoxin reductase 1 (TrxR1) and gastrointestinal glutathione peroxidase (GPx2), which are targets of ITCs, in Caco-2 cells.	Selenium	66-74	glutathione peroxidase 2	Homo sapiens	324-328
22820176-7	2012	Furthermore, a single and double knockdown of TrxR1 and/or GPx2 suggested that both selenoproteins were responsible for protecting against H(2)O(2)-induced cell death.	Hydrogen Peroxide	139-147	glutathione peroxidase 2	Homo sapiens	59-63
22758632-6	2012	The model further revealed a GPx2-independent decrease in tumor development by selenium (Se) and detrimental effects of the Nrf2-activator sulforaphane in moderate Se deficiency.	Selenium	89-91	glutathione peroxidase 2	Homo sapiens	29-33
21382479-12	2011	Deletion of glutathione peroxidase-2 using siRNA aggravated the BID-Cav-1 interaction and tBID formation.	tBID	90-94	glutathione peroxidase 2	Homo sapiens	12-36
21932842-6	2011	Plasmin digests of HC fibrinogen produced fragments that were similar to normal D and E; further, as with normal fibrinogen, the knob "A" peptide, GPRP, reversed the plasmin cleavage associated with addition of EDTA.	Edetic Acid	211-215	glutathione peroxidase 2	Homo sapiens	147-151
21677072-7	2011	Exposure of infant intestinal cells to tryptophan resulted in Nrf-2 activation and an increase in the gene transcript level of glutathione peroxidase 2.	Tryptophan	39-49	glutathione peroxidase 2	Homo sapiens	127-151
18479189-0	2008	GPx2 counteracts PGE2 production by dampening COX-2 and mPGES-1 expression in human colon cancer cells.	Dinoprostone	17-21	glutathione peroxidase 2	Homo sapiens	0-4
20868228-5	2010	We therefore investigated myrosinase-treated GRA, nGBS and synthetic SFN for their ability to induce NAD(P)H:quinone oxidoreductase 1 (NQO1) as typical phase 2 enzyme, and glutathione peroxidase 2 (GPx2) as novel Nrf2 target in HepG2 cells.	sulforaphane	69-72	glutathione peroxidase 2	Homo sapiens	172-196
20868228-5	2010	We therefore investigated myrosinase-treated GRA, nGBS and synthetic SFN for their ability to induce NAD(P)H:quinone oxidoreductase 1 (NQO1) as typical phase 2 enzyme, and glutathione peroxidase 2 (GPx2) as novel Nrf2 target in HepG2 cells.	sulforaphane	69-72	glutathione peroxidase 2	Homo sapiens	198-202
20868228-6	2010	Breakdown products of nGBS potently inhibit both GRA-mediated stimulation of NQO1 enzyme and Gpx2 promoter activity.	neoglucobrassicin	22-26	glutathione peroxidase 2	Homo sapiens	93-97
20572871-2	2010	Two structural homologues of the mammalian glutathione peroxidase, Gpx2 and Gpx3, have been proven to be atypical 2-Cys peroxiredoxins, which prefer to use thioredoxin as an electron donor.	2-cys peroxiredoxins	114-134	glutathione peroxidase 2	Homo sapiens	67-71
20406884-7	2010	We further identify superoxide dismutase 1 (SOD1) and glutathione peroxidase 2 (GPX2) as interaction partners of both AtDJ-1a and human DJ-1, and show that this interaction results in AtDJ-1a- and DJ-1-mediated cytosolic SOD1 activation in a copper-dependent fashion.	Copper	242-248	glutathione peroxidase 2	Homo sapiens	54-78
20406884-7	2010	We further identify superoxide dismutase 1 (SOD1) and glutathione peroxidase 2 (GPX2) as interaction partners of both AtDJ-1a and human DJ-1, and show that this interaction results in AtDJ-1a- and DJ-1-mediated cytosolic SOD1 activation in a copper-dependent fashion.	Copper	242-248	glutathione peroxidase 2	Homo sapiens	80-84
19650644-4	2009	Alignment of the normal and gammaN308K structures showed the global structure of the variant was not changed and the knob "A" peptide GPRP was bound as usual to hole "a".	gamman308	28-37	glutathione peroxidase 2	Homo sapiens	134-138
19650644-7	2009	We examined GPRP binding to gammaN308K in solution by plasmin protection assay.	gamman308	28-37	glutathione peroxidase 2	Homo sapiens	12-16
18479189-7	2008	A stable knockdown of GPx2 in HT-29 cells by siRNA resulted in a high basal and IL-1-induced expression of COX-2 and mPGES-1, enzymes required for the production of the pro-inflammatory PGE(2).	Prostaglandins E	118-121	glutathione peroxidase 2	Homo sapiens	22-26
18479189-8	2008	Accordingly, si-GPx2 cells released high concentrations of PGE(2).	Prostaglandins E	59-62	glutathione peroxidase 2	Homo sapiens	16-20
18479189-10	2008	It is concluded that GPx2 by compartmentalized removal of hydroperoxides silences COX-2 activity and suppresses PGE(2)-dependent COX-2 expression.	Hydrogen Peroxide	58-72	glutathione peroxidase 2	Homo sapiens	21-25
18479189-10	2008	It is concluded that GPx2 by compartmentalized removal of hydroperoxides silences COX-2 activity and suppresses PGE(2)-dependent COX-2 expression.	Dinoprostone	112-118	glutathione peroxidase 2	Homo sapiens	21-25
15878612-6	2006	During CRP- or convulxin-triggered platelet activation, inhibition of fibrin polymerisation with GPRP potentiated the antiaggregatory effects of tirofiban and eptifibatide to reach that of abciximab.	Tirofiban	145-154	glutathione peroxidase 2	Homo sapiens	97-101
18054426-5	2008	Expression level of selenoproteins such as GPx-1, GPx-3, and SePP, which are rapidly degraded during selenium deprivation, was significantly decreased in tumorous tissues, whereas that of GPx-2, which is resistant to selenium deprivation, was increased.	Selenium	217-225	glutathione peroxidase 2	Homo sapiens	188-193
15878612-6	2006	During CRP- or convulxin-triggered platelet activation, inhibition of fibrin polymerisation with GPRP potentiated the antiaggregatory effects of tirofiban and eptifibatide to reach that of abciximab.	Eptifibatide	159-171	glutathione peroxidase 2	Homo sapiens	97-101
11502879-7	2001	Interestingly, in addition to a decrease in ROS production, the activation of neutral sphingomyelinase, sphingomyelin hydrolysis, and ceramide generation in response to doxorubicin was impaired in T47D/GPx2 cells compared with control cells.	Sphingomyelins	86-99	glutathione peroxidase 2	Homo sapiens	202-206
15923610-1	2005	The gastrointestinal glutathione peroxidase (GI-GPx, GPx2) is a selenoprotein that was suggested to act as barrier against hydroperoxide absorption but has also been implicated in the control of inflammation and malignant growth.	Hydrogen Peroxide	123-136	glutathione peroxidase 2	Homo sapiens	4-43
15623509-7	2005	Moreover, activating the endogenous gene coding for GI-GPx by all-trans-retinoic acid (RA) was sufficient to cause down-regulation of the HCV replicon.	Tretinoin	62-85	glutathione peroxidase 2	Homo sapiens	52-58
12674495-3	2003	In the familiy of selenium-dependent glutathione peroxidases (GPx) the ranking is GI-GPx > or = PHGPx > cGPx = pGPx.	Selenium	18-26	glutathione peroxidase 2	Homo sapiens	82-88
12674495-3	2003	In the familiy of selenium-dependent glutathione peroxidases (GPx) the ranking is GI-GPx > or = PHGPx > cGPx = pGPx.	pgpx	117-121	glutathione peroxidase 2	Homo sapiens	82-88
12513841-6	2002	Gly-Pro-Arg-Pro acetate salt (GPRP) was applied to prevent platelets aggregation and fibrin formation, stabilize platelets and minimize the artificial platelets activation.	GPRP acetate	0-28	glutathione peroxidase 2	Homo sapiens	30-34
11811519-1	2001	The gastrointestinal glutathione peroxidase (GI-GPx) is believed to prevent absorption of hydroperoxides.	Hydrogen Peroxide	90-104	glutathione peroxidase 2	Homo sapiens	4-43
11811519-1	2001	The gastrointestinal glutathione peroxidase (GI-GPx) is believed to prevent absorption of hydroperoxides.	Hydrogen Peroxide	90-104	glutathione peroxidase 2	Homo sapiens	45-51
11811519-10	2001	These observations support the hypothesis that GI-GPx, apart from being a barrier against hydroperoxide absorption, might be involved in cell growth and differentiation.	Hydrogen Peroxide	90-103	glutathione peroxidase 2	Homo sapiens	47-53
16251189-6	2005	Here we show that GPX2 encodes an atypical 2-Cys peroxiredoxin which uses thioredoxin as an electron donor.	2-cys peroxiredoxin	43-62	glutathione peroxidase 2	Homo sapiens	18-22
16097939-6	2005	The oxidative processes induced by tBOOH in red blood cells can be described as follows: 1) rapid GSH oxidation (30-60 sec) by glutathione peroxidase; 2) formation of radicals in the reaction between tBOOH and cellular Hb, which are then immediately consumed in lipid peroxidation reactions; 3) generation of chemiluminescence by the radicals formed.	tert-Butylhydroperoxide	35-40	glutathione peroxidase 2	Homo sapiens	127-152
16097939-6	2005	The oxidative processes induced by tBOOH in red blood cells can be described as follows: 1) rapid GSH oxidation (30-60 sec) by glutathione peroxidase; 2) formation of radicals in the reaction between tBOOH and cellular Hb, which are then immediately consumed in lipid peroxidation reactions; 3) generation of chemiluminescence by the radicals formed.	Glutathione	98-101	glutathione peroxidase 2	Homo sapiens	127-152
16097939-6	2005	The oxidative processes induced by tBOOH in red blood cells can be described as follows: 1) rapid GSH oxidation (30-60 sec) by glutathione peroxidase; 2) formation of radicals in the reaction between tBOOH and cellular Hb, which are then immediately consumed in lipid peroxidation reactions; 3) generation of chemiluminescence by the radicals formed.	tert-Butylhydroperoxide	200-205	glutathione peroxidase 2	Homo sapiens	127-152
15923610-1	2005	The gastrointestinal glutathione peroxidase (GI-GPx, GPx2) is a selenoprotein that was suggested to act as barrier against hydroperoxide absorption but has also been implicated in the control of inflammation and malignant growth.	Hydrogen Peroxide	123-136	glutathione peroxidase 2	Homo sapiens	45-51
15923610-1	2005	The gastrointestinal glutathione peroxidase (GI-GPx, GPx2) is a selenoprotein that was suggested to act as barrier against hydroperoxide absorption but has also been implicated in the control of inflammation and malignant growth.	Hydrogen Peroxide	123-136	glutathione peroxidase 2	Homo sapiens	53-57
15923610-2	2005	In CaCo-2 cells, GI-GPx was induced by t-butyl hydroquinone (tBHQ) and sulforaphane (SFN), i.e., "antioxidants" known to activate the "antioxidant response element" (ARE) via electrophilic thiol modification of Keap1 in the Nrf2/Keap1 system.	2-tert-butylhydroquinone	39-59	glutathione peroxidase 2	Homo sapiens	17-23
15923610-2	2005	In CaCo-2 cells, GI-GPx was induced by t-butyl hydroquinone (tBHQ) and sulforaphane (SFN), i.e., "antioxidants" known to activate the "antioxidant response element" (ARE) via electrophilic thiol modification of Keap1 in the Nrf2/Keap1 system.	2-tert-butylhydroquinone	61-65	glutathione peroxidase 2	Homo sapiens	17-23
15923610-2	2005	In CaCo-2 cells, GI-GPx was induced by t-butyl hydroquinone (tBHQ) and sulforaphane (SFN), i.e., "antioxidants" known to activate the "antioxidant response element" (ARE) via electrophilic thiol modification of Keap1 in the Nrf2/Keap1 system.	sulforaphane	71-83	glutathione peroxidase 2	Homo sapiens	17-23
15923610-2	2005	In CaCo-2 cells, GI-GPx was induced by t-butyl hydroquinone (tBHQ) and sulforaphane (SFN), i.e., "antioxidants" known to activate the "antioxidant response element" (ARE) via electrophilic thiol modification of Keap1 in the Nrf2/Keap1 system.	sulforaphane	85-88	glutathione peroxidase 2	Homo sapiens	17-23
15923610-2	2005	In CaCo-2 cells, GI-GPx was induced by t-butyl hydroquinone (tBHQ) and sulforaphane (SFN), i.e., "antioxidants" known to activate the "antioxidant response element" (ARE) via electrophilic thiol modification of Keap1 in the Nrf2/Keap1 system.	Sulfhydryl Compounds	189-194	glutathione peroxidase 2	Homo sapiens	17-23
15923610-3	2005	The functional significance of a putative ARE in the GI-GPx promoter was validated by transcriptional activation of reporter gene constructs upon exposure to electrophiles (tBHQ, SFN, and curcumin) or overexpression of Nrf2 and by reversal of these effects by mutation of the ARE in the promoter and by overexpressed Keap1.	2-tert-butylhydroquinone	173-177	glutathione peroxidase 2	Homo sapiens	53-59
15923610-3	2005	The functional significance of a putative ARE in the GI-GPx promoter was validated by transcriptional activation of reporter gene constructs upon exposure to electrophiles (tBHQ, SFN, and curcumin) or overexpression of Nrf2 and by reversal of these effects by mutation of the ARE in the promoter and by overexpressed Keap1.	sulforaphane	179-182	glutathione peroxidase 2	Homo sapiens	53-59
15923610-3	2005	The functional significance of a putative ARE in the GI-GPx promoter was validated by transcriptional activation of reporter gene constructs upon exposure to electrophiles (tBHQ, SFN, and curcumin) or overexpression of Nrf2 and by reversal of these effects by mutation of the ARE in the promoter and by overexpressed Keap1.	Curcumin	188-196	glutathione peroxidase 2	Homo sapiens	53-59
15923610-5	2005	Thus, the presumed natural antioxidants sulforaphane and curcumin may exert their anti-inflammatory and anticarcinogenic effects not only by induction of phase 2 enzymes but also by the up-regulation of the selenoprotein GI-GPx.	sulforaphane	40-52	glutathione peroxidase 2	Homo sapiens	221-227
15923610-5	2005	Thus, the presumed natural antioxidants sulforaphane and curcumin may exert their anti-inflammatory and anticarcinogenic effects not only by induction of phase 2 enzymes but also by the up-regulation of the selenoprotein GI-GPx.	Curcumin	57-65	glutathione peroxidase 2	Homo sapiens	221-227
15203372-3	2004	Due to their antioxidative potential, the selenoproteins gastrointestinal glutathione peroxidase (GI-GPx) and selenoprotein P (SePP) are considered to provide protection against reactive oxygen species (ROS), thereby reducing DNA damage and preventing development of colon cancer.	Reactive Oxygen Species	178-201	glutathione peroxidase 2	Homo sapiens	57-96
15203372-3	2004	Due to their antioxidative potential, the selenoproteins gastrointestinal glutathione peroxidase (GI-GPx) and selenoprotein P (SePP) are considered to provide protection against reactive oxygen species (ROS), thereby reducing DNA damage and preventing development of colon cancer.	Reactive Oxygen Species	178-201	glutathione peroxidase 2	Homo sapiens	98-104
15203372-3	2004	Due to their antioxidative potential, the selenoproteins gastrointestinal glutathione peroxidase (GI-GPx) and selenoprotein P (SePP) are considered to provide protection against reactive oxygen species (ROS), thereby reducing DNA damage and preventing development of colon cancer.	Reactive Oxygen Species	203-206	glutathione peroxidase 2	Homo sapiens	57-96
15203372-3	2004	Due to their antioxidative potential, the selenoproteins gastrointestinal glutathione peroxidase (GI-GPx) and selenoprotein P (SePP) are considered to provide protection against reactive oxygen species (ROS), thereby reducing DNA damage and preventing development of colon cancer.	Reactive Oxygen Species	203-206	glutathione peroxidase 2	Homo sapiens	98-104
12033453-9	2002	We concluded that food-born hydroperoxy fatty acids are instantly reduced by the gastrointestinal glutathione peroxidase, which was previously shown to persist in selenium deficiency.	hydroperoxy fatty acids	28-51	glutathione peroxidase 2	Homo sapiens	81-120
12033453-9	2002	We concluded that food-born hydroperoxy fatty acids are instantly reduced by the gastrointestinal glutathione peroxidase, which was previously shown to persist in selenium deficiency.	Selenium	163-171	glutathione peroxidase 2	Homo sapiens	81-120
11502879-5	2001	We show that T47D/GPx2 cells were significantly more resistant than T47D/H3 cells to doxorubicin (1 microM).	Doxorubicin	85-96	glutathione peroxidase 2	Homo sapiens	18-22
11502879-7	2001	Interestingly, in addition to a decrease in ROS production, the activation of neutral sphingomyelinase, sphingomyelin hydrolysis, and ceramide generation in response to doxorubicin was impaired in T47D/GPx2 cells compared with control cells.	Ceramides	134-142	glutathione peroxidase 2	Homo sapiens	202-206
11502879-7	2001	Interestingly, in addition to a decrease in ROS production, the activation of neutral sphingomyelinase, sphingomyelin hydrolysis, and ceramide generation in response to doxorubicin was impaired in T47D/GPx2 cells compared with control cells.	Doxorubicin	169-180	glutathione peroxidase 2	Homo sapiens	202-206
10930377-0	2000	Gastrointestinal glutathione peroxidase prevents transport of lipid hydroperoxides in CaCo-2 cells.	Lipid Peroxides	62-82	glutathione peroxidase 2	Homo sapiens	0-39
11568446-0	2001	Functions of GI-GPx: lessons from selenium-dependent expression and intracellular localization.	Selenium	34-42	glutathione peroxidase 2	Homo sapiens	13-19
11568446-4	2001	The GI-GPx mRNA rather increases than decreases in selenium deficiency.	Selenium	51-59	glutathione peroxidase 2	Homo sapiens	4-10
11568446-5	2001	GI-GPx protein responds poorly to selenium deprivation and increases fast upon resupplementation.	Selenium	34-42	glutathione peroxidase 2	Homo sapiens	0-6
10930377-1	2000	BACKGROUND & AIMS: Gastrointestinal glutathione peroxidase (GI-GPx), 1 of the 4 types of selenium-dependent glutathione peroxidases, is expressed exclusively in the gastrointestinal system and has therefore been suggested to function as a barrier against the absorption of dietary hydroperoxides.	Adenosine Monophosphate	12-15	glutathione peroxidase 2	Homo sapiens	23-62
10930377-1	2000	BACKGROUND & AIMS: Gastrointestinal glutathione peroxidase (GI-GPx), 1 of the 4 types of selenium-dependent glutathione peroxidases, is expressed exclusively in the gastrointestinal system and has therefore been suggested to function as a barrier against the absorption of dietary hydroperoxides.	Adenosine Monophosphate	12-15	glutathione peroxidase 2	Homo sapiens	64-70
10930377-1	2000	BACKGROUND & AIMS: Gastrointestinal glutathione peroxidase (GI-GPx), 1 of the 4 types of selenium-dependent glutathione peroxidases, is expressed exclusively in the gastrointestinal system and has therefore been suggested to function as a barrier against the absorption of dietary hydroperoxides.	Selenium	93-101	glutathione peroxidase 2	Homo sapiens	23-62
10930377-1	2000	BACKGROUND & AIMS: Gastrointestinal glutathione peroxidase (GI-GPx), 1 of the 4 types of selenium-dependent glutathione peroxidases, is expressed exclusively in the gastrointestinal system and has therefore been suggested to function as a barrier against the absorption of dietary hydroperoxides.	Selenium	93-101	glutathione peroxidase 2	Homo sapiens	64-70
10930377-1	2000	BACKGROUND & AIMS: Gastrointestinal glutathione peroxidase (GI-GPx), 1 of the 4 types of selenium-dependent glutathione peroxidases, is expressed exclusively in the gastrointestinal system and has therefore been suggested to function as a barrier against the absorption of dietary hydroperoxides.	Hydrogen Peroxide	285-299	glutathione peroxidase 2	Homo sapiens	23-62
10930377-1	2000	BACKGROUND & AIMS: Gastrointestinal glutathione peroxidase (GI-GPx), 1 of the 4 types of selenium-dependent glutathione peroxidases, is expressed exclusively in the gastrointestinal system and has therefore been suggested to function as a barrier against the absorption of dietary hydroperoxides.	Hydrogen Peroxide	285-299	glutathione peroxidase 2	Homo sapiens	64-70
10930377-2	2000	METHODS: The selenium-dependent expression of GI-GPx and cytosolic GPx (cGPx) was analyzed by Western blotting.	Selenium	13-21	glutathione peroxidase 2	Homo sapiens	46-52
10930377-3	2000	Transport of 13-hydroperoxy octadecadienoic acid (13-HPODE) was investigated in a CaCo-2 cell monolayer modulated in GI-GPx and cGPx by selenium restriction or repletion.	13-hydroperoxy octadecadienoic acid	13-48	glutathione peroxidase 2	Homo sapiens	117-123
10930377-3	2000	Transport of 13-hydroperoxy octadecadienoic acid (13-HPODE) was investigated in a CaCo-2 cell monolayer modulated in GI-GPx and cGPx by selenium restriction or repletion.	13-Hpode	50-58	glutathione peroxidase 2	Homo sapiens	117-123
10930377-5	2000	RESULTS: Low but significant GI-GPx levels were detected in selenium-deficient CaCo-2 cells and in the gastrointestinal tract of selenium-deficient rats, whereas cGPx was completely absent.	Selenium	60-68	glutathione peroxidase 2	Homo sapiens	29-35
10930377-5	2000	RESULTS: Low but significant GI-GPx levels were detected in selenium-deficient CaCo-2 cells and in the gastrointestinal tract of selenium-deficient rats, whereas cGPx was completely absent.	Selenium	129-137	glutathione peroxidase 2	Homo sapiens	29-35
10930377-6	2000	Selenium supplementation of CaCo-2 cells resulted in a 5-fold increase of GI-GPx protein, whereas total GPx activity increased by a factor of 13, with most of the GPx activity under selenium-adequate conditions being cGPx.	Selenium	0-8	glutathione peroxidase 2	Homo sapiens	74-80
10930377-10	2000	CONCLUSIONS: Low GI-GPx levels, as present in selenium deficiency, suffice to prevent transport of 13-HPODE.	Selenium	46-54	glutathione peroxidase 2	Homo sapiens	17-23
10930377-11	2000	GI-GPx may thus function as a barrier against hydroperoxide absorption.	Hydrogen Peroxide	46-59	glutathione peroxidase 2	Homo sapiens	0-6
10806356-11	2000	The ability of GPX2 to respond transcriptionally to redox stress is likely to be more physiologically relevant than post-transcriptional regulation which is dependent upon selenium availability.	Selenium	172-180	glutathione peroxidase 2	Homo sapiens	15-19
10498757-0	1999	Retinoic acid induces Gpx2 gene expression in MCF-7 human breast cancer cells.	Tretinoin	0-13	glutathione peroxidase 2	Homo sapiens	22-26
10498757-4	1999	Because we identified three putative retinoic acid response elements (RARE) in the Gpx2 gene, we examined the regulation of the Gpx2 gene expression by all-trans retinoic acid (RA) in RA-sensitive MCF-7 cells and RA-resistant HT29 cells.	Tretinoin	37-50	glutathione peroxidase 2	Homo sapiens	83-87
10498757-4	1999	Because we identified three putative retinoic acid response elements (RARE) in the Gpx2 gene, we examined the regulation of the Gpx2 gene expression by all-trans retinoic acid (RA) in RA-sensitive MCF-7 cells and RA-resistant HT29 cells.	Tretinoin	162-175	glutathione peroxidase 2	Homo sapiens	128-132
10498757-4	1999	Because we identified three putative retinoic acid response elements (RARE) in the Gpx2 gene, we examined the regulation of the Gpx2 gene expression by all-trans retinoic acid (RA) in RA-sensitive MCF-7 cells and RA-resistant HT29 cells.	Tretinoin	70-72	glutathione peroxidase 2	Homo sapiens	83-87
10498757-4	1999	Because we identified three putative retinoic acid response elements (RARE) in the Gpx2 gene, we examined the regulation of the Gpx2 gene expression by all-trans retinoic acid (RA) in RA-sensitive MCF-7 cells and RA-resistant HT29 cells.	Tretinoin	177-179	glutathione peroxidase 2	Homo sapiens	128-132
10498757-6	1999	RA treatment increased Gpx2 mRNA level 3- to 11-fold and resulted in a fourfold increase of GPX activity (80 mU/mg protein) in MCF-7 cells.	Tretinoin	0-2	glutathione peroxidase 2	Homo sapiens	23-27
10498757-8	1999	These results show that the Gpx2 gene is expressed in both breast and intestinal epithelium cells, and suggest that its expression can be highly regulated by retinoic acid, a known differentiation agent.	Tretinoin	158-171	glutathione peroxidase 2	Homo sapiens	28-32