PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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.	Peroxides	74-82	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.	Peroxides	11-19	periaxin	Homo sapiens	46-49	
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.	Peroxides	147-155	periaxin	Homo sapiens	46-49	
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.	Peroxides	160-168	periaxin	Homo sapiens	26-29	
31229571-7	2019	Cellular levels of superoxide and peroxides increased at 40  C and 42  C. Heat shock (42  C)-induced increases in Prx3 and Prx-SO3 were inhibited by antioxidants (PEG-catalase, MnTBAP) and a Nrf2 shRNA.	Peroxides	34-43	periaxin	Homo sapiens	114-117	
31158443-1	2019	Peroxiredoxin 1 (Prx1) is a member of the Prx family that detoxifies various peroxide substrates through conserved catalytic cysteine residues with the use of reducing equivalents.	Peroxides	77-85	periaxin	Homo sapiens	17-20	
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.	Peroxides	96-104	periaxin	Homo sapiens	63-66	
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.	Peroxides	84-93	periaxin	Homo sapiens	103-106	
25399604-4	2014	Prx, by having a low pKa cysteine, is less efficient than Gpx in reduction of peroxides under physiological conditions, but the chemistry of the sulfur together with the peculiar structural arrangement of the active site, in typical Prxs, make it suitable to sense a redox environment and to switch-in-function so as to exert holdase activity under redox-stress conditions.	Peroxides	78-87	periaxin	Homo sapiens	0-3