PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 12392085-5 2002 In the case of DES, the spectra of DMPO-OH adducts did not increase concentration-dependently in the absence of RAW 264.7 cells, however in their presence, they increased concentration-dependently, especially when these cells were stimulated with LPS and IFN-gamma. dmpo-oh 35-42 toll-like receptor 4 Mus musculus 247-250 12392085-5 2002 In the case of DES, the spectra of DMPO-OH adducts did not increase concentration-dependently in the absence of RAW 264.7 cells, however in their presence, they increased concentration-dependently, especially when these cells were stimulated with LPS and IFN-gamma. dmpo-oh 35-42 interferon gamma Mus musculus 255-264 9337622-15 1997 The complementary inhibition of DMPO-OH production by azide and 9,10-anthracenedipropionic acid (ADPA) was consistent with 1O2 production by BCA followed by reaction of 1O2 with DMPO and decay of the intermediate complex to form DMPO-OH and free OH.. All our results seem to indicate that BCA is a 50%/50% type 1/type 2 sensitizer in buffered aqueous solutions and confirmed that the dye-induced hemolysis of erythrocytes was cell caused by a mixed type 1/type 2 mechanism. dmpo-oh 32-39 B cell linker Homo sapiens 141-144 9657042-5 1998 SOD also inhibited the formation of GA-induced DMPO-OH adducts. dmpo-oh 47-54 superoxide dismutase 1 Homo sapiens 0-3 9337622-14 1997 radical adducts, indicating the presence of free OH.. Production of DMPO-OH was partly inhibited by superoxide dismutase (SOD), catalase and desferrioxamine, suggesting that the iron-catalyzed decomposition of H2O2 was partly involved in the formation of one part of the observed OH.. dmpo-oh 68-75 catalase Homo sapiens 128-136 9337622-15 1997 The complementary inhibition of DMPO-OH production by azide and 9,10-anthracenedipropionic acid (ADPA) was consistent with 1O2 production by BCA followed by reaction of 1O2 with DMPO and decay of the intermediate complex to form DMPO-OH and free OH.. All our results seem to indicate that BCA is a 50%/50% type 1/type 2 sensitizer in buffered aqueous solutions and confirmed that the dye-induced hemolysis of erythrocytes was cell caused by a mixed type 1/type 2 mechanism. dmpo-oh 32-39 B cell linker Homo sapiens 289-292 9337622-15 1997 The complementary inhibition of DMPO-OH production by azide and 9,10-anthracenedipropionic acid (ADPA) was consistent with 1O2 production by BCA followed by reaction of 1O2 with DMPO and decay of the intermediate complex to form DMPO-OH and free OH.. All our results seem to indicate that BCA is a 50%/50% type 1/type 2 sensitizer in buffered aqueous solutions and confirmed that the dye-induced hemolysis of erythrocytes was cell caused by a mixed type 1/type 2 mechanism. dmpo-oh 229-236 B cell linker Homo sapiens 141-144 7639532-2 1995 Although a weak signal corresponding to the DMPO-hydroxyl radical spin adduct (.DMPO-OH) is observed when peroxynitrite is allowed to decompose in the presence of DMPO, it is concluded that this does not constitute proof of the presence of free hydroxyl radicals. dmpo-oh 80-87 spindlin 1 Homo sapiens 66-70 19772319-2 2009 Spin trapping with 5,5"-dimethylpyrroline 1-N-oxide (DMPO) gave a composite spectrum of a carbon-centered radical and the well-known DMPO-OH adduct. dmpo-oh 133-140 spindlin 1 Homo sapiens 0-4 7811256-5 1994 The spin adducts of superoxide and hydroxyl radical (DMPO-OOH and DMPO-OH, respectively) were generated in the reaction of NCS with the NADPH/cyt P-450 reductase system. dmpo-oh 66-73 2,4-dienoyl-CoA reductase 1 Homo sapiens 136-141 8301214-3 1994 The addition of gp120 to MDM increased the production of DMPO-OH and after 1 h, the amount of DMPO-OH produced by 40 micrograms/ml gp120 was about 300% that of untreated MDM. dmpo-oh 57-64 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 16-21 8301214-3 1994 The addition of gp120 to MDM increased the production of DMPO-OH and after 1 h, the amount of DMPO-OH produced by 40 micrograms/ml gp120 was about 300% that of untreated MDM. dmpo-oh 57-64 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 131-136 8301214-3 1994 The addition of gp120 to MDM increased the production of DMPO-OH and after 1 h, the amount of DMPO-OH produced by 40 micrograms/ml gp120 was about 300% that of untreated MDM. dmpo-oh 94-101 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 16-21 8301214-3 1994 The addition of gp120 to MDM increased the production of DMPO-OH and after 1 h, the amount of DMPO-OH produced by 40 micrograms/ml gp120 was about 300% that of untreated MDM. dmpo-oh 94-101 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 131-136 8301214-8 1994 Soluble CD4 did not modify the intensity of the DMPO-OH adduct, whereas yeast mannan and Ca(2+)-chelators abolished the increase in the DMPO-OH signal induced by gp120. dmpo-oh 136-143 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 162-167 8386688-2 1993 When oxy- or metmyoglobin is added to such a system the initial yield and the halife of DMPO-OH are reduced, and at high myoglobin concentrations (about 0.1 mmol dm-3) DMPO-OH becomes undetectable. dmpo-oh 88-95 myoglobin Homo sapiens 16-25 8386688-2 1993 When oxy- or metmyoglobin is added to such a system the initial yield and the halife of DMPO-OH are reduced, and at high myoglobin concentrations (about 0.1 mmol dm-3) DMPO-OH becomes undetectable. dmpo-oh 168-175 myoglobin Homo sapiens 16-25 8386688-4 1993 From the evidence of these and other experiments it was concluded that the DMPO-OH adduct reacts with hydrogen peroxide and myoglobin to give non-paramagnetic products, and hence that the use of the DMPO spin trap to detect hydroxyl or other active radicals in systems containing physiological concentrations of myoglobin may give misleading results. dmpo-oh 75-82 myoglobin Homo sapiens 124-133 8386688-4 1993 From the evidence of these and other experiments it was concluded that the DMPO-OH adduct reacts with hydrogen peroxide and myoglobin to give non-paramagnetic products, and hence that the use of the DMPO spin trap to detect hydroxyl or other active radicals in systems containing physiological concentrations of myoglobin may give misleading results. dmpo-oh 75-82 myoglobin Homo sapiens 312-321 1652585-7 1991 The DMPO-OH signal decreased on addition of superoxide dismutase, catalase, or diethylenetriaminepentaacetic acid, indicating that the hydroxyl radical was generated via the metal-catalyzed Haber-Weiss reaction from the superoxide radical and hydrogen peroxide. dmpo-oh 4-11 catalase Homo sapiens 66-74 2554813-6 1989 Addition of purified human MPO and H2O2 to DMPO yielded EPR spectra consisting of small DMPO-OH peaks. dmpo-oh 88-95 myeloperoxidase Homo sapiens 27-30 2554813-7 1989 The addition of MPO and H2O2 to preformed DMPO-OH and DMPO-CH3 resulted in rapid destruction of these spin adducts. dmpo-oh 42-49 myeloperoxidase Homo sapiens 16-19 2822547-2 1987 A hydroxyl spin adduct (DMPO-OH) was identified in coronary effluent during the initial seconds of reperfusion by Electron Spin Resonance (ESR) Spectroscopy. dmpo-oh 24-31 spindlin 1 Rattus norvegicus 11-15 2822547-2 1987 A hydroxyl spin adduct (DMPO-OH) was identified in coronary effluent during the initial seconds of reperfusion by Electron Spin Resonance (ESR) Spectroscopy. dmpo-oh 24-31 spindlin 1 Rattus norvegicus 123-127 2854101-3 1987 Since myeloperoxidase (MPO), which is also active during the respiratory burst, produces hypochlorous acid (HOCl) (HOCl) in the presence of chloride ions (Cl-) and hydrogen peroxide (H2O2), this species has been investigated as a possible source of the DMPO-OH adduct. dmpo-oh 253-260 myeloperoxidase Homo sapiens 6-21 2854101-3 1987 Since myeloperoxidase (MPO), which is also active during the respiratory burst, produces hypochlorous acid (HOCl) (HOCl) in the presence of chloride ions (Cl-) and hydrogen peroxide (H2O2), this species has been investigated as a possible source of the DMPO-OH adduct. dmpo-oh 253-260 myeloperoxidase Homo sapiens 23-26 2545706-5 1989 However, superoxide destroys the preformed hydroxyl radical spin-trapped adduct, 2,2-dimethyl-5-hydroxy-1-pyrrolidinyloxy (DMPO-OH), and DMPO-CH3. dmpo-oh 123-130 spindlin 1 Homo sapiens 60-64 2844279-7 1988 An increase in the DMPO-OH steady-state concentration was observed if the photolysis of NBQCl was performed in the presence of superoxide dismutase (SOD). dmpo-oh 19-26 superoxide dismutase 1 Homo sapiens 127-147 2844279-7 1988 An increase in the DMPO-OH steady-state concentration was observed if the photolysis of NBQCl was performed in the presence of superoxide dismutase (SOD). dmpo-oh 19-26 superoxide dismutase 1 Homo sapiens 149-152 2844279-8 1988 Our results suggest that this effect is due to the SOD inhibition of the destruction of DMPO-OH.by superoxide ion. dmpo-oh 88-95 superoxide dismutase 1 Homo sapiens 51-54 24257538-6 2014 The presence of catalase inhibited DMPO-OH generation whereas BSA had no influence on DMPO-OH formation. dmpo-oh 36-43 catalase Homo sapiens 16-24