PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11487528-7 2001 Peroxynitrite, a highly reactive nitrogen molecule derived from the interaction of NO and superoxide anion, significantly increased COX-2 expression. Superoxides 90-106 mitochondrially encoded cytochrome c oxidase II Homo sapiens 132-137 14988266-6 2004 In addition, an antioxidant and inhibitors of mitochondrial superoxide, NADPH oxidase, and glucose metabolism to glucosamine also blocked high glucose-induced COX-2 expression to varying degrees. Superoxides 60-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 159-164 11721898-7 2001 On the basis of the studies of the CL, fluorescence, UV-vis and ESCA spectra and the effect of dissolved oxygen in luminol solution, a mechanism for CL emission in unbuffered solution was considered as the formation of a superoxide radical ion during the decomposition of H2O2 catalyzed by the Co(II)-ethanolamine immobilized resin. Superoxides 221-239 mitochondrially encoded cytochrome c oxidase II Homo sapiens 294-299 34999424-0 2022 Reaction of a {Co(NO)}8 complex with superoxide: Formation of a six coordinated (CoII(NO)(O2-)) species followed by peroxynitrite intermediate. Superoxides 37-47 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-85 8595067-5 1995 The time dependence of COX-2 inhibitors might afford some clues to a better understanding of the mechanism of COX-2 selective inhibition, on the discrepancy between some authors about the potency of the drug and on the relationship between COX-2 inhibition and inhibition of superoxide anion production, an event also characterized by a time dependence. Superoxides 275-291 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-28 8595067-5 1995 The time dependence of COX-2 inhibitors might afford some clues to a better understanding of the mechanism of COX-2 selective inhibition, on the discrepancy between some authors about the potency of the drug and on the relationship between COX-2 inhibition and inhibition of superoxide anion production, an event also characterized by a time dependence. Superoxides 275-291 mitochondrially encoded cytochrome c oxidase II Homo sapiens 110-115 8595067-5 1995 The time dependence of COX-2 inhibitors might afford some clues to a better understanding of the mechanism of COX-2 selective inhibition, on the discrepancy between some authors about the potency of the drug and on the relationship between COX-2 inhibition and inhibition of superoxide anion production, an event also characterized by a time dependence. Superoxides 275-291 mitochondrially encoded cytochrome c oxidase II Homo sapiens 110-115 1316186-3 1992 Superoxide radical was generated from the reaction of H2O2 with Co(II), but was inhibited when Co(II) was chelated with adenosine 5"-diphosphate or citrate. Superoxides 0-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-70 1316186-3 1992 Superoxide radical was generated from the reaction of H2O2 with Co(II), but was inhibited when Co(II) was chelated with adenosine 5"-diphosphate or citrate. Superoxides 0-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 1316186-9 1992 In the presence of ethylenediamine, Co(II) bound molecular O2 and directly oxidized DMPO to its DMPO/.OH adduct without first forming free superoxide, hydroxyl radical, or hydrogen peroxide. Superoxides 139-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-42 1848978-2 1991 The order of inducing effect of metal ions on hydralazine-dependent DNA damage [Cu(II) greater than Co(II) greater than Fe(III)] was related to that of accelerating effect on the O2 consumption rate of hydralazine autoxidation. Superoxides 179-181 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 31867480-4 2019 The Co(II) ion in complex Co1 was coordinated by the N4O2 mode provided by two L ligands and two SCN- anions. Superoxides 53-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 31867480-5 2019 The two Co(II) ions in Co2 were in the N2O4 and NO5 coordination environment and were linked by two mu2-OAc- bridges and one rare mu3-OAc- bridge. Superoxides 39-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 8-14 26799113-0 2016 Oxygen Activation by Co(II) and a Redox Non-Innocent Ligand: Spectroscopic Characterization of a Radical-Co(II)-Superoxide Complex with Divergent Catalytic Reactivity. Superoxides 112-122 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-27 26799113-0 2016 Oxygen Activation by Co(II) and a Redox Non-Innocent Ligand: Spectroscopic Characterization of a Radical-Co(II)-Superoxide Complex with Divergent Catalytic Reactivity. Superoxides 112-122 mitochondrially encoded cytochrome c oxidase II Homo sapiens 105-111 18854902-6 2008 The results indicate that Co(II) binds O2 in the presence of GGH, and leads to the formation of a DMPO-HO adduct without first forming free superoxide or hydroxyl radical, supporting the participation of a reactive high-valent cobalt complex. Superoxides 140-150 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 21731109-7 2008 Redox potentials for structurally-related Co(II) complexes are shown to be cathodically-shifted relative to their Fe(II) analogues, making them ineffective reducing agents for substrates such as superoxide. Superoxides 195-205 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-48 15998028-7 2005 As the redox potentials to convert the Co(II) to Co(III) are high, it can be inferred that the redox potential of the Co(II)-substituted SOD may be outside the range required to convert the superoxide radical (O2*-) to hydrogen peroxide, and this is sufficient to explain the inactivity of the enzyme. Superoxides 190-208 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 15998028-7 2005 As the redox potentials to convert the Co(II) to Co(III) are high, it can be inferred that the redox potential of the Co(II)-substituted SOD may be outside the range required to convert the superoxide radical (O2*-) to hydrogen peroxide, and this is sufficient to explain the inactivity of the enzyme. Superoxides 190-208 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-124 15998028-7 2005 As the redox potentials to convert the Co(II) to Co(III) are high, it can be inferred that the redox potential of the Co(II)-substituted SOD may be outside the range required to convert the superoxide radical (O2*-) to hydrogen peroxide, and this is sufficient to explain the inactivity of the enzyme. Superoxides 210-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 15998028-7 2005 As the redox potentials to convert the Co(II) to Co(III) are high, it can be inferred that the redox potential of the Co(II)-substituted SOD may be outside the range required to convert the superoxide radical (O2*-) to hydrogen peroxide, and this is sufficient to explain the inactivity of the enzyme. Superoxides 210-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-124 31691474-6 2020 The experimental studies and DFT calculations reveal that the high performance of the Co@FLG is mainly attributed to its great O2 absorptivity endowed by the abundant Co-Nx and pyridinic-N in the FLG shell and the strong electron-donating ability from the Co ND core to the FLG shell to elevate the eg-orbital energy of Co(II) and lower the activation energy for breaking the O=O/O-O bonds. Superoxides 127-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 320-326 31691474-6 2020 The experimental studies and DFT calculations reveal that the high performance of the Co@FLG is mainly attributed to its great O2 absorptivity endowed by the abundant Co-Nx and pyridinic-N in the FLG shell and the strong electron-donating ability from the Co ND core to the FLG shell to elevate the eg-orbital energy of Co(II) and lower the activation energy for breaking the O=O/O-O bonds. Superoxides 380-383 mitochondrially encoded cytochrome c oxidase II Homo sapiens 320-326 31841322-3 2020 The organic ligands coordinate equatorially to the two CoII ions via two bidentate (O,S) N-acylthiourea moieties and tridentate to the central Ln ion via the (O,N,O) 2,6-dipicolinoyl moieties. Superoxides 159-164 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-59 31648572-7 2020 Abbreviations AKT protein kinase B ARMS alveolar rhabdomyosarcoma ATM ataxia telangiectasia mutated Bax Bcl-2-associated X protein Bcl-2 B-cell lymphoma 2 CDC2 cyclin-dependent kinase 2 Bcl-xL B-cell lymphoma-extra large c-FLIP cellular FLICE-like inhibitory protein CDDP cisplatin COX-2 cyclooxygenase-2 cyt c cytochrome c DNA-PKcs DNA-dependent protein kinase EGFR epidermal growth factor receptor EMT epithelial-mesenchymal transition ERK extracellular signal-regulated kinase ES Ewing`s sarcoma ETS2 erythroblastosis virus transcription factor 2 GBM glioblastoma multiforme HCC hepatocellular carcinoma HNSCC head and neck squamous cell carcinoma IAP inhibitor of apoptosis protein IkappaBalpha inhibitor of kappaB alpha IKK inhibitor of kappaB kinase IR ionizing radiation lncRNA long non-coding RNA luc luciferase Mcl-1 myeloid cell leukemia-1 MDR1 multidrug resistance protein 1 miR microRNA MMP-9 matrix metalloproteinase-9 mTOR mammalian target of rapamycin NB neuroblastoma NF-kappaB nuclear factor-kappaB NPC nasopharyngeal carcinoma NSCLC non-small cell lung cancer OSCC oral squamous cell carcinoma PARP poly-(ADP-ribose)-polymerase pH2AX phosphorylated histone 2AX-immunoreactive PI3K phosphatidylinositol 3-kinase Prp4K Pre-mRNA processing factor 4 kinase RCC renal cell carcinoma ROS reactive oxygen species SCC squamous cell carcinoma SLN solid lipid nanoparticle SOD2 superoxide dismutase 2 TERT telomerase reverse transcriptase TNF-alpha tumor necrosis factor-alpha TxnRd1 thioredoxin reductase-1 VEGF vascular endothelial growth factor XIAP X-linked inhibitor of apoptosis protein DeltaPsim mitochondrial membrane potential. Superoxides 1386-1396 mitochondrially encoded cytochrome c oxidase II Homo sapiens 282-287 26140661-7 2015 Comparable changes in COX-2 mRNA, miR-16 and c-Myc detected in dHUVEC were produced in nHUVEC exposed to transient high glucose and then stimulated with IL-1beta under physiological glucose levels; superoxide anion production was enhanced under these experimental conditions. Superoxides 198-214 mitochondrially encoded cytochrome c oxidase II Homo sapiens 22-27 26140661-8 2015 CONCLUSIONS AND IMPLICATIONS: Our results describe a possible mechanism operating in GDM that links the enhanced superoxide anion production and epigenetic changes, associated with hyperglycaemic memory, to endothelial dysfunction through dysregulated post-transcriptional control of COX-2 gene expression in response to inflammatory stimuli. Superoxides 113-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 284-289 22354161-6 2012 Investigation of the antioxidative properties showed that the polymeric Co(II) complex has a strong radical scavenging potency against hydroxyl radicals, 2,2-diphenyl-1-picrylhydrazyl radicals, nitric oxide and superoxide anion radicals. Superoxides 211-236 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-78 22175783-1 2012 The first example of an O(2) adduct of an active Co-substituted oxygenase has been observed in the extradiol ring cleavage of the electron-poor substrate 4-nitrocatechol (4NC) by Co(II)-homoprotocatechuate 2,3-dioxygenase (Co-HPCD). Superoxides 24-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 179-185 22175783-2 2012 Upon O(2) binding to the high-spin Co(II) (S = (3)/(2)) enzyme-substrate complex, an S = (1)/(2) EPR signal exhibiting (59)Co hyperfine splitting (A = 24 G) typical of a low-spin Co(III)-superoxide complex was observed. Superoxides 5-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 22175783-2 2012 Upon O(2) binding to the high-spin Co(II) (S = (3)/(2)) enzyme-substrate complex, an S = (1)/(2) EPR signal exhibiting (59)Co hyperfine splitting (A = 24 G) typical of a low-spin Co(III)-superoxide complex was observed. Superoxides 187-197 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 21866283-6 2011 DFT calculations support a proposal that [Co(II)(mebpena)](+) reacts with O(2) to form a Co(III)-superoxide complex which can abstract an H atom from a ligand methylene C atom as the initial step towards the observed oxidative C-N bond cleavage. Superoxides 97-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-47 17893865-5 2007 For example, 1"-acetoxychavicol acetate, which occurs in the rhizomes of the subtropical Zingiberaceae plant, has been shown to attenuate NOX-derived superoxide generation in macrophages, as well as lipopolysaccharide-induced nitric oxide and prostaglandin E(2) production through the suppression of iNOS and COX-2 synthesis, respectively. Superoxides 150-160 mitochondrially encoded cytochrome c oxidase II Homo sapiens 309-314