PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25011585-10	2014	Exogenous H2O2 treatment decreased ERalpha protein levels in ER-positive cells.	Hydrogen Peroxide	10-14	estrogen receptor 1	Homo sapiens	35-42	
21270601-13	2011	Further, apoptosis induced by H2O2 was inhibited by estrogen in the ER-alpha-positive cells.	Hydrogen Peroxide	30-34	estrogen receptor 1	Homo sapiens	68-76	
20962025-6	2011	Under these conditions, ERalpha activation selectively prevented increased hydrogen peroxide (H(2)O(2)) and total intracellular reactive oxygen species (ROS) production, caused up-regulation of manganese superoxide dismutase protein and activity, and inhibited prolonged ERK phosphorylation.	Hydrogen Peroxide	75-92	estrogen receptor 1	Homo sapiens	24-31	
17915203-8	2007	The percentage of residual damage after H(2)O(2) treatment followed by 3h of post-incubation is significantly higher in patients and also correlates positively with SOD activity, ER and PR expression and negatively with the basal DNA damage.	Hydrogen Peroxide	40-48	estrogen receptor 1	Homo sapiens	179-181	
32998583-3	2020	In the placenta tissues of PE patients and H2O2-treated human trophoblast cell line HTR-8/SVneo, the expressions of LncRNA NEAT1, p53, and estrogen receptor alpha (ESRalpha) were increased whereas miR-18a-5p expression was decreased.	Hydrogen Peroxide	43-47	estrogen receptor 1	Homo sapiens	139-162	
32998583-3	2020	In the placenta tissues of PE patients and H2O2-treated human trophoblast cell line HTR-8/SVneo, the expressions of LncRNA NEAT1, p53, and estrogen receptor alpha (ESRalpha) were increased whereas miR-18a-5p expression was decreased.	Hydrogen Peroxide	43-47	estrogen receptor 1	Homo sapiens	164-172	
12361722-6	2002	We demonstrated here, for the first time, that oxidative stress induced by hydrogen peroxide (H(2)O(2)), Fe(2+), 2,2"-azobis(2-amidinopropane)dihydrochloride (AAPH) and activated macrophages, affect the expression of estrogen receptors alpha and beta (ERalpha and ERbeta) differently, demonstrating cell-specific response which can be blocked by antioxidants.	Hydrogen Peroxide	75-92	estrogen receptor 1	Homo sapiens	217-250	
12361722-6	2002	We demonstrated here, for the first time, that oxidative stress induced by hydrogen peroxide (H(2)O(2)), Fe(2+), 2,2"-azobis(2-amidinopropane)dihydrochloride (AAPH) and activated macrophages, affect the expression of estrogen receptors alpha and beta (ERalpha and ERbeta) differently, demonstrating cell-specific response which can be blocked by antioxidants.	Hydrogen Peroxide	75-92	estrogen receptor 1	Homo sapiens	252-259	
12361722-6	2002	We demonstrated here, for the first time, that oxidative stress induced by hydrogen peroxide (H(2)O(2)), Fe(2+), 2,2"-azobis(2-amidinopropane)dihydrochloride (AAPH) and activated macrophages, affect the expression of estrogen receptors alpha and beta (ERalpha and ERbeta) differently, demonstrating cell-specific response which can be blocked by antioxidants.	Hydrogen Peroxide	94-102	estrogen receptor 1	Homo sapiens	217-250	
12361722-6	2002	We demonstrated here, for the first time, that oxidative stress induced by hydrogen peroxide (H(2)O(2)), Fe(2+), 2,2"-azobis(2-amidinopropane)dihydrochloride (AAPH) and activated macrophages, affect the expression of estrogen receptors alpha and beta (ERalpha and ERbeta) differently, demonstrating cell-specific response which can be blocked by antioxidants.	Hydrogen Peroxide	94-102	estrogen receptor 1	Homo sapiens	252-259	
10913246-2	2000	Full-length (67 kDa) ER or its 11 kDa recombinant DNA-binding domain (ER-DBD) is also susceptible to loss of structure and function by the action of oxidants such as diamide and hydrogen peroxide; however, prior DNA binding by ER or ER-DBD protects against this oxidant induced loss of function.	Hydrogen Peroxide	178-195	estrogen receptor 1	Homo sapiens	21-23	
10913246-2	2000	Full-length (67 kDa) ER or its 11 kDa recombinant DNA-binding domain (ER-DBD) is also susceptible to loss of structure and function by the action of oxidants such as diamide and hydrogen peroxide; however, prior DNA binding by ER or ER-DBD protects against this oxidant induced loss of function.	Hydrogen Peroxide	178-195	estrogen receptor 1	Homo sapiens	70-72	
10913246-2	2000	Full-length (67 kDa) ER or its 11 kDa recombinant DNA-binding domain (ER-DBD) is also susceptible to loss of structure and function by the action of oxidants such as diamide and hydrogen peroxide; however, prior DNA binding by ER or ER-DBD protects against this oxidant induced loss of function.	Hydrogen Peroxide	178-195	estrogen receptor 1	Homo sapiens	70-72	
28755608-5	2018	The ERalpha-MP-Ab-HRP bioconjugate formed was injected into the microFED and incubated with the DNA-ERE-modified electrodes, followed by amperometric detection with application of -0.2V vs. Ag AgCl while a mixture of H2O2 and hydroquinone was injected into the microfluidic device.	Hydrogen Peroxide	217-221	estrogen receptor 1	Homo sapiens	4-11	
26383254-5	2015	We found that in human SY5Y and IMR-32 cells, the estrogen neuroprotection against H2O2 toxicity was abrogated by knockdown of a variant of estrogen receptor-alpha, ER-alpha36.	Hydrogen Peroxide	83-87	estrogen receptor 1	Homo sapiens	140-163	
25280774-8	2015	Down-regulation of ERalpha expression by siRNA before E2 addition resulted in the failure of the E2-mediated inhibition of H2O2-induced protein PARylation and AIF nucleolar translocation.	Hydrogen Peroxide	123-127	estrogen receptor 1	Homo sapiens	19-26