PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34552582-4	2021	Properdin in WT kidneys was also upregulated by IR, while H2O2-increased properdin in TECs was reduced by its small-interfering RNA (siRNA), with raised HMGB1 and apoptosis.	Hydrogen Peroxide	58-62	high mobility group box 1	Mus musculus	153-158	
31159590-8	2019	Additionally, our results demonstrate that anagliptin decreased the vulnerability of cells to hydrogen peroxide (H2O2)-induced secondary insult by increasing cell viability and reducing the secretion of lactate dehydrogenase (LDH) and high mobility group box 1 protein (HMGB-1).	Hydrogen Peroxide	94-111	high mobility group box 1	Mus musculus	235-268	
31159590-8	2019	Additionally, our results demonstrate that anagliptin decreased the vulnerability of cells to hydrogen peroxide (H2O2)-induced secondary insult by increasing cell viability and reducing the secretion of lactate dehydrogenase (LDH) and high mobility group box 1 protein (HMGB-1).	Hydrogen Peroxide	94-111	high mobility group box 1	Mus musculus	270-276	
31159590-8	2019	Additionally, our results demonstrate that anagliptin decreased the vulnerability of cells to hydrogen peroxide (H2O2)-induced secondary insult by increasing cell viability and reducing the secretion of lactate dehydrogenase (LDH) and high mobility group box 1 protein (HMGB-1).	Hydrogen Peroxide	113-117	high mobility group box 1	Mus musculus	235-268	
31159590-8	2019	Additionally, our results demonstrate that anagliptin decreased the vulnerability of cells to hydrogen peroxide (H2O2)-induced secondary insult by increasing cell viability and reducing the secretion of lactate dehydrogenase (LDH) and high mobility group box 1 protein (HMGB-1).	Hydrogen Peroxide	113-117	high mobility group box 1	Mus musculus	270-276	
27924516-4	2016	Immunofluorescence staining showed that HMGB1 in the medium- and CORM-2-treated groups was predominantly localized in the nucleus of the cells, whereas higher amounts of HMGB1 translocated to the cytoplasm in the H2O2- and inactive CORM-2 (iCORM-2)-treated groups.	Hydrogen Peroxide	213-217	high mobility group box 1	Mus musculus	40-45	
31026770-2	2019	Acetylation and phosphorylation of HMGB1 are implicated in the regulation of its nucleocytoplasmic translocation for secretion, although inflammatory stimuli are known to induce H2O2 production.	Hydrogen Peroxide	178-182	high mobility group box 1	Mus musculus	35-40	
31026770-3	2019	Here we show that H2O2-induced oxidation of HMGB1, which results in the formation of an intramolecular disulfide bond between Cys23 and Cys45, is necessary and sufficient for its nucleocytoplasmic translocation and secretion.	Hydrogen Peroxide	18-22	high mobility group box 1	Mus musculus	44-49	
31026770-4	2019	The oxidation is catalyzed by peroxiredoxin I (PrxI) and PrxII, which are first oxidized by H2O2 and then transfer their disulfide oxidation state to HMGB1.	Hydrogen Peroxide	92-96	high mobility group box 1	Mus musculus	150-155	
27924516-4	2016	Immunofluorescence staining showed that HMGB1 in the medium- and CORM-2-treated groups was predominantly localized in the nucleus of the cells, whereas higher amounts of HMGB1 translocated to the cytoplasm in the H2O2- and inactive CORM-2 (iCORM-2)-treated groups.	Hydrogen Peroxide	213-217	high mobility group box 1	Mus musculus	170-175	
27924516-5	2016	Western blotting of HMGB1 showed that the total amounts of cytoplasmic HMGB1 in the H2O2-treated (0.59+-0.27) and iCORM-2-treated (0.57+-0.22) groups were markedly higher than those in the medium-treated (0.19+-0.05) and CORM-2-treated (0.21+-0.10) groups (P<0.05).	Hydrogen Peroxide	84-88	high mobility group box 1	Mus musculus	71-76	
24970745-5	2014	In vitro studies confirmed that exposure to hydrogen peroxide and CCl4 induced an intracellular mobilization and extracellular release of nuclear HMGB1 peptides in clone-9 and primary hepatocytes, respectively.	Hydrogen Peroxide	44-61	high mobility group box 1	Mus musculus	146-151