PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
32218363-3	2020	2-Cys peroxiredoxins, in particular Prx1 and Prx2, were detected as being S-nitrosated in multiple mammalian cells under a variety of conditions.	2-cys	0-5	peroxiredoxin 2	Homo sapiens	45-49	
31629169-7	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	
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	
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	
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	
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	
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	
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	
15941719-1	2005	Although biochemical properties of 2-Cys peroxiredoxins (Prxs) have been extensively studied, their real physiological functions in higher eukaryotic cells remain obscure and certainly warrant further study.	2-cys	35-40	peroxiredoxin 2	Homo sapiens	41-55	
16597467-0	2006	2-Cys Peroxiredoxin TPx-1 is involved in gametocyte development in Plasmodium berghei.	2-cys	0-5	peroxiredoxin 2	Homo sapiens	20-25	
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	
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