PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
22833674-8	2012	Moreover, the dynamic features associated with the electron transfer to the thioredoxin module are altered in the presence of 2-Cys Prx.	2-cys	126-131	thioredoxin	Homo sapiens	76-87
22833674-8	2012	Moreover, the dynamic features associated with the electron transfer to the thioredoxin module are altered in the presence of 2-Cys Prx.	2-cys	126-131	periaxin	Homo sapiens	132-135
22833674-9	2012	NTRC shows structural constraints that may locate the thioredoxin module in positions with different efficiencies for electron transfer, the presence of 2-Cys Prx shifting the conformational equilibrium of the thioredoxin module to a specific position, which is not the most efficient.	2-cys	153-158	periaxin	Homo sapiens	159-162
22833674-9	2012	NTRC shows structural constraints that may locate the thioredoxin module in positions with different efficiencies for electron transfer, the presence of 2-Cys Prx shifting the conformational equilibrium of the thioredoxin module to a specific position, which is not the most efficient.	2-cys	153-158	thioredoxin	Homo sapiens	210-221
22659048-4	2012	S. cerevisiae has three GPX genes (GPX1, GPX2, and GPX3) encoding atypical 2-Cys peroxiredoxins.	2-cys	75-80	glutathione peroxidase GPX2	Saccharomyces cerevisiae S288C	24-27
22659048-4	2012	S. cerevisiae has three GPX genes (GPX1, GPX2, and GPX3) encoding atypical 2-Cys peroxiredoxins.	2-cys	75-80	glutathione peroxidase GPX1	Saccharomyces cerevisiae S288C	35-39
22659048-4	2012	S. cerevisiae has three GPX genes (GPX1, GPX2, and GPX3) encoding atypical 2-Cys peroxiredoxins.	2-cys	75-80	glutathione peroxidase GPX2	Saccharomyces cerevisiae S288C	41-45
22659048-4	2012	S. cerevisiae has three GPX genes (GPX1, GPX2, and GPX3) encoding atypical 2-Cys peroxiredoxins.	2-cys	75-80	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	51-55
22385109-3	2012	Here, we reveal that the plant counterpart regulates the self-polymerization of 2-Cys Prx triggered by ATP and Mg(2+).	2-cys	80-85	periaxin	Homo sapiens	86-89
22474296-2	2012	Alkyl hydroperoxide reductase Ahp1 belongs to the Prx5 subfamily and is a two-cysteine (2-Cys) Prx that forms an intermolecular disulfide bond.	2-cys	88-93	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	30-34
22474296-4	2012	Thus Ahp1 represents the first 2-Cys Prx with a peroxidatic cysteine after the resolving cysteine in the primary sequence.	2-cys	31-36	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	5-9
22474296-8	2012	An intermolecular C(P)-C(R) disulfide bond crossing the A-type dimer interface distinguishes Ahp1 from other typical 2-Cys Prxs.	2-cys	117-122	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	93-97
22634055-2	2012	Members of the 2-Cys Prx subfamily of Prxs (Prx I to IV in mammals) are inactivated via hyperoxidation of the active-site cysteine to sulfinic acid (Cys-SO(2)H) during catalysis and are reactivated via an ATP-consuming reaction catalyzed by sulfiredoxin (Srx).	2-cys	15-20	periaxin	Homo sapiens	21-24
22634055-2	2012	Members of the 2-Cys Prx subfamily of Prxs (Prx I to IV in mammals) are inactivated via hyperoxidation of the active-site cysteine to sulfinic acid (Cys-SO(2)H) during catalysis and are reactivated via an ATP-consuming reaction catalyzed by sulfiredoxin (Srx).	2-cys	15-20	periaxin	Homo sapiens	38-41
22634055-2	2012	Members of the 2-Cys Prx subfamily of Prxs (Prx I to IV in mammals) are inactivated via hyperoxidation of the active-site cysteine to sulfinic acid (Cys-SO(2)H) during catalysis and are reactivated via an ATP-consuming reaction catalyzed by sulfiredoxin (Srx).	2-cys	15-20	sulfiredoxin 1	Homo sapiens	241-253
22634055-2	2012	Members of the 2-Cys Prx subfamily of Prxs (Prx I to IV in mammals) are inactivated via hyperoxidation of the active-site cysteine to sulfinic acid (Cys-SO(2)H) during catalysis and are reactivated via an ATP-consuming reaction catalyzed by sulfiredoxin (Srx).	2-cys	15-20	sulfiredoxin 1	Homo sapiens	255-258
22634633-8	2012	In contrast to the previous report, 2-Cys MsrB containing a resolving Cys was reducible by the glutaredoxins.	2-cys	36-41	methionine sulfoxide reductase B2	Homo sapiens	42-46
22385109-4	2012	This feature is of particular importance under oxidative stress because the interaction of ATP with 2-Cys Prx rapidly integrates nonredox chemistry of signaling pathways into a network hub governed by multiple redox transformations at cysteine residues.	2-cys	100-105	periaxin	Homo sapiens	106-109
22302711-2	2012	There are six known mammalian isozymes (Prx1-6), classified as typical 2-Cys, atypical 2-Cys, or 1-Cys Prxs.	2-cys	71-76	peroxiredoxin 1	Homo sapiens	40-46
22114845-4	2012	Typical 2-Cys Prx also functions as a molecular chaperone when it exists as a decamer and/or higher molecular weight complexes.	2-cys	8-13	periaxin	Homo sapiens	14-17
22114845-5	2012	The hyperoxidized sulfinic derivative of 2-Cys Prx is reactivated by sulfiredoxin (Srx).	2-cys	41-46	periaxin	Homo sapiens	47-50
22114845-5	2012	The hyperoxidized sulfinic derivative of 2-Cys Prx is reactivated by sulfiredoxin (Srx).	2-cys	41-46	sulfiredoxin 1	Homo sapiens	69-81
22114845-5	2012	The hyperoxidized sulfinic derivative of 2-Cys Prx is reactivated by sulfiredoxin (Srx).	2-cys	41-46	sulfiredoxin 1	Homo sapiens	83-86
22302711-2	2012	There are six known mammalian isozymes (Prx1-6), classified as typical 2-Cys, atypical 2-Cys, or 1-Cys Prxs.	2-cys	87-92	peroxiredoxin 1	Homo sapiens	40-46
22140244-7	2012	Further analysis revealed a novel combination of compensatory mechanisms in order to maintain redox homeostasis in the nadp-mdh plants under high-light conditions, particularly an increase in the NTRC/2-Cys peroxiredoxin (Prx) system in chloroplasts.	2-cys	201-206	lactate/malate dehydrogenase family protein	Arabidopsis thaliana	119-127
20059400-7	2010	The activity is highest at alkaline pH, consistent with the conditions of active respiring mitochondria, and the process is highly specific for 1-Cys Prx because Grx2p is totally inactive with human PRX1, a typical 2-Cys Prx, as opposed to the promiscuity of Trx.	2-cys	215-220	periaxin	Homo sapiens	150-153
23029461-2	2012	Arabidopsis NADPH-dependent thioredoxin reductase isotype C (AtNTRC) was identified as efficient electron donor for chloroplastic 2-Cys Prx-A.	2-cys	130-135	periaxin	Homo sapiens	136-139
21994946-4	2011	We show that PrxIV has a similar structure to other typical 2-Cys peroxiredoxins and undergoes a conformational change from a fully folded to a locally unfolded form following the formation of a disulfide between the peroxidatic and resolving cysteine residues.	2-cys	60-65	peroxiredoxin 4	Homo sapiens	13-18
21994946-5	2011	Unlike other mammalian typical 2-Cys peroxiredoxins, we show that human PrxIV forms a stable decameric structure even in its disulfide-bonded state.	2-cys	31-36	peroxiredoxin 4	Homo sapiens	72-77
21773675-0	2011	Engineering of 2-Cys peroxiredoxin for enhanced stress-tolerance.	2-cys	15-20	peroxiredoxin	Pseudomonas putida KT2440	21-34
21773675-1	2011	A typical 2-cysteine peroxiredoxin (2-Cys Prx)-like protein (PpPrx) that alternatively acts as a peroxidase or a molecular chaperone in Pseudomonas putida KT2440 was previously characterized.	2-cys	36-41	peroxiredoxin	Pseudomonas putida KT2440	21-34
21466852-3	2011	A small redox protein, sulfiredoxin (Srx), conserved only in eukaryotes, has been shown to reduce sulfinylated 2-Cys Prx"s, adding to the complexity of the H2O2 signaling network.	2-cys	111-116	sulfiredoxin 1	Homo sapiens	23-35
21466852-3	2011	A small redox protein, sulfiredoxin (Srx), conserved only in eukaryotes, has been shown to reduce sulfinylated 2-Cys Prx"s, adding to the complexity of the H2O2 signaling network.	2-cys	111-116	sulfiredoxin 1	Homo sapiens	37-40
21466852-3	2011	A small redox protein, sulfiredoxin (Srx), conserved only in eukaryotes, has been shown to reduce sulfinylated 2-Cys Prx"s, adding to the complexity of the H2O2 signaling network.	2-cys	111-116	periaxin	Homo sapiens	117-120
21525006-4	2011	Here, we disclose that ATP and Mg(2+) (ATP/Mg) promote the self-polymerization of chloroplast 2-Cys Prx (polypeptide 23.5 kDa) into soluble higher order assemblies (>2 MDa) that proceed to insoluble aggregates beyond 5 mM ATP.	2-cys	94-99	periaxin	Homo sapiens	100-103
21525006-7	2011	Circular dichroism studies on ATP-labeled 2-Cys Prx reveal that ATP/Mg enhance the proportion of beta-sheets with the concurrent decrease in the content of alpha-helices.	2-cys	42-47	periaxin	Homo sapiens	48-51
21525006-10	2011	Collectively, our data uncover that non-covalent interactions of ATP/Mg with 2-Cys Prx modulate dynamically the quaternary structure, thereby coupling the non-redox chemistry of cell energy with redox transformations at cysteine residues.	2-cys	77-82	periaxin	Homo sapiens	83-86
21237158-1	2011	The eukaryotic sulfiredoxin (Srx) catalyzes the reduction of overoxidized typical 2-Cys peroxiredoxins PrxSO(2) via ATP/Mg(2+)-dependent phosphorylation of the sulfinic acid group, followed by formation of a PrxSO-SSrx thiolsulfinate intermediate.	2-cys	82-87	sulfiredoxin 1	Homo sapiens	15-27
21237158-1	2011	The eukaryotic sulfiredoxin (Srx) catalyzes the reduction of overoxidized typical 2-Cys peroxiredoxins PrxSO(2) via ATP/Mg(2+)-dependent phosphorylation of the sulfinic acid group, followed by formation of a PrxSO-SSrx thiolsulfinate intermediate.	2-cys	82-87	sulfiredoxin 1	Homo sapiens	29-32
22104267-1	2011	A typical 2-cysteine peroxiredoxin (2-Cys Prx) PaPrx can act alternatively as thioredoxin (Trx)-dependent peroxidase and molecular chaperone in Pseudomonas aeruginosa PAO1.	2-cys	36-41	thioredoxin	Pseudomonas aeruginosa PAO1	78-89
22104267-1	2011	A typical 2-cysteine peroxiredoxin (2-Cys Prx) PaPrx can act alternatively as thioredoxin (Trx)-dependent peroxidase and molecular chaperone in Pseudomonas aeruginosa PAO1.	2-cys	36-41	thioredoxin	Pseudomonas aeruginosa PAO1	91-94
22086924-6	2012	In contrast, loss-of-function studies using Srx-depleted A549 and Srx-/- MEF cells demonstrate a dramatic increase in extra- and intracellular H2O2, sulfinic 2-Cys Prxs, and apoptosis.	2-cys	158-163	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	44-47
22086924-6	2012	In contrast, loss-of-function studies using Srx-depleted A549 and Srx-/- MEF cells demonstrate a dramatic increase in extra- and intracellular H2O2, sulfinic 2-Cys Prxs, and apoptosis.	2-cys	158-163	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	66-69
22086924-8	2012	Furthermore, adenoviral re-expression of Srx in Srx-depleted A549 or Srx-/- MEF cells promotes the reactivation of sulfinic 2-Cys Prxs and results in cellular resistance to apoptosis, with enhanced removal of H2O2.	2-cys	124-129	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	41-44
22086924-8	2012	Furthermore, adenoviral re-expression of Srx in Srx-depleted A549 or Srx-/- MEF cells promotes the reactivation of sulfinic 2-Cys Prxs and results in cellular resistance to apoptosis, with enhanced removal of H2O2.	2-cys	124-129	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	48-51
22086924-8	2012	Furthermore, adenoviral re-expression of Srx in Srx-depleted A549 or Srx-/- MEF cells promotes the reactivation of sulfinic 2-Cys Prxs and results in cellular resistance to apoptosis, with enhanced removal of H2O2.	2-cys	124-129	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	48-51
20919930-3	2011	On the basis of the location or absence of the C(R), Prxs are classified into 2-Cys, atypical 2-Cys, and 1-Cys Prx subfamilies.	2-cys	78-83	periaxin	Homo sapiens	53-56
20919930-3	2011	On the basis of the location or absence of the C(R), Prxs are classified into 2-Cys, atypical 2-Cys, and 1-Cys Prx subfamilies.	2-cys	94-99	periaxin	Homo sapiens	53-56
20919930-4	2011	In addition to their peroxidase activity, members of the 2-Cys Prx subfamily appear to serve as peroxide sensors for other proteins and as molecular chaperones.	2-cys	57-62	periaxin	Homo sapiens	63-66
21319188-2	2011	The active site cysteine residue of members of the 2-Cys Prx subgroup (Prx I to IV) of Prxs is hyperoxidized to cysteine sulfinic acid (Cys-SO(2) ) during catalysis with concomitant loss of peroxidase activity.	2-cys	51-56	periaxin	Mus musculus	57-60
21319188-2	2011	The active site cysteine residue of members of the 2-Cys Prx subgroup (Prx I to IV) of Prxs is hyperoxidized to cysteine sulfinic acid (Cys-SO(2) ) during catalysis with concomitant loss of peroxidase activity.	2-cys	51-56	peroxiredoxin 1	Mus musculus	71-76
21319188-7	2011	This result suggests that Prx I is the most active 2-Cys Prx in elimination of ROS from the liver of ethanol-fed mice and that, despite the up-regulation of Srx expression by ethanol, the capacity of Srx is not sufficient to counteract the hyperoxidation of Prx I that occurs during ROS reduction.	2-cys	51-56	periaxin	Mus musculus	26-29
20929858-0	2010	Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.	2-cys	87-92	thioredoxin 2	Homo sapiens	5-18
20929858-0	2010	Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.	2-cys	87-92	glutaredoxin 2	Homo sapiens	23-37
20929858-0	2010	Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.	2-cys	87-92	peroxiredoxin 3	Mus musculus	107-111
20929858-5	2010	The reduction of the catalytic disulfide of the atypical 2-Cys Prx5 is limited to the Trx system.	2-cys	57-62	thioredoxin	Homo sapiens	86-89
20059400-7	2010	The activity is highest at alkaline pH, consistent with the conditions of active respiring mitochondria, and the process is highly specific for 1-Cys Prx because Grx2p is totally inactive with human PRX1, a typical 2-Cys Prx, as opposed to the promiscuity of Trx.	2-cys	215-220	glutaredoxin 2	Homo sapiens	162-167
20059400-8	2010	Our results suggest that although Trx is the reductant involved in the reduction of peroxides by 2-Cys-Prx, Grx might be the natural resolving partner of 1-Cys Prx through a monothiolic mechanism.	2-cys	97-102	thioredoxin	Homo sapiens	34-37
20059400-8	2010	Our results suggest that although Trx is the reductant involved in the reduction of peroxides by 2-Cys-Prx, Grx might be the natural resolving partner of 1-Cys Prx through a monothiolic mechanism.	2-cys	97-102	periaxin	Homo sapiens	103-106
20308573-4	2010	The Tsa1/Tsa2 Prxs, like other 2-Cys Prxs, have dual activities as peroxidases and chaperones, and we show that the peroxidase activity is required to suppress spontaneous de novo [PSI(+)] prion formation.	2-cys	31-36	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	4-8
20615439-3	2010	In addition to CFP and YFP the DsRed derivative mCherry was genetically fused in frame to the coding region of the plastidic 2-Cys peroxiredoxin and co-expressed in plant cells resulting in detectable radiationless energy transfer from CFP via YFP to mCherry.	2-cys	125-130	complement factor properdin	Homo sapiens	236-239
20615439-6	2010	This finding together with previous reports on structural dynamics and functional switching of 2-Cys peroxiredoxin might indicate a conformation linked redox-signalling function of the 2-Cys Prx.	2-cys	95-100	periaxin	Homo sapiens	191-194
20615439-6	2010	This finding together with previous reports on structural dynamics and functional switching of 2-Cys peroxiredoxin might indicate a conformation linked redox-signalling function of the 2-Cys Prx.	2-cys	185-190	periaxin	Homo sapiens	191-194
20643022-3	2010	We suggest a novel noninvasive method to characterize HER2 expression in vivo, using optical imaging, based on HER2-specific probes (albumin-binding domain-fused-(ZHER2:342)2-Cys Affibody molecules [Affibody AB, Solna, Sweden], labeled with Alexa Fluor 750 [Molecular Probes, Invitrogen, Carlsbad, CA]) that could be used concomitantly with HER2-targeted therapy.	2-cys	173-178	erb-b2 receptor tyrosine kinase 2	Homo sapiens	54-58
20643022-3	2010	We suggest a novel noninvasive method to characterize HER2 expression in vivo, using optical imaging, based on HER2-specific probes (albumin-binding domain-fused-(ZHER2:342)2-Cys Affibody molecules [Affibody AB, Solna, Sweden], labeled with Alexa Fluor 750 [Molecular Probes, Invitrogen, Carlsbad, CA]) that could be used concomitantly with HER2-targeted therapy.	2-cys	173-178	erb-b2 receptor tyrosine kinase 2	Homo sapiens	111-115
20643022-3	2010	We suggest a novel noninvasive method to characterize HER2 expression in vivo, using optical imaging, based on HER2-specific probes (albumin-binding domain-fused-(ZHER2:342)2-Cys Affibody molecules [Affibody AB, Solna, Sweden], labeled with Alexa Fluor 750 [Molecular Probes, Invitrogen, Carlsbad, CA]) that could be used concomitantly with HER2-targeted therapy.	2-cys	173-178	erb-b2 receptor tyrosine kinase 2	Homo sapiens	111-115
20616155-7	2010	Moreover, the redox status of the 2-Cys Prx was imbalanced in the ntrc mutant but not in the trxx mutant.	2-cys	34-39	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	66-70
20616155-8	2010	These results show that NTRC is the most relevant pathway for chloroplast 2-Cys Prx reduction in vivo, but the antioxidant function of this system is not essential.	2-cys	74-79	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	24-28
20340159-7	2010	Furthermore, we found a novel thioredoxin as a subunit of the PEP, a 2-Cys-peroxiredoxin complex and a (soluble) ferredoxin:NADP-oxido-reductase, which represent potential redox regulator of plastid gene expression.	2-cys	69-74	thioredoxin H-type 1	Arabidopsis thaliana	30-41
20340159-7	2010	Furthermore, we found a novel thioredoxin as a subunit of the PEP, a 2-Cys-peroxiredoxin complex and a (soluble) ferredoxin:NADP-oxido-reductase, which represent potential redox regulator of plastid gene expression.	2-cys	69-74	RNA-binding KH domain-containing protein	Arabidopsis thaliana	62-65
20308573-4	2010	The Tsa1/Tsa2 Prxs, like other 2-Cys Prxs, have dual activities as peroxidases and chaperones, and we show that the peroxidase activity is required to suppress spontaneous de novo [PSI(+)] prion formation.	2-cys	31-36	thioredoxin peroxidase TSA2	Saccharomyces cerevisiae S288C	9-13
20176891-3	2010	An enzyme recently discovered, named sulfiredoxin (Srx), reduces the sulphinic 2-Cys Prx (Prx-SO(2)H).	2-cys	79-84	sulfiredoxin	Arabidopsis thaliana	37-49
20176891-3	2010	An enzyme recently discovered, named sulfiredoxin (Srx), reduces the sulphinic 2-Cys Prx (Prx-SO(2)H).	2-cys	79-84	sulfiredoxin	Arabidopsis thaliana	51-54
19457862-6	2009	Activity assays carried out using a series of cysteine mutants and various reductants combined with measurements of free thiols under distinct oxidation conditions and mass spectrometry experiments show that the 2-Cys MSRB2 is reduced by Trx through a dithiol-disulfide exchange involving both redox-active Cys of the two partners.	2-cys	212-217	methionine sulfoxide reductase B 2	Arabidopsis thaliana	218-223
19766713-6	2009	Among 2-Cys-peroxiredoxin isoforms, mainly peroxiredoxin-1 was found in cell bodies and nerve endings.	2-cys	6-11	peroxiredoxin 1	Homo sapiens	43-58
19561357-0	2009	Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.	2-cys	23-28	sulfiredoxin 1	Homo sapiens	72-84
19561357-2	2009	Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin.	2-cys	95-100	sulfiredoxin 1	Homo sapiens	0-12
19561357-2	2009	Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin.	2-cys	95-100	sulfiredoxin 1	Homo sapiens	14-17
19561357-2	2009	Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin.	2-cys	117-122	sulfiredoxin 1	Homo sapiens	0-12
19561357-2	2009	Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin.	2-cys	117-122	sulfiredoxin 1	Homo sapiens	14-17
19561357-3	2009	We show that deglutathionylation of 2-Cys Prx, a family of peroxidases, is specifically catalyzed by Srx.	2-cys	36-41	periaxin	Homo sapiens	42-45
19561357-3	2009	We show that deglutathionylation of 2-Cys Prx, a family of peroxidases, is specifically catalyzed by Srx.	2-cys	36-41	sulfiredoxin 1	Homo sapiens	101-104
19561357-4	2009	Using the ubiquitously expressed member of 2-Cys Prx, Prx I, we revealed the following.	2-cys	43-48	periaxin	Homo sapiens	49-52
19561357-4	2009	Using the ubiquitously expressed member of 2-Cys Prx, Prx I, we revealed the following.	2-cys	43-48	peroxiredoxin 1	Homo sapiens	54-59
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
18503776-7	2008	However, A. marina PRDX6 possesses five Cys among which two Cys function as peroxidatic and resolving Cys of typical 2-Cys PRDXs.	2-cys	117-122	peroxiredoxin 6	Homo sapiens	19-24
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	177-182	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	0-29
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	177-182	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	31-35
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	177-182	thioredoxin H-type 1	Arabidopsis thaliana	6-17
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	177-182	thioredoxin H-type 1	Arabidopsis thaliana	85-96
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	177-182	thioredoxin H-type 1	Arabidopsis thaliana	130-133
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	198-203	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	0-29
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	198-203	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	31-35
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	198-203	thioredoxin H-type 1	Arabidopsis thaliana	6-17
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	198-203	thioredoxin H-type 1	Arabidopsis thaliana	85-96
19825629-1	2009	NADPH thioredoxin reductase C (NTRC) is a chloroplast enzyme able to conjugate NADPH thioredoxin reductase (NTR) and thioredoxin (TRX) activities for the efficient reduction of 2-Cys peroxiredoxin (2-Cys PRX).	2-cys	198-203	thioredoxin H-type 1	Arabidopsis thaliana	130-133
19113821-1	2009	The active-site cysteine of 2-Cys peroxiredoxins (Prxs), a subgroup of the Prx family, is reversibly hyperoxidized to cysteine sulfinic acid during catalysis with concomitant loss of peroxidase activity.	2-cys	28-33	periaxin	Mus musculus	50-53
19113821-2	2009	The reduction of sulfinic 2-Cys Prx enzymes, the first known biologic of such a reaction, has been reported to be catalyzed by either sulfiredoxin (Srx) or sestrin (Sesn) 2.	2-cys	26-31	periaxin	Mus musculus	32-35
19113821-2	2009	The reduction of sulfinic 2-Cys Prx enzymes, the first known biologic of such a reaction, has been reported to be catalyzed by either sulfiredoxin (Srx) or sestrin (Sesn) 2.	2-cys	26-31	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	134-146
19113821-2	2009	The reduction of sulfinic 2-Cys Prx enzymes, the first known biologic of such a reaction, has been reported to be catalyzed by either sulfiredoxin (Srx) or sestrin (Sesn) 2.	2-cys	26-31	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	148-151
19113821-2	2009	The reduction of sulfinic 2-Cys Prx enzymes, the first known biologic of such a reaction, has been reported to be catalyzed by either sulfiredoxin (Srx) or sestrin (Sesn) 2.	2-cys	26-31	sestrin 2	Mus musculus	156-172
19825615-1	2009	Chloroplast 2-Cys peroxiredoxins (2-Cys Prxs) are efficiently reduced by NADPH Thioredoxin reductase C (NTRC).	2-cys	12-17	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	104-108
19825615-1	2009	Chloroplast 2-Cys peroxiredoxins (2-Cys Prxs) are efficiently reduced by NADPH Thioredoxin reductase C (NTRC).	2-cys	34-39	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	104-108
19825615-4	2009	NTRC deficiency caused a lower content of fully reduced 2-Cys Prxs, which was undetectable in darkness, suggesting that NTRC is the most important pathway for 2-Cys Prx reduction, probably the only one during the night.	2-cys	56-61	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	0-4
19825615-4	2009	NTRC deficiency caused a lower content of fully reduced 2-Cys Prxs, which was undetectable in darkness, suggesting that NTRC is the most important pathway for 2-Cys Prx reduction, probably the only one during the night.	2-cys	159-164	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	0-4
19825615-7	2009	2-Cys Prx overoxidation was lower in the NTRC mutant.	2-cys	0-5	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	41-45
19825615-8	2009	These results show the important function of NTRC to maintain the redox equilibrium of chloroplast 2-Cys Prxs.	2-cys	99-104	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	45-49
18708590-0	2008	Helminth 2-Cys peroxiredoxin drives Th2 responses through a mechanism involving alternatively activated macrophages.	2-cys	9-14	heart and neural crest derivatives expressed 2	Mus musculus	36-39
19462976-2	2009	In this study, we investigated the redox properties of human Prx 3, a typical 2-Cys Prx that is localized to the mitochondrial matrix.	2-cys	78-83	periaxin	Homo sapiens	61-64
19462976-2	2009	In this study, we investigated the redox properties of human Prx 3, a typical 2-Cys Prx that is localized to the mitochondrial matrix.	2-cys	78-83	periaxin	Homo sapiens	84-87
19176523-4	2009	When 2-Cys Prxs are inactivated in vitro, sulfiredoxin (Srx) reduces the cysteine sulfinic acid to cysteines.	2-cys	5-10	sulfiredoxin 1	Homo sapiens	42-54
19176523-4	2009	When 2-Cys Prxs are inactivated in vitro, sulfiredoxin (Srx) reduces the cysteine sulfinic acid to cysteines.	2-cys	5-10	sulfiredoxin 1	Homo sapiens	56-59
18489898-2	2008	PRDX5 is classified in the atypical 2-Cys subfamily of PRDXs.	2-cys	36-41	peroxiredoxin 5	Homo sapiens	0-5
18503776-8	2008	Thus, A. marina PRDX6 belongs to a transient group exhibiting sequence homologies with mammalian 1-Cys PRDX6 but must be mechanistically classified into typical 2-Cys PRDXs.	2-cys	161-166	peroxiredoxin 6	Homo sapiens	16-21
18625226-3	2008	A specific involvement of NTRC during biosynthesis of protochlorophyllide is indicated from in vitro aerobic cyclase assays in which the conversion of Mg-protoporhyrin monomethyl ester into protochlorophyllide is stimulated by addition of the NTRC/2-Cys peroxiredoxin system.	2-cys	248-253	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	26-30
18534986-9	2008	The glutathionylation of HSP70B, chloroplastic 2-Cys peroxiredoxin and isocitrate lyase was confirmed in vitro on purified proteins and the targeted residues were identified.	2-cys	47-52	uncharacterized protein	Chlamydomonas reinhardtii	53-66
18346073-5	2008	NTRC is able to conjugate both NTR and Trx activities to efficiently reduce 2-Cys Prx using NADPH as a source of reducing power.	2-cys	76-81	neurotensin receptor 1	Homo sapiens	0-3
18346073-5	2008	NTRC is able to conjugate both NTR and Trx activities to efficiently reduce 2-Cys Prx using NADPH as a source of reducing power.	2-cys	76-81	thioredoxin	Homo sapiens	39-42
18346073-5	2008	NTRC is able to conjugate both NTR and Trx activities to efficiently reduce 2-Cys Prx using NADPH as a source of reducing power.	2-cys	76-81	periaxin	Homo sapiens	82-85
18165315-1	2008	Typical 2-Cys peroxiredoxins (Prxs) are ubiquitous peroxidases that are involved in peroxide scavenging and/or the regulation of peroxide signaling in eukaryotes.	2-cys	8-13	peroxiredoxin 4	Homo sapiens	14-28
18271751-1	2008	The yeast Tsa1 peroxiredoxin, like other 2-Cys peroxiredoxins, has dual activities as a peroxidase and as a molecular chaperone.	2-cys	41-46	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	10-14
18052930-2	2008	In addition, the typical 2-Cys peroxiredoxins function in signalling of peroxide stress and as molecular chaperones, functions that are influenced by their oligomeric state.	2-cys	25-30	peroxiredoxin 4	Homo sapiens	31-45
18279387-1	2008	2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous thiol-containing peroxidases that have been implicated in antioxidant defense and signal transduction.	2-cys	0-5	periaxin	Homo sapiens	28-31
18279387-1	2008	2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous thiol-containing peroxidases that have been implicated in antioxidant defense and signal transduction.	2-cys	22-27	periaxin	Homo sapiens	28-31
18279387-3	2008	Here we report that the concerted action of a nucleoside triphosphate and Mg(2+) on rapeseed 2-Cys Prx reversibly impairs the peroxidase activity and promotes the formation of high molecular mass species.	2-cys	93-98	periaxin	Homo sapiens	99-102
18279387-5	2008	More importantly, we found that ATP facilitates the autophosphorylation of 2-Cys Prx when the protein is successively reduced with thiol-bearing compounds and oxidized with hydroperoxides or quinones.	2-cys	75-80	periaxin	Homo sapiens	81-84
18279387-6	2008	MS analyses reveal that 2-Cys Prx incorporates the phosphoryl group into the Cys175 residue yielding the sulfinic-phosphoryl [Prx-(Cys175)-SO(2)PO(3)(2-)] and the sulfonic-phosphoryl [Prx-(Cys175)-SO(3)PO(3)(2-)] anhydrides.	2-cys	24-29	periaxin	Homo sapiens	30-33
18279387-6	2008	MS analyses reveal that 2-Cys Prx incorporates the phosphoryl group into the Cys175 residue yielding the sulfinic-phosphoryl [Prx-(Cys175)-SO(2)PO(3)(2-)] and the sulfonic-phosphoryl [Prx-(Cys175)-SO(3)PO(3)(2-)] anhydrides.	2-cys	24-29	periaxin	Homo sapiens	126-129
18279387-6	2008	MS analyses reveal that 2-Cys Prx incorporates the phosphoryl group into the Cys175 residue yielding the sulfinic-phosphoryl [Prx-(Cys175)-SO(2)PO(3)(2-)] and the sulfonic-phosphoryl [Prx-(Cys175)-SO(3)PO(3)(2-)] anhydrides.	2-cys	24-29	periaxin	Homo sapiens	126-129
18279387-7	2008	Hence, the functional coupling between ATP and 2-Cys Prx gives novel insights into not only the removal of reactive oxygen species, but also mechanisms that link the energy status of the cell and the oxidation of cysteine residues.	2-cys	47-52	periaxin	Homo sapiens	53-56
17325201-1	2007	Mammalian 2-Cys peroxiredoxin II (Prx II) is a cellular peroxidase that eliminates endogenous H(2)O(2).	2-cys	10-15	peroxiredoxin 2	Mus musculus	16-32
17362873-4	2007	Expression levels of three isozymes of the 2-Cys peroxiredoxin (Prdx) family were quantified by Western blotting, the results showing 4.0- and 12.9-fold increases in Prdx1 protein in brown adipose tissue (BAT) and heart, respectively, during hibernation compared with euthermia.	2-cys	43-48	peroxiredoxin-1	Ictidomys tridecemlineatus	166-171
17974571-1	2008	Rat heme-binding protein 23 (HBP23)/peroxiredoxin (Prx I) belongs to the 2-Cys peroxiredoxin type I family and exhibits peroxidase activity coupled with reduced thioredoxin (Trx) as an electron donor.	2-cys	73-78	peroxiredoxin 1	Rattus norvegicus	29-34
17974571-1	2008	Rat heme-binding protein 23 (HBP23)/peroxiredoxin (Prx I) belongs to the 2-Cys peroxiredoxin type I family and exhibits peroxidase activity coupled with reduced thioredoxin (Trx) as an electron donor.	2-cys	73-78	peroxiredoxin 1	Homo sapiens	51-56
17974571-1	2008	Rat heme-binding protein 23 (HBP23)/peroxiredoxin (Prx I) belongs to the 2-Cys peroxiredoxin type I family and exhibits peroxidase activity coupled with reduced thioredoxin (Trx) as an electron donor.	2-cys	73-78	thioredoxin	Homo sapiens	174-177
17921138-6	2007	In addition, studies using macrophages from sulfiredoxin (Srx)-deficient mice indicated that regeneration of 2-Cys Prxs to the active form was dependent on Srx.	2-cys	109-114	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	44-56
17921138-6	2007	In addition, studies using macrophages from sulfiredoxin (Srx)-deficient mice indicated that regeneration of 2-Cys Prxs to the active form was dependent on Srx.	2-cys	109-114	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	58-61
17921138-6	2007	In addition, studies using macrophages from sulfiredoxin (Srx)-deficient mice indicated that regeneration of 2-Cys Prxs to the active form was dependent on Srx.	2-cys	109-114	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	156-159
17921138-7	2007	Last, we show that NO increased Srx expression and hastened Srx-dependent recovery of 2-Cys Prxs.	2-cys	86-91	sulfiredoxin 1 homolog (S. cerevisiae)	Mus musculus	60-63
17707404-1	2007	The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent peroxidase operating in tandem with its cognate partners, an organelle-specific thioredoxin (Trx2) and NADP-linked thioredoxin reductase (TRR2).	2-cys	18-23	peroxiredoxin 3	Homo sapiens	38-44
17707404-1	2007	The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent peroxidase operating in tandem with its cognate partners, an organelle-specific thioredoxin (Trx2) and NADP-linked thioredoxin reductase (TRR2).	2-cys	18-23	thioredoxin	Homo sapiens	57-68
17707404-1	2007	The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent peroxidase operating in tandem with its cognate partners, an organelle-specific thioredoxin (Trx2) and NADP-linked thioredoxin reductase (TRR2).	2-cys	18-23	thioredoxin	Homo sapiens	159-170
17707404-1	2007	The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent peroxidase operating in tandem with its cognate partners, an organelle-specific thioredoxin (Trx2) and NADP-linked thioredoxin reductase (TRR2).	2-cys	18-23	thioredoxin 2	Homo sapiens	172-176
17707404-1	2007	The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent peroxidase operating in tandem with its cognate partners, an organelle-specific thioredoxin (Trx2) and NADP-linked thioredoxin reductase (TRR2).	2-cys	18-23	thioredoxin	Homo sapiens	159-170
17707404-1	2007	The mitochondrial 2-Cys peroxiredoxin PrxIII serves as a thioredoxin-dependent peroxidase operating in tandem with its cognate partners, an organelle-specific thioredoxin (Trx2) and NADP-linked thioredoxin reductase (TRR2).	2-cys	18-23	tRNA-Arg (anticodon ACG) 1-2	Homo sapiens	217-221
17653208-0	2007	Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significance.	2-cys	63-68	sulfiredoxin 1	Homo sapiens	0-12
17653208-6	2007	Srx appears to exist solely to support the reversible sulfinic modification of 2-Cys Prx enzymes.	2-cys	79-84	sulfiredoxin 1	Homo sapiens	0-3
17653208-7	2007	Srx specifically binds to 2-Cys Prx enzymes by recognizing several critical surface-exposed residues of the Prxs, and transfer the gamma-phosphate of ATP to their sulfinic moiety, using its conserved cysteine as the phosphate carrier.	2-cys	26-31	sulfiredoxin 1	Homo sapiens	0-3
17325201-1	2007	Mammalian 2-Cys peroxiredoxin II (Prx II) is a cellular peroxidase that eliminates endogenous H(2)O(2).	2-cys	10-15	peroxiredoxin 2	Mus musculus	34-40
17217469-5	2007	AtSrx is a chloroplastic enzyme displaying sulfinic acid reductase activity, as shown by the ability of the recombinant AtSrx to reduce the overoxidized 2-Cys-Prx form in vitro, and by the accumulation of the overoxidized Prx in mutant lines lacking Srx in vivo.	2-cys	153-158	sulfiredoxin	Arabidopsis thaliana	0-5
17217469-5	2007	AtSrx is a chloroplastic enzyme displaying sulfinic acid reductase activity, as shown by the ability of the recombinant AtSrx to reduce the overoxidized 2-Cys-Prx form in vitro, and by the accumulation of the overoxidized Prx in mutant lines lacking Srx in vivo.	2-cys	153-158	sulfiredoxin	Arabidopsis thaliana	120-125
17217469-5	2007	AtSrx is a chloroplastic enzyme displaying sulfinic acid reductase activity, as shown by the ability of the recombinant AtSrx to reduce the overoxidized 2-Cys-Prx form in vitro, and by the accumulation of the overoxidized Prx in mutant lines lacking Srx in vivo.	2-cys	153-158	sulfiredoxin	Arabidopsis thaliana	2-5
17217469-7	2007	These data establish that, as in yeast and in mammals, plant 2-Cys-Prxs are subject to substrate-mediated inactivation reversed by Srx, and suggest that the 2-Cys-Prx redox status and sulfiredoxin are parts of a signaling mechanism participating in plant responses to oxidative stress.	2-cys	61-66	sulfiredoxin	Saccharomyces cerevisiae S288C	131-134
18084899-2	2007	Likewise, the complexity of reductive regenerants is very high, e.g. the chloroplast 2-Cys Prx is reduced by various thioredoxins, cyclophilin Cyp20-3, the drought induced CDSP32 and the NADPH-dependent reductant NTRC.	2-cys	85-90	periaxin	Homo sapiens	91-94
18084900-3	2007	The relative contributions of mitochondrial, enzyme-linked, antioxidant defence systems to tissue protection are also reviewed as is the emerging importance of the peroxiredoxin family in general to H2O2-mediated signalling The constituent enzymes of the mitochondrial PrxIII pathway are discussed in detail including the roles of PrxIII and PrxV in their capacities as typical 2-cys and atypical 2-cys thioredoxin-dependent hydroperoxide reductases, respectively.	2-cys	378-383	peroxiredoxin 3	Homo sapiens	269-275
18084900-3	2007	The relative contributions of mitochondrial, enzyme-linked, antioxidant defence systems to tissue protection are also reviewed as is the emerging importance of the peroxiredoxin family in general to H2O2-mediated signalling The constituent enzymes of the mitochondrial PrxIII pathway are discussed in detail including the roles of PrxIII and PrxV in their capacities as typical 2-cys and atypical 2-cys thioredoxin-dependent hydroperoxide reductases, respectively.	2-cys	397-402	peroxiredoxin 3	Homo sapiens	269-275
16916801-7	2006	This work demonstrates for the first time the existence of a redox-dependent dimer-monomer switch in the Prx family, similar to the decamer-dimer switch for the 2-Cys Prxs.	2-cys	161-166	periaxin	Homo sapiens	105-108
16891402-2	2006	We show that rice (Oryza sativa) chloroplast NADPH THIOREDOXIN REDUCTASE (NTRC), with a thioredoxin domain, uses NADPH to reduce the chloroplast 2-Cys peroxiredoxin BAS1, which then reduces hydrogen peroxide.	2-cys	145-150	Cytochrome P450 superfamily protein	Arabidopsis thaliana	165-169
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
16540402-4	2006	We identified an Anopheles stephensi 2-Cys Prx ortholog of Drosophila melanogaster Prx-4783, which protects fly cells against oxidative stresses.	2-cys	37-42	thioredoxin peroxidase 1	Drosophila melanogaster	83-91
15590625-4	2005	Purified sulfiredoxin reduced the sulfinic forms of the four 2-Cys members (Prx I to Prx IV) of the Prx family in vitro, but it did not affect those of Prx V, Prx VI, or GAPDH.	2-cys	61-66	sulfiredoxin 1	Homo sapiens	9-21
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
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
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	periaxin	Homo sapiens	36-39
16251189-0	2005	GPX2, encoding a phospholipid hydroperoxide glutathione peroxidase homologue, codes for an atypical 2-Cys peroxiredoxin in Saccharomyces cerevisiae.	2-cys	100-105	glutathione peroxidase GPX2	Saccharomyces cerevisiae S288C	0-4
16290020-3	2005	2-Cys peroxiredoxins are members of a novel peroxidase family that catalyze the H(2)O(2) reduction reaction in the presence of thioredoxin, thioredoxin reductase and NADPH.	2-cys	0-5	thioredoxin	Homo sapiens	127-138
16290020-3	2005	2-Cys peroxiredoxins are members of a novel peroxidase family that catalyze the H(2)O(2) reduction reaction in the presence of thioredoxin, thioredoxin reductase and NADPH.	2-cys	0-5	peroxiredoxin 5	Homo sapiens	140-161
16290020-3	2005	2-Cys peroxiredoxins are members of a novel peroxidase family that catalyze the H(2)O(2) reduction reaction in the presence of thioredoxin, thioredoxin reductase and NADPH.	2-cys	0-5	2,4-dienoyl-CoA reductase 1	Homo sapiens	166-171
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
15632145-3	2005	Therefore, it might be assumed to have functions similar to the human 2-Cys Prx (PRDX3) and type II Prx (PRDX5) and yeast 1-Cys Prx that likewise have mitochondrial localizations.	2-cys	70-75	peroxiredoxin 3	Homo sapiens	76-79
15632145-3	2005	Therefore, it might be assumed to have functions similar to the human 2-Cys Prx (PRDX3) and type II Prx (PRDX5) and yeast 1-Cys Prx that likewise have mitochondrial localizations.	2-cys	70-75	peroxiredoxin 3	Homo sapiens	81-86
15590625-4	2005	Purified sulfiredoxin reduced the sulfinic forms of the four 2-Cys members (Prx I to Prx IV) of the Prx family in vitro, but it did not affect those of Prx V, Prx VI, or GAPDH.	2-cys	61-66	peroxiredoxin 1	Homo sapiens	76-81
15590625-4	2005	Purified sulfiredoxin reduced the sulfinic forms of the four 2-Cys members (Prx I to Prx IV) of the Prx family in vitro, but it did not affect those of Prx V, Prx VI, or GAPDH.	2-cys	61-66	peroxiredoxin 4	Homo sapiens	85-91
15590625-4	2005	Purified sulfiredoxin reduced the sulfinic forms of the four 2-Cys members (Prx I to Prx IV) of the Prx family in vitro, but it did not affect those of Prx V, Prx VI, or GAPDH.	2-cys	61-66	periaxin	Homo sapiens	76-79
15590625-5	2005	Furthermore, Srx bound specifically to the four 2-Cys Prxs in vitro and in cells.	2-cys	48-53	sulfiredoxin 1	Homo sapiens	13-16
15590625-7	2005	These results suggest that reduction of Cys-SO2H by Srx is specific to 2-Cys Prx isoforms.	2-cys	71-76	sulfiredoxin 1	Homo sapiens	52-55
15590625-7	2005	These results suggest that reduction of Cys-SO2H by Srx is specific to 2-Cys Prx isoforms.	2-cys	71-76	periaxin	Homo sapiens	77-80
15607657-2	2005	The B. mori TPx (BmTPx) cDNA contains an open reading frame of 585 bp encoding 195 amino acid residues and possesses two cysteine residues that are characteristic of 2-Cys subgroup of peroxiredoxin family.	2-cys	166-171	thioredoxin peroxidase	Bombyx mori	12-15
15607657-3	2005	The deduced amino acid sequence of the BmTPx cDNA showed 78% identity to Drosophila melanogaster (DmTPx-1), 73% to Aedes aegypti (AaTPx), and 54-48% to other insect 2-Cys TPx.	2-cys	165-170	thioredoxin peroxidase	Bombyx mori	41-44
12529539-4	2003	The steady-state transcript amounts of the chloroplast-targeted prxs, namely the two-cysteine (2-Cys) prxs, prx Q and prx II E, decreased upon application of ascorbate.	2-cys	95-100	Thioredoxin superfamily protein	Arabidopsis thaliana	108-126
12714747-3	2003	By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity.	2-cys	59-64	periaxin	Homo sapiens	65-68
12714747-3	2003	By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity.	2-cys	59-64	periaxin	Homo sapiens	127-130
12714747-3	2003	By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity.	2-cys	121-126	periaxin	Homo sapiens	65-68
12714747-3	2003	By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity.	2-cys	121-126	periaxin	Homo sapiens	127-130
11929977-1	2002	The 2-cysteine peroxiredoxins (2-Cys Prx) constitute an ancient family of peroxide detoxifying enzymes and have acquired a plant-specific function in the oxygenic environment of the chloroplast.	2-cys	31-36	periaxin	Homo sapiens	37-40
11929977-5	2002	During the peroxide reduction reaction, 2-Cys Prx is alternatively oxidized and reduced as it catalyzes an electron flow from an electron donor to peroxide.	2-cys	40-45	periaxin	Homo sapiens	46-49
11929977-6	2002	Escherichia coli thioredoxin, but also spinach thioredoxin f and m were able to reduce oxidized 2-Cys Prx.	2-cys	96-101	periaxin	Homo sapiens	102-105
11929977-7	2002	The midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the malate valve for export of excess reduction equivalents to the cytosol.	2-cys	47-52	periaxin	Homo sapiens	53-56
11929977-8	2002	Thus the 2-Cys Prx has a defined and preferential place in the hierarchy of photosynthetic electron transport.	2-cys	9-14	periaxin	Homo sapiens	15-18
11929977-9	2002	The activity of 2-Cys Prx also is linked to chloroplastic NAD(P)H metabolism as indicated by the presence of the reduced form of the enzyme after feeding dihydroxyacetone phosphate to intact chloroplasts.	2-cys	16-21	periaxin	Homo sapiens	22-25
11929977-10	2002	The function of the 2-Cys Prx is therefore not confined to its role in the water-water cycle pathway for energy dissipation in photosynthesis but also mediates peroxide detoxification in the plastids during the dark phase.	2-cys	20-25	periaxin	Homo sapiens	26-29
11929977-2	2002	Immunocytochemical analysis and work with isolated intact chloroplasts revealed a reversible binding of the oligomeric form of 2-Cys Prx to the thylakoid membrane.	2-cys	127-132	periaxin	Homo sapiens	133-136
11929977-4	2002	The 2-Cys Prx has a broad substrate specificity with activity toward hydrogen peroxides and complex alkyl hydroperoxides.	2-cys	4-9	periaxin	Homo sapiens	10-13
10535922-0	1999	Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product.	2-cys	39-44	peroxiredoxin 1	Rattus norvegicus	59-86
10873855-2	2000	Thioredoxin peroxidase B (TPx-B), a 2-Cys type II Prx from erythrocytes, promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue.	2-cys	36-41	periaxin	Homo sapiens	50-53
10873855-8	2000	A comparison with two previously reported dimeric Prx structures reveals that the catalytic cycle of 2-Cys Prx requires significant conformational changes that include the unwinding of the active-site helix and the movement of four loops.	2-cys	101-106	periaxin	Homo sapiens	50-53
10873855-8	2000	A comparison with two previously reported dimeric Prx structures reveals that the catalytic cycle of 2-Cys Prx requires significant conformational changes that include the unwinding of the active-site helix and the movement of four loops.	2-cys	101-106	periaxin	Homo sapiens	107-110
10821871-3	2000	Moreover, 2-Cys Prxs, also named thioredoxin peroxidases, have peroxide reductase activity with the use of thioredoxin as biological electron donor.	2-cys	10-15	thioredoxin	Homo sapiens	33-44
10821871-3	2000	Moreover, 2-Cys Prxs, also named thioredoxin peroxidases, have peroxide reductase activity with the use of thioredoxin as biological electron donor.	2-cys	10-15	thioredoxin	Homo sapiens	107-118
11677042-2	2001	Three of the genes (DPx-4156, DPx-4783, and DPx-5037) fall into the 2-Cys subgroup, while the other two (DPx-2540 and DPx-6005) belong to the 1-Cys subgroup.	2-cys	68-73	Thioredoxin peroxidase 2	Drosophila melanogaster	20-28
11677042-2	2001	Three of the genes (DPx-4156, DPx-4783, and DPx-5037) fall into the 2-Cys subgroup, while the other two (DPx-2540 and DPx-6005) belong to the 1-Cys subgroup.	2-cys	68-73	thioredoxin peroxidase 1	Drosophila melanogaster	30-38
11677042-2	2001	Three of the genes (DPx-4156, DPx-4783, and DPx-5037) fall into the 2-Cys subgroup, while the other two (DPx-2540 and DPx-6005) belong to the 1-Cys subgroup.	2-cys	68-73	Peroxiredoxin 3	Drosophila melanogaster	44-52
11677042-4	2001	The three 2-Cys Prx were also shown to be active in the thioredoxin system and were, consequently, classified as thioredoxin peroxidases.	2-cys	10-15	thioredoxin peroxidase 1	Drosophila melanogaster	16-19
11233141-3	1999	This review focuses on the four mammalian 2-Cys members (Prx I-IV) that utilize thioredoxin as the electron donor for antioxidation.	2-cys	42-47	thioredoxin	Homo sapiens	80-91
34782858-3	2021	Although Urm1 conjugation coincides with oxidative stress and targets proteins like 2-Cys peroxiredoxins from yeast (Ahp1) and fly (Prx5), it was unclear how urmylation proceeds molecularly and whether it is affected by the activity of these antioxidant enzymes.	2-cys	84-89	ubiquitin-related modifier URM1	Saccharomyces cerevisiae S288C	9-13
8611543-2	1996	Cross-linking of Fab" fragments by (DCT)2-cys is limited to linear dimers, and we find that (DCT)2-cys dissociation from Fab" occurs with a single kinetic coefficient [(4.2 +/- 0.6) x 10-3 s-1] that corresponds to the lower of the two kinetic coefficients observed with the bivalent IgE [(4.7 +/- 0.7) x 10-2 s-1 and (4.4 +/- 0.3) x 10-3 s-1].	2-cys	97-102	FA complementation group B	Homo sapiens	17-20
8611543-2	1996	Cross-linking of Fab" fragments by (DCT)2-cys is limited to linear dimers, and we find that (DCT)2-cys dissociation from Fab" occurs with a single kinetic coefficient [(4.2 +/- 0.6) x 10-3 s-1] that corresponds to the lower of the two kinetic coefficients observed with the bivalent IgE [(4.7 +/- 0.7) x 10-2 s-1 and (4.4 +/- 0.3) x 10-3 s-1].	2-cys	97-102	FA complementation group B	Homo sapiens	121-124
8611543-2	1996	Cross-linking of Fab" fragments by (DCT)2-cys is limited to linear dimers, and we find that (DCT)2-cys dissociation from Fab" occurs with a single kinetic coefficient [(4.2 +/- 0.6) x 10-3 s-1] that corresponds to the lower of the two kinetic coefficients observed with the bivalent IgE [(4.7 +/- 0.7) x 10-2 s-1 and (4.4 +/- 0.3) x 10-3 s-1].	2-cys	97-102	immunoglobulin heavy constant epsilon	Homo sapiens	283-286
9047325-10	1997	Phosphorylation of Syk occurs at the higher (DCT)2-cys concentrations in parallel with beta phosphorylation but does not occur in its absence at the lower (DCT)2-cys concentrations.	2-cys	49-54	spleen associated tyrosine kinase	Rattus norvegicus	19-22
9047325-10	1997	Phosphorylation of Syk occurs at the higher (DCT)2-cys concentrations in parallel with beta phosphorylation but does not occur in its absence at the lower (DCT)2-cys concentrations.	2-cys	160-165	spleen associated tyrosine kinase	Rattus norvegicus	19-22
8611543-2	1996	Cross-linking of Fab" fragments by (DCT)2-cys is limited to linear dimers, and we find that (DCT)2-cys dissociation from Fab" occurs with a single kinetic coefficient [(4.2 +/- 0.6) x 10-3 s-1] that corresponds to the lower of the two kinetic coefficients observed with the bivalent IgE [(4.7 +/- 0.7) x 10-2 s-1 and (4.4 +/- 0.3) x 10-3 s-1].	2-cys	40-45	FA complementation group B	Homo sapiens	17-20
8611543-2	1996	Cross-linking of Fab" fragments by (DCT)2-cys is limited to linear dimers, and we find that (DCT)2-cys dissociation from Fab" occurs with a single kinetic coefficient [(4.2 +/- 0.6) x 10-3 s-1] that corresponds to the lower of the two kinetic coefficients observed with the bivalent IgE [(4.7 +/- 0.7) x 10-2 s-1 and (4.4 +/- 0.3) x 10-3 s-1].	2-cys	40-45	FA complementation group B	Homo sapiens	121-124
34884692-4	2021	The results showed that a group of sperm mitochondrial (LDHAL6B, CS, ACO2, SDHA, ACAPM) and actin cytoskeleton proteins (CAPZB, ALDOA, CCIN) is oxidized due to the action of 2-Cys PRDXs under control conditions.	2-cys	174-179	lactate dehydrogenase A like 6B	Homo sapiens	56-63
34884692-4	2021	The results showed that a group of sperm mitochondrial (LDHAL6B, CS, ACO2, SDHA, ACAPM) and actin cytoskeleton proteins (CAPZB, ALDOA, CCIN) is oxidized due to the action of 2-Cys PRDXs under control conditions.	2-cys	174-179	citrate synthase	Homo sapiens	65-67
34884692-4	2021	The results showed that a group of sperm mitochondrial (LDHAL6B, CS, ACO2, SDHA, ACAPM) and actin cytoskeleton proteins (CAPZB, ALDOA, CCIN) is oxidized due to the action of 2-Cys PRDXs under control conditions.	2-cys	174-179	aconitase 2	Homo sapiens	69-73
34884692-4	2021	The results showed that a group of sperm mitochondrial (LDHAL6B, CS, ACO2, SDHA, ACAPM) and actin cytoskeleton proteins (CAPZB, ALDOA, CCIN) is oxidized due to the action of 2-Cys PRDXs under control conditions.	2-cys	174-179	succinate dehydrogenase complex flavoprotein subunit A	Homo sapiens	75-79
34884692-4	2021	The results showed that a group of sperm mitochondrial (LDHAL6B, CS, ACO2, SDHA, ACAPM) and actin cytoskeleton proteins (CAPZB, ALDOA, CCIN) is oxidized due to the action of 2-Cys PRDXs under control conditions.	2-cys	174-179	capping actin protein of muscle Z-line subunit beta	Homo sapiens	121-126
34884692-4	2021	The results showed that a group of sperm mitochondrial (LDHAL6B, CS, ACO2, SDHA, ACAPM) and actin cytoskeleton proteins (CAPZB, ALDOA, CCIN) is oxidized due to the action of 2-Cys PRDXs under control conditions.	2-cys	174-179	aldolase, fructose-bisphosphate A	Homo sapiens	128-133
34782858-3	2021	Although Urm1 conjugation coincides with oxidative stress and targets proteins like 2-Cys peroxiredoxins from yeast (Ahp1) and fly (Prx5), it was unclear how urmylation proceeds molecularly and whether it is affected by the activity of these antioxidant enzymes.	2-cys	84-89	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	117-121
34782858-3	2021	Although Urm1 conjugation coincides with oxidative stress and targets proteins like 2-Cys peroxiredoxins from yeast (Ahp1) and fly (Prx5), it was unclear how urmylation proceeds molecularly and whether it is affected by the activity of these antioxidant enzymes.	2-cys	84-89	Peroxiredoxin 5	Drosophila melanogaster	132-136
34782858-5	2021	The results clearly show that the dimer interface and the 2-Cys based redox-active centers of Ahp1 are affecting the Urm1 conjugation reaction.	2-cys	58-63	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	94-98
34782858-5	2021	The results clearly show that the dimer interface and the 2-Cys based redox-active centers of Ahp1 are affecting the Urm1 conjugation reaction.	2-cys	58-63	ubiquitin-related modifier URM1	Saccharomyces cerevisiae S288C	117-121
34208049-3	2021	Here, we present a study on the structural requirements for the repair of hyperoxidized 2-Cys Prxs by human sulfiredoxin (Srx) and the relative efficacy of physiological reductants hydrogen sulfide (H2S) and glutathione (GSH) in this reaction.	2-cys	88-93	sulfiredoxin 1	Homo sapiens	108-120
34618130-4	2021	However, NTRC was proposed to participate in redox regulation of additional targets, prompting inquiry into whether the function of NTRC depends on its capacity to maintain the redox balance of 2-Cys Prxs or by direct redox interaction with chloroplast enzymes.	2-cys	194-199	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	132-136
34618130-7	2021	These results suggest that the most relevant function of NTRC is in controlling the redox balance of 2-Cys Prxs.	2-cys	101-106	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	57-61
34208049-3	2021	Here, we present a study on the structural requirements for the repair of hyperoxidized 2-Cys Prxs by human sulfiredoxin (Srx) and the relative efficacy of physiological reductants hydrogen sulfide (H2S) and glutathione (GSH) in this reaction.	2-cys	88-93	sulfiredoxin 1	Homo sapiens	122-125
34254679-7	2021	To counter NTRC-mediated defenses, BSMV employs the gammab protein to competitively interfere with NbNTRC binding to 2-Cys Prx.	2-cys	117-122	periaxin	Homo sapiens	123-126
33744653-7	2021	On-NKEF-A protein contained a typical 2-Cys family domain, two active sites (51aa and 172aa) that were conserved in mammals, birds, amphibians and fish.	2-cys	38-43	macrophage stimulating 1 receptor	Rattus norvegicus	0-2
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 1	Homo sapiens	16-30
33308115-6	2021	The system contains different redox cascades, where trypanothione and tryparedoxins, play together a central role in transferring reduced power to different enzymes, such as 2-Cys peroxiredoxins, non-selenium glutathione peroxidases, ascorbate peroxidases, glutaredoxins and methionine sulfoxide reductases, through NADPH as a source of electrons.	2-cys	174-179	2,4-dienoyl-CoA reductase 1	Homo sapiens	316-321
33142810-5	2020	Interestingly, Arabidopsis mutants combining the deficiencies of x- or f-type Trxs and NTRC display very severe growth inhibition phenotypes, which are partially rescued by decreased levels of 2-Cys peroxiredoxins (Prxs).	2-cys	193-198	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	87-91
33142810-6	2020	These findings indicate that the reducing capacity of Trxs f and x is modulated by the redox balance of 2-Cys Prxs, which is controlled by NTRC.	2-cys	104-109	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	139-143
32632849-2	2020	There are six mammalian Prx isozymes (Prx1-6), classified as typical 2-Cys, atypical 2-Cys, or 1-Cys Prxs based on the mechanism and the number of cysteine residues involved during catalysis.	2-cys	69-74	peroxiredoxin 1	Homo sapiens	38-44
32632849-2	2020	There are six mammalian Prx isozymes (Prx1-6), classified as typical 2-Cys, atypical 2-Cys, or 1-Cys Prxs based on the mechanism and the number of cysteine residues involved during catalysis.	2-cys	85-90	peroxiredoxin 1	Homo sapiens	38-44
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.	2-cys	32-37	periaxin	Homo sapiens	0-3
33060708-3	2020	Mammalian Prdx"s are classified according to the number of Cys implicated in their catalytic activity by the formation of either inter-molecular (typical 2-Cys, Prdx1-4) or intra-molecular (atypical 2-Cys, Prdx5) disulfide bond, or non-covalent interactions (1-Cys, Prdx6).	2-cys	154-159	peroxiredoxin 1	Homo sapiens	10-14
33060708-3	2020	Mammalian Prdx"s are classified according to the number of Cys implicated in their catalytic activity by the formation of either inter-molecular (typical 2-Cys, Prdx1-4) or intra-molecular (atypical 2-Cys, Prdx5) disulfide bond, or non-covalent interactions (1-Cys, Prdx6).	2-cys	199-204	peroxiredoxin 1	Homo sapiens	10-14
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
32050573-6	2020	Pull-down experiments showed that ThTrx bound 2-Cys peroxiredoxin BAS1-like protein that influences stress response-associated redox, hormone signal transduction, and transcription factor functions.	2-cys	46-51	Cytochrome P450 superfamily protein	Arabidopsis thaliana	66-70
32751232-0	2020	Comparative Study of Protective Action of Exogenous 2-Cys Peroxiredoxins (Prx1 and Prx2) Under Renal Ischemia-Reperfusion Injury.	2-cys	52-57	peroxiredoxin 4	Homo sapiens	58-72
32751232-0	2020	Comparative Study of Protective Action of Exogenous 2-Cys Peroxiredoxins (Prx1 and Prx2) Under Renal Ischemia-Reperfusion Injury.	2-cys	52-57	paired related homeobox 1	Homo sapiens	74-78
32751232-5	2020	In an animal model of bilateral I/R injury of kidneys (using histological, biochemical, and molecular biological methods) it was shown that intravenous administration of recombinant typical 2-Cys peroxiredoxins (Prx1 and Prx2) effectively reduces the severity of I/R damage, contributing to the normalization of the structural and functional state of the kidneys and an almost 2-fold increase in the survival of experimental animals.	2-cys	190-195	peroxiredoxin 4	Homo sapiens	196-210
32751232-5	2020	In an animal model of bilateral I/R injury of kidneys (using histological, biochemical, and molecular biological methods) it was shown that intravenous administration of recombinant typical 2-Cys peroxiredoxins (Prx1 and Prx2) effectively reduces the severity of I/R damage, contributing to the normalization of the structural and functional state of the kidneys and an almost 2-fold increase in the survival of experimental animals.	2-cys	190-195	paired related homeobox 2	Homo sapiens	221-225
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 1	Homo sapiens	36-40
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
32098329-3	2020	In mammals, six PRDX members have been identified and are subdivided into three subfamilies: typical 2-Cys (PRDX1, PRDX2, PRDX3, and PRDX4), atypical 2-Cys (PRDX5), and 1-Cys (PRDX6) subfamilies.	2-cys	101-106	peroxiredoxin 1	Mus musculus	16-20
32098329-3	2020	In mammals, six PRDX members have been identified and are subdivided into three subfamilies: typical 2-Cys (PRDX1, PRDX2, PRDX3, and PRDX4), atypical 2-Cys (PRDX5), and 1-Cys (PRDX6) subfamilies.	2-cys	150-155	peroxiredoxin 1	Mus musculus	16-20
32151745-0	2020	Multiple functions of 2-Cys peroxiredoxins, I and II, and their regulations via post-translational modifications.	2-cys	22-27	peroxiredoxin 1	Homo sapiens	28-42
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
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	epiregulin	Mus musculus	91-101
32414504-10	2020	Expression of the gene encoding 2-cysteine peroxiredoxin (2-Cys Prx) was up-regulated in 100 microM H2O2 group at 6 hpe, but was down-regulated in 100 microM H2O2 group at 3 and 6 hpe.	2-cys	58-63	periaxin	Homo sapiens	64-67
32414504-11	2020	A negative relationship between the 2-Cys Prx transcript levels and intracellular ROS levels was detected.	2-cys	36-41	periaxin	Homo sapiens	42-45
32414504-12	2020	Results of the 2-DE proteomic analysis confirmed that the 500 microM H2O2 treatment down-regulated the expression of 2-Cys Prx and induced more damage to photosynthetic abilities of C. marina var.	2-cys	117-122	periaxin	Homo sapiens	123-126
31366734-1	2019	2-Cys peroxiredoxins (Prxs) rapidly reduce H2O2, thereby acting as antioxidants and also as sensors and transmitters of H2O2 signals in cells.	2-cys	0-5	peroxiredoxin 1	Homo sapiens	6-20
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
31294455-7	2019	The identification of proteins co-purified in these complexes by MS revealed the relevance of the NTRC-2-Cys PRX system in the redox regulation of multiple chloroplast processes.	2-cys	103-108	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	98-102
31185618-2	2019	Mammalian Prxs comprise six isoforms (typical 2-Cys Prxs; Prx1-4, atypical 2-Cys Prx; Prx5, and 1-Cys Prx; Prx6) that are distributed over various cellular compartments as they are classified according to the position and number of conserved cysteine.	2-cys	46-51	periaxin	Homo sapiens	10-13
31185618-2	2019	Mammalian Prxs comprise six isoforms (typical 2-Cys Prxs; Prx1-4, atypical 2-Cys Prx; Prx5, and 1-Cys Prx; Prx6) that are distributed over various cellular compartments as they are classified according to the position and number of conserved cysteine.	2-cys	75-80	periaxin	Homo sapiens	10-13
31185618-3	2019	2-Cys Prx1 and Prx2 are abundant proteins that are ubiquitously expressed mainly in the cytosol, and over 90% of their amino acid sequences are homologous.	2-cys	0-5	paired related homeobox 1	Homo sapiens	6-10
31185618-7	2019	This review focuses on cytosolic 2-Cys Prx1 and Prx2 and their role in the regulation of redox signaling based on protein-protein interaction.	2-cys	33-38	paired related homeobox 1	Homo sapiens	39-43
31311441-4	2019	Peroxiredoxin 4, a typical endoplasmic reticulum-resident 2-Cys antioxidant of peroxiredoxins, can fine-tune hydrogen peroxide catabolism which affects cell survival by affecting redox balance, oxidative protein folding, and regulation of hydrogen peroxide signaling.	2-cys	58-63	peroxiredoxin 4	Homo sapiens	0-15
31019520-9	2019	Here, we update the current knowledge of these two redox systems focusing on recent evidence showing their functional interrelationship through the action of the thiol-dependent peroxidase, 2-Cys peroxiredoxin (2-Cys Prx).	2-cys	190-195	periaxin	Homo sapiens	217-220
30784599-0	2019	Absence of Cytosolic 2-Cys Prx Subtypes I and II Exacerbates TNF-alpha-Induced Apoptosis via Different Routes.	2-cys	21-26	tumor necrosis factor	Homo sapiens	61-70
31311441-4	2019	Peroxiredoxin 4, a typical endoplasmic reticulum-resident 2-Cys antioxidant of peroxiredoxins, can fine-tune hydrogen peroxide catabolism which affects cell survival by affecting redox balance, oxidative protein folding, and regulation of hydrogen peroxide signaling.	2-cys	58-63	peroxiredoxin 4	Homo sapiens	79-93
28605287-8	2018	Notably, impairment of both lipophagic flux and cholesterol efflux was restored by the 2-Cys PRDX-mimics ebselen and gliotoxin.	2-cys	87-92	peroxiredoxin 1	Homo sapiens	93-97
28776692-7	2018	BR increased transcripts of RESPIRATORY BURST OXIDASE HOMOLOG1 (RBOH1) and GLUTAREDOXIN (GRX) genes, and BR-induced chilling tolerance was associated with an increase in the ratio of reduced/oxidized 2-cysteine peroxiredoxin (2-Cys Prx) and activation of antioxidant enzymes.	2-cys	226-231	NADPH oxidase	Solanum lycopersicum	64-69
29400317-2	2018	The 2-Cys PRX from Chlamydomonas reinhardtii (CrPRX1) is a chloroplast-localized protein that is critical for clearing reactive oxygen species in chloroplasts.	2-cys	4-9	uncharacterized protein	Chlamydomonas reinhardtii	46-52
29304480-0	2018	Mapping the phenotypic repertoire of the cytoplasmic 2-Cys peroxiredoxin - Thioredoxin system.	2-cys	53-58	thioredoxin	Homo sapiens	75-86
29445382-14	2018	Secondly, high levels of 2-Cys peroxiredoxin BAS1, chloroplastic, thioredoxin reductase (NADPH) and cysteine synthase, chloroplastic/chromoplastic, O-acetylserine sulfhydrylase, involved in protection against oxidative stress and cysteine synthase activity, respectively, were observed in leaves.	2-cys	25-30	cysteine synthase, chloroplastic/chromoplastic	Beta vulgaris subsp. vulgaris	100-176
29078290-0	2017	NTRC-dependent redox balance of 2-Cys peroxiredoxins is needed for optimal function of the photosynthetic apparatus.	2-cys	32-37	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	0-4
29078290-4	2017	NTRC efficiently reduces 2-Cys peroxiredoxins (Prxs), thus having antioxidant function, but also participates in redox regulation of metabolic pathways previously established to be regulated by Trxs.	2-cys	25-30	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	0-4
29078290-6	2017	Here we show that decreased levels of 2-Cys Prxs suppress the phenotype of the Arabidopsis thaliana ntrc KO mutant.	2-cys	38-43	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	100-104
29078290-7	2017	The excess of oxidized 2-Cys Prxs in NTRC-deficient plants drains reducing power from chloroplast Trxs, which results in low efficiency of light energy utilization and impaired redox regulation of Calvin-Benson cycle enzymes.	2-cys	23-28	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	37-41
29078290-8	2017	Moreover, the dramatic phenotype of the ntrc-trxf1f2 triple mutant, lacking NTRC and f-type Trxs, was also suppressed by decreased 2-Cys Prxs contents, as the ntrc-trxf1f2-Delta2cp mutant partially recovered the efficiency of light energy utilization and exhibited WT rate of CO2 fixation and growth phenotype.	2-cys	131-136	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	40-44
29078290-10	2017	It is proposed that the Fd-FTR-Trx and NTRC redox systems are linked by the redox balance of 2-Cys Prxs, which is crucial for chloroplast function.	2-cys	93-98	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	39-43
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.	2-cys	48-53	peroxiredoxin 1	Homo sapiens	54-58
28692378-4	2017	NTRC efficiently reduces 2-Cys peroxiredoxins (Prxs), hence having antioxidant function.	2-cys	25-30	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	0-4
28805482-4	2017	Under stressed states, OPDA - accumulated in the chloroplasts - binds and promotes CYP20-3 to transfer electron (e-) from thioredoxins (i.e., type-f2 and -x) to 2-Cys peroxiredoxin B (2-CysPrxB) or serine acetyltransferase 1 (SAT1).	2-cys	161-166	peptidylprolyl isomerase H	Homo sapiens	83-88
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
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	APC regulator of WNT signaling pathway	Homo sapiens	144-147
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
27629822-7	2016	As a general trend, mutations in a yeast 2-Cys Prx (Tsa1) favoring the dimeric state also displayed a decreased catalytic activity.	2-cys	41-46	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	52-56
26612102-2	2016	Human Prx2 is a typical 2-Cys Prx arranged as pentamers of head-to-tail homodimers.	2-cys	24-29	periaxin	Homo sapiens	6-9
26894543-3	2016	Furthermore, several 2-Cys peroxiredoxins, including S. cerevisiae TSA1 and TSA2, are able to switch to chaperone activity upon hyperoxidation of their peroxidatic cysteine.	2-cys	21-26	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	67-71
26894543-3	2016	Furthermore, several 2-Cys peroxiredoxins, including S. cerevisiae TSA1 and TSA2, are able to switch to chaperone activity upon hyperoxidation of their peroxidatic cysteine.	2-cys	21-26	thioredoxin peroxidase TSA2	Saccharomyces cerevisiae S288C	76-80
26486164-4	2015	Therefore, the objective of this study was to test the hypothesis that repeated PMSG/hCG treatment induces 2-Cys Prx expression and overoxidation in the reproductive tracts of female mice.	2-cys	107-112	periaxin	Mus musculus	113-116
26486164-8	2015	Intracellular 2-Cys Prx therefore plays an important role in maintaining the reproductive organ environment of female mice upon exogenous gonadotropin treatment.	2-cys	14-19	periaxin	Mus musculus	20-23
25808059-2	2015	In contrast to most animals, the nematode worm, Caenorhabditis elegans, encodes a single cytosolic 2-Cys Prx, PRDX-2, rendering it an excellent model for examining how peroxiredoxins affect animal physiology and ageing.	2-cys	99-104	Peroxiredoxin prdx-2	Caenorhabditis elegans	110-116
26170166-4	2015	Sulfiredoxin (Srx) is an antioxidant protein that exclusively reduces over-oxidized typical 2-Cys Prx.	2-cys	92-97	sulfiredoxin 1	Homo sapiens	0-12
26170166-4	2015	Sulfiredoxin (Srx) is an antioxidant protein that exclusively reduces over-oxidized typical 2-Cys Prx.	2-cys	92-97	sulfiredoxin 1	Homo sapiens	14-17
26141131-0	2015	Site-directed mutagenesis substituting cysteine for serine in 2-Cys peroxiredoxin (2-Cys Prx A) of Arabidopsis thaliana effectively improves its peroxidase and chaperone functions.	2-cys	62-67	peroxidase	Arabidopsis thaliana	145-155
26141131-1	2015	BACKGROUND AND AIMS: The 2-Cys peroxiredoxin (Prx) A protein of Arabidopsis thaliana performs the dual functions of a peroxidase and a molecular chaperone depending on its conformation and the metabolic conditions.	2-cys	25-30	peroxidase	Arabidopsis thaliana	118-128
26141131-9	2015	KEY RESULTS: Replacement of Ser(150) with Cys(150) led to a marked increase in holdase chaperone and peroxidase activities of 2-Cys Prx A, which was associated with a change in the structure of an important domain of the protein.	2-cys	126-131	peroxidase	Arabidopsis thaliana	101-111
26424450-2	2015	Previous studies showed that the chloroplastic atypical thioredoxin ACHT1 is oxidized by 2-Cys peroxiredoxin (2-Cys Prx) in Arabidopsis plants illuminated with growth light and in turn transmits a disulfide-based signal via yet unknown target proteins in a feedback regulation of photosynthesis.	2-cys	89-94	atypical CYS HIS rich thioredoxin 1	Arabidopsis thaliana	68-73
26424450-2	2015	Previous studies showed that the chloroplastic atypical thioredoxin ACHT1 is oxidized by 2-Cys peroxiredoxin (2-Cys Prx) in Arabidopsis plants illuminated with growth light and in turn transmits a disulfide-based signal via yet unknown target proteins in a feedback regulation of photosynthesis.	2-cys	110-115	atypical CYS HIS rich thioredoxin 1	Arabidopsis thaliana	68-73
26424450-4	2015	Likewise, ACHT4 reacted in planta with 2-Cys Prx, indicating that it is oxidized by a similar disulfide exchange reaction.	2-cys	39-44	atypical CYS HIS rich thioredoxin 4	Arabidopsis thaliana	10-15
26424450-5	2015	ACHT4 further reacted uniquely with the small subunit (APS1) of ADP-glucose pyrophosphorylase (AGPase), the first committed enzyme of the starch synthesis pathway, suggesting that it transfers the disulfides it receives from 2-Cys Prx to APS1 and turns off AGPase.	2-cys	225-230	atypical CYS HIS rich thioredoxin 4	Arabidopsis thaliana	0-5
26424450-5	2015	ACHT4 further reacted uniquely with the small subunit (APS1) of ADP-glucose pyrophosphorylase (AGPase), the first committed enzyme of the starch synthesis pathway, suggesting that it transfers the disulfides it receives from 2-Cys Prx to APS1 and turns off AGPase.	2-cys	225-230	ATP sulfurylase 1	Arabidopsis thaliana	55-59
25407820-0	2015	Sulfiredoxin-1 attenuates oxidative stress via Nrf2/ARE pathway and 2-Cys Prdxs after oxygen-glucose deprivation in astrocytes.	2-cys	68-73	sulfiredoxin 1	Homo sapiens	0-14
25914057-4	2015	We used single-particle analysis and helical processing of electron cryomicroscopy images of human Prx3 filaments induced by low pH to generate a ~7-A resolution 3D structure of the HMW form, the first such structure for a 2-Cys Prx.	2-cys	223-228	periaxin	Homo sapiens	99-102
25560178-4	2015	Under oxidizing conditions, 2-Cys Prxs are susceptible to inactivation by overoxidation of their peroxidatic cysteine, which is enzymatically reverted by sulfiredoxin (Srx).	2-cys	28-33	sulfiredoxin	Arabidopsis thaliana	154-166
25560178-5	2015	In chloroplasts, the redox status of 2-Cys Prxs is highly dependent on NADPH-thioredoxin reductase C (NTRC) and Srx; however, the relationship of these activities in determining the level of 2-Cys Prx overoxidation is unknown.	2-cys	37-42	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	71-100
25560178-5	2015	In chloroplasts, the redox status of 2-Cys Prxs is highly dependent on NADPH-thioredoxin reductase C (NTRC) and Srx; however, the relationship of these activities in determining the level of 2-Cys Prx overoxidation is unknown.	2-cys	37-42	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	102-106
25560178-8	2015	The deficiency of NTRC causes reduced overoxidation of 2-Cys Prxs, whereas the deficiency of Srx has the opposite effect.	2-cys	55-60	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	18-22
25560178-9	2015	Moreover, in vitro analyses show that the disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation, thus explaining the dominant role of NTRC on the level of 2-Cys Prx overoxidation in vivo.	2-cys	203-208	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	182-186
25560178-11	2015	Additionally, the low level of 2-Cys Prx overoxidation in the ntrc mutant is light dependent, suggesting that the redox status of 2-Cys Prxs in chloroplasts depends on light rather than the circadian clock.	2-cys	31-36	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	62-66
25560178-11	2015	Additionally, the low level of 2-Cys Prx overoxidation in the ntrc mutant is light dependent, suggesting that the redox status of 2-Cys Prxs in chloroplasts depends on light rather than the circadian clock.	2-cys	130-135	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	62-66
24624337-1	2014	Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1-4), thiol peroxidases implicated in redox homeostasis and cell signaling.	2-cys	113-118	peroxiredoxin 5	Homo sapiens	23-25
25667319-1	2015	Different peroxidases, including 2-cysteine (2-Cys) peroxiredoxins (PRXs) and thylakoid ascorbate peroxidase (tAPX), have been proposed to be involved in the water-water cycle (WWC) and hydrogen peroxide (H2O2)-mediated signaling in plastids.	2-cys	45-50	peroxidase	Arabidopsis thaliana	10-20
25232487-2	2014	2-Cys Prxs, including Prx1, 2, 3 and 4, have been indicated in multiple oncogenic signaling pathways and thus may contribute to various processes of cancer development.	2-cys	0-5	peroxiredoxin 1	Homo sapiens	22-38
25232487-5	2014	We found that 2-Cys Prxs, in particular, Prx1 and Prx4, were preferentially expressed in cell lines derived from human lung cancer.	2-cys	14-19	peroxiredoxin 1	Homo sapiens	41-45
25232487-5	2014	We found that 2-Cys Prxs, in particular, Prx1 and Prx4, were preferentially expressed in cell lines derived from human lung cancer.	2-cys	14-19	peroxiredoxin 4	Homo sapiens	50-54
25092340-1	2014	The catalytic cysteine of the typical 2-Cys Prx subfamily of peroxiredoxins is occasionally hyperoxidized to cysteine sulfinic acid during the peroxidase catalytic cycle.	2-cys	38-43	periaxin	Mus musculus	44-47
25092340-1	2014	The catalytic cysteine of the typical 2-Cys Prx subfamily of peroxiredoxins is occasionally hyperoxidized to cysteine sulfinic acid during the peroxidase catalytic cycle.	2-cys	38-43	peroxiredoxin 2	Mus musculus	61-75
25002520-3	2014	We solved the crystal structure of the catalytic domain of mouse deiodinase 3 (Dio3), which reveals a close structural similarity to atypical 2-Cys peroxiredoxin(s) (Prx).	2-cys	142-147	deiodinase, iodothyronine type III	Mus musculus	65-77
25002520-3	2014	We solved the crystal structure of the catalytic domain of mouse deiodinase 3 (Dio3), which reveals a close structural similarity to atypical 2-Cys peroxiredoxin(s) (Prx).	2-cys	142-147	deiodinase, iodothyronine type III	Mus musculus	79-83
25009779-2	2014	In mammals, the four typical 2-Cys Prxs (Prxs 1, 2, 3 and 4) are known to regulate H2O2-mediated intracellular signaling.	2-cys	29-34	peroxiredoxin 1	Mus musculus	41-59
25666622-0	2015	How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily.	2-cys	54-59	paired related homeobox 1	Homo sapiens	84-88
25666622-1	2015	2-Cys peroxiredoxins belonging to the Prx1 subfamily are Cys-based peroxidases that control the intracellular levels of H2O2 and seem to assume a chaperone function under oxidative stress conditions.	2-cys	0-5	paired related homeobox 1	Homo sapiens	38-42
25387359-1	2015	AIMS: Typical 2-Cys peroxiredoxins (2-Cys Prxs) are Cys peroxidases that undergo inactivation by hyperoxidation of the catalytic Cys, a modification reversed by ATP-dependent reduction by sulfiredoxin (Srx).	2-cys	14-19	sulfiredoxin	Saccharomyces cerevisiae S288C	188-200
25387359-1	2015	AIMS: Typical 2-Cys peroxiredoxins (2-Cys Prxs) are Cys peroxidases that undergo inactivation by hyperoxidation of the catalytic Cys, a modification reversed by ATP-dependent reduction by sulfiredoxin (Srx).	2-cys	36-41	sulfiredoxin	Saccharomyces cerevisiae S288C	188-200
25448674-3	2014	The interaction of NTRC and chloroplastic thioredoxin x with 2-Cys Prxs has been confirmed in vivo, by bimolecular fluorescence complementation (BiFC) assays, and in vitro, by isothermal titration calorimetry (ITC) experiments.	2-cys	61-66	thioredoxin	Homo sapiens	42-53
25448674-4	2014	In comparison with thioredoxin x, NTRC interacts with 2-Cys Prx with higher affinity, both the thioredoxin and NTR domains of NTRC contributing significantly to this interaction, as demonstrated by using the NTR and thioredoxin modules of the enzyme expressed separately.	2-cys	54-59	periaxin	Homo sapiens	60-63
24624337-1	2014	Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1-4), thiol peroxidases implicated in redox homeostasis and cell signaling.	2-cys	113-118	peroxiredoxin 5	Homo sapiens	0-21
24624337-1	2014	Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1-4), thiol peroxidases implicated in redox homeostasis and cell signaling.	2-cys	113-118	thioredoxin	Homo sapiens	54-65
24624337-1	2014	Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1-4), thiol peroxidases implicated in redox homeostasis and cell signaling.	2-cys	113-118	thioredoxin	Homo sapiens	67-70
24624337-2	2014	Typical 2-Cys PRXs are inactivated by hyperoxidation of the peroxidatic cysteine to cysteine-sulfinic acid, and regenerated in a two-step process involving retro-reduction by sulfiredoxin (SRX) and reduction by TRX.	2-cys	8-13	sulfiredoxin 1	Homo sapiens	175-187
24624337-2	2014	Typical 2-Cys PRXs are inactivated by hyperoxidation of the peroxidatic cysteine to cysteine-sulfinic acid, and regenerated in a two-step process involving retro-reduction by sulfiredoxin (SRX) and reduction by TRX.	2-cys	8-13	sulfiredoxin 1	Homo sapiens	189-192
24624337-2	2014	Typical 2-Cys PRXs are inactivated by hyperoxidation of the peroxidatic cysteine to cysteine-sulfinic acid, and regenerated in a two-step process involving retro-reduction by sulfiredoxin (SRX) and reduction by TRX.	2-cys	8-13	thioredoxin	Homo sapiens	211-214
23967002-7	2013	Here we discuss the current knowledge about the mechanisms controlling 2-Cys Prx overoxidation in chloroplasts, organelles with an important signaling function in plants.	2-cys	71-76	periaxin	Homo sapiens	77-80
24025459-2	2014	Here, we cloned a 2-Cys Prx, BgTPx-1, from the canine Babesia parasite B. gibsoni.	2-cys	18-23	periaxin	Canis lupus familiaris	24-27
24025459-3	2014	Sequence identity between BgTPx-1 and 2-Cys Prx of B. bovis was 81% at the amino acid level.	2-cys	38-43	periaxin	Canis lupus familiaris	44-47
24098506-1	2013	Peroxiredoxin 4 (PRDX4), a member of Peroxiredoxin (PRDX) family, is a typical 2-Cys PRDX.	2-cys	79-84	peroxiredoxin 4	Homo sapiens	0-15
24098506-1	2013	Peroxiredoxin 4 (PRDX4), a member of Peroxiredoxin (PRDX) family, is a typical 2-Cys PRDX.	2-cys	79-84	peroxiredoxin 4	Homo sapiens	17-22
24003226-2	2013	The typical 2-Cys subclass of Prxs (human Prx1-4) utilizes a Cys sulfenic acid (Cys-SOH) intermediate and disulfide bond formation across two subunits during catalysis.	2-cys	12-17	peroxiredoxin 1	Homo sapiens	42-48
23967002-8	2013	Given the prokaryotic origin of chloroplasts, we discuss the occurrence of 2-Cys Prx overoxidation in cyanobacteria with the aim of identifying similarities between chloroplasts and their ancestors regarding their response to hydrogen peroxide.	2-cys	75-80	periaxin	Homo sapiens	81-84
23553940-9	2013	We further found that the decreased Srxn1 correlated with a reduction in 2-Cys Prdxs activity.	2-cys	73-78	sulfiredoxin 1	Rattus norvegicus	36-41
23516120-9	2013	2-cysteine peroxiredoxins (2-Cys Prx) undergo redox-dependent modifications and play important roles in antioxidant defense and signaling.	2-cys	27-32	periaxin	Homo sapiens	33-36
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.	2-cys	8-13	periaxin	Homo sapiens	30-33
23516120-10	2013	The identification of 2-Cys Prx was expected based on its high affinity to H2O2 and is considered as a proof of concept for the approach.	2-cys	22-27	periaxin	Homo sapiens	28-31
23421996-5	2013	The Pin1 binding motif, Thr-Pro, is conserved in the 2-Cys PRDXs, PRDX1-4 and the interactions between Pin1 and PRDX2-4 are also demonstrated.	2-cys	53-58	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	4-8
23421996-5	2013	The Pin1 binding motif, Thr-Pro, is conserved in the 2-Cys PRDXs, PRDX1-4 and the interactions between Pin1 and PRDX2-4 are also demonstrated.	2-cys	53-58	peroxiredoxin 1	Mus musculus	66-71
23421996-5	2013	The Pin1 binding motif, Thr-Pro, is conserved in the 2-Cys PRDXs, PRDX1-4 and the interactions between Pin1 and PRDX2-4 are also demonstrated.	2-cys	53-58	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	103-107
23421996-5	2013	The Pin1 binding motif, Thr-Pro, is conserved in the 2-Cys PRDXs, PRDX1-4 and the interactions between Pin1 and PRDX2-4 are also demonstrated.	2-cys	53-58	peroxiredoxin 2	Mus musculus	112-117
23421996-6	2013	An increase in hydrogen peroxide buildup and a decrease in the peroxidase activity of 2-Cys PRDXs were observed in Pin1 (-/-) mouse embryonic fibroblasts (MEFs), with the activity of PRDXs restored when Pin1 was re-introduced into the cells.	2-cys	86-91	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	115-119
23421996-6	2013	An increase in hydrogen peroxide buildup and a decrease in the peroxidase activity of 2-Cys PRDXs were observed in Pin1 (-/-) mouse embryonic fibroblasts (MEFs), with the activity of PRDXs restored when Pin1 was re-introduced into the cells.	2-cys	86-91	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	203-207
23396059-0	2013	Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin.	2-cys	12-17	sulfiredoxin	Saccharomyces cerevisiae S288C	51-63
23830628-3	2013	A small redox protein, sulfiredoxin (Srx), has been shown to reduce sulfinylated 2-Cys-Prxs and thus to regenerate active 2-Cys-Prxs.	2-cys	122-127	sulfiredoxin 1	Homo sapiens	37-40
22985967-0	2012	Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin.	2-cys	26-31	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	106-110
22985967-5	2012	In this work, we present the crystallographic structure at 2.8A resolution of Tsa1(C47S) in the decameric form [(alpha(2))(5)] with a DTT molecule bound to the active site, representing one of the few available reports of a 2-Cys Prx (AhpC-Prx1 subfamily) (AhpC, alkyl hydroperoxide reductase subunit C) structure that incorporates a ligand.	2-cys	224-229	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	78-82
23830628-3	2013	A small redox protein, sulfiredoxin (Srx), has been shown to reduce sulfinylated 2-Cys-Prxs and thus to regenerate active 2-Cys-Prxs.	2-cys	81-86	sulfiredoxin 1	Homo sapiens	23-35
23830628-3	2013	A small redox protein, sulfiredoxin (Srx), has been shown to reduce sulfinylated 2-Cys-Prxs and thus to regenerate active 2-Cys-Prxs.	2-cys	81-86	sulfiredoxin 1	Homo sapiens	37-40
23830628-3	2013	A small redox protein, sulfiredoxin (Srx), has been shown to reduce sulfinylated 2-Cys-Prxs and thus to regenerate active 2-Cys-Prxs.	2-cys	122-127	sulfiredoxin 1	Homo sapiens	23-35