PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
33631924-6	2021	Proteins of interest, including PRDX2, PRDX6, and Gelsolin, were differentially expressed in chemo-sensitive tumors versus chemo-resistant tissues and these observations were validated by immunohistochemistry in 92 formalin-fixed and paraffin-embedded (FFPE) specimens.	Formaldehyde	215-223	peroxiredoxin 2	Homo sapiens	32-37
33901418-4	2021	Among these, the peroxiredoxins (PRDXs) are of interest due to a high reactivity with reactive oxygen species (ROS) through the functioning of the thioredoxin/thioredoxin reductase system.	Reactive Oxygen Species	86-109	peroxiredoxin 2	Homo sapiens	17-31
33901418-4	2021	Among these, the peroxiredoxins (PRDXs) are of interest due to a high reactivity with reactive oxygen species (ROS) through the functioning of the thioredoxin/thioredoxin reductase system.	Reactive Oxygen Species	111-114	peroxiredoxin 2	Homo sapiens	17-31
33869202-9	2021	Meanwhile, the global gene expressing in cumulus cells was also modulated by melatonin, especially the genes related to antioxidants (SOD1, GPX1, GPX3, GPX4, PRDX2, and PRDX5), lipid metabolism (FABP3, FABP5, ACACB, TECR, etc.	Melatonin	77-86	peroxiredoxin 2	Homo sapiens	158-163
33905956-0	2021	Peroxiredoxin 2 oxidation reveals hydrogen peroxide generation within erythrocytes during high-dose vitamin C administration.	Hydrogen Peroxide	34-51	peroxiredoxin 2	Homo sapiens	0-15
33905956-0	2021	Peroxiredoxin 2 oxidation reveals hydrogen peroxide generation within erythrocytes during high-dose vitamin C administration.	Ascorbic Acid	100-109	peroxiredoxin 2	Homo sapiens	0-15
33905956-5	2021	Within 10 min of ascorbate addition, we detected increased oxidation of erythrocyte peroxiredoxin 2 (Prx2), a major thiol antioxidant protein and a sensitive marker of H2O2 production.	Ascorbic Acid	17-26	peroxiredoxin 2	Homo sapiens	84-99
33905956-5	2021	Within 10 min of ascorbate addition, we detected increased oxidation of erythrocyte peroxiredoxin 2 (Prx2), a major thiol antioxidant protein and a sensitive marker of H2O2 production.	Ascorbic Acid	17-26	peroxiredoxin 2	Homo sapiens	101-105
33905956-5	2021	Within 10 min of ascorbate addition, we detected increased oxidation of erythrocyte peroxiredoxin 2 (Prx2), a major thiol antioxidant protein and a sensitive marker of H2O2 production.	Sulfhydryl Compounds	116-121	peroxiredoxin 2	Homo sapiens	84-99
33905956-5	2021	Within 10 min of ascorbate addition, we detected increased oxidation of erythrocyte peroxiredoxin 2 (Prx2), a major thiol antioxidant protein and a sensitive marker of H2O2 production.	Sulfhydryl Compounds	116-121	peroxiredoxin 2	Homo sapiens	101-105
33905956-5	2021	Within 10 min of ascorbate addition, we detected increased oxidation of erythrocyte peroxiredoxin 2 (Prx2), a major thiol antioxidant protein and a sensitive marker of H2O2 production.	Hydrogen Peroxide	168-172	peroxiredoxin 2	Homo sapiens	84-99
33905956-5	2021	Within 10 min of ascorbate addition, we detected increased oxidation of erythrocyte peroxiredoxin 2 (Prx2), a major thiol antioxidant protein and a sensitive marker of H2O2 production.	Hydrogen Peroxide	168-172	peroxiredoxin 2	Homo sapiens	101-105
33905956-7	2021	The presence of extracellular catalase, removal of plasma or the addition of a metal chelator did not prevent ascorbate-induced Prx2 oxidation, suggesting that the H2O2 responsible for Prx2 oxidation was generated within the erythrocyte.	Hydrogen Peroxide	164-168	peroxiredoxin 2	Homo sapiens	185-189
34030134-10	2021	Therefore, our results indicate that Prx II accelerated wound healing by protecting DMSCs from reactive oxygen species-induced apoptosis; however, Prx II did not regulate cell/growth factor secretion.	Reactive Oxygen Species	95-118	peroxiredoxin 2	Homo sapiens	37-43
33947873-9	2021	We propose that plasma levels of PRDX2, CA-1, FARSB, MMP9, and PCSK9 may be associated with BD-II as potential biomarkers.	bd-ii	92-97	peroxiredoxin 2	Homo sapiens	33-38
33791345-1	2021	Peroxiredoxin 2 (PRDX2), an inhibitor of reactive oxygen species (ROS), is potentially involved in the progression of atherosclerosis (AS).	Reactive Oxygen Species	41-64	peroxiredoxin 2	Homo sapiens	0-15
33791345-1	2021	Peroxiredoxin 2 (PRDX2), an inhibitor of reactive oxygen species (ROS), is potentially involved in the progression of atherosclerosis (AS).	Reactive Oxygen Species	41-64	peroxiredoxin 2	Homo sapiens	17-22
33791345-1	2021	Peroxiredoxin 2 (PRDX2), an inhibitor of reactive oxygen species (ROS), is potentially involved in the progression of atherosclerosis (AS).	Reactive Oxygen Species	66-69	peroxiredoxin 2	Homo sapiens	0-15
33791345-1	2021	Peroxiredoxin 2 (PRDX2), an inhibitor of reactive oxygen species (ROS), is potentially involved in the progression of atherosclerosis (AS).	Reactive Oxygen Species	66-69	peroxiredoxin 2	Homo sapiens	17-22
33791345-6	2021	The catalase, hydrogen peroxide (H2O2) scavenger, was used to further confirm that PRDX2-induced inhibitory effects might be mediated through reducing ROS levels.	Hydrogen Peroxide	14-31	peroxiredoxin 2	Homo sapiens	83-88
33791345-6	2021	The catalase, hydrogen peroxide (H2O2) scavenger, was used to further confirm that PRDX2-induced inhibitory effects might be mediated through reducing ROS levels.	Hydrogen Peroxide	33-37	peroxiredoxin 2	Homo sapiens	83-88
33791345-6	2021	The catalase, hydrogen peroxide (H2O2) scavenger, was used to further confirm that PRDX2-induced inhibitory effects might be mediated through reducing ROS levels.	Reactive Oxygen Species	151-154	peroxiredoxin 2	Homo sapiens	83-88
33791345-13	2021	Our results suggest a protective role of PRDX2, as a scavenger of ROS, in AS progression through inhibiting the VSMC phenotype alteration and function via MAPK signaling pathway.	Reactive Oxygen Species	66-69	peroxiredoxin 2	Homo sapiens	41-46
33631924-6	2021	Proteins of interest, including PRDX2, PRDX6, and Gelsolin, were differentially expressed in chemo-sensitive tumors versus chemo-resistant tissues and these observations were validated by immunohistochemistry in 92 formalin-fixed and paraffin-embedded (FFPE) specimens.	Paraffin	234-242	peroxiredoxin 2	Homo sapiens	32-37
33535382-0	2021	Tyrosine Phosphorylation Modulates Peroxiredoxin-2 Activity in Normal and Diseased Red Cells.	Tyrosine	0-8	peroxiredoxin 2	Homo sapiens	35-50
33672092-6	2021	We summarize the association findings between drug hypersensitivity reactions and variants in the genes that encode the enzymes related to the redox system such as enzymes related to glutathione: Glutathione S-transferase (GSTM1, GSTP, GSTT1) and glutathione peroxidase (GPX1), thioredoxin reductase (TXNRD1 and TXNRD2), superoxide dismutase (SOD1, SOD2, and SOD3), catalase (CAT), aldo-keto reductase (AKR), and the peroxiredoxin system (PRDX1, PRDX2, PRDX3, PRDX4, PRDX5, PRDX6).	Glutathione	183-194	peroxiredoxin 2	Homo sapiens	446-451
33535382-3	2021	Prx2 is a typical, homodimeric, 2-Cys Prx that uses two cysteine residues to accomplish the task of detoxifying a vast range of organic peroxides, H2O2, and peroxynitrite.	2-cys	32-37	peroxiredoxin 2	Homo sapiens	0-4
33535382-3	2021	Prx2 is a typical, homodimeric, 2-Cys Prx that uses two cysteine residues to accomplish the task of detoxifying a vast range of organic peroxides, H2O2, and peroxynitrite.	Cysteine	56-64	peroxiredoxin 2	Homo sapiens	0-4
33535382-3	2021	Prx2 is a typical, homodimeric, 2-Cys Prx that uses two cysteine residues to accomplish the task of detoxifying a vast range of organic peroxides, H2O2, and peroxynitrite.	organic peroxides	128-145	peroxiredoxin 2	Homo sapiens	0-4
33535382-3	2021	Prx2 is a typical, homodimeric, 2-Cys Prx that uses two cysteine residues to accomplish the task of detoxifying a vast range of organic peroxides, H2O2, and peroxynitrite.	Hydrogen Peroxide	147-151	peroxiredoxin 2	Homo sapiens	0-4
33535382-3	2021	Prx2 is a typical, homodimeric, 2-Cys Prx that uses two cysteine residues to accomplish the task of detoxifying a vast range of organic peroxides, H2O2, and peroxynitrite.	Peroxynitrous Acid	157-170	peroxiredoxin 2	Homo sapiens	0-4
33535382-5	2021	Here, we first show that Prx2 is Tyrosine (Tyr) phosphorylated by Syk in red cells exposed to oxidation induced by diamide.	Tyrosine	33-41	peroxiredoxin 2	Homo sapiens	25-29
33535382-5	2021	Here, we first show that Prx2 is Tyrosine (Tyr) phosphorylated by Syk in red cells exposed to oxidation induced by diamide.	Tyrosine	33-36	peroxiredoxin 2	Homo sapiens	25-29
33535382-5	2021	Here, we first show that Prx2 is Tyrosine (Tyr) phosphorylated by Syk in red cells exposed to oxidation induced by diamide.	Diamide	115-122	peroxiredoxin 2	Homo sapiens	25-29
33535382-6	2021	We identified Tyr-193 in both recombinant Prx2 and native Prx2 from red cells as a specific target of Syk.	Tyrosine	14-17	peroxiredoxin 2	Homo sapiens	42-46
33535382-6	2021	We identified Tyr-193 in both recombinant Prx2 and native Prx2 from red cells as a specific target of Syk.	Tyrosine	14-17	peroxiredoxin 2	Homo sapiens	58-62
33535382-7	2021	Bioinformatic analysis suggests that phosphorylation of Tyr-193 allows Prx2 conformational change that is more favorable for its peroxidase activity.	Tyrosine	56-59	peroxiredoxin 2	Homo sapiens	71-75
33535382-8	2021	Indeed, Syk-induced Tyr phosphorylation of Prx2 enhances in vitro Prx2 activity, but also contributes to Prx2 translocation to the membrane of red cells exposed to diamide.	Tyrosine	20-23	peroxiredoxin 2	Homo sapiens	43-47
33535382-8	2021	Indeed, Syk-induced Tyr phosphorylation of Prx2 enhances in vitro Prx2 activity, but also contributes to Prx2 translocation to the membrane of red cells exposed to diamide.	Tyrosine	20-23	peroxiredoxin 2	Homo sapiens	66-70
33535382-8	2021	Indeed, Syk-induced Tyr phosphorylation of Prx2 enhances in vitro Prx2 activity, but also contributes to Prx2 translocation to the membrane of red cells exposed to diamide.	Tyrosine	20-23	peroxiredoxin 2	Homo sapiens	66-70
33535382-8	2021	Indeed, Syk-induced Tyr phosphorylation of Prx2 enhances in vitro Prx2 activity, but also contributes to Prx2 translocation to the membrane of red cells exposed to diamide.	Diamide	164-171	peroxiredoxin 2	Homo sapiens	43-47
33535382-9	2021	The biologic importance of Tyr-193 phospho-Prx2 is further supported by data on red cells from a mouse model of humanized sickle cell disease (SCD).	Tyrosine	27-30	peroxiredoxin 2	Homo sapiens	43-47
33535382-11	2021	SCD red cells show Tyr-phosphorylated Prx2 bound to the membrane and increased Prx2 activity when compared to healthy erythrocytes.	Tyrosine	19-22	peroxiredoxin 2	Homo sapiens	38-42
33256145-3	2020	Validation by nonreducing WB was performed for peroxiredoxin-2 (PRDX2) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by using antibodies against the sulfinylated/sulfonylated cysteine of these proteins to better evaluate their redox-oligomeric states under OSA and/or in response to PAP therapy.	Cysteine	182-190	peroxiredoxin 2	Homo sapiens	47-62
33341544-7	2021	Following inhibition of mitochondrial complex 1 with rotenone we observe elevated spikes of H2O2 in the cell periphery and complementary oxidation of mitochondrial peroxiredoxin 3 (PRX3) and cytosolic peroxiredoxin 2 (PRX2).	Rotenone	53-61	peroxiredoxin 2	Homo sapiens	201-216
33341544-7	2021	Following inhibition of mitochondrial complex 1 with rotenone we observe elevated spikes of H2O2 in the cell periphery and complementary oxidation of mitochondrial peroxiredoxin 3 (PRX3) and cytosolic peroxiredoxin 2 (PRX2).	Rotenone	53-61	peroxiredoxin 2	Homo sapiens	218-222
33332365-0	2020	Peroxiredoxin 2 is highly expressed in human oral squamous cell carcinoma cells and is upregulated by human papillomavirus oncoproteins and arecoline, promoting proliferation.	Arecoline	140-149	peroxiredoxin 2	Homo sapiens	0-15
33332365-3	2020	This study aimed to investigate the effect of arecoline, an alkaloid of the betel nut, and human papillomavirus type 16 (HPV16) E6/E7 oncoproteins on induction of PRDX2 expression, and also the effects of PRDX2 overexpression in oral cell lines.	Arecoline	46-55	peroxiredoxin 2	Homo sapiens	163-168
33332365-3	2020	This study aimed to investigate the effect of arecoline, an alkaloid of the betel nut, and human papillomavirus type 16 (HPV16) E6/E7 oncoproteins on induction of PRDX2 expression, and also the effects of PRDX2 overexpression in oral cell lines.	Arecoline	46-55	peroxiredoxin 2	Homo sapiens	205-210
33332365-8	2020	PRDX2 expression levels tended to be higher in OSCC samples that were positive for HPV infection and had history of betel quid chewing.	betel	116-121	peroxiredoxin 2	Homo sapiens	0-5
33332365-9	2020	Arecoline treatment in vitro at low concentrations and overexpression of HPV16 E6 or E6/E7 in oral cells induced PRDX2 overexpression.	Arecoline	0-9	peroxiredoxin 2	Homo sapiens	113-118
33332365-11	2020	Upregulation of PRDX2 in oral cells was induced by arecoline and HPV16 oncoproteins and promoted growth of OSCC cells.	Arecoline	51-60	peroxiredoxin 2	Homo sapiens	16-21
33256145-4	2020	The results indicated that the redox-oligomeric state of GAPDH and PRDX2 involving overoxidation by sulfinic/sulfonic acids were differentially modulated in OSA RBC, which might be compromising RBC homeostasis.	sulfinic	100-108	peroxiredoxin 2	Homo sapiens	67-72
33256145-4	2020	The results indicated that the redox-oligomeric state of GAPDH and PRDX2 involving overoxidation by sulfinic/sulfonic acids were differentially modulated in OSA RBC, which might be compromising RBC homeostasis.	Sulfonic Acids	109-123	peroxiredoxin 2	Homo sapiens	67-72
32915529-4	2020	Herein, we describe for the first time that selenium compounds having intramolecular diselenide or selenenyl sulfide moieties can prevent the oxidative stress-induced eryptosis by exhibiting an unusual Prx2-like redox activity under conditions when the cellular Prx2 and CAT enzymes are inhibited.	Selenium	44-52	peroxiredoxin 2	Homo sapiens	202-206
33182509-0	2020	Upregulation of Peroxiredoxin-2 in Well-Differentiated Pancreatic Neuroendocrine Tumors and Its Utility as a Biomarker for Predicting the Response to Everolimus.	Everolimus	150-160	peroxiredoxin 2	Homo sapiens	16-31
33182509-11	2020	The results suggest that Prdx2 expression level and its activity may be a potential predictive biomarker for therapeutic response or resistance to everolimus in pNEN.	Everolimus	147-157	peroxiredoxin 2	Homo sapiens	25-30
32915529-4	2020	Herein, we describe for the first time that selenium compounds having intramolecular diselenide or selenenyl sulfide moieties can prevent the oxidative stress-induced eryptosis by exhibiting an unusual Prx2-like redox activity under conditions when the cellular Prx2 and CAT enzymes are inhibited.	Selenium	44-52	peroxiredoxin 2	Homo sapiens	262-266
32915529-4	2020	Herein, we describe for the first time that selenium compounds having intramolecular diselenide or selenenyl sulfide moieties can prevent the oxidative stress-induced eryptosis by exhibiting an unusual Prx2-like redox activity under conditions when the cellular Prx2 and CAT enzymes are inhibited.	diselenium	85-95	peroxiredoxin 2	Homo sapiens	202-206
32915529-4	2020	Herein, we describe for the first time that selenium compounds having intramolecular diselenide or selenenyl sulfide moieties can prevent the oxidative stress-induced eryptosis by exhibiting an unusual Prx2-like redox activity under conditions when the cellular Prx2 and CAT enzymes are inhibited.	diselenium	85-95	peroxiredoxin 2	Homo sapiens	262-266
32915529-4	2020	Herein, we describe for the first time that selenium compounds having intramolecular diselenide or selenenyl sulfide moieties can prevent the oxidative stress-induced eryptosis by exhibiting an unusual Prx2-like redox activity under conditions when the cellular Prx2 and CAT enzymes are inhibited.	selenium disulfide	99-116	peroxiredoxin 2	Homo sapiens	202-206
32915529-4	2020	Herein, we describe for the first time that selenium compounds having intramolecular diselenide or selenenyl sulfide moieties can prevent the oxidative stress-induced eryptosis by exhibiting an unusual Prx2-like redox activity under conditions when the cellular Prx2 and CAT enzymes are inhibited.	selenium disulfide	99-116	peroxiredoxin 2	Homo sapiens	262-266
33011678-2	2020	Humans have six peroxiredoxins, hPrxI-VI, out of which hPrxI and hPrxII belongs to the typical 2-Cys class sharing 90% conservation in their amino acid sequence including catalytic residues required to carry out their peroxidase and chaperone activities.	2-cys	95-100	peroxiredoxin 2	Homo sapiens	65-71
32639620-0	2020	Peroxiredoxin 2 deficiency reduces white adipogenesis due to the excessive ROS generation.	Reactive Oxygen Species	75-78	peroxiredoxin 2	Homo sapiens	0-15
32639620-4	2020	Prx2 is present in the cytoplasm and cell membranes and demonstrates ROS scavenging activity.	Reactive Oxygen Species	69-72	peroxiredoxin 2	Homo sapiens	0-4
32702382-0	2020	Intra-dimer cooperativity between the active site cysteines during the oxidation of peroxiredoxin 2.	Cysteine	50-59	peroxiredoxin 2	Homo sapiens	84-99
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Hydrogen Peroxide	86-103	peroxiredoxin 2	Homo sapiens	0-15
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Hydrogen Peroxide	86-103	peroxiredoxin 2	Homo sapiens	17-22
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Cysteine	130-138	peroxiredoxin 2	Homo sapiens	0-15
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Cysteine	130-138	peroxiredoxin 2	Homo sapiens	17-22
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Sulfenic Acids	144-157	peroxiredoxin 2	Homo sapiens	0-15
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Sulfenic Acids	144-157	peroxiredoxin 2	Homo sapiens	17-22
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Cysteine	198-206	peroxiredoxin 2	Homo sapiens	0-15
32702382-1	2020	Peroxiredoxin 2 (Prdx2) and other typical 2-Cys Prdxs function as homodimers in which hydrogen peroxide oxidizes each active site cysteine to a sulfenic acid which then condenses with the resolving cysteine on the alternate chain.	Cysteine	198-206	peroxiredoxin 2	Homo sapiens	17-22
32908147-2	2020	Peroxiredoxins (Prxs) have the ability to transfer H2O2-derived oxidizing equivalents to redox-regulated target proteins, thus facilitating the transmission of H2O2 signals.	Hydrogen Peroxide	51-55	peroxiredoxin 2	Homo sapiens	0-14
32925922-9	2020	Comparison of these results with redox Western blots of Prx3 and Prx2 oxidation states demonstrated reasonable trend agreement at short times (<= 15 min) for a range of experimentally perturbed H2O2 generation rates.	Hydrogen Peroxide	194-198	peroxiredoxin 2	Homo sapiens	65-69
32925922-10	2020	At longer times, substantial efflux of H2O2 from the mitochondria to the cytosol was evidenced by peroxiredoxin-2 (Prx2) oxidation, and Prx3 collapse was not observed.	Hydrogen Peroxide	39-43	peroxiredoxin 2	Homo sapiens	98-113
32925922-10	2020	At longer times, substantial efflux of H2O2 from the mitochondria to the cytosol was evidenced by peroxiredoxin-2 (Prx2) oxidation, and Prx3 collapse was not observed.	Hydrogen Peroxide	39-43	peroxiredoxin 2	Homo sapiens	115-119
32908147-2	2020	Peroxiredoxins (Prxs) have the ability to transfer H2O2-derived oxidizing equivalents to redox-regulated target proteins, thus facilitating the transmission of H2O2 signals.	Hydrogen Peroxide	160-164	peroxiredoxin 2	Homo sapiens	0-14
32929349-0	2020	Celastrol induces ROS-mediated apoptosis via directly targeting peroxiredoxin-2 in gastric cancer cells.	celastrol	0-9	peroxiredoxin 2	Homo sapiens	64-79
32929349-0	2020	Celastrol induces ROS-mediated apoptosis via directly targeting peroxiredoxin-2 in gastric cancer cells.	Reactive Oxygen Species	18-21	peroxiredoxin 2	Homo sapiens	64-79
32929349-8	2020	Results: Our data show that Celastrol directly binds to an antioxidant enzyme, peroxiredoxin-2 (Prdx2), which then inhibits its enzyme activity at both molecular and cellular level.	celastrol	28-37	peroxiredoxin 2	Homo sapiens	79-94
32929349-13	2020	Conclusion: Our studies have uncovered a potential Celastrol-interacting protein Prdx2 and a ROS-dependent mechanism of its action.	celastrol	51-60	peroxiredoxin 2	Homo sapiens	81-86
32692719-7	2020	The P38 activator dehydrocorydaline chloride partially rescued the effects of sh-PRDX2 on the expression of proteins related to cell-cycle progression and autophagy.	Dehydrocorydaline chloride	18-44	peroxiredoxin 2	Homo sapiens	81-86
31838004-8	2020	Peroxiredoxin 2 and catalase, in particular, played an important role in endogenous and exogenous H2O2 degradation, respectively.	Water	98-102	peroxiredoxin 2	Homo sapiens	0-15
32002772-3	2020	Prdx2 reduces the production of reactive oxygen species and participates in regulating various signaling pathways in neurons by catalyzing hydrogen peroxide (H2O2), thereby protecting neurons against oxidative stress and an inflammatory injury.	Oxygen	41-47	peroxiredoxin 2	Homo sapiens	0-5
31838004-9	2020	Accordingly, inhibitors of peroxiredoxin 2 and catalase significantly decreased erythrocyte HbNO concentration.	hemoglobin A, glycosylated-nitric oxide complex	92-96	peroxiredoxin 2	Homo sapiens	27-42
32119756-13	2020	In addition, ESIMS of intact proteins shows that GSH can S-transthiolate S-homocysteinylated Grx-1, HHb and Prdx2.	Glutathione	49-52	peroxiredoxin 2	Homo sapiens	108-113
32389179-4	2020	Treatment of COCs in culture with conoidin A (50microM), a 2-cys Prdx inhibitor, abolished epiregulin (EPI)-induced cumulus expansion.	cocs	13-17	peroxiredoxin 2	Homo sapiens	65-69
32389179-4	2020	Treatment of COCs in culture with conoidin A (50microM), a 2-cys Prdx inhibitor, abolished epiregulin (EPI)-induced cumulus expansion.	conoidin A	34-44	peroxiredoxin 2	Homo sapiens	65-69
32389179-4	2020	Treatment of COCs in culture with conoidin A (50microM), a 2-cys Prdx inhibitor, abolished epiregulin (EPI)-induced cumulus expansion.	2-cys	59-64	peroxiredoxin 2	Homo sapiens	65-69
32002772-3	2020	Prdx2 reduces the production of reactive oxygen species and participates in regulating various signaling pathways in neurons by catalyzing hydrogen peroxide (H2O2), thereby protecting neurons against oxidative stress and an inflammatory injury.	Hydrogen Peroxide	139-156	peroxiredoxin 2	Homo sapiens	0-5
32002772-3	2020	Prdx2 reduces the production of reactive oxygen species and participates in regulating various signaling pathways in neurons by catalyzing hydrogen peroxide (H2O2), thereby protecting neurons against oxidative stress and an inflammatory injury.	Hydrogen Peroxide	158-162	peroxiredoxin 2	Homo sapiens	0-5
32218363-3	2020	2-Cys peroxiredoxins, in particular Prx1 and Prx2, were detected as being S-nitrosated in multiple mammalian cells under a variety of conditions.	2-cys	0-5	peroxiredoxin 2	Homo sapiens	45-49
31629169-5	2020	In line with the emerging role of peroxiredoxins as H2O2 sensors and signal transmitters we observe an H2O2-dependent interaction between Mekk1 and the cytosolic peroxiredoxin of Drosophila, Jafrac1.	Hydrogen Peroxide	103-107	peroxiredoxin 2	Homo sapiens	34-48
32062888-9	2020	Conclusion: Prx2 overexpression inhibits fibroblast proliferation and collagen synthesis induced by TGF-beta1 through inhibiting reactive oxygen species and activating the JNK and P38 pathways.	Reactive Oxygen Species	129-152	peroxiredoxin 2	Homo sapiens	12-16
31629169-0	2020	A role for peroxiredoxins in H2O2- and MEKK-dependent activation of the p38 signaling pathway.	Hydrogen Peroxide	29-33	peroxiredoxin 2	Homo sapiens	11-25
31629169-5	2020	In line with the emerging role of peroxiredoxins as H2O2 sensors and signal transmitters we observe an H2O2-dependent interaction between Mekk1 and the cytosolic peroxiredoxin of Drosophila, Jafrac1.	Hydrogen Peroxide	52-56	peroxiredoxin 2	Homo sapiens	34-48
31629169-5	2020	In line with the emerging role of peroxiredoxins as H2O2 sensors and signal transmitters we observe an H2O2-dependent interaction between Mekk1 and the cytosolic peroxiredoxin of Drosophila, Jafrac1.	Hydrogen Peroxide	52-56	peroxiredoxin 2	Homo sapiens	34-47
31629169-5	2020	In line with the emerging role of peroxiredoxins as H2O2 sensors and signal transmitters we observe an H2O2-dependent interaction between Mekk1 and the cytosolic peroxiredoxin of Drosophila, Jafrac1.	Hydrogen Peroxide	103-107	peroxiredoxin 2	Homo sapiens	34-47
31629169-7	2020	In both organisms, H2O2 induces transient disulfide-linked conjugates between the MAP3K and a typical 2-Cys peroxiredoxin.	Hydrogen Peroxide	19-23	peroxiredoxin 2	Homo sapiens	108-121
31629169-7	2020	In both organisms, H2O2 induces transient disulfide-linked conjugates between the MAP3K and a typical 2-Cys peroxiredoxin.	Disulfides	42-51	peroxiredoxin 2	Homo sapiens	108-121
31629169-7	2020	In both organisms, H2O2 induces transient disulfide-linked conjugates between the MAP3K and a typical 2-Cys peroxiredoxin.	2-cys	102-107	peroxiredoxin 2	Homo sapiens	108-121
31629169-9	2020	Indeed, the depletion of cytosolic 2-Cys peroxiredoxins in human cells diminished H2O2-induced activation of p38 MAPK.	2-cys	35-40	peroxiredoxin 2	Homo sapiens	41-55
31536951-0	2020	PRDX2 protects against oxidative stress induced by H. pylori and promotes resistance to cisplatin in gastric cancer.	Cisplatin	88-97	peroxiredoxin 2	Homo sapiens	0-5
31629169-9	2020	Indeed, the depletion of cytosolic 2-Cys peroxiredoxins in human cells diminished H2O2-induced activation of p38 MAPK.	Hydrogen Peroxide	82-86	peroxiredoxin 2	Homo sapiens	41-55
31472963-0	2019	Differential oxidation processes of peroxiredoxin 2 dependent on the reaction with several peroxides in human red blood cells.	Peroxides	91-100	peroxiredoxin 2	Homo sapiens	36-51
31536951-7	2020	The knockdown of PRDX2 led to an increase in the levels of reactive oxygen species (ROS), oxidative DNA damage, and double-strand DNA breaks, in response to H. pylori infection, as measured by H2DCFDA, 8-oxoguanine, and p-H2AXgamma assays.	Reactive Oxygen Species	59-82	peroxiredoxin 2	Homo sapiens	17-22
31536951-7	2020	The knockdown of PRDX2 led to an increase in the levels of reactive oxygen species (ROS), oxidative DNA damage, and double-strand DNA breaks, in response to H. pylori infection, as measured by H2DCFDA, 8-oxoguanine, and p-H2AXgamma assays.	Reactive Oxygen Species	84-87	peroxiredoxin 2	Homo sapiens	17-22
31536951-7	2020	The knockdown of PRDX2 led to an increase in the levels of reactive oxygen species (ROS), oxidative DNA damage, and double-strand DNA breaks, in response to H. pylori infection, as measured by H2DCFDA, 8-oxoguanine, and p-H2AXgamma assays.	2',7'-dichlorodihydrofluorescein diacetate	193-200	peroxiredoxin 2	Homo sapiens	17-22
31536951-7	2020	The knockdown of PRDX2 led to an increase in the levels of reactive oxygen species (ROS), oxidative DNA damage, and double-strand DNA breaks, in response to H. pylori infection, as measured by H2DCFDA, 8-oxoguanine, and p-H2AXgamma assays.	8-hydroxyguanine	202-214	peroxiredoxin 2	Homo sapiens	17-22
31536951-7	2020	The knockdown of PRDX2 led to an increase in the levels of reactive oxygen species (ROS), oxidative DNA damage, and double-strand DNA breaks, in response to H. pylori infection, as measured by H2DCFDA, 8-oxoguanine, and p-H2AXgamma assays.	p-h2axgamma	220-231	peroxiredoxin 2	Homo sapiens	17-22
31536951-9	2020	The inhibition of PRDX2 significantly sensitized AGS and SNU-1 cells to cisplatin treatment.	Cisplatin	72-81	peroxiredoxin 2	Homo sapiens	18-23
31580947-6	2019	In contrast, hPrxII was present predominantly as the disulfide in unstressed cells and readily converted to its hyperoxidized, peroxidase-inactive form even with mild oxidative stress.	Disulfides	53-62	peroxiredoxin 2	Homo sapiens	13-19
31472963-1	2019	Peroxiredoxins (Prxs) detoxify hydrogen peroxide (H2O2), peroxynitrite, and various organic hydroperoxides.	Hydrogen Peroxide	31-48	peroxiredoxin 2	Homo sapiens	0-14
31472963-1	2019	Peroxiredoxins (Prxs) detoxify hydrogen peroxide (H2O2), peroxynitrite, and various organic hydroperoxides.	Hydrogen Peroxide	50-54	peroxiredoxin 2	Homo sapiens	0-14
31472963-1	2019	Peroxiredoxins (Prxs) detoxify hydrogen peroxide (H2O2), peroxynitrite, and various organic hydroperoxides.	Peroxynitrous Acid	57-70	peroxiredoxin 2	Homo sapiens	0-14
31472963-1	2019	Peroxiredoxins (Prxs) detoxify hydrogen peroxide (H2O2), peroxynitrite, and various organic hydroperoxides.	Hydrogen Peroxide	92-106	peroxiredoxin 2	Homo sapiens	0-14
31472963-3	2019	In the present study, we focused on the oxidative alteration of Prxs and demonstrated that, in human red blood cells (RBCs), peroxiredoxin 2 (Prx2) is readily reactive with H2O2, forming disulfide dimers, but was not easily hyperoxidized.	Hydrogen Peroxide	173-177	peroxiredoxin 2	Homo sapiens	125-140
31472963-3	2019	In the present study, we focused on the oxidative alteration of Prxs and demonstrated that, in human red blood cells (RBCs), peroxiredoxin 2 (Prx2) is readily reactive with H2O2, forming disulfide dimers, but was not easily hyperoxidized.	Hydrogen Peroxide	173-177	peroxiredoxin 2	Homo sapiens	142-146
31472963-3	2019	In the present study, we focused on the oxidative alteration of Prxs and demonstrated that, in human red blood cells (RBCs), peroxiredoxin 2 (Prx2) is readily reactive with H2O2, forming disulfide dimers, but was not easily hyperoxidized.	Disulfides	187-196	peroxiredoxin 2	Homo sapiens	125-140
31472963-3	2019	In the present study, we focused on the oxidative alteration of Prxs and demonstrated that, in human red blood cells (RBCs), peroxiredoxin 2 (Prx2) is readily reactive with H2O2, forming disulfide dimers, but was not easily hyperoxidized.	Disulfides	187-196	peroxiredoxin 2	Homo sapiens	142-146
31472963-4	2019	In contrast, Prx2 was highly sensitive to the relatively hydrophobic oxidants, such as tert-butyl hydroperoxide (t-BHP) and cumene hydroperoxide.	tert-Butylhydroperoxide	87-111	peroxiredoxin 2	Homo sapiens	13-17
31472963-4	2019	In contrast, Prx2 was highly sensitive to the relatively hydrophobic oxidants, such as tert-butyl hydroperoxide (t-BHP) and cumene hydroperoxide.	tert-Butylhydroperoxide	113-118	peroxiredoxin 2	Homo sapiens	13-17
31472963-4	2019	In contrast, Prx2 was highly sensitive to the relatively hydrophobic oxidants, such as tert-butyl hydroperoxide (t-BHP) and cumene hydroperoxide.	cumene hydroperoxide	124-144	peroxiredoxin 2	Homo sapiens	13-17
31472963-5	2019	These peroxides hyperoxidized Prx2 into oxidatively damaged forms in RBCs.	Peroxides	6-15	peroxiredoxin 2	Homo sapiens	30-34
31472963-6	2019	The t-BHP treatment formed hyperoxidized Prx2 in a dose-dependent manner.	tert-Butylhydroperoxide	4-9	peroxiredoxin 2	Homo sapiens	41-45
31472963-7	2019	When organic hydroperoxide-treated RBC lysates were subjected to reverse-phase high performance liquid chromatography, two peaks derived from hyperoxidized Prx2 appeared along with the decrease of that corresponding to native Prx2.	organic hydroperoxide	5-26	peroxiredoxin 2	Homo sapiens	156-160
31472963-7	2019	When organic hydroperoxide-treated RBC lysates were subjected to reverse-phase high performance liquid chromatography, two peaks derived from hyperoxidized Prx2 appeared along with the decrease of that corresponding to native Prx2.	organic hydroperoxide	5-26	peroxiredoxin 2	Homo sapiens	226-230
31472963-8	2019	Liquid chromatography-tandem mass spectrometry analysis clearly showed that hyperoxidation to sulfonic acid (-SO3H) at Cys-51 residue was more advanced in a newfound hyperoxidized Prx2 compared to another hydrophobic hyperoxidized form previously identified.	Sulfonic Acids	94-107	peroxiredoxin 2	Homo sapiens	180-184
31472963-8	2019	Liquid chromatography-tandem mass spectrometry analysis clearly showed that hyperoxidation to sulfonic acid (-SO3H) at Cys-51 residue was more advanced in a newfound hyperoxidized Prx2 compared to another hydrophobic hyperoxidized form previously identified.	so3h	110-114	peroxiredoxin 2	Homo sapiens	180-184
31472963-8	2019	Liquid chromatography-tandem mass spectrometry analysis clearly showed that hyperoxidation to sulfonic acid (-SO3H) at Cys-51 residue was more advanced in a newfound hyperoxidized Prx2 compared to another hydrophobic hyperoxidized form previously identified.	Cysteine	119-122	peroxiredoxin 2	Homo sapiens	180-184
31472963-9	2019	These results indicate that irreversible hyperoxidation of the Prx2 monomer in RBCs was easily caused by organic hydroperoxide but not H2O2.	organic hydroperoxide	105-126	peroxiredoxin 2	Homo sapiens	63-67
31472963-9	2019	These results indicate that irreversible hyperoxidation of the Prx2 monomer in RBCs was easily caused by organic hydroperoxide but not H2O2.	Hydrogen Peroxide	135-139	peroxiredoxin 2	Homo sapiens	63-67
31472963-10	2019	Thus, it is important to detect the hyperoxidation of Prx2 into sulfinic or sulfonic acid derivates of Cys-51 because hyperoxidized Prx2 is a potential marker of oxidative injury caused by organic hydroperoxides in human RBCs.	sulfinic	64-72	peroxiredoxin 2	Homo sapiens	54-58
31472963-10	2019	Thus, it is important to detect the hyperoxidation of Prx2 into sulfinic or sulfonic acid derivates of Cys-51 because hyperoxidized Prx2 is a potential marker of oxidative injury caused by organic hydroperoxides in human RBCs.	Cysteine	103-106	peroxiredoxin 2	Homo sapiens	54-58
31472963-10	2019	Thus, it is important to detect the hyperoxidation of Prx2 into sulfinic or sulfonic acid derivates of Cys-51 because hyperoxidized Prx2 is a potential marker of oxidative injury caused by organic hydroperoxides in human RBCs.	Cysteine	103-106	peroxiredoxin 2	Homo sapiens	132-136
31472963-10	2019	Thus, it is important to detect the hyperoxidation of Prx2 into sulfinic or sulfonic acid derivates of Cys-51 because hyperoxidized Prx2 is a potential marker of oxidative injury caused by organic hydroperoxides in human RBCs.	Hydrogen Peroxide	197-211	peroxiredoxin 2	Homo sapiens	54-58
31636515-8	2019	Meanwhile, using PRM, we identified three proteins that were closely related to abortion, B4DTF1 (highly similar to PSG1), P11464 (PSG1), and B4DF70 (highly similar to Prdx-2).	Phlorhizin	123-129	peroxiredoxin 2	Homo sapiens	168-174
31472963-10	2019	Thus, it is important to detect the hyperoxidation of Prx2 into sulfinic or sulfonic acid derivates of Cys-51 because hyperoxidized Prx2 is a potential marker of oxidative injury caused by organic hydroperoxides in human RBCs.	Hydrogen Peroxide	197-211	peroxiredoxin 2	Homo sapiens	132-136
31323313-2	2019	The first step in catalysis, the reduction of peroxide substrate, is fast, 107 - 108 M-1s-1 for human Prx2.	Peroxides	46-54	peroxiredoxin 2	Homo sapiens	102-106
31323313-7	2019	We previously reported that treatment of human Prx2 with peroxynitrite results in tyrosine nitration, a post-translational modification on non-catalytic residues, yielding a more active peroxidase with higher resistance to hyperoxidation.	Peroxynitrous Acid	57-70	peroxiredoxin 2	Homo sapiens	47-51
31323313-7	2019	We previously reported that treatment of human Prx2 with peroxynitrite results in tyrosine nitration, a post-translational modification on non-catalytic residues, yielding a more active peroxidase with higher resistance to hyperoxidation.	Tyrosine	82-90	peroxiredoxin 2	Homo sapiens	47-51
31470801-1	2019	BACKGROUND: This study aims to investigate the expression of thioredoxin 1, peroxiredoxin 1 and peroxiredoxin 2 in bulky cervical squamous carcinoma and its predictive role in cisplatin-based neoadjuvant chemotherapy.	Cisplatin	176-185	peroxiredoxin 2	Homo sapiens	96-111
30444369-8	2019	Two additional proteins, peroxiredoxin-2 and endophilin-1, are implicated in Abeta-ABAD complex-mediated toxicity.	abeta-abad	77-87	peroxiredoxin 2	Homo sapiens	25-40
31197039-4	2019	Here, using in vitro biochemical assays with purified, recombinant protein, along with experiments in the adenocarcinoma cell line A431, we discovered that bicarbonate, which reacts with H2O2 to form the more reactive peroxymonocarbonate, potently facilitates H2O2-mediated PTP1B inactivation in the presence of thioredoxin reductase 1 (TrxR1), thioredoxin 1 (Trx1), and peroxiredoxin 2 (Prx2) together with NADPH.	Bicarbonates	156-167	peroxiredoxin 2	Homo sapiens	371-386
31197039-4	2019	Here, using in vitro biochemical assays with purified, recombinant protein, along with experiments in the adenocarcinoma cell line A431, we discovered that bicarbonate, which reacts with H2O2 to form the more reactive peroxymonocarbonate, potently facilitates H2O2-mediated PTP1B inactivation in the presence of thioredoxin reductase 1 (TrxR1), thioredoxin 1 (Trx1), and peroxiredoxin 2 (Prx2) together with NADPH.	Bicarbonates	156-167	peroxiredoxin 2	Homo sapiens	388-392
31197039-4	2019	Here, using in vitro biochemical assays with purified, recombinant protein, along with experiments in the adenocarcinoma cell line A431, we discovered that bicarbonate, which reacts with H2O2 to form the more reactive peroxymonocarbonate, potently facilitates H2O2-mediated PTP1B inactivation in the presence of thioredoxin reductase 1 (TrxR1), thioredoxin 1 (Trx1), and peroxiredoxin 2 (Prx2) together with NADPH.	Hydrogen Peroxide	187-191	peroxiredoxin 2	Homo sapiens	371-386
31197039-4	2019	Here, using in vitro biochemical assays with purified, recombinant protein, along with experiments in the adenocarcinoma cell line A431, we discovered that bicarbonate, which reacts with H2O2 to form the more reactive peroxymonocarbonate, potently facilitates H2O2-mediated PTP1B inactivation in the presence of thioredoxin reductase 1 (TrxR1), thioredoxin 1 (Trx1), and peroxiredoxin 2 (Prx2) together with NADPH.	Hydrogen Peroxide	187-191	peroxiredoxin 2	Homo sapiens	388-392
30611866-0	2019	Prx2 links ROS homeostasis to stemness of cancer stem cells.	Reactive Oxygen Species	11-14	peroxiredoxin 2	Homo sapiens	0-4
30862546-8	2019	In contrast, Prx1 and Prx2 were present in neutrophils from human blood as disulfides, and PMA or S. aureus caused no further oxidation.	Disulfides	75-85	peroxiredoxin 2	Homo sapiens	22-26
30879771-2	2019	Peroxiredoxin2 (Prx2) functions as a reactive oxygen species (ROS)-mediated signaling regulator that controls H2O2 in mammalian cells, and it is involved in the survival of various malignant tumors.	Reactive Oxygen Species	37-60	peroxiredoxin 2	Homo sapiens	0-14
30879771-2	2019	Peroxiredoxin2 (Prx2) functions as a reactive oxygen species (ROS)-mediated signaling regulator that controls H2O2 in mammalian cells, and it is involved in the survival of various malignant tumors.	Reactive Oxygen Species	37-60	peroxiredoxin 2	Homo sapiens	16-20
30879771-2	2019	Peroxiredoxin2 (Prx2) functions as a reactive oxygen species (ROS)-mediated signaling regulator that controls H2O2 in mammalian cells, and it is involved in the survival of various malignant tumors.	Reactive Oxygen Species	62-65	peroxiredoxin 2	Homo sapiens	0-14
30879771-2	2019	Peroxiredoxin2 (Prx2) functions as a reactive oxygen species (ROS)-mediated signaling regulator that controls H2O2 in mammalian cells, and it is involved in the survival of various malignant tumors.	Reactive Oxygen Species	62-65	peroxiredoxin 2	Homo sapiens	16-20
30879771-2	2019	Peroxiredoxin2 (Prx2) functions as a reactive oxygen species (ROS)-mediated signaling regulator that controls H2O2 in mammalian cells, and it is involved in the survival of various malignant tumors.	Hydrogen Peroxide	110-114	peroxiredoxin 2	Homo sapiens	0-14
30879771-2	2019	Peroxiredoxin2 (Prx2) functions as a reactive oxygen species (ROS)-mediated signaling regulator that controls H2O2 in mammalian cells, and it is involved in the survival of various malignant tumors.	Hydrogen Peroxide	110-114	peroxiredoxin 2	Homo sapiens	16-20
30879771-5	2019	Furthermore, an experiment using conoidinA, a Prx2 inhibitor, revealed that Prx2 inhibition can overcome 5-FU resistance in GC cells.	Fluorouracil	105-109	peroxiredoxin 2	Homo sapiens	76-80
30988280-0	2019	S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway.	Sulfur	0-1	peroxiredoxin 2	Homo sapiens	23-38
30988280-0	2019	S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway.	S-Nitrosoglutathione	50-68	peroxiredoxin 2	Homo sapiens	23-38
30988280-3	2019	Peroxiredoxin-2 (Prdx2), an antioxidant enzyme, plays an important role in the protection of cancer cells from oxidative radical damage caused by hydrogen dioxide (H2O2), which is a potential target for cancer therapy.	Hydrogen Peroxide	146-162	peroxiredoxin 2	Homo sapiens	0-15
30988280-3	2019	Peroxiredoxin-2 (Prdx2), an antioxidant enzyme, plays an important role in the protection of cancer cells from oxidative radical damage caused by hydrogen dioxide (H2O2), which is a potential target for cancer therapy.	Hydrogen Peroxide	146-162	peroxiredoxin 2	Homo sapiens	17-22
30988280-3	2019	Peroxiredoxin-2 (Prdx2), an antioxidant enzyme, plays an important role in the protection of cancer cells from oxidative radical damage caused by hydrogen dioxide (H2O2), which is a potential target for cancer therapy.	Hydrogen Peroxide	164-168	peroxiredoxin 2	Homo sapiens	0-15
30988280-3	2019	Peroxiredoxin-2 (Prdx2), an antioxidant enzyme, plays an important role in the protection of cancer cells from oxidative radical damage caused by hydrogen dioxide (H2O2), which is a potential target for cancer therapy.	Hydrogen Peroxide	164-168	peroxiredoxin 2	Homo sapiens	17-22
30988280-4	2019	Our studies showed that, as an endogenous NO carrier, S-nitrosoglutathione (GSNO) induced apoptosis in lung cancer cells via nitrosylating Prdx2.	S-Nitrosoglutathione	54-74	peroxiredoxin 2	Homo sapiens	139-144
30988280-4	2019	Our studies showed that, as an endogenous NO carrier, S-nitrosoglutathione (GSNO) induced apoptosis in lung cancer cells via nitrosylating Prdx2.	S-Nitrosoglutathione	76-80	peroxiredoxin 2	Homo sapiens	139-144
30988280-5	2019	The nitrosylation of Prdx2 at Cys51 and Cys172 sites disrupted the formation of Prdx2 dimer and repressed the Prdx2 antioxidant activity, causing the accumulation of endogenous H2O2.	Hydrogen Peroxide	177-181	peroxiredoxin 2	Homo sapiens	21-26
30959964-9	2019	Furthermore, we also reveal that ANXA2 inversely regulates the expression of the peroxidase, peroxiredoxin 2, in a reactive oxygen species dependent manner.	Reactive Oxygen Species	115-138	peroxiredoxin 2	Homo sapiens	93-108
30605715-2	2019	Prx2 belongs to an evolutionarily ancient family of peroxidases that are involved in enzymatic degradation of a wide variety of organic and inorganic hydroperoxides.	Hydrogen Peroxide	150-164	peroxiredoxin 2	Homo sapiens	0-4
30605715-7	2019	The radioprotective properties of exogenous Prx2 are stipulated by its broad substrate peroxidase activity, chaperone activity in the oxidized state, and are also due to the signal-regulatory function of Prx2 mediated by the regulation of the level of hydroperoxides as well as via interaction with redox-sensitive regulatory proteins.	Hydrogen Peroxide	252-266	peroxiredoxin 2	Homo sapiens	44-48
30605715-7	2019	The radioprotective properties of exogenous Prx2 are stipulated by its broad substrate peroxidase activity, chaperone activity in the oxidized state, and are also due to the signal-regulatory function of Prx2 mediated by the regulation of the level of hydroperoxides as well as via interaction with redox-sensitive regulatory proteins.	Hydrogen Peroxide	252-266	peroxiredoxin 2	Homo sapiens	204-208
31065010-5	2019	Torin, PP242, and a PKCzeta inhibitory peptide, but not rapamycin, prevented these biliverdin-induced responses and TLR4 inhibition.	Biliverdine	83-93	peroxiredoxin 2	Homo sapiens	0-5
30611866-2	2019	Peroxiredoxin 2 (Prx2) is a redox regulatory protein that plays a key role in maintaining ROS homeostasis in the tumor microenvironment.	Reactive Oxygen Species	90-93	peroxiredoxin 2	Homo sapiens	0-15
30611866-2	2019	Peroxiredoxin 2 (Prx2) is a redox regulatory protein that plays a key role in maintaining ROS homeostasis in the tumor microenvironment.	Reactive Oxygen Species	90-93	peroxiredoxin 2	Homo sapiens	17-21
30611866-3	2019	However, despite the role of Prx2 in ROS-mediated signal transduction, the association of Prx2 with stemness via ROS in CSC has not been thoroughly investigated.	Reactive Oxygen Species	113-116	peroxiredoxin 2	Homo sapiens	90-94
30611866-4	2019	In this study, we investigated the link between Prx2 and CSC stemness through regulation of ROS levels in hepatocellular carcinoma (HCC) cells.	Reactive Oxygen Species	92-95	peroxiredoxin 2	Homo sapiens	48-52
30611866-6	2019	Prx2 knockdown decreased CSC sphere formation and expression of stem cell makers with increasing intracellular ROS levels.	Reactive Oxygen Species	111-114	peroxiredoxin 2	Homo sapiens	0-4
30611866-7	2019	This effect was reversed by the ROS scavengers NAC and GSH in Prx2 knockdown cells.	Reactive Oxygen Species	32-35	peroxiredoxin 2	Homo sapiens	62-66
30611866-7	2019	This effect was reversed by the ROS scavengers NAC and GSH in Prx2 knockdown cells.	Glutathione	55-58	peroxiredoxin 2	Homo sapiens	62-66
30611866-10	2019	Taken together, our findings demonstrate that Prx2 links ROS homeostasis to CSC stemness; Prx2 is a mediator between ROS homeostasis and CSC stemness.	Reactive Oxygen Species	57-60	peroxiredoxin 2	Homo sapiens	46-50
30611866-10	2019	Taken together, our findings demonstrate that Prx2 links ROS homeostasis to CSC stemness; Prx2 is a mediator between ROS homeostasis and CSC stemness.	Reactive Oxygen Species	117-120	peroxiredoxin 2	Homo sapiens	90-94
30844732-2	2019	To this end, the interactions between the different hemoglobin (Hb) subunits and peroxiredoxin 2, which is a ubiquitous member of the antioxidant enzymes that also controls the cytokine-induced peroxide levels, were assessed.	Peroxides	194-202	peroxiredoxin 2	Homo sapiens	81-96
30844732-6	2019	Adding Prx2 to hemoglobin A altered the second shell of iron embedded in hemoglobin A.	Iron	56-60	peroxiredoxin 2	Homo sapiens	7-11
30284335-3	2019	Using recombinant human PRDX1 and PRDX2, the kinetics of oxidation and hyperoxidation with H2 O2 and peroxynitrite were followed by intrinsic fluorescence.	Peroxynitrous Acid	101-114	peroxiredoxin 2	Homo sapiens	34-39
30284335-6	2019	As previously observed, a crucial difference between PRDX1 and PRDX2 is on the resolution step of the catalytic cycle, the rate of disulfide formation (11 s-1 for PRDX1, 0.2 s-1 for PRDX2, independent of the oxidant) which correlates with their different sensitivity to hyperoxidation.	Disulfides	131-140	peroxiredoxin 2	Homo sapiens	63-68
30284335-6	2019	As previously observed, a crucial difference between PRDX1 and PRDX2 is on the resolution step of the catalytic cycle, the rate of disulfide formation (11 s-1 for PRDX1, 0.2 s-1 for PRDX2, independent of the oxidant) which correlates with their different sensitivity to hyperoxidation.	Disulfides	131-140	peroxiredoxin 2	Homo sapiens	182-187
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Sulfenic Acids	29-42	peroxiredoxin 2	Homo sapiens	23-28
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Sulfhydryl Compounds	81-87	peroxiredoxin 2	Homo sapiens	23-28
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Disulfides	138-147	peroxiredoxin 2	Homo sapiens	23-28
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Cysteine	175-183	peroxiredoxin 2	Homo sapiens	23-28
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Disulfides	228-237	peroxiredoxin 2	Homo sapiens	23-28
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Cysteine	262-270	peroxiredoxin 2	Homo sapiens	23-28
30187908-9	2018	The H2O2-induced reduction in sperm motility was reversed by recombinant PRDX2 or PRDX6 in a dose-dependent manner.	Hydrogen Peroxide	4-8	peroxiredoxin 2	Homo sapiens	73-78
30521599-6	2018	Despite the importance of these enzymes, Prdx1 and Prdx2 may have their peroxidase activity inactivated by hyperoxidation at high hydroperoxide concentrations, which also promotes the molecular chaperone activity of these proteins.	Hydrogen Peroxide	130-143	peroxiredoxin 2	Homo sapiens	51-56
30396550-8	2018	RESULT(S): In normozoospermic and asthenozoospermic groups, the addition of 150 mug/mL TAT-PRDX2 significantly reduced intracellular ROS and malondialdehyde levels and enhanced post-thaw sperm motility and viability when compared with the cryopreserved control of the respective groups but did not produce any significant protective effect in the oligoasthenozoospermic group.	Reactive Oxygen Species	133-136	peroxiredoxin 2	Homo sapiens	91-96
30396550-8	2018	RESULT(S): In normozoospermic and asthenozoospermic groups, the addition of 150 mug/mL TAT-PRDX2 significantly reduced intracellular ROS and malondialdehyde levels and enhanced post-thaw sperm motility and viability when compared with the cryopreserved control of the respective groups but did not produce any significant protective effect in the oligoasthenozoospermic group.	Malondialdehyde	141-156	peroxiredoxin 2	Homo sapiens	91-96
30396550-10	2018	Although the penetration rate and the penetration index were not markedly improved, TAT-PRDX2 supplementation obviously reduced spontaneous acrosome reaction and increased calcium ionophore-induced acrosome reaction in the normozoospermic and asthenozoospermic groups.	Calcium	172-179	peroxiredoxin 2	Homo sapiens	88-93
30396550-11	2018	CONCLUSION(S): TAT-PRDX2 protein effectively exerted cryoprotective effects on spermatozoa by reducing intracellular ROS level and thereby improved post-thaw sperm quality and function, especially for asthenozoospermic samples.	Reactive Oxygen Species	117-120	peroxiredoxin 2	Homo sapiens	19-24
30245403-4	2018	We found that DNMT3A-R882H/C mutations upregulated the expression of an antioxidant protein, pyroxiredoxin-2 (PRDX2), at the mRNA and protein levels with decreased accumulation of reactive oxygen species (ROS).	Reactive Oxygen Species	180-203	peroxiredoxin 2	Homo sapiens	110-115
30245403-4	2018	We found that DNMT3A-R882H/C mutations upregulated the expression of an antioxidant protein, pyroxiredoxin-2 (PRDX2), at the mRNA and protein levels with decreased accumulation of reactive oxygen species (ROS).	Reactive Oxygen Species	205-208	peroxiredoxin 2	Homo sapiens	110-115
30245403-5	2018	Augmentation of ROS generation by ROS accumulating agent or by knockdown of PRDX2 from myeloid cells effectively increased drug sensitivity and apoptosis as a consequence of reduced cell proliferation.	Reactive Oxygen Species	16-19	peroxiredoxin 2	Homo sapiens	76-81
29627155-9	2018	Proteomic studies on the 20 micromol/L FTI-277 and 5 micromol/L alendronate +20 micromol/L FTI-277 treated cells revealed altered expression of different proteins including peroxiredoxin 2 (Prx2), glutathione S transferase 1 (GSTP1), Rho GTPase activating protein (RhoGAP), triosephosphate isomerase (TPI), and heat shock protein 60 (HSP60).	Alendronate	64-75	peroxiredoxin 2	Homo sapiens	173-188
29627155-9	2018	Proteomic studies on the 20 micromol/L FTI-277 and 5 micromol/L alendronate +20 micromol/L FTI-277 treated cells revealed altered expression of different proteins including peroxiredoxin 2 (Prx2), glutathione S transferase 1 (GSTP1), Rho GTPase activating protein (RhoGAP), triosephosphate isomerase (TPI), and heat shock protein 60 (HSP60).	Alendronate	64-75	peroxiredoxin 2	Homo sapiens	190-194
29574146-0	2018	A mathematical analysis of Prx2-STAT3 disulfide exchange rate constants for a bimolecular reaction mechanism.	Disulfides	38-47	peroxiredoxin 2	Homo sapiens	27-31
29574146-1	2018	Appreciation of peroxiredoxins as the major regulators of H2O2 concentrations in human cells has led to a new understanding of redox signaling.	Hydrogen Peroxide	58-62	peroxiredoxin 2	Homo sapiens	16-30
29574146-2	2018	In addition to their status as the primary reducers of H2O2 to water, the oxidized peroxiredoxin byproduct of this reaction has recently been shown capable of participation in H2O2-mediated signaling pathways through disulfide exchange reactions with the transcription factor STAT3.	Hydrogen Peroxide	55-59	peroxiredoxin 2	Homo sapiens	83-96
29574146-2	2018	In addition to their status as the primary reducers of H2O2 to water, the oxidized peroxiredoxin byproduct of this reaction has recently been shown capable of participation in H2O2-mediated signaling pathways through disulfide exchange reactions with the transcription factor STAT3.	Water	63-68	peroxiredoxin 2	Homo sapiens	83-96
29574146-2	2018	In addition to their status as the primary reducers of H2O2 to water, the oxidized peroxiredoxin byproduct of this reaction has recently been shown capable of participation in H2O2-mediated signaling pathways through disulfide exchange reactions with the transcription factor STAT3.	Hydrogen Peroxide	176-180	peroxiredoxin 2	Homo sapiens	83-96
29574146-2	2018	In addition to their status as the primary reducers of H2O2 to water, the oxidized peroxiredoxin byproduct of this reaction has recently been shown capable of participation in H2O2-mediated signaling pathways through disulfide exchange reactions with the transcription factor STAT3.	Disulfides	217-226	peroxiredoxin 2	Homo sapiens	83-96
29574146-4	2018	In this study, we used a kinetic model of oxidation and reduction reactions related to H2O2 metabolism in the cytosol of human cells to study the dynamics of peroxiredoxin-2 mediated oxidation of the redox-regulated transcription factor STAT3.	Hydrogen Peroxide	87-91	peroxiredoxin 2	Homo sapiens	158-173
29574146-8	2018	This analysis suggests the existence of more complex mechanisms, potentially involving currently unknown protein-protein recognition partners, which facilitate disulfide exchange reactions between peroxiredoxin-2 and STAT3.	Disulfides	160-169	peroxiredoxin 2	Homo sapiens	197-212
30177619-6	2018	Peroxiredoxin II (Prx II) is a member of peroxiredoxin antioxidant enzyme family which considers as a regulator of ROS in cellular environments by modulating redox status to maintain CSC phenotype and stemness properties.	Reactive Oxygen Species	115-118	peroxiredoxin 2	Homo sapiens	0-16
30177619-6	2018	Peroxiredoxin II (Prx II) is a member of peroxiredoxin antioxidant enzyme family which considers as a regulator of ROS in cellular environments by modulating redox status to maintain CSC phenotype and stemness properties.	Reactive Oxygen Species	115-118	peroxiredoxin 2	Homo sapiens	18-24
30087344-4	2018	We report a fluorescent sensor based upon human peroxiredoxin-2, which acts as the natural indicator of small H2O2 fluctuations in human cells.	Hydrogen Peroxide	110-114	peroxiredoxin 2	Homo sapiens	48-63
28348082-0	2017	Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2.	urate hydroperoxide	0-19	peroxiredoxin 2	Homo sapiens	55-70
29063293-0	2017	Two mTOR inhibitors, rapamycin and Torin 1, differentially regulate iron-induced generation of mitochondrial ROS.	Iron	68-72	peroxiredoxin 2	Homo sapiens	35-40
29063293-0	2017	Two mTOR inhibitors, rapamycin and Torin 1, differentially regulate iron-induced generation of mitochondrial ROS.	ros	109-112	peroxiredoxin 2	Homo sapiens	35-40
29063293-5	2017	Two mTOR inhibitors, rapamycin and Torin 1, had similar effects in cells exposed to a relatively low concentration of iron.	Iron	118-122	peroxiredoxin 2	Homo sapiens	35-40
29063293-6	2017	At a higher concentration of iron, Torin 1, instead of rapamycin, could further aggravate iron-induced cytotoxicity, and mitochondrial ROS levels were significantly higher in Torin 1-treated cells.	Iron	29-33	peroxiredoxin 2	Homo sapiens	35-40
29063293-6	2017	At a higher concentration of iron, Torin 1, instead of rapamycin, could further aggravate iron-induced cytotoxicity, and mitochondrial ROS levels were significantly higher in Torin 1-treated cells.	Iron	29-33	peroxiredoxin 2	Homo sapiens	175-180
29063293-6	2017	At a higher concentration of iron, Torin 1, instead of rapamycin, could further aggravate iron-induced cytotoxicity, and mitochondrial ROS levels were significantly higher in Torin 1-treated cells.	Iron	90-94	peroxiredoxin 2	Homo sapiens	35-40
29063293-6	2017	At a higher concentration of iron, Torin 1, instead of rapamycin, could further aggravate iron-induced cytotoxicity, and mitochondrial ROS levels were significantly higher in Torin 1-treated cells.	ros	135-138	peroxiredoxin 2	Homo sapiens	175-180
29123070-2	2017	We find that perturbation of ribonucleotide reductase (RNR) in humans elevates reactive oxygen species (ROS) that are detected by peroxiredoxin 2 (PRDX2).	Reactive Oxygen Species	79-102	peroxiredoxin 2	Homo sapiens	130-145
29123070-2	2017	We find that perturbation of ribonucleotide reductase (RNR) in humans elevates reactive oxygen species (ROS) that are detected by peroxiredoxin 2 (PRDX2).	Reactive Oxygen Species	79-102	peroxiredoxin 2	Homo sapiens	147-152
29123070-2	2017	We find that perturbation of ribonucleotide reductase (RNR) in humans elevates reactive oxygen species (ROS) that are detected by peroxiredoxin 2 (PRDX2).	Reactive Oxygen Species	104-107	peroxiredoxin 2	Homo sapiens	130-145
29123070-2	2017	We find that perturbation of ribonucleotide reductase (RNR) in humans elevates reactive oxygen species (ROS) that are detected by peroxiredoxin 2 (PRDX2).	Reactive Oxygen Species	104-107	peroxiredoxin 2	Homo sapiens	147-152
29123070-3	2017	In the oligomeric state, PRDX2 forms a replisome-associated ROS sensor, which binds the fork accelerator TIMELESS when exposed to low levels of ROS.	Reactive Oxygen Species	60-63	peroxiredoxin 2	Homo sapiens	25-30
29123070-3	2017	In the oligomeric state, PRDX2 forms a replisome-associated ROS sensor, which binds the fork accelerator TIMELESS when exposed to low levels of ROS.	Reactive Oxygen Species	144-147	peroxiredoxin 2	Homo sapiens	25-30
29123070-4	2017	Elevated ROS levels generated by RNR attenuation disrupt oligomerized PRDX2 to smaller subunits, whose dissociation from chromatin enforces the displacement of TIMELESS from the replisome.	Reactive Oxygen Species	9-12	peroxiredoxin 2	Homo sapiens	70-75
28698499-9	2017	Exposure to L-DOPA may result in hypoxia condition and further induction of ORP150 (150-kDa oxygen-regulated protein) with its concomitant cytoprotective effects but Edaravone seems to protect cells via direct induction of Peroxiredoxin-2 and inhibition of apoptosis.	Levodopa	12-18	peroxiredoxin 2	Homo sapiens	223-238
28661480-1	2017	Peroxiredoxin (Prdx) 2 is an antioxidant protein that utilizes its redox-sensitive cysteine groups to reduce hydrogen peroxide molecules and protect cells against oxidative damage from reactive oxygen species (ROS).	Cysteine	83-91	peroxiredoxin 2	Homo sapiens	0-22
28661480-1	2017	Peroxiredoxin (Prdx) 2 is an antioxidant protein that utilizes its redox-sensitive cysteine groups to reduce hydrogen peroxide molecules and protect cells against oxidative damage from reactive oxygen species (ROS).	Hydrogen Peroxide	109-126	peroxiredoxin 2	Homo sapiens	0-22
28661480-1	2017	Peroxiredoxin (Prdx) 2 is an antioxidant protein that utilizes its redox-sensitive cysteine groups to reduce hydrogen peroxide molecules and protect cells against oxidative damage from reactive oxygen species (ROS).	Reactive Oxygen Species	185-208	peroxiredoxin 2	Homo sapiens	0-22
28661480-1	2017	Peroxiredoxin (Prdx) 2 is an antioxidant protein that utilizes its redox-sensitive cysteine groups to reduce hydrogen peroxide molecules and protect cells against oxidative damage from reactive oxygen species (ROS).	Reactive Oxygen Species	210-213	peroxiredoxin 2	Homo sapiens	0-22
28661480-5	2017	The reason for this may be an increase in the level of cellular ROS after knockdown of Prdx2, which may subsequently lead to an increase in the expression of phosphorylated p53 (p-p53) and p38-MAPK/p21.	Reactive Oxygen Species	64-67	peroxiredoxin 2	Homo sapiens	87-92
28661480-6	2017	Prdx2 knockdown also impaired the fusion of BeWo cells induced by forskolin.	Colforsin	66-75	peroxiredoxin 2	Homo sapiens	0-5
28434171-0	2017	Peroxidatic cysteine residue of peroxiredoxin 2 separated from human red blood cells treated by tert-butyl hydroperoxide is hyperoxidized into sulfinic and sulfonic acids.	Cysteine	12-20	peroxiredoxin 2	Homo sapiens	32-47
28434171-0	2017	Peroxidatic cysteine residue of peroxiredoxin 2 separated from human red blood cells treated by tert-butyl hydroperoxide is hyperoxidized into sulfinic and sulfonic acids.	tert-Butylhydroperoxide	96-120	peroxiredoxin 2	Homo sapiens	32-47
28434171-0	2017	Peroxidatic cysteine residue of peroxiredoxin 2 separated from human red blood cells treated by tert-butyl hydroperoxide is hyperoxidized into sulfinic and sulfonic acids.	sulfinic	143-151	peroxiredoxin 2	Homo sapiens	32-47
28434171-0	2017	Peroxidatic cysteine residue of peroxiredoxin 2 separated from human red blood cells treated by tert-butyl hydroperoxide is hyperoxidized into sulfinic and sulfonic acids.	Sulfonic Acids	156-170	peroxiredoxin 2	Homo sapiens	32-47
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	Cysteine	110-118	peroxiredoxin 2	Homo sapiens	48-52
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	Cysteine	131-134	peroxiredoxin 2	Homo sapiens	48-52
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	Sulfinic Acids	210-223	peroxiredoxin 2	Homo sapiens	48-52
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	so2h	226-230	peroxiredoxin 2	Homo sapiens	48-52
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	Sulfonic Acids	236-249	peroxiredoxin 2	Homo sapiens	48-52
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	so3h	252-256	peroxiredoxin 2	Homo sapiens	48-52
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	tert-Butylhydroperoxide	280-304	peroxiredoxin 2	Homo sapiens	48-52
28434171-4	2017	The LC-MS/MS analysis of the trypsin digests of Prx2 fractionated by reverse-phase HPLC demonstrated that the cysteine-51 residue (Cys-51) of the protein was modified with the hyperoxidative functional groups, sulfinic acid (-SO2H) and sulfonic acid (-SO3H), in RBCs treated with tert-butyl hydroperoxide (t-BHP).	tert-Butylhydroperoxide	306-311	peroxiredoxin 2	Homo sapiens	48-52
28434171-5	2017	Furthermore, a selected ion monitoring (SIM) analysis quantitatively showed that sulfinic acid- and sulfonic acid-induced modifications in Prx2 Cys-51 were increased by the treatment with the oxidant.	Sulfinic Acids	81-94	peroxiredoxin 2	Homo sapiens	139-143
28434171-5	2017	Furthermore, a selected ion monitoring (SIM) analysis quantitatively showed that sulfinic acid- and sulfonic acid-induced modifications in Prx2 Cys-51 were increased by the treatment with the oxidant.	Sulfonic Acids	100-113	peroxiredoxin 2	Homo sapiens	139-143
28434171-5	2017	Furthermore, a selected ion monitoring (SIM) analysis quantitatively showed that sulfinic acid- and sulfonic acid-induced modifications in Prx2 Cys-51 were increased by the treatment with the oxidant.	Cysteine	144-147	peroxiredoxin 2	Homo sapiens	139-143
28434171-6	2017	It was demonstrated that the peroxidatic cysteine of Prx2 separated using our HPLC system for oxidative monitoring was hyperoxidized into sulfinic acid and sulfonic acid in RBCs under an oxidative stress condition.	Cysteine	41-49	peroxiredoxin 2	Homo sapiens	53-57
28434171-6	2017	It was demonstrated that the peroxidatic cysteine of Prx2 separated using our HPLC system for oxidative monitoring was hyperoxidized into sulfinic acid and sulfonic acid in RBCs under an oxidative stress condition.	Sulfinic Acids	138-151	peroxiredoxin 2	Homo sapiens	53-57
28434171-6	2017	It was demonstrated that the peroxidatic cysteine of Prx2 separated using our HPLC system for oxidative monitoring was hyperoxidized into sulfinic acid and sulfonic acid in RBCs under an oxidative stress condition.	Sulfonic Acids	156-169	peroxiredoxin 2	Homo sapiens	53-57
28427860-7	2017	Cells with low levels of Akt Ser-473 phosphorylation were more resistant to the cytotoxic effects of mTOR inhibition with Torin-2, but not KU-0063794.	Serine	29-32	peroxiredoxin 2	Homo sapiens	122-127
28427860-8	2017	Exposure to Torin-2 and KU-0063794 both potently and rapidly inhibited phosphorylation of Akt Ser-473 and Thr-308, and 4E-BP1 T37/46 in cell lines that included basal and nontype subtypes.	Serine	94-97	peroxiredoxin 2	Homo sapiens	12-17
28427860-8	2017	Exposure to Torin-2 and KU-0063794 both potently and rapidly inhibited phosphorylation of Akt Ser-473 and Thr-308, and 4E-BP1 T37/46 in cell lines that included basal and nontype subtypes.	Threonine	106-109	peroxiredoxin 2	Homo sapiens	12-17
28823893-9	2017	Pharmacological inhibition of HDAC6 with specific inhibitor tubastatin A increased acetylation of Prx1 and Prx2, reduced ROS production and ameliorated dopaminergic neurotoxicity.	tubastatin A	60-72	peroxiredoxin 2	Homo sapiens	107-111
28461233-5	2017	The redox state of peroxiredoxins (Prx1, Prx2 and Prx3) was markedly shifted to dimer 30min after treatment with 100muM 2-AAPA, an event preceding 2-AAPA-induced decrease in cell viability.	2-acetylamino-3-(4-(2-acetylamino-2-carboxyethylsulfanylthiocarbonylamino)phenylthiocarbamoylsulfanyl)propionic acid	120-126	peroxiredoxin 2	Homo sapiens	41-45
28461233-5	2017	The redox state of peroxiredoxins (Prx1, Prx2 and Prx3) was markedly shifted to dimer 30min after treatment with 100muM 2-AAPA, an event preceding 2-AAPA-induced decrease in cell viability.	2-acetylamino-3-(4-(2-acetylamino-2-carboxyethylsulfanylthiocarbonylamino)phenylthiocarbamoylsulfanyl)propionic acid	147-153	peroxiredoxin 2	Homo sapiens	41-45
28489720-10	2017	The increase of VEGFR2 might be related to the increase of peroxiredoxin 2 in response to excessive reactive oxygen species from ultraviolet exposure.	Reactive Oxygen Species	100-123	peroxiredoxin 2	Homo sapiens	59-74
28659575-8	2017	Collectively, this study reveals a redox mechanism for regulating tankyrase activity and implicates PrxII as a targetable antioxidant enzyme in APC-mutation-positive colorectal cancer.2-Cys peroxiredoxin (Prx) enzymes are highly expressed in most cancers but how they promote cancer progression is unclear.	2-cys	184-189	peroxiredoxin 2	Homo sapiens	100-105
28348082-4	2017	The kinetics for the oxidation of the cytosolic 2-Cys Prx1 and Prx2 revealed that urate hydroperoxide oxidizes these enzymes at rates comparable with hydrogen peroxide.	urate hydroperoxide	82-101	peroxiredoxin 2	Homo sapiens	63-67
28348082-6	2017	Kinetic and simulation data suggest that the oxidation of Prx2 by urate hydroperoxide occurs by a three-step mechanism, where the peroxide reversibly associates with the enzyme; then it oxidizes the peroxidatic cysteine, and finally, the rate-limiting disulfide bond is formed.	urate hydroperoxide	66-85	peroxiredoxin 2	Homo sapiens	58-62
28348082-6	2017	Kinetic and simulation data suggest that the oxidation of Prx2 by urate hydroperoxide occurs by a three-step mechanism, where the peroxide reversibly associates with the enzyme; then it oxidizes the peroxidatic cysteine, and finally, the rate-limiting disulfide bond is formed.	Peroxides	77-85	peroxiredoxin 2	Homo sapiens	58-62
28348082-6	2017	Kinetic and simulation data suggest that the oxidation of Prx2 by urate hydroperoxide occurs by a three-step mechanism, where the peroxide reversibly associates with the enzyme; then it oxidizes the peroxidatic cysteine, and finally, the rate-limiting disulfide bond is formed.	Cysteine	211-219	peroxiredoxin 2	Homo sapiens	58-62
28348082-6	2017	Kinetic and simulation data suggest that the oxidation of Prx2 by urate hydroperoxide occurs by a three-step mechanism, where the peroxide reversibly associates with the enzyme; then it oxidizes the peroxidatic cysteine, and finally, the rate-limiting disulfide bond is formed.	Disulfides	252-261	peroxiredoxin 2	Homo sapiens	58-62
28348082-7	2017	Of relevance, the disulfide bond formation was much slower in Prx2 (k3 = 0.31 s-1) than Prx1 (k3 = 14.9 s-1).	Disulfides	18-27	peroxiredoxin 2	Homo sapiens	62-66
28348082-8	2017	In addition, Prx2 was more sensitive than Prx1 to hyperoxidation caused by both urate hydroperoxide and hydrogen peroxide.	urate hydroperoxide	80-99	peroxiredoxin 2	Homo sapiens	13-17
28348082-8	2017	In addition, Prx2 was more sensitive than Prx1 to hyperoxidation caused by both urate hydroperoxide and hydrogen peroxide.	Hydrogen Peroxide	104-121	peroxiredoxin 2	Homo sapiens	13-17
28348082-9	2017	Urate hydroperoxide oxidized Prx2 from intact erythrocytes to the same extent as hydrogen peroxide.	urate hydroperoxide	0-19	peroxiredoxin 2	Homo sapiens	29-33
28348082-10	2017	Therefore, Prx1 and Prx2 are likely targets of urate hydroperoxide in cells.	urate hydroperoxide	47-66	peroxiredoxin 2	Homo sapiens	20-24
28432271-6	2017	Our data also suggested that the PI3K/AKT signaling pathway links PRDX2 with 5-FU-induced apoptosis in colon cancer.	Fluorouracil	77-81	peroxiredoxin 2	Homo sapiens	66-71
28432271-11	2017	Taken together, our study suggests that decreasing the expression of PRDX2 could be a promising strategy for increasing the sensitivity of colon cancer cells to 5-FU.	Fluorouracil	161-165	peroxiredoxin 2	Homo sapiens	69-74
27821734-0	2016	Role of sulfiredoxin as a peroxiredoxin-2 denitrosylase in human iPSC-derived dopaminergic neurons.	sulfiredoxin	8-20	peroxiredoxin 2	Homo sapiens	26-41
28392212-4	2017	Peroxiredoxin-2 was also affected during storage, with a progressive accumulation of disulfide-linked dimers and hetero-protein complexes in the cytosol and also in the membrane of stored RBC.	Disulfides	85-94	peroxiredoxin 2	Homo sapiens	0-15
27864139-5	2017	Morning levels of overoxidized PRDX2 correlated with polysomnographic (PSG)-arousal index and metabolic parameters whereas the evening level of disulfide-linked dimer (associated with peroxidase activity of PRDX2) correlated with PSG parameters.	Disulfides	144-153	peroxiredoxin 2	Homo sapiens	207-212
27864139-6	2017	After treatment, morning overoxidized multimer of PRDX2 negatively correlated with fasting glucose and dopamine levels.	Glucose	91-98	peroxiredoxin 2	Homo sapiens	50-55
27864139-6	2017	After treatment, morning overoxidized multimer of PRDX2 negatively correlated with fasting glucose and dopamine levels.	Dopamine	103-111	peroxiredoxin 2	Homo sapiens	50-55
27744069-7	2017	H2O2 generated during catechol crosslinking exhibited localized cytotoxicity in culture and upregulated the expression of an antioxidant enzyme, peroxiredoxin 2, in primary dermal and tendon fibroblasts.	Hydrogen Peroxide	0-4	peroxiredoxin 2	Homo sapiens	145-160
27744069-7	2017	H2O2 generated during catechol crosslinking exhibited localized cytotoxicity in culture and upregulated the expression of an antioxidant enzyme, peroxiredoxin 2, in primary dermal and tendon fibroblasts.	catechol	22-30	peroxiredoxin 2	Homo sapiens	145-160
27894099-5	2016	We demonstrated that knockdown of Prdx2 reduced the self-renewal and sphere formation and resulted in increased 5-FU-induced apoptosis in human colon CSCs.	Fluorouracil	112-116	peroxiredoxin 2	Homo sapiens	34-39
28432271-0	2017	Knockdown of PRDX2 sensitizes colon cancer cells to 5-FU by suppressing the PI3K/AKT signaling pathway.	Fluorouracil	52-56	peroxiredoxin 2	Homo sapiens	13-18
28432271-3	2017	Peroxiredoxin-2 (PRDX2), is an important member of the ROS scavenging system, and may be a potential target that promotes chemosensitivity to 5-FU in colon cancer.	Reactive Oxygen Species	55-58	peroxiredoxin 2	Homo sapiens	0-15
28432271-3	2017	Peroxiredoxin-2 (PRDX2), is an important member of the ROS scavenging system, and may be a potential target that promotes chemosensitivity to 5-FU in colon cancer.	Reactive Oxygen Species	55-58	peroxiredoxin 2	Homo sapiens	17-22
28432271-3	2017	Peroxiredoxin-2 (PRDX2), is an important member of the ROS scavenging system, and may be a potential target that promotes chemosensitivity to 5-FU in colon cancer.	Fluorouracil	142-146	peroxiredoxin 2	Homo sapiens	0-15
28432271-3	2017	Peroxiredoxin-2 (PRDX2), is an important member of the ROS scavenging system, and may be a potential target that promotes chemosensitivity to 5-FU in colon cancer.	Fluorouracil	142-146	peroxiredoxin 2	Homo sapiens	17-22
28432271-4	2017	Here, we depleted PRDX2 by PRDX2-shRNA-LV transduction in two colon cancer cell lines and found that in vitro PRDX2 knockdown facilitates cell death, and apoptosis in 5-FU-treated colon cancer cells.	Fluorouracil	167-171	peroxiredoxin 2	Homo sapiens	18-23
28003121-0	2017	Silencing peroxiredoxin-2 sensitizes human colorectal cancer cells to ionizing radiation and oxaliplatin.	Oxaliplatin	93-104	peroxiredoxin 2	Homo sapiens	10-25
28003121-6	2017	Constitutive and transient Prx2 silencing in CRC cells increase ROS levels, and most importantly, enhance in vitro radiation sensitivity.	ros	64-67	peroxiredoxin 2	Homo sapiens	27-31
28003121-7	2017	In addition, we showed that administration of IR plus oxaliplatin in down regulated Prx2 HCT116 cells has higher citotoxic effect than in control cells.	Oxaliplatin	54-65	peroxiredoxin 2	Homo sapiens	84-88
28095627-7	2017	Concomitantly, melatonin treatment upregulated gene expression related to fatty acid beta-oxidation (CPT1a, CPT1b, CPT2, and ACADS) and mitochondrial biogenesis (PGC-1alpha, TFAM, and PRDX2).	Melatonin	15-24	peroxiredoxin 2	Homo sapiens	184-189
27677384-4	2016	Membrane binding of Prx2 in erythrocytes decreased when the cells were treated with H2O2, but studies with purified Prx2 and isolated ghosts showed that the interaction was independent of Prx2 redox state.	Hydrogen Peroxide	84-88	peroxiredoxin 2	Homo sapiens	20-24
27677384-7	2016	The increased membrane binding of Prx2 seen with increasing intracellular calcium was less sensitive to H2O2 or hemichrome, suggesting an alternative mode of binding.	Calcium	74-81	peroxiredoxin 2	Homo sapiens	34-38
27677384-7	2016	The increased membrane binding of Prx2 seen with increasing intracellular calcium was less sensitive to H2O2 or hemichrome, suggesting an alternative mode of binding.	Hydrogen Peroxide	104-108	peroxiredoxin 2	Homo sapiens	34-38
27821734-3	2016	Here, using in vitro and in vivo approaches, we identify a role and reaction mechanism of the reductase sulfiredoxin (Srxn1) as an enzyme that denitrosylates (thus removing -SNO) from Prx2 in an ATP-dependent manner.	Adenosine Triphosphate	195-198	peroxiredoxin 2	Homo sapiens	184-188
26497580-4	2016	Torin, an ATP-competitive mTOR inhibitor, was found to have both cytotoxic and cytostatic effects on U-937, THP-1, and RPMI-8226 cells, but not on Jurkat or K-562 cells.	Adenosine Triphosphate	10-13	peroxiredoxin 2	Homo sapiens	0-5
27350002-5	2016	It also caused some unique oxidative shifts, including for peroxiredoxin 2 (PRDX2), uroporphyrinogen decarboxylase (UROD), and thioredoxin (TXN), proteins reportedly affected by cellular reactive oxygen species production.	Reactive Oxygen Species	187-210	peroxiredoxin 2	Homo sapiens	59-74
27350002-7	2016	Moreover, with H2O2, significant oxidative shifts were observed only in redox active proteins, like PRDX2, peroxiredoxin 1 (PRDX1), TXN, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH).	Hydrogen Peroxide	15-19	peroxiredoxin 2	Homo sapiens	100-105
27082744-0	2016	Role of peroxiredoxin 2 in H2O2-induced oxidative stress of primary Leydig cells.	Hydrogen Peroxide	27-31	peroxiredoxin 2	Homo sapiens	8-23
27082744-3	2016	Peroxiredoxin 2 (Prdx2), a member of the peroxiredoxin family, is an antioxidant protein, the predominant function of which is to neutralize ROS.	Reactive Oxygen Species	141-144	peroxiredoxin 2	Homo sapiens	0-15
27082744-3	2016	Peroxiredoxin 2 (Prdx2), a member of the peroxiredoxin family, is an antioxidant protein, the predominant function of which is to neutralize ROS.	Reactive Oxygen Species	141-144	peroxiredoxin 2	Homo sapiens	17-22
27082744-3	2016	Peroxiredoxin 2 (Prdx2), a member of the peroxiredoxin family, is an antioxidant protein, the predominant function of which is to neutralize ROS.	Reactive Oxygen Species	141-144	peroxiredoxin 2	Homo sapiens	41-54
27082744-9	2016	In addition, the expression of Prdx2 was decreased by H2O2 in a dose- and time-dependent manner, and this decrease may have been caused by the induction of its molecular structure transformation due to H2O2 elimination.	Hydrogen Peroxide	54-58	peroxiredoxin 2	Homo sapiens	31-36
27082744-9	2016	In addition, the expression of Prdx2 was decreased by H2O2 in a dose- and time-dependent manner, and this decrease may have been caused by the induction of its molecular structure transformation due to H2O2 elimination.	Hydrogen Peroxide	202-206	peroxiredoxin 2	Homo sapiens	31-36
27082744-10	2016	The above findings indicated that Prdx2 may prevent H2O2 accumulation in Leydig cells, and may be important in oxidative stress-induced apoptosis and decreased testosterone production.	Hydrogen Peroxide	52-56	peroxiredoxin 2	Homo sapiens	34-39
27082744-10	2016	The above findings indicated that Prdx2 may prevent H2O2 accumulation in Leydig cells, and may be important in oxidative stress-induced apoptosis and decreased testosterone production.	Testosterone	160-172	peroxiredoxin 2	Homo sapiens	34-39
26945066-0	2016	Oxidant-induced Interprotein Disulfide Formation in Cardiac Protein DJ-1 Occurs via an Interaction with Peroxiredoxin 2.	Disulfides	29-38	peroxiredoxin 2	Homo sapiens	104-119
27266564-9	2016	SM-exposed individuals demonstrated expression of PRDX3 4.6231 (p = 0.000134), PRDX6 3.4964 (p = 0.001102), SRXN1 3.3719 (p &lt; 0.0001) and PRDX2 2.7725-folds (p = 0.000383) higher than those of controls that reveal.	Mustard Gas	0-2	peroxiredoxin 2	Homo sapiens	141-146
26585682-12	2016	CONCLUSIONS: This study shows that supplementation of TAT-peroxiredoxin 2 fusion protein in the sperm suspension from asthenozoospermic men effectively improved sperm motility and DNA integrity by reducing levels of reactive oxygen species.	Reactive Oxygen Species	216-239	peroxiredoxin 2	Homo sapiens	58-73
27602166-5	2016	Because the role of PRDX2 in HCC has not yet been reported, it is of interest to explore how PRDX2 may affect reactive oxygen species (ROS)-mediated cell death in HCC cells.	Reactive Oxygen Species	110-133	peroxiredoxin 2	Homo sapiens	93-98
27602166-5	2016	Because the role of PRDX2 in HCC has not yet been reported, it is of interest to explore how PRDX2 may affect reactive oxygen species (ROS)-mediated cell death in HCC cells.	Reactive Oxygen Species	135-138	peroxiredoxin 2	Homo sapiens	93-98
27602166-6	2016	The present study analyzed the effects of PRDX2 knockdown or overexpression on hydrogen peroxide (H2O2)-induced cell death in HCC SMMC-7721 cells.	Hydrogen Peroxide	79-96	peroxiredoxin 2	Homo sapiens	42-47
27602166-6	2016	The present study analyzed the effects of PRDX2 knockdown or overexpression on hydrogen peroxide (H2O2)-induced cell death in HCC SMMC-7721 cells.	Hydrogen Peroxide	98-102	peroxiredoxin 2	Homo sapiens	42-47
27602166-8	2016	It was found that PRDX2 knockdown augmented H2O2-induced cell death in SMMC-7721 cells, whereas PRDX2 overexpression exhibited opposite effects.	Hydrogen Peroxide	44-48	peroxiredoxin 2	Homo sapiens	18-23
27602166-8	2016	It was found that PRDX2 knockdown augmented H2O2-induced cell death in SMMC-7721 cells, whereas PRDX2 overexpression exhibited opposite effects.	smmc	71-75	peroxiredoxin 2	Homo sapiens	18-23
27602166-10	2016	Further exploration confirmed PRDX2 knockdown led to enhanced ROS generation in response to H2O2.	Reactive Oxygen Species	62-65	peroxiredoxin 2	Homo sapiens	30-35
27602166-10	2016	Further exploration confirmed PRDX2 knockdown led to enhanced ROS generation in response to H2O2.	Hydrogen Peroxide	92-96	peroxiredoxin 2	Homo sapiens	30-35
27602166-11	2016	Taken together, the present study supports that PRDX2 serves a pro-tumorigenic role in HCC through, at least partially, limiting ROS-mediated apoptosis under oxidative stress.	Reactive Oxygen Species	129-132	peroxiredoxin 2	Homo sapiens	48-53
26905788-7	2016	Measuring peroxiredoxin-2 (Prx-2) oxidation as evidence of increased H2O2, only piperlongumine treatment shows elevation and it is GSH independent.	Hydrogen Peroxide	69-73	peroxiredoxin 2	Homo sapiens	10-25
26905788-7	2016	Measuring peroxiredoxin-2 (Prx-2) oxidation as evidence of increased H2O2, only piperlongumine treatment shows elevation and it is GSH independent.	Hydrogen Peroxide	69-73	peroxiredoxin 2	Homo sapiens	27-32
26866938-5	2016	Downregulation of Prx II in Huh7 cells with treatment of siRNA reduced expression of EpCAM and CD133 as well as Sox2 in accordance with increased ROS and apoptosis, which were reversed in Huh7-hPrx II cells.	ros	146-149	peroxiredoxin 2	Homo sapiens	18-24
27052304-2	2016	METHODS: In this study, a cellular OA model was generated by stimulating SW1353 cells with IL-1beta and a rabbit OA model was established by intra-articular injection of collagenase, followed by treatment with Torin 1 or 3-Methyladenine (3-MA).	3-methyladenine	221-236	peroxiredoxin 2	Homo sapiens	210-215
27052304-2	2016	METHODS: In this study, a cellular OA model was generated by stimulating SW1353 cells with IL-1beta and a rabbit OA model was established by intra-articular injection of collagenase, followed by treatment with Torin 1 or 3-Methyladenine (3-MA).	3-methyladenine	238-242	peroxiredoxin 2	Homo sapiens	210-215
26614766-1	2016	Mammalian 2-cysteine peroxiredoxins (Prxs) are susceptible to hyperoxidation by excess H2O2.	Hydrogen Peroxide	87-91	peroxiredoxin 2	Homo sapiens	21-35
26614766-2	2016	The cytoplasmic family member Prx2 hyperoxidizes more readily than mitochondrial Prx3 due to slower dimerization of the sulfenic acid (SpOH) intermediate.	Sulfenic Acids	120-133	peroxiredoxin 2	Homo sapiens	30-34
26614766-2	2016	The cytoplasmic family member Prx2 hyperoxidizes more readily than mitochondrial Prx3 due to slower dimerization of the sulfenic acid (SpOH) intermediate.	spoh	135-139	peroxiredoxin 2	Homo sapiens	30-34
26614766-8	2016	For Prx2, increasing the H2O2 concentration resulted in complete hyperoxidation.	Hydrogen Peroxide	25-29	peroxiredoxin 2	Homo sapiens	4-8
26614766-11	2016	Notably the species with one disulfide and one hyperoxidized active site was decameric for Prx2 and dimeric for Prx3.	Disulfides	29-38	peroxiredoxin 2	Homo sapiens	91-95
26612102-0	2016	Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form.	Peroxynitrous Acid	24-37	peroxiredoxin 2	Homo sapiens	60-75
26612102-0	2016	Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form.	Peroxynitrous Acid	24-37	peroxiredoxin 2	Homo sapiens	86-90
26612102-0	2016	Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form.	Disulfides	105-114	peroxiredoxin 2	Homo sapiens	60-75
26612102-0	2016	Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form.	Disulfides	105-114	peroxiredoxin 2	Homo sapiens	86-90
26612102-1	2016	Peroxiredoxins are cys-based peroxidases that function in peroxide detoxification and H2O2-induced signaling.	Cysteine	19-22	peroxiredoxin 2	Homo sapiens	0-14
26612102-1	2016	Peroxiredoxins are cys-based peroxidases that function in peroxide detoxification and H2O2-induced signaling.	Peroxides	58-66	peroxiredoxin 2	Homo sapiens	0-14
26612102-1	2016	Peroxiredoxins are cys-based peroxidases that function in peroxide detoxification and H2O2-induced signaling.	Hydrogen Peroxide	86-90	peroxiredoxin 2	Homo sapiens	0-14
26612102-2	2016	Human Prx2 is a typical 2-Cys Prx arranged as pentamers of head-to-tail homodimers.	2-cys	24-29	peroxiredoxin 2	Homo sapiens	6-10
26612102-5	2016	We have recently reported that nitration of Prx2, a post-translational modification on non-catalytic tyrosines, unexpectedly increases its peroxidase activity and resistance to overoxidation.	Tyrosine	101-110	peroxiredoxin 2	Homo sapiens	44-48
26612102-8	2016	Our results show that the reduced nitrated Prx2 structurally resembles the disulfide-oxidized native form of the enzyme favoring a locally unfolded conformation that facilitates disulfide formation.	Disulfides	75-84	peroxiredoxin 2	Homo sapiens	43-47
26612102-8	2016	Our results show that the reduced nitrated Prx2 structurally resembles the disulfide-oxidized native form of the enzyme favoring a locally unfolded conformation that facilitates disulfide formation.	Disulfides	178-187	peroxiredoxin 2	Homo sapiens	43-47
25808059-3	2015	Our previous work revealed that, although PRDX-2 protects against the toxicity of peroxides, enigmatically, prdx-2-mutant animals are hyper-resistant to other forms of oxidative stress.	Peroxides	82-91	peroxiredoxin 2	Homo sapiens	42-48
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	citrate/isocitrate	177-195	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	malic acid	201-207	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	NAD	221-254	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	NAD	256-260	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	Flavin-Adenine Dinucleotide	266-293	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	Flavin-Adenine Dinucleotide	295-298	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	Adenosine Triphosphate	305-308	peroxiredoxin 2	Homo sapiens	12-17
28217402-13	2016	When HPAF-II cells were incubated with both Torin-2 and metformin, there was a significant reduction in NAD+ and FAD, suggesting decreased levels of the energy equivalents that are available to the electron transport chain.	NAD	104-108	peroxiredoxin 2	Homo sapiens	44-49
28217402-13	2016	When HPAF-II cells were incubated with both Torin-2 and metformin, there was a significant reduction in NAD+ and FAD, suggesting decreased levels of the energy equivalents that are available to the electron transport chain.	Flavin-Adenine Dinucleotide	113-116	peroxiredoxin 2	Homo sapiens	44-49
28217402-14	2016	Targeted metabolomics data indicate that mTOR complexes inhibition by Torin 2 reduced glycolytic intermediates and TCA metabolites in HPAF- II and may synergize with metformin to decrease the electron acceptors NAD+ and FAD which may lead to reduced energy production.	Trichloroacetic Acid	115-118	peroxiredoxin 2	Homo sapiens	70-75
28217402-14	2016	Targeted metabolomics data indicate that mTOR complexes inhibition by Torin 2 reduced glycolytic intermediates and TCA metabolites in HPAF- II and may synergize with metformin to decrease the electron acceptors NAD+ and FAD which may lead to reduced energy production.	Metformin	166-175	peroxiredoxin 2	Homo sapiens	70-75
28217402-14	2016	Targeted metabolomics data indicate that mTOR complexes inhibition by Torin 2 reduced glycolytic intermediates and TCA metabolites in HPAF- II and may synergize with metformin to decrease the electron acceptors NAD+ and FAD which may lead to reduced energy production.	NAD	211-215	peroxiredoxin 2	Homo sapiens	70-75
28217402-14	2016	Targeted metabolomics data indicate that mTOR complexes inhibition by Torin 2 reduced glycolytic intermediates and TCA metabolites in HPAF- II and may synergize with metformin to decrease the electron acceptors NAD+ and FAD which may lead to reduced energy production.	Flavin-Adenine Dinucleotide	220-223	peroxiredoxin 2	Homo sapiens	70-75
26232623-8	2015	Edaravone seems to reverse the H2O2-mediated effects at both the cellular and protein level via induction of Peroxiredoxin-2.	Edaravone	0-9	peroxiredoxin 2	Homo sapiens	109-124
26232623-8	2015	Edaravone seems to reverse the H2O2-mediated effects at both the cellular and protein level via induction of Peroxiredoxin-2.	Hydrogen Peroxide	31-35	peroxiredoxin 2	Homo sapiens	109-124
28217402-7	2016	The objective of this study is to determine the targeted-metabolomics profile in PDAC cell line (HPAF-II) with mTOR inhibition and the interaction between mTOR ATP-competitive inhibitor (Torin 2) and metformin as potential combined therapy in PC.	Adenosine Triphosphate	160-163	peroxiredoxin 2	Homo sapiens	187-192
28217402-7	2016	The objective of this study is to determine the targeted-metabolomics profile in PDAC cell line (HPAF-II) with mTOR inhibition and the interaction between mTOR ATP-competitive inhibitor (Torin 2) and metformin as potential combined therapy in PC.	Metformin	200-209	peroxiredoxin 2	Homo sapiens	187-192
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	2-phosphoglycerate	107-125	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	3-phosphoglycerate	126-144	peroxiredoxin 2	Homo sapiens	12-17
28217402-12	2016	After 24 h, Torin-2 significantly decreased glycolysis intermediates (fructose 1,6-bisphosphate (FBP), and 2-phosphoglycerate/3-phosphoglycerate), TCA intermediate metabolites (citrate/isocitrate, and malate), as well as Nicotinamide Adenine Dinucleotide (NAD+) and Flavin Adenine Dinucleotide (FAD), and ATP levels.	Trichloroacetic Acid	147-150	peroxiredoxin 2	Homo sapiens	12-17
29227081-3	2016	In thisstudy, we attempted to evaluate a possible association between ubiquitous Prx II and ATP/ADP bufferingenzyme - brain-type creatine kinase (CK BB).	Adenosine Triphosphate	92-95	peroxiredoxin 2	Homo sapiens	81-87
29227081-3	2016	In thisstudy, we attempted to evaluate a possible association between ubiquitous Prx II and ATP/ADP bufferingenzyme - brain-type creatine kinase (CK BB).	Adenosine Diphosphate	96-99	peroxiredoxin 2	Homo sapiens	81-87
29227081-4	2016	Our co-immunoprecipitation (Co-IP) results from the A549and HeLa cell lysates with overexpressed HA-Prx II and Flag-CK BB have demonstrated strong associationbetween two proteins under non-stressed conditions.	veratric acid	166-169	peroxiredoxin 2	Homo sapiens	100-106
26202471-10	2015	RBCs that oxidized nitrite faster on Day 7 were associated with the greatest levels of storage-dependent hemolysis and increases in Prx-2 oxidation.	Nitrites	19-26	peroxiredoxin 2	Homo sapiens	132-137
25808059-8	2015	Intriguingly, loss of PRDX-2 increases DAF-16 and SKN-1 activities sufficiently to increase arsenite resistance without initiating other IIS-inhibited processes.	arsenite	92-100	peroxiredoxin 2	Homo sapiens	22-28
26023849-9	2015	Furthermore, treatment of EOC cells with a subtoxic dose of Torin2 potentiated a cisplatin-induced apoptotic response in EOC cell lines.	Cisplatin	81-90	peroxiredoxin 2	Homo sapiens	60-65
26113455-6	2015	SDS-PAGE and mass spectrometric analysis showed that the proteins comprising the peak were almost exclusively Prx2.	Sodium Dodecyl Sulfate	0-3	peroxiredoxin 2	Homo sapiens	110-114
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Sulfhydryl Compounds	16-21	peroxiredoxin 2	Homo sapiens	30-45
26021759-3	2015	Prx II was remarkably increased only in A549/GR (gefitinib-resistant) cells compared with A549 cells, consistent with methylation/demethylation.	Gefitinib	49-58	peroxiredoxin 2	Homo sapiens	0-6
26021759-6	2015	When Prx II mRNA in the A549/GR cells was knocked down, the levels of ROS and apoptosis were significantly recovered to the levels of the controls.	Reactive Oxygen Species	70-73	peroxiredoxin 2	Homo sapiens	5-11
26021759-10	2015	Our findings suggest that Prx II has an important role in cancer cell survival via the modulation of signaling molecules involved in apoptosis and the phosphorylation of JNK by the downregulation of ROS levels in A549/GR cells.	Reactive Oxygen Species	199-202	peroxiredoxin 2	Homo sapiens	26-32
26028291-5	2015	PRDX2 overexpressing cells were protected from H2O2-induced oxidative stress.	Hydrogen Peroxide	47-51	peroxiredoxin 2	Homo sapiens	0-5
26028291-6	2015	The amplitude of the Bmal1 promoter activity was significantly dampened in PRDX2-MycNuc versus EV cells when synchronized either by dexamethasone treatment or temperature cycles.	Dexamethasone	132-145	peroxiredoxin 2	Homo sapiens	75-80
26028291-9	2015	Noteworthy, H2O2 treatment rescued proper oscillation of the clock in synchronized PRDX2-MycNuc HaCaT cells.	Hydrogen Peroxide	12-16	peroxiredoxin 2	Homo sapiens	83-88
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Sulfhydryl Compounds	16-21	peroxiredoxin 2	Homo sapiens	47-51
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Hydrogen Peroxide	114-128	peroxiredoxin 2	Homo sapiens	30-45
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Hydrogen Peroxide	114-128	peroxiredoxin 2	Homo sapiens	47-51
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Disulfides	176-185	peroxiredoxin 2	Homo sapiens	30-45
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Disulfides	176-185	peroxiredoxin 2	Homo sapiens	47-51
25720945-8	2015	Additional, Prx2 oxidation occurred when hydrogen peroxide was added.	Hydrogen Peroxide	41-58	peroxiredoxin 2	Homo sapiens	12-16
25264713-9	2015	Specifically, Prx-2 recycling was blunted in beta93Ala RBC, which was reversed by carbon monoxide-treatment, suggesting that heme autoxidation-derived H2O2 maintains Prx-2 in the oxidized form in these cells.	Carbon Monoxide	82-97	peroxiredoxin 2	Homo sapiens	14-19
25742636-7	2015	PRDX2 and -6 levels were negatively correlated with diastolic blood pressure, fasting blood sugar, and hemoglobin A1c.	Sugars	92-97	peroxiredoxin 2	Homo sapiens	0-5
25264713-2	2015	Peroxiredoxin-2 (Prx-2) is a primary RBC antioxidant that limits hydrogen peroxide (H2O2)-mediated toxicity.	Hydrogen Peroxide	65-82	peroxiredoxin 2	Homo sapiens	0-15
25264713-9	2015	Specifically, Prx-2 recycling was blunted in beta93Ala RBC, which was reversed by carbon monoxide-treatment, suggesting that heme autoxidation-derived H2O2 maintains Prx-2 in the oxidized form in these cells.	Carbon Monoxide	82-97	peroxiredoxin 2	Homo sapiens	166-171
25264713-2	2015	Peroxiredoxin-2 (Prx-2) is a primary RBC antioxidant that limits hydrogen peroxide (H2O2)-mediated toxicity.	Hydrogen Peroxide	65-82	peroxiredoxin 2	Homo sapiens	17-22
25264713-9	2015	Specifically, Prx-2 recycling was blunted in beta93Ala RBC, which was reversed by carbon monoxide-treatment, suggesting that heme autoxidation-derived H2O2 maintains Prx-2 in the oxidized form in these cells.	Hydrogen Peroxide	151-155	peroxiredoxin 2	Homo sapiens	14-19
25264713-2	2015	Peroxiredoxin-2 (Prx-2) is a primary RBC antioxidant that limits hydrogen peroxide (H2O2)-mediated toxicity.	Hydrogen Peroxide	84-88	peroxiredoxin 2	Homo sapiens	0-15
25264713-9	2015	Specifically, Prx-2 recycling was blunted in beta93Ala RBC, which was reversed by carbon monoxide-treatment, suggesting that heme autoxidation-derived H2O2 maintains Prx-2 in the oxidized form in these cells.	Hydrogen Peroxide	151-155	peroxiredoxin 2	Homo sapiens	166-171
25264713-2	2015	Peroxiredoxin-2 (Prx-2) is a primary RBC antioxidant that limits hydrogen peroxide (H2O2)-mediated toxicity.	Hydrogen Peroxide	84-88	peroxiredoxin 2	Homo sapiens	17-22
25264713-4	2015	RESULTS: Basal and H2O2-induced Prx-2 activity was measured in RBCs (stored for 7-35 days).	Hydrogen Peroxide	19-23	peroxiredoxin 2	Homo sapiens	32-37
25264713-11	2015	INNOVATION: A novel mechanism for regulated Prx-2 activity in RBC via the beta93Cys residue is suggested.	beta93cys	74-83	peroxiredoxin 2	Homo sapiens	44-49
25264713-5	2015	Basal Prx-2 thiol oxidation increased with RBC age, whereas H2O2-dependent formation of dimeric Prx-2 was similar.	Sulfhydryl Compounds	12-17	peroxiredoxin 2	Homo sapiens	6-11
25264713-5	2015	Basal Prx-2 thiol oxidation increased with RBC age, whereas H2O2-dependent formation of dimeric Prx-2 was similar.	Hydrogen Peroxide	60-64	peroxiredoxin 2	Homo sapiens	96-101
25264713-6	2015	However, reduction of Prx-2 dimers to monomers became progressively slower with RBC storage, which was associated with increased H2O2-induced hemolysis.	Hydrogen Peroxide	129-133	peroxiredoxin 2	Homo sapiens	22-27
25471788-1	2015	The mammalian peroxiredoxin 2 (Prdx2) is a member of thiol-dependent antioxidant proteins and plays an important role in the progression of colorectal cancer (CRC).	Sulfhydryl Compounds	53-58	peroxiredoxin 2	Homo sapiens	14-29
25786472-0	2015	Peroxiredoxin 2, glutathione peroxidase, and catalase in the cytosol and membrane of erythrocytes under H2O2-induced oxidative stress.	Hydrogen Peroxide	104-108	peroxiredoxin 2	Homo sapiens	0-15
25786472-3	2015	Our aim was to contribute to a better understanding of the interplay between Prx2, Cat, and GPx under H2O2-induced oxidative stress, by studying their changes in the red blood cell cytosol and membrane, in different conditions.	Hydrogen Peroxide	102-106	peroxiredoxin 2	Homo sapiens	77-81
25786472-7	2015	We showed that under increasing H2O2 concentrations, inhibition of the three enzymes with or without metHb formation lead to the binding of Prx2 and GPx (but not Cat) to the erythrocyte membrane.	Hydrogen Peroxide	32-36	peroxiredoxin 2	Homo sapiens	140-144
25471788-1	2015	The mammalian peroxiredoxin 2 (Prdx2) is a member of thiol-dependent antioxidant proteins and plays an important role in the progression of colorectal cancer (CRC).	Sulfhydryl Compounds	53-58	peroxiredoxin 2	Homo sapiens	31-36
25296981-2	2014	Torin-2 is a novel, second-generation ATP-competitive inhibitor that is potent and selective for mTOR with a superior pharmacokinetic profile to previous inhibitors.	Adenosine Triphosphate	38-41	peroxiredoxin 2	Homo sapiens	0-5
25402766-0	2015	Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling.	Hydrogen Peroxide	49-53	peroxiredoxin 2	Homo sapiens	0-15
25289458-6	2014	We confirmed that adenanthin underwent Michael addition to isolated Prx2, thereby inhibiting oxidation to a disulfide-linked dimer.	adenanthin	18-28	peroxiredoxin 2	Homo sapiens	68-72
25289458-6	2014	We confirmed that adenanthin underwent Michael addition to isolated Prx2, thereby inhibiting oxidation to a disulfide-linked dimer.	Disulfides	108-117	peroxiredoxin 2	Homo sapiens	68-72
25289458-9	2014	With 50 microM adenanthin, the peroxidatic and resolving Cys of Prx2 reacted with half-times of 7 and 40 min, respectively, compared with 10 min for GSH.	adenanthin	15-25	peroxiredoxin 2	Homo sapiens	64-68
25289458-9	2014	With 50 microM adenanthin, the peroxidatic and resolving Cys of Prx2 reacted with half-times of 7 and 40 min, respectively, compared with 10 min for GSH.	Cysteine	57-60	peroxiredoxin 2	Homo sapiens	64-68
25289458-9	2014	With 50 microM adenanthin, the peroxidatic and resolving Cys of Prx2 reacted with half-times of 7 and 40 min, respectively, compared with 10 min for GSH.	Glutathione	149-152	peroxiredoxin 2	Homo sapiens	64-68
25068294-8	2014	Antioxidant proteins including heme oxygenase-1 and peroxiredoxin-2 levels were also increased in retinal AC under high glucose conditions through nuclear localization of transcription factor nuclear factor-erythroid 2-related factor-2.	Glucose	120-127	peroxiredoxin 2	Homo sapiens	52-67
25379381-0	2014	Irreversible hyperoxidation of peroxiredoxin 2 is caused by tert-butyl hydroperoxide in human red blood cells.	tert-Butylhydroperoxide	60-84	peroxiredoxin 2	Homo sapiens	31-46
25379381-3	2014	The detection of a peak corresponding to Prx2-SO2/3 was clearly observed following treatment of tert-butyl hydroperoxide (t-BHP), but not H2O2, and was found to be dose-dependent.	tert-Butylhydroperoxide	96-120	peroxiredoxin 2	Homo sapiens	41-45
25379381-3	2014	The detection of a peak corresponding to Prx2-SO2/3 was clearly observed following treatment of tert-butyl hydroperoxide (t-BHP), but not H2O2, and was found to be dose-dependent.	tert-Butylhydroperoxide	122-127	peroxiredoxin 2	Homo sapiens	41-45
25379381-3	2014	The detection of a peak corresponding to Prx2-SO2/3 was clearly observed following treatment of tert-butyl hydroperoxide (t-BHP), but not H2O2, and was found to be dose-dependent.	Hydrogen Peroxide	138-142	peroxiredoxin 2	Homo sapiens	41-45
25379381-5	2014	Our results suggest that t-BHP hyperoxidizes cysteine residues in Prx2 more readily than H2O2, and that accumulation of hyperoxidized Prx2 might reflect disruption of redox homeostasis in RBCs.	Cysteine	45-53	peroxiredoxin 2	Homo sapiens	66-70
26461315-6	2014	The significance of Prx2 inhibition was assessed by comparing the behavior of this model with that of an otherwise identical model lacking inhibition.Our analysis shows that Prx2 inhibition leads to 25-40% lower NADPH consumption under low to moderately high H2O2 supply (&lt;0.8microM H2O2/s).	NADP	212-217	peroxiredoxin 2	Homo sapiens	20-24
26461315-6	2014	The significance of Prx2 inhibition was assessed by comparing the behavior of this model with that of an otherwise identical model lacking inhibition.Our analysis shows that Prx2 inhibition leads to 25-40% lower NADPH consumption under low to moderately high H2O2 supply (&lt;0.8microM H2O2/s).	NADP	212-217	peroxiredoxin 2	Homo sapiens	174-178
26461315-6	2014	The significance of Prx2 inhibition was assessed by comparing the behavior of this model with that of an otherwise identical model lacking inhibition.Our analysis shows that Prx2 inhibition leads to 25-40% lower NADPH consumption under low to moderately high H2O2 supply (&lt;0.8microM H2O2/s).	Hydrogen Peroxide	259-263	peroxiredoxin 2	Homo sapiens	20-24
26461315-6	2014	The significance of Prx2 inhibition was assessed by comparing the behavior of this model with that of an otherwise identical model lacking inhibition.Our analysis shows that Prx2 inhibition leads to 25-40% lower NADPH consumption under low to moderately high H2O2 supply (&lt;0.8microM H2O2/s).	Hydrogen Peroxide	259-263	peroxiredoxin 2	Homo sapiens	174-178
26461315-6	2014	The significance of Prx2 inhibition was assessed by comparing the behavior of this model with that of an otherwise identical model lacking inhibition.Our analysis shows that Prx2 inhibition leads to 25-40% lower NADPH consumption under low to moderately high H2O2 supply (&lt;0.8microM H2O2/s).	Hydrogen Peroxide	286-290	peroxiredoxin 2	Homo sapiens	20-24
26461315-6	2014	The significance of Prx2 inhibition was assessed by comparing the behavior of this model with that of an otherwise identical model lacking inhibition.Our analysis shows that Prx2 inhibition leads to 25-40% lower NADPH consumption under low to moderately high H2O2 supply (&lt;0.8microM H2O2/s).	Hydrogen Peroxide	286-290	peroxiredoxin 2	Homo sapiens	174-178
26461315-7	2014	Further, the inhibition extends the range where the concentrations of potential redox signaling readouts - H2O2, Prx2 sulfenic acid, Prx2 disulfide and Trx disulfide- show a proportional response to changes in H2O2 supply, covering practically the whole physiological range of the latter.	Sulfenic Acids	118-131	peroxiredoxin 2	Homo sapiens	113-117
26461315-7	2014	Further, the inhibition extends the range where the concentrations of potential redox signaling readouts - H2O2, Prx2 sulfenic acid, Prx2 disulfide and Trx disulfide- show a proportional response to changes in H2O2 supply, covering practically the whole physiological range of the latter.	Disulfides	138-147	peroxiredoxin 2	Homo sapiens	133-137
26461315-7	2014	Further, the inhibition extends the range where the concentrations of potential redox signaling readouts - H2O2, Prx2 sulfenic acid, Prx2 disulfide and Trx disulfide- show a proportional response to changes in H2O2 supply, covering practically the whole physiological range of the latter.	Hydrogen Peroxide	210-214	peroxiredoxin 2	Homo sapiens	113-117
26461315-7	2014	Further, the inhibition extends the range where the concentrations of potential redox signaling readouts - H2O2, Prx2 sulfenic acid, Prx2 disulfide and Trx disulfide- show a proportional response to changes in H2O2 supply, covering practically the whole physiological range of the latter.	Hydrogen Peroxide	210-214	peroxiredoxin 2	Homo sapiens	133-137
26461315-8	2014	This is desirable for analogic signal transduction and allows the Prx2/Trx/TrxR system to reliably transduce changes in H2O2 supply as changes in thiol oxidation.	Hydrogen Peroxide	120-124	peroxiredoxin 2	Homo sapiens	66-70
26461315-8	2014	This is desirable for analogic signal transduction and allows the Prx2/Trx/TrxR system to reliably transduce changes in H2O2 supply as changes in thiol oxidation.	Sulfhydryl Compounds	146-151	peroxiredoxin 2	Homo sapiens	66-70
26461315-9	2014	Finally, the inhibition allows other less abundant peroxiredoxins in the erythrocyte to be oxidized by H2O2 at physiological H2O2 supplies.Altogether, these results suggest that the postulated reversible inhibition of Prx2"s peroxidase facilitates signal transduction by the peroxiredoxins and spares NADPH.We acknowledge: fellowship SFRH/BD/51199/2010, grants PEst-C/SAU/LA0001/2013-2014, PEst-OE/QUI/UI0612/2013, PEst-OE/QUI/UI0313/2014, and FCOMP-01-0124-FEDER-020978 co-financed by FEDER through the COMPETE program and by FCT (project PTDC/QUI-BIQ/119657/2010).	Hydrogen Peroxide	103-107	peroxiredoxin 2	Homo sapiens	218-222
26461315-9	2014	Finally, the inhibition allows other less abundant peroxiredoxins in the erythrocyte to be oxidized by H2O2 at physiological H2O2 supplies.Altogether, these results suggest that the postulated reversible inhibition of Prx2"s peroxidase facilitates signal transduction by the peroxiredoxins and spares NADPH.We acknowledge: fellowship SFRH/BD/51199/2010, grants PEst-C/SAU/LA0001/2013-2014, PEst-OE/QUI/UI0612/2013, PEst-OE/QUI/UI0313/2014, and FCOMP-01-0124-FEDER-020978 co-financed by FEDER through the COMPETE program and by FCT (project PTDC/QUI-BIQ/119657/2010).	Hydrogen Peroxide	125-129	peroxiredoxin 2	Homo sapiens	218-222
24952139-4	2014	The high rate constant (10(7)-10(8) M(-1) s(-1)) for H2O2 reduction determined for purified peroxiredoxin II (Prx2) and the high abundance of this protein indicate that under physiological conditions it consumes practically all the H2O2.	Hydrogen Peroxide	53-57	peroxiredoxin 2	Homo sapiens	110-114
24952139-4	2014	The high rate constant (10(7)-10(8) M(-1) s(-1)) for H2O2 reduction determined for purified peroxiredoxin II (Prx2) and the high abundance of this protein indicate that under physiological conditions it consumes practically all the H2O2.	Hydrogen Peroxide	232-236	peroxiredoxin 2	Homo sapiens	110-114
24952139-5	2014	However, this is inconsistent with extensive evidence that Prx2"s contribution to H2O2 elimination is comparable to that of catalase.	Hydrogen Peroxide	82-86	peroxiredoxin 2	Homo sapiens	59-63
24952139-8	2014	Simulations of the responses to physiological H2O2 stimuli highlight that a design combining abundant Prx2 with a low effective peroxidase activity spares NADPH while improving potential signaling properties of the Prx2/thioredoxin/thioredoxin reductase system.	Hydrogen Peroxide	46-50	peroxiredoxin 2	Homo sapiens	102-106
24952139-8	2014	Simulations of the responses to physiological H2O2 stimuli highlight that a design combining abundant Prx2 with a low effective peroxidase activity spares NADPH while improving potential signaling properties of the Prx2/thioredoxin/thioredoxin reductase system.	Hydrogen Peroxide	46-50	peroxiredoxin 2	Homo sapiens	215-219
25097261-4	2014	The oxidative coupling of glutathione (GSH) to PRDX2 cysteine residues (i.e., protein glutathionylation) occurs before or during PRDX2 release, a process central to the regulation of immunity.	Glutathione	26-37	peroxiredoxin 2	Homo sapiens	47-52
25097261-4	2014	The oxidative coupling of glutathione (GSH) to PRDX2 cysteine residues (i.e., protein glutathionylation) occurs before or during PRDX2 release, a process central to the regulation of immunity.	Glutathione	26-37	peroxiredoxin 2	Homo sapiens	129-134
25097261-4	2014	The oxidative coupling of glutathione (GSH) to PRDX2 cysteine residues (i.e., protein glutathionylation) occurs before or during PRDX2 release, a process central to the regulation of immunity.	Glutathione	39-42	peroxiredoxin 2	Homo sapiens	47-52
25097261-4	2014	The oxidative coupling of glutathione (GSH) to PRDX2 cysteine residues (i.e., protein glutathionylation) occurs before or during PRDX2 release, a process central to the regulation of immunity.	Glutathione	39-42	peroxiredoxin 2	Homo sapiens	129-134
25097261-4	2014	The oxidative coupling of glutathione (GSH) to PRDX2 cysteine residues (i.e., protein glutathionylation) occurs before or during PRDX2 release, a process central to the regulation of immunity.	Cysteine	53-61	peroxiredoxin 2	Homo sapiens	47-52
24814289-7	2014	Furthermore, PRDX2 knockdown increased intracellular levels of reactive oxygen species (ROS) and impaired cell cycle progression and proliferation.	Reactive Oxygen Species	63-86	peroxiredoxin 2	Homo sapiens	13-18
24814289-7	2014	Furthermore, PRDX2 knockdown increased intracellular levels of reactive oxygen species (ROS) and impaired cell cycle progression and proliferation.	Reactive Oxygen Species	88-91	peroxiredoxin 2	Homo sapiens	13-18
26461310-1	2014	H2O2 elimination in human erythrocytes is mainly carried out by catalase (Cat), glutathione peroxidase (GPx1) and the more recently discovered peroxiredoxin 2 (Prx2).	Hydrogen Peroxide	0-4	peroxiredoxin 2	Homo sapiens	143-158
26461310-1	2014	H2O2 elimination in human erythrocytes is mainly carried out by catalase (Cat), glutathione peroxidase (GPx1) and the more recently discovered peroxiredoxin 2 (Prx2).	Hydrogen Peroxide	0-4	peroxiredoxin 2	Homo sapiens	160-164
26461310-5	2014	In order for this to be attained, Prx2"s effective rate constant with H2O2would have to be just ~10(5) M(-1)s(-1), much lower than that determined in multiple experiments with the purified proteins.	h2o2would	70-79	peroxiredoxin 2	Homo sapiens	34-38
26461310-6	2014	Nevertheless, nearly all Prx2 is oxidized within 1min of exposing erythrocytes to a H2O2 bolus, which is inconsistent with an irreversible inhibition.	Hydrogen Peroxide	84-88	peroxiredoxin 2	Homo sapiens	25-29
26461315-1	2014	In human erythrocytes H2O2 is mainly consumed by glutathione peroxidase, catalase and peroxiredoxin 2 (Prx2).	Hydrogen Peroxide	22-26	peroxiredoxin 2	Homo sapiens	86-101
26461315-1	2014	In human erythrocytes H2O2 is mainly consumed by glutathione peroxidase, catalase and peroxiredoxin 2 (Prx2).	Hydrogen Peroxide	22-26	peroxiredoxin 2	Homo sapiens	103-107
26461315-3	2014	If this activity is inhibited then the main role of Prx2 cannot be to eliminate H2O2.	Hydrogen Peroxide	80-84	peroxiredoxin 2	Homo sapiens	52-56
26461315-5	2014	We then applied it to analyze the behavior of Prx2 and Trx under the H2O2 exposure dynamics that erythrocytes face in circulation.	Hydrogen Peroxide	69-73	peroxiredoxin 2	Homo sapiens	46-50
24862795-4	2014	Using 2-dimensional difference gel electrophoresis and protein identification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry, we found that peroxiredoxin 2 (PRDX2), a member of the peroxiredoxin family that regulates reactive oxygen species, was markedly upregulated in neutrophils of RCMD patients compared to healthy donors.	Reactive Oxygen Species	250-273	peroxiredoxin 2	Homo sapiens	173-188
24862795-4	2014	Using 2-dimensional difference gel electrophoresis and protein identification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry, we found that peroxiredoxin 2 (PRDX2), a member of the peroxiredoxin family that regulates reactive oxygen species, was markedly upregulated in neutrophils of RCMD patients compared to healthy donors.	Reactive Oxygen Species	250-273	peroxiredoxin 2	Homo sapiens	190-195
24952139-8	2014	Simulations of the responses to physiological H2O2 stimuli highlight that a design combining abundant Prx2 with a low effective peroxidase activity spares NADPH while improving potential signaling properties of the Prx2/thioredoxin/thioredoxin reductase system.	NADP	155-160	peroxiredoxin 2	Homo sapiens	102-106
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Hydrogen Peroxide	82-99	peroxiredoxin 2	Homo sapiens	0-14
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Hydrogen Peroxide	82-99	peroxiredoxin 2	Homo sapiens	16-20
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Hydrogen Peroxide	101-105	peroxiredoxin 2	Homo sapiens	0-14
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Hydrogen Peroxide	101-105	peroxiredoxin 2	Homo sapiens	16-20
24719319-6	2014	In this work we characterize Prx2 tyrosine nitration, a post-translational modification on a noncatalytic residue that increases its peroxidase activity and its resistance to overoxidation.	Tyrosine	34-42	peroxiredoxin 2	Homo sapiens	29-33
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Hydrogen Peroxide	119-133	peroxiredoxin 2	Homo sapiens	0-14
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Hydrogen Peroxide	119-133	peroxiredoxin 2	Homo sapiens	16-20
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Water	137-142	peroxiredoxin 2	Homo sapiens	0-14
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Water	137-142	peroxiredoxin 2	Homo sapiens	16-20
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Alcohols	147-155	peroxiredoxin 2	Homo sapiens	0-14
24631653-2	2014	Peroxiredoxin2 (PRX2) is one of six mammalian isoenzymes (PRX1-6) that can reduce hydrogen peroxide (H2O2) and organic hydroperoxides to water and alcohols.	Alcohols	147-155	peroxiredoxin 2	Homo sapiens	16-20
24636884-2	2014	Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form.	Disulfides	98-107	peroxiredoxin 2	Homo sapiens	0-15
24636884-2	2014	Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form.	Disulfides	98-107	peroxiredoxin 2	Homo sapiens	17-21
24636884-7	2014	When treated with reagent H2O2, the G6PD-deficient erythrocytes were severely compromised in their ability to recycle oxidized Prx2, with only 27 or 4% reduction after 1 h treatment with 0.1 or 1 mM H2O2 respectively, compared with &gt;97% reduction in control erythrocytes.	Hydrogen Peroxide	26-30	peroxiredoxin 2	Homo sapiens	127-131
24636884-7	2014	When treated with reagent H2O2, the G6PD-deficient erythrocytes were severely compromised in their ability to recycle oxidized Prx2, with only 27 or 4% reduction after 1 h treatment with 0.1 or 1 mM H2O2 respectively, compared with &gt;97% reduction in control erythrocytes.	Hydrogen Peroxide	199-203	peroxiredoxin 2	Homo sapiens	127-131
24719319-7	2014	Mass spectrometry analysis revealed that treatment of disulfide-oxidized Prx2 with excess peroxynitrite renders mainly mononitrated and dinitrated species.	Disulfides	54-63	peroxiredoxin 2	Homo sapiens	73-77
24719319-7	2014	Mass spectrometry analysis revealed that treatment of disulfide-oxidized Prx2 with excess peroxynitrite renders mainly mononitrated and dinitrated species.	Peroxynitrous Acid	90-103	peroxiredoxin 2	Homo sapiens	73-77
24976757-2	2014	PrxII is induced by various oxidative stimuli and plays an important protective role against oxidative radical damage by reactive oxygen species.	Reactive Oxygen Species	121-144	peroxiredoxin 2	Homo sapiens	0-5
24627081-5	2014	Using a 2-DE-based proteomic approach, 3 upregulated oxidative stress markers, Hsp70-1, Hop and Prdx2, were identified in the HepG2 cells treated with 40 microM oridonin for 24 h. A pattern of alteration in Hsp70-1 was verified by western blotting.	oridonin	161-169	peroxiredoxin 2	Homo sapiens	96-101
24631019-6	2014	Among the 20 differential proteins identified, 8 were found to be modulated by SET in TCE-induced cytotoxicity and three of them (cofilin-1, peroxiredoxin-2 and S100-A11) were validated by Western-blot analysis.	Trichloroethylene	86-89	peroxiredoxin 2	Homo sapiens	141-156
24616707-6	2014	The bulk of the ROS are neutralized by the RBC antioxidant system consisting of both non-enzymatic and enzymatic antioxidants including catalase, glutathione peroxidase and peroxiredoxin-2.	Reactive Oxygen Species	16-19	peroxiredoxin 2	Homo sapiens	173-188
24397869-9	2014	Cysteine modifications of PARK7/DJ-1, peroxiredoxin-2, and other proteins were identified, quantified, and compared to overall levels of protein S-nitrosylation.	Cysteine	0-8	peroxiredoxin 2	Homo sapiens	38-53
24424027-4	2014	A mutation of the Tor2 glycine residue (G2040D) that lies adjacent to the key Torin-interacting tryptophan provides Torin1 resistance, confirming the specificity of Torin1 for TOR.	Glycine	23-30	peroxiredoxin 2	Homo sapiens	78-83
24424027-4	2014	A mutation of the Tor2 glycine residue (G2040D) that lies adjacent to the key Torin-interacting tryptophan provides Torin1 resistance, confirming the specificity of Torin1 for TOR.	Tryptophan	96-106	peroxiredoxin 2	Homo sapiens	78-83
24500687-6	2014	Fatty acid overload led to a redox imbalance which deactivated the antioxidant protein peroxiredoxin 2 and caused a peroxide-mediated apoptosis through the redox-sensitive pJNK/caspase-3 pathway.	Fatty Acids	0-10	peroxiredoxin 2	Homo sapiens	87-102
24500687-6	2014	Fatty acid overload led to a redox imbalance which deactivated the antioxidant protein peroxiredoxin 2 and caused a peroxide-mediated apoptosis through the redox-sensitive pJNK/caspase-3 pathway.	Peroxides	116-124	peroxiredoxin 2	Homo sapiens	87-102
24699133-1	2014	The human erythrocyte contains an abundance of the thiol-dependant peroxidase Peroxiredoxin-2 (Prx2), which protects the cell from the pro-oxidant environment it encounters during its 120 days of life in the blood stream.	Sulfhydryl Compounds	51-56	peroxiredoxin 2	Homo sapiens	78-93
24699133-1	2014	The human erythrocyte contains an abundance of the thiol-dependant peroxidase Peroxiredoxin-2 (Prx2), which protects the cell from the pro-oxidant environment it encounters during its 120 days of life in the blood stream.	Sulfhydryl Compounds	51-56	peroxiredoxin 2	Homo sapiens	95-99
24699133-2	2014	In malarial infections, the Plasmodium parasite invades red cells and imports Prx2 during intraerythrocytic development, presumably to supplement in its own degradation of peroxides generated during cell metabolism, especially hemoglobin (Hb) digestion.	Peroxides	172-181	peroxiredoxin 2	Homo sapiens	78-82
24699133-3	2014	Here we demonstrate that an irreversible Prx2 inhibitor, Conoidin A (2,3-bis(bromomethyl)-1,4-dioxide-quinoxaline; BBMQ), has potent cytocidal activity against cultured P. falciparum.	conoidin	57-65	peroxiredoxin 2	Homo sapiens	41-45
24699133-3	2014	Here we demonstrate that an irreversible Prx2 inhibitor, Conoidin A (2,3-bis(bromomethyl)-1,4-dioxide-quinoxaline; BBMQ), has potent cytocidal activity against cultured P. falciparum.	2,3-bis(bromomethyl)-1,4-dioxide-quinoxaline	69-113	peroxiredoxin 2	Homo sapiens	41-45
24699133-3	2014	Here we demonstrate that an irreversible Prx2 inhibitor, Conoidin A (2,3-bis(bromomethyl)-1,4-dioxide-quinoxaline; BBMQ), has potent cytocidal activity against cultured P. falciparum.	bbmq	115-119	peroxiredoxin 2	Homo sapiens	41-45
23911960-8	2013	Gene silencing assay demonstrated that reduced expression of PRDX2 was associated with increased sensitivity of OS cells to chemotherapeutic drugs such as methotrexate, doxorubicin and cisplatin.	Methotrexate	155-167	peroxiredoxin 2	Homo sapiens	61-66
24234423-1	2014	Peroxiredoxin 2 (Prdx2) is a member of the peroxiredoxin family, which is responsible for neutralizing reactive oxygen species.	Reactive Oxygen Species	103-126	peroxiredoxin 2	Homo sapiens	0-15
24234423-1	2014	Peroxiredoxin 2 (Prdx2) is a member of the peroxiredoxin family, which is responsible for neutralizing reactive oxygen species.	Reactive Oxygen Species	103-126	peroxiredoxin 2	Homo sapiens	17-22
24234423-1	2014	Peroxiredoxin 2 (Prdx2) is a member of the peroxiredoxin family, which is responsible for neutralizing reactive oxygen species.	Reactive Oxygen Species	103-126	peroxiredoxin 2	Homo sapiens	43-56
24234423-8	2014	Suppression of Prdx2 using a lentiviral vector-mediated Prdx2-specific shRNA in the LoVo cell line restored H2O2 sensitivity.	Hydrogen Peroxide	108-112	peroxiredoxin 2	Homo sapiens	15-20
24234423-8	2014	Suppression of Prdx2 using a lentiviral vector-mediated Prdx2-specific shRNA in the LoVo cell line restored H2O2 sensitivity.	Hydrogen Peroxide	108-112	peroxiredoxin 2	Homo sapiens	56-61
24222118-0	2013	Human pancreatic cancer cells with acquired gemcitabine resistance exhibit significant up-regulation of peroxiredoxin-2 compared to sensitive parental cells.	gemcitabine	44-55	peroxiredoxin 2	Homo sapiens	104-119
24222118-9	2013	These results suggest that peroxiredoxin-2 is a possible candidate biomarker for predicting the response of patients with pancreatic cancer to treatment with gemcitabine.	gemcitabine	158-169	peroxiredoxin 2	Homo sapiens	27-42
24648762-4	2013	Our results, presented here, show that silencing PrxII gene expression increased cellular toxicity by altering cellular thiol status, inhibiting Ca(2+) efflux from the cells, and perturbing the intracellular Ca(2+) homeostasis.	Sulfhydryl Compounds	120-125	peroxiredoxin 2	Homo sapiens	49-54
23911960-8	2013	Gene silencing assay demonstrated that reduced expression of PRDX2 was associated with increased sensitivity of OS cells to chemotherapeutic drugs such as methotrexate, doxorubicin and cisplatin.	Doxorubicin	169-180	peroxiredoxin 2	Homo sapiens	61-66
23911960-8	2013	Gene silencing assay demonstrated that reduced expression of PRDX2 was associated with increased sensitivity of OS cells to chemotherapeutic drugs such as methotrexate, doxorubicin and cisplatin.	Cisplatin	185-194	peroxiredoxin 2	Homo sapiens	61-66
23572564-7	2013	In these categories, Peroxiredoxin-2 and 6, that control hydrogen peroxide metabolic processes, are the main enriched molecules together with the anti-apoptotic 78 kDa glucose regulated protein.	Hydrogen Peroxide	57-74	peroxiredoxin 2	Homo sapiens	21-42
23713588-5	2013	Mutant analyses revealed that loss of the peroxidative cysteine residue of Prx2 also facilitated complex formation with ERp46, even without H2O2 treatment, whereas the resolving cysteine residue of Prx2 was indispensible for the interaction to occur.	Cysteine	178-186	peroxiredoxin 2	Homo sapiens	198-202
23713588-6	2013	The complex involved a stable non-covalent interaction that was disassociated by the reduction of intramolecular disulfides in ERp46, or by disruption of the decameric structure of hyperoxidized Prx2.	Disulfides	113-123	peroxiredoxin 2	Homo sapiens	195-199
23889121-11	2013	Excessive accumulation of reactive oxygen species induced by ultra-endurance exercise may underlie depletion of lymphocyte PRDX-2 by triggering its turnover after oxidation.	Reactive Oxygen Species	26-49	peroxiredoxin 2	Homo sapiens	123-129
23713588-4	2013	In the present study we have searched for binding partners of Prx2 in H2O2-treated Jurkat and human umbilical vein endothelial cells and discovered that the hyperoxidized form selectively co-precipitated with the protein disulfide-isomerase ERp46.	Hydrogen Peroxide	70-74	peroxiredoxin 2	Homo sapiens	62-66
23713588-5	2013	Mutant analyses revealed that loss of the peroxidative cysteine residue of Prx2 also facilitated complex formation with ERp46, even without H2O2 treatment, whereas the resolving cysteine residue of Prx2 was indispensible for the interaction to occur.	Cysteine	55-63	peroxiredoxin 2	Homo sapiens	75-79
22430214-7	2013	The 435-L3 cells silenced for PRDX2 were significantly more sensitive to H(2)O(2)-induced oxidative stress than the parental and scrambled transfected cells.	Hydrogen Peroxide	73-81	peroxiredoxin 2	Homo sapiens	30-35
23543738-0	2013	Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine.	Sulfenic Acids	82-95	peroxiredoxin 2	Homo sapiens	18-40
23543738-0	2013	Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine.	Cysteine	115-123	peroxiredoxin 2	Homo sapiens	18-40
23543738-1	2013	Typical 2-Cys peroxiredoxins (Prxs) react rapidly with H2O2 to form a sulfenic acid, which then condenses with the resolving cysteine of the adjacent Prx in the homodimer or reacts with another H2O2 to become hyperoxidized.	2-cys	8-13	peroxiredoxin 2	Homo sapiens	14-28
23543738-1	2013	Typical 2-Cys peroxiredoxins (Prxs) react rapidly with H2O2 to form a sulfenic acid, which then condenses with the resolving cysteine of the adjacent Prx in the homodimer or reacts with another H2O2 to become hyperoxidized.	Hydrogen Peroxide	55-59	peroxiredoxin 2	Homo sapiens	14-28
23543738-1	2013	Typical 2-Cys peroxiredoxins (Prxs) react rapidly with H2O2 to form a sulfenic acid, which then condenses with the resolving cysteine of the adjacent Prx in the homodimer or reacts with another H2O2 to become hyperoxidized.	Sulfenic Acids	70-83	peroxiredoxin 2	Homo sapiens	14-28
23543738-1	2013	Typical 2-Cys peroxiredoxins (Prxs) react rapidly with H2O2 to form a sulfenic acid, which then condenses with the resolving cysteine of the adjacent Prx in the homodimer or reacts with another H2O2 to become hyperoxidized.	Cysteine	125-133	peroxiredoxin 2	Homo sapiens	14-28
23543738-1	2013	Typical 2-Cys peroxiredoxins (Prxs) react rapidly with H2O2 to form a sulfenic acid, which then condenses with the resolving cysteine of the adjacent Prx in the homodimer or reacts with another H2O2 to become hyperoxidized.	Hydrogen Peroxide	194-198	peroxiredoxin 2	Homo sapiens	14-28
23543738-4	2013	We determined rate constants for disulfide formation and hyperoxidation for human recombinant Prx2 and Prx3 by analyzing the relative proportions of hyperoxidized and dimeric products using mass spectrometry as a function of H2O2 concentration (in the absence of reductive cycling) and in competition with catalase at a fixed concentration of H2O2.	Disulfides	33-42	peroxiredoxin 2	Homo sapiens	94-98
23543738-4	2013	We determined rate constants for disulfide formation and hyperoxidation for human recombinant Prx2 and Prx3 by analyzing the relative proportions of hyperoxidized and dimeric products using mass spectrometry as a function of H2O2 concentration (in the absence of reductive cycling) and in competition with catalase at a fixed concentration of H2O2.	Hydrogen Peroxide	225-229	peroxiredoxin 2	Homo sapiens	94-98
23543738-4	2013	We determined rate constants for disulfide formation and hyperoxidation for human recombinant Prx2 and Prx3 by analyzing the relative proportions of hyperoxidized and dimeric products using mass spectrometry as a function of H2O2 concentration (in the absence of reductive cycling) and in competition with catalase at a fixed concentration of H2O2.	Hydrogen Peroxide	343-347	peroxiredoxin 2	Homo sapiens	94-98
23543738-5	2013	This gave a second order rate constant for hyperoxidation of 12,000 M(-1) s(-1) and a rate constant for disulfide formation of 2 s(-1) for Prx2.	Disulfides	104-113	peroxiredoxin 2	Homo sapiens	139-143
23543738-9	2013	Although the sulfenic acid forms of Prx2 and Prx3 are ~1000-fold less reactive with H2O2 than their active site thiols, they react several orders of magnitude faster than most reduced thiol proteins.	Sulfenic Acids	13-26	peroxiredoxin 2	Homo sapiens	36-40
23543738-9	2013	Although the sulfenic acid forms of Prx2 and Prx3 are ~1000-fold less reactive with H2O2 than their active site thiols, they react several orders of magnitude faster than most reduced thiol proteins.	Hydrogen Peroxide	84-88	peroxiredoxin 2	Homo sapiens	36-40
23543738-9	2013	Although the sulfenic acid forms of Prx2 and Prx3 are ~1000-fold less reactive with H2O2 than their active site thiols, they react several orders of magnitude faster than most reduced thiol proteins.	Sulfhydryl Compounds	112-118	peroxiredoxin 2	Homo sapiens	36-40
23543738-9	2013	Although the sulfenic acid forms of Prx2 and Prx3 are ~1000-fold less reactive with H2O2 than their active site thiols, they react several orders of magnitude faster than most reduced thiol proteins.	Sulfhydryl Compounds	112-117	peroxiredoxin 2	Homo sapiens	36-40
22430214-8	2013	BO2/PRDX2 cells produced less ROS than BO2/green fluorescent protein control cells under oxidative stress.	Reactive Oxygen Species	30-33	peroxiredoxin 2	Homo sapiens	4-9
22430214-11	2013	Furthermore, PRDX2 expression in breast cancer cells was associated with a glucose-dependent phenotype, different from bone metastatic cells.	Glucose	75-82	peroxiredoxin 2	Homo sapiens	13-18
24205432-7	2013	Novel cytoprotective systems such as ASHP, eIF2 alpha, and peroxiredoxin-2 have been suggested to be important against ROS in beta-thalassemic erythropoiesis.	Reactive Oxygen Species	119-122	peroxiredoxin 2	Homo sapiens	59-74
23123411-7	2013	Hemichrome formation induced by phenylhydrazine of RBCs prevented membrane association of PRDX2, implying overlapping binding sites.	phenylhydrazine	32-47	peroxiredoxin 2	Homo sapiens	90-95
23113308-2	2012	It was found that drug resistance formation was accompanied by a significant increase in the expression of PRDX1, PRDX2, PRDX3, PRDX6 genes in all cancer cell strains, which confirms the important contribution of redox-dependent mechanisms into the development of cisplatin resistance of cancer cells.	Cisplatin	264-273	peroxiredoxin 2	Homo sapiens	114-119
23151508-5	2012	MPP(+) induces CDK5/p25-dependent phosphorylation of peroxiredoxin 2 (Prx2), resulting in inhibition of its peroxireductase activity and accumulation of reactive oxygen species (ROS).	Reactive Oxygen Species	153-176	peroxiredoxin 2	Homo sapiens	53-68
23151508-5	2012	MPP(+) induces CDK5/p25-dependent phosphorylation of peroxiredoxin 2 (Prx2), resulting in inhibition of its peroxireductase activity and accumulation of reactive oxygen species (ROS).	Reactive Oxygen Species	153-176	peroxiredoxin 2	Homo sapiens	70-74
23151508-5	2012	MPP(+) induces CDK5/p25-dependent phosphorylation of peroxiredoxin 2 (Prx2), resulting in inhibition of its peroxireductase activity and accumulation of reactive oxygen species (ROS).	Reactive Oxygen Species	178-181	peroxiredoxin 2	Homo sapiens	53-68
23151508-5	2012	MPP(+) induces CDK5/p25-dependent phosphorylation of peroxiredoxin 2 (Prx2), resulting in inhibition of its peroxireductase activity and accumulation of reactive oxygen species (ROS).	Reactive Oxygen Species	178-181	peroxiredoxin 2	Homo sapiens	70-74
22537912-1	2012	Peroxiredoxin 2, a typical 2-Cys peroxiredoxin, is the third most abundant protein in erythrocytes.	2-cys peroxiredoxin	27-46	peroxiredoxin 2	Homo sapiens	0-15
22960070-3	2012	Upon oxidative stress, ROS and Heinz body formation were significantly increased in Prx II knockout RBCs compared to wild-type (WT), which ultimately accelerated the accumulation of hemosiderin and heme-oxygenase 1 in the Prx II knock-out livers.	Reactive Oxygen Species	23-26	peroxiredoxin 2	Homo sapiens	84-90
22805285-1	2012	Human peroxiredoxin 2 (Prx2), which is abundant in erythrocytes, has been shown to play a key role in protecting erythrocytes against oxidative stress by scavenging reactive oxygen species as well as participating in cell signal transduction.	Reactive Oxygen Species	165-188	peroxiredoxin 2	Homo sapiens	6-21
22805285-1	2012	Human peroxiredoxin 2 (Prx2), which is abundant in erythrocytes, has been shown to play a key role in protecting erythrocytes against oxidative stress by scavenging reactive oxygen species as well as participating in cell signal transduction.	Reactive Oxygen Species	165-188	peroxiredoxin 2	Homo sapiens	23-27
22805285-5	2012	The peroxidase activity of Prx2 to scavenge H(2)O(2) was determined by a ferrithiocyanate assay.	Hydrogen Peroxide	44-52	peroxiredoxin 2	Homo sapiens	27-31
22805285-5	2012	The peroxidase activity of Prx2 to scavenge H(2)O(2) was determined by a ferrithiocyanate assay.	ferrithiocyanate	73-89	peroxiredoxin 2	Homo sapiens	27-31
22261619-7	2012	Interacting with peroxiredoxin 2 (Prdx2), amino-Nogo-A reduces reactive oxygen species (ROS) generation and extracellular signal-regulated kinase phosphorylation to exert neuroprotective effects.	Reactive Oxygen Species	63-86	peroxiredoxin 2	Homo sapiens	17-32
22261619-7	2012	Interacting with peroxiredoxin 2 (Prdx2), amino-Nogo-A reduces reactive oxygen species (ROS) generation and extracellular signal-regulated kinase phosphorylation to exert neuroprotective effects.	Reactive Oxygen Species	63-86	peroxiredoxin 2	Homo sapiens	34-39
22261619-7	2012	Interacting with peroxiredoxin 2 (Prdx2), amino-Nogo-A reduces reactive oxygen species (ROS) generation and extracellular signal-regulated kinase phosphorylation to exert neuroprotective effects.	Reactive Oxygen Species	88-91	peroxiredoxin 2	Homo sapiens	17-32
22261619-7	2012	Interacting with peroxiredoxin 2 (Prdx2), amino-Nogo-A reduces reactive oxygen species (ROS) generation and extracellular signal-regulated kinase phosphorylation to exert neuroprotective effects.	Reactive Oxygen Species	88-91	peroxiredoxin 2	Homo sapiens	34-39
22537912-2	2012	It is understood that the physiologically functional state of peroxiredoxin 2 is the monomer, and that its role in scavenging low levels of H(2)O(2) results in the formation of disulfide-linked dimers, which are reversibly reduced to monomers by the thioredoxin-thioredoxin reductase system.	Hydrogen Peroxide	140-148	peroxiredoxin 2	Homo sapiens	62-77
22537912-2	2012	It is understood that the physiologically functional state of peroxiredoxin 2 is the monomer, and that its role in scavenging low levels of H(2)O(2) results in the formation of disulfide-linked dimers, which are reversibly reduced to monomers by the thioredoxin-thioredoxin reductase system.	Disulfides	177-186	peroxiredoxin 2	Homo sapiens	62-77
21840697-8	2012	Of particular interest was the regulation of a number of proteins involved in stress response--peroxiredoxin-2, peroxiredoxin-3 and peroxiredoxin-6-all of which were shown to be down-regulated with H2O2 exposure.	Hydrogen Peroxide	198-202	peroxiredoxin 2	Homo sapiens	95-110
21423689-5	2011	Proteins that showed increased expression levels upon Sal B treatment were vimentin, T-complex protein 1, protein disulfide isomerase, tropomyosin alpha, heat shock protein beta-1, UBX domain-containing protein 1, alpha enolase, and peroxiredoxin-2.	salvianolic acid B	54-59	peroxiredoxin 2	Homo sapiens	233-248
22623418-7	2012	For example, the detoxification enzyme NQO1 was increased with treatment in both cell lines, while disparate members of the peroxiredoxin family, PRDX2 or PRDX5 and PRDX6, were elevated with 5-FU exposure in either SW480 or SW620, respectively.	Fluorouracil	191-195	peroxiredoxin 2	Homo sapiens	124-137
22623418-7	2012	For example, the detoxification enzyme NQO1 was increased with treatment in both cell lines, while disparate members of the peroxiredoxin family, PRDX2 or PRDX5 and PRDX6, were elevated with 5-FU exposure in either SW480 or SW620, respectively.	Fluorouracil	191-195	peroxiredoxin 2	Homo sapiens	146-151
22207736-4	2012	H3Ac was decreased at the PRDX2 gene promoter in AML, which correlated with low mRNA and protein expression.	h3ac	0-4	peroxiredoxin 2	Homo sapiens	26-31
22207736-7	2012	Functionally, PRDX2 acted as inhibitor of myeloid cell growth by reducing levels of reactive oxygen species (ROS) generated in response to cytokines.	Reactive Oxygen Species	84-107	peroxiredoxin 2	Homo sapiens	14-19
22207736-7	2012	Functionally, PRDX2 acted as inhibitor of myeloid cell growth by reducing levels of reactive oxygen species (ROS) generated in response to cytokines.	Reactive Oxygen Species	109-112	peroxiredoxin 2	Homo sapiens	14-19
22207736-9	2012	Taken together, epigenome-wide analyses of H3Ac in AML led to the identification of PRDX2 as an epigenetically silenced growth suppressor, suggesting a possible role of ROS in the malignant phenotype in AML.	h3ac	43-47	peroxiredoxin 2	Homo sapiens	84-89
22207736-9	2012	Taken together, epigenome-wide analyses of H3Ac in AML led to the identification of PRDX2 as an epigenetically silenced growth suppressor, suggesting a possible role of ROS in the malignant phenotype in AML.	Reactive Oxygen Species	169-172	peroxiredoxin 2	Homo sapiens	84-89
22003971-9	2012	Anti-Prx 2-positive patients had significantly greater excretion of urinary 8-isoprostaglandin than did anti-Prx 2-negative patients.	8-isoprostaglandin	76-94	peroxiredoxin 2	Homo sapiens	5-10
22916248-11	2012	The mRNA profiler array showed more than 2-fold differential expression of 32 oxidative stress-related genes in unstimulated moDCs, including peroxiredoxin-2 (PRDX2), an enzyme reducing hydrogen peroxide and lipid peroxides.	Hydrogen Peroxide	186-203	peroxiredoxin 2	Homo sapiens	142-157
22916248-11	2012	The mRNA profiler array showed more than 2-fold differential expression of 32 oxidative stress-related genes in unstimulated moDCs, including peroxiredoxin-2 (PRDX2), an enzyme reducing hydrogen peroxide and lipid peroxides.	Hydrogen Peroxide	186-203	peroxiredoxin 2	Homo sapiens	159-164
22916248-11	2012	The mRNA profiler array showed more than 2-fold differential expression of 32 oxidative stress-related genes in unstimulated moDCs, including peroxiredoxin-2 (PRDX2), an enzyme reducing hydrogen peroxide and lipid peroxides.	Lipid Peroxides	208-223	peroxiredoxin 2	Homo sapiens	142-157
22916248-11	2012	The mRNA profiler array showed more than 2-fold differential expression of 32 oxidative stress-related genes in unstimulated moDCs, including peroxiredoxin-2 (PRDX2), an enzyme reducing hydrogen peroxide and lipid peroxides.	Lipid Peroxides	208-223	peroxiredoxin 2	Homo sapiens	159-164
22916248-13	2012	Silencing PRDX2 in moDCs by means of siRNA significantly increased CM-DCF fluorescence and cell death upon tert-BHP-stimulation.	Pentostatin	70-73	peroxiredoxin 2	Homo sapiens	10-15
22916248-13	2012	Silencing PRDX2 in moDCs by means of siRNA significantly increased CM-DCF fluorescence and cell death upon tert-BHP-stimulation.	tert-Butylhydroperoxide	107-115	peroxiredoxin 2	Homo sapiens	10-15
22916248-15	2012	Upregulation of PRDX2 is involved in the neutralization of ROS in moDCs.	Reactive Oxygen Species	59-62	peroxiredoxin 2	Homo sapiens	16-21
22099303-3	2011	Here, we report that the VEGFR2 RTK has an oxidation-sensitive cysteine residue whose reduced state is preserved specifically by peroxiredoxin II (PrxII) in vascular endothelial cells.	Cysteine	63-71	peroxiredoxin 2	Homo sapiens	129-145
22099303-3	2011	Here, we report that the VEGFR2 RTK has an oxidation-sensitive cysteine residue whose reduced state is preserved specifically by peroxiredoxin II (PrxII) in vascular endothelial cells.	Cysteine	63-71	peroxiredoxin 2	Homo sapiens	147-152
21750082-4	2011	We exposed normal cells and K562 cells with silenced peroxiredoxin-2 to H(2)O(2) and generated a recombinant peroxiredoxin-2 for kinetic measurements in the presence of H(2)O(2) or hemin.	Water	72-77	peroxiredoxin 2	Homo sapiens	53-68
21750082-5	2011	RESULTS: In beta-thalassemia the increased production of reactive oxygen species was associated with down-regulation of heme oxygenase-1 and biliverdin reductase and up-regulation of peroxiredoxin-2.	Reactive Oxygen Species	57-80	peroxiredoxin 2	Homo sapiens	183-198
21750082-10	2011	We then showed that peroxiredoxin-2 binds heme in erythroid precursors with high affinity, suggesting a possible multifunctional cytoprotective role of peroxiredoxin-2 in beta-thalassemia.	Heme	42-46	peroxiredoxin 2	Homo sapiens	20-35
21354257-5	2011	Interestingly, the 440 kDa complex contained both reduced and oxidized (disulphide-linked dimers) PrxII decamers.	disulphide	72-82	peroxiredoxin 2	Homo sapiens	98-103
21209210-0	2011	Peroxiredoxin-2 protects against 6-hydroxydopamine-induced dopaminergic neurodegeneration via attenuation of the apoptosis signal-regulating kinase (ASK1) signaling cascade.	Oxidopamine	33-50	peroxiredoxin 2	Homo sapiens	0-15
21209210-5	2011	Of the 2-cysteine PRXs that were tested in MN9D DA neurons, endogenous PRX2 was most beneficial to cell survival.	2-cysteine	7-17	peroxiredoxin 2	Homo sapiens	71-75
22189915-9	2012	In particular, based on the affinity purification approach, peroxiredoxin 2 was identified as a microglial target of obovatol.	obovatol	117-125	peroxiredoxin 2	Homo sapiens	60-75
21805023-13	2011	PRDX2 and GSTP1 may play roles in compensating mechanisms for reduction of ROS stress, and SFN may play roles in prevention of cancer development in proliferating cells through G2/M cell cycle arrest upon accidental DNA damage within psoriatic skin lesions.	Reactive Oxygen Species	75-78	peroxiredoxin 2	Homo sapiens	0-5
21385867-0	2011	Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study.	Hydrogen Peroxide	68-85	peroxiredoxin 2	Homo sapiens	40-62
21385867-2	2011	We present strong experimental evidence that two highly conserved arginine residues play a vital role in this activity of human Prx2 and Prx3.	Arginine	66-74	peroxiredoxin 2	Homo sapiens	128-132
20980255-6	2011	However, inhibition of the mTORC2 cascade through the dual mTORC1/mTORC2 inhibitor Torin, or through rictor-targeted shRNA, resulted in a significant attenuation in PGE(2)-mediated chemotaxis, which was associated with a comparable decrease in actin polymerization.	Dinoprostone	165-171	peroxiredoxin 2	Homo sapiens	83-88
20347000-0	2010	Formaldehyde induces apoptosis through decreased Prx 2 via p38 MAPK in lung epithelial cells.	Formaldehyde	0-12	peroxiredoxin 2	Homo sapiens	49-54
20347000-12	2010	The FA-induced decrease in Prx 2 and increase in cell apoptosis was restored by treatment with SB203580 [a p38 mitogen activated protein kinase (MAPK) inhibitor], but not by SP600125 [a c-jun-N-terminal kinase (JNK) inhibitor].	SB 203580	95-103	peroxiredoxin 2	Homo sapiens	27-32
20840079-0	2010	Removal of amino acid, peptide and protein hydroperoxides by reaction with peroxiredoxins 2 and 3.	Hydrogen Peroxide	43-57	peroxiredoxin 2	Homo sapiens	75-97
20840079-1	2010	Prxs (peroxiredoxins) are a ubiquitous family of cysteine-dependent peroxidases that react rapidly with H2O2 and alkyl hydroperoxides and provide defence against these reactive oxidants.	Cysteine	49-57	peroxiredoxin 2	Homo sapiens	6-20
20840079-1	2010	Prxs (peroxiredoxins) are a ubiquitous family of cysteine-dependent peroxidases that react rapidly with H2O2 and alkyl hydroperoxides and provide defence against these reactive oxidants.	Hydrogen Peroxide	104-108	peroxiredoxin 2	Homo sapiens	6-20
20840079-1	2010	Prxs (peroxiredoxins) are a ubiquitous family of cysteine-dependent peroxidases that react rapidly with H2O2 and alkyl hydroperoxides and provide defence against these reactive oxidants.	alkyl hydroperoxides	113-133	peroxiredoxin 2	Homo sapiens	6-20
20840079-4	2010	Isolated Prx2, which is a cytosolic protein, and Prx3, which resides within mitochondria, were reacted with a selection of hydroperoxides generated by gamma-radiolysis or singlet oxygen, on free amino acids, peptides and proteins.	Hydrogen Peroxide	123-137	peroxiredoxin 2	Homo sapiens	9-13
20840079-4	2010	Isolated Prx2, which is a cytosolic protein, and Prx3, which resides within mitochondria, were reacted with a selection of hydroperoxides generated by gamma-radiolysis or singlet oxygen, on free amino acids, peptides and proteins.	Singlet Oxygen	171-185	peroxiredoxin 2	Homo sapiens	9-13
20840079-4	2010	Isolated Prx2, which is a cytosolic protein, and Prx3, which resides within mitochondria, were reacted with a selection of hydroperoxides generated by gamma-radiolysis or singlet oxygen, on free amino acids, peptides and proteins.	Peptides	208-216	peroxiredoxin 2	Homo sapiens	9-13
20840079-7	2010	N-acetyl leucine hydroperoxides reacted with Prx2 with a rate constant of 4 x 10(4) M-1   s-1.	n-acetyl leucine hydroperoxides	0-31	peroxiredoxin 2	Homo sapiens	45-49
20840079-10	2010	Addition of an uncharged derivative of leucine hydroperoxide to intact erythrocytes caused Prx2 oxidation with no concomitant loss in GSH, as did BSA hydroperoxide when added to concentrated erythrocyte lysate.	leucine hydroperoxide	39-60	peroxiredoxin 2	Homo sapiens	91-95
20660758-4	2010	We show that erythrocytes can efficiently eliminate H(2)O(2) derived from urate oxidation to prevent cell injury in vitro; during therapy, disulfide-linked peroxiredoxin 2 dimer did not accumulate in red blood cells, indicating that their peroxidase capacity was not exceeded.	Disulfides	139-148	peroxiredoxin 2	Homo sapiens	156-171
20823825-0	2010	[Torin (sertraline) in the treatment of depressive and obsessive-compulsive disorders in children].	Sertraline	8-18	peroxiredoxin 2	Homo sapiens	1-6
20823825-2	2010	Patients were treated with torin (sertraline) in dosage 25-50 mg daily during 4 weeks.	Sertraline	34-44	peroxiredoxin 2	Homo sapiens	27-32
19666612-0	2009	The malarial parasite Plasmodium falciparum imports the human protein peroxiredoxin 2 for peroxide detoxification.	Peroxides	90-98	peroxiredoxin 2	Homo sapiens	70-85
19716412-0	2009	Chloramines and hypochlorous acid oxidize erythrocyte peroxiredoxin 2.	Chloramines	0-11	peroxiredoxin 2	Homo sapiens	54-69
19716412-0	2009	Chloramines and hypochlorous acid oxidize erythrocyte peroxiredoxin 2.	Hypochlorous Acid	16-33	peroxiredoxin 2	Homo sapiens	54-69
19716412-1	2009	Peroxiredoxin 2 (Prx2) is an abundant thiol protein that is readily oxidized in erythrocytes exposed to hydrogen peroxide.	Hydrogen Peroxide	104-121	peroxiredoxin 2	Homo sapiens	0-15
19716412-1	2009	Peroxiredoxin 2 (Prx2) is an abundant thiol protein that is readily oxidized in erythrocytes exposed to hydrogen peroxide.	Hydrogen Peroxide	104-121	peroxiredoxin 2	Homo sapiens	17-21
19716412-3	2009	Prx2 was oxidized to a disulfide-linked dimer by HOCl, glycine chloramine (GlyCl), and monochloramine (NH(2)Cl) in a dose-dependent manner.	Disulfides	23-32	peroxiredoxin 2	Homo sapiens	0-4
19716412-3	2009	Prx2 was oxidized to a disulfide-linked dimer by HOCl, glycine chloramine (GlyCl), and monochloramine (NH(2)Cl) in a dose-dependent manner.	Hypochlorous Acid	49-53	peroxiredoxin 2	Homo sapiens	0-4
19716412-3	2009	Prx2 was oxidized to a disulfide-linked dimer by HOCl, glycine chloramine (GlyCl), and monochloramine (NH(2)Cl) in a dose-dependent manner.	glycine chloramine	55-73	peroxiredoxin 2	Homo sapiens	0-4
19716412-3	2009	Prx2 was oxidized to a disulfide-linked dimer by HOCl, glycine chloramine (GlyCl), and monochloramine (NH(2)Cl) in a dose-dependent manner.	glycine chloramine	75-80	peroxiredoxin 2	Homo sapiens	0-4
19716412-3	2009	Prx2 was oxidized to a disulfide-linked dimer by HOCl, glycine chloramine (GlyCl), and monochloramine (NH(2)Cl) in a dose-dependent manner.	chloramine	87-101	peroxiredoxin 2	Homo sapiens	0-4
19716412-3	2009	Prx2 was oxidized to a disulfide-linked dimer by HOCl, glycine chloramine (GlyCl), and monochloramine (NH(2)Cl) in a dose-dependent manner.	nh(2)cl	103-110	peroxiredoxin 2	Homo sapiens	0-4
19716412-5	2009	Second-order rate constants for the reactions of Prx2 with NH(2)Cl and GlyCl were 1.5 x 10(4) and 8 M(-1) s(-1), respectively.	nh(2)cl	59-66	peroxiredoxin 2	Homo sapiens	49-53
19716412-5	2009	Second-order rate constants for the reactions of Prx2 with NH(2)Cl and GlyCl were 1.5 x 10(4) and 8 M(-1) s(-1), respectively.	glycine chloramine	71-76	peroxiredoxin 2	Homo sapiens	49-53
19716412-6	2009	The NH(2)Cl value is approximately 10 times higher than that for GSH, whereas Prx2 is approximately 30 times less sensitive than GSH to GlyCl.	glycine chloramine	136-141	peroxiredoxin 2	Homo sapiens	78-82
19716412-7	2009	Thus, the relative sensitivity of Prx2 to GlyCl is greater in the erythrocyte.	glycine chloramine	42-47	peroxiredoxin 2	Homo sapiens	34-38
19716412-8	2009	Oxidation of erythrocyte Prx2 and GSH was less in the presence of glucose, probably because of recycling.	Glucose	66-73	peroxiredoxin 2	Homo sapiens	25-29
19716412-9	2009	High doses of NH(2)Cl resulted in incomplete regeneration of reduced Prx2, suggesting impairment of the recycling mechanism.	nh(2)cl	14-21	peroxiredoxin 2	Homo sapiens	69-73
19716412-10	2009	Our results show that, although HOCl and chloramines are less selective than H(2)O(2), they nevertheless oxidize Prx2.	Hypochlorous Acid	32-36	peroxiredoxin 2	Homo sapiens	113-117
19716412-10	2009	Our results show that, although HOCl and chloramines are less selective than H(2)O(2), they nevertheless oxidize Prx2.	Chloramines	41-52	peroxiredoxin 2	Homo sapiens	113-117
19720829-5	2009	RNA interference-mediated neuronal knockdown of Jafrac1 enhanced, while neuronal overexpression of Jafrac1 and hPrxII suppressed, paraquat-induced lethality in flies.	Paraquat	130-138	peroxiredoxin 2	Homo sapiens	111-117
19666612-6	2009	hPrx-2 accounts for roughly 50% of thioredoxin peroxidase activity in parasite extracts, thus indicating a functional role of hPrx-2 as an enzymatic scavenger of peroxides in the parasite.	Peroxides	162-171	peroxiredoxin 2	Homo sapiens	0-6
19666612-6	2009	hPrx-2 accounts for roughly 50% of thioredoxin peroxidase activity in parasite extracts, thus indicating a functional role of hPrx-2 as an enzymatic scavenger of peroxides in the parasite.	Peroxides	162-171	peroxiredoxin 2	Homo sapiens	126-132
19666612-7	2009	Under chloroquine treatment, a drug promoting oxidative stress, the abundance of hPrx-2 in the parasite increases significantly.	Chloroquine	6-17	peroxiredoxin 2	Homo sapiens	81-87
19375361-0	2009	Linkage of cytosolic peroxiredoxin 2 to erythrocyte membrane imposed by hydrogen peroxide-induced oxidative stress.	Hydrogen Peroxide	72-89	peroxiredoxin 2	Homo sapiens	21-36
18682255-8	2009	Smaller effects were also seen for one-carbon metabolism genes choline dehydrogenase (CHDH) (rs9001, rs7626693) and 5-methyltetrahydrofolate-homocysteine methyltransferase reductase (MTRR) (rs1801394) and genes involved in reduction reactions, glutaredoxin (GLRX) (rs3822751) and peroxiredoxin 2 (PRDX2) (rs10427027, rs12151144).	Carbon	39-45	peroxiredoxin 2	Homo sapiens	280-295
18682255-8	2009	Smaller effects were also seen for one-carbon metabolism genes choline dehydrogenase (CHDH) (rs9001, rs7626693) and 5-methyltetrahydrofolate-homocysteine methyltransferase reductase (MTRR) (rs1801394) and genes involved in reduction reactions, glutaredoxin (GLRX) (rs3822751) and peroxiredoxin 2 (PRDX2) (rs10427027, rs12151144).	Carbon	39-45	peroxiredoxin 2	Homo sapiens	297-302
19375361-1	2009	Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity.	2-cys	54-59	peroxiredoxin 2	Homo sapiens	18-33
19375361-1	2009	Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity.	2-cys	54-59	peroxiredoxin 2	Homo sapiens	35-39
19375361-1	2009	Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity.	Sulfhydryl Compounds	89-94	peroxiredoxin 2	Homo sapiens	18-33
19375361-1	2009	Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity.	Sulfhydryl Compounds	89-94	peroxiredoxin 2	Homo sapiens	35-39
19375361-1	2009	Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity.	Hydrogen Peroxide	105-122	peroxiredoxin 2	Homo sapiens	18-33
19375361-1	2009	Human erythrocyte peroxiredoxin 2 (Prx2) is a typical 2-cys cytosolic peroxiredoxin with thiol-dependent hydrogen peroxide scavenger activity.	Hydrogen Peroxide	105-122	peroxiredoxin 2	Homo sapiens	35-39
19375361-7	2009	Prx2 linkage to the membrane also rose with increasing H(2)O(2) concentration, and was only observed when the oxidized form of the enzyme was present in the cytosol.	Hydrogen Peroxide	55-63	peroxiredoxin 2	Homo sapiens	0-4
19286652-9	2009	A comparative study of non-N(alpha)-acetylated and N(alpha)-terminal acetylated Prx II revealed that N(alpha)-Ac of Prx II induces a significant shift in the circular dichroism spectrum and elevation of T(m) from 59.6 to 70.9 degrees C. These findings suggest that the structural maintenance of Prx II by N(alpha)-Ac may be responsible for preventing its hyperoxidation to form C(P)-SO(3)H.	n(alpha)-ac	101-112	peroxiredoxin 2	Homo sapiens	80-86
19151395-0	2009	Nipradilol and timolol induce Foxo3a and peroxiredoxin 2 expression and protect trabecular meshwork cells from oxidative stress.	nipradilol	0-10	peroxiredoxin 2	Homo sapiens	41-56
19151395-0	2009	Nipradilol and timolol induce Foxo3a and peroxiredoxin 2 expression and protect trabecular meshwork cells from oxidative stress.	Timolol	15-22	peroxiredoxin 2	Homo sapiens	41-56
19151395-7	2009	Nipradilol and timolol, but not latanoprost, induce the expression of peroxiredoxin 2 through the activation of the Foxo3a transcription factor.	nipradilol	0-10	peroxiredoxin 2	Homo sapiens	70-85
19151395-7	2009	Nipradilol and timolol, but not latanoprost, induce the expression of peroxiredoxin 2 through the activation of the Foxo3a transcription factor.	Timolol	15-22	peroxiredoxin 2	Homo sapiens	70-85
18491044-6	2008	Peroxiredoxin 2 expression was also induced in vivo and in vitro by ethanol.	Ethanol	68-75	peroxiredoxin 2	Homo sapiens	0-15
19061854-1	2009	Peroxiredoxin 2 (Prx2) is a 2-Cys peroxiredoxin extremely abundant in the erythrocyte.	2-cys peroxiredoxin	28-47	peroxiredoxin 2	Homo sapiens	0-15
19061854-1	2009	Peroxiredoxin 2 (Prx2) is a 2-Cys peroxiredoxin extremely abundant in the erythrocyte.	2-cys peroxiredoxin	28-47	peroxiredoxin 2	Homo sapiens	17-21
18491044-7	2008	Although ethanol and PACAP exert opposite effects on caspase-3 activity, inhibition of peroxiredoxin 2 expression, using siRNAs, only reduced the ability of PACAP to prevent ethanol-induced caspase-3 activity.	Ethanol	174-181	peroxiredoxin 2	Homo sapiens	87-102
18718523-0	2008	Decreasing peroxiredoxin II expression decreases glutathione, alters cell cycle distribution, and sensitizes glioma cells to ionizing radiation and H(2)O(2).	Glutathione	49-60	peroxiredoxin 2	Homo sapiens	11-27
18718523-6	2008	Analysis of the redox environment revealed that decreasing Prx II increased intracellular reactive oxygen species in 36B10 cells; extracellular levels of H(2)O(2) were also increased in both C6 and 36B10 cells.	Reactive Oxygen Species	90-113	peroxiredoxin 2	Homo sapiens	59-65
18718523-7	2008	Treatment with H(2)O(2) led to a further elevation in intracellular reactive oxygen species in cells where Prx II was decreased.	Hydrogen Peroxide	15-23	peroxiredoxin 2	Homo sapiens	107-113
18718523-7	2008	Treatment with H(2)O(2) led to a further elevation in intracellular reactive oxygen species in cells where Prx II was decreased.	Reactive Oxygen Species	68-91	peroxiredoxin 2	Homo sapiens	107-113
18718523-9	2008	Furthermore, lowering Prx II expression decreased intracellular glutathione and resulted in a significant decline in glutathione reductase activity, suggesting a possible mechanism for the observed increased sensitivity to oxidative insults.	Glutathione	64-75	peroxiredoxin 2	Homo sapiens	22-28
18387321-5	2008	Human erythrocyte Prx2 is a peroxiredoxin with thiol-specific antioxidant activity.	Sulfhydryl Compounds	47-52	peroxiredoxin 2	Homo sapiens	18-22
18578994-4	2008	Furthermore, dichlorodihydrofluorescein diacetate (DCFH-DA) and thiobarbituric acid (TBA) assays, for measuring the products of oxidative reaction, such as the reactive oxygen species (ROS) and malondialdehyde (MDA), were applied to explore whether the antioxidant mechanism was involved in the effects of PrxII functioning on Hep3B cell.	Reactive Oxygen Species	160-183	peroxiredoxin 2	Homo sapiens	306-311
18578994-8	2008	The levels of endogenous ROS and MDA were significantly higher in the two PrxII-silent groups than those in the mock and blank control groups (P less than 0.05).	Reactive Oxygen Species	25-28	peroxiredoxin 2	Homo sapiens	74-79
17964282-3	2007	Valsartan, a selective Ang II type 1 (AT1) receptor blocker, and N-acetylcysteine, an antioxidant, inhibited both of these modifications, indicating the contribution of AT1 receptor and reactive oxygen species to oxidation of Prx2 and phosphorylation of GRP58 by Ang II.	Valsartan	0-9	peroxiredoxin 2	Homo sapiens	226-230
18833106-1	2008	Zoloft (sertraline) is an original antidepressant of "Pfizer", torin is a generic form of sertraline of Veropharm.	Sertraline	90-100	peroxiredoxin 2	Homo sapiens	63-68
17964282-3	2007	Valsartan, a selective Ang II type 1 (AT1) receptor blocker, and N-acetylcysteine, an antioxidant, inhibited both of these modifications, indicating the contribution of AT1 receptor and reactive oxygen species to oxidation of Prx2 and phosphorylation of GRP58 by Ang II.	Acetylcysteine	65-81	peroxiredoxin 2	Homo sapiens	226-230
17964282-3	2007	Valsartan, a selective Ang II type 1 (AT1) receptor blocker, and N-acetylcysteine, an antioxidant, inhibited both of these modifications, indicating the contribution of AT1 receptor and reactive oxygen species to oxidation of Prx2 and phosphorylation of GRP58 by Ang II.	Reactive Oxygen Species	186-209	peroxiredoxin 2	Homo sapiens	226-230
17163455-8	2007	In addition, we found that Prx I and II transfection enabled MCF10A cells to resist H2O2-induced cell death.	Hydrogen Peroxide	84-88	peroxiredoxin 2	Homo sapiens	27-39
18022079-6	2007	RESULTS: Among 11 differentially expressed proteins, we identified 2 locally produced factors: peroxiredoxin II (PRXII), exclusively expressed in BOS; and surfactant protein A (SP-A), expressed consistently less in BOS patients than in stable LTRs.	N-[4-(Aminosulfonyl)phenyl]-2-Mercaptobenzamide	146-149	peroxiredoxin 2	Homo sapiens	95-111
18022079-6	2007	RESULTS: Among 11 differentially expressed proteins, we identified 2 locally produced factors: peroxiredoxin II (PRXII), exclusively expressed in BOS; and surfactant protein A (SP-A), expressed consistently less in BOS patients than in stable LTRs.	N-[4-(Aminosulfonyl)phenyl]-2-Mercaptobenzamide	146-149	peroxiredoxin 2	Homo sapiens	113-118
18003920-3	2007	Here we report that Prx2 is S-nitrosylated (forming SNO-Prx2) by reaction with nitric oxide at two critical cysteine residues (C51 and C172), preventing its reaction with peroxides.	Nitric Oxide	79-91	peroxiredoxin 2	Homo sapiens	20-24
18003920-3	2007	Here we report that Prx2 is S-nitrosylated (forming SNO-Prx2) by reaction with nitric oxide at two critical cysteine residues (C51 and C172), preventing its reaction with peroxides.	Nitric Oxide	79-91	peroxiredoxin 2	Homo sapiens	56-60
18003920-3	2007	Here we report that Prx2 is S-nitrosylated (forming SNO-Prx2) by reaction with nitric oxide at two critical cysteine residues (C51 and C172), preventing its reaction with peroxides.	Cysteine	108-116	peroxiredoxin 2	Homo sapiens	20-24
18003920-3	2007	Here we report that Prx2 is S-nitrosylated (forming SNO-Prx2) by reaction with nitric oxide at two critical cysteine residues (C51 and C172), preventing its reaction with peroxides.	Cysteine	108-116	peroxiredoxin 2	Homo sapiens	56-60
18003920-3	2007	Here we report that Prx2 is S-nitrosylated (forming SNO-Prx2) by reaction with nitric oxide at two critical cysteine residues (C51 and C172), preventing its reaction with peroxides.	Peroxides	171-180	peroxiredoxin 2	Homo sapiens	20-24
17692604-5	2007	Three of the proteins belong to the Peroxiredoxin family of hydroperoxide scavengers, PrxI, PrxII, and Prx VI, that showed changes in their pI as result of hyperoxidation.	Hydrogen Peroxide	60-73	peroxiredoxin 2	Homo sapiens	92-97
17292933-8	2007	Quercetin inhibited both BaP-mediated effects on Prx I and II in 22Rv1 cells.	Quercetin	0-9	peroxiredoxin 2	Homo sapiens	49-61
17329258-0	2007	The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents.	Hydrogen Peroxide	44-52	peroxiredoxin 2	Homo sapiens	23-38
17329258-0	2007	The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents.	Sulfhydryl Compounds	110-115	peroxiredoxin 2	Homo sapiens	23-38
17329258-1	2007	Peroxiredoxin 2 is a member of the mammalian peroxiredoxin family of thiol proteins that is important in antioxidant defense and redox signaling.	Sulfhydryl Compounds	69-74	peroxiredoxin 2	Homo sapiens	0-15
17329258-3	2007	Human erythrocyte peroxiredoxin 2 was oxidized stoichiometrically to its disulfide-bonded homodimer by hydrogen peroxide, as monitored electrophoretically under nonreducing conditions.	Disulfides	73-82	peroxiredoxin 2	Homo sapiens	18-33
17329258-3	2007	Human erythrocyte peroxiredoxin 2 was oxidized stoichiometrically to its disulfide-bonded homodimer by hydrogen peroxide, as monitored electrophoretically under nonreducing conditions.	Hydrogen Peroxide	103-120	peroxiredoxin 2	Homo sapiens	18-33
17329258-6	2007	Experiments measuring inhibition of dimerization indicated that at pH 7.4 catalase and peroxiredoxin 2 react with hydrogen peroxide at comparable rates.	Hydrogen Peroxide	114-131	peroxiredoxin 2	Homo sapiens	87-102
17329258-12	2007	The alkylating agent iodoacetamide also reacted extremely slowly with peroxiredoxin 2.	Iodoacetamide	21-34	peroxiredoxin 2	Homo sapiens	70-85
17329258-13	2007	These results demonstrate that peroxiredoxin 2 has a tertiary structure that facilitates reaction of the active site thiol with hydrogen peroxide while restricting its reactivity with other thiol reagents.	Sulfhydryl Compounds	117-122	peroxiredoxin 2	Homo sapiens	31-46
17329258-13	2007	These results demonstrate that peroxiredoxin 2 has a tertiary structure that facilitates reaction of the active site thiol with hydrogen peroxide while restricting its reactivity with other thiol reagents.	Hydrogen Peroxide	128-145	peroxiredoxin 2	Homo sapiens	31-46
17329258-13	2007	These results demonstrate that peroxiredoxin 2 has a tertiary structure that facilitates reaction of the active site thiol with hydrogen peroxide while restricting its reactivity with other thiol reagents.	Sulfhydryl Compounds	190-195	peroxiredoxin 2	Homo sapiens	31-46
17522728-12	2007	Finally, most membrane proteins of cryopreserved red blood cells were similar to the membrane proteins of fresh red blood cells, but trehalose can result in loss of glyceraldehyde phosphate dehydrogenase (GAPD) and peroxiredoxin 2.	Trehalose	133-142	peroxiredoxin 2	Homo sapiens	215-230
21136693-7	2007	Further biochemical studies demonstrated that AE enhanced the intracellular level of reactive oxygen species and oxidation of PRDX-2, -4, and DJ-1.	aloe emodin	46-48	peroxiredoxin 2	Homo sapiens	126-132
17105810-0	2007	Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte.	Hydrogen Peroxide	67-84	peroxiredoxin 2	Homo sapiens	0-15
17105810-3	2007	In contrast to Prx2 in Jurkat T lymphocytes, Prx2 was resistant to overoxidation (oxidation of the cysteine thiol to a sulfinic/sulfonic acid) in erythrocytes.	cysteine thiol	99-113	peroxiredoxin 2	Homo sapiens	45-49
17105810-3	2007	In contrast to Prx2 in Jurkat T lymphocytes, Prx2 was resistant to overoxidation (oxidation of the cysteine thiol to a sulfinic/sulfonic acid) in erythrocytes.	sulfinic/sulfonic acid	119-141	peroxiredoxin 2	Homo sapiens	45-49
17105810-7	2007	We also found that Prx2 was oxidized by endogenously generated H(2)O(2), which was mainly derived from hemoglobin autoxidation.	Hydrogen Peroxide	63-71	peroxiredoxin 2	Homo sapiens	19-23
17105810-8	2007	Our results demonstrate that in the erythrocyte Prx2 is extremely efficient at scavenging H(2)O(2) noncatalytically.	Hydrogen Peroxide	90-98	peroxiredoxin 2	Homo sapiens	48-52
16690325-6	2007	The deduced amino acids of the two genes are highly homologous with mammalian NKEF-A and NKEF-B proteins, including two well conserved Val-Cys-Pro (VCP) motifs.	Val-Cys-Pro	135-146	peroxiredoxin 2	Homo sapiens	89-95
17145963-4	2006	In contrast, H2O2-dependent cell cycle arrest was correlated with hyperoxidation of PrxII, which resulted in quantitative recruitment of approximately 66- and approximately 140-kD PrxII complexes into large filamentous oligomers.	Hydrogen Peroxide	13-17	peroxiredoxin 2	Homo sapiens	84-89
16839769-1	2007	The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol.	Carbon	148-154	peroxiredoxin 2	Homo sapiens	45-60
16839769-1	2007	The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol.	Carbon	148-154	peroxiredoxin 2	Homo sapiens	62-67
16839769-1	2007	The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol.	ammonium molybdate	189-207	peroxiredoxin 2	Homo sapiens	45-60
16839769-1	2007	The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol.	ammonium molybdate	189-207	peroxiredoxin 2	Homo sapiens	62-67
16839769-1	2007	The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol.	Polyethylene Glycols	212-231	peroxiredoxin 2	Homo sapiens	45-60
16839769-1	2007	The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol.	Polyethylene Glycols	212-231	peroxiredoxin 2	Homo sapiens	62-67
17145963-4	2006	In contrast, H2O2-dependent cell cycle arrest was correlated with hyperoxidation of PrxII, which resulted in quantitative recruitment of approximately 66- and approximately 140-kD PrxII complexes into large filamentous oligomers.	Hydrogen Peroxide	13-17	peroxiredoxin 2	Homo sapiens	180-185
15941719-1	2005	Although biochemical properties of 2-Cys peroxiredoxins (Prxs) have been extensively studied, their real physiological functions in higher eukaryotic cells remain obscure and certainly warrant further study.	2-cys	35-40	peroxiredoxin 2	Homo sapiens	41-55
16597467-0	2006	2-Cys Peroxiredoxin TPx-1 is involved in gametocyte development in Plasmodium berghei.	2-cys	0-5	peroxiredoxin 2	Homo sapiens	20-25
16178011-0	2006	Elucidation of ATP-stimulated stress protein expression of RBA-2 type-2 astrocytes: ATP potentiate HSP60 and Cu/Zn SOD expression and stimulates pI shift of peroxiredoxin II.	Adenosine Triphosphate	15-18	peroxiredoxin 2	Homo sapiens	157-173
16178011-0	2006	Elucidation of ATP-stimulated stress protein expression of RBA-2 type-2 astrocytes: ATP potentiate HSP60 and Cu/Zn SOD expression and stimulates pI shift of peroxiredoxin II.	Adenosine Triphosphate	84-87	peroxiredoxin 2	Homo sapiens	157-173
16178011-9	2006	ATP and exogenous H2O2 stimulated Prx II shifting from oxidized form to reduced form.	Adenosine Triphosphate	0-3	peroxiredoxin 2	Homo sapiens	34-40
16178011-9	2006	ATP and exogenous H2O2 stimulated Prx II shifting from oxidized form to reduced form.	Hydrogen Peroxide	18-22	peroxiredoxin 2	Homo sapiens	34-40
16288023-7	2005	The up-regulation of the PrxII protein in radioresistant cancer cells suggested that human peroxiredoxin plays an important role in eliminating the generation of reactive oxygen species by ionizing radiation.	Reactive Oxygen Species	162-185	peroxiredoxin 2	Homo sapiens	25-30
16288023-8	2005	The present finding, together with the observation that PrxII is also up-regulated in response to ionizing radiation in other cell systems, strengthens the hypothesis that the PrxII antioxidant protein is involved in the cellular response to ionizing radiation and functions to reduce the intracellular reactive oxygen species levels, resulting in increased resistance of breast cancer cells to ionizing radiation.	Reactive Oxygen Species	303-326	peroxiredoxin 2	Homo sapiens	56-61
16288023-8	2005	The present finding, together with the observation that PrxII is also up-regulated in response to ionizing radiation in other cell systems, strengthens the hypothesis that the PrxII antioxidant protein is involved in the cellular response to ionizing radiation and functions to reduce the intracellular reactive oxygen species levels, resulting in increased resistance of breast cancer cells to ionizing radiation.	Reactive Oxygen Species	303-326	peroxiredoxin 2	Homo sapiens	176-181
16307478-2	2005	As novel electron acceptor of reduced TPx1, we characterised peroxynitrite; the rate constant for ONOO- reduction by the enzyme (1 x 10(6) M(-1) s(-1) at pH 7.4 and 37 degrees C) was determined by stopped-flow measurements.	onoo	98-102	peroxiredoxin 2	Homo sapiens	38-42
16307478-6	2005	For the catalytic cycle of TPx1, we conclude that oxidation of the peroxidatic Cys50 by the oxidising substrate is followed by the formation of an intermolecular disulfide bond between Cys50 and Cys170" of the second subunit, which is then attacked by an external electron donor such as thioredoxin or plasmoredoxin.	Disulfides	162-171	peroxiredoxin 2	Homo sapiens	27-31
16932348-6	2006	Reduced expression of PRDX2 validated at the mRNA and protein level, in topo IIbeta-deficient cells correlated with increased accumulation of reactive oxygen species (ROS) following ATRA-induced differentiation.	Reactive Oxygen Species	142-165	peroxiredoxin 2	Homo sapiens	22-27
16932348-6	2006	Reduced expression of PRDX2 validated at the mRNA and protein level, in topo IIbeta-deficient cells correlated with increased accumulation of reactive oxygen species (ROS) following ATRA-induced differentiation.	Reactive Oxygen Species	167-170	peroxiredoxin 2	Homo sapiens	22-27
16932348-6	2006	Reduced expression of PRDX2 validated at the mRNA and protein level, in topo IIbeta-deficient cells correlated with increased accumulation of reactive oxygen species (ROS) following ATRA-induced differentiation.	Tretinoin	182-186	peroxiredoxin 2	Homo sapiens	22-27
16932348-7	2006	Overexpression of PRDX2 in topo IIbeta-deficient cells led to reduced accumulation of ROS and partially reversed ATRA-induced apoptosis.	Reactive Oxygen Species	86-89	peroxiredoxin 2	Homo sapiens	18-23
16932348-7	2006	Overexpression of PRDX2 in topo IIbeta-deficient cells led to reduced accumulation of ROS and partially reversed ATRA-induced apoptosis.	Tretinoin	113-117	peroxiredoxin 2	Homo sapiens	18-23
16932348-10	2006	Thus, suppression of topo IIbeta and/or PRDX2 levels in myeloid leukemia cells provides a novel approach for improving ATRA-based differentiation therapy.	Tretinoin	119-123	peroxiredoxin 2	Homo sapiens	40-45
16307478-1	2005	Thioredoxin peroxidase 1 (TPx1) of the malarial parasite Plasmodium falciparum is a 2-Cys peroxiredoxin involved in the detoxification of reactive oxygen species and - as shown here - of reactive nitrogen species.	2-cys peroxiredoxin	84-103	peroxiredoxin 2	Homo sapiens	26-30
16307478-1	2005	Thioredoxin peroxidase 1 (TPx1) of the malarial parasite Plasmodium falciparum is a 2-Cys peroxiredoxin involved in the detoxification of reactive oxygen species and - as shown here - of reactive nitrogen species.	Reactive Oxygen Species	138-161	peroxiredoxin 2	Homo sapiens	26-30
16307478-1	2005	Thioredoxin peroxidase 1 (TPx1) of the malarial parasite Plasmodium falciparum is a 2-Cys peroxiredoxin involved in the detoxification of reactive oxygen species and - as shown here - of reactive nitrogen species.	Reactive Nitrogen Species	187-212	peroxiredoxin 2	Homo sapiens	26-30
16307478-2	2005	As novel electron acceptor of reduced TPx1, we characterised peroxynitrite; the rate constant for ONOO- reduction by the enzyme (1 x 10(6) M(-1) s(-1) at pH 7.4 and 37 degrees C) was determined by stopped-flow measurements.	Peroxynitrous Acid	61-74	peroxiredoxin 2	Homo sapiens	38-42
15941719-2	2005	Here we demonstrated that human (h) PrxII, a cytosolic isotype of human 2-Cys Prx, has dual functions as a peroxidase and a molecular chaperone, and that these different functions are closely associated with its adoption of distinct protein structures.	2-cys	72-77	peroxiredoxin 2	Homo sapiens	36-41
15801906-8	2005	At 20 microM H2O2, changes were fewer, but GAPDH and peroxiredoxin 2 were still modified.	Hydrogen Peroxide	13-17	peroxiredoxin 2	Homo sapiens	53-68
15977174-9	2005	Peroxiredoxin II (Prx II), a protein that is involved in eliminating reactive oxygen species (ROS), showed increased expression intensity in p53Y220S fibroblasts after DX treatment, as observed by two-dimensional electrophoresis analysis.	Reactive Oxygen Species	69-92	peroxiredoxin 2	Homo sapiens	18-24
16045763-0	2005	Peroxiredoxin II functions as a signal terminator for H2O2-activated phospholipase D1.	Hydrogen Peroxide	54-58	peroxiredoxin 2	Homo sapiens	0-16
16045763-4	2005	A novel interaction with peroxiredoxin II (PrxII), an enzyme that eliminates cellular H2O2, which is a known stimulator of PLD1, was identified by PLD1-affinity pull-down and MS. PMA stimulation was confirmed to promote physical interaction between PLD1 and PrxII and to cause PLD1 and PrxII to colocalize subcellularly.	Hydrogen Peroxide	86-90	peroxiredoxin 2	Homo sapiens	25-41
16045763-4	2005	A novel interaction with peroxiredoxin II (PrxII), an enzyme that eliminates cellular H2O2, which is a known stimulator of PLD1, was identified by PLD1-affinity pull-down and MS. PMA stimulation was confirmed to promote physical interaction between PLD1 and PrxII and to cause PLD1 and PrxII to colocalize subcellularly.	Hydrogen Peroxide	86-90	peroxiredoxin 2	Homo sapiens	43-48
16045763-4	2005	A novel interaction with peroxiredoxin II (PrxII), an enzyme that eliminates cellular H2O2, which is a known stimulator of PLD1, was identified by PLD1-affinity pull-down and MS. PMA stimulation was confirmed to promote physical interaction between PLD1 and PrxII and to cause PLD1 and PrxII to colocalize subcellularly.	Hydrogen Peroxide	86-90	peroxiredoxin 2	Homo sapiens	258-263
16045763-4	2005	A novel interaction with peroxiredoxin II (PrxII), an enzyme that eliminates cellular H2O2, which is a known stimulator of PLD1, was identified by PLD1-affinity pull-down and MS. PMA stimulation was confirmed to promote physical interaction between PLD1 and PrxII and to cause PLD1 and PrxII to colocalize subcellularly.	Hydrogen Peroxide	86-90	peroxiredoxin 2	Homo sapiens	258-263
16045763-5	2005	Functional significance of the interaction was suggested by the observation that over-expression of PrxII specifically reduces the response of PLD1 to stimulation by H2O2.	Hydrogen Peroxide	166-170	peroxiredoxin 2	Homo sapiens	100-105
16045763-6	2005	These results indicate that PrxII may have a signal-terminating role for PLD1 by being recruited to sites containing activated PLD1 after cellular stimulation involving production of H2O2.	Hydrogen Peroxide	183-187	peroxiredoxin 2	Homo sapiens	28-33
15977174-9	2005	Peroxiredoxin II (Prx II), a protein that is involved in eliminating reactive oxygen species (ROS), showed increased expression intensity in p53Y220S fibroblasts after DX treatment, as observed by two-dimensional electrophoresis analysis.	Reactive Oxygen Species	94-97	peroxiredoxin 2	Homo sapiens	18-24
15936593-3	2005	We found most extensive and reproducible down-regulation of NADP dependent isocitrate dehydrogenase cytoplasmic (IDPc) and peroxiredoxin-II (Prx-II), in poorly differentiated T24 compared to well-differentiated RT4 bladder cancer cell line.	NADP	60-64	peroxiredoxin 2	Homo sapiens	141-147
16188094-0	2005	[Identification of protein peroxiredoxin 2 related to crystalline NiS-induced neoplastic transformation].	Nickel	66-69	peroxiredoxin 2	Homo sapiens	27-42
16188094-6	2005	CONCLUSION: PDX2 was involved in malignant transformation of human bronchial epithelial cell induced by crystalline nickel sulfide.	nickel sulfide	116-130	peroxiredoxin 2	Homo sapiens	12-16
15902258-2	2005	Mammalian 2-Cys peroxiredoxin type II (Prx II; gene symbol Prdx2) is a cellular peroxidase that eliminates endogenous H2O2 produced in response to growth factors such as PDGF and epidermal growth factor; however, its involvement in growth factor signalling is largely unknown.	2-cys	10-15	peroxiredoxin 2	Homo sapiens	16-45
15902258-2	2005	Mammalian 2-Cys peroxiredoxin type II (Prx II; gene symbol Prdx2) is a cellular peroxidase that eliminates endogenous H2O2 produced in response to growth factors such as PDGF and epidermal growth factor; however, its involvement in growth factor signalling is largely unknown.	2-cys	10-15	peroxiredoxin 2	Homo sapiens	59-64
15902258-2	2005	Mammalian 2-Cys peroxiredoxin type II (Prx II; gene symbol Prdx2) is a cellular peroxidase that eliminates endogenous H2O2 produced in response to growth factors such as PDGF and epidermal growth factor; however, its involvement in growth factor signalling is largely unknown.	Hydrogen Peroxide	118-122	peroxiredoxin 2	Homo sapiens	16-45
15902258-2	2005	Mammalian 2-Cys peroxiredoxin type II (Prx II; gene symbol Prdx2) is a cellular peroxidase that eliminates endogenous H2O2 produced in response to growth factors such as PDGF and epidermal growth factor; however, its involvement in growth factor signalling is largely unknown.	Hydrogen Peroxide	118-122	peroxiredoxin 2	Homo sapiens	59-64
15788230-7	2005	Three of these proteins belong to the Peroxiredoxin family of hydroperoxide scavengers, namely PrxI, PrxII and PrxVI, that showed changes in their pI as result of overoxidation.	Hydrogen Peroxide	62-75	peroxiredoxin 2	Homo sapiens	101-106
11877442-4	2002	In its disulfide form, the 13-kDa protein thioredoxin-2 is a substrate of thioredoxin reductase-1 (K(m) = 5.2 microm, k(cat) = 14.5 s(-1)) and in its dithiol form, an electron donor for TPx-1 (K(m) = 9 microm, k(cat) = 5.4 s(-1)).	Disulfides	7-16	peroxiredoxin 2	Homo sapiens	186-191
11904290-4	2002	Peroxiredoxins are enzymes catalyzing the destruction of peroxides.	Peroxides	57-66	peroxiredoxin 2	Homo sapiens	0-14
11904290-6	2002	Cellular thiols (e.g. thioredoxin) are used to regenerate the peroxiredoxins to their active state.	Sulfhydryl Compounds	9-15	peroxiredoxin 2	Homo sapiens	62-76
11904290-9	2002	This strongly suggested that peroxiredoxins behave as a dam upon oxidative stress, being both important peroxide-destroying enzymes and peroxide targets.	Peroxides	104-112	peroxiredoxin 2	Homo sapiens	29-43
11904290-9	2002	This strongly suggested that peroxiredoxins behave as a dam upon oxidative stress, being both important peroxide-destroying enzymes and peroxide targets.	Peroxides	136-144	peroxiredoxin 2	Homo sapiens	29-43
12960131-9	2003	CONCLUSIONS: In conclusion, we found that expression of peroxiredoxins, especially III, IV and V, is increased in breast malignancy, suggesting the induction of Prxs as response to increased production of reactive oxygen species in carcinomatous tissue.	Reactive Oxygen Species	205-228	peroxiredoxin 2	Homo sapiens	56-70
12515392-1	2002	Peroxiredoxin II (Prx II) is known not only to protect cells from oxidative damage caused by hydrogen peroxide (H202), but also to endow cancer cells with resistance to both H202 and cisplatin and to grant them radioresistance.	Hydrogen Peroxide	93-110	peroxiredoxin 2	Homo sapiens	18-24
12515392-1	2002	Peroxiredoxin II (Prx II) is known not only to protect cells from oxidative damage caused by hydrogen peroxide (H202), but also to endow cancer cells with resistance to both H202 and cisplatin and to grant them radioresistance.	h202	112-116	peroxiredoxin 2	Homo sapiens	18-24
12515392-1	2002	Peroxiredoxin II (Prx II) is known not only to protect cells from oxidative damage caused by hydrogen peroxide (H202), but also to endow cancer cells with resistance to both H202 and cisplatin and to grant them radioresistance.	Cisplatin	183-192	peroxiredoxin 2	Homo sapiens	18-24
12515392-2	2002	In this study, we examined whether Prx II antisense could enhance cisplatin-induced cell death.	Cisplatin	66-75	peroxiredoxin 2	Homo sapiens	35-41
12515392-3	2002	When gastric cancer cells were transfected with various concentrations of Prx II antisense plasmid, pPrxII/AS, and then treated with the same concentrations of cisplatin, Prx II antisense enhanced cisplatin-induced cell death.	Cisplatin	197-206	peroxiredoxin 2	Homo sapiens	74-80
12515392-3	2002	When gastric cancer cells were transfected with various concentrations of Prx II antisense plasmid, pPrxII/AS, and then treated with the same concentrations of cisplatin, Prx II antisense enhanced cisplatin-induced cell death.	Cisplatin	197-206	peroxiredoxin 2	Homo sapiens	171-177
12515392-4	2002	The combination index (CI) at all doses of the combination was below 1, indicating that Prx II antisense sensitized cisplatin-induced cell death.	Cisplatin	116-125	peroxiredoxin 2	Homo sapiens	88-94
12515392-6	2002	Our present results, therefore, suggest that Prx II antisense would be a very good sensitizer for cisplatin, and that Prx II as a target for chemosensitizers constitutes a promising avenue for future research.	Cisplatin	98-107	peroxiredoxin 2	Homo sapiens	45-51
11469800-0	2001	Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin.	Dexamethasone	206-219	peroxiredoxin 2	Homo sapiens	0-24
11697128-1	2001	We previously found hydroperoxide-responsive proteins (HPRPs), which are comprised of peroxiredoxin I (Prx I), Prx II, Prx III, Prx VI, HSP27, G3PDH and two unidentified proteins (HPRP-2" and HPRP-5"), in human umbilical vein endothelial cells.	Hydrogen Peroxide	20-33	peroxiredoxin 2	Homo sapiens	111-117
11390385-9	2001	hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems.	Sulfhydryl Compounds	72-77	peroxiredoxin 2	Homo sapiens	41-47
11390385-9	2001	hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems.	Dithiothreitol	79-93	peroxiredoxin 2	Homo sapiens	41-47
11390385-9	2001	hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems.	Metals	106-111	peroxiredoxin 2	Homo sapiens	41-47
11390385-9	2001	hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems.	Ascorbic Acid	150-159	peroxiredoxin 2	Homo sapiens	41-47
11390385-10	2001	Prx II was reduced by hCyP-A without help from any other reductant, and the reduction was cyclosporin A-independent.	Cyclosporine	90-103	peroxiredoxin 2	Homo sapiens	0-6
11469800-0	2001	Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin.	Hydrogen Peroxide	154-171	peroxiredoxin 2	Homo sapiens	0-24
11469800-0	2001	Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin.	Etoposide	221-230	peroxiredoxin 2	Homo sapiens	0-24
11469800-0	2001	Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin.	Doxorubicin	236-247	peroxiredoxin 2	Homo sapiens	0-24
11469800-4	2001	Transfection of mouse WEHI7.2 lymphoma cells with human TrxP-1 or TrxP-2, but not TrxP-4, protects the cells against H(2)O(2) induced apoptosis but does not protect against apoptosis induced by dexamethasone, etoposide, or doxorubicin.	Dexamethasone	194-207	peroxiredoxin 2	Homo sapiens	56-62
11469800-4	2001	Transfection of mouse WEHI7.2 lymphoma cells with human TrxP-1 or TrxP-2, but not TrxP-4, protects the cells against H(2)O(2) induced apoptosis but does not protect against apoptosis induced by dexamethasone, etoposide, or doxorubicin.	Etoposide	209-218	peroxiredoxin 2	Homo sapiens	56-62
11469800-4	2001	Transfection of mouse WEHI7.2 lymphoma cells with human TrxP-1 or TrxP-2, but not TrxP-4, protects the cells against H(2)O(2) induced apoptosis but does not protect against apoptosis induced by dexamethasone, etoposide, or doxorubicin.	Doxorubicin	223-234	peroxiredoxin 2	Homo sapiens	56-62
11469800-5	2001	The results show that an increase in TrxP-1 expression contributes to the protection against H(2)O(2) induced apoptosis caused by Trx-1, but does not protect against apoptosis induced by other agents.	Hydrogen Peroxide	93-101	peroxiredoxin 2	Homo sapiens	37-43
11410278-1	2001	The decameric human erythrocyte protein torin is identical to the thiol-specific antioxidant protein-II (TSA-II), also termed peroxiredoxin-II (Prx-II).	Sulfhydryl Compounds	66-71	peroxiredoxin 2	Homo sapiens	40-45
11410278-1	2001	The decameric human erythrocyte protein torin is identical to the thiol-specific antioxidant protein-II (TSA-II), also termed peroxiredoxin-II (Prx-II).	Sulfhydryl Compounds	66-71	peroxiredoxin 2	Homo sapiens	126-142
11410278-1	2001	The decameric human erythrocyte protein torin is identical to the thiol-specific antioxidant protein-II (TSA-II), also termed peroxiredoxin-II (Prx-II).	Sulfhydryl Compounds	66-71	peroxiredoxin 2	Homo sapiens	144-150
11410278-2	2001	Single particle analysis from electron micrographs of Prx-II molecules homogeneously orientated across holes in the presence of a thin film of ammonium molybdate and trehalose has facilitated the production of a &gt;/=20 A 3-D reconstruction by angular reconstitution that emphasises the D5 symmetry of the ring-like decamer.	ammonium molybdate	143-161	peroxiredoxin 2	Homo sapiens	54-60
11410278-2	2001	Single particle analysis from electron micrographs of Prx-II molecules homogeneously orientated across holes in the presence of a thin film of ammonium molybdate and trehalose has facilitated the production of a &gt;/=20 A 3-D reconstruction by angular reconstitution that emphasises the D5 symmetry of the ring-like decamer.	Trehalose	166-175	peroxiredoxin 2	Homo sapiens	54-60
11410278-6	2001	2-D crystallisation of the Prx-II protein on mica as part of a TEM study resulted in the formation of a p2 crystal form with parallel linear arrays of stacked rings.	mica	45-49	peroxiredoxin 2	Homo sapiens	27-33
11396151-1	2001	Peroxiredoxin II (Prx II) has been known to be induced by various oxidative stimuli and to play an important protective role from oxidative damage by hydrogen peroxide (H2O2).	Hydrogen Peroxide	150-167	peroxiredoxin 2	Homo sapiens	0-24
11396151-1	2001	Peroxiredoxin II (Prx II) has been known to be induced by various oxidative stimuli and to play an important protective role from oxidative damage by hydrogen peroxide (H2O2).	Hydrogen Peroxide	169-173	peroxiredoxin 2	Homo sapiens	0-24
11396151-2	2001	In this study, we observed that cisplatin as well as H2O2 induced Prx II expression.	Cisplatin	32-41	peroxiredoxin 2	Homo sapiens	66-72
11396151-2	2001	In this study, we observed that cisplatin as well as H2O2 induced Prx II expression.	Hydrogen Peroxide	53-57	peroxiredoxin 2	Homo sapiens	66-72
11396151-3	2001	To examine the correlation between the increased expression of Prx II and chemoresistance, we prepared a Prx II-overexpressing cell line, SNU638 cells, and found it to be more resistant to cell death induced by cisplatin and H2O2 than neo-transfectant cells.	Hydrogen Peroxide	225-229	peroxiredoxin 2	Homo sapiens	63-69
11396151-4	2001	We also observed that enhanced expression of Prx II inhibited cisplatin- and H2O2-induced apoptosis, demonstrating that resistance to these cytotoxic agents was due to inhibition of apoptosis.	Cisplatin	62-71	peroxiredoxin 2	Homo sapiens	45-51
11396151-4	2001	We also observed that enhanced expression of Prx II inhibited cisplatin- and H2O2-induced apoptosis, demonstrating that resistance to these cytotoxic agents was due to inhibition of apoptosis.	Hydrogen Peroxide	77-81	peroxiredoxin 2	Homo sapiens	45-51
11396151-5	2001	The above results led us to suggest that the overexpressed Prx II protein inhibits cisplatin-induced apoptosis, thereby contributing to chemoresistance of tumor cells, especially to oxidative stress producing anticancer drugs.	Cisplatin	83-92	peroxiredoxin 2	Homo sapiens	59-65
10494109-7	1999	We have examined regional and cell-type-specific expression of Prx-I and Prx-II in paraffin sections of human brain using immunohistochemical methods.	Paraffin	83-91	peroxiredoxin 2	Homo sapiens	73-79
9356316-2	1997	The role of NKEF-B as an antioxidant was demonstrated by its protection of transfected cells to oxidative damage by hydrogen peroxide.	Hydrogen Peroxide	116-133	peroxiredoxin 2	Homo sapiens	12-18
9602152-3	1998	Native NKEF-B readily forms disulphide-linked dimers, but when fully reduced, the protein forms discrete oligomers containing 16 +/- 1 monomers.	disulphide	28-38	peroxiredoxin 2	Homo sapiens	7-13
9602152-7	1998	This in vitro cleavage data provides support to the hypothesis that calpromotin (NKEF-B), an erythron peroxiredoxin involved in the regulation of calcium-dependent potassium transport across the plasma membrane, is cleaved by calpain in vivo.	calpromotin	68-79	peroxiredoxin 2	Homo sapiens	81-87
9602152-7	1998	This in vitro cleavage data provides support to the hypothesis that calpromotin (NKEF-B), an erythron peroxiredoxin involved in the regulation of calcium-dependent potassium transport across the plasma membrane, is cleaved by calpain in vivo.	Calcium	146-153	peroxiredoxin 2	Homo sapiens	81-87
9602152-7	1998	This in vitro cleavage data provides support to the hypothesis that calpromotin (NKEF-B), an erythron peroxiredoxin involved in the regulation of calcium-dependent potassium transport across the plasma membrane, is cleaved by calpain in vivo.	Potassium	164-173	peroxiredoxin 2	Homo sapiens	81-87
9356316-8	1997	The expression of NKEF-B mRNA was induced when the parental cell line ECV304 was treated with 2 mm HP.	histidylproline	99-101	peroxiredoxin 2	Homo sapiens	18-24
9356316-11	1997	These results demonstrate antioxidant activities of NKEF-B toward prooxidants such as alkyl hydroperoxide and MeHg.	alkyl hydroperoxide	86-105	peroxiredoxin 2	Homo sapiens	52-58
9161849-4	1997	Nkef-B-transfected cells displayed significantly lower levels of reactive oxygen species (ROS) compared with control or vector-transfected cells.	Reactive Oxygen Species	65-88	peroxiredoxin 2	Homo sapiens	0-6
9161849-4	1997	Nkef-B-transfected cells displayed significantly lower levels of reactive oxygen species (ROS) compared with control or vector-transfected cells.	Reactive Oxygen Species	90-93	peroxiredoxin 2	Homo sapiens	0-6
9161849-5	1997	Tert-Butylhydroperoxide-induced ROS was 15% lower in nkef-B-transfected cells and cytotoxicity was slightly, though not significantly, lower.	Reactive Oxygen Species	32-35	peroxiredoxin 2	Homo sapiens	53-59
9161849-7	1997	NKEF-B overexpression resulted in slightly (approximately 10%) lower levels of cellular glutathione (GSH) and had no effect on rate or extent of GSH depletion following either diethylmaleate (DEM) or buthionine sulfoximine (BSO) treatment.	Glutathione	88-99	peroxiredoxin 2	Homo sapiens	0-6
9161849-7	1997	NKEF-B overexpression resulted in slightly (approximately 10%) lower levels of cellular glutathione (GSH) and had no effect on rate or extent of GSH depletion following either diethylmaleate (DEM) or buthionine sulfoximine (BSO) treatment.	Glutathione	101-104	peroxiredoxin 2	Homo sapiens	0-6
9161849-8	1997	Lipid peroxidation, assessed as thiobarbituric acid-reactive substances, was 40% lower in nkef-B-transfected cells compared with vector-only-transfected cells.	thiobarbituric acid	32-51	peroxiredoxin 2	Homo sapiens	90-96
9161849-8	1997	Lipid peroxidation, assessed as thiobarbituric acid-reactive substances, was 40% lower in nkef-B-transfected cells compared with vector-only-transfected cells.	substance S	61-71	peroxiredoxin 2	Homo sapiens	90-96
9161849-9	1997	DEM-induced lipid peroxidation was suppressed by NKEF-B at DEM concentrations of 20 microM to 1 mM.	diethyl maleate	0-3	peroxiredoxin 2	Homo sapiens	49-55
9161849-9	1997	DEM-induced lipid peroxidation was suppressed by NKEF-B at DEM concentrations of 20 microM to 1 mM.	diethyl maleate	59-62	peroxiredoxin 2	Homo sapiens	49-55
9161849-11	1997	NKEF-B expression also protected cells against menadione-induced inhibition of [3H]-thymidine uptake.	Vitamin K 3	47-56	peroxiredoxin 2	Homo sapiens	0-6
9161849-11	1997	NKEF-B expression also protected cells against menadione-induced inhibition of [3H]-thymidine uptake.	Tritium	80-82	peroxiredoxin 2	Homo sapiens	0-6
9161849-11	1997	NKEF-B expression also protected cells against menadione-induced inhibition of [3H]-thymidine uptake.	Thymidine	84-93	peroxiredoxin 2	Homo sapiens	0-6
8554508-1	1995	The acidic peroxidoxin [also named thiol-specific antioxidant protein (TSA) or protector protein (PRP)], which plays a role in the response against oxidative stress, is one of the major proteins of red blood cells.	Sulfhydryl Compounds	35-40	peroxiredoxin 2	Homo sapiens	79-96
8994946-1	1996	The CPI PRxII is a recently approved, multitiered implantable cardioverter defibrillator (ICD) that delivers high and low energy biphasic shocks, antitachycardia (ATP) and bradycardia pacing, and stores 2.5 minutes of electrograms from the widely spaced shocking electrodes.	Adenosine Triphosphate	163-166	peroxiredoxin 2	Homo sapiens	8-13
8994946-12	1996	We conclude the PRxII achieves low DFTs that obviate the need for thoracotomy and effectively treats ventricular arrhythmias with ATP and shock, with programming guided by noninvasive electrophysiology.	Adenosine Triphosphate	130-133	peroxiredoxin 2	Homo sapiens	16-21
8554508-1	1995	The acidic peroxidoxin [also named thiol-specific antioxidant protein (TSA) or protector protein (PRP)], which plays a role in the response against oxidative stress, is one of the major proteins of red blood cells.	Sulfhydryl Compounds	35-40	peroxiredoxin 2	Homo sapiens	98-101
7785299-9	1995	We conclude that there is a high efficacy rate in AE termination by the Ventak PRxII, using ATP or countershock.	Adenosine Triphosphate	92-95	peroxiredoxin 2	Homo sapiens	79-84
7607688-9	1995	Oxygen radical metabolism has been hypothesized to be important for cancer, muscular dystrophy, and other disorders, so TDPX1 should be considered a candidate gene for these diseases.	Reactive Oxygen Species	0-14	peroxiredoxin 2	Homo sapiens	120-125
34340028-0	2021	Thiol-disulphide independent in-cell trapping for the identification of peroxiredoxin 2 interactors.	thiol-disulphide	0-16	peroxiredoxin 2	Homo sapiens	72-87
1919738-6	1991	In comparison to conventional monoexponential fitting of 11C-acetate tissue kinetics, the model approach improved the correlation coefficients of scintigraphic MVO2 estimates and PRP values from 0.61 to 0.91.	carbon-11 acetate	57-68	peroxiredoxin 2	Homo sapiens	179-182
34852234-3	2021	Our results show that CypA forms an intramolecular disulfide bond between Cys115 and Cys161 upon oxidative stress and the oxidized cysteines in CypA are recycled to a reduced state by peroxiredoxin-2 (PRDX2).	Disulfides	51-60	peroxiredoxin 2	Homo sapiens	184-199
34852234-3	2021	Our results show that CypA forms an intramolecular disulfide bond between Cys115 and Cys161 upon oxidative stress and the oxidized cysteines in CypA are recycled to a reduced state by peroxiredoxin-2 (PRDX2).	Cysteine	131-140	peroxiredoxin 2	Homo sapiens	184-199
34852234-3	2021	Our results show that CypA forms an intramolecular disulfide bond between Cys115 and Cys161 upon oxidative stress and the oxidized cysteines in CypA are recycled to a reduced state by peroxiredoxin-2 (PRDX2).	Cysteine	131-140	peroxiredoxin 2	Homo sapiens	201-206
34785665-2	2021	Here we show that arterial glutathione peroxidases and peroxiredoxins that rapidly eliminate H2O2, have little impact on relaxation of IDO1-expressing arteries, and that purified IDO1 forms cis-WOOH in the presence of peroxiredoxin 2.	Hydrogen Peroxide	93-97	peroxiredoxin 2	Homo sapiens	55-69
34785665-2	2021	Here we show that arterial glutathione peroxidases and peroxiredoxins that rapidly eliminate H2O2, have little impact on relaxation of IDO1-expressing arteries, and that purified IDO1 forms cis-WOOH in the presence of peroxiredoxin 2.	cis-wooh	190-198	peroxiredoxin 2	Homo sapiens	55-69
34785665-4	2021	Compared with its epimer trans-WOOH and H2O2, cis-WOOH reacts slower with the major arterial forms of glutathione peroxidases and peroxiredoxins while it reacts more readily with its target, protein kinase G 1alpha.	Hydrogen Peroxide	40-44	peroxiredoxin 2	Homo sapiens	130-144
34785665-4	2021	Compared with its epimer trans-WOOH and H2O2, cis-WOOH reacts slower with the major arterial forms of glutathione peroxidases and peroxiredoxins while it reacts more readily with its target, protein kinase G 1alpha.	cis-wooh	46-54	peroxiredoxin 2	Homo sapiens	130-144
34678160-3	2022	Here we use a genetically encoded fluorescent probe for human peroxiredoxin-2 (Prx2) oxidation in screens for small-molecule compounds that modulate H2O2 pathways.	Hydrogen Peroxide	149-153	peroxiredoxin 2	Homo sapiens	79-83
33819194-8	2021	In addition, PRDX2 knockdown led to increased ROS production in CD133+CD44+ CCSCs, sensitizing CCSCs to oxidative stress and chemotherapy.	ros	46-49	peroxiredoxin 2	Homo sapiens	13-18
34340028-5	2021	Here, we explore the applicability of two thiol-disulphide independent in-cell trapping methodological approaches in combination with mass spectrometry for the identification of interaction partners of peroxiredoxin 2 (Prdx2).	thiol-disulphide	42-58	peroxiredoxin 2	Homo sapiens	202-217
34340028-5	2021	Here, we explore the applicability of two thiol-disulphide independent in-cell trapping methodological approaches in combination with mass spectrometry for the identification of interaction partners of peroxiredoxin 2 (Prdx2).	thiol-disulphide	42-58	peroxiredoxin 2	Homo sapiens	219-224
34340028-6	2021	The first is biotin-dependent proximity-labelling (BioID) with a biotin ligase A (BirA*)-fused Prdx2, which has never been applied on redox-active proteins.	Biotin	13-19	peroxiredoxin 2	Homo sapiens	95-100
34340028-7	2021	The second is crosslinker co-immunoprecipitation with an N-terminally His-tagged Prdx2.	Histidine	70-73	peroxiredoxin 2	Homo sapiens	81-86
34072455-10	2021	Increased sensitivity of Treg cells from adults with asthma to H2O2 resulted from a reduction of peroxiredoxin-2, -3, -4 and increased pERK1/2 via impaired Ca2+ response in these cells.	Hydrogen Peroxide	63-67	peroxiredoxin 2	Homo sapiens	97-120
34111615-9	2021	Additionally, we analyzed the binding of UA to human PRDX2 and Skn-1 proteins by molecular docking and microscale thermophoresis.	ursolic acid	41-43	peroxiredoxin 2	Homo sapiens	53-58
34111615-14	2021	CONCLUSION: Our findings implicate that the strong antioxidant activity of UA may exert anti-depressive effects by its interaction with the Skn-1 transcription factor, which is part of a detoxification network, and the antioxidant PRDX2 protein, which protects the organism from the detrimental effects of radical oxygen species.	ursolic acid	75-77	peroxiredoxin 2	Homo sapiens	231-236
35474765-5	2022	We have performed siRNA-mediated silencing and n-carbamoyl alanine (NCA)-mediated inhibition of PRDX2 in CHEK2-null HCT116 cells to confirm the synthetic lethal (SL) interaction between PRDX2 and CHEK2 as the cell population reduced significantly after silencing/inhibition of PRDX2.	CARBAMOYL-DL-ALA-OH	47-66	peroxiredoxin 2	Homo sapiens	96-101
35474765-5	2022	We have performed siRNA-mediated silencing and n-carbamoyl alanine (NCA)-mediated inhibition of PRDX2 in CHEK2-null HCT116 cells to confirm the synthetic lethal (SL) interaction between PRDX2 and CHEK2 as the cell population reduced significantly after silencing/inhibition of PRDX2.	nca	68-71	peroxiredoxin 2	Homo sapiens	96-101
35474765-6	2022	Additionally, treatment with NCA resulted in an increased level of total ROS in both cell types (HCT116 and CHEK2-null HCT116 cells), which further confirms that inhibition of PRDX2 results in an increased ROS level, which are mainly responsible for DNA double-strand breaks (DSBs).	nca	29-32	peroxiredoxin 2	Homo sapiens	176-181
35474765-6	2022	Additionally, treatment with NCA resulted in an increased level of total ROS in both cell types (HCT116 and CHEK2-null HCT116 cells), which further confirms that inhibition of PRDX2 results in an increased ROS level, which are mainly responsible for DNA double-strand breaks (DSBs).	ros	73-76	peroxiredoxin 2	Homo sapiens	176-181
35474765-6	2022	Additionally, treatment with NCA resulted in an increased level of total ROS in both cell types (HCT116 and CHEK2-null HCT116 cells), which further confirms that inhibition of PRDX2 results in an increased ROS level, which are mainly responsible for DNA double-strand breaks (DSBs).	ros	206-209	peroxiredoxin 2	Homo sapiens	176-181
35474765-9	2022	The findings of this study suggest that PRDX2 has a SL interaction with CHEK2, and this interaction can be exploited for the targeted cancer therapy using NCA as a drug inhibitor of PRDX2 for the therapy of colorectal cancer having CHEK2 defects.	nca	155-158	peroxiredoxin 2	Homo sapiens	40-45
35474765-9	2022	The findings of this study suggest that PRDX2 has a SL interaction with CHEK2, and this interaction can be exploited for the targeted cancer therapy using NCA as a drug inhibitor of PRDX2 for the therapy of colorectal cancer having CHEK2 defects.	nca	155-158	peroxiredoxin 2	Homo sapiens	182-187
35306694-2	2022	Prx-2 is oxidized to a disulfide covalently-bound dimer by H2 O2 , and then reduced back by the NADPH-dependent thioredoxin-thioredoxin reductase system.	Disulfides	23-32	peroxiredoxin 2	Homo sapiens	0-5
35306694-2	2022	Prx-2 is oxidized to a disulfide covalently-bound dimer by H2 O2 , and then reduced back by the NADPH-dependent thioredoxin-thioredoxin reductase system.	Hydrogen Peroxide	59-64	peroxiredoxin 2	Homo sapiens	0-5
35306694-2	2022	Prx-2 is oxidized to a disulfide covalently-bound dimer by H2 O2 , and then reduced back by the NADPH-dependent thioredoxin-thioredoxin reductase system.	NADP	96-101	peroxiredoxin 2	Homo sapiens	0-5
35306694-10	2022	Treatment with glucose attenuated slowed Prx-2 recycling in older RBCs and SCD RBCs, but not stored RBCs.	Glucose	15-22	peroxiredoxin 2	Homo sapiens	41-46