PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31079497-4 2019 RESULTS: Knockdown of Srxn1 could promote the secretion of LDH and MDA, decrease the activity of SOD and aggravate apoptosis of astrocytes induced by H2O2. Hydrogen Peroxide 150-154 sulfiredoxin 1 Homo sapiens 22-27 31079497-0 2019 Effects of Srxn1 on growth and Notch signalling of astrocyte induced by hydrogen peroxide. Hydrogen Peroxide 72-89 sulfiredoxin 1 Homo sapiens 11-16 31079497-1 2019 OBJECTIVE: To investigate the effect of Sulfiredoxin-1 (Srxn1) on astrocyte injury induced by hydrogen peroxide (H2O2). Hydrogen Peroxide 94-111 sulfiredoxin 1 Homo sapiens 40-54 31079497-5 2019 The results of Western blot, ELISA assay and flow cytometry indicated that activation of the Notch signalling pathway attenuated the effect of Srxn1 on H2O2-induced oxidative damage and apoptosis of astrocytes. Hydrogen Peroxide 152-156 sulfiredoxin 1 Homo sapiens 143-148 31079497-1 2019 OBJECTIVE: To investigate the effect of Sulfiredoxin-1 (Srxn1) on astrocyte injury induced by hydrogen peroxide (H2O2). Hydrogen Peroxide 94-111 sulfiredoxin 1 Homo sapiens 56-61 31079497-1 2019 OBJECTIVE: To investigate the effect of Sulfiredoxin-1 (Srxn1) on astrocyte injury induced by hydrogen peroxide (H2O2). Hydrogen Peroxide 113-117 sulfiredoxin 1 Homo sapiens 40-54 31079497-6 2019 CONCLUSION: Srxn1 may protect astrocytes from oxidative stress injury induced by H2O2 by activation of Notch signalling pathway. Hydrogen Peroxide 81-85 sulfiredoxin 1 Homo sapiens 12-17 31079497-1 2019 OBJECTIVE: To investigate the effect of Sulfiredoxin-1 (Srxn1) on astrocyte injury induced by hydrogen peroxide (H2O2). Hydrogen Peroxide 113-117 sulfiredoxin 1 Homo sapiens 56-61 27497909-0 2016 Mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin: Linking mitochondrial function to circadian rhythm. Hydrogen Peroxide 14-18 sulfiredoxin 1 Homo sapiens 92-104 31079497-2 2019 METHODS: Observing the changes of H2O2 on contents of lactate dehydrogenase (LDH), malondialdehyde (MDA), superoxide dismutase (SOD) and apoptosis after transfected Srxn1 siRNA into astrocytes. Hydrogen Peroxide 34-38 sulfiredoxin 1 Homo sapiens 165-170 28236420-0 2016 Mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin: Linking mitochondrial function to circadian rhythm. Hydrogen Peroxide 14-18 sulfiredoxin 1 Homo sapiens 92-104 28236420-8 2016 Cytosolic Srx was found to be imported into mitochondria via a mechanism that requires formation of a disulfide-linked complex with heat shock protein 90, which is likely promoted by H2O2 released from mitochondria. Hydrogen Peroxide 183-187 sulfiredoxin 1 Homo sapiens 10-13 30863778-7 2019 Western blotting showed that, in the gastric tumor cell line BGC823, the Srx protein was upregulated in response to H2O2 treatment, although it was inadequate to counteract the increased oxidative stress, as indicated by the gradually increasing level of malondialdehyde (MDA). Hydrogen Peroxide 116-120 sulfiredoxin 1 Homo sapiens 73-76 27497909-8 2016 Cytosolic Srx was found to be imported into mitochondria via a mechanism that requires formation of a disulfide-linked complex with heat shock protein 90, which is likely promoted by H2O2 released from mitochondria. Hydrogen Peroxide 183-187 sulfiredoxin 1 Homo sapiens 10-13 25620665-7 2015 In addition, Srxn1 appeared to influence the strength of TLR4 signaling pathway; the expression of COX-2, IL-6, and NOS2 were strongly induced by OGD/R and H2O2 in astrocyte cultures with Srxn1-shRNAs. Hydrogen Peroxide 156-160 sulfiredoxin 1 Homo sapiens 13-18 25620665-7 2015 In addition, Srxn1 appeared to influence the strength of TLR4 signaling pathway; the expression of COX-2, IL-6, and NOS2 were strongly induced by OGD/R and H2O2 in astrocyte cultures with Srxn1-shRNAs. Hydrogen Peroxide 156-160 sulfiredoxin 1 Homo sapiens 188-193 25620665-8 2015 Our results suggested that loss of Srxn1 expression in astrocytes may cause excessive activation of inflammatory responses which contribute to OGD/R- and H2O2-induced cell death. Hydrogen Peroxide 154-158 sulfiredoxin 1 Homo sapiens 35-40 23830628-5 2013 Here, we describe the methods used to monitor the interplay between NO and H2O2 in the regulation of the Prx/Srx system in immunostimulated macrophages, which produce both reactive oxygen species and NO. Hydrogen Peroxide 75-79 sulfiredoxin 1 Homo sapiens 109-112 21466852-3 2011 A small redox protein, sulfiredoxin (Srx), conserved only in eukaryotes, has been shown to reduce sulfinylated 2-Cys Prx"s, adding to the complexity of the H2O2 signaling network. Hydrogen Peroxide 156-160 sulfiredoxin 1 Homo sapiens 23-35 21466852-3 2011 A small redox protein, sulfiredoxin (Srx), conserved only in eukaryotes, has been shown to reduce sulfinylated 2-Cys Prx"s, adding to the complexity of the H2O2 signaling network. Hydrogen Peroxide 156-160 sulfiredoxin 1 Homo sapiens 37-40 15952770-1 2005 Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell signaling. Hydrogen Peroxide 102-119 sulfiredoxin 1 Homo sapiens 14-17 23830628-0 2013 Peroxiredoxins and sulfiredoxin at the crossroads of the NO and H2O2 signaling pathways. Hydrogen Peroxide 64-68 sulfiredoxin 1 Homo sapiens 19-31 22989627-4 2012 LH treatment increased H(2)O(2) levels within 15 min, which, in turn, induced Srx gene expression in cultured preovulatory follicles. Hydrogen Peroxide 23-31 sulfiredoxin 1 Homo sapiens 78-81 22989627-6 2012 LH- or H(2)O(2)-stimulated Srx mRNA levels were suppressed by inhibitors of antioxidant agents and MAPK kinase. Hydrogen Peroxide 7-15 sulfiredoxin 1 Homo sapiens 27-30 19176523-10 2009 These results indicate that Srx plays a crucial role in the reactivation of sulfinic mitochondrial Prx III and that its mitochondrial translocation is critical in maintaining the balance between mitochondrial H(2)O(2) production and elimination. Hydrogen Peroxide 209-217 sulfiredoxin 1 Homo sapiens 28-31 15590625-6 2005 Sulfinic forms of Prx I and Prx II, but not of Prx VI or GAPDH, present in H2O2-treated A549 cells were gradually reduced after removal of H2O2; overexpression of Srx increased the rate of the reduction of Prx I and Prx II but did not induce that of Prx VI or GAPDH. Hydrogen Peroxide 75-79 sulfiredoxin 1 Homo sapiens 163-166