PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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.	1-cys	105-110	periaxin	Homo sapiens	53-56	
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.	1-cys	96-101	periaxin	Homo sapiens	10-13	
27353378-6	2016	Among the six Prxs in mammals, Prx6 is the only 1-Cys Prx.	1-cys	48-53	periaxin	Homo sapiens	14-17	
24194195-15	2014	The C(31) residue does not function as a resolving Cys and therefore the TcPrx2 must follow the reaction mechanism of 1-Cys Prx.	1-cys	118-123	periaxin	Homo sapiens	75-78	
23178658-5	2013	In this study 1-Cys peroxiredoxin (1-Cys-Prx) from Plasmodium vivax and Plasmodium knowlesi were cloned and characterized.	1-cys	14-19	periaxin	Homo sapiens	41-44	
23178658-5	2013	In this study 1-Cys peroxiredoxin (1-Cys-Prx) from Plasmodium vivax and Plasmodium knowlesi were cloned and characterized.	1-cys	35-40	periaxin	Homo sapiens	41-44	
23178658-6	2013	The complete genes coding for 1-Cys-Prx of P. vivax (Pv1-Cys-Prx) and P. knowlesi (Pk1-Cys-Prx) were PCR amplified and the recombinant proteins were produced by heterologous over-expression in Escherichia coli.	1-cys	30-35	periaxin	Homo sapiens	36-39	
23178658-6	2013	The complete genes coding for 1-Cys-Prx of P. vivax (Pv1-Cys-Prx) and P. knowlesi (Pk1-Cys-Prx) were PCR amplified and the recombinant proteins were produced by heterologous over-expression in Escherichia coli.	1-cys	30-35	periaxin	Homo sapiens	61-64	
23178658-6	2013	The complete genes coding for 1-Cys-Prx of P. vivax (Pv1-Cys-Prx) and P. knowlesi (Pk1-Cys-Prx) were PCR amplified and the recombinant proteins were produced by heterologous over-expression in Escherichia coli.	1-cys	30-35	periaxin	Homo sapiens	61-64	
20059400-2	2010	Saccharomyces cerevisiae Prx1 is a mitochondrial enzyme belonging to the 1-Cys Prx, whereas Grx2 is involved in antioxidant defense and localizes at the mitochondria, so we hypothesized that it could be a perfect candidate to resolve the sulfenate in Prx1 with GSH.	1-cys	73-78	periaxin	Homo sapiens	25-28	
21472329-3	2010	In a previous study, differentially regulated proteins under DEK knockdown conditions, including the up-regulated protein 1-cys peroxiredoxin (1-cys Prx), were identified by proteome analysis.	1-cys	122-127	periaxin	Homo sapiens	149-152	
21472329-4	2010	Here, an in vivo reporter assay with short hairpin RNA-mediated DEK knockdown revealed that DEK negatively regulated 1-cys Prx transcription, and that the NF-kappaB subunit p65 had a synergistic effect on this DEK-mediated repression.	1-cys	117-122	periaxin	Homo sapiens	123-126	
21472329-5	2010	Both proteins are recruited to the 1-cys Prx promoter region and regulate its transcription.	1-cys	35-40	periaxin	Homo sapiens	41-44	
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.	1-cys	144-149	periaxin	Homo sapiens	150-153	
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.	1-cys	154-159	periaxin	Homo sapiens	160-163	
16916801-2	2006	1-Cys B-Prxs, homologous to human PrxVI, were recently shown to be reactivated by glutathione S-transferase (GST) pi via the formation of a GST-Prx heterodimer and Prx glutathionylation.	1-cys	0-5	periaxin	Homo sapiens	8-11	
17103164-5	2007	A gene encoding an antioxidant enzyme, 1-cysteine peroxiredoxin (1-Cys Prx), was identified in an expressed sequence tag database of the A. camphorata and cloned by polymerase chain reaction.	1-cys	65-70	periaxin	Homo sapiens	71-74	
17103164-6	2007	The 1-Cys Prx cDNA (837 bp, accession no.	1-cys	4-9	periaxin	Homo sapiens	10-13	
17103164-8	2007	The deduced protein shared 44-58% identity with 1-Cys Prx from Homo sapiens, Bos taurus, and Saccharomyces cerevisia.	1-cys	48-53	periaxin	Homo sapiens	54-57	
17103164-11	2007	The recombinant 1-Cys Prx was purified by Ni(2+)-nitrilotriacetic acid (Sepharose).	1-cys	16-21	periaxin	Homo sapiens	22-25	
16916801-2	2006	1-Cys B-Prxs, homologous to human PrxVI, were recently shown to be reactivated by glutathione S-transferase (GST) pi via the formation of a GST-Prx heterodimer and Prx glutathionylation.	1-cys	0-5	periaxin	Homo sapiens	34-37	
16916801-4	2006	To investigate the mechanistic events that mediate the 1-Cys D-Prx regeneration, interaction of the Prx with glutathione was studied by mass spectrometry and NMR.	1-cys	55-60	periaxin	Homo sapiens	63-66	
16916801-4	2006	To investigate the mechanistic events that mediate the 1-Cys D-Prx regeneration, interaction of the Prx with glutathione was studied by mass spectrometry and NMR.	1-cys	55-60	periaxin	Homo sapiens	100-103	
16916801-6	2006	Evidences are reported that the glutathionylation of 1-Cys D-Prx induces the dissociation of the Prx non-covalent homodimer, which can be recovered by reduction with dithiothreitol.	1-cys	53-58	periaxin	Homo sapiens	61-64	
16916801-6	2006	Evidences are reported that the glutathionylation of 1-Cys D-Prx induces the dissociation of the Prx non-covalent homodimer, which can be recovered by reduction with dithiothreitol.	1-cys	53-58	periaxin	Homo sapiens	97-100	
15701514-4	2005	We describe the common Prx fold and show that the dimeric PfAOP can be mechanistically categorized as a 1-Cys Prx.	1-cys	104-109	periaxin	Homo sapiens	110-113	
16401067-1	2006	Glutathione S-transferase pi (GST pi) has been shown to reactivate oxidized 1-cysteine peroxiredoxin (1-Cys Prx, Prx VI, Prdx6, and AOP2).	1-cys	102-107	periaxin	Homo sapiens	108-111	
16401067-5	2006	In the heterodimer, 1-Cys Prx is fully active toward either H2O2 or phospholipid hydroperoxide, while the GST pi activity is approximately 25% of that of the GST pi homodimer.	1-cys	20-25	periaxin	Homo sapiens	26-29	
16401067-12	2006	For 1-Cys Prx, neither Cys47 nor Ser32 is required for heterodimer formation but Cys47 is essential for 1-Cys Prx activation.	1-cys	4-9	periaxin	Homo sapiens	10-13	
16401067-14	2006	We conclude that reactivation of oxidized 1-Cys Prx by GST pi occurs by heterodimerization of 1-Cys Prx and GST pi harboring bound GSH, followed by glutathionylation of 1-Cys Prx and then formation of an intersubunit disulfide.	1-cys	42-47	periaxin	Homo sapiens	48-51	
11463468-3	2001	The sequence identity between the PfPrx-1 and the previously reported 1-Cys Prx of P. falciparum (PfPrx-2), which corresponded to mammalian type VI Prx, was 25%.	1-cys	70-75	periaxin	Homo sapiens	36-39	
11463468-3	2001	The sequence identity between the PfPrx-1 and the previously reported 1-Cys Prx of P. falciparum (PfPrx-2), which corresponded to mammalian type VI Prx, was 25%.	1-cys	70-75	periaxin	Homo sapiens	76-79