PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 33918289-7 2021 We also used several other cytotoxic nitric oxide donors, e.g., molsidomine and S-nitroso glutathione; however, both P-gp- and BCRP-expressing cells were found to be highly resistant to these NO-donors. S-Nitrosoglutathione 80-101 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 127-131 33990008-2 2021 S-NITROSOGLUTATHIONE REDUCTASE (GSNOR) governs NO bioavailability by the breakdown of S-nitrosoglutathione (GSNO), fine-tunes NO signalling and controls total cellular S-nitrosylated proteins. S-Nitrosoglutathione 86-106 alcohol dehydrogenase class III Solanum lycopersicum 0-30 33990008-2 2021 S-NITROSOGLUTATHIONE REDUCTASE (GSNOR) governs NO bioavailability by the breakdown of S-nitrosoglutathione (GSNO), fine-tunes NO signalling and controls total cellular S-nitrosylated proteins. S-Nitrosoglutathione 86-106 alcohol dehydrogenase class III Solanum lycopersicum 32-37 33990008-2 2021 S-NITROSOGLUTATHIONE REDUCTASE (GSNOR) governs NO bioavailability by the breakdown of S-nitrosoglutathione (GSNO), fine-tunes NO signalling and controls total cellular S-nitrosylated proteins. S-Nitrosoglutathione 32-36 alcohol dehydrogenase class III Solanum lycopersicum 0-30 33780653-3 2021 We have shown the GSNO catabolic enzyme encoded by adh5, GSNO reductase, is epigenetically upregulated in hyperoxia. S-Nitrosoglutathione 18-22 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 51-55 33494625-6 2021 In HEK cells, S-nitrosoglutathione led to a PKG-dependent increase in plasmalemmal density of the insulin-independent glucose transporter, GLUT-1. S-Nitrosoglutathione 14-34 solute carrier family 2 (facilitated glucose transporter), member 1 Mus musculus 139-145 33266126-4 2020 S-nitrosoglutathione reductase (GSNOR) thereby acts as a mediator to pathways regulated by NO due to its activity in the irreversible reduction of GSNO to oxidized glutathione (GSSG) and ammonia. S-Nitrosoglutathione 32-36 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-30 33518717-2 2021 S-nitrosoglutathione is regarded as the most abundant low-molecular-weight S-nitrosothiol in plants, where its intracellular concentrations are modulated by S-nitrosoglutathione reductase. S-Nitrosoglutathione 0-20 alcohol dehydrogenase class III Solanum lycopersicum 157-187 33004257-3 2021 A conserved enzyme in the S-nitrosoglutathione (GSNO) metabolism, GSNO reductase (GSNOR), modulates a multitude of abiotic and biotic stress responses. S-Nitrosoglutathione 26-46 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 66-80 33004257-3 2021 A conserved enzyme in the S-nitrosoglutathione (GSNO) metabolism, GSNO reductase (GSNOR), modulates a multitude of abiotic and biotic stress responses. S-Nitrosoglutathione 26-46 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 82-87 33004257-3 2021 A conserved enzyme in the S-nitrosoglutathione (GSNO) metabolism, GSNO reductase (GSNOR), modulates a multitude of abiotic and biotic stress responses. S-Nitrosoglutathione 48-52 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 66-80 33004257-3 2021 A conserved enzyme in the S-nitrosoglutathione (GSNO) metabolism, GSNO reductase (GSNOR), modulates a multitude of abiotic and biotic stress responses. S-Nitrosoglutathione 48-52 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 82-87 33126056-7 2021 Further confirming a role for PKC nitrosylation, preincubation of aortas with GSNO attenuated the responses to both angiotensin II and to a direct PKC activator, and this effect was attenuated by ascorbate (reverses GSNO-induced nitrosylation). S-Nitrosoglutathione 78-82 proline rich transmembrane protein 2 Homo sapiens 30-33 33126056-7 2021 Further confirming a role for PKC nitrosylation, preincubation of aortas with GSNO attenuated the responses to both angiotensin II and to a direct PKC activator, and this effect was attenuated by ascorbate (reverses GSNO-induced nitrosylation). S-Nitrosoglutathione 78-82 angiotensinogen Rattus norvegicus 116-130 33126056-7 2021 Further confirming a role for PKC nitrosylation, preincubation of aortas with GSNO attenuated the responses to both angiotensin II and to a direct PKC activator, and this effect was attenuated by ascorbate (reverses GSNO-induced nitrosylation). S-Nitrosoglutathione 78-82 proline rich transmembrane protein 2 Homo sapiens 147-150 33126056-8 2021 GSNO-induced nitrosylation also inhibited the increases in Ca2+ mobilization in angiotensin II-stimulated HEK293T cells expressing angiotensin type 1 receptor. S-Nitrosoglutathione 0-4 angiotensinogen Homo sapiens 80-94 32005394-4 2020 The physiological NO donor; S-nitrosoglutathione (GSNO), inhibits ALDH3H1 in a time- and concentration-dependent manner. S-Nitrosoglutathione 28-48 aldehyde dehydrogenase 3H1 Arabidopsis thaliana 66-73 31880198-8 2020 In conclusion, our research reveals a novel molecular mechanism that oxidative modification at Cys292 and Cys361 sites regulates ATG4B function, which modulates autophagy.Abbreviations: Air-ox: air-oxidation; ATG4B: autophagy related 4B cysteine peptidase; BCNU: 1,3-bis(2-chloroethyl)-1-nitrosourea; CBB: Coomassie Brilliant Blue; CM: complete medium; CQ: chloroquine; DTT: dithiothreitol; GSH: reduced glutathione; GSNO: S-nitrosoglutathione; GSSG: oxidized glutathione; HMW: high molecular weight; H2O2: hydrogen peroxide; NAC: N-acetyl-L-cysteine; NEM: N-ethylmaleimide; PE: phosphatidylethanolamine; PTM: post-translational modification; ROS, reactive oxygen species; WT: wild type. S-Nitrosoglutathione 417-421 autophagy related 4B cysteine peptidase Homo sapiens 129-134 31880198-8 2020 In conclusion, our research reveals a novel molecular mechanism that oxidative modification at Cys292 and Cys361 sites regulates ATG4B function, which modulates autophagy.Abbreviations: Air-ox: air-oxidation; ATG4B: autophagy related 4B cysteine peptidase; BCNU: 1,3-bis(2-chloroethyl)-1-nitrosourea; CBB: Coomassie Brilliant Blue; CM: complete medium; CQ: chloroquine; DTT: dithiothreitol; GSH: reduced glutathione; GSNO: S-nitrosoglutathione; GSSG: oxidized glutathione; HMW: high molecular weight; H2O2: hydrogen peroxide; NAC: N-acetyl-L-cysteine; NEM: N-ethylmaleimide; PE: phosphatidylethanolamine; PTM: post-translational modification; ROS, reactive oxygen species; WT: wild type. S-Nitrosoglutathione 417-421 autophagy related 4B cysteine peptidase Homo sapiens 209-214 31880198-8 2020 In conclusion, our research reveals a novel molecular mechanism that oxidative modification at Cys292 and Cys361 sites regulates ATG4B function, which modulates autophagy.Abbreviations: Air-ox: air-oxidation; ATG4B: autophagy related 4B cysteine peptidase; BCNU: 1,3-bis(2-chloroethyl)-1-nitrosourea; CBB: Coomassie Brilliant Blue; CM: complete medium; CQ: chloroquine; DTT: dithiothreitol; GSH: reduced glutathione; GSNO: S-nitrosoglutathione; GSSG: oxidized glutathione; HMW: high molecular weight; H2O2: hydrogen peroxide; NAC: N-acetyl-L-cysteine; NEM: N-ethylmaleimide; PE: phosphatidylethanolamine; PTM: post-translational modification; ROS, reactive oxygen species; WT: wild type. S-Nitrosoglutathione 423-443 autophagy related 4B cysteine peptidase Homo sapiens 129-134 31880198-8 2020 In conclusion, our research reveals a novel molecular mechanism that oxidative modification at Cys292 and Cys361 sites regulates ATG4B function, which modulates autophagy.Abbreviations: Air-ox: air-oxidation; ATG4B: autophagy related 4B cysteine peptidase; BCNU: 1,3-bis(2-chloroethyl)-1-nitrosourea; CBB: Coomassie Brilliant Blue; CM: complete medium; CQ: chloroquine; DTT: dithiothreitol; GSH: reduced glutathione; GSNO: S-nitrosoglutathione; GSSG: oxidized glutathione; HMW: high molecular weight; H2O2: hydrogen peroxide; NAC: N-acetyl-L-cysteine; NEM: N-ethylmaleimide; PE: phosphatidylethanolamine; PTM: post-translational modification; ROS, reactive oxygen species; WT: wild type. S-Nitrosoglutathione 423-443 autophagy related 4B cysteine peptidase Homo sapiens 209-214 32413758-5 2020 Additionally, caspase-3 and -9 activities and caspase-3 activation were greatly decreased by GSNO treatment and increased by l-NAME treatment (P < 0.05). S-Nitrosoglutathione 93-97 caspase 3 Homo sapiens 14-30 32413758-5 2020 Additionally, caspase-3 and -9 activities and caspase-3 activation were greatly decreased by GSNO treatment and increased by l-NAME treatment (P < 0.05). S-Nitrosoglutathione 93-97 caspase 3 Homo sapiens 14-23 32932594-0 2020 The Reactions of H2O2 and GSNO with the Zinc Finger Motif of XPA. S-Nitrosoglutathione 26-30 XPA, DNA damage recognition and repair factor Homo sapiens 61-64 32932594-3 2020 We used the synthetic 37-residue peptide representing the tetrathiolate zinc finger domain of the DNA repair protein XPA, acetyl-DYVICEECGKEFMSYLMNHFDLPTCDNCRDADDKHK-amide (XPAzf) as a working model to study the reaction of its Zn(II) complex (ZnXPAzf) with hydrogen peroxide and S-nitrosoglutathione (GSNO), as oxidative and nitrosative stress agents, respectively. S-Nitrosoglutathione 280-300 XPA, DNA damage recognition and repair factor Homo sapiens 117-120 32932594-3 2020 We used the synthetic 37-residue peptide representing the tetrathiolate zinc finger domain of the DNA repair protein XPA, acetyl-DYVICEECGKEFMSYLMNHFDLPTCDNCRDADDKHK-amide (XPAzf) as a working model to study the reaction of its Zn(II) complex (ZnXPAzf) with hydrogen peroxide and S-nitrosoglutathione (GSNO), as oxidative and nitrosative stress agents, respectively. S-Nitrosoglutathione 302-306 XPA, DNA damage recognition and repair factor Homo sapiens 117-120 32418890-2 2020 The major NO metabolite S-nitrosoglutahione (GSNO) is essential for S-nitrosylation-based signaling events and the inhibition of S-nitrosoglutahione (GSNO)-metabolizing enzyme GSNO reductase (GSNOR) provides protective effects following cardiac ischemia. S-Nitrosoglutathione 45-49 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 176-190 32418890-2 2020 The major NO metabolite S-nitrosoglutahione (GSNO) is essential for S-nitrosylation-based signaling events and the inhibition of S-nitrosoglutahione (GSNO)-metabolizing enzyme GSNO reductase (GSNOR) provides protective effects following cardiac ischemia. S-Nitrosoglutathione 45-49 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 192-197 32418890-2 2020 The major NO metabolite S-nitrosoglutahione (GSNO) is essential for S-nitrosylation-based signaling events and the inhibition of S-nitrosoglutahione (GSNO)-metabolizing enzyme GSNO reductase (GSNOR) provides protective effects following cardiac ischemia. S-Nitrosoglutathione 150-154 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 176-190 32418890-2 2020 The major NO metabolite S-nitrosoglutahione (GSNO) is essential for S-nitrosylation-based signaling events and the inhibition of S-nitrosoglutahione (GSNO)-metabolizing enzyme GSNO reductase (GSNOR) provides protective effects following cardiac ischemia. S-Nitrosoglutathione 150-154 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 192-197 32719710-3 2020 Deficiency of SL synthesis or signaling (max1-1 and max2-1) resulted in elevated NO and S-nitrosothiol (SNO) levels due to decreased S-nitrosoglutathione (GSNO) reductase (GSNOR) protein abundance and activity indicating that there is a signal interaction between SLs and GSNOR-regulated levels of NO/SNO. S-Nitrosoglutathione 133-153 cytochrome P450, family 711, subfamily A, polypeptide 1 Arabidopsis thaliana 41-45 32719710-3 2020 Deficiency of SL synthesis or signaling (max1-1 and max2-1) resulted in elevated NO and S-nitrosothiol (SNO) levels due to decreased S-nitrosoglutathione (GSNO) reductase (GSNOR) protein abundance and activity indicating that there is a signal interaction between SLs and GSNOR-regulated levels of NO/SNO. S-Nitrosoglutathione 133-153 RNI-like superfamily protein Arabidopsis thaliana 52-56 32719710-3 2020 Deficiency of SL synthesis or signaling (max1-1 and max2-1) resulted in elevated NO and S-nitrosothiol (SNO) levels due to decreased S-nitrosoglutathione (GSNO) reductase (GSNOR) protein abundance and activity indicating that there is a signal interaction between SLs and GSNOR-regulated levels of NO/SNO. S-Nitrosoglutathione 155-159 cytochrome P450, family 711, subfamily A, polypeptide 1 Arabidopsis thaliana 41-45 32719710-3 2020 Deficiency of SL synthesis or signaling (max1-1 and max2-1) resulted in elevated NO and S-nitrosothiol (SNO) levels due to decreased S-nitrosoglutathione (GSNO) reductase (GSNOR) protein abundance and activity indicating that there is a signal interaction between SLs and GSNOR-regulated levels of NO/SNO. S-Nitrosoglutathione 155-159 RNI-like superfamily protein Arabidopsis thaliana 52-56 32576932-7 2020 In HEK293T cells, enhanced free basal cytosolic Ca2+ and SOCE mediated by STIM2 overexpression could be attenuated by GSNO or mutation of the modifiable Cys located in the luminal domain. S-Nitrosoglutathione 118-122 stromal interaction molecule 2 Homo sapiens 74-79 32218363-0 2020 The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione. S-Nitrosoglutathione 58-76 peroxiredoxin 1 Homo sapiens 25-40 32218363-4 2020 Here, we investigated the kinetics of Prx1 S-nitrosation by nitrosoglutathione (GSNO), a recognized biological nitrosating agent, and by the dinitrosyl-iron complex of glutathione (DNIC-GS; [Fe(NO)2(GS)2]-), a hypothetical nitrosating agent. S-Nitrosoglutathione 60-78 peroxiredoxin 1 Homo sapiens 38-42 32218363-4 2020 Here, we investigated the kinetics of Prx1 S-nitrosation by nitrosoglutathione (GSNO), a recognized biological nitrosating agent, and by the dinitrosyl-iron complex of glutathione (DNIC-GS; [Fe(NO)2(GS)2]-), a hypothetical nitrosating agent. S-Nitrosoglutathione 80-84 peroxiredoxin 1 Homo sapiens 38-42 32218363-5 2020 Kinetics studies following the intrinsic fluorescence of Prx1 and its mutants (C83SC173S and C52S) were complemented by product analysis; all experiments were performed at pH 7.4 and 25 C. The results show GSNO-mediated nitrosation of Prx1 peroxidatic residue ( k + N O C y s 52 = 15.4 +- 0.4 M-1. S-Nitrosoglutathione 206-210 peroxiredoxin 1 Homo sapiens 57-61 33225882-9 2020 GFAP was significantly increased in GSNO-induced cells, but the knockdown of KCNA2-AS reversed this result. S-Nitrosoglutathione 36-40 glial fibrillary acidic protein Rattus norvegicus 0-4 33225882-9 2020 GFAP was significantly increased in GSNO-induced cells, but the knockdown of KCNA2-AS reversed this result. S-Nitrosoglutathione 36-40 potassium voltage-gated channel subfamily A member 2 Rattus norvegicus 77-82 33225882-10 2020 Meanwhile, pSTAT3 was significantly increased in GSNO-induced cells, but knockdown of KCNA2-AS reduced pSTAT3 within the nucleus while the total pSTAT3 did not change significantly. S-Nitrosoglutathione 49-53 potassium voltage-gated channel subfamily A member 2 Rattus norvegicus 86-91 33225882-11 2020 pSTAT3 bound to KCNA2-AS and this binding increased with GSNO treatment. S-Nitrosoglutathione 57-61 potassium voltage-gated channel subfamily A member 2 Rattus norvegicus 16-21 32953945-12 2020 We used Western blotting and flow cytometry to demonstrate that incubation of a murine macrophage cell line (Raw 264.7 cells) with GSNO reduced the surface Dectin-1 expression as a result of shedding to the media. S-Nitrosoglutathione 131-135 C-type lectin domain family 7, member a Mus musculus 156-164 32953945-14 2020 GSNO also induces Dectin-1 shedding from the cell surface. S-Nitrosoglutathione 0-4 C-type lectin domain family 7, member a Mus musculus 18-26 32953945-15 2020 The functional significance of GSNO treatment of macrophages is shown by reduced beta-glucan-mediated signaling in terms of NF-kappaB function and IL-6 expression. S-Nitrosoglutathione 31-35 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 124-133 32953945-15 2020 The functional significance of GSNO treatment of macrophages is shown by reduced beta-glucan-mediated signaling in terms of NF-kappaB function and IL-6 expression. S-Nitrosoglutathione 31-35 interleukin 6 Mus musculus 147-151 32576932-0 2020 Synergistic stabilization by nitrosoglutathione-induced thiol modifications in the stromal interaction molecule-2 luminal domain suppresses basal and store operated calcium entry. S-Nitrosoglutathione 29-47 stromal interaction molecule 2 Homo sapiens 83-113 32576932-4 2020 Here, we demonstrate that the nitric oxide (NO) donor nitrosoglutathione (GSNO) thermodynamically stabilizes the STIM2 Ca2+ sensing region in a Cys-specific manner. S-Nitrosoglutathione 54-72 stromal interaction molecule 2 Homo sapiens 113-118 32576932-4 2020 Here, we demonstrate that the nitric oxide (NO) donor nitrosoglutathione (GSNO) thermodynamically stabilizes the STIM2 Ca2+ sensing region in a Cys-specific manner. S-Nitrosoglutathione 74-78 stromal interaction molecule 2 Homo sapiens 113-118 32528086-0 2020 Author Correction: S-nitrosoglutathione inhibits adipogenesis in 3T3-L1 preadipocytes by S-nitrosation of CCAAT/enhancer-binding protein beta. S-Nitrosoglutathione 19-39 CCAAT enhancer binding protein beta Homo sapiens 106-141 32450498-9 2020 We further constructed a CD47 surface immobilized silicone tubing filled with NO releasing S-nitrosoglutathione/ascorbic acid (GSNO/AA) solution for synergistic biocompatibility evaluation. S-Nitrosoglutathione 91-111 CD47 molecule Homo sapiens 25-29 32450498-9 2020 We further constructed a CD47 surface immobilized silicone tubing filled with NO releasing S-nitrosoglutathione/ascorbic acid (GSNO/AA) solution for synergistic biocompatibility evaluation. S-Nitrosoglutathione 127-131 CD47 molecule Homo sapiens 25-29 32005394-4 2020 The physiological NO donor; S-nitrosoglutathione (GSNO), inhibits ALDH3H1 in a time- and concentration-dependent manner. S-Nitrosoglutathione 50-54 aldehyde dehydrogenase 3H1 Arabidopsis thaliana 66-73 32005394-5 2020 Mutagenesis and ESI-MS/MS analyses show that all Cys residues of ALDH3H1 are targets of GSNO-mediated S-nitrosation. S-Nitrosoglutathione 88-92 aldehyde dehydrogenase 3H1 Arabidopsis thaliana 65-72 32005394-7 2020 GSNO has the same effect on the chloroplastic ALDH3I1, suggesting that susceptibility of the catalytic Cys to NO is a common feature of ALDHs. S-Nitrosoglutathione 0-4 aldehyde dehydrogenase 3I1 Arabidopsis thaliana 46-53 31680031-0 2019 S-Nitrosoglutathione Mimics the Beneficial Activity of Endothelial Nitric Oxide Synthase-Derived Nitric Oxide in a Mouse Model of Stroke. S-Nitrosoglutathione 0-20 nitric oxide synthase 3, endothelial cell Mus musculus 55-88 31622832-5 2020 In addition, mu-calpain autolysis, myofibrillar protein and desmin degradation were reduced by GSNO treatment and accelerated by L-NAME treatment (p < 0.05). S-Nitrosoglutathione 95-99 calpain 1 Bos taurus 13-23 31622832-5 2020 In addition, mu-calpain autolysis, myofibrillar protein and desmin degradation were reduced by GSNO treatment and accelerated by L-NAME treatment (p < 0.05). S-Nitrosoglutathione 95-99 desmin Bos taurus 60-66 31595469-3 2020 GSNOR, which has been identified as a key component of S-nitrosothiols catabolism, catalyzes an irreversible decomposition of abundant intracellular S-nitrosothiol, S-nitrosoglutathione (GSNO) to oxidized glutathione using reduced NADH cofactor. S-Nitrosoglutathione 165-185 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-5 31596601-5 2019 Confocal microscopy and IP studies showed the cellular colocalization of CFTR and CHIP, and showed that S-nitrosoglutathione inhibits the CHIP-CFTR interaction. S-Nitrosoglutathione 104-124 CF transmembrane conductance regulator Homo sapiens 73-77 31596601-5 2019 Confocal microscopy and IP studies showed the cellular colocalization of CFTR and CHIP, and showed that S-nitrosoglutathione inhibits the CHIP-CFTR interaction. S-Nitrosoglutathione 104-124 CF transmembrane conductance regulator Homo sapiens 143-147 31596601-8 2019 S-nitrosoglutathione-treated cells also had more S-nitrosylated CHIP and less ubiquitinated CFTR than cells that were not treated, suggesting that the S-nitrosylation of CHIP prevents the ubiquitination of CFTR by inhibiting CHIP"s E3 ubiquitin ligase function. S-Nitrosoglutathione 0-20 CF transmembrane conductance regulator Homo sapiens 92-96 31596601-8 2019 S-nitrosoglutathione-treated cells also had more S-nitrosylated CHIP and less ubiquitinated CFTR than cells that were not treated, suggesting that the S-nitrosylation of CHIP prevents the ubiquitination of CFTR by inhibiting CHIP"s E3 ubiquitin ligase function. S-Nitrosoglutathione 0-20 CF transmembrane conductance regulator Homo sapiens 206-210 31680031-2 2019 However, the activity of the eNOS enzyme and the metabolism of major NO metabolite S-nitrosoglutathione (GSNO) are dysregulated after stroke, causing endothelial dysfunction. S-Nitrosoglutathione 83-103 nitric oxide synthase 3, endothelial cell Mus musculus 29-33 31473210-9 2019 GSNO and 3D cultures reduced MMPs -2, -9, and increased TIMP-1 release in AAA-SMC cultures (p < 0.05 for GSNO vs. non-GSNO cultures). S-Nitrosoglutathione 0-4 TIMP metallopeptidase inhibitor 1 Homo sapiens 56-62 31680031-2 2019 However, the activity of the eNOS enzyme and the metabolism of major NO metabolite S-nitrosoglutathione (GSNO) are dysregulated after stroke, causing endothelial dysfunction. S-Nitrosoglutathione 105-109 nitric oxide synthase 3, endothelial cell Mus musculus 29-33 31680031-8 2019 Pre- or postinjury treatment with either GSNO or N6022 significantly reduced infarct volume, improved neurological and sensorimotor function in both WT and eNOS-null mice. S-Nitrosoglutathione 41-45 nitric oxide synthase 3, endothelial cell Mus musculus 156-160 31680031-9 2019 CONCLUSION: Reduced brain infarctions and edema, and improved neurobehavioral functions by pre- or postinjury GSNO treatment of eNOS knock out mice indicate that GSNO can attenuate IR injury, likely by mimicking the eNOS-derived NO-dependent anti-ischemic and anti-inflammatory functions. S-Nitrosoglutathione 110-114 nitric oxide synthase 3, endothelial cell Mus musculus 128-132 31680031-9 2019 CONCLUSION: Reduced brain infarctions and edema, and improved neurobehavioral functions by pre- or postinjury GSNO treatment of eNOS knock out mice indicate that GSNO can attenuate IR injury, likely by mimicking the eNOS-derived NO-dependent anti-ischemic and anti-inflammatory functions. S-Nitrosoglutathione 162-166 nitric oxide synthase 3, endothelial cell Mus musculus 128-132 31680031-9 2019 CONCLUSION: Reduced brain infarctions and edema, and improved neurobehavioral functions by pre- or postinjury GSNO treatment of eNOS knock out mice indicate that GSNO can attenuate IR injury, likely by mimicking the eNOS-derived NO-dependent anti-ischemic and anti-inflammatory functions. S-Nitrosoglutathione 162-166 nitric oxide synthase 3, endothelial cell Mus musculus 216-220 31486289-2 2019 The endogenous nonadrenergic, noncholinergic signaling molecule, S-nitrosoglutathione (GSNO) and its catabolism by GSNO reductase (GSNOR) modulate airway reactivity. S-Nitrosoglutathione 65-85 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 115-129 31486289-2 2019 The endogenous nonadrenergic, noncholinergic signaling molecule, S-nitrosoglutathione (GSNO) and its catabolism by GSNO reductase (GSNOR) modulate airway reactivity. S-Nitrosoglutathione 65-85 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 131-136 31486289-2 2019 The endogenous nonadrenergic, noncholinergic signaling molecule, S-nitrosoglutathione (GSNO) and its catabolism by GSNO reductase (GSNOR) modulate airway reactivity. S-Nitrosoglutathione 87-91 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 115-129 31486289-2 2019 The endogenous nonadrenergic, noncholinergic signaling molecule, S-nitrosoglutathione (GSNO) and its catabolism by GSNO reductase (GSNOR) modulate airway reactivity. S-Nitrosoglutathione 87-91 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 131-136 31486289-10 2019 Pharmacologic or genetic ablation of GSNOR abolished the exaggerated BPD tracheal relaxation to GSNO and also augmented BPD IPB relaxation to GSNO. S-Nitrosoglutathione 96-100 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 37-42 31486289-13 2019 CONCLUSION: GSNO dramatically relaxed the trachealis in our BPD model, an effect paradoxically reversed by loss of GSNOR. S-Nitrosoglutathione 12-16 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 115-120 31649033-6 2019 Kinetic analyses suggested an AKR1A1 substrate preference of SNO-CoA > GSNO. S-Nitrosoglutathione 71-75 aldo-keto reductase family 1 member A1 Homo sapiens 30-36 31649033-8 2019 Conversely, GSNOR-deficient mice had increased AKR1A1 activity, revealing potential cross-talk among GSNO-dependent denitrosylases. S-Nitrosoglutathione 12-16 aldo-keto reductase family 1, member A1 (aldehyde reductase) Mus musculus 47-53 31649033-9 2019 Molecular modeling and mutagenesis of AKR1A1 identified Arg-312 as a key residue mediating the specific interaction with GSNO; in contrast, substitution of the SNO-CoA-binding residue Lys-127 minimally affected the GSNO-reducing activity of AKR1A1. S-Nitrosoglutathione 121-125 aldo-keto reductase family 1, member A1 (aldehyde reductase) Mus musculus 38-44 31649033-9 2019 Molecular modeling and mutagenesis of AKR1A1 identified Arg-312 as a key residue mediating the specific interaction with GSNO; in contrast, substitution of the SNO-CoA-binding residue Lys-127 minimally affected the GSNO-reducing activity of AKR1A1. S-Nitrosoglutathione 215-219 aldo-keto reductase family 1, member A1 (aldehyde reductase) Mus musculus 38-44 31649033-10 2019 Together, these findings indicate that AKR1A1 is a multi-LMW-SNO reductase that can distinguish between and metabolize the two major LMW-SNO signaling molecules GSNO and SNO-CoA, allowing for wide-ranging control of protein S-nitrosylation under both physiological and pathological conditions. S-Nitrosoglutathione 161-165 aldo-keto reductase family 1, member A1 (aldehyde reductase) Mus musculus 39-45 31766125-0 2019 Evidence for an Allosteric S-Nitrosoglutathione Binding Site in S-Nitrosoglutathione Reductase (GSNOR). S-Nitrosoglutathione 27-47 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 64-94 31766125-0 2019 Evidence for an Allosteric S-Nitrosoglutathione Binding Site in S-Nitrosoglutathione Reductase (GSNOR). S-Nitrosoglutathione 27-47 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 96-101 31766125-3 2019 This study demonstrates the kinetic activation of GSNOR by its substrate S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 73-93 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 50-55 31659183-0 2019 S-nitrosoglutathione inhibits adipogenesis in 3T3-L1 preadipocytes by S-nitrosation of CCAAT/enhancer-binding protein beta. S-Nitrosoglutathione 0-20 CCAAT/enhancer binding protein (C/EBP), beta Mus musculus 87-122 31659183-4 2019 Biochemical analysis after 7 days of differentiation showed a prominent anti-adipogenic effect of GSNO which was evident as reduced cellular triglycerides and total protein content as well as decreased mRNA and protein expression of late transcription factors (e.g. peroxisome proliferator activated receptor gamma) and markers of terminal differentiation (e.g. leptin). S-Nitrosoglutathione 98-102 peroxisome proliferator activated receptor gamma Mus musculus 266-314 31659183-4 2019 Biochemical analysis after 7 days of differentiation showed a prominent anti-adipogenic effect of GSNO which was evident as reduced cellular triglycerides and total protein content as well as decreased mRNA and protein expression of late transcription factors (e.g. peroxisome proliferator activated receptor gamma) and markers of terminal differentiation (e.g. leptin). S-Nitrosoglutathione 98-102 leptin Mus musculus 362-368 31374192-8 2019 GSNO supplementation to OVX mice was able to reinstate HAT(CBP/p300) and HDAC balance through S-nitrosylation. S-Nitrosoglutathione 0-4 CREB binding protein Mus musculus 59-63 31374192-8 2019 GSNO supplementation to OVX mice was able to reinstate HAT(CBP/p300) and HDAC balance through S-nitrosylation. S-Nitrosoglutathione 0-4 E1A binding protein p300 Mus musculus 63-67 31374192-9 2019 GSNO restored histone acetylation at BDNF promoters (pII, pIV) thereby ameliorating BDNF levels and improving brain morphology and cognition. S-Nitrosoglutathione 0-4 brain derived neurotrophic factor Mus musculus 37-41 31374192-9 2019 GSNO restored histone acetylation at BDNF promoters (pII, pIV) thereby ameliorating BDNF levels and improving brain morphology and cognition. S-Nitrosoglutathione 0-4 brain derived neurotrophic factor Mus musculus 84-88 31562350-6 2019 Cebpd-/- mice show decreased GSH/GSSG ratio, increased S-nitrosoglutathione and 3-nitrotyrosine in the intestine indicative of basal oxidative and nitrosative stress, which was exacerbated by IR. S-Nitrosoglutathione 55-75 CCAAT/enhancer binding protein (C/EBP), delta Mus musculus 0-5 31089684-3 2019 The enzyme S-nitrosoglutathione reductase (GSNOR) indirectly controls the total levels of cellular S-nitrosylation, by depleting S-nitrosoglutathione (GSNO), the major cellular NO donor. S-Nitrosoglutathione 11-31 alcohol dehydrogenase class III Solanum lycopersicum 43-48 31089684-3 2019 The enzyme S-nitrosoglutathione reductase (GSNOR) indirectly controls the total levels of cellular S-nitrosylation, by depleting S-nitrosoglutathione (GSNO), the major cellular NO donor. S-Nitrosoglutathione 43-47 alcohol dehydrogenase class III Solanum lycopersicum 11-41 31434939-7 2019 VSMC stimulation with GSNO, a nitric oxide analogue or with 8-br-cGMP, but not with 8-br-cAMP, up-regulated PDE5 and NOTCH-3 protein levels, indicating a negative feedback loop to protect the arterial wall from excessive relaxation. S-Nitrosoglutathione 22-26 phosphodiesterase 5A Homo sapiens 108-112 31438648-4 2019 Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). S-Nitrosoglutathione 38-58 NADPH oxidase Solanum lycopersicum 150-163 31438648-4 2019 Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). S-Nitrosoglutathione 38-58 NADPH oxidase Solanum lycopersicum 165-172 31438648-4 2019 Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). S-Nitrosoglutathione 38-58 peroxidase Solanum lycopersicum 188-198 31438648-4 2019 Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). S-Nitrosoglutathione 60-64 NADPH oxidase Solanum lycopersicum 150-163 31539160-8 2019 The administration of 7-NI, GSNO, and MK-801 increased the S-nitrosylation and phosphorylation of nNOS, leading to the attenuation of increased S-nitrosylation and decreased autophosphorylation of CaMKII after cerebral ischemia-reperfusion (p<0.05). S-Nitrosoglutathione 28-32 nitric oxide synthase 1 Rattus norvegicus 98-102 31539160-9 2019 Administration of MK-801, GSNO, and 7-NI significantly decreased the neuronal damage in rat hippocampal CA1 caused by cerebral ischemia-reperfusion (p<0.05). S-Nitrosoglutathione 26-30 carbonic anhydrase 1 Rattus norvegicus 104-107 31434939-7 2019 VSMC stimulation with GSNO, a nitric oxide analogue or with 8-br-cGMP, but not with 8-br-cAMP, up-regulated PDE5 and NOTCH-3 protein levels, indicating a negative feedback loop to protect the arterial wall from excessive relaxation. S-Nitrosoglutathione 22-26 notch receptor 3 Homo sapiens 117-124 31438648-4 2019 Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). S-Nitrosoglutathione 60-64 NADPH oxidase Solanum lycopersicum 165-172 31438648-4 2019 Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). S-Nitrosoglutathione 60-64 peroxidase Solanum lycopersicum 188-198 31115903-0 2019 S-nitrosoglutathione protects lipopolysaccharide-induced acute kidney injury by inhibiting toll-like receptor 4-nuclear factor-kappaB signal pathway. S-Nitrosoglutathione 0-20 toll-like receptor 4 Mus musculus 91-111 31438648-4 2019 Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). S-Nitrosoglutathione 60-64 cytosolic ascorbate peroxidase 2 Solanum lycopersicum 200-203 31440429-4 2019 The growth of atwakl10 on media supplemented with oxidative or nitrosative stress resulted in differential results with improved growth following treatment with CysNO but reduced growth in response to S-nitrosoglutatione (GSNO) and methyl-viologen. S-Nitrosoglutathione 222-226 WALL ASSOCIATED KINASE (WAK)-LIKE 10 Arabidopsis thaliana 14-22 31115903-6 2019 CONCLUSIONS: S-nitrosoglutathione attenuates the severity of LPS-induced AKI by inhibiting the TLR4-NF-kappaB signalling pathway and may act as a protective agent for septic AKI. S-Nitrosoglutathione 13-33 toll-like receptor 4 Mus musculus 95-99 31115903-6 2019 CONCLUSIONS: S-nitrosoglutathione attenuates the severity of LPS-induced AKI by inhibiting the TLR4-NF-kappaB signalling pathway and may act as a protective agent for septic AKI. S-Nitrosoglutathione 13-33 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 100-109 30409642-5 2019 More desmin and titin (T2, the degraded fragment of original titin) were degraded by calpain-1 when myofibrils were incubated with 1000 microM GSNO. S-Nitrosoglutathione 143-147 titin Homo sapiens 16-21 30890744-7 2019 GSNO increased glutathionylation of Na,K-ATPase alpha-2 subunit, the principal ion-transporter of cardiac myocyte sarcolemma, which prevents irreversible oxidation of Na,K-ATPase and regulates its function to support normal Ca2+ ion handling in hypoxic cardiomyocytes. S-Nitrosoglutathione 0-4 ATPase Na+/K+ transporting subunit alpha 2 Rattus norvegicus 36-63 30822355-9 2019 KEY RESULTS: GSNO or SNP completely abolished the AngII-dependent AT1 receptor-mediated vasoconstriction of cerebral arteries. S-Nitrosoglutathione 13-17 angiotensinogen Rattus norvegicus 50-55 30822355-13 2019 CONCLUSIONS AND IMPLICATIONS: In rat middle cerebral arteries, GSNO pretreatment specifically affects the AT1 receptor and reduces both AngII-dependent and AngII-independent activation, most likely through AT1 receptor S-nitrosation. S-Nitrosoglutathione 63-67 angiotensinogen Rattus norvegicus 136-141 30822355-13 2019 CONCLUSIONS AND IMPLICATIONS: In rat middle cerebral arteries, GSNO pretreatment specifically affects the AT1 receptor and reduces both AngII-dependent and AngII-independent activation, most likely through AT1 receptor S-nitrosation. S-Nitrosoglutathione 63-67 angiotensinogen Rattus norvegicus 156-161 30988280-0 2019 S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway. S-Nitrosoglutathione 50-68 peroxiredoxin 2 Homo sapiens 23-38 30988280-0 2019 S-nitrosylation of the Peroxiredoxin-2 promotes S-nitrosoglutathione-mediated lung cancer cells apoptosis via AMPK-SIRT1 pathway. S-Nitrosoglutathione 50-68 sirtuin 1 Homo sapiens 115-120 30988280-4 2019 Our studies showed that, as an endogenous NO carrier, S-nitrosoglutathione (GSNO) induced apoptosis in lung cancer cells via nitrosylating Prdx2. S-Nitrosoglutathione 54-74 peroxiredoxin 2 Homo sapiens 139-144 30988280-4 2019 Our studies showed that, as an endogenous NO carrier, S-nitrosoglutathione (GSNO) induced apoptosis in lung cancer cells via nitrosylating Prdx2. S-Nitrosoglutathione 76-80 peroxiredoxin 2 Homo sapiens 139-144 30409642-5 2019 More desmin and titin (T2, the degraded fragment of original titin) were degraded by calpain-1 when myofibrils were incubated with 1000 microM GSNO. S-Nitrosoglutathione 143-147 titin Homo sapiens 61-66 30409642-5 2019 More desmin and titin (T2, the degraded fragment of original titin) were degraded by calpain-1 when myofibrils were incubated with 1000 microM GSNO. S-Nitrosoglutathione 143-147 calpain 1 Homo sapiens 85-94 30409642-6 2019 Incubation with 250 and 1000 microM GSNO suppressed calpain-1-catalyzed cleavage of troponin-T. S-Nitrosoglutathione 36-40 calpain 1 Homo sapiens 52-61 30795534-4 2019 This review summarizes current knowledge on S-nitrosoglutathione reductase (GSNOR), a key enzyme which regulates intracellular levels of S-nitrosoglutathione (GSNO) and indirectly also of protein S-nitrosothiols. S-Nitrosoglutathione 76-80 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 44-74 31245758-2 2019 Arabidopsis GSNO reductase1 (AtGSNOR1) catalyzes metabolism of S-nitrosoglutathione (GSNO) which is a major biologically active NO species. S-Nitrosoglutathione 63-83 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 29-37 31245758-2 2019 Arabidopsis GSNO reductase1 (AtGSNOR1) catalyzes metabolism of S-nitrosoglutathione (GSNO) which is a major biologically active NO species. S-Nitrosoglutathione 12-16 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 29-37 31245758-3 2019 The GSNOR1 loss-of-function mutant gsnor1-3 overaccumulates GSNO with inherent high S-nitrosylation level and resistance to the oxidative stress inducer paraquat (1,1"-dimethyl-4,4"-bipyridinium dichloride). S-Nitrosoglutathione 4-8 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 35-41 30590116-6 2019 However, exogenous GSNO treatment attenuated the thrombin-induced cell signaling pathways for endothelial barrier disruption, thus suggesting the role of a shift of NO metabolism (GSNO vs. ONOO-) toward ONOO- synthesis in cell signaling for endothelial barrier disruption. S-Nitrosoglutathione 19-23 coagulation factor II, thrombin Homo sapiens 49-57 30660098-7 2019 Functionally, KLF4 dependent vasodilatory response was impaired after S-nitrosoglutathione (GSNO) treatment. S-Nitrosoglutathione 70-90 Kruppel like factor 4 Rattus norvegicus 14-18 30660098-7 2019 Functionally, KLF4 dependent vasodilatory response was impaired after S-nitrosoglutathione (GSNO) treatment. S-Nitrosoglutathione 92-96 Kruppel like factor 4 Rattus norvegicus 14-18 30590116-6 2019 However, exogenous GSNO treatment attenuated the thrombin-induced cell signaling pathways for endothelial barrier disruption, thus suggesting the role of a shift of NO metabolism (GSNO vs. ONOO-) toward ONOO- synthesis in cell signaling for endothelial barrier disruption. S-Nitrosoglutathione 180-184 coagulation factor II, thrombin Homo sapiens 49-57 30514762-5 2019 PTS can be oxidized and consequently inactivated by H2O2 treatment, oxidized GSH, or S-nitrosoglutathione, and determining the oxidized modifications of PTS induced by each oxidant by MALDI-TOF MS, we show that PTS is S-glutathionylated in the presence of GSH and H2O2 S-Glutathionylation at Cys-43 protected PTS from H2O2-induced irreversible sulfinylation and sulfonylation. S-Nitrosoglutathione 85-105 6-pyruvoyltetrahydropterin synthase Homo sapiens 0-3 29960806-0 2018 Regulation of IL-10 and IL-17 mediated experimental autoimmune encephalomyelitis by S-nitrosoglutathione. S-Nitrosoglutathione 84-104 interleukin 10 Mus musculus 14-19 30625997-7 2019 However, it does affect the sensitivity of the enzyme to GSNO, indicating that S-glutathionylation of Cys363 is involved in the inhibition of cICDH activity upon GSNO treatments. S-Nitrosoglutathione 57-61 cytosolic NADP+-dependent isocitrate dehydrogenase Arabidopsis thaliana 142-147 30625997-7 2019 However, it does affect the sensitivity of the enzyme to GSNO, indicating that S-glutathionylation of Cys363 is involved in the inhibition of cICDH activity upon GSNO treatments. S-Nitrosoglutathione 162-166 cytosolic NADP+-dependent isocitrate dehydrogenase Arabidopsis thaliana 142-147 30625997-8 2019 We also show that glutaredoxin are able to rescue the GSNO-dependent inhibition of cICDH activity, suggesting that they act as a deglutathionylation system in vitro. S-Nitrosoglutathione 54-58 CAX interacting protein 1 Arabidopsis thaliana 18-30 30625997-8 2019 We also show that glutaredoxin are able to rescue the GSNO-dependent inhibition of cICDH activity, suggesting that they act as a deglutathionylation system in vitro. S-Nitrosoglutathione 54-58 cytosolic NADP+-dependent isocitrate dehydrogenase Arabidopsis thaliana 83-88 31148063-6 2019 These studies revealed that the two isoforms of hBCAT, namely hBCATc and hBCATm, were differently regulated by S-nitrosation or S-glutathionylation pointing to distinct functional/mechanistic responses to GSNO modification. S-Nitrosoglutathione 205-209 branched chain amino acid transaminase 1 Homo sapiens 62-68 31148063-6 2019 These studies revealed that the two isoforms of hBCAT, namely hBCATc and hBCATm, were differently regulated by S-nitrosation or S-glutathionylation pointing to distinct functional/mechanistic responses to GSNO modification. S-Nitrosoglutathione 205-209 branched chain amino acid transaminase 2 Homo sapiens 73-79 30322928-5 2018 GSNO inhibited both the abundance of antiinflammatory (M2) macrophages and expression of pERK, indicating that tumor-associated macrophages activity is influenced by NO. S-Nitrosoglutathione 0-4 eukaryotic translation initiation factor 2 alpha kinase 3 Homo sapiens 89-93 30322928-6 2018 Additionally, GSNO decreased IL-34, indicating suppression of tumor-associated macrophage differentiation. S-Nitrosoglutathione 14-18 interleukin 34 Homo sapiens 29-34 30322928-7 2018 Cytokine profiling of CRPC tumor grafts exposed to GSNO revealed a significant decrease in expression of G-CSF and M-CSF compared with grafts not exposed to GSNO. S-Nitrosoglutathione 51-55 colony stimulating factor 3 Homo sapiens 105-110 30322928-7 2018 Cytokine profiling of CRPC tumor grafts exposed to GSNO revealed a significant decrease in expression of G-CSF and M-CSF compared with grafts not exposed to GSNO. S-Nitrosoglutathione 51-55 colony stimulating factor 1 Homo sapiens 115-120 30625997-3 2019 Here, we show that cICDH is susceptible to oxidation and that several cysteine (Cys) residues are prone to S-nitrosylation upon nitrosoglutathione (GSNO) treatment. S-Nitrosoglutathione 148-152 cytosolic NADP+-dependent isocitrate dehydrogenase Arabidopsis thaliana 19-24 30464072-0 2018 Pathophysiological Role of S-Nitrosylation and Transnitrosylation Depending on S-Nitrosoglutathione Levels Regulated by S-Nitrosoglutathione Reductase. S-Nitrosoglutathione 79-99 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 120-150 30464072-4 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. S-Nitrosoglutathione 27-47 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 102-116 30464072-4 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. S-Nitrosoglutathione 27-47 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 118-123 30464072-4 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. S-Nitrosoglutathione 49-53 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 102-116 30464072-4 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. S-Nitrosoglutathione 49-53 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 118-123 30464072-6 2018 This review introduces recent evidence of GSNO-mediated NO/SNO signaling depending on GSNOR expression or activity. S-Nitrosoglutathione 42-46 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 86-91 29960806-0 2018 Regulation of IL-10 and IL-17 mediated experimental autoimmune encephalomyelitis by S-nitrosoglutathione. S-Nitrosoglutathione 84-104 interleukin 17A Mus musculus 24-29 29960806-2 2018 In active EAE model, GSNO treatment attenuated EAE severity and splenic CD4+ T cells isolated from these mice exhibited decreased IL-17 expression without affecting the IFN-gamma expression compared to the cells from untreated EAE mice. S-Nitrosoglutathione 21-25 interleukin 17A Mus musculus 130-135 29960806-4 2018 CD4+ T cells isolated from GSNO treated EAE mice, as compared to untreated EAE mice, still expressed lower levels of IL-17 under TH17 skewing conditions, but expressed similar levels of IFN-gamma under TH1 skewing condition. S-Nitrosoglutathione 27-31 interleukin 17A Mus musculus 117-122 29960806-4 2018 CD4+ T cells isolated from GSNO treated EAE mice, as compared to untreated EAE mice, still expressed lower levels of IL-17 under TH17 skewing conditions, but expressed similar levels of IFN-gamma under TH1 skewing condition. S-Nitrosoglutathione 27-31 interferon gamma Mus musculus 186-195 29960806-4 2018 CD4+ T cells isolated from GSNO treated EAE mice, as compared to untreated EAE mice, still expressed lower levels of IL-17 under TH17 skewing conditions, but expressed similar levels of IFN-gamma under TH1 skewing condition. S-Nitrosoglutathione 27-31 negative elongation factor complex member C/D, Th1l Mus musculus 129-132 29960806-5 2018 Interestingly, under both TH17 and TH1 skewing condition, CD4+ T cells isolated from GSNO treated EAE mice, as compared to untreated EAE mice, expressed higher levels of IL-10 and adoptive transfer of these TH17 and TH1 skewed cells seemingly exhibited milder EAE disease. S-Nitrosoglutathione 85-89 negative elongation factor complex member C/D, Th1l Mus musculus 26-29 29960806-5 2018 Interestingly, under both TH17 and TH1 skewing condition, CD4+ T cells isolated from GSNO treated EAE mice, as compared to untreated EAE mice, expressed higher levels of IL-10 and adoptive transfer of these TH17 and TH1 skewed cells seemingly exhibited milder EAE disease. S-Nitrosoglutathione 85-89 interleukin 10 Mus musculus 170-175 29960806-5 2018 Interestingly, under both TH17 and TH1 skewing condition, CD4+ T cells isolated from GSNO treated EAE mice, as compared to untreated EAE mice, expressed higher levels of IL-10 and adoptive transfer of these TH17 and TH1 skewed cells seemingly exhibited milder EAE disease. S-Nitrosoglutathione 85-89 negative elongation factor complex member C/D, Th1l Mus musculus 35-38 29960806-6 2018 In addition, adoptive transfer of CD4+ T cells from GSNO treated EAE mice to active EAE mice also ameliorated EAE disease with induction of spinal cord expression of IL-10 and reduction in of IL-17, thus suggesting the participation of IL-10 mechanism in GSNO mediated immunomodulation. S-Nitrosoglutathione 52-56 interleukin 10 Mus musculus 166-171 29960806-6 2018 In addition, adoptive transfer of CD4+ T cells from GSNO treated EAE mice to active EAE mice also ameliorated EAE disease with induction of spinal cord expression of IL-10 and reduction in of IL-17, thus suggesting the participation of IL-10 mechanism in GSNO mediated immunomodulation. S-Nitrosoglutathione 52-56 interleukin 17A Mus musculus 192-197 29960806-6 2018 In addition, adoptive transfer of CD4+ T cells from GSNO treated EAE mice to active EAE mice also ameliorated EAE disease with induction of spinal cord expression of IL-10 and reduction in of IL-17, thus suggesting the participation of IL-10 mechanism in GSNO mediated immunomodulation. S-Nitrosoglutathione 52-56 interleukin 10 Mus musculus 236-241 29960806-6 2018 In addition, adoptive transfer of CD4+ T cells from GSNO treated EAE mice to active EAE mice also ameliorated EAE disease with induction of spinal cord expression of IL-10 and reduction in of IL-17, thus suggesting the participation of IL-10 mechanism in GSNO mediated immunomodulation. S-Nitrosoglutathione 255-259 interleukin 10 Mus musculus 236-241 29960806-8 2018 Overall, these data document a modulatory role of GSNO in IL-17/IL-10 axis of EAE and other autoimmune diseases. S-Nitrosoglutathione 50-54 interleukin 17A Mus musculus 58-63 29960806-8 2018 Overall, these data document a modulatory role of GSNO in IL-17/IL-10 axis of EAE and other autoimmune diseases. S-Nitrosoglutathione 50-54 interleukin 10 Mus musculus 64-69 30254659-3 2018 GSNO content is regulated by the GSNO-degrading enzyme S-nitrosoglutathione reductase (GSNOR). S-Nitrosoglutathione 0-4 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 33-85 30254659-3 2018 GSNO content is regulated by the GSNO-degrading enzyme S-nitrosoglutathione reductase (GSNOR). S-Nitrosoglutathione 0-4 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 87-92 30103682-11 2018 Reduced levels of peroxynitrite resulted from the GSNO-mediated inhibition of aberrant activity of neuronal nitric oxide synthase (nNOS). S-Nitrosoglutathione 50-54 nitric oxide synthase 1 Rattus norvegicus 99-129 30193463-7 2018 This was done by using a model NO-releasing polymer film system, plasticized poly(vinyl chloride) (PVC) and S-nitrosoglutathione, to examine how NO-mediated pre-adsorbed Fb, a major blood serum protein that initiates the blood clotting cascade, affects platelet adhesion and activation. S-Nitrosoglutathione 108-128 fibrinogen beta chain Homo sapiens 170-172 29792953-11 2018 GSNO administration to diabetic animals, on the other hand, was able to ameliorate loss of ZO-1 and occludin as well as normalize ICAM-1 and VCAM-1 expression, restore BBB integrity, and improve cognitive deficits. S-Nitrosoglutathione 0-4 tight junction protein 1 Mus musculus 91-95 29792953-11 2018 GSNO administration to diabetic animals, on the other hand, was able to ameliorate loss of ZO-1 and occludin as well as normalize ICAM-1 and VCAM-1 expression, restore BBB integrity, and improve cognitive deficits. S-Nitrosoglutathione 0-4 occludin Mus musculus 100-108 29792953-11 2018 GSNO administration to diabetic animals, on the other hand, was able to ameliorate loss of ZO-1 and occludin as well as normalize ICAM-1 and VCAM-1 expression, restore BBB integrity, and improve cognitive deficits. S-Nitrosoglutathione 0-4 intercellular adhesion molecule 1 Mus musculus 130-136 29792953-11 2018 GSNO administration to diabetic animals, on the other hand, was able to ameliorate loss of ZO-1 and occludin as well as normalize ICAM-1 and VCAM-1 expression, restore BBB integrity, and improve cognitive deficits. S-Nitrosoglutathione 0-4 vascular cell adhesion molecule 1 Mus musculus 141-147 30103682-11 2018 Reduced levels of peroxynitrite resulted from the GSNO-mediated inhibition of aberrant activity of neuronal nitric oxide synthase (nNOS). S-Nitrosoglutathione 50-54 nitric oxide synthase 1 Rattus norvegicus 131-135 29929044-6 2018 Interestingly, using the Fluorescence-based Multiplexed Host Cell Reactivation Assay (FM-HCR), we show that GSNO actually enhances AAG activity, which is consistent with the literature. S-Nitrosoglutathione 108-112 coiled-coil alpha-helical rod protein 1 Homo sapiens 89-92 29929044-6 2018 Interestingly, using the Fluorescence-based Multiplexed Host Cell Reactivation Assay (FM-HCR), we show that GSNO actually enhances AAG activity, which is consistent with the literature. S-Nitrosoglutathione 108-112 N-methylpurine DNA glycosylase Homo sapiens 131-134 29605742-6 2018 Degradation of desmin and troponin-T was increased by L-NAME while decreased by GSNO. S-Nitrosoglutathione 80-84 desmin Homo sapiens 15-21 29777958-9 2018 A preliminary in vivo study on full-thickness excisional wounds in mice showed that topical NO release from the PAA:F127/GSNO hydrogels is triggered by exudate absorption and leads to increased angiogenesis and collagen fiber organization, as well as TGF-beta, IGF-1, SDF-1, and IL-10 gene expressions in the cicatricial tissue. S-Nitrosoglutathione 121-125 insulin-like growth factor 1 Mus musculus 261-266 29777958-9 2018 A preliminary in vivo study on full-thickness excisional wounds in mice showed that topical NO release from the PAA:F127/GSNO hydrogels is triggered by exudate absorption and leads to increased angiogenesis and collagen fiber organization, as well as TGF-beta, IGF-1, SDF-1, and IL-10 gene expressions in the cicatricial tissue. S-Nitrosoglutathione 121-125 chemokine (C-X-C motif) ligand 12 Mus musculus 268-273 29777958-9 2018 A preliminary in vivo study on full-thickness excisional wounds in mice showed that topical NO release from the PAA:F127/GSNO hydrogels is triggered by exudate absorption and leads to increased angiogenesis and collagen fiber organization, as well as TGF-beta, IGF-1, SDF-1, and IL-10 gene expressions in the cicatricial tissue. S-Nitrosoglutathione 121-125 interleukin 10 Mus musculus 279-284 30008318-2 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major bioactive NO species, is regulated by GSNO reductase (GSNOR), a highly conserved master regulator of NO signaling. S-Nitrosoglutathione 27-47 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 102-116 30008318-2 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major bioactive NO species, is regulated by GSNO reductase (GSNOR), a highly conserved master regulator of NO signaling. S-Nitrosoglutathione 27-47 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 118-123 30008318-2 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major bioactive NO species, is regulated by GSNO reductase (GSNOR), a highly conserved master regulator of NO signaling. S-Nitrosoglutathione 49-53 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 102-116 30008318-2 2018 The intracellular level of S-nitrosoglutathione (GSNO), a major bioactive NO species, is regulated by GSNO reductase (GSNOR), a highly conserved master regulator of NO signaling. S-Nitrosoglutathione 49-53 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 118-123 29203326-3 2018 The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). S-Nitrosoglutathione 13-17 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 81-95 29203326-3 2018 The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). S-Nitrosoglutathione 13-17 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 97-102 29705071-6 2018 Consistently, NO donor S-nitrosoglutathione inhibited STIM1 puncta formation and ICRAC in HEK293 cells, but this effect was absent in cells expressing the Cys49Ser/Cys56Ser STIM1 double mutant. S-Nitrosoglutathione 23-43 stromal interaction molecule 1 Homo sapiens 54-59 29705509-5 2018 PTP1B-deficient macrophages exhibited an enhanced response to gamma-radiation, UV-light, LPS and S-nitroso-glutathione. S-Nitrosoglutathione 97-118 protein tyrosine phosphatase, non-receptor type 1 Mus musculus 0-5 29946131-8 2018 S-nitrosoglutathione induced PP1-dependent CBF desensitization in mouse tracheal rings, cultured cells and isolated cilia. S-Nitrosoglutathione 0-20 protein phosphatase 1 catalytic subunit gamma Mus musculus 29-32 29705071-6 2018 Consistently, NO donor S-nitrosoglutathione inhibited STIM1 puncta formation and ICRAC in HEK293 cells, but this effect was absent in cells expressing the Cys49Ser/Cys56Ser STIM1 double mutant. S-Nitrosoglutathione 23-43 stromal interaction molecule 1 Homo sapiens 173-178 29600466-5 2018 GSNOR irreversibly degrades S-nitrosoglutathione (GSNO), the major low molecular weight S-nitrosothiol involved in the formation of protein S-nitrosothiols through transnitrosylation. S-Nitrosoglutathione 28-48 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-5 29857826-9 2018 GSNO treatment reduced lipid peroxidation and MPO levels and inhibited expression of NF-kappaB and iNOS in the intestine. S-Nitrosoglutathione 0-4 myeloperoxidase Rattus norvegicus 46-49 29857826-9 2018 GSNO treatment reduced lipid peroxidation and MPO levels and inhibited expression of NF-kappaB and iNOS in the intestine. S-Nitrosoglutathione 0-4 nitric oxide synthase 2 Rattus norvegicus 99-103 29618799-5 2018 Examination of the enzymatic regulator of endogenous S-nitrosoglutathione availability, S-nitrosoglutathione reductase, reveals increased expression of the reductase in preterm myometrium associated with decreased total protein S-nitrosation. S-Nitrosoglutathione 53-73 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 88-118 29309132-8 2018 Treatment of recombinant BAM3 and BAM1 with GSNO caused significant, dose-dependent inhibition of BAM3 activity while BAM1 was largely unaffected. S-Nitrosoglutathione 44-48 beta-amylase 3 Arabidopsis thaliana 25-29 29309132-8 2018 Treatment of recombinant BAM3 and BAM1 with GSNO caused significant, dose-dependent inhibition of BAM3 activity while BAM1 was largely unaffected. S-Nitrosoglutathione 44-48 beta-amylase 1 Arabidopsis thaliana 34-38 29309132-8 2018 Treatment of recombinant BAM3 and BAM1 with GSNO caused significant, dose-dependent inhibition of BAM3 activity while BAM1 was largely unaffected. S-Nitrosoglutathione 44-48 beta-amylase 3 Arabidopsis thaliana 98-102 29309132-10 2018 In addition, we generated a BAM1 mutant resembling BAM3 that was sensitive to GSNO inhibition. S-Nitrosoglutathione 78-82 beta-amylase 1 Arabidopsis thaliana 28-32 29309132-10 2018 In addition, we generated a BAM1 mutant resembling BAM3 that was sensitive to GSNO inhibition. S-Nitrosoglutathione 78-82 beta-amylase 3 Arabidopsis thaliana 51-55 29309132-11 2018 These findings demonstrate a differential response of two BAM paralogs to the Cys-modifying reagent GSNO and provide a possible molecular basis for reduced BAM3 activity in cold-stressed plants. S-Nitrosoglutathione 100-104 beta-amylase 3 Arabidopsis thaliana 156-160 29694854-2 2018 Cellular GSNO homeostasis is regulated via its synthesis by reaction between nitric oxide and glutathione and its enzymatic catabolism by GSNO reductase (GSNOR). S-Nitrosoglutathione 9-13 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 138-152 29694854-2 2018 Cellular GSNO homeostasis is regulated via its synthesis by reaction between nitric oxide and glutathione and its enzymatic catabolism by GSNO reductase (GSNOR). S-Nitrosoglutathione 9-13 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 154-159 29694854-5 2018 Both N6022 and exogenous GSNO treatments increased the spleen levels of GSNO, as documented by increased protein-associated S-nitrosothiols, and inhibited polarization and CNS effector function of proinflammatory TH17 cells while inducing the polarization and CNS effector function of anti-inflammatory CD4+ CD25+ FOXP3- regulatory T (Treg) cells. S-Nitrosoglutathione 25-29 interleukin 2 receptor, alpha chain Mus musculus 308-312 29694854-5 2018 Both N6022 and exogenous GSNO treatments increased the spleen levels of GSNO, as documented by increased protein-associated S-nitrosothiols, and inhibited polarization and CNS effector function of proinflammatory TH17 cells while inducing the polarization and CNS effector function of anti-inflammatory CD4+ CD25+ FOXP3- regulatory T (Treg) cells. S-Nitrosoglutathione 25-29 forkhead box P3 Mus musculus 314-319 29694854-9 2018 Taken together, these data document that optimization of cellular GSNO homeostasis by GSNOR inhibitor (N6022) in NO metabolizing cells attenuates EAE disease via selective inhibition of pro-inflammatory subsets of CD4+ cells (TH1/TH17) while upregulating anti-inflammatory subsets of CD4+ cells (TH2/Treg) without causing lymphopenic effects and thus offers a potential treatment option for MS/EAE. S-Nitrosoglutathione 66-70 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 86-91 29522778-6 2018 The icv-STZ induced elevations in Abeta40 and Abeta42 and reduced levels of BDNF in hippocampal homogenates were also attenuated after GSNO treatment in these rats. S-Nitrosoglutathione 135-139 brain-derived neurotrophic factor Rattus norvegicus 76-80 29522778-8 2018 The results suggest that GSNO ameliorates the cognitive deficits and associated brain biochemical changes in this experimental model of sporadic AD, and NO-BDNF interactions could play crucial role in these effects. S-Nitrosoglutathione 25-29 brain-derived neurotrophic factor Rattus norvegicus 156-160 29570672-3 2018 Stimulation of the NO-GCs by S-nitrosoglutathione (GSNO) reduced BP in normotensive and hypertensive wildtype (WT) and NO-GC2-KO mice more efficiently than in NO-GC1-KO. S-Nitrosoglutathione 29-49 guanylate cyclase 2f Mus musculus 122-125 29570672-3 2018 Stimulation of the NO-GCs by S-nitrosoglutathione (GSNO) reduced BP in normotensive and hypertensive wildtype (WT) and NO-GC2-KO mice more efficiently than in NO-GC1-KO. S-Nitrosoglutathione 51-55 guanylate cyclase 2f Mus musculus 122-125 27780722-0 2018 GSNO promotes functional recovery in experimental TBI by stabilizing HIF-1alpha. S-Nitrosoglutathione 0-4 hypoxia inducible factor 1 subunit alpha Homo sapiens 69-79 27780722-3 2018 Based on reports that HIF-1alpha could be stabilized via S-nitrosylation, we tested the hypothesis that the S-nitrosylating agent S-nitrosoglutathione (GSNO) would stabilize HIF-1alpha, thereby stimulating neurorepair mechanisms and aiding in functional recovery. S-Nitrosoglutathione 130-150 hypoxia inducible factor 1 subunit alpha Homo sapiens 22-32 27780722-3 2018 Based on reports that HIF-1alpha could be stabilized via S-nitrosylation, we tested the hypothesis that the S-nitrosylating agent S-nitrosoglutathione (GSNO) would stabilize HIF-1alpha, thereby stimulating neurorepair mechanisms and aiding in functional recovery. S-Nitrosoglutathione 130-150 hypoxia inducible factor 1 subunit alpha Homo sapiens 174-184 27780722-3 2018 Based on reports that HIF-1alpha could be stabilized via S-nitrosylation, we tested the hypothesis that the S-nitrosylating agent S-nitrosoglutathione (GSNO) would stabilize HIF-1alpha, thereby stimulating neurorepair mechanisms and aiding in functional recovery. S-Nitrosoglutathione 152-156 hypoxia inducible factor 1 subunit alpha Homo sapiens 174-184 27780722-8 2018 The mechanisms of GSNO-mediated S-nitrosylation of HIF-1alpha were determined using brain endothelial cells. S-Nitrosoglutathione 18-22 hypoxia inducible factor 1 subunit alpha Homo sapiens 51-61 27780722-10 2018 GSNO also increased the expression of HIF-1alpha and VEGF. S-Nitrosoglutathione 0-4 hypoxia inducible factor 1 subunit alpha Homo sapiens 38-48 27780722-10 2018 GSNO also increased the expression of HIF-1alpha and VEGF. S-Nitrosoglutathione 0-4 vascular endothelial growth factor A Homo sapiens 53-57 27780722-11 2018 The beneficial effects of GSNO on neurobehavioral functions in TBI animals were blocked by treatment with the HIF-1alpha inhibitor 2-methoxyestradiol (2-ME). S-Nitrosoglutathione 26-30 hypoxia inducible factor 1 subunit alpha Homo sapiens 110-120 27780722-12 2018 The stimulatory effect of GSNO on VEGF was reversed not only by 2-ME but also by the denitrosylating agent dithiothreitol, confirming our hypothesis that GSNO"s benefits are mediated by the stabilization of HIF-1alpha via S-nitrosylation. S-Nitrosoglutathione 26-30 vascular endothelial growth factor A Homo sapiens 34-38 27780722-12 2018 The stimulatory effect of GSNO on VEGF was reversed not only by 2-ME but also by the denitrosylating agent dithiothreitol, confirming our hypothesis that GSNO"s benefits are mediated by the stabilization of HIF-1alpha via S-nitrosylation. S-Nitrosoglutathione 26-30 hypoxia inducible factor 1 subunit alpha Homo sapiens 207-217 27780722-12 2018 The stimulatory effect of GSNO on VEGF was reversed not only by 2-ME but also by the denitrosylating agent dithiothreitol, confirming our hypothesis that GSNO"s benefits are mediated by the stabilization of HIF-1alpha via S-nitrosylation. S-Nitrosoglutathione 154-158 vascular endothelial growth factor A Homo sapiens 34-38 27780722-12 2018 The stimulatory effect of GSNO on VEGF was reversed not only by 2-ME but also by the denitrosylating agent dithiothreitol, confirming our hypothesis that GSNO"s benefits are mediated by the stabilization of HIF-1alpha via S-nitrosylation. S-Nitrosoglutathione 154-158 hypoxia inducible factor 1 subunit alpha Homo sapiens 207-217 27780722-13 2018 GSNO"s S-nitrosylation of HIF-1alpha was further confirmed using a biotin switch assay in endothelial cells. S-Nitrosoglutathione 0-4 hypoxia inducible factor 1 subunit alpha Homo sapiens 26-36 27780722-14 2018 The data provide evidence that GSNO treatment of TBI aids functional recovery through stabilizing HIF-1alpha via S-nitrosylation. S-Nitrosoglutathione 31-35 hypoxia inducible factor 1 subunit alpha Homo sapiens 98-108 29545820-16 2018 GSNO could be decomposed by the GSNO reductase (GSNOR) to GSSG which, in turn, is reduced to GSH by glutathione reductase (GR). S-Nitrosoglutathione 0-4 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 32-46 29545820-16 2018 GSNO could be decomposed by the GSNO reductase (GSNOR) to GSSG which, in turn, is reduced to GSH by glutathione reductase (GR). S-Nitrosoglutathione 0-4 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 48-53 29545820-16 2018 GSNO could be decomposed by the GSNO reductase (GSNOR) to GSSG which, in turn, is reduced to GSH by glutathione reductase (GR). S-Nitrosoglutathione 0-4 glutathione-disulfide reductase Homo sapiens 100-121 29545820-16 2018 GSNO could be decomposed by the GSNO reductase (GSNOR) to GSSG which, in turn, is reduced to GSH by glutathione reductase (GR). S-Nitrosoglutathione 0-4 glutathione-disulfide reductase Homo sapiens 123-125 29286066-11 2018 The present study demonstrated that treatment with the NO donors SNP or GSNO led to an increase in ERK1/2 S-nitrosylation, and a reduction in ERK1/2 phosphorylation, which was accompanied by growth inhibition of U251 glioma cells. S-Nitrosoglutathione 72-76 mitogen-activated protein kinase 3 Homo sapiens 99-105 29286066-11 2018 The present study demonstrated that treatment with the NO donors SNP or GSNO led to an increase in ERK1/2 S-nitrosylation, and a reduction in ERK1/2 phosphorylation, which was accompanied by growth inhibition of U251 glioma cells. S-Nitrosoglutathione 72-76 mitogen-activated protein kinase 3 Homo sapiens 142-148 29286066-12 2018 Mutational analysis demonstrated that Cys183 was vital for S-nitrosylation of ERK1, and that preventing ERK1 S-nitrosylation by replacing Cys183 with alanine partially reversed GSNO-induced cell apoptosis, and reductions in cell viability and ERK1/2 phosphorylation. S-Nitrosoglutathione 177-181 mitogen-activated protein kinase 3 Homo sapiens 78-82 29286066-12 2018 Mutational analysis demonstrated that Cys183 was vital for S-nitrosylation of ERK1, and that preventing ERK1 S-nitrosylation by replacing Cys183 with alanine partially reversed GSNO-induced cell apoptosis, and reductions in cell viability and ERK1/2 phosphorylation. S-Nitrosoglutathione 177-181 mitogen-activated protein kinase 3 Homo sapiens 104-108 29286066-12 2018 Mutational analysis demonstrated that Cys183 was vital for S-nitrosylation of ERK1, and that preventing ERK1 S-nitrosylation by replacing Cys183 with alanine partially reversed GSNO-induced cell apoptosis, and reductions in cell viability and ERK1/2 phosphorylation. S-Nitrosoglutathione 177-181 mitogen-activated protein kinase 3 Homo sapiens 243-249 29445102-7 2018 Analysis of high shear conditions indicated that platelets activated on fibrinogen, induced stress fibre formation, which was reversed by GSNO treatment. S-Nitrosoglutathione 138-142 fibrinogen beta chain Homo sapiens 72-82 30568058-13 2018 However, ADH3 contributes to the development of alcoholic osteoporosis under CAC by participating in alcohol metabolism, increasing metabolic toxicity, and lowering GSNO reducing activity. S-Nitrosoglutathione 165-169 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide Mus musculus 9-13 29368397-9 2018 Treatment with high [Ca2+ ] and without GSNO produced proteolysis of RyR, DHPR, and JP1. S-Nitrosoglutathione 40-44 ryanodine receptor 2 Rattus norvegicus 69-72 29368397-9 2018 Treatment with high [Ca2+ ] and without GSNO produced proteolysis of RyR, DHPR, and JP1. S-Nitrosoglutathione 40-44 junctophilin 1 Rattus norvegicus 84-87 29368397-10 2018 On the other hand, treatment with high [Ca2+ ] and GSNO caused complete inhibition of RyR and DHPR proteolysis and partial inhibition of JP1 proteolysis. S-Nitrosoglutathione 51-55 ryanodine receptor 2 Rattus norvegicus 86-89 29368397-10 2018 On the other hand, treatment with high [Ca2+ ] and GSNO caused complete inhibition of RyR and DHPR proteolysis and partial inhibition of JP1 proteolysis. S-Nitrosoglutathione 51-55 junctophilin 1 Rattus norvegicus 137-140 28972151-4 2017 Moreover, the kinase activity of SlPDK1 was inhibited by S-nitrosoglutathione in a concentration-dependent manner, indicating that SlPDK1 activity is abrogated by S-nitrosylation. S-Nitrosoglutathione 57-77 3-phosphoinositide-dependent protein kinase-1 Solanum lycopersicum 33-39 28972151-4 2017 Moreover, the kinase activity of SlPDK1 was inhibited by S-nitrosoglutathione in a concentration-dependent manner, indicating that SlPDK1 activity is abrogated by S-nitrosylation. S-Nitrosoglutathione 57-77 3-phosphoinositide-dependent protein kinase-1 Solanum lycopersicum 131-137 29218054-8 2017 In addition, the exogenously applied GSNO not only compromised the endocytosis of PIN2-GFP but also inhibited the root elongation in a concentration-dependent manner. S-Nitrosoglutathione 37-41 Auxin efflux carrier family protein Arabidopsis thaliana 82-86 28705807-5 2017 H2S levels were increased in response to l-cysteine, and the effect of l-cysteine was augmented by GSNO in a cGMP-dependent protein kinase-sensitive manner, suggesting augmentation of CSE/H2S by cGMP/PKG pathway. S-Nitrosoglutathione 99-103 cystathionine gamma-lyase Homo sapiens 184-187 28917840-4 2017 Surprisingly, non-cytotoxic NO (S-nitrosoglutathione) and nitrite markedly reduced Hcy-induced IRE1alpha phosphorylation, Xbp1 mRNA splicing, CHOP expression, and Annexin V-positive cells, indicating the cytoprotection of NO and nitrite against Hcy-induced ER stress and apoptosis. S-Nitrosoglutathione 32-52 endoplasmic reticulum (ER) to nucleus signalling 1 Mus musculus 95-104 28917840-4 2017 Surprisingly, non-cytotoxic NO (S-nitrosoglutathione) and nitrite markedly reduced Hcy-induced IRE1alpha phosphorylation, Xbp1 mRNA splicing, CHOP expression, and Annexin V-positive cells, indicating the cytoprotection of NO and nitrite against Hcy-induced ER stress and apoptosis. S-Nitrosoglutathione 32-52 X-box binding protein 1 Mus musculus 122-126 28917840-4 2017 Surprisingly, non-cytotoxic NO (S-nitrosoglutathione) and nitrite markedly reduced Hcy-induced IRE1alpha phosphorylation, Xbp1 mRNA splicing, CHOP expression, and Annexin V-positive cells, indicating the cytoprotection of NO and nitrite against Hcy-induced ER stress and apoptosis. S-Nitrosoglutathione 32-52 DNA-damage inducible transcript 3 Mus musculus 142-146 28917840-4 2017 Surprisingly, non-cytotoxic NO (S-nitrosoglutathione) and nitrite markedly reduced Hcy-induced IRE1alpha phosphorylation, Xbp1 mRNA splicing, CHOP expression, and Annexin V-positive cells, indicating the cytoprotection of NO and nitrite against Hcy-induced ER stress and apoptosis. S-Nitrosoglutathione 32-52 annexin A5 Mus musculus 163-172 28705807-5 2017 H2S levels were increased in response to l-cysteine, and the effect of l-cysteine was augmented by GSNO in a cGMP-dependent protein kinase-sensitive manner, suggesting augmentation of CSE/H2S by cGMP/PKG pathway. S-Nitrosoglutathione 99-103 protein kinase cGMP-dependent 1 Homo sapiens 200-203 28705807-6 2017 As a result, GSNO-induced relaxation was inhibited by dl-PPG. S-Nitrosoglutathione 13-17 serglycin Homo sapiens 57-60 28121054-9 2017 Moreover, GSNO-induced PI3 K (phosphoinositide 3-kinase)/Akt phosphorylation might contribute to HIF-1alpha stabilization and nucleus translocation, thereby aiding aldolase A and GLUT1 mRNAs upregulation. S-Nitrosoglutathione 10-14 solute carrier family 2 member 1 Homo sapiens 179-184 28006950-0 2017 Augmentation of S-Nitrosoglutathione Controls Cigarette Smoke-Induced Inflammatory-Oxidative Stress and Chronic Obstructive Pulmonary Disease-Emphysema Pathogenesis by Restoring Cystic Fibrosis Transmembrane Conductance Regulator Function. S-Nitrosoglutathione 16-36 cystic fibrosis transmembrane conductance regulator Mus musculus 178-229 28006950-5 2017 We further demonstrate that treatment with GSNO or S-nitrosoglutathione reductase (GSNOR)-inhibitor (N6022) significantly inhibits cigarette smoke extract (CSE; 5%)-induced decrease in membrane CFTR expression by rescuing it from ubiquitin (Ub)-positive aggresome bodies (p < 0.05). S-Nitrosoglutathione 43-47 cystic fibrosis transmembrane conductance regulator Mus musculus 194-198 28006950-7 2017 In addition, GSNO augmentation inhibits protein misfolding as CSE-induced colocalization of ubiquitinated proteins and LC3B (in autophagy bodies) is significantly reduced by GSNO/N6022 treatment. S-Nitrosoglutathione 13-17 microtubule-associated protein 1 light chain 3 beta Mus musculus 119-123 28006950-7 2017 In addition, GSNO augmentation inhibits protein misfolding as CSE-induced colocalization of ubiquitinated proteins and LC3B (in autophagy bodies) is significantly reduced by GSNO/N6022 treatment. S-Nitrosoglutathione 174-178 microtubule-associated protein 1 light chain 3 beta Mus musculus 119-123 28006950-9 2017 As a proof of concept, we demonstrate that GSNO augmentation suppresses Ch-CS-induced perinuclear CFTR protein accumulation (p < 0.05), which restores both acquired CFTR dysfunction and autophagy impairment, seen in COPD-emphysema subjects. S-Nitrosoglutathione 43-47 cystic fibrosis transmembrane conductance regulator Mus musculus 98-102 28006950-10 2017 INNOVATION: GSNO augmentation alleviates CS-induced acquired CFTR dysfunction and resulting autophagy impairment. S-Nitrosoglutathione 12-16 cystic fibrosis transmembrane conductance regulator Mus musculus 61-65 28006950-11 2017 CONCLUSION: Overall, we found that augmenting GSNO levels controls COPD-emphysema pathogenesis by reducing CS-induced acquired CFTR dysfunction and resulting autophagy impairment and chronic inflammatory-oxidative stress. S-Nitrosoglutathione 46-50 cystic fibrosis transmembrane conductance regulator Mus musculus 127-131 28603024-6 2017 Moreover, the denitrosylation of Trx1 following KA treatment could be suppressed by the Fas ligand (FasL) antisense oligodeoxynucleotides (AS-ODNs), the Trx reductase (TrxR) inhibitor dinitrochlorobenzene (DNCB), or the Nitric oxide (NO) donors sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 276-296 thioredoxin 1 Rattus norvegicus 33-37 28603024-6 2017 Moreover, the denitrosylation of Trx1 following KA treatment could be suppressed by the Fas ligand (FasL) antisense oligodeoxynucleotides (AS-ODNs), the Trx reductase (TrxR) inhibitor dinitrochlorobenzene (DNCB), or the Nitric oxide (NO) donors sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 276-296 Fas ligand Rattus norvegicus 88-98 28603024-6 2017 Moreover, the denitrosylation of Trx1 following KA treatment could be suppressed by the Fas ligand (FasL) antisense oligodeoxynucleotides (AS-ODNs), the Trx reductase (TrxR) inhibitor dinitrochlorobenzene (DNCB), or the Nitric oxide (NO) donors sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 276-296 Fas ligand Rattus norvegicus 100-104 28603024-6 2017 Moreover, the denitrosylation of Trx1 following KA treatment could be suppressed by the Fas ligand (FasL) antisense oligodeoxynucleotides (AS-ODNs), the Trx reductase (TrxR) inhibitor dinitrochlorobenzene (DNCB), or the Nitric oxide (NO) donors sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 298-302 thioredoxin 1 Rattus norvegicus 33-37 28603024-6 2017 Moreover, the denitrosylation of Trx1 following KA treatment could be suppressed by the Fas ligand (FasL) antisense oligodeoxynucleotides (AS-ODNs), the Trx reductase (TrxR) inhibitor dinitrochlorobenzene (DNCB), or the Nitric oxide (NO) donors sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 298-302 Fas ligand Rattus norvegicus 88-98 28603024-6 2017 Moreover, the denitrosylation of Trx1 following KA treatment could be suppressed by the Fas ligand (FasL) antisense oligodeoxynucleotides (AS-ODNs), the Trx reductase (TrxR) inhibitor dinitrochlorobenzene (DNCB), or the Nitric oxide (NO) donors sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 298-302 Fas ligand Rattus norvegicus 100-104 28603024-8 2017 NS102, FasL AS-ODNs, GSNO and SNP could provide neuroprotection of the pyramidal neurons of CA1 and CA3/dentate gyrus (DG) regions by attenuating Trx1 denitrosylation. S-Nitrosoglutathione 21-25 carbonic anhydrase 1 Rattus norvegicus 92-95 28603024-8 2017 NS102, FasL AS-ODNs, GSNO and SNP could provide neuroprotection of the pyramidal neurons of CA1 and CA3/dentate gyrus (DG) regions by attenuating Trx1 denitrosylation. S-Nitrosoglutathione 21-25 carbonic anhydrase 3 Rattus norvegicus 100-103 28121054-0 2017 Enhanced Aerobic Glycolysis by S-Nitrosoglutathione via HIF-1alpha Associated GLUT1/Aldolase A Axis in Human Endothelial Cells. S-Nitrosoglutathione 31-51 hypoxia inducible factor 1 subunit alpha Homo sapiens 56-66 28121054-0 2017 Enhanced Aerobic Glycolysis by S-Nitrosoglutathione via HIF-1alpha Associated GLUT1/Aldolase A Axis in Human Endothelial Cells. S-Nitrosoglutathione 31-51 solute carrier family 2 member 1 Homo sapiens 78-83 28121054-1 2017 S-nitrosoglutathione (GSNO)-induced apoptosis is associated with reactive oxygen species and loss of mitochondrial Omi/HtrA2 in human endothelial cells (ECs). S-Nitrosoglutathione 0-20 HtrA serine peptidase 2 Homo sapiens 119-124 28121054-1 2017 S-nitrosoglutathione (GSNO)-induced apoptosis is associated with reactive oxygen species and loss of mitochondrial Omi/HtrA2 in human endothelial cells (ECs). S-Nitrosoglutathione 22-26 HtrA serine peptidase 2 Homo sapiens 119-124 28121054-3 2017 Here, we demonstrate that hypoxia induced factor-1alpha (HIF-1alpha)-linked aerobic glycolysis is associated with mitochondrial abnormality by treatment of human EC-derived EA.hy926 cells with GSNO (500 microM) for 6 h. GSNO exposure increased the levels of Aldolase A and glucose transporter-1 (GLUT1) mRNAs and proteins. S-Nitrosoglutathione 193-197 hypoxia inducible factor 1 subunit alpha Homo sapiens 57-67 28121054-3 2017 Here, we demonstrate that hypoxia induced factor-1alpha (HIF-1alpha)-linked aerobic glycolysis is associated with mitochondrial abnormality by treatment of human EC-derived EA.hy926 cells with GSNO (500 microM) for 6 h. GSNO exposure increased the levels of Aldolase A and glucose transporter-1 (GLUT1) mRNAs and proteins. S-Nitrosoglutathione 193-197 solute carrier family 2 member 1 Homo sapiens 273-294 28121054-3 2017 Here, we demonstrate that hypoxia induced factor-1alpha (HIF-1alpha)-linked aerobic glycolysis is associated with mitochondrial abnormality by treatment of human EC-derived EA.hy926 cells with GSNO (500 microM) for 6 h. GSNO exposure increased the levels of Aldolase A and glucose transporter-1 (GLUT1) mRNAs and proteins. S-Nitrosoglutathione 193-197 solute carrier family 2 member 1 Homo sapiens 296-301 28121054-3 2017 Here, we demonstrate that hypoxia induced factor-1alpha (HIF-1alpha)-linked aerobic glycolysis is associated with mitochondrial abnormality by treatment of human EC-derived EA.hy926 cells with GSNO (500 microM) for 6 h. GSNO exposure increased the levels of Aldolase A and glucose transporter-1 (GLUT1) mRNAs and proteins. S-Nitrosoglutathione 220-224 hypoxia inducible factor 1 subunit alpha Homo sapiens 57-67 28121054-5 2017 Using the biotin switch assay, we found that GSNO increased the S-nitrosylating levels of total protein and HIF-1alpha. S-Nitrosoglutathione 45-49 hypoxia inducible factor 1 subunit alpha Homo sapiens 108-118 28121054-9 2017 Moreover, GSNO-induced PI3 K (phosphoinositide 3-kinase)/Akt phosphorylation might contribute to HIF-1alpha stabilization and nucleus translocation, thereby aiding aldolase A and GLUT1 mRNAs upregulation. S-Nitrosoglutathione 10-14 AKT serine/threonine kinase 1 Homo sapiens 57-60 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 8-28 coagulation factor II, thrombin Homo sapiens 46-54 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 8-28 myosin heavy chain 14 Homo sapiens 89-95 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 8-28 modulator of VRAC current 1 Homo sapiens 119-137 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 8-28 modulator of VRAC current 1 Homo sapiens 139-142 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 30-34 coagulation factor II, thrombin Homo sapiens 46-54 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 30-34 myosin heavy chain 14 Homo sapiens 89-95 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 30-34 modulator of VRAC current 1 Homo sapiens 119-137 28509344-8 2017 Results S-nitrosoglutathione (GSNO) inhibited thrombin-induced platelet shape change and myosin phosphorylation of the myosin light chain (MLC). S-Nitrosoglutathione 30-34 modulator of VRAC current 1 Homo sapiens 139-142 28509344-11 2017 Treatment of platelets with GSNO blocked ROCK-mediated increases in phosphoMLCP-thr853 induced by thrombin. S-Nitrosoglutathione 28-32 coagulation factor II, thrombin Homo sapiens 98-106 28509344-13 2017 Further exploration of the mechanism demonstrated that GSNO stimulated the association of RhoA with protein kinase G (PKG) and the inhibitory phosphorylation (serine188) of RhoA in a cGMP-dependent manner. S-Nitrosoglutathione 55-59 ras homolog family member A Homo sapiens 90-94 28509344-13 2017 Further exploration of the mechanism demonstrated that GSNO stimulated the association of RhoA with protein kinase G (PKG) and the inhibitory phosphorylation (serine188) of RhoA in a cGMP-dependent manner. S-Nitrosoglutathione 55-59 protein kinase cGMP-dependent 1 Homo sapiens 100-116 28509344-13 2017 Further exploration of the mechanism demonstrated that GSNO stimulated the association of RhoA with protein kinase G (PKG) and the inhibitory phosphorylation (serine188) of RhoA in a cGMP-dependent manner. S-Nitrosoglutathione 55-59 protein kinase cGMP-dependent 1 Homo sapiens 118-121 28509344-13 2017 Further exploration of the mechanism demonstrated that GSNO stimulated the association of RhoA with protein kinase G (PKG) and the inhibitory phosphorylation (serine188) of RhoA in a cGMP-dependent manner. S-Nitrosoglutathione 55-59 ras homolog family member A Homo sapiens 173-177 28509344-15 2017 The inhibition of RhoA by GSNO prevented ROCK-mediated phosphorylation and inhibition of MLCP activity. S-Nitrosoglutathione 26-30 ras homolog family member A Homo sapiens 18-22 28109803-6 2017 Light-driven increments in NO scavenging rates coincided with pronounced rises in S-nitrosothiol content and GSNO reductase (GSNOR) activity, thereby suggesting that GSNO formation and subsequent removal via GSNOR might be key for controlling NO levels during seedling deetiolation. S-Nitrosoglutathione 109-113 alcohol dehydrogenase class III Solanum lycopersicum 125-130 28109803-6 2017 Light-driven increments in NO scavenging rates coincided with pronounced rises in S-nitrosothiol content and GSNO reductase (GSNOR) activity, thereby suggesting that GSNO formation and subsequent removal via GSNOR might be key for controlling NO levels during seedling deetiolation. S-Nitrosoglutathione 109-113 alcohol dehydrogenase class III Solanum lycopersicum 208-213 28121054-9 2017 Moreover, GSNO-induced PI3 K (phosphoinositide 3-kinase)/Akt phosphorylation might contribute to HIF-1alpha stabilization and nucleus translocation, thereby aiding aldolase A and GLUT1 mRNAs upregulation. S-Nitrosoglutathione 10-14 hypoxia inducible factor 1 subunit alpha Homo sapiens 97-107 28121054-10 2017 Taken together, higher concentration GSNO promotes glycolytic flux enhancement and methylglyoxal formation via HIF-1alpha S-nitrosylation. S-Nitrosoglutathione 37-41 hypoxia inducible factor 1 subunit alpha Homo sapiens 111-121 28419866-9 2017 The perinuclear OAbz-GSNO fluorescence increases in a time dependent manner and this increase in fluorescence is abolished by siRNA knockdown of GSNOR or by treatment with GSNOR-specific inhibitors N6022 and C3. S-Nitrosoglutathione 21-25 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 145-150 28419866-9 2017 The perinuclear OAbz-GSNO fluorescence increases in a time dependent manner and this increase in fluorescence is abolished by siRNA knockdown of GSNOR or by treatment with GSNOR-specific inhibitors N6022 and C3. S-Nitrosoglutathione 21-25 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 172-177 28419866-10 2017 Taken together, these data demonstrate that OAbz-GSNO can be used as a tool to monitor the activity of GSNOR in live cells. S-Nitrosoglutathione 49-53 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 103-108 28393572-3 2017 GSNOR metabolizes S-nitrosoglutathione (GSNO), S-hydroxymethylglutathione (the spontaneous adduct of formaldehyde and glutathione), and some alcohols. S-Nitrosoglutathione 18-38 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-5 28393572-4 2017 GSNOR modulates reactive nitric oxide ( NO) availability in the cell by catalyzing the breakdown of GSNO, and indirectly regulates S-nitrosothiols (RSNOs) through GSNO-mediated protein S-nitrosation. S-Nitrosoglutathione 100-104 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-5 28222773-4 2017 RESULTS: GSNO released considerable NO in the culture medium of PK-15 cells, and NO was scavenged by its scavenger hemoglobin (Hb) in a dose-dependent manner. S-Nitrosoglutathione 9-13 HGB Sus scrofa 115-125 28616019-8 2017 Exogenously administered GSNO was found not only to stabilize HIF-1alpha and to induce HIF-1alpha-dependent genes but also to stimulate the regeneration process and to aid in functional recovery in TBI animals. S-Nitrosoglutathione 25-29 hypoxia inducible factor 1 subunit alpha Homo sapiens 62-72 28616019-8 2017 Exogenously administered GSNO was found not only to stabilize HIF-1alpha and to induce HIF-1alpha-dependent genes but also to stimulate the regeneration process and to aid in functional recovery in TBI animals. S-Nitrosoglutathione 25-29 hypoxia inducible factor 1 subunit alpha Homo sapiens 87-97 28337758-3 2017 MAT-I/III activity is stimulated by Met, but inhibited by S-nitrosoglutathione, and the methylation index (MI) increases after Met stimulation of L02 cells. S-Nitrosoglutathione 58-78 methionine adenosyltransferase 1A Homo sapiens 0-9 28337758-4 2017 Met and S-nitrosoglutathione inhibit MAT-II activity, and the MI decreases after Met stimulation of HepG2 cells. S-Nitrosoglutathione 8-28 methionine adenosyltransferase 2B Homo sapiens 37-43 27880005-0 2017 S-nitrosoglutathione promotes cell wall remodelling, alters the transcriptional profile and induces root hair formation in the hairless root hair defective 6 (rhd6) mutant of Arabidopsis thaliana. S-Nitrosoglutathione 0-20 ROOT HAIR DEFECTIVE6 Arabidopsis thaliana 159-163 27880005-3 2017 GSNO and auxin restored the root hair phenotype of the hairless root hair defective 6 (rhd6) mutant. S-Nitrosoglutathione 0-4 ROOT HAIR DEFECTIVE6 Arabidopsis thaliana 87-91 27880005-6 2017 GSNO, but not auxin, restored the wild-type root glycome and transcriptome profiles in rhd6, modulating the expression of a large number of genes related to cell wall composition and metabolism, as well as those encoding ribosomal proteins, DNA and histone-modifying enzymes and proteins involved in post-translational modification. S-Nitrosoglutathione 0-4 ROOT HAIR DEFECTIVE6 Arabidopsis thaliana 87-91 27484743-11 2016 GSNO treatment of LPS-challenged rats decreased caspase-3, iNOS, TNF-alpha, T lymphocyte infiltration and remarkably increased levels of IL-10, PPAR-gamma and GSH. S-Nitrosoglutathione 0-4 caspase 3 Rattus norvegicus 48-57 27216010-3 2016 GSNO is degraded by GSNO reductase (GSNOR). S-Nitrosoglutathione 0-4 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 20-34 27216010-3 2016 GSNO is degraded by GSNO reductase (GSNOR). S-Nitrosoglutathione 0-4 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 36-41 28066263-1 2016 Aims: Gamma-glutamyl transferase (GGT), an enzyme present on the endothelium, is involved in the release of nitric oxide (NO) from S-nitrosoglutathione (GSNO) and in the GSNO-induced vasodilation. S-Nitrosoglutathione 131-151 gamma-glutamyltransferase 1 Rattus norvegicus 6-32 28066263-1 2016 Aims: Gamma-glutamyl transferase (GGT), an enzyme present on the endothelium, is involved in the release of nitric oxide (NO) from S-nitrosoglutathione (GSNO) and in the GSNO-induced vasodilation. S-Nitrosoglutathione 131-151 gamma-glutamyltransferase 1 Rattus norvegicus 34-37 28066263-1 2016 Aims: Gamma-glutamyl transferase (GGT), an enzyme present on the endothelium, is involved in the release of nitric oxide (NO) from S-nitrosoglutathione (GSNO) and in the GSNO-induced vasodilation. S-Nitrosoglutathione 153-157 gamma-glutamyltransferase 1 Rattus norvegicus 6-32 28066263-1 2016 Aims: Gamma-glutamyl transferase (GGT), an enzyme present on the endothelium, is involved in the release of nitric oxide (NO) from S-nitrosoglutathione (GSNO) and in the GSNO-induced vasodilation. S-Nitrosoglutathione 153-157 gamma-glutamyltransferase 1 Rattus norvegicus 34-37 28066263-1 2016 Aims: Gamma-glutamyl transferase (GGT), an enzyme present on the endothelium, is involved in the release of nitric oxide (NO) from S-nitrosoglutathione (GSNO) and in the GSNO-induced vasodilation. S-Nitrosoglutathione 170-174 gamma-glutamyltransferase 1 Rattus norvegicus 6-32 28066263-1 2016 Aims: Gamma-glutamyl transferase (GGT), an enzyme present on the endothelium, is involved in the release of nitric oxide (NO) from S-nitrosoglutathione (GSNO) and in the GSNO-induced vasodilation. S-Nitrosoglutathione 170-174 gamma-glutamyltransferase 1 Rattus norvegicus 34-37 28066263-7 2016 That of protein disulfide isomerase (PDI), another redox sensitive enzyme involved in GSNO metabolism, was assessed following inhibition with bacitracin. S-Nitrosoglutathione 86-90 prolyl 4-hydroxylase subunit beta Rattus norvegicus 8-35 28066263-7 2016 That of protein disulfide isomerase (PDI), another redox sensitive enzyme involved in GSNO metabolism, was assessed following inhibition with bacitracin. S-Nitrosoglutathione 86-90 prolyl 4-hydroxylase subunit beta Rattus norvegicus 37-40 28066263-12 2016 Involvements of GGT, as that of PDI, in the GSNO effects were similar in all groups (pD2 for GSNO -0.5 to -1.5 following enzymatic inhibition). S-Nitrosoglutathione 44-48 gamma-glutamyltransferase 1 Rattus norvegicus 16-19 28066263-12 2016 Involvements of GGT, as that of PDI, in the GSNO effects were similar in all groups (pD2 for GSNO -0.5 to -1.5 following enzymatic inhibition). S-Nitrosoglutathione 44-48 prolyl 4-hydroxylase subunit beta Rattus norvegicus 32-35 27451206-4 2016 The catalytic ability of nitrosylated mu-calpain to degrade titin, nebulin, troponin-T and desmin was significantly reduced when the GSNO concentration was higher than 300muM. S-Nitrosoglutathione 133-137 titin Homo sapiens 60-65 27451206-4 2016 The catalytic ability of nitrosylated mu-calpain to degrade titin, nebulin, troponin-T and desmin was significantly reduced when the GSNO concentration was higher than 300muM. S-Nitrosoglutathione 133-137 nebulin Homo sapiens 67-74 27451206-4 2016 The catalytic ability of nitrosylated mu-calpain to degrade titin, nebulin, troponin-T and desmin was significantly reduced when the GSNO concentration was higher than 300muM. S-Nitrosoglutathione 133-137 desmin Homo sapiens 91-97 27756843-4 2016 Here, we show that Sirt1 is transnitrosated and inhibited by the physiologically relevant nitrosothiol S-nitrosoglutathione. S-Nitrosoglutathione 103-123 sirtuin 1 Homo sapiens 19-24 27756843-9 2016 Reversal of S-nitrosation resulted in full restoration of Sirt1 activity only in the presence of Zn2+, consistent with S-nitrosation of the Zn2+-tetrathiolate as the primary source of Sirt1 inhibition upon S-nitrosoglutathione treatment. S-Nitrosoglutathione 206-226 sirtuin 1 Homo sapiens 58-63 27756843-9 2016 Reversal of S-nitrosation resulted in full restoration of Sirt1 activity only in the presence of Zn2+, consistent with S-nitrosation of the Zn2+-tetrathiolate as the primary source of Sirt1 inhibition upon S-nitrosoglutathione treatment. S-Nitrosoglutathione 206-226 sirtuin 1 Homo sapiens 184-189 27126574-4 2016 METHODS: Serum albumin (SA) was S-nitrosated by reacting with (i) NaNO2 in acidic medium; (ii) different low-molecular weight S-nitrosothiols (RSNO) (S-nitrosocysteine (CysNO), S-nitrosoglutathione (GSNO), and S,S"-dinitrosobucillamine (Buc(NO)2)); and (iii) diethylamine NONOate (DEA/NO). S-Nitrosoglutathione 177-197 albumin Homo sapiens 9-22 27126574-4 2016 METHODS: Serum albumin (SA) was S-nitrosated by reacting with (i) NaNO2 in acidic medium; (ii) different low-molecular weight S-nitrosothiols (RSNO) (S-nitrosocysteine (CysNO), S-nitrosoglutathione (GSNO), and S,S"-dinitrosobucillamine (Buc(NO)2)); and (iii) diethylamine NONOate (DEA/NO). S-Nitrosoglutathione 199-203 albumin Homo sapiens 9-22 27891135-4 2016 The breakdown of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). S-Nitrosoglutathione 17-21 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 85-99 27891135-4 2016 The breakdown of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). S-Nitrosoglutathione 17-21 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 101-106 27484743-11 2016 GSNO treatment of LPS-challenged rats decreased caspase-3, iNOS, TNF-alpha, T lymphocyte infiltration and remarkably increased levels of IL-10, PPAR-gamma and GSH. S-Nitrosoglutathione 0-4 nitric oxide synthase 2 Rattus norvegicus 59-63 27484743-11 2016 GSNO treatment of LPS-challenged rats decreased caspase-3, iNOS, TNF-alpha, T lymphocyte infiltration and remarkably increased levels of IL-10, PPAR-gamma and GSH. S-Nitrosoglutathione 0-4 tumor necrosis factor Rattus norvegicus 65-74 27484743-11 2016 GSNO treatment of LPS-challenged rats decreased caspase-3, iNOS, TNF-alpha, T lymphocyte infiltration and remarkably increased levels of IL-10, PPAR-gamma and GSH. S-Nitrosoglutathione 0-4 interleukin 10 Rattus norvegicus 137-142 27484743-11 2016 GSNO treatment of LPS-challenged rats decreased caspase-3, iNOS, TNF-alpha, T lymphocyte infiltration and remarkably increased levels of IL-10, PPAR-gamma and GSH. S-Nitrosoglutathione 0-4 peroxisome proliferator-activated receptor gamma Rattus norvegicus 144-154 27545131-12 2016 (6) The expression of AKT/p-AKT was significantly lower in GSNO group than in the blank control group (P< 0.05), which could be significantly upregulated by pretreatment with high, medium and low concentration ICA in a concentration-dependent manner, above effects could be blocked by LY294002 (all P<0.05). S-Nitrosoglutathione 59-63 AKT serine/threonine kinase 1 Homo sapiens 22-25 27545131-12 2016 (6) The expression of AKT/p-AKT was significantly lower in GSNO group than in the blank control group (P< 0.05), which could be significantly upregulated by pretreatment with high, medium and low concentration ICA in a concentration-dependent manner, above effects could be blocked by LY294002 (all P<0.05). S-Nitrosoglutathione 59-63 AKT serine/threonine kinase 1 Homo sapiens 28-31 27545131-13 2016 (7) The expression of P53 was significantly higher in GSNO group than in the blank control group (P< 0.05), which could be significantly down regulated by pretreatment with high, medium and low concentration ICA in a concentration-dependent manner, above effects could be blocked by LY294002(all P<0.05). S-Nitrosoglutathione 54-58 tumor protein p53 Homo sapiens 22-25 27545131-14 2016 (8) The expression of CYC and caspase-3 was significantly reduced in the mitochondria and increased in cytoplasm post GSNO treatment compared to blank control group, which could be reversed by pretreatment with high, medium and low concentration ICA(all P<0.05). S-Nitrosoglutathione 118-122 cytochrome c, somatic Homo sapiens 22-25 27545131-14 2016 (8) The expression of CYC and caspase-3 was significantly reduced in the mitochondria and increased in cytoplasm post GSNO treatment compared to blank control group, which could be reversed by pretreatment with high, medium and low concentration ICA(all P<0.05). S-Nitrosoglutathione 118-122 caspase 3 Homo sapiens 30-39 27545131-16 2016 CONCLUSION: Icariin could reduce GSNO induced endothelial cell apoptosis through activating AKT pathway and downregulating P53 activity. S-Nitrosoglutathione 33-37 AKT serine/threonine kinase 1 Homo sapiens 92-95 27261193-3 2016 Here, we demonstrated that peroxiredoxin 2 (Prdx-2) nitrosylation was involved in cardiomyocyte differentiation of mouse embryonic stem (ES) cells induced by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 158-178 peroxiredoxin 2 Mus musculus 27-42 27261193-3 2016 Here, we demonstrated that peroxiredoxin 2 (Prdx-2) nitrosylation was involved in cardiomyocyte differentiation of mouse embryonic stem (ES) cells induced by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 158-178 peroxiredoxin 2 Mus musculus 44-50 27261193-3 2016 Here, we demonstrated that peroxiredoxin 2 (Prdx-2) nitrosylation was involved in cardiomyocyte differentiation of mouse embryonic stem (ES) cells induced by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 180-184 peroxiredoxin 2 Mus musculus 27-42 27261193-3 2016 Here, we demonstrated that peroxiredoxin 2 (Prdx-2) nitrosylation was involved in cardiomyocyte differentiation of mouse embryonic stem (ES) cells induced by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 180-184 peroxiredoxin 2 Mus musculus 44-50 27420046-4 2016 In vitro, Fyn could be S-nitrosylated by S-nitrosoglutathione (GSNO, an exogenous NO donor), and in vivo, endogenous NO synthesized by NO synthases (NOS) could enhance Fyn S-nitrosylation. S-Nitrosoglutathione 41-61 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 10-13 27420046-4 2016 In vitro, Fyn could be S-nitrosylated by S-nitrosoglutathione (GSNO, an exogenous NO donor), and in vivo, endogenous NO synthesized by NO synthases (NOS) could enhance Fyn S-nitrosylation. S-Nitrosoglutathione 63-67 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 10-13 27129464-8 2016 In reduced glutathione (GSH) containing aqueous buffer (pH 7.4), human and bovine erythrocytic CAII-mediated formation of GSNO from nitrite and GS(15)NO from (15)N-nitrite. S-Nitrosoglutathione 122-126 carbonic anhydrase 2 Bos taurus 95-99 26891162-11 2016 RESULTS: Compared with the endotoxemic rats, the addition of GSNO reduced the intestinal injury observed in histologic sections, decreased permeability to fluorescein isothiocyanate dextran, attenuated damage of the junction between epithelia, and protected against the LPS-induced expression decrease of ZO-1. S-Nitrosoglutathione 61-65 tight junction protein 1 Rattus norvegicus 305-309 26984419-6 2016 Additionally, this inhibitory effect of GSNO on KNa channel activity was diminished by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ), an inhibitor of soluble guanylate cyclase (sGC), and KT5823, an inhibitor of protein kinase G (PKG). S-Nitrosoglutathione 40-44 protein kinase cGMP-dependent 1 Homo sapiens 215-231 26984419-6 2016 Additionally, this inhibitory effect of GSNO on KNa channel activity was diminished by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ), an inhibitor of soluble guanylate cyclase (sGC), and KT5823, an inhibitor of protein kinase G (PKG). S-Nitrosoglutathione 40-44 protein kinase cGMP-dependent 1 Homo sapiens 233-236 26891162-12 2016 Furthermore, addition of GSNO reduced plasma and intestinal tumor necrosis factor and interleukin 1beta levels as well as inhibited the LPS-induced up-regulation of myosin light-chain kinase expression and NF-kappaB p65 level in the intestine. S-Nitrosoglutathione 25-29 myosin light chain kinase Rattus norvegicus 165-190 26891162-12 2016 Furthermore, addition of GSNO reduced plasma and intestinal tumor necrosis factor and interleukin 1beta levels as well as inhibited the LPS-induced up-regulation of myosin light-chain kinase expression and NF-kappaB p65 level in the intestine. S-Nitrosoglutathione 25-29 interleukin 1 beta Rattus norvegicus 86-103 27116554-5 2016 Treatment with HPMC/GSNO 10 mM solution significantly reduced alveolar bone loss, oxidative stress and TNF-alpha e IL-1beta levels in the surrounding gingival tissue, and led to a decreased transcription of RANK and TNF-alpha genes and elevated bone alkaline phosphatase, compared to the HPMC group. S-Nitrosoglutathione 20-24 tumor necrosis factor Rattus norvegicus 103-112 27064847-3 2016 GSNO accumulation is attenuated by GSNO reductase (GSNOR), a cysteine-rich cytosolic enzyme. S-Nitrosoglutathione 0-4 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 35-49 27064847-3 2016 GSNO accumulation is attenuated by GSNO reductase (GSNOR), a cysteine-rich cytosolic enzyme. S-Nitrosoglutathione 0-4 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 51-56 27116554-5 2016 Treatment with HPMC/GSNO 10 mM solution significantly reduced alveolar bone loss, oxidative stress and TNF-alpha e IL-1beta levels in the surrounding gingival tissue, and led to a decreased transcription of RANK and TNF-alpha genes and elevated bone alkaline phosphatase, compared to the HPMC group. S-Nitrosoglutathione 20-24 interleukin 1 beta Rattus norvegicus 115-123 27116554-5 2016 Treatment with HPMC/GSNO 10 mM solution significantly reduced alveolar bone loss, oxidative stress and TNF-alpha e IL-1beta levels in the surrounding gingival tissue, and led to a decreased transcription of RANK and TNF-alpha genes and elevated bone alkaline phosphatase, compared to the HPMC group. S-Nitrosoglutathione 20-24 tumor necrosis factor Rattus norvegicus 216-225 26596859-6 2016 GSNO treatment at 2h after CCI decreased the expression levels of phospho neuronal nitric oxide synthase (pnNOS), alpha II spectrin degraded products, and 3-NT, while also decreasing the activities of nNOS and calpains. S-Nitrosoglutathione 0-4 spectrin alpha, non-erythrocytic 1 Mus musculus 114-131 26742737-0 2016 Effects of S-Nitrosoglutathione on the Expression of MMP-1 mRNA in HT1080 Cells during Hypoxic Hypoxia. S-Nitrosoglutathione 11-31 matrix metallopeptidase 1 Homo sapiens 53-58 26742737-1 2016 Synthetic antioxidant S-nitrosoglutathione suppressed the expression of MMP-1 mRNA in HT1080 cells exposed to hypoxic hypoxia; hyperexpression of superoxide dismutase 2 increased and hyperexpression of catalase inhibited the expression of MMP-1 mRNA in HT1080 cells. S-Nitrosoglutathione 22-42 matrix metallopeptidase 1 Homo sapiens 72-77 26742737-1 2016 Synthetic antioxidant S-nitrosoglutathione suppressed the expression of MMP-1 mRNA in HT1080 cells exposed to hypoxic hypoxia; hyperexpression of superoxide dismutase 2 increased and hyperexpression of catalase inhibited the expression of MMP-1 mRNA in HT1080 cells. S-Nitrosoglutathione 22-42 catalase Homo sapiens 202-210 26742737-1 2016 Synthetic antioxidant S-nitrosoglutathione suppressed the expression of MMP-1 mRNA in HT1080 cells exposed to hypoxic hypoxia; hyperexpression of superoxide dismutase 2 increased and hyperexpression of catalase inhibited the expression of MMP-1 mRNA in HT1080 cells. S-Nitrosoglutathione 22-42 matrix metallopeptidase 1 Homo sapiens 239-244 26917471-4 2016 Earlier characterization was conducted on a purified sGC treated with S-nitrosoglutathione, and identified three S-nitrosated cysteines (SNO-Cys). S-Nitrosoglutathione 70-90 guanylate cyclase 1 soluble subunit beta 2 Rattus norvegicus 53-56 26596859-6 2016 GSNO treatment at 2h after CCI decreased the expression levels of phospho neuronal nitric oxide synthase (pnNOS), alpha II spectrin degraded products, and 3-NT, while also decreasing the activities of nNOS and calpains. S-Nitrosoglutathione 0-4 nitric oxide synthase 1, neuronal Mus musculus 107-111 26596859-10 2016 These data indicate that peroxynitrite-mediated activation and GSNO-mediated inhibition of the deleterious nNOS/calpain system play critical roles in the pathobiology of neuronal protection and functional recovery in TBI disease. S-Nitrosoglutathione 63-67 nitric oxide synthase 1, neuronal Mus musculus 107-111 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 119-137 solute carrier family 18 member A2 Homo sapiens 243-248 27094420-1 2016 S-nitrosoglutathione reductase (GSNOR) is considered a key enzyme in the regulation of intracellular levels of S-nitrosoglutathione and protein S-nitrosylation. S-Nitrosoglutathione 0-20 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 32-37 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 119-137 solute carrier family 18 member A3 Homo sapiens 250-255 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 119-137 solute carrier family 17 member 7 Homo sapiens 257-263 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 119-137 solute carrier family 17 member 6 Homo sapiens 268-274 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 139-143 solute carrier family 18 member A2 Homo sapiens 243-248 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 139-143 solute carrier family 18 member A3 Homo sapiens 250-255 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 139-143 solute carrier family 17 member 7 Homo sapiens 257-263 26541750-5 2015 Using the biotin switch assay followed by avidin precipitation and immunoblotting we found that the nitric oxide donor nitrosoglutathione (GSNO) not only increased total cysteine S-nitrosylation, but also increased cysteine S-nitrosylation of VMAT2, VAChT, VGLUT1 and VGLUT2 in the mouse brain. S-Nitrosoglutathione 139-143 solute carrier family 17 member 6 Homo sapiens 268-274 26177470-0 2015 S-Nitrosoglutathione-mediated STAT3 regulation in efficacy of radiotherapy and cisplatin therapy in head and neck squamous cell carcinoma. S-Nitrosoglutathione 0-20 signal transducer and activator of transcription 3 Mus musculus 30-35 26407725-6 2015 However, gating of VDAC3 was evoked by dithiothreitol (DTT) and S-nitrosoglutathione (GSNO), which are thought to suppress disulfide-bond formation. S-Nitrosoglutathione 64-84 voltage dependent anion channel 3 Homo sapiens 19-24 26407725-6 2015 However, gating of VDAC3 was evoked by dithiothreitol (DTT) and S-nitrosoglutathione (GSNO), which are thought to suppress disulfide-bond formation. S-Nitrosoglutathione 86-90 voltage dependent anion channel 3 Homo sapiens 19-24 26177470-2 2015 Recent studies have reported that GSNO regulates the activities of STAT3 and NF-kappaB via S-nitrosylation dependent mechanisms. S-Nitrosoglutathione 34-38 signal transducer and activator of transcription 3 Mus musculus 67-72 26177470-2 2015 Recent studies have reported that GSNO regulates the activities of STAT3 and NF-kappaB via S-nitrosylation dependent mechanisms. S-Nitrosoglutathione 34-38 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 77-86 26177470-6 2015 GSNO treatment of these cell lines reversibly decreased the STAT3 phosphorylation in a concentration dependent manner. S-Nitrosoglutathione 0-4 signal transducer and activator of transcription 3 Mus musculus 60-65 26177470-7 2015 GSNO treatment also decreased the basal and cytokine-stimulated activation of NF-kappaB in SCC14a cells and reduced the basal low degree of nitrotyrosine by inhibition of inducible NO synthase (iNOS) expression. S-Nitrosoglutathione 0-4 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 78-87 26177470-7 2015 GSNO treatment also decreased the basal and cytokine-stimulated activation of NF-kappaB in SCC14a cells and reduced the basal low degree of nitrotyrosine by inhibition of inducible NO synthase (iNOS) expression. S-Nitrosoglutathione 0-4 colon tumor susceptibility 14 Mus musculus 91-96 26177470-7 2015 GSNO treatment also decreased the basal and cytokine-stimulated activation of NF-kappaB in SCC14a cells and reduced the basal low degree of nitrotyrosine by inhibition of inducible NO synthase (iNOS) expression. S-Nitrosoglutathione 0-4 nitric oxide synthase 2, inducible Mus musculus 171-192 26177470-7 2015 GSNO treatment also decreased the basal and cytokine-stimulated activation of NF-kappaB in SCC14a cells and reduced the basal low degree of nitrotyrosine by inhibition of inducible NO synthase (iNOS) expression. S-Nitrosoglutathione 0-4 nitric oxide synthase 2, inducible Mus musculus 194-198 26177470-8 2015 The reduced STAT3/NF-kappaB activity by GSNO treatment was correlated with the decreased cell proliferation and increased apoptosis of HNSCC cells. S-Nitrosoglutathione 40-44 signal transducer and activator of transcription 3 Mus musculus 12-17 26177470-8 2015 The reduced STAT3/NF-kappaB activity by GSNO treatment was correlated with the decreased cell proliferation and increased apoptosis of HNSCC cells. S-Nitrosoglutathione 40-44 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 18-27 26177470-10 2015 Accordingly, GSNO treatment also resulted in decreased levels of phosphorylated STAT3. S-Nitrosoglutathione 13-17 signal transducer and activator of transcription 3 Mus musculus 80-85 26177470-11 2015 In summary, these studies demonstrate that GSNO treatment blocks the NF-kappaB and STAT3 pathways which are responsible for cell survival, proliferation and that GSNO mediated mechanisms complement cispaltin and radiation therapy, and thus could potentiate the therapeutic effect in HNSCC. S-Nitrosoglutathione 43-47 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 69-78 26177470-11 2015 In summary, these studies demonstrate that GSNO treatment blocks the NF-kappaB and STAT3 pathways which are responsible for cell survival, proliferation and that GSNO mediated mechanisms complement cispaltin and radiation therapy, and thus could potentiate the therapeutic effect in HNSCC. S-Nitrosoglutathione 43-47 signal transducer and activator of transcription 3 Mus musculus 83-88 26319693-5 2015 In this study, we reported that RIP3 could be S-nitrosylated by the exogenous NO donor GSNO in HEK293 cells and the Cys(119) residue was the key nitrosylation site. S-Nitrosoglutathione 87-91 receptor interacting serine/threonine kinase 3 Homo sapiens 32-36 26421519-5 2015 In demembranated (skinned) fibers, S-nitrosylation with 1 muM GSNO also decreased Ca(2+) sensitivity of contraction and 10 muM reduced maximal isometric force, while inhibition of relaxation and myofibrillar ATPase required higher concentrations (>= 100 muM). S-Nitrosoglutathione 62-66 dynein, axonemal, heavy chain 8 Mus musculus 208-214 26271717-6 2015 GSNO attenuated the increased calpain activities and calpain-mediated cleavage of p35 leading to production of p25 and aberrant Cdk5 activation. S-Nitrosoglutathione 0-4 cyclin-dependent kinase 5 regulatory subunit 1 Rattus norvegicus 82-85 26096525-4 2015 The NO donor S-nitrosoglutathione (GSNO) promoted the nuclear accumulation of NONEXPRESSOR OF PATHOGENESIS-RELATED GENES 1 (NPR1) protein accompanied by an elevated SA concentration and the activation of pathogenesis-related (PR) genes, leading to induced resistance of A. thaliana against Pseudomonas infection. S-Nitrosoglutathione 13-33 regulatory protein (NPR1) Arabidopsis thaliana 78-122 26096525-4 2015 The NO donor S-nitrosoglutathione (GSNO) promoted the nuclear accumulation of NONEXPRESSOR OF PATHOGENESIS-RELATED GENES 1 (NPR1) protein accompanied by an elevated SA concentration and the activation of pathogenesis-related (PR) genes, leading to induced resistance of A. thaliana against Pseudomonas infection. S-Nitrosoglutathione 13-33 regulatory protein (NPR1) Arabidopsis thaliana 124-128 26096525-4 2015 The NO donor S-nitrosoglutathione (GSNO) promoted the nuclear accumulation of NONEXPRESSOR OF PATHOGENESIS-RELATED GENES 1 (NPR1) protein accompanied by an elevated SA concentration and the activation of pathogenesis-related (PR) genes, leading to induced resistance of A. thaliana against Pseudomonas infection. S-Nitrosoglutathione 35-39 regulatory protein (NPR1) Arabidopsis thaliana 78-122 26096525-4 2015 The NO donor S-nitrosoglutathione (GSNO) promoted the nuclear accumulation of NONEXPRESSOR OF PATHOGENESIS-RELATED GENES 1 (NPR1) protein accompanied by an elevated SA concentration and the activation of pathogenesis-related (PR) genes, leading to induced resistance of A. thaliana against Pseudomonas infection. S-Nitrosoglutathione 35-39 regulatory protein (NPR1) Arabidopsis thaliana 124-128 26381869-7 2015 Supplementation of S-nitroso-l-glutathione (GSNO), a NO donor, or MG132, a potent inhibitor of the 26S proteasome, prevented eNOS silencing and PTIO-induced DHFR reduction in human umbilical vein endothelial cells. S-Nitrosoglutathione 19-42 dihydrofolate reductase Homo sapiens 157-161 26381869-7 2015 Supplementation of S-nitroso-l-glutathione (GSNO), a NO donor, or MG132, a potent inhibitor of the 26S proteasome, prevented eNOS silencing and PTIO-induced DHFR reduction in human umbilical vein endothelial cells. S-Nitrosoglutathione 44-48 dihydrofolate reductase Homo sapiens 157-161 26381869-8 2015 PTIO suppressed S-nitrosylation of DHFR, whereas GSNO promoted DHFR S-nitrosylation. S-Nitrosoglutathione 49-53 dihydrofolate reductase Homo sapiens 63-67 26271717-6 2015 GSNO attenuated the increased calpain activities and calpain-mediated cleavage of p35 leading to production of p25 and aberrant Cdk5 activation. S-Nitrosoglutathione 0-4 lipocalin 2 Rattus norvegicus 111-114 26271717-6 2015 GSNO attenuated the increased calpain activities and calpain-mediated cleavage of p35 leading to production of p25 and aberrant Cdk5 activation. S-Nitrosoglutathione 0-4 cyclin-dependent kinase 5 Rattus norvegicus 128-132 26271717-8 2015 In pBCCAO rat brains, GSNO treatment attenuated the expression of inducible nitric oxide synthase (iNOS) expression and also reduced the brain levels of nitro-tyrosine formation, thereby indicating the protective role of GSNO in iNOS/nitrosative-stress mediated calpain/tau pathologies under CCH conditions. S-Nitrosoglutathione 22-26 nitric oxide synthase 2 Rattus norvegicus 66-97 26271717-8 2015 In pBCCAO rat brains, GSNO treatment attenuated the expression of inducible nitric oxide synthase (iNOS) expression and also reduced the brain levels of nitro-tyrosine formation, thereby indicating the protective role of GSNO in iNOS/nitrosative-stress mediated calpain/tau pathologies under CCH conditions. S-Nitrosoglutathione 22-26 nitric oxide synthase 2 Rattus norvegicus 99-103 26271717-8 2015 In pBCCAO rat brains, GSNO treatment attenuated the expression of inducible nitric oxide synthase (iNOS) expression and also reduced the brain levels of nitro-tyrosine formation, thereby indicating the protective role of GSNO in iNOS/nitrosative-stress mediated calpain/tau pathologies under CCH conditions. S-Nitrosoglutathione 22-26 nitric oxide synthase 2 Rattus norvegicus 229-233 24853799-15 2015 In addition, the SCI-induced increase in immune cell infiltration, collagen deposition, iNOS, and ICAM-1 expression and apoptosis were attenuated by GSNO. S-Nitrosoglutathione 149-153 nitric oxide synthase 2 Rattus norvegicus 88-92 26163703-5 2015 The NO donor S-nitrosoglutathione rescued the growth phenotype of the nia mutants under phosphate deprivation to some extent, and it also increased the respiratory capacity of AOX. S-Nitrosoglutathione 13-33 acyl-CoA oxidase 1 Homo sapiens 176-179 24853799-15 2015 In addition, the SCI-induced increase in immune cell infiltration, collagen deposition, iNOS, and ICAM-1 expression and apoptosis were attenuated by GSNO. S-Nitrosoglutathione 149-153 intercellular adhesion molecule 1 Rattus norvegicus 98-104 28162277-3 2015 STAT3 S-nitrosylation was associated with inducible nitric oxide synthase (iNOS)-produced nitric oxide (NO) and S-nitrosoglutathione (GSNO), whereas S-glutathionylation of STAT3 was associated with cellular oxidative stress. S-Nitrosoglutathione 112-132 signal transducer and activator of transcription 3 Mus musculus 0-5 28162277-3 2015 STAT3 S-nitrosylation was associated with inducible nitric oxide synthase (iNOS)-produced nitric oxide (NO) and S-nitrosoglutathione (GSNO), whereas S-glutathionylation of STAT3 was associated with cellular oxidative stress. S-Nitrosoglutathione 134-138 signal transducer and activator of transcription 3 Mus musculus 0-5 28162277-7 2015 In this study, we identified that Cys259 was the target Cys residue of GSNO-mediated S-nitrosylation of STAT3. S-Nitrosoglutathione 71-75 signal transducer and activator of transcription 3 Mus musculus 104-109 28162277-3 2015 STAT3 S-nitrosylation was associated with inducible nitric oxide synthase (iNOS)-produced nitric oxide (NO) and S-nitrosoglutathione (GSNO), whereas S-glutathionylation of STAT3 was associated with cellular oxidative stress. S-Nitrosoglutathione 134-138 nitric oxide synthase 2, inducible Mus musculus 75-79 28162277-8 2015 The replacement of Cys259 residue with Ala abolished the inhibitory role of GSNO in IL-6-induced STAT3 phosphorylation and transactivation, suggesting the role of Cys259S-nitrosylation in STAT3phosphorylation. S-Nitrosoglutathione 76-80 interleukin 6 Mus musculus 84-88 28162277-8 2015 The replacement of Cys259 residue with Ala abolished the inhibitory role of GSNO in IL-6-induced STAT3 phosphorylation and transactivation, suggesting the role of Cys259S-nitrosylation in STAT3phosphorylation. S-Nitrosoglutathione 76-80 signal transducer and activator of transcription 3 Mus musculus 97-102 28162277-4 2015 NO produced by iNOS or treatment of microglia with exogenous GSNO inhibited STAT3 activation via inhibiting STAT3 phosphorylation (Tyr705). S-Nitrosoglutathione 61-65 signal transducer and activator of transcription 3 Mus musculus 76-81 28162277-10 2015 GSNO treatment of HNSCCN cell lines reversibly decreases the activation (phosphorylation) of STAT3 in a concentration dependent manner. S-Nitrosoglutathione 0-4 signal transducer and activator of transcription 3 Mus musculus 93-98 28162277-4 2015 NO produced by iNOS or treatment of microglia with exogenous GSNO inhibited STAT3 activation via inhibiting STAT3 phosphorylation (Tyr705). S-Nitrosoglutathione 61-65 signal transducer and activator of transcription 3 Mus musculus 108-113 28162277-11 2015 The reduced STAT3/NF-kB activity by GSNO correlated with decreased cell proliferation and increased apoptosis of HNSCC cells. S-Nitrosoglutathione 36-40 signal transducer and activator of transcription 3 Mus musculus 12-17 28162277-6 2015 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 Janus kinase 2 Mus musculus 41-45 28162277-6 2015 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Mus musculus 50-55 28162277-6 2015 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Mus musculus 57-62 28162277-6 2015 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Mus musculus 57-62 28162277-6 2015 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Mus musculus 57-62 26174015-4 2015 We therefore investigated whether GSNO-mediated neuroprotection and improved neurological functions depend on blocking nNOS/peroxynitrite-associated injurious mechanisms using a rat model of cerebral ischemia reperfusion (IR). S-Nitrosoglutathione 34-38 nitric oxide synthase 1 Rattus norvegicus 119-123 26070564-5 2015 Pharmacological inhibition or gene silencing of inducible NOS abrogated LPS-induced LKB1 degradation, whereas exposure of RAW 264.7 cells to S-nitroso-l-glutathione, a NO donor, triggered LKB1 S-nitrosylation. S-Nitrosoglutathione 141-164 serine/threonine kinase 11 Homo sapiens 188-192 26174015-6 2015 GSNO treatment of IR animals decreased IR-activated nNOS activity and neuronal peroxynitrite levels by reducing nNOS phosphorylation at Ser(1412). S-Nitrosoglutathione 0-4 nitric oxide synthase 1 Homo sapiens 52-56 26174015-0 2015 Blocking a vicious cycle nNOS/peroxynitrite/AMPK by S-nitrosoglutathione: implication for stroke therapy. S-Nitrosoglutathione 52-72 nitric oxide synthase 1 Homo sapiens 25-29 26174015-0 2015 Blocking a vicious cycle nNOS/peroxynitrite/AMPK by S-nitrosoglutathione: implication for stroke therapy. S-Nitrosoglutathione 52-72 protein kinase AMP-activated catalytic subunit alpha 1 Homo sapiens 44-48 26174015-6 2015 GSNO treatment of IR animals decreased IR-activated nNOS activity and neuronal peroxynitrite levels by reducing nNOS phosphorylation at Ser(1412). S-Nitrosoglutathione 0-4 nitric oxide synthase 1 Homo sapiens 112-116 26174015-9 2015 GSNO also decreased the activation of AMP Kinase (AMPK) and its upstream kinase LKB1, both of which were activated in IR brain. S-Nitrosoglutathione 0-4 protein kinase AMP-activated catalytic subunit alpha 1 Homo sapiens 38-48 26174015-9 2015 GSNO also decreased the activation of AMP Kinase (AMPK) and its upstream kinase LKB1, both of which were activated in IR brain. S-Nitrosoglutathione 0-4 protein kinase AMP-activated catalytic subunit alpha 1 Homo sapiens 50-54 26174015-9 2015 GSNO also decreased the activation of AMP Kinase (AMPK) and its upstream kinase LKB1, both of which were activated in IR brain. S-Nitrosoglutathione 0-4 serine/threonine kinase 11 Homo sapiens 80-84 25929187-5 2015 Here we reported that PYK2 over-expressed in human embryonic kidney (HEK293) cells was S-nitrosylated (forming SNO-PYK2) by reacting with GSNO, an exogenous NO donor, at one critical cysteine residue (Cys534) with a biotin switch assay. S-Nitrosoglutathione 138-142 protein tyrosine kinase 2 beta Homo sapiens 22-26 25929187-5 2015 Here we reported that PYK2 over-expressed in human embryonic kidney (HEK293) cells was S-nitrosylated (forming SNO-PYK2) by reacting with GSNO, an exogenous NO donor, at one critical cysteine residue (Cys534) with a biotin switch assay. S-Nitrosoglutathione 138-142 protein tyrosine kinase 2 beta Homo sapiens 115-119 25917852-4 2015 NO donors, sodium nitroprusside (SNP), S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione (GSNO), reduced Panx1 currents by 25-41%. S-Nitrosoglutathione 82-102 pannexin 1 Homo sapiens 119-124 25934761-1 2015 S-nitrosoglutathione supplementation to ovalbumin-sensitized and -challenged mice ameliorates methacholine-induced bronchoconstriction. S-Nitrosoglutathione 0-20 serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene Mus musculus 40-49 25819133-6 2015 NO-derived from BK stimulation of RAEC and incubation of the cells with the s-nitrosothiol S-nitrosoglutathione (GSNO) activated Rac1. S-Nitrosoglutathione 113-117 ras-related C3 botulinum toxin substrate 1 Oryctolagus cuniculus 129-133 25945035-0 2015 Promoting endothelial function by S-nitrosoglutathione through the HIF-1alpha/VEGF pathway stimulates neurorepair and functional recovery following experimental stroke in rats. S-Nitrosoglutathione 34-54 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 67-77 25945035-7 2015 Brain capillary endothelial cells were used to show that GSNO promotes angiogenesis and that GSNO-mediated induction of VEGF and the stimulation of angiogenesis are dependent on HIF-1alpha activity. S-Nitrosoglutathione 93-97 vascular endothelial growth factor A Rattus norvegicus 120-124 25945035-0 2015 Promoting endothelial function by S-nitrosoglutathione through the HIF-1alpha/VEGF pathway stimulates neurorepair and functional recovery following experimental stroke in rats. S-Nitrosoglutathione 34-54 vascular endothelial growth factor A Rattus norvegicus 78-82 25945035-7 2015 Brain capillary endothelial cells were used to show that GSNO promotes angiogenesis and that GSNO-mediated induction of VEGF and the stimulation of angiogenesis are dependent on HIF-1alpha activity. S-Nitrosoglutathione 93-97 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 178-188 25945035-3 2015 Using a rat model of cerebral ischemia and reperfusion (IR) in this study, we tested the hypothesis that GSNO invokes the neurorepair process and improves neurobehavioral functions through the angiogenic HIF-1alpha/VEGF pathway. S-Nitrosoglutathione 105-109 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 204-214 25945035-9 2015 GSNO treatment of IR not only remarkably enhanced further the expression of HIF-1alpha, VEGF, and PECAM-1 but also improved functioning compared with IR. S-Nitrosoglutathione 0-4 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 76-86 25945035-9 2015 GSNO treatment of IR not only remarkably enhanced further the expression of HIF-1alpha, VEGF, and PECAM-1 but also improved functioning compared with IR. S-Nitrosoglutathione 0-4 vascular endothelial growth factor A Rattus norvegicus 88-92 25945035-3 2015 Using a rat model of cerebral ischemia and reperfusion (IR) in this study, we tested the hypothesis that GSNO invokes the neurorepair process and improves neurobehavioral functions through the angiogenic HIF-1alpha/VEGF pathway. S-Nitrosoglutathione 105-109 vascular endothelial growth factor A Rattus norvegicus 215-219 25597545-9 2015 Multi-fold increases in the synthesis and deposition of elastin, glycosaminoglycans, hyaluronic acid, and lysyl oxidase crosslinking enzyme (LOX) were noted at higher GSNO dosages, and coculturing with ECs significantly furthered these trends. S-Nitrosoglutathione 167-171 elastin Homo sapiens 56-63 25945035-9 2015 GSNO treatment of IR not only remarkably enhanced further the expression of HIF-1alpha, VEGF, and PECAM-1 but also improved functioning compared with IR. S-Nitrosoglutathione 0-4 platelet and endothelial cell adhesion molecule 1 Rattus norvegicus 98-105 25945035-11 2015 Increased expression of VEGF and the degree of tube formation (angiogenesis) by GSNO were reduced after the inhibition of HIF-1alpha by 2-ME in an endothelial cell culture model. S-Nitrosoglutathione 80-84 vascular endothelial growth factor A Rattus norvegicus 24-28 25945035-11 2015 Increased expression of VEGF and the degree of tube formation (angiogenesis) by GSNO were reduced after the inhibition of HIF-1alpha by 2-ME in an endothelial cell culture model. S-Nitrosoglutathione 80-84 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 122-132 25945035-12 2015 2-ME treatment of the GSNO group also blocked not only GSNO"s effect of reduced infarct volume, decreased neuronal loss, and enhanced expression of PECAM-1 (P<0.001), but also its improvement of motor and neurological functions (P<0.001). S-Nitrosoglutathione 22-26 platelet and endothelial cell adhesion molecule 1 Rattus norvegicus 148-155 25945035-12 2015 2-ME treatment of the GSNO group also blocked not only GSNO"s effect of reduced infarct volume, decreased neuronal loss, and enhanced expression of PECAM-1 (P<0.001), but also its improvement of motor and neurological functions (P<0.001). S-Nitrosoglutathione 55-59 platelet and endothelial cell adhesion molecule 1 Rattus norvegicus 148-155 25945035-13 2015 CONCLUSION: GSNO stimulates the process of neurorepair, promotes angiogenesis, and aids functional recovery through the HIF-1alpha-dependent pathway, showing therapeutic and translational promise for stroke. S-Nitrosoglutathione 12-16 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 120-130 25652185-6 2015 In addition, the present study shows evidence that conformational changes in AChE promoted by incubation with N-19 and C-16 antibodies alter the enzyme"s functional connection to acetylcholine (ACh) (AChE-ACh complex) in an irreversible manner, resulting in impaired GSNO concentration and NO efflux from the erythrocyte. S-Nitrosoglutathione 267-271 acetylcholinesterase (Cartwright blood group) Homo sapiens 77-81 25652185-6 2015 In addition, the present study shows evidence that conformational changes in AChE promoted by incubation with N-19 and C-16 antibodies alter the enzyme"s functional connection to acetylcholine (ACh) (AChE-ACh complex) in an irreversible manner, resulting in impaired GSNO concentration and NO efflux from the erythrocyte. S-Nitrosoglutathione 267-271 acetylcholinesterase (Cartwright blood group) Homo sapiens 200-204 25597545-9 2015 Multi-fold increases in the synthesis and deposition of elastin, glycosaminoglycans, hyaluronic acid, and lysyl oxidase crosslinking enzyme (LOX) were noted at higher GSNO dosages, and coculturing with ECs significantly furthered these trends. S-Nitrosoglutathione 167-171 lysyl oxidase Homo sapiens 141-144 25597545-10 2015 Similar increases in TIMP-1 and MMP-9 levels were noted within cocultures with increasing GSNO dosages. S-Nitrosoglutathione 90-94 TIMP metallopeptidase inhibitor 1 Homo sapiens 21-27 25597545-10 2015 Similar increases in TIMP-1 and MMP-9 levels were noted within cocultures with increasing GSNO dosages. S-Nitrosoglutathione 90-94 matrix metallopeptidase 9 Homo sapiens 32-37 25187090-0 2015 S-nitrosoglutathione prevents blood-brain barrier disruption associated with increased matrix metalloproteinase-9 activity in experimental diabetes. S-Nitrosoglutathione 0-20 matrix metallopeptidase 9 Mus musculus 87-113 25699590-2 2015 A major biologically active species of NO is S-nitrosoglutathione (GSNO), which is irreversibly degraded by GSNO reductase (GSNOR). S-Nitrosoglutathione 45-65 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 108-122 25699590-2 2015 A major biologically active species of NO is S-nitrosoglutathione (GSNO), which is irreversibly degraded by GSNO reductase (GSNOR). S-Nitrosoglutathione 45-65 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 124-129 25699590-2 2015 A major biologically active species of NO is S-nitrosoglutathione (GSNO), which is irreversibly degraded by GSNO reductase (GSNOR). S-Nitrosoglutathione 67-71 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 108-122 25699590-2 2015 A major biologically active species of NO is S-nitrosoglutathione (GSNO), which is irreversibly degraded by GSNO reductase (GSNOR). S-Nitrosoglutathione 67-71 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 124-129 25511472-8 2015 Addition of an exogenous NO donor (0.8 mM of S-nitroso-l-glutathione) to the iNOS-deficient MEFs augmented COX-2 expression. S-Nitrosoglutathione 45-68 nitric oxide synthase 2 Homo sapiens 77-81 25511472-8 2015 Addition of an exogenous NO donor (0.8 mM of S-nitroso-l-glutathione) to the iNOS-deficient MEFs augmented COX-2 expression. S-Nitrosoglutathione 45-68 prostaglandin-endoperoxide synthase 2 Mus musculus 107-112 25187090-10 2015 However, GSNO supplementation to diabetic animals was able to abridge MMP-9 activation as well as tissue inhibitor of matrix metalloproteinase-1 levels, restoring BBB integrity and also improving learning and memory. S-Nitrosoglutathione 9-13 matrix metallopeptidase 9 Mus musculus 70-75 25187090-11 2015 Our findings clearly suggest that GSNO could prevent hyperglycemia-induced disruption of BBB by suppressing MMP-9 activity. S-Nitrosoglutathione 34-38 matrix metallopeptidase 9 Mus musculus 108-113 25433859-6 2015 Our analysis suggested that beta-CDH induced an increase in endogenous NO production, followed by up-regulation of tomato HO1 gene and LR formation, all of which were mimicked by hemin and two NO-releasing compounds (SNP and GSNO). S-Nitrosoglutathione 225-229 heme oxygenase 1 Solanum lycopersicum 122-125 25483557-7 2015 Notably, CB3 mimicked the activity of thioredoxin by coupling with thioredoxin reductase to enhance GSNO reduction. S-Nitrosoglutathione 100-104 thioredoxin Homo sapiens 67-78 25640839-5 2015 GSNO treatment also attenuated the Abeta25-35-induced activation of GSK-3beta which is known to play critical role in tau hyperphosphorylation in addition to Cdk5. S-Nitrosoglutathione 0-4 glycogen synthase kinase 3 alpha Rattus norvegicus 68-77 25640839-5 2015 GSNO treatment also attenuated the Abeta25-35-induced activation of GSK-3beta which is known to play critical role in tau hyperphosphorylation in addition to Cdk5. S-Nitrosoglutathione 0-4 cyclin-dependent kinase 5 Rattus norvegicus 158-162 25640839-6 2015 Consistent with above studies using cultured neurons, we also observed that systemic GSNO treatment of transgenic mouse model of AD (APPSw/PS1(dE9)) attenuated calpain-mediated p35 proteolysis and Cdk5/GSK-3beta activities as well as tau hyperphosphorylation. S-Nitrosoglutathione 85-89 cyclin-dependent kinase 5, regulatory subunit 1 (p35) Mus musculus 177-180 25640839-6 2015 Consistent with above studies using cultured neurons, we also observed that systemic GSNO treatment of transgenic mouse model of AD (APPSw/PS1(dE9)) attenuated calpain-mediated p35 proteolysis and Cdk5/GSK-3beta activities as well as tau hyperphosphorylation. S-Nitrosoglutathione 85-89 cyclin-dependent kinase 5 Mus musculus 197-201 25640839-6 2015 Consistent with above studies using cultured neurons, we also observed that systemic GSNO treatment of transgenic mouse model of AD (APPSw/PS1(dE9)) attenuated calpain-mediated p35 proteolysis and Cdk5/GSK-3beta activities as well as tau hyperphosphorylation. S-Nitrosoglutathione 85-89 glycogen synthase kinase 3 alpha Mus musculus 202-211 25619132-3 2015 A proteomic analysis identified Gal-2 as a protein that was S-nitrosylated when mouse gastric mucosal lysates were reacted with S-nitrosoglutathione, a physiologically relevant S-nitrosylating agent. S-Nitrosoglutathione 128-148 lectin, galactose-binding, soluble 2 Mus musculus 32-37 25655275-8 2015 GH prevents motorneuronal death caused by GSNO and homocysteine, but not that by A23187. S-Nitrosoglutathione 42-46 growth hormone Mus musculus 0-2 25483557-7 2015 Notably, CB3 mimicked the activity of thioredoxin by coupling with thioredoxin reductase to enhance GSNO reduction. S-Nitrosoglutathione 100-104 thioredoxin Homo sapiens 38-49 24958331-2 2015 GSNO has been regarded as a store and transporter of NO, with significant interest as a potential therapeutic agent, acting as an NO donor.NO metabolism inside the erythrocyte generates several derivatives, which can be altered by external and internal stimuli such as acetylcholine (ACh), a natural substrate of acetylcholinesterase (AChE). S-Nitrosoglutathione 0-4 acetylcholinesterase (Cartwright blood group) Homo sapiens 335-339 24958331-4 2015 Hence, the objective of this research was to evaluate the efflux of GSNO, concomitant with the efflux of NO, after stimulation with AChE effectors. S-Nitrosoglutathione 68-72 acetylcholinesterase (Cartwright blood group) Homo sapiens 132-136 25359343-9 2015 Consistent with a link between S-nitrosoglutathione biochemistry and atopy: 1) interleukin 13 increased S-nitrosoglutathione reductase expression and 2) subjects with an S-nitrosoglutathione reductase single nucleotide polymorphism previously associated with asthma had higher IgE than those without this single nucleotide polymorphism. S-Nitrosoglutathione 31-51 interleukin 13 Homo sapiens 79-93 25557257-10 2015 It was previously reported that different types of SNOs, such as GSNO and S-nitrosoglutathione diethyl ester will increase CFTR maturation and function at the plasma membrane in human airway epithelial cells. S-Nitrosoglutathione 65-69 CF transmembrane conductance regulator Homo sapiens 123-127 25359343-9 2015 Consistent with a link between S-nitrosoglutathione biochemistry and atopy: 1) interleukin 13 increased S-nitrosoglutathione reductase expression and 2) subjects with an S-nitrosoglutathione reductase single nucleotide polymorphism previously associated with asthma had higher IgE than those without this single nucleotide polymorphism. S-Nitrosoglutathione 31-51 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 104-134 25359343-9 2015 Consistent with a link between S-nitrosoglutathione biochemistry and atopy: 1) interleukin 13 increased S-nitrosoglutathione reductase expression and 2) subjects with an S-nitrosoglutathione reductase single nucleotide polymorphism previously associated with asthma had higher IgE than those without this single nucleotide polymorphism. S-Nitrosoglutathione 31-51 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 170-200 25388371-5 2014 Mechanistic differences in apoptotic responses were observed as differential patterns of DNA fragmentation and levels of BAX, BCL-XL, CASP8, and p-ERK in response to GSNO and STS treatment. S-Nitrosoglutathione 166-170 BCL2 associated X, apoptosis regulator Homo sapiens 121-124 27668143-5 2015 In this short review, we assess the evidence supporting exogenous administration of GSNO after experimental stroke as a means to stimulate neuroregeneration and aid in functional recovery via stabilization of the HIF-1alpha/VEGF pathway. S-Nitrosoglutathione 84-88 hypoxia inducible factor 1 subunit alpha Homo sapiens 213-223 27668143-5 2015 In this short review, we assess the evidence supporting exogenous administration of GSNO after experimental stroke as a means to stimulate neuroregeneration and aid in functional recovery via stabilization of the HIF-1alpha/VEGF pathway. S-Nitrosoglutathione 84-88 vascular endothelial growth factor A Homo sapiens 224-228 26024299-4 2015 Here, we show that like SnRK2.6, SnRK2.2 can be inactivated by S-nitrosoglutathione (GSNO) treatment through S-nitrosylation. S-Nitrosoglutathione 63-83 SNF1-related protein kinase 2.2 Arabidopsis thaliana 33-40 26024299-4 2015 Here, we show that like SnRK2.6, SnRK2.2 can be inactivated by S-nitrosoglutathione (GSNO) treatment through S-nitrosylation. S-Nitrosoglutathione 85-89 SNF1-related protein kinase 2.2 Arabidopsis thaliana 33-40 25388371-5 2014 Mechanistic differences in apoptotic responses were observed as differential patterns of DNA fragmentation and levels of BAX, BCL-XL, CASP8, and p-ERK in response to GSNO and STS treatment. S-Nitrosoglutathione 166-170 BCL2 like 1 Homo sapiens 126-132 25388371-5 2014 Mechanistic differences in apoptotic responses were observed as differential patterns of DNA fragmentation and levels of BAX, BCL-XL, CASP8, and p-ERK in response to GSNO and STS treatment. S-Nitrosoglutathione 166-170 caspase 8 Homo sapiens 134-139 25388371-5 2014 Mechanistic differences in apoptotic responses were observed as differential patterns of DNA fragmentation and levels of BAX, BCL-XL, CASP8, and p-ERK in response to GSNO and STS treatment. S-Nitrosoglutathione 166-170 mitogen-activated protein kinase 1 Homo sapiens 147-150 25236749-7 2014 Omission of superoxide dismutase (SOD) reduced by half the GSNO yield in the absence of Mg(2+), demonstrating O2(-) formation. S-Nitrosoglutathione 59-63 superoxide dismutase 1 Homo sapiens 12-32 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 cAMP responsive element binding protein 1 Homo sapiens 137-141 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 inhibitor of nuclear factor kappa B kinase subunit beta Homo sapiens 218-226 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 caspase 1 Homo sapiens 228-237 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 tumor necrosis factor Homo sapiens 336-344 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 interleukin 1 beta Homo sapiens 346-354 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 interferon gamma Homo sapiens 356-365 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 interleukin 4 Homo sapiens 367-371 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 C-X-C motif chemokine ligand 8 Homo sapiens 373-377 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 C-C motif chemokine ligand 5 Homo sapiens 379-385 25135357-2 2014 At molecular level, GSNO effects have been shown to modulate the activity of a series of transcription factors (notably NF-kappaB, AP-1, CREB and others) as well as other components of signal transduction chains (e.g. IKK-beta, caspase 1, calpain and others), resulting in the modulation of several cytokines and chemokines expression (TNFalpha, IL-1beta, IFN-gamma, IL-4, IL-8, RANTES, MCP-1 and others). S-Nitrosoglutathione 20-24 C-C motif chemokine ligand 2 Homo sapiens 387-392 24777815-4 2014 Isoproterenol and S-nitrosoglutathione (GSNO) induced phosphorylation of PLC-beta3 and inhibited CPA-induced PI hydrolysis, Ca(2+) release, and muscle contraction. S-Nitrosoglutathione 18-38 phospholipase C beta 3 Homo sapiens 73-82 24777815-4 2014 Isoproterenol and S-nitrosoglutathione (GSNO) induced phosphorylation of PLC-beta3 and inhibited CPA-induced PI hydrolysis, Ca(2+) release, and muscle contraction. S-Nitrosoglutathione 40-44 phospholipase C beta 3 Homo sapiens 73-82 24777815-5 2014 The effect of isoproterenol on all three responses was inhibited by PKA inhibitor, myristoylated PKI, or AKAP inhibitor, Ht-31, whereas the effect of GSNO was selectively inhibited by PKG inhibitor, Rp-cGMPS. S-Nitrosoglutathione 150-154 protein kinase cGMP-dependent 1 Homo sapiens 184-187 24777815-6 2014 GSNO, but not isoproterenol, also phosphorylated Galphai-GTPase-activating protein, RGS2, and enhanced association of Galphai3-GTP and RGS2. S-Nitrosoglutathione 0-4 regulator of G protein signaling 2 Homo sapiens 84-88 24777815-6 2014 GSNO, but not isoproterenol, also phosphorylated Galphai-GTPase-activating protein, RGS2, and enhanced association of Galphai3-GTP and RGS2. S-Nitrosoglutathione 0-4 regulator of G protein signaling 2 Homo sapiens 135-139 24777815-7 2014 The effect of GSNO on PI hydrolysis was partly reversed in cells (i) expressing constitutively active GTPase-resistant Galphai mutant (Q204L), (ii) phosphorylation-site-deficient RGS2 mutant (S46A/S64A), or (iii) siRNA for RGS2. S-Nitrosoglutathione 14-18 regulator of G protein signaling 2 Homo sapiens 179-183 24777815-7 2014 The effect of GSNO on PI hydrolysis was partly reversed in cells (i) expressing constitutively active GTPase-resistant Galphai mutant (Q204L), (ii) phosphorylation-site-deficient RGS2 mutant (S46A/S64A), or (iii) siRNA for RGS2. S-Nitrosoglutathione 14-18 regulator of G protein signaling 2 Homo sapiens 223-227 25236749-7 2014 Omission of superoxide dismutase (SOD) reduced by half the GSNO yield in the absence of Mg(2+), demonstrating O2(-) formation. S-Nitrosoglutathione 59-63 superoxide dismutase 1 Homo sapiens 34-37 25274121-5 2014 The most stable form of [GSNO + H](+), SN1, protonated at the amino group, presents a syn conformation at the S-N (partial) double bond and all peptidic carbonyls involved in (strong) C O H-N hydrogen bonds, so allowing closure of a C5 (beta-strand), two C7 (gamma-turn), and one C9-membered rings. S-Nitrosoglutathione 25-29 solute carrier family 38 member 3 Homo sapiens 39-42 24627995-4 2014 The dose of GSNO was increased incrementally to 100 mug min(-1) whilst maintaining blood pressure of >140/80 mmHg. S-Nitrosoglutathione 12-16 CD59 molecule (CD59 blood group) Homo sapiens 56-62 24627995-7 2014 RESULTS: Augmentation index fell at 30 mug min(-1) S-nitrosoglutathione (-6%, 95% confidence interval 0.6 to 13%), a dose that did not affect blood pressure. S-Nitrosoglutathione 51-71 CD59 molecule (CD59 blood group) Homo sapiens 43-49 24887420-3 2014 GSNO treatment abrogated growth factor (HB-EGF) induced signal transduction including phosphorylation of Akt, p42/44 and STAT3, which are known to play critical roles in ovarian cancer growth and progression. S-Nitrosoglutathione 0-4 heparin-binding EGF-like growth factor Mus musculus 40-46 24654711-1 2014 S-nitrosoglutathione reductase (GSNOR) is the key enzyme controlling the intracellular levels of S-nitrosoglutathione and S-nitrosothiols. S-Nitrosoglutathione 0-20 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 32-37 24887420-3 2014 GSNO treatment abrogated growth factor (HB-EGF) induced signal transduction including phosphorylation of Akt, p42/44 and STAT3, which are known to play critical roles in ovarian cancer growth and progression. S-Nitrosoglutathione 0-4 thymoma viral proto-oncogene 1 Mus musculus 105-108 24887420-3 2014 GSNO treatment abrogated growth factor (HB-EGF) induced signal transduction including phosphorylation of Akt, p42/44 and STAT3, which are known to play critical roles in ovarian cancer growth and progression. S-Nitrosoglutathione 0-4 erythrocyte membrane protein band 4.2 Mus musculus 110-113 24887420-3 2014 GSNO treatment abrogated growth factor (HB-EGF) induced signal transduction including phosphorylation of Akt, p42/44 and STAT3, which are known to play critical roles in ovarian cancer growth and progression. S-Nitrosoglutathione 0-4 signal transducer and activator of transcription 3 Mus musculus 121-126 24887420-7 2014 GSNO"s nitrosylating ability was reflected in the induced nitrosylation of various known proteins including NFkappaB p65, Akt and EGFR. S-Nitrosoglutathione 0-4 v-rel reticuloendotheliosis viral oncogene homolog A (avian) Mus musculus 117-120 24887420-7 2014 GSNO"s nitrosylating ability was reflected in the induced nitrosylation of various known proteins including NFkappaB p65, Akt and EGFR. S-Nitrosoglutathione 0-4 thymoma viral proto-oncogene 1 Mus musculus 122-125 24887420-7 2014 GSNO"s nitrosylating ability was reflected in the induced nitrosylation of various known proteins including NFkappaB p65, Akt and EGFR. S-Nitrosoglutathione 0-4 epidermal growth factor receptor Mus musculus 130-134 24887420-8 2014 As a novel finding, we observed that GSNO also induced nitrosylation with inverse relationship at tyrosine 705 phosphorylation of STAT3, an established player in chemoresistance and cell proliferation in ovarian cancer and in cancer in general. S-Nitrosoglutathione 37-41 signal transducer and activator of transcription 3 Mus musculus 130-135 24063605-9 2014 The replacement of Cys(259) residue with Ala abolished the inhibitory role of GSNO in IL-6-induced STAT3 phosphorylation and transactivation, suggesting the role of Cys(259) S-nitrosylation in STAT3 phosphorylation. S-Nitrosoglutathione 78-82 interleukin 6 Homo sapiens 86-90 24063605-4 2014 STAT3 S-nitrosylation was associated with inducible nitric oxide synthase (iNOS)-produced nitric oxide (NO) and S-nitrosoglutathione (GSNO), whereas S-glutathionylation of STAT3 was associated with cellular oxidative stress. S-Nitrosoglutathione 112-132 signal transducer and activator of transcription 3 Homo sapiens 0-5 24063605-9 2014 The replacement of Cys(259) residue with Ala abolished the inhibitory role of GSNO in IL-6-induced STAT3 phosphorylation and transactivation, suggesting the role of Cys(259) S-nitrosylation in STAT3 phosphorylation. S-Nitrosoglutathione 78-82 signal transducer and activator of transcription 3 Homo sapiens 99-104 24063605-4 2014 STAT3 S-nitrosylation was associated with inducible nitric oxide synthase (iNOS)-produced nitric oxide (NO) and S-nitrosoglutathione (GSNO), whereas S-glutathionylation of STAT3 was associated with cellular oxidative stress. S-Nitrosoglutathione 134-138 signal transducer and activator of transcription 3 Homo sapiens 0-5 24063605-9 2014 The replacement of Cys(259) residue with Ala abolished the inhibitory role of GSNO in IL-6-induced STAT3 phosphorylation and transactivation, suggesting the role of Cys(259) S-nitrosylation in STAT3 phosphorylation. S-Nitrosoglutathione 78-82 signal transducer and activator of transcription 3 Homo sapiens 193-198 24063605-4 2014 STAT3 S-nitrosylation was associated with inducible nitric oxide synthase (iNOS)-produced nitric oxide (NO) and S-nitrosoglutathione (GSNO), whereas S-glutathionylation of STAT3 was associated with cellular oxidative stress. S-Nitrosoglutathione 134-138 nitric oxide synthase 2 Homo sapiens 75-79 24462770-6 2014 Recombinant (re) PON1 was trans-S-nitrosylated by several NO donors, glutathione-NO (GSNO) was found to be the most effective. S-Nitrosoglutathione 85-89 paraoxonase 1 Homo sapiens 17-21 24063605-5 2014 NO produced by iNOS or treatment of microglia with exogenous GSNO inhibited STAT3 activation via inhibiting STAT3 phosphorylation (Tyr(705)). S-Nitrosoglutathione 61-65 signal transducer and activator of transcription 3 Homo sapiens 76-81 24063605-5 2014 NO produced by iNOS or treatment of microglia with exogenous GSNO inhibited STAT3 activation via inhibiting STAT3 phosphorylation (Tyr(705)). S-Nitrosoglutathione 61-65 signal transducer and activator of transcription 3 Homo sapiens 108-113 24063605-7 2014 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 Janus kinase 2 Homo sapiens 41-45 24063605-7 2014 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Homo sapiens 50-55 24063605-7 2014 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Homo sapiens 57-62 24063605-7 2014 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Homo sapiens 57-62 24063605-7 2014 In cell-free kinase assay using purified JAK2 and STAT3, STAT3 phosphorylation was inhibited by its selective preincubation with GSNO, but not by preincubation of JAK2 with GSNO, indicating that GSNO-mediated mechanisms inhibit STAT3 phosphorylation through S-nitrosylation of STAT3 rather than JAK2. S-Nitrosoglutathione 129-133 signal transducer and activator of transcription 3 Homo sapiens 57-62 24063605-8 2014 In this study, we identified that Cys(259) was the target Cys residue of GSNO-mediated S-nitrosylation of STAT3. S-Nitrosoglutathione 73-77 signal transducer and activator of transcription 3 Homo sapiens 106-111 24523418-4 2014 METHODS AND RESULTS: We demonstrated that systemic administration of endogenous nitric oxide donor S-nitrosoglutathione in mice blocked the reduction of extracellular superoxide dismutase (EcSOD) protein expression, as well as the induction of MAFbx/Atrogin-1 mRNA expression and muscle atrophy induced by glucocorticoid. S-Nitrosoglutathione 99-119 superoxide dismutase 3, extracellular Mus musculus 153-187 24523418-4 2014 METHODS AND RESULTS: We demonstrated that systemic administration of endogenous nitric oxide donor S-nitrosoglutathione in mice blocked the reduction of extracellular superoxide dismutase (EcSOD) protein expression, as well as the induction of MAFbx/Atrogin-1 mRNA expression and muscle atrophy induced by glucocorticoid. S-Nitrosoglutathione 99-119 superoxide dismutase 3, extracellular Mus musculus 189-194 24523418-4 2014 METHODS AND RESULTS: We demonstrated that systemic administration of endogenous nitric oxide donor S-nitrosoglutathione in mice blocked the reduction of extracellular superoxide dismutase (EcSOD) protein expression, as well as the induction of MAFbx/Atrogin-1 mRNA expression and muscle atrophy induced by glucocorticoid. S-Nitrosoglutathione 99-119 F-box protein 32 Mus musculus 244-249 24523418-4 2014 METHODS AND RESULTS: We demonstrated that systemic administration of endogenous nitric oxide donor S-nitrosoglutathione in mice blocked the reduction of extracellular superoxide dismutase (EcSOD) protein expression, as well as the induction of MAFbx/Atrogin-1 mRNA expression and muscle atrophy induced by glucocorticoid. S-Nitrosoglutathione 99-119 F-box protein 32 Mus musculus 250-259 24487118-8 2014 Additionally, we found that treatment with the cardioprotective S-nitrosylating agent S-nitrosoglutathione (GSNO), was able to preserve TRIM72(WT) protein levels and enhance TRIM72(WT)-mediated cell survival, but had no effect on TRIM72(C144S) levels. S-Nitrosoglutathione 86-106 tripartite motif containing 72 Homo sapiens 136-142 24487118-8 2014 Additionally, we found that treatment with the cardioprotective S-nitrosylating agent S-nitrosoglutathione (GSNO), was able to preserve TRIM72(WT) protein levels and enhance TRIM72(WT)-mediated cell survival, but had no effect on TRIM72(C144S) levels. S-Nitrosoglutathione 86-106 tripartite motif containing 72 Homo sapiens 174-180 24487118-8 2014 Additionally, we found that treatment with the cardioprotective S-nitrosylating agent S-nitrosoglutathione (GSNO), was able to preserve TRIM72(WT) protein levels and enhance TRIM72(WT)-mediated cell survival, but had no effect on TRIM72(C144S) levels. S-Nitrosoglutathione 86-106 tripartite motif containing 72 Homo sapiens 174-180 24699383-0 2014 S-nitrosoglutathione inhibits inducible nitric oxide synthase upregulation by redox posttranslational modification in experimental diabetic retinopathy. S-Nitrosoglutathione 0-20 nitric oxide synthase 2 Homo sapiens 30-61 24699383-5 2014 RESULTS: In animals with DM, GSNO decreased inducible nitric oxide synthase (iNOS) expression and prevented tyrosine nitration formation, ameliorating glial dysfunction measured with glial fibrillary acidic protein, resulting in improved retinal function. S-Nitrosoglutathione 29-33 nitric oxide synthase 2 Homo sapiens 44-75 24699383-5 2014 RESULTS: In animals with DM, GSNO decreased inducible nitric oxide synthase (iNOS) expression and prevented tyrosine nitration formation, ameliorating glial dysfunction measured with glial fibrillary acidic protein, resulting in improved retinal function. S-Nitrosoglutathione 29-33 nitric oxide synthase 2 Homo sapiens 77-81 24699383-8 2014 In vitro study showed that treatment with GSNO under high glucose condition counteracted nitrosative stress due to iNOS downregulation by S-glutathionylation, and not by prevention of decreased GSNO and reduced glutathione levels. S-Nitrosoglutathione 42-46 nitric oxide synthase 2 Homo sapiens 115-119 24699383-11 2014 CONCLUSIONS: In this study, a new therapeutic modality (GSNO eye drop) targeting nitrosative stress by redox posttranslational modification of iNOS was efficient against early damage in the retina due to experimental DR. S-Nitrosoglutathione 56-60 nitric oxide synthase 2 Homo sapiens 143-147 24487118-8 2014 Additionally, we found that treatment with the cardioprotective S-nitrosylating agent S-nitrosoglutathione (GSNO), was able to preserve TRIM72(WT) protein levels and enhance TRIM72(WT)-mediated cell survival, but had no effect on TRIM72(C144S) levels. S-Nitrosoglutathione 108-112 tripartite motif containing 72 Homo sapiens 136-142 24487118-8 2014 Additionally, we found that treatment with the cardioprotective S-nitrosylating agent S-nitrosoglutathione (GSNO), was able to preserve TRIM72(WT) protein levels and enhance TRIM72(WT)-mediated cell survival, but had no effect on TRIM72(C144S) levels. S-Nitrosoglutathione 108-112 tripartite motif containing 72 Homo sapiens 174-180 24487118-8 2014 Additionally, we found that treatment with the cardioprotective S-nitrosylating agent S-nitrosoglutathione (GSNO), was able to preserve TRIM72(WT) protein levels and enhance TRIM72(WT)-mediated cell survival, but had no effect on TRIM72(C144S) levels. S-Nitrosoglutathione 108-112 tripartite motif containing 72 Homo sapiens 174-180 24487118-9 2014 Consistent with our hypothesis, GSNO was also found to increase SNO levels and inhibit H2O2-induced irreversible oxidation for TRIM72(WT) without affecting TRIM72(C144S). S-Nitrosoglutathione 32-36 tripartite motif containing 72 Homo sapiens 127-133 24487118-10 2014 In further support of our hypothesis, GSNO blocked the ischemia/reperfusion-induced decrease in TRIM72 levels and reduced infarct size in a Langendorff-perfused heart model. S-Nitrosoglutathione 38-42 tripartite motif containing 72 Homo sapiens 96-102 24460629-7 2014 RESULTS: We show that platelet aggregation induced by CLEC-2 agonists is resistant to GSNO but inhibited by PGI2 . S-Nitrosoglutathione 86-90 C-type lectin domain family 1, member b Mus musculus 54-60 24586043-9 2014 However, the NO donor S-nitrosoglutathione induced closure of uvr8-1 stomata to the same extent as in the wild type. S-Nitrosoglutathione 22-42 Regulator of chromosome condensation (RCC1) family protein Arabidopsis thaliana 62-66 24462770-11 2014 This is the first report of PON1"s S-nitrosylation via GSNO and HSA-NO. S-Nitrosoglutathione 55-59 paraoxonase 1 Homo sapiens 28-32 24211189-8 2014 In both organisms, preformed GAPDH/CP12/PRK complexes are protected from GSSG or GSNO oxidation, and in Arabidopsis also from H2O2 treatment. S-Nitrosoglutathione 81-85 CP12 domain-containing protein 2 Arabidopsis thaliana 35-39 24405692-2 2014 Decreased levels of GSNO in the lungs of asthmatics have been attributed to increased GSNO catabolism via GSNO reductase (GSNOR) leading to loss of GSNO- and NO- mediated bronchodilatory and anti-inflammatory actions. S-Nitrosoglutathione 20-24 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 106-120 24393850-3 2014 We and others have demonstrated that S-nitrosoglutathione (GSNO) increases the expression, maturation, and function of wild-type and mutant F508del cystic fibrosis transmembrane conductance regulator (CFTR) in human bronchial airway epithelial (HBAE) cells. S-Nitrosoglutathione 37-57 CF transmembrane conductance regulator Homo sapiens 148-199 24393850-3 2014 We and others have demonstrated that S-nitrosoglutathione (GSNO) increases the expression, maturation, and function of wild-type and mutant F508del cystic fibrosis transmembrane conductance regulator (CFTR) in human bronchial airway epithelial (HBAE) cells. S-Nitrosoglutathione 37-57 CF transmembrane conductance regulator Homo sapiens 201-205 24393850-3 2014 We and others have demonstrated that S-nitrosoglutathione (GSNO) increases the expression, maturation, and function of wild-type and mutant F508del cystic fibrosis transmembrane conductance regulator (CFTR) in human bronchial airway epithelial (HBAE) cells. S-Nitrosoglutathione 59-63 CF transmembrane conductance regulator Homo sapiens 148-199 24393850-3 2014 We and others have demonstrated that S-nitrosoglutathione (GSNO) increases the expression, maturation, and function of wild-type and mutant F508del cystic fibrosis transmembrane conductance regulator (CFTR) in human bronchial airway epithelial (HBAE) cells. S-Nitrosoglutathione 59-63 CF transmembrane conductance regulator Homo sapiens 201-205 24405692-2 2014 Decreased levels of GSNO in the lungs of asthmatics have been attributed to increased GSNO catabolism via GSNO reductase (GSNOR) leading to loss of GSNO- and NO- mediated bronchodilatory and anti-inflammatory actions. S-Nitrosoglutathione 20-24 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 122-127 24405692-2 2014 Decreased levels of GSNO in the lungs of asthmatics have been attributed to increased GSNO catabolism via GSNO reductase (GSNOR) leading to loss of GSNO- and NO- mediated bronchodilatory and anti-inflammatory actions. S-Nitrosoglutathione 86-90 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 106-120 24405692-2 2014 Decreased levels of GSNO in the lungs of asthmatics have been attributed to increased GSNO catabolism via GSNO reductase (GSNOR) leading to loss of GSNO- and NO- mediated bronchodilatory and anti-inflammatory actions. S-Nitrosoglutathione 86-90 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 122-127 24405692-2 2014 Decreased levels of GSNO in the lungs of asthmatics have been attributed to increased GSNO catabolism via GSNO reductase (GSNOR) leading to loss of GSNO- and NO- mediated bronchodilatory and anti-inflammatory actions. S-Nitrosoglutathione 86-90 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 106-120 24405692-2 2014 Decreased levels of GSNO in the lungs of asthmatics have been attributed to increased GSNO catabolism via GSNO reductase (GSNOR) leading to loss of GSNO- and NO- mediated bronchodilatory and anti-inflammatory actions. S-Nitrosoglutathione 86-90 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 122-127 24405692-14 2014 CONCLUSIONS: The significant bronchodilatory and anti-inflammatory actions of N6022 in the airways are consistent with restoration of GSNO levels through GSNOR inhibition. S-Nitrosoglutathione 134-138 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 154-159 24239886-2 2013 Pharmacological inhibition of GSNOR is being actively pursued as a therapeutic approach to increase S-nitrosoglutathione levels for the treatment of asthma and cystic fibrosis. S-Nitrosoglutathione 100-120 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 30-35 23723008-5 2014 Activators of PKG (GSNO or cGMP) decreased MLC20 phosphorylation and contraction in response to 10 muM Ca(2+), implying existence of inhibitory mechanism independent of Ca(2+) and RhoA. S-Nitrosoglutathione 19-23 protein kinase cGMP-dependent 1 Homo sapiens 14-17 23723008-5 2014 Activators of PKG (GSNO or cGMP) decreased MLC20 phosphorylation and contraction in response to 10 muM Ca(2+), implying existence of inhibitory mechanism independent of Ca(2+) and RhoA. S-Nitrosoglutathione 19-23 myosin light chain 12B Homo sapiens 43-48 23723008-5 2014 Activators of PKG (GSNO or cGMP) decreased MLC20 phosphorylation and contraction in response to 10 muM Ca(2+), implying existence of inhibitory mechanism independent of Ca(2+) and RhoA. S-Nitrosoglutathione 19-23 ras homolog family member A Homo sapiens 180-184 23723008-7 2014 Both GSNO and 8-pCPT-cGMP induced phosphorylation of M-RIP; phosphorylation was accompanied by an increase in the association of M-RIP with MYPT1 and MLCP activity. S-Nitrosoglutathione 5-9 myosin phosphatase Rho interacting protein Homo sapiens 53-58 23723008-7 2014 Both GSNO and 8-pCPT-cGMP induced phosphorylation of M-RIP; phosphorylation was accompanied by an increase in the association of M-RIP with MYPT1 and MLCP activity. S-Nitrosoglutathione 5-9 myosin phosphatase Rho interacting protein Homo sapiens 129-134 23723008-7 2014 Both GSNO and 8-pCPT-cGMP induced phosphorylation of M-RIP; phosphorylation was accompanied by an increase in the association of M-RIP with MYPT1 and MLCP activity. S-Nitrosoglutathione 5-9 protein phosphatase 1 regulatory subunit 12A Homo sapiens 140-145 23979125-4 2014 The objectives of this study were to investigate effects of the Maillard reaction on the interaction of methemoglobin (metHb) with S-nitrosoglutathione (GSNO) and nitrite. S-Nitrosoglutathione 131-151 hemoglobin subunit gamma 2 Homo sapiens 104-117 23979125-4 2014 The objectives of this study were to investigate effects of the Maillard reaction on the interaction of methemoglobin (metHb) with S-nitrosoglutathione (GSNO) and nitrite. S-Nitrosoglutathione 153-157 hemoglobin subunit gamma 2 Homo sapiens 104-117 23963842-5 2013 These changes of spark frequency could be mimicked by exposure to the NO donor GSNO and were sensitive to the CaMKII inhibitors KN-93 and AIP. S-Nitrosoglutathione 79-83 calcium/calmodulin dependent protein kinase II gamma Homo sapiens 110-116 23963842-5 2013 These changes of spark frequency could be mimicked by exposure to the NO donor GSNO and were sensitive to the CaMKII inhibitors KN-93 and AIP. S-Nitrosoglutathione 79-83 aryl hydrocarbon receptor interacting protein Homo sapiens 128-141 23963842-6 2013 In vitro, CaMKII became nitrosated and its activity remained increased independent of Ca(2+) in the presence of GSNO, as assessed with biochemical assays. S-Nitrosoglutathione 112-116 calcium/calmodulin dependent protein kinase II gamma Homo sapiens 10-16 24204370-1 2013 S-nitrosoglutathione reductase (GSNOR) is believed to modulate effects of reactive oxygen and nitrogen species through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 0-20 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 32-37 23820266-0 2013 gamma-Glutamyltransferase catabolism of S-nitrosoglutathione modulates IL-8 expression in cystic fibrosis bronchial epithelial cells. S-Nitrosoglutathione 40-60 gamma-glutamyltransferase light chain family member 3 Homo sapiens 0-25 23820266-0 2013 gamma-Glutamyltransferase catabolism of S-nitrosoglutathione modulates IL-8 expression in cystic fibrosis bronchial epithelial cells. S-Nitrosoglutathione 40-60 C-X-C motif chemokine ligand 8 Homo sapiens 71-75 23820266-2 2013 A role for GSNO has been envisaged in the expression of inflammatory cytokines such as IL-8; however, conflicting results have been reported. S-Nitrosoglutathione 11-15 C-X-C motif chemokine ligand 8 Homo sapiens 87-91 23820266-3 2013 gamma-Glutamyltransferase (GGT) enzyme activity can hydrolyze the gamma-glutamyl bond present in the GSNO molecule thus greatly accelerating the release of bioactive nitric oxide. S-Nitrosoglutathione 101-105 gamma-glutamyltransferase light chain family member 3 Homo sapiens 0-25 23820266-3 2013 gamma-Glutamyltransferase (GGT) enzyme activity can hydrolyze the gamma-glutamyl bond present in the GSNO molecule thus greatly accelerating the release of bioactive nitric oxide. S-Nitrosoglutathione 101-105 gamma-glutamyltransferase light chain family member 3 Homo sapiens 27-30 23820266-5 2013 This study was aimed at evaluating the effect of GSNO catabolism mediated by GGT on production of IL-8 in CF transmembrane regulation protein-mutated IB3-1 bronchial cells. S-Nitrosoglutathione 49-53 gamma-glutamyltransferase light chain family member 3 Homo sapiens 77-80 23820266-5 2013 This study was aimed at evaluating the effect of GSNO catabolism mediated by GGT on production of IL-8 in CF transmembrane regulation protein-mutated IB3-1 bronchial cells. S-Nitrosoglutathione 49-53 C-X-C motif chemokine ligand 8 Homo sapiens 98-102 23820266-6 2013 The rapid, GGT-catalyzed catabolism of GSNO caused a decrease in both basal and lipopolysaccharide-stimulated IL-8 production in IB3-1 cells, by modulating both NF-kappaB and ERK1/2 pathways, along with a decrease in cell proliferation. S-Nitrosoglutathione 39-43 C-X-C motif chemokine ligand 8 Homo sapiens 110-114 23820266-6 2013 The rapid, GGT-catalyzed catabolism of GSNO caused a decrease in both basal and lipopolysaccharide-stimulated IL-8 production in IB3-1 cells, by modulating both NF-kappaB and ERK1/2 pathways, along with a decrease in cell proliferation. S-Nitrosoglutathione 39-43 mitogen-activated protein kinase 3 Homo sapiens 175-181 23820266-7 2013 In contrast, a slow decomposition of GSNO produced a significant increase in both cell proliferation and expression of IL-8, the latter possibly through p38-mediated stabilization of IL-8 mRNA. S-Nitrosoglutathione 37-41 C-X-C motif chemokine ligand 8 Homo sapiens 119-123 23820266-7 2013 In contrast, a slow decomposition of GSNO produced a significant increase in both cell proliferation and expression of IL-8, the latter possibly through p38-mediated stabilization of IL-8 mRNA. S-Nitrosoglutathione 37-41 mitogen-activated protein kinase 1 Homo sapiens 153-156 23820266-7 2013 In contrast, a slow decomposition of GSNO produced a significant increase in both cell proliferation and expression of IL-8, the latter possibly through p38-mediated stabilization of IL-8 mRNA. S-Nitrosoglutathione 37-41 C-X-C motif chemokine ligand 8 Homo sapiens 183-187 23820266-8 2013 Our data suggest that the differential GSNO catabolism mediated by GGT enzyme activity can downregulate the production of IL-8 in CF cells. S-Nitrosoglutathione 39-43 gamma-glutamyltransferase light chain family member 3 Homo sapiens 67-70 23820266-8 2013 Our data suggest that the differential GSNO catabolism mediated by GGT enzyme activity can downregulate the production of IL-8 in CF cells. S-Nitrosoglutathione 39-43 C-X-C motif chemokine ligand 8 Homo sapiens 122-126 23820266-9 2013 Hence, the role of GGT activity should be considered when evaluating GSNO for both in vitro and in vivo studies, the more so in the case of GSNO-based therapies for cystic fibrosis. S-Nitrosoglutathione 69-73 gamma-glutamyltransferase light chain family member 3 Homo sapiens 19-22 24204370-1 2013 S-nitrosoglutathione reductase (GSNOR) is believed to modulate effects of reactive oxygen and nitrogen species through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 32-36 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-30 23888047-7 2013 In contrast to the deglutathionylation activity, we also found that GSTO1-1 is associated with the rapid glutathionylation of cellular proteins when the cells are exposed to S-nitrosoglutathione. S-Nitrosoglutathione 174-194 glutathione S-transferase omega 1 Homo sapiens 68-75 23788476-10 2013 Topical GSNO treatment was also efficient at suppressing lesion growth in IFN-gamma-KO mice infected with L. braziliensis. S-Nitrosoglutathione 8-12 interferon gamma Mus musculus 74-83 23813099-7 2013 Expression of wild-type CaV3.2 channels or a quadruple Cys-Ala mutant in human embryonic kidney cells revealed that Cys residues in repeats I and II on the extracellular face of the channel were required for channel inhibition by GSNO. S-Nitrosoglutathione 230-234 calcium voltage-gated channel subunit alpha1 H Homo sapiens 24-30 23792322-2 2013 In the present study, we aimed to investigate the effects of GSNO pre-treatment on the S-nitrosylation of Fas and subsequent events in the Fas pathway, and reveal the correlation between Fas S-nitrosylation and nNOS activation in the rat hippocampal CA1 region after global cerebral ischemia. S-Nitrosoglutathione 61-65 carbonic anhydrase 1 Rattus norvegicus 250-253 23792322-3 2013 The results showed that GSNO pre-treatment not only facilitated the survival of hippocampal CA1 pyramidal neurons, but also abolished the activation of pro-apoptotic Caspase-8, Bid, Caspase-9 and Caspase-3. S-Nitrosoglutathione 24-28 carbonic anhydrase 1 Rattus norvegicus 92-95 23792322-3 2013 The results showed that GSNO pre-treatment not only facilitated the survival of hippocampal CA1 pyramidal neurons, but also abolished the activation of pro-apoptotic Caspase-8, Bid, Caspase-9 and Caspase-3. S-Nitrosoglutathione 24-28 caspase 8 Rattus norvegicus 166-175 23792322-3 2013 The results showed that GSNO pre-treatment not only facilitated the survival of hippocampal CA1 pyramidal neurons, but also abolished the activation of pro-apoptotic Caspase-8, Bid, Caspase-9 and Caspase-3. S-Nitrosoglutathione 24-28 BH3 interacting domain death agonist Rattus norvegicus 177-180 23792322-3 2013 The results showed that GSNO pre-treatment not only facilitated the survival of hippocampal CA1 pyramidal neurons, but also abolished the activation of pro-apoptotic Caspase-8, Bid, Caspase-9 and Caspase-3. S-Nitrosoglutathione 24-28 caspase 9 Rattus norvegicus 182-191 23792322-3 2013 The results showed that GSNO pre-treatment not only facilitated the survival of hippocampal CA1 pyramidal neurons, but also abolished the activation of pro-apoptotic Caspase-8, Bid, Caspase-9 and Caspase-3. S-Nitrosoglutathione 24-28 caspase 3 Rattus norvegicus 196-205 23792322-5 2013 Global cerebral ischemia/reperfusion promoted the binding between neuronal nitric oxide synthase (nNOS) and postsynaptic density protein 95 that has been reported to activate nNOS, and GSNO inhibited the post-ischemic nNOS activation and NO release. S-Nitrosoglutathione 185-189 nitric oxide synthase 1 Rattus norvegicus 98-102 23792322-8 2013 These results indicate that GSNO-induced nNOS inactivation associates with the down-regulation of Fas S-nitrosylation and consequent Fas signal cascade, which is responsible for the GSNO-mediated neuronal survival after brain ischemia. S-Nitrosoglutathione 28-32 nitric oxide synthase 1 Rattus norvegicus 41-45 23792322-8 2013 These results indicate that GSNO-induced nNOS inactivation associates with the down-regulation of Fas S-nitrosylation and consequent Fas signal cascade, which is responsible for the GSNO-mediated neuronal survival after brain ischemia. S-Nitrosoglutathione 182-186 nitric oxide synthase 1 Rattus norvegicus 41-45 23846260-6 2013 H2S-induced GSNO decomposition was slowed by the presence of other thiols, such as L-cysteine (Cys), N-acetyl-L-cysteine (NAC) and L-glutathione (GSH), but not in the presence of L-methionine (Met) or oxidized glutathione (GSSG). S-Nitrosoglutathione 12-16 X-linked Kx blood group Homo sapiens 122-125 23846260-7 2013 In sharp contrast, at pH 6.0, H2S-induced GSNO decomposition was negligible, yet the presence of Cys, NAC and GSH induced the H2S-driven GSNO decomposition (whilst Met and GSSG were inactive). S-Nitrosoglutathione 137-141 X-linked Kx blood group Homo sapiens 102-105 23998610-4 2013 The changes of CD42b and CD62P in fresh liquid platelet group, frozen platelet group and frozen platelets with GSNO were significant different. S-Nitrosoglutathione 111-115 glycoprotein Ib platelet subunit alpha Homo sapiens 15-20 23764893-6 2013 The NO donor S-nitrosoglutathione (GSNO) caused an increase in PDE5 activity and intra- and extracellular cGMP levels in both fundus and antrum. S-Nitrosoglutathione 13-33 phosphodiesterase 5A Homo sapiens 63-67 23764893-6 2013 The NO donor S-nitrosoglutathione (GSNO) caused an increase in PDE5 activity and intra- and extracellular cGMP levels in both fundus and antrum. S-Nitrosoglutathione 35-39 phosphodiesterase 5A Homo sapiens 63-67 23764893-8 2013 GSNO-induced increase in extracellular cGMP was blocked in dispersed cells by the cyclic nucleotide export blocker probenecid and in cultured muscle cells by depletion of ATP or suppression of MRP5 by siRNA, providing evidence that cGMP efflux was mediated by ATP-dependent export via MRP5. S-Nitrosoglutathione 0-4 ATP binding cassette subfamily C member 5 Homo sapiens 193-197 23764893-8 2013 GSNO-induced increase in extracellular cGMP was blocked in dispersed cells by the cyclic nucleotide export blocker probenecid and in cultured muscle cells by depletion of ATP or suppression of MRP5 by siRNA, providing evidence that cGMP efflux was mediated by ATP-dependent export via MRP5. S-Nitrosoglutathione 0-4 ATP binding cassette subfamily C member 5 Homo sapiens 285-289 23764893-9 2013 Consistent with the higher expression and activity levels of PDE5 and MRP5, GSNO-induced PKG activity and muscle relaxation were significantly lower in muscle cells from fundus compared with antrum. S-Nitrosoglutathione 76-80 phosphodiesterase 5A Homo sapiens 61-65 23764893-9 2013 Consistent with the higher expression and activity levels of PDE5 and MRP5, GSNO-induced PKG activity and muscle relaxation were significantly lower in muscle cells from fundus compared with antrum. S-Nitrosoglutathione 76-80 ATP binding cassette subfamily C member 5 Homo sapiens 70-74 23764893-9 2013 Consistent with the higher expression and activity levels of PDE5 and MRP5, GSNO-induced PKG activity and muscle relaxation were significantly lower in muscle cells from fundus compared with antrum. S-Nitrosoglutathione 76-80 protein kinase cGMP-dependent 1 Homo sapiens 89-92 23749990-10 2013 GSH-dependent denitrosylation of GAPC1 was found to be linked to the [GSH]/[GSNO] ratio and to be independent of the [GSH]/[GSSG] ratio. S-Nitrosoglutathione 76-80 glyceraldehyde-3-phosphate dehydrogenase C subunit 1 Arabidopsis thaliana 33-38 23998610-4 2013 The changes of CD42b and CD62P in fresh liquid platelet group, frozen platelet group and frozen platelets with GSNO were significant different. S-Nitrosoglutathione 111-115 selectin P Homo sapiens 25-30 23684363-15 2013 Exposure of CECs to propofol attenuated GSNO-induced cell death, apoptosis, and caspase-3 activation (P < .01). S-Nitrosoglutathione 40-44 caspase 3 Mus musculus 80-89 23665321-6 2013 Incubation with NO donors GSNO and DETA/NO in the presence of IL-1beta abolished VSMCs proliferation and increased p21Waf1/Cip1 protein content. S-Nitrosoglutathione 26-30 interleukin 1 beta Homo sapiens 62-70 23840906-10 2013 Further, treatment of epithelial monolayers with GSNO also prevented Cytomix-induced increases in permeability and exhibited a similar improvement in expression and localization of occludin, ZO-1, and P-MLC. S-Nitrosoglutathione 49-53 occludin Homo sapiens 181-189 23840906-10 2013 Further, treatment of epithelial monolayers with GSNO also prevented Cytomix-induced increases in permeability and exhibited a similar improvement in expression and localization of occludin, ZO-1, and P-MLC. S-Nitrosoglutathione 49-53 tight junction protein 1 Homo sapiens 191-195 23665321-6 2013 Incubation with NO donors GSNO and DETA/NO in the presence of IL-1beta abolished VSMCs proliferation and increased p21Waf1/Cip1 protein content. S-Nitrosoglutathione 26-30 cyclin dependent kinase inhibitor 1A Homo sapiens 123-127 23523754-13 2013 It can be concluded that the effect of GSNO on Cl(-) efflux is, at least in part, due to its properties as an NO-donor, and the effect is likely to be mediated by CFTR, not by Ca(2+)-activated Cl(-) channels. S-Nitrosoglutathione 39-43 CF transmembrane conductance regulator Homo sapiens 163-167 23479738-4 2013 We found that, both in a cell-free system and in cells, NO/SNO donors such as S-nitrosocysteine and S-nitrosoglutathione readily induced the S-nitrosylation of Prx1, causing structural and functional alterations. S-Nitrosoglutathione 100-120 strawberry notch homolog 1 Homo sapiens 59-62 23572520-3 2013 We used transient kinetic methods to determine a minimal mechanism for spontaneous S-nitrosoglutathione (GSNO)-mediated transnitrosation of human glutathione transferase (GST) P1-1, a major detoxification enzyme and key regulator of cell proliferation. S-Nitrosoglutathione 83-103 glutathione S-transferase pi 1 Homo sapiens 146-180 23572520-3 2013 We used transient kinetic methods to determine a minimal mechanism for spontaneous S-nitrosoglutathione (GSNO)-mediated transnitrosation of human glutathione transferase (GST) P1-1, a major detoxification enzyme and key regulator of cell proliferation. S-Nitrosoglutathione 105-109 glutathione S-transferase pi 1 Homo sapiens 146-180 23572520-6 2013 Despite the presence of a GSNO binding site at the active site of GSTP1-1, isothermal titration calorimetry as well as nitrosation experiments using S-nitrosocysteine demonstrate that GSNO binding does not precede S-nitrosation of GSTP1-1. S-Nitrosoglutathione 26-30 glutathione S-transferase pi 1 Homo sapiens 66-73 23479738-4 2013 We found that, both in a cell-free system and in cells, NO/SNO donors such as S-nitrosocysteine and S-nitrosoglutathione readily induced the S-nitrosylation of Prx1, causing structural and functional alterations. S-Nitrosoglutathione 100-120 peroxiredoxin 1 Homo sapiens 160-164 22639878-7 2013 The exogenous NO donor sodium nitroprusside, S-nitrosoglutathione, 7-nitroindazole, the inhibitor of the neuronal nitric oxide synthase, inhibited the activation of p38 signal pathway induced by cerebral ischaemia/reperfusion and attenuated the damage in rat hippocampal neurones. S-Nitrosoglutathione 45-65 mitogen-activated protein kinase 14 Homo sapiens 165-168 22998676-9 2013 Furthermore, the incidences of GSNO- and VP-16-induced skin melanomas were also observed to be lower in the skin-specific top2beta-knockout mice. S-Nitrosoglutathione 31-35 topoisomerase (DNA) II beta Mus musculus 122-130 23277143-5 2013 S-nitrosylation reactivity profiling was performed by quantitatively comparing the site-specific SNO modification levels in samples treated with S-nitrosoglutathione, an NO donor, at two different concentrations (i.e., 10 and 100 muM). S-Nitrosoglutathione 145-165 latexin Homo sapiens 230-233 22998676-4 2013 RESULTS: Similar to the TOP2-targeting drug, etoposide (VP-16), the NO-donor, S-nitrosoglutathione (GSNO), induces skin melanomas formation in 7,12-dimethyl- benz[a]anthracene (DMBA)-initiated mice. S-Nitrosoglutathione 78-98 host cell factor C1 Homo sapiens 56-61 22998676-4 2013 RESULTS: Similar to the TOP2-targeting drug, etoposide (VP-16), the NO-donor, S-nitrosoglutathione (GSNO), induces skin melanomas formation in 7,12-dimethyl- benz[a]anthracene (DMBA)-initiated mice. S-Nitrosoglutathione 100-104 host cell factor C1 Homo sapiens 56-61 23298187-4 2013 In Raw264.7 cells treated with MNSFbeta small interfering RNA (siRNA), LPS/IFNgamma- or NO donor S-nitrosoglutathione-induced apoptosis was inhibited. S-Nitrosoglutathione 97-117 Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed (fox derived) Mus musculus 31-39 23246566-7 2013 GSNO treatment of NRK cells led to mitochondrial membrane depolarization and significant reduction in activities of mitochondrial complex IV and manganese superoxide dismutase enzyme (MnSOD). S-Nitrosoglutathione 0-4 superoxide dismutase 2 Rattus norvegicus 145-182 23246566-7 2013 GSNO treatment of NRK cells led to mitochondrial membrane depolarization and significant reduction in activities of mitochondrial complex IV and manganese superoxide dismutase enzyme (MnSOD). S-Nitrosoglutathione 0-4 superoxide dismutase 2 Rattus norvegicus 184-189 23246566-11 2013 Endogenous GSH is an essential mediator in S-glutathionylation of cellular proteins, and the current studies revealed that GSH is required for MnSOD inactivation after GSNO or diamide treatment in rat kidney cells as well as in isolated kidneys. S-Nitrosoglutathione 168-172 superoxide dismutase 2 Rattus norvegicus 143-148 23246566-12 2013 Further studies showed that GSNO led to glutathionylation of MnSOD; however, glutathionylated recombinant MnSOD was not inactivated. S-Nitrosoglutathione 28-32 superoxide dismutase 2 Rattus norvegicus 61-66 23246566-13 2013 This suggests that a more complex pathway, possibly involving the participation of multiple proteins, leads to MnSOD inactivation after GSNO treatment. S-Nitrosoglutathione 136-140 superoxide dismutase 2 Rattus norvegicus 111-116 23246566-14 2013 The major highlight of these studies is the fact that dithiothreitol can restore MnSOD activity after GSNO treatment. S-Nitrosoglutathione 102-106 superoxide dismutase 2 Rattus norvegicus 81-86 23201478-5 2013 Under optimal growth conditions, GSNOR(OE) had the lowest SNO and NO levels and GSNOR(AS) the highest, as expected by the GSNO-consuming activity of GSNOR. S-Nitrosoglutathione 33-37 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 80-85 23201478-5 2013 Under optimal growth conditions, GSNOR(OE) had the lowest SNO and NO levels and GSNOR(AS) the highest, as expected by the GSNO-consuming activity of GSNOR. S-Nitrosoglutathione 33-37 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 80-85 23298187-8 2013 Co-over-expression of MNSFbeta and Bcl-G reduced S-nitrosoglutathione-induced ERK1/2 phosphorylation. S-Nitrosoglutathione 49-69 Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed (fox derived) Mus musculus 22-30 23298187-8 2013 Co-over-expression of MNSFbeta and Bcl-G reduced S-nitrosoglutathione-induced ERK1/2 phosphorylation. S-Nitrosoglutathione 49-69 BCL2-like 14 (apoptosis facilitator) Mus musculus 35-40 23298187-8 2013 Co-over-expression of MNSFbeta and Bcl-G reduced S-nitrosoglutathione-induced ERK1/2 phosphorylation. S-Nitrosoglutathione 49-69 mitogen-activated protein kinase 3 Mus musculus 78-84 23224322-4 2013 NO donor S-nitrosoglutathione antagonized CRP-mediated reduction of protein S-nitrosylation. S-Nitrosoglutathione 9-29 C-reactive protein Homo sapiens 42-45 23314241-4 2013 For the in vitro studies, Akt1/PKBalpha was S-nitrosylated with S-nitrosoglutathione and derivatized by three methods. S-Nitrosoglutathione 76-96 AKT serine/threonine kinase 1 Rattus norvegicus 26-30 23314241-4 2013 For the in vitro studies, Akt1/PKBalpha was S-nitrosylated with S-nitrosoglutathione and derivatized by three methods. S-Nitrosoglutathione 76-96 AKT serine/threonine kinase 1 Rattus norvegicus 31-39 23111882-12 2013 Despite this change, GSNO was effective in inhibition of P-selectin expression, platelet aggregation, protein carbonylation and apoptosis. S-Nitrosoglutathione 21-25 selectin P Homo sapiens 57-67 23111882-13 2013 The results suggest that L-arginine and GSNO-mediated NO leads to the inhibition of key apoptotic processes including caspase-3 activation, PS exposure and low mitochondrial membrane potential in washed platelets. S-Nitrosoglutathione 40-44 caspase 3 Homo sapiens 118-127 23295225-0 2013 S-nitrosoglutathione covalently modifies cysteine residues of human carbonyl reductase 1 and affects its activity. S-Nitrosoglutathione 0-20 carbonyl reductase 1 Homo sapiens 68-88 23295225-4 2013 GSNO has also been shown to covalently modify and inhibit CBR1. S-Nitrosoglutathione 0-4 carbonyl reductase 1 Homo sapiens 58-62 23295225-11 2013 GSNO treatment of CBR1 resulted in a 2-5-fold decrease in kcat with menadione, 4-benzoylpyridine, 2,3-hexanedione, daunorubicin and 1,4-naphthoquinone. S-Nitrosoglutathione 0-4 carbonyl reductase 1 Homo sapiens 18-22 23295225-14 2013 The findings indicate that GSNO-induced covalent modification of cysteine residues affects the kinetic mechanism of CBR1 both in terms of substrate binding and turnover rate, probably by covalent modification of Cys-226 and/or Cys-227. S-Nitrosoglutathione 27-31 carbonyl reductase 1 Homo sapiens 116-120 23295225-7 2013 The analysis confirmed GSNO concentration-dependent S-glutathionylation of cysteines at positions 122, 150, 226, 227 which was 2-700 times higher compared to wild-type CBR1 (WT-CBR1). S-Nitrosoglutathione 23-27 carbonyl reductase 1 Homo sapiens 168-172 23295225-7 2013 The analysis confirmed GSNO concentration-dependent S-glutathionylation of cysteines at positions 122, 150, 226, 227 which was 2-700 times higher compared to wild-type CBR1 (WT-CBR1). S-Nitrosoglutathione 23-27 carbonyl reductase 1 Homo sapiens 177-181 23264628-0 2013 S-nitrosoglutathione induces ciliary neurotrophic factor expression in astrocytes, which has implications to protect the central nervous system under pathological conditions. S-Nitrosoglutathione 0-20 ciliary neurotrophic factor Homo sapiens 29-56 23264628-5 2013 The enhanced CNTF expression in GSNO-treated astrocytes was ascribed to NO-mediated sGC/cGMP/PKG signaling. S-Nitrosoglutathione 32-36 ciliary neurotrophic factor Homo sapiens 13-17 23264628-4 2013 GSNO enhanced the expressions of glial fibrillary acidic protein and neurotrophic factors including ciliary neurotrophic factor (CNTF) in astrocytes in a dose-dependent manner. S-Nitrosoglutathione 0-4 ciliary neurotrophic factor Homo sapiens 100-127 23264628-4 2013 GSNO enhanced the expressions of glial fibrillary acidic protein and neurotrophic factors including ciliary neurotrophic factor (CNTF) in astrocytes in a dose-dependent manner. S-Nitrosoglutathione 0-4 ciliary neurotrophic factor Homo sapiens 129-133 23264628-5 2013 The enhanced CNTF expression in GSNO-treated astrocytes was ascribed to NO-mediated sGC/cGMP/PKG signaling. S-Nitrosoglutathione 32-36 sarcoglycan beta Homo sapiens 84-87 23254638-5 2013 GSNO treatment (50 mug/kg/day for 2 months) significantly improved learning and memory performance of BCCAO rats and reduced the Abeta levels and ICAM-1/VCAM-1 expression in the brain. S-Nitrosoglutathione 0-4 amyloid beta precursor protein Rattus norvegicus 129-134 23264628-7 2013 In addition, the chromatin accessibility of peroxisome proliferator-activated receptor-gamma accompanied with ATF2 and CREB (cAMP-response element-binding protein) was enhanced across the CNTF gene promoter in GSNO treated astrocytes. S-Nitrosoglutathione 210-214 peroxisome proliferator activated receptor gamma Homo sapiens 44-92 23264628-7 2013 In addition, the chromatin accessibility of peroxisome proliferator-activated receptor-gamma accompanied with ATF2 and CREB (cAMP-response element-binding protein) was enhanced across the CNTF gene promoter in GSNO treated astrocytes. S-Nitrosoglutathione 210-214 activating transcription factor 2 Homo sapiens 110-114 23264628-7 2013 In addition, the chromatin accessibility of peroxisome proliferator-activated receptor-gamma accompanied with ATF2 and CREB (cAMP-response element-binding protein) was enhanced across the CNTF gene promoter in GSNO treated astrocytes. S-Nitrosoglutathione 210-214 cAMP responsive element binding protein 1 Homo sapiens 119-123 23264628-7 2013 In addition, the chromatin accessibility of peroxisome proliferator-activated receptor-gamma accompanied with ATF2 and CREB (cAMP-response element-binding protein) was enhanced across the CNTF gene promoter in GSNO treated astrocytes. S-Nitrosoglutathione 210-214 cAMP responsive element binding protein 1 Homo sapiens 125-162 23264628-7 2013 In addition, the chromatin accessibility of peroxisome proliferator-activated receptor-gamma accompanied with ATF2 and CREB (cAMP-response element-binding protein) was enhanced across the CNTF gene promoter in GSNO treated astrocytes. S-Nitrosoglutathione 210-214 ciliary neurotrophic factor Homo sapiens 188-192 23264628-8 2013 Interestingly, secreted CNTF was responsible for increased expression of glial fibrillary acidic protein in GSNO-treated astrocytes in an autocrine manner via a JAK2- and STAT3-dependent mechanism. S-Nitrosoglutathione 108-112 ciliary neurotrophic factor Homo sapiens 24-28 23264628-8 2013 Interestingly, secreted CNTF was responsible for increased expression of glial fibrillary acidic protein in GSNO-treated astrocytes in an autocrine manner via a JAK2- and STAT3-dependent mechanism. S-Nitrosoglutathione 108-112 Janus kinase 2 Homo sapiens 161-165 23264628-8 2013 Interestingly, secreted CNTF was responsible for increased expression of glial fibrillary acidic protein in GSNO-treated astrocytes in an autocrine manner via a JAK2- and STAT3-dependent mechanism. S-Nitrosoglutathione 108-112 signal transducer and activator of transcription 3 Homo sapiens 171-176 23264628-9 2013 In addition, CNTF secreted by GSNO-treated astrocytes enhanced the differentiation of immature oligodendrocytes in vitro. S-Nitrosoglutathione 30-34 ciliary neurotrophic factor Homo sapiens 13-17 22894707-4 2013 HeLa cells overexpressing H-Ras(wt) containing the spatiotemporal probe green fluorescent protein (GFP) fused to the Ras-binding domain of Raf-1 (GFP-RBD) incubated with 100 muM GSNO stimulated a rapid and transient redistribution of GFP-RBD to the plasma membrane, followed by a delayed and sustained recruitment to the Golgi. S-Nitrosoglutathione 178-182 HRas proto-oncogene, GTPase Homo sapiens 26-31 22894707-4 2013 HeLa cells overexpressing H-Ras(wt) containing the spatiotemporal probe green fluorescent protein (GFP) fused to the Ras-binding domain of Raf-1 (GFP-RBD) incubated with 100 muM GSNO stimulated a rapid and transient redistribution of GFP-RBD to the plasma membrane, followed by a delayed and sustained recruitment to the Golgi. S-Nitrosoglutathione 178-182 Raf-1 proto-oncogene, serine/threonine kinase Homo sapiens 139-144 22894707-6 2013 Inhibition of Src kinase prevented cell proliferation and activation of H-Ras by GSNO at the Golgi. S-Nitrosoglutathione 81-85 HRas proto-oncogene, GTPase Homo sapiens 72-77 23137546-8 2013 The exogenous NO (SNP and GSNO) reversed the effect of endogenous NO by suppressing S-nitrosylation of ASK1 and exerted neuroprotection during ischemia-reperfusion. S-Nitrosoglutathione 26-30 mitogen-activated protein kinase kinase kinase 5 Rattus norvegicus 103-107 23331028-4 2013 We and several research groups have reported that S-nitrosoglutathione (GSNO), a class of endogenous S-nitrosothiols, increases the maturation and function of CFTR in human airway epithelial cells. S-Nitrosoglutathione 50-70 CF transmembrane conductance regulator Homo sapiens 159-163 23331028-4 2013 We and several research groups have reported that S-nitrosoglutathione (GSNO), a class of endogenous S-nitrosothiols, increases the maturation and function of CFTR in human airway epithelial cells. S-Nitrosoglutathione 72-76 CF transmembrane conductance regulator Homo sapiens 159-163 23662713-0 2013 Interaction of S-nitrosoglutathione with methemoglobin under conditions of modeling carbonyl stress. S-Nitrosoglutathione 15-35 hemoglobin subunit gamma 2 Homo sapiens 41-54 23662713-3 2013 Under the above conditions and in the presence of S-nitrosoglutathione (GSNO), metHb nitrosylation took place. S-Nitrosoglutathione 50-70 hemoglobin subunit gamma 2 Homo sapiens 79-84 23662713-3 2013 Under the above conditions and in the presence of S-nitrosoglutathione (GSNO), metHb nitrosylation took place. S-Nitrosoglutathione 72-76 hemoglobin subunit gamma 2 Homo sapiens 79-84 22940110-5 2013 Larval exposure to GSNO resulted in lower activities of aconitase in both sexes and also lower activities of catalase and isocitrate dehydrogenase in adult males relative to the control cohort. S-Nitrosoglutathione 19-23 Mitochondrial aconitase 1 Drosophila melanogaster 56-65 22940110-5 2013 Larval exposure to GSNO resulted in lower activities of aconitase in both sexes and also lower activities of catalase and isocitrate dehydrogenase in adult males relative to the control cohort. S-Nitrosoglutathione 19-23 Catalase Drosophila melanogaster 109-117 22940110-5 2013 Larval exposure to GSNO resulted in lower activities of aconitase in both sexes and also lower activities of catalase and isocitrate dehydrogenase in adult males relative to the control cohort. S-Nitrosoglutathione 19-23 Glycerol-3-phosphate dehydrogenase 1 Drosophila melanogaster 133-146 22940110-6 2013 Larval treatment with GSNO resulted in higher carbonyl protein content and higher activities of glucose-6-phosphate dehydrogenase in males and higher activities of superoxide dismutase and glutathione-S-transferase in both sexes. S-Nitrosoglutathione 22-26 Zwischenferment Drosophila melanogaster 96-129 22940110-6 2013 Larval treatment with GSNO resulted in higher carbonyl protein content and higher activities of glucose-6-phosphate dehydrogenase in males and higher activities of superoxide dismutase and glutathione-S-transferase in both sexes. S-Nitrosoglutathione 22-26 Superoxide dismutase 1 Drosophila melanogaster 164-184 22940110-6 2013 Larval treatment with GSNO resulted in higher carbonyl protein content and higher activities of glucose-6-phosphate dehydrogenase in males and higher activities of superoxide dismutase and glutathione-S-transferase in both sexes. S-Nitrosoglutathione 22-26 Glutathione S transferase E7 Drosophila melanogaster 189-214 22940110-7 2013 Among the parameters tested, aconitase activity and developmental end points may be useful early indicators of toxicity caused by GSNO. S-Nitrosoglutathione 130-134 Mitochondrial aconitase 1 Drosophila melanogaster 29-38 23254638-5 2013 GSNO treatment (50 mug/kg/day for 2 months) significantly improved learning and memory performance of BCCAO rats and reduced the Abeta levels and ICAM-1/VCAM-1 expression in the brain. S-Nitrosoglutathione 0-4 intercellular adhesion molecule 1 Rattus norvegicus 146-152 23254638-5 2013 GSNO treatment (50 mug/kg/day for 2 months) significantly improved learning and memory performance of BCCAO rats and reduced the Abeta levels and ICAM-1/VCAM-1 expression in the brain. S-Nitrosoglutathione 0-4 vascular cell adhesion molecule 1 Rattus norvegicus 153-159 23254638-6 2013 Further, in in vitro cell culture studies, GSNO treatment also decreased the cytokine-induced proinflammatory responses, such as activations of NFkappaB and STAT3 and expression of ICAM-1 and VCAM-1 in endothelial cells. S-Nitrosoglutathione 43-47 signal transducer and activator of transcription 3 Rattus norvegicus 157-162 23254638-6 2013 Further, in in vitro cell culture studies, GSNO treatment also decreased the cytokine-induced proinflammatory responses, such as activations of NFkappaB and STAT3 and expression of ICAM-1 and VCAM-1 in endothelial cells. S-Nitrosoglutathione 43-47 intercellular adhesion molecule 1 Rattus norvegicus 181-187 23254638-6 2013 Further, in in vitro cell culture studies, GSNO treatment also decreased the cytokine-induced proinflammatory responses, such as activations of NFkappaB and STAT3 and expression of ICAM-1 and VCAM-1 in endothelial cells. S-Nitrosoglutathione 43-47 vascular cell adhesion molecule 1 Rattus norvegicus 192-198 23254638-7 2013 In addition, GSNO treatment increased the endothelial and microglial Abeta uptake. S-Nitrosoglutathione 13-17 amyloid beta precursor protein Rattus norvegicus 69-74 23254638-8 2013 Additionally, GSNO treatment inhibited the beta-secretase activity in primary rat neuron cell culture, thus reducing secretion of Abeta, suggesting GSNO mediated mechanisms in anti-inflammatory and anti-amyloidogenic activities. S-Nitrosoglutathione 14-18 amyloid beta precursor protein Rattus norvegicus 130-135 23254638-8 2013 Additionally, GSNO treatment inhibited the beta-secretase activity in primary rat neuron cell culture, thus reducing secretion of Abeta, suggesting GSNO mediated mechanisms in anti-inflammatory and anti-amyloidogenic activities. S-Nitrosoglutathione 148-152 amyloid beta precursor protein Rattus norvegicus 130-135 22796369-5 2012 KEY FINDINGS: In the presence of high concentrations of fibrinogen and ACh (10 muM) in the blood samples from healthy humans the erythrocyte nitrites, nitrates and GSNO concentrations increased without significant changes in NO efflux. S-Nitrosoglutathione 164-168 fibrinogen beta chain Homo sapiens 56-66 23033481-9 2012 Indeed, we found that mutation of both Cys-40 and Cys-346 (Panx1(C40A/C346A)) prevented Panx1 S-nitrosylation by GSNO as well as the GSNO-mediated inhibition of Panx1 current and ATP release. S-Nitrosoglutathione 113-117 pannexin 1 Homo sapiens 59-64 23033481-9 2012 Indeed, we found that mutation of both Cys-40 and Cys-346 (Panx1(C40A/C346A)) prevented Panx1 S-nitrosylation by GSNO as well as the GSNO-mediated inhibition of Panx1 current and ATP release. S-Nitrosoglutathione 113-117 pannexin 1 Homo sapiens 88-93 23033481-3 2012 Using the biotin switch assay, we found that application of the NO donor S-nitrosoglutathione (GSNO) or diethylammonium (Z)-1-1(N,N-diethylamino)diazen-1-ium-1,2-diolate (DEA NONOate) to human embryonic kidney (HEK) 293T cells expressing wild type (WT) Panx1 and mouse aortic endothelial cells induced Panx1 S-nitrosylation. S-Nitrosoglutathione 73-93 pannexin 1 Homo sapiens 253-258 23033481-3 2012 Using the biotin switch assay, we found that application of the NO donor S-nitrosoglutathione (GSNO) or diethylammonium (Z)-1-1(N,N-diethylamino)diazen-1-ium-1,2-diolate (DEA NONOate) to human embryonic kidney (HEK) 293T cells expressing wild type (WT) Panx1 and mouse aortic endothelial cells induced Panx1 S-nitrosylation. S-Nitrosoglutathione 73-93 pannexin 1 Mus musculus 302-307 23033481-4 2012 Functionally, GSNO and DEA NONOate attenuated Panx1 currents; consistent with a role for S-nitrosylation, current inhibition was reversed by the reducing agent dithiothreitol and unaffected by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one, a blocker of guanylate cyclase activity. S-Nitrosoglutathione 14-18 pannexin 1 Homo sapiens 46-51 23033481-9 2012 Indeed, we found that mutation of both Cys-40 and Cys-346 (Panx1(C40A/C346A)) prevented Panx1 S-nitrosylation by GSNO as well as the GSNO-mediated inhibition of Panx1 current and ATP release. S-Nitrosoglutathione 113-117 pannexin 1 Homo sapiens 88-93 23033481-9 2012 Indeed, we found that mutation of both Cys-40 and Cys-346 (Panx1(C40A/C346A)) prevented Panx1 S-nitrosylation by GSNO as well as the GSNO-mediated inhibition of Panx1 current and ATP release. S-Nitrosoglutathione 133-137 pannexin 1 Homo sapiens 59-64 22705913-6 2012 NAC-SNO-np exhibited higher efficiency for generating GSNO from GSH and maintained higher levels of GSNO concentration for longer time (24 h) as compared to SNO-np as well as a previously characterized nitric oxide releasing platform, NO-np (nitric oxide releasing nanoparticles). S-Nitrosoglutathione 54-58 synuclein alpha Homo sapiens 0-3 22705913-6 2012 NAC-SNO-np exhibited higher efficiency for generating GSNO from GSH and maintained higher levels of GSNO concentration for longer time (24 h) as compared to SNO-np as well as a previously characterized nitric oxide releasing platform, NO-np (nitric oxide releasing nanoparticles). S-Nitrosoglutathione 54-58 strawberry notch homolog 1 Homo sapiens 4-7 22705913-6 2012 NAC-SNO-np exhibited higher efficiency for generating GSNO from GSH and maintained higher levels of GSNO concentration for longer time (24 h) as compared to SNO-np as well as a previously characterized nitric oxide releasing platform, NO-np (nitric oxide releasing nanoparticles). S-Nitrosoglutathione 100-104 synuclein alpha Homo sapiens 0-3 22705913-6 2012 NAC-SNO-np exhibited higher efficiency for generating GSNO from GSH and maintained higher levels of GSNO concentration for longer time (24 h) as compared to SNO-np as well as a previously characterized nitric oxide releasing platform, NO-np (nitric oxide releasing nanoparticles). S-Nitrosoglutathione 100-104 strawberry notch homolog 1 Homo sapiens 4-7 22707614-12 2012 p14(ARF)-hypermethylated IPF fibroblasts were significantly more resistant to staurosporine-and S-nitrosoglutathione-induced apoptosis compared with normal and nonmethylated IPF fibroblasts (P < 0.01) and showed reduced levels of p53. S-Nitrosoglutathione 96-116 ribonuclease P/MRP subunit p14 Homo sapiens 0-3 23997981-9 2012 GSNO also increased the expression of VEGF, reduced cellular infiltration (H&E staining) and apoptotic cell death (TUNEL assay), and hampered demyelination (LFB staining and g-ratio). S-Nitrosoglutathione 0-4 vascular endothelial growth factor A Rattus norvegicus 38-42 22847419-5 2012 Furthermore, the GAPDH substrate glyceraldehyde-3-phosphate (G3P) and the nitric oxide donor S-nitrosoglutathione (GSNO) both negatively regulate GAPDH inhibition of telomerase activity. S-Nitrosoglutathione 93-113 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 146-151 22847419-5 2012 Furthermore, the GAPDH substrate glyceraldehyde-3-phosphate (G3P) and the nitric oxide donor S-nitrosoglutathione (GSNO) both negatively regulate GAPDH inhibition of telomerase activity. S-Nitrosoglutathione 115-119 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 146-151 22849540-1 2012 BACKGROUND: adhC from Haemophilus influenzae encodes a glutathione-dependent alcohol dehydrogenase that has previously been shown to be required for protection against killing by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 179-199 S-(hydroxymethyl)glutathione dehydrogenase Haemophilus influenzae Rd KW20 12-16 22849540-1 2012 BACKGROUND: adhC from Haemophilus influenzae encodes a glutathione-dependent alcohol dehydrogenase that has previously been shown to be required for protection against killing by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 201-205 S-(hydroxymethyl)glutathione dehydrogenase Haemophilus influenzae Rd KW20 12-16 22849540-4 2012 adhC could also be induced in response to formaldehyde but not GSNO. S-Nitrosoglutathione 63-67 S-(hydroxymethyl)glutathione dehydrogenase Haemophilus influenzae Rd KW20 0-4 22378818-6 2012 The NO donor S-nitrosoglutathione (GSNO) and Bay 41-2272 stimulated PKG activity and induced phosphorylation of Akt protein in human proximal tubular cells. S-Nitrosoglutathione 13-33 protein kinase cGMP-dependent 1 Homo sapiens 68-71 22517771-9 2012 The NO release by GSNO countered the upregulation of Icam-1 by increasing the transcription of global HDAC3 and its association with the Icam-1 promoter, and by suppressing H4K12 acetylation. S-Nitrosoglutathione 18-22 intercellular adhesion molecule 1 Rattus norvegicus 53-59 22517771-9 2012 The NO release by GSNO countered the upregulation of Icam-1 by increasing the transcription of global HDAC3 and its association with the Icam-1 promoter, and by suppressing H4K12 acetylation. S-Nitrosoglutathione 18-22 histone deacetylase 3 Rattus norvegicus 102-107 22517771-9 2012 The NO release by GSNO countered the upregulation of Icam-1 by increasing the transcription of global HDAC3 and its association with the Icam-1 promoter, and by suppressing H4K12 acetylation. S-Nitrosoglutathione 18-22 intercellular adhesion molecule 1 Rattus norvegicus 137-143 22378818-6 2012 The NO donor S-nitrosoglutathione (GSNO) and Bay 41-2272 stimulated PKG activity and induced phosphorylation of Akt protein in human proximal tubular cells. S-Nitrosoglutathione 13-33 AKT serine/threonine kinase 1 Homo sapiens 112-115 22378818-6 2012 The NO donor S-nitrosoglutathione (GSNO) and Bay 41-2272 stimulated PKG activity and induced phosphorylation of Akt protein in human proximal tubular cells. S-Nitrosoglutathione 35-39 protein kinase cGMP-dependent 1 Homo sapiens 68-71 22378818-6 2012 The NO donor S-nitrosoglutathione (GSNO) and Bay 41-2272 stimulated PKG activity and induced phosphorylation of Akt protein in human proximal tubular cells. S-Nitrosoglutathione 35-39 AKT serine/threonine kinase 1 Homo sapiens 112-115 22378818-7 2012 GSNO also induced phosphorylation of eukaryotic initiation factor 4E-binding protein and ribosomal protein S6. S-Nitrosoglutathione 0-4 ribosomal protein S6 Mus musculus 89-109 22465477-5 2012 The results with allopurinol and cyanamide suggest that only mitochondrial aldehyde dehydrogenase is involved in the bioactivation of GTN, sodium nitrite, and GSNO, whereas both pathways are involved in the bioactivation of nitrite anion in the intact rat. S-Nitrosoglutathione 159-163 aldehyde dehydrogenase 2 family member Rattus norvegicus 61-97 22371078-2 2012 It has been demonstrated previously that GSNO reductase (GSNOR) is the main enzyme responsible for the in vivo control of intracellular levels of GSNO. S-Nitrosoglutathione 41-45 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 57-62 21910597-4 2012 RESULTS: PVP/GSNO formulations at doses of 25 and/or 100, but not 500 nmol caused significant inhibition of alveolar bone loss, increase of bone alkaline phosphatase, decrease of myeloperoxidase activity, as well as significant reduction of inflammatory and oxidative stress markers when compared to saline and PVP groups. S-Nitrosoglutathione 13-17 myeloperoxidase Rattus norvegicus 179-194 22554503-10 2012 Our data demonstrated that, GSNO"s antiapoptotic effect against reoxygenation injury involves ERK signaling pathway. S-Nitrosoglutathione 28-32 mitogen-activated protein kinase 1 Homo sapiens 94-97 22554503-5 2012 Consistent with this, when administered with adenoviral vector encoding dominant negative ERK (Ad-dnERK), GSNO"s effect was also blocked. S-Nitrosoglutathione 106-110 mitogen-activated protein kinase 1 Homo sapiens 90-93 22554503-6 2012 Western blotting revealed that GSNO increased the ERK phosphorylation during reoxygenation. S-Nitrosoglutathione 31-35 mitogen-activated protein kinase 1 Homo sapiens 50-53 22025280-4 2012 We determined the effects of S-nitrosoglutathione (GSNO, NO-donor) and U0126 (MEK inhibitor) on insulin-like growth factor-I (IGF-I) and epidermal growth factor (EGF) signaling, proliferation and invasion in cancer cell lines. S-Nitrosoglutathione 63-67 insulin like growth factor 1 Homo sapiens 120-148 22335564-1 2012 N6022 is a novel, first-in-class drug with potent inhibitory activity against S-nitrosoglutathione reductase (GSNOR), an enzyme important in the metabolism of S-nitrosoglutathione (GSNO) and in the maintenance of nitric oxide (NO) homeostasis. S-Nitrosoglutathione 110-114 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 78-108 22025280-4 2012 We determined the effects of S-nitrosoglutathione (GSNO, NO-donor) and U0126 (MEK inhibitor) on insulin-like growth factor-I (IGF-I) and epidermal growth factor (EGF) signaling, proliferation and invasion in cancer cell lines. S-Nitrosoglutathione 63-67 insulin like growth factor 1 Homo sapiens 150-155 22025280-4 2012 We determined the effects of S-nitrosoglutathione (GSNO, NO-donor) and U0126 (MEK inhibitor) on insulin-like growth factor-I (IGF-I) and epidermal growth factor (EGF) signaling, proliferation and invasion in cancer cell lines. S-Nitrosoglutathione 63-67 epidermal growth factor Homo sapiens 161-184 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 insulin like growth factor 1 receptor Homo sapiens 45-59 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 insulin like growth factor 1 receptor Homo sapiens 61-67 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 epidermal growth factor receptor Homo sapiens 70-82 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 epidermal growth factor receptor Homo sapiens 84-88 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 AKT serine/threonine kinase 1 Homo sapiens 94-97 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 mitogen-activated protein kinase 3 Homo sapiens 115-121 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 insulin like growth factor 1 Homo sapiens 45-50 22025280-5 2012 GSNO inhibits phosphorylation of IGF-I receptor (IGF-IR), EGF receptor (EGFR) and Akt, but upregulates ERK1/2 phosphorylation in MIAPaCa-2 and HCT-116 cells after stimulation by IGF-I and EGF. S-Nitrosoglutathione 0-4 epidermal growth factor Homo sapiens 70-73 22025280-7 2012 The combination of GSNO and U0126 downregulates phosphorylation of IGF-IR, EGFR, Akt and ERK1/2 after stimulation by IGF-I and EGF. S-Nitrosoglutathione 31-35 insulin like growth factor 1 receptor Homo sapiens 79-85 22025280-7 2012 The combination of GSNO and U0126 downregulates phosphorylation of IGF-IR, EGFR, Akt and ERK1/2 after stimulation by IGF-I and EGF. S-Nitrosoglutathione 31-35 epidermal growth factor receptor Homo sapiens 87-91 22025280-7 2012 The combination of GSNO and U0126 downregulates phosphorylation of IGF-IR, EGFR, Akt and ERK1/2 after stimulation by IGF-I and EGF. S-Nitrosoglutathione 31-35 AKT serine/threonine kinase 1 Homo sapiens 93-96 22025280-7 2012 The combination of GSNO and U0126 downregulates phosphorylation of IGF-IR, EGFR, Akt and ERK1/2 after stimulation by IGF-I and EGF. S-Nitrosoglutathione 31-35 mitogen-activated protein kinase 3 Homo sapiens 101-107 22025280-7 2012 The combination of GSNO and U0126 downregulates phosphorylation of IGF-IR, EGFR, Akt and ERK1/2 after stimulation by IGF-I and EGF. S-Nitrosoglutathione 31-35 insulin like growth factor 1 Homo sapiens 79-84 22025280-7 2012 The combination of GSNO and U0126 downregulates phosphorylation of IGF-IR, EGFR, Akt and ERK1/2 after stimulation by IGF-I and EGF. S-Nitrosoglutathione 31-35 epidermal growth factor Homo sapiens 87-90 22070099-3 2012 Recently, we observed that ferric cytochrome c can promote S-nitrosoglutathione formation from NO and glutathione by acting as an electron acceptor under anaerobic conditions. S-Nitrosoglutathione 59-79 cytochrome c, somatic Homo sapiens 34-46 22123824-9 2012 In addition, treatment with sodium nitroprusside (an exogenous NO donor) and S-nitrosoglutathione or MK801, an antagonist of the N-methyl-D-aspartate receptor, also diminished the S-nitrosylation and activation of MLK3 induced by cerebral ischemia/reperfusion. S-Nitrosoglutathione 77-97 mitogen-activated protein kinase kinase kinase 11 Homo sapiens 214-218 22123824-4 2012 We report here that MLK3, overexpressed in HEK293 cells, is S-nitrosylated (forming SNO-MLK3) via a reaction with S-nitrosoglutathione, an exogenous nitric oxide (NO) donor, at one critical cysteine residue (Cys-688). S-Nitrosoglutathione 114-134 mitogen-activated protein kinase kinase kinase 11 Homo sapiens 20-24 23285246-2 2012 Reduced GSNO levels have been implicated in several respiratory diseases, and inhibition of GSNO reductase, (GSNOR) the primary enzyme that metabolizes GSNO, represents a novel approach to treating inflammatory lung diseases. S-Nitrosoglutathione 8-12 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 109-114 22123824-4 2012 We report here that MLK3, overexpressed in HEK293 cells, is S-nitrosylated (forming SNO-MLK3) via a reaction with S-nitrosoglutathione, an exogenous nitric oxide (NO) donor, at one critical cysteine residue (Cys-688). S-Nitrosoglutathione 114-134 mitogen-activated protein kinase kinase kinase 11 Homo sapiens 88-92 22024253-3 2012 AIM: The purpose of the present study was to investigate the effect of GSNO in ameliorating SCI-induced amenorrhea through affecting the expression of CX43, NFkB, and ERbeta protein. S-Nitrosoglutathione 71-75 gap junction protein, alpha 1 Rattus norvegicus 151-155 22024253-3 2012 AIM: The purpose of the present study was to investigate the effect of GSNO in ameliorating SCI-induced amenorrhea through affecting the expression of CX43, NFkB, and ERbeta protein. S-Nitrosoglutathione 71-75 RELA proto-oncogene, NF-kB subunit Rattus norvegicus 157-161 22024253-3 2012 AIM: The purpose of the present study was to investigate the effect of GSNO in ameliorating SCI-induced amenorrhea through affecting the expression of CX43, NFkB, and ERbeta protein. S-Nitrosoglutathione 71-75 estrogen receptor 2 Rattus norvegicus 167-173 22024253-13 2012 The increased CX43 expression observed with SCI ovary was decreased by GSNO. S-Nitrosoglutathione 71-75 gap junction protein, alpha 1 Rattus norvegicus 14-18 22024253-14 2012 ERbeta expression decreased significantly on day 7 and 14 post-SCI and was restored with GSNO treatment. S-Nitrosoglutathione 89-93 estrogen receptor 2 Rattus norvegicus 0-6 22024253-15 2012 Following SCI, NFkB expression was increased in the ovarian follicles and the expression was reduced with GSNO administration. S-Nitrosoglutathione 106-110 RELA proto-oncogene, NF-kB subunit Rattus norvegicus 15-19 23285183-3 2012 We found that overexpressed nNOS in HEK293 (human embryonic kidney) cells could be S-nitrosylated by exogenous NO donor GSNO and which is associated with the enzyme activity decrease. S-Nitrosoglutathione 120-124 nitric oxide synthase 1 Homo sapiens 28-32 23285183-7 2012 Further more, we document that nNOS denitrosylation could be suppressed by pretreatment of neurons with MK801, an antagonist of NMDAR, GSNO, EGTA, BAPTA, W-7, an inhibitor of calmodulin as well as TrxR1 antisense oligonucleotide (AS-ODN) respectively. S-Nitrosoglutathione 135-139 nitric oxide synthase 1 Homo sapiens 31-35 23285246-2 2012 Reduced GSNO levels have been implicated in several respiratory diseases, and inhibition of GSNO reductase, (GSNOR) the primary enzyme that metabolizes GSNO, represents a novel approach to treating inflammatory lung diseases. S-Nitrosoglutathione 92-96 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 109-114 22984412-0 2012 Endothelial gamma-glutamyltransferase contributes to the vasorelaxant effect of S-nitrosoglutathione in rat aorta. S-Nitrosoglutathione 80-100 gamma-glutamyltransferase 1 Rattus norvegicus 12-37 22984412-2 2012 Breakdown of GSNO can be catalyzed by gamma-glutamyltransferase (GGT). S-Nitrosoglutathione 13-17 gamma-glutamyltransferase 1 Rattus norvegicus 38-63 22984412-2 2012 Breakdown of GSNO can be catalyzed by gamma-glutamyltransferase (GGT). S-Nitrosoglutathione 13-17 gamma-glutamyltransferase 1 Rattus norvegicus 65-68 22984412-3 2012 We investigated whether vascular GGT influences the vasorelaxant effect of GSNO in isolated rat aorta. S-Nitrosoglutathione 75-79 gamma-glutamyltransferase 1 Rattus norvegicus 33-36 22984412-5 2012 The role of GGT in GSNO metabolism was evaluated by measuring GSNO consumption rate (absorbance decay at 334 nm), ( )NO release was visualized and quantified with the fluorescent probe 4,5-diaminofluorescein diacetate. S-Nitrosoglutathione 19-23 gamma-glutamyltransferase 1 Rattus norvegicus 12-15 22984412-12 2012 These data demonstrate the important role of endothelial GGT activity in mediating the vasorelaxant effect of GSNO in rat aorta under physiological conditions. S-Nitrosoglutathione 110-114 gamma-glutamyltransferase 1 Rattus norvegicus 57-60 22496859-10 2012 The prompt release of GGT may have consequences on all GGT substrates, including major inflammatory mediators such as S-nitrosoglutathione and leukotrienes, and could participate in early modulation of inflammatory response. S-Nitrosoglutathione 118-138 gamma-glutamyltransferase light chain family member 3 Homo sapiens 22-25 22364021-4 2011 At the same time, GSNO increased the levels of protein carbonyls and inactivated enzymes ascorbate peroxidase, guaiacol peroxidase and dehydroascorbate reductase in almost all investigated plant lines. S-Nitrosoglutathione 18-22 peroxidase Arabidopsis thaliana 99-109 21784966-2 2011 Airway GSNO levels decrease in severe respiratory failure and asthma, which is attributable to increased metabolism by GSNO reductase (GSNOR). S-Nitrosoglutathione 7-11 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 119-133 21784966-2 2011 Airway GSNO levels decrease in severe respiratory failure and asthma, which is attributable to increased metabolism by GSNO reductase (GSNOR). S-Nitrosoglutathione 7-11 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 135-140 21834791-6 2011 These results suggest that the increased cytotoxic effect of combined doxorubicin and GSNO treatment involves the glutathionylation of histones through a mechanism that requires high glutathione levels and increased expression of GSTP1-1. S-Nitrosoglutathione 86-90 glutathione S-transferase pi 1 Homo sapiens 230-237 22189680-1 2011 Aberrant GAPDH expression following S-nitrosoglutathione (GSNO) treatment was compared in HepG2 cells, which express functional p53, and Hep3B cells, which lack functional p53. S-Nitrosoglutathione 36-56 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 9-14 22189680-1 2011 Aberrant GAPDH expression following S-nitrosoglutathione (GSNO) treatment was compared in HepG2 cells, which express functional p53, and Hep3B cells, which lack functional p53. S-Nitrosoglutathione 58-62 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 9-14 22189680-3 2011 This finding suggests that p53 may not be necessary for the GSNO-induced translocation of GAPDH to the nucleus during apoptotic cell death in hepatoma cells. S-Nitrosoglutathione 60-64 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 90-95 21930693-8 2011 Surprisingly, C203S-CypD reconstituted MEFs were resistant to mPTP opening in the presence or absence of GSNO, suggesting a crucial role for Cys-203 in mPTP activation. S-Nitrosoglutathione 105-109 peptidylprolyl isomerase F (cyclophilin F) Mus musculus 20-24 22364021-4 2011 At the same time, GSNO increased the levels of protein carbonyls and inactivated enzymes ascorbate peroxidase, guaiacol peroxidase and dehydroascorbate reductase in almost all investigated plant lines. S-Nitrosoglutathione 18-22 peroxidase Arabidopsis thaliana 120-130 21855338-2 2011 GSNOR is a member of the alcohol dehydrogenase family (ADH) and regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 133-153 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 0-5 21642009-4 2011 Many of the genes, whose expression was induced by GSNO, contain a cAMP-response element (CRE), of which one encoded the inducible cAMP early repressor (ICER). S-Nitrosoglutathione 51-55 cAMP responsive element modulator Homo sapiens 121-158 21642009-7 2011 Pre-treatment of RPaSMC with the intracellular calcium (Ca(2+)) chelator, BAPTA-AM, blocked the induction of ICER gene expression by GSNO. S-Nitrosoglutathione 133-137 cAMP responsive element modulator Homo sapiens 109-113 21642009-8 2011 The store-operated Ca(2+) channel inhibitors, 2-ABP, and SKF-96365, reduced the GSNO-mediated increase in ICER mRNA levels, while 2-ABP did not inhibit GSNO-induced CREB phosphorylation. S-Nitrosoglutathione 80-84 sex hormone binding globulin Homo sapiens 48-51 21642009-8 2011 The store-operated Ca(2+) channel inhibitors, 2-ABP, and SKF-96365, reduced the GSNO-mediated increase in ICER mRNA levels, while 2-ABP did not inhibit GSNO-induced CREB phosphorylation. S-Nitrosoglutathione 80-84 cAMP responsive element modulator Homo sapiens 106-110 21642009-10 2011 Transcription profiling of RPaSMC exposed to GSNO revealed important roles for sGC, PKA, CREB, and Ca(2+) in the regulation of gene expression by NO. S-Nitrosoglutathione 45-49 cAMP responsive element binding protein 1 Homo sapiens 89-93 21642009-11 2011 The induction of ICER in GSNO-treated RPaSMC highlights a novel cross-talk mechanism between cGMP and cAMP signaling pathways. S-Nitrosoglutathione 25-29 cAMP responsive element modulator Homo sapiens 17-21 21855338-2 2011 GSNOR is a member of the alcohol dehydrogenase family (ADH) and regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 133-153 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 55-58 21855338-2 2011 GSNOR is a member of the alcohol dehydrogenase family (ADH) and regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 0-4 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 55-58 21503714-8 2011 However maximal inhibition of the succinate dependent H(2)O(2) release is obtained in the presence of low GSNO (20-100 muM), but not with SNP. S-Nitrosoglutathione 106-110 latexin Homo sapiens 119-122 21820121-4 2011 In vitro nitrosylation model-BSA subjected to S-nitrosoglutathione (GSNO) optimized the labeling reactions and characterized the response of the LIF detector. S-Nitrosoglutathione 46-66 leukemia inhibitory factor Mus musculus 145-148 21820121-4 2011 In vitro nitrosylation model-BSA subjected to S-nitrosoglutathione (GSNO) optimized the labeling reactions and characterized the response of the LIF detector. S-Nitrosoglutathione 68-72 leukemia inhibitory factor Mus musculus 145-148 21724851-7 2011 Cultured differentiated pre-adipocyte cell lines exposed to the NO donors S-nitrosoglutathione (GSNO) or S-nitroso-N-acetylpenicillamine exhibited diminished insulin-stimulated phosphorylation of Akt but not of GSK3 nor of insulin-stimulated glucose uptake. S-Nitrosoglutathione 74-94 glycogen synthase kinase 3 beta Mus musculus 211-215 21724851-7 2011 Cultured differentiated pre-adipocyte cell lines exposed to the NO donors S-nitrosoglutathione (GSNO) or S-nitroso-N-acetylpenicillamine exhibited diminished insulin-stimulated phosphorylation of Akt but not of GSK3 nor of insulin-stimulated glucose uptake. S-Nitrosoglutathione 96-100 glycogen synthase kinase 3 beta Mus musculus 211-215 21724851-11 2011 Site-directed mutagenesis revealed that Cys-768 and Cys-1040, two putative sites for S-nitrosylation adjacent to the substrate-binding site of PDE3B, accounted for ~50% of its GSNO-induced S-nitrosylation. S-Nitrosoglutathione 176-180 phosphodiesterase 3B, cGMP-inhibited Mus musculus 143-148 21723853-4 2011 In an in vitro VHL capture assay, hydroxylation of the 19mer HIF peptide (corresponding to HIF-1alpha residues 556-574) by HPH-2 was effectively prevented by nitric oxide (NO) donors, (+-)-S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione. S-Nitrosoglutathione 232-252 hypoxia inducible factor 1 subunit alpha Homo sapiens 91-101 21723853-4 2011 In an in vitro VHL capture assay, hydroxylation of the 19mer HIF peptide (corresponding to HIF-1alpha residues 556-574) by HPH-2 was effectively prevented by nitric oxide (NO) donors, (+-)-S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione. S-Nitrosoglutathione 232-252 egl-9 family hypoxia inducible factor 1 Homo sapiens 123-128 21539916-5 2011 GSNO was the most powerful inhibitor (IC(50) values, muM): (a) in human, GSNO=0.52+-0.09, SNP=2.83 +- 0.53, SIN-1=2.98 +- 1.06; (b) in rat, GSNO = 28.4 +- 6.9, SNP = 265 +- 73, SIN-1=108 +- 85. S-Nitrosoglutathione 0-4 latexin Homo sapiens 53-56 21539916-5 2011 GSNO was the most powerful inhibitor (IC(50) values, muM): (a) in human, GSNO=0.52+-0.09, SNP=2.83 +- 0.53, SIN-1=2.98 +- 1.06; (b) in rat, GSNO = 28.4 +- 6.9, SNP = 265 +- 73, SIN-1=108 +- 85. S-Nitrosoglutathione 0-4 MAPK associated protein 1 Homo sapiens 108-113 21539916-5 2011 GSNO was the most powerful inhibitor (IC(50) values, muM): (a) in human, GSNO=0.52+-0.09, SNP=2.83 +- 0.53, SIN-1=2.98 +- 1.06; (b) in rat, GSNO = 28.4 +- 6.9, SNP = 265 +- 73, SIN-1=108 +- 85. S-Nitrosoglutathione 0-4 MAPK associated protein 1 Homo sapiens 177-182 21539916-6 2011 GSNO action in both species was mediated by cGMP-independent mechanisms and characterized by the highest NO release in PRP. S-Nitrosoglutathione 0-4 proline rich protein 2-like 1 Rattus norvegicus 119-122 21849622-5 2011 Using the transnitrosation agent, S-nitrosoglutathione, a kinetic analysis of the selectivity and redox dependence of Trx nitrosation at physiologically relevant concentrations and times was performed, utilizing a mass spectrometry-based method for the direct analysis of the nitrosated Trx. S-Nitrosoglutathione 34-54 thioredoxin Homo sapiens 118-121 21570838-1 2011 S-Nitrosoglutathione reductase (GSNOR) is a member of the alcohol dehydrogenase family (ADH) that regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 167-187 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-30 21570838-1 2011 S-Nitrosoglutathione reductase (GSNOR) is a member of the alcohol dehydrogenase family (ADH) that regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 167-187 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 32-37 21570838-1 2011 S-Nitrosoglutathione reductase (GSNOR) is a member of the alcohol dehydrogenase family (ADH) that regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 167-187 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 88-91 21570838-1 2011 S-Nitrosoglutathione reductase (GSNOR) is a member of the alcohol dehydrogenase family (ADH) that regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 32-36 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-30 21570838-1 2011 S-Nitrosoglutathione reductase (GSNOR) is a member of the alcohol dehydrogenase family (ADH) that regulates the levels of S-nitrosothiols (SNOs) through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 32-36 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 88-91 21414799-3 2011 Using sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO) as NO-donating compounds, we observed that both mRNA and protein levels of IL-6 increased at lower (<=10muM) and decreased at higher (>100muM) concentrations of NO donors. S-Nitrosoglutathione 37-57 interleukin 6 Homo sapiens 140-144 21414799-3 2011 Using sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO) as NO-donating compounds, we observed that both mRNA and protein levels of IL-6 increased at lower (<=10muM) and decreased at higher (>100muM) concentrations of NO donors. S-Nitrosoglutathione 59-63 interleukin 6 Homo sapiens 140-144 21503714-10 2011 )NO release since muM GSNO does not affect mitochondrial respiration, or the H(2)O(2) detection systems and its effect is very rapid. S-Nitrosoglutathione 22-26 latexin Homo sapiens 18-21 21256830-0 2011 Studies on reduction of S-nitrosoglutathione by human carbonyl reductases 1 and 3. S-Nitrosoglutathione 24-44 carbonyl reductase 1 Homo sapiens 54-81 21543898-1 2011 During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC 1.2.1.1), catalyzes the NADH-dependent reduction of S-nitrosoglutathione (GSNO) and therefore was also designated as GSNO reductase. S-Nitrosoglutathione 225-245 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 85-89 21543898-1 2011 During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC 1.2.1.1), catalyzes the NADH-dependent reduction of S-nitrosoglutathione (GSNO) and therefore was also designated as GSNO reductase. S-Nitrosoglutathione 225-245 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 113-161 21543898-1 2011 During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC 1.2.1.1), catalyzes the NADH-dependent reduction of S-nitrosoglutathione (GSNO) and therefore was also designated as GSNO reductase. S-Nitrosoglutathione 225-245 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 163-168 21543898-1 2011 During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC 1.2.1.1), catalyzes the NADH-dependent reduction of S-nitrosoglutathione (GSNO) and therefore was also designated as GSNO reductase. S-Nitrosoglutathione 247-251 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 85-89 21543898-1 2011 During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC 1.2.1.1), catalyzes the NADH-dependent reduction of S-nitrosoglutathione (GSNO) and therefore was also designated as GSNO reductase. S-Nitrosoglutathione 247-251 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 113-161 21543898-1 2011 During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC 1.2.1.1), catalyzes the NADH-dependent reduction of S-nitrosoglutathione (GSNO) and therefore was also designated as GSNO reductase. S-Nitrosoglutathione 247-251 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 163-168 21256830-3 2011 Recently, the endogenous low molecular weight S-nitrosothiol S-nitrosoglutathione (GSNO) has been added to the broad substrate spectrum of CBR1. S-Nitrosoglutathione 61-81 carbonyl reductase 1 Homo sapiens 139-143 21256830-3 2011 Recently, the endogenous low molecular weight S-nitrosothiol S-nitrosoglutathione (GSNO) has been added to the broad substrate spectrum of CBR1. S-Nitrosoglutathione 83-87 carbonyl reductase 1 Homo sapiens 139-143 21256830-4 2011 The current study initially addressed whether CBR3 could equally reduce GSNO which was not the case. S-Nitrosoglutathione 72-76 carbonyl reductase 3 Homo sapiens 46-50 21256830-6 2011 However, exchanging amino acids 236-244 in CBR3 to correspond to CBR1 was sufficient to engender catalytic activity towards GSNO. S-Nitrosoglutathione 124-128 carbonyl reductase 3 Homo sapiens 43-47 21256830-6 2011 However, exchanging amino acids 236-244 in CBR3 to correspond to CBR1 was sufficient to engender catalytic activity towards GSNO. S-Nitrosoglutathione 124-128 carbonyl reductase 1 Homo sapiens 65-69 21256830-8 2011 Hence, the same residues previously reported as important for reduction of carbonyl compounds appear to be key to CBR1-mediated reduction of GSNO. S-Nitrosoglutathione 141-145 carbonyl reductase 1 Homo sapiens 114-118 21256830-9 2011 Furthermore, for CBR1-mediated reduction of GSNO, considerable substrate inhibition at concentrations >5 K(m) was observed. S-Nitrosoglutathione 44-48 carbonyl reductase 1 Homo sapiens 17-21 21256830-10 2011 Treatment of CBR1 with GSNO followed by removal of low molecular weight compounds decreased the GSNO reducing activity, suggesting a covalent modification. S-Nitrosoglutathione 23-27 carbonyl reductase 1 Homo sapiens 13-17 21256830-10 2011 Treatment of CBR1 with GSNO followed by removal of low molecular weight compounds decreased the GSNO reducing activity, suggesting a covalent modification. S-Nitrosoglutathione 96-100 carbonyl reductase 1 Homo sapiens 13-17 21256830-13 2011 Collectively, the results clearly argue for a physiological role of CBR1, but not for CBR3, in GSNO reduction and thus ultimately in regulation of NO signaling. S-Nitrosoglutathione 95-99 carbonyl reductase 1 Homo sapiens 68-72 21256830-14 2011 Furthermore, at higher concentrations, GSNO appears to work as a suicide inhibitor for CBR1, probably through glutathionylation of C227. S-Nitrosoglutathione 39-43 carbonyl reductase 1 Homo sapiens 87-91 20965165-1 2011 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), has been proposed as a possible pharmacological remedy that reverses the DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) maturation defect and increases CFTR-mediated chloride efflux in cultured cystic fibrosis airway epithelial cells (CFBE41o(-)). S-Nitrosoglutathione 31-51 CF transmembrane conductance regulator Homo sapiens 143-147 21139062-10 2011 Furthermore, expression of Cdc42 and phospho-PAK in Caco-2 monolayers was significantly reduced in the presence of EGCs or GSNO. S-Nitrosoglutathione 123-127 cell division cycle 42 Homo sapiens 27-32 21139062-11 2011 In addition, changes in ZO-1 expression and distribution induced by S flexneri were prevented by EGCs and GSNO. S-Nitrosoglutathione 106-110 tight junction protein 1 Homo sapiens 24-28 21148565-4 2011 Moreover, the ubiquitin-dependent degradation of Bcl-2 was found to be promoted after KA treatment, which could be suppressed by the proteasome inhibitor MG132 and the NO donors, sodium nitroprusside and S-nitrosoglutathione. S-Nitrosoglutathione 204-224 BCL2 apoptosis regulator Homo sapiens 49-54 21148565-6 2011 At the same time, it was found that the exogenous NO donor GSNO could protect neurons when Bcl-2 is targeted. S-Nitrosoglutathione 59-63 BCL2 apoptosis regulator Homo sapiens 91-96 21148565-8 2011 NS102, GSNO, sodium nitroprusside, and MG132 contribute to the survival of CA1 and CA3/DG pyramidal neurons by attenuating Bcl-2 denitrosylation. S-Nitrosoglutathione 7-11 carbonic anhydrase 1 Homo sapiens 75-78 21148565-8 2011 NS102, GSNO, sodium nitroprusside, and MG132 contribute to the survival of CA1 and CA3/DG pyramidal neurons by attenuating Bcl-2 denitrosylation. S-Nitrosoglutathione 7-11 carbonic anhydrase 3 Homo sapiens 83-86 21148565-8 2011 NS102, GSNO, sodium nitroprusside, and MG132 contribute to the survival of CA1 and CA3/DG pyramidal neurons by attenuating Bcl-2 denitrosylation. S-Nitrosoglutathione 7-11 BCL2 apoptosis regulator Homo sapiens 123-128 21393240-6 2011 A C141S-Syntaxin 4 mutant resisted S-nitrosylation induced in vitro by the nitric oxide donor compound S-nitroso-L-glutathione, failed to exhibit glucose-induced activation and VAMP2 binding, and failed to potentiate insulin release akin to that of wild-type Syntaxin 4. S-Nitrosoglutathione 103-126 syntaxin 4 Homo sapiens 8-18 20811048-6 2011 RESULTS: NO production in 5-FMO-treated hTERT-RPE cells was increased by ornithine, and the NO donors S-nitroso-N-acetyl-DL-penicillamine (SNAP) and S-nitrosoglutathione induced cytotoxicity. S-Nitrosoglutathione 149-169 telomerase reverse transcriptase Homo sapiens 40-45 24900320-1 2011 S-Nitrosoglutathione reductase (GSNOR) regulates S-nitrosothiols (SNOs) and nitric oxide (NO) in vivo through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 124-144 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 0-30 24900320-1 2011 S-Nitrosoglutathione reductase (GSNOR) regulates S-nitrosothiols (SNOs) and nitric oxide (NO) in vivo through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 124-144 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 32-37 24900320-1 2011 S-Nitrosoglutathione reductase (GSNOR) regulates S-nitrosothiols (SNOs) and nitric oxide (NO) in vivo through catabolism of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 32-36 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 0-30 20965165-1 2011 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), has been proposed as a possible pharmacological remedy that reverses the DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) maturation defect and increases CFTR-mediated chloride efflux in cultured cystic fibrosis airway epithelial cells (CFBE41o(-)). S-Nitrosoglutathione 31-51 CF transmembrane conductance regulator Homo sapiens 149-200 20965165-1 2011 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), has been proposed as a possible pharmacological remedy that reverses the DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) maturation defect and increases CFTR-mediated chloride efflux in cultured cystic fibrosis airway epithelial cells (CFBE41o(-)). S-Nitrosoglutathione 31-51 CF transmembrane conductance regulator Homo sapiens 234-238 20965165-1 2011 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), has been proposed as a possible pharmacological remedy that reverses the DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) maturation defect and increases CFTR-mediated chloride efflux in cultured cystic fibrosis airway epithelial cells (CFBE41o(-)). S-Nitrosoglutathione 53-57 CF transmembrane conductance regulator Homo sapiens 143-147 20965165-1 2011 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), has been proposed as a possible pharmacological remedy that reverses the DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) maturation defect and increases CFTR-mediated chloride efflux in cultured cystic fibrosis airway epithelial cells (CFBE41o(-)). S-Nitrosoglutathione 53-57 CF transmembrane conductance regulator Homo sapiens 149-200 20965165-1 2011 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), has been proposed as a possible pharmacological remedy that reverses the DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) maturation defect and increases CFTR-mediated chloride efflux in cultured cystic fibrosis airway epithelial cells (CFBE41o(-)). S-Nitrosoglutathione 53-57 CF transmembrane conductance regulator Homo sapiens 234-238 21422596-4 2011 It was found that HDAC8 can be S-nitrosylated by the NO donor S-nitrosoglutathione (GSNO) in vitro, and the activity of HDAC8 was significantly inhibited when incubated with GSNO and S-nitrosocysteine in a time- and dosage-dependent manner, but sodium nitroprusside (SNP), and dithiothreitol cannot reverse this inhibition. S-Nitrosoglutathione 62-82 histone deacetylase 8 Homo sapiens 18-23 21203591-5 2010 Transnitrosation to form S-nitrosoglutathione (GSNO) was observed only in the absence of oxygen or presence of SOD. S-Nitrosoglutathione 47-51 superoxide dismutase 1 Homo sapiens 111-114 21804223-7 2011 Intravenous injection of a high dose of Alb-SNO (300 nmol/kg) significantly reduced blood pressure with the appearance not only Alb-SNO in micromolar level in plasma, but also G-SNO in lesser degree. S-Nitrosoglutathione 176-181 albumin Oryctolagus cuniculus 40-43 21109971-6 2011 Interestingly, administration of S-nitroso-L-glutathione (GSNO) a nitric oxide (NO) donor, was found to enhance AID and iNOS expression in LoVo cells treated with 5-Aza-dC. S-Nitrosoglutathione 58-62 activation induced cytidine deaminase Homo sapiens 112-115 21109971-6 2011 Interestingly, administration of S-nitroso-L-glutathione (GSNO) a nitric oxide (NO) donor, was found to enhance AID and iNOS expression in LoVo cells treated with 5-Aza-dC. S-Nitrosoglutathione 58-62 nitric oxide synthase 2 Homo sapiens 120-124 21203591-5 2010 Transnitrosation to form S-nitrosoglutathione (GSNO) was observed only in the absence of oxygen or presence of SOD. S-Nitrosoglutathione 25-45 superoxide dismutase 1 Homo sapiens 111-114 21422596-4 2011 It was found that HDAC8 can be S-nitrosylated by the NO donor S-nitrosoglutathione (GSNO) in vitro, and the activity of HDAC8 was significantly inhibited when incubated with GSNO and S-nitrosocysteine in a time- and dosage-dependent manner, but sodium nitroprusside (SNP), and dithiothreitol cannot reverse this inhibition. S-Nitrosoglutathione 62-82 histone deacetylase 8 Homo sapiens 120-125 21422596-4 2011 It was found that HDAC8 can be S-nitrosylated by the NO donor S-nitrosoglutathione (GSNO) in vitro, and the activity of HDAC8 was significantly inhibited when incubated with GSNO and S-nitrosocysteine in a time- and dosage-dependent manner, but sodium nitroprusside (SNP), and dithiothreitol cannot reverse this inhibition. S-Nitrosoglutathione 84-88 histone deacetylase 8 Homo sapiens 18-23 21422596-4 2011 It was found that HDAC8 can be S-nitrosylated by the NO donor S-nitrosoglutathione (GSNO) in vitro, and the activity of HDAC8 was significantly inhibited when incubated with GSNO and S-nitrosocysteine in a time- and dosage-dependent manner, but sodium nitroprusside (SNP), and dithiothreitol cannot reverse this inhibition. S-Nitrosoglutathione 84-88 histone deacetylase 8 Homo sapiens 120-125 21422596-4 2011 It was found that HDAC8 can be S-nitrosylated by the NO donor S-nitrosoglutathione (GSNO) in vitro, and the activity of HDAC8 was significantly inhibited when incubated with GSNO and S-nitrosocysteine in a time- and dosage-dependent manner, but sodium nitroprusside (SNP), and dithiothreitol cannot reverse this inhibition. S-Nitrosoglutathione 174-178 histone deacetylase 8 Homo sapiens 18-23 21422596-4 2011 It was found that HDAC8 can be S-nitrosylated by the NO donor S-nitrosoglutathione (GSNO) in vitro, and the activity of HDAC8 was significantly inhibited when incubated with GSNO and S-nitrosocysteine in a time- and dosage-dependent manner, but sodium nitroprusside (SNP), and dithiothreitol cannot reverse this inhibition. S-Nitrosoglutathione 174-178 histone deacetylase 8 Homo sapiens 120-125 20392170-2 2010 Our purpose was to determine whether SIRT1 activity is sensitive to the low molecular weight nitrosothiol, S-nitrosoglutathione (GSNO), which can transduce oxidative signals into physiological responses. S-Nitrosoglutathione 107-127 sirtuin 1 Homo sapiens 37-42 21103380-8 2010 The ability of GSNO-R to be activated by S-nitrosylation was confirmed by: 1) the ability of S-nitrosoglutathione (GSNO) to increase the activity of GSNO-R in murine pulmonary endothelial cells and 2) reduced activity of GSNO-R in lung homogenates from eNOS(-/-) mice. S-Nitrosoglutathione 93-113 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 15-21 21103380-8 2010 The ability of GSNO-R to be activated by S-nitrosylation was confirmed by: 1) the ability of S-nitrosoglutathione (GSNO) to increase the activity of GSNO-R in murine pulmonary endothelial cells and 2) reduced activity of GSNO-R in lung homogenates from eNOS(-/-) mice. S-Nitrosoglutathione 93-113 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 149-155 21103380-8 2010 The ability of GSNO-R to be activated by S-nitrosylation was confirmed by: 1) the ability of S-nitrosoglutathione (GSNO) to increase the activity of GSNO-R in murine pulmonary endothelial cells and 2) reduced activity of GSNO-R in lung homogenates from eNOS(-/-) mice. S-Nitrosoglutathione 93-113 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 149-155 21103380-8 2010 The ability of GSNO-R to be activated by S-nitrosylation was confirmed by: 1) the ability of S-nitrosoglutathione (GSNO) to increase the activity of GSNO-R in murine pulmonary endothelial cells and 2) reduced activity of GSNO-R in lung homogenates from eNOS(-/-) mice. S-Nitrosoglutathione 15-19 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 149-155 20923703-5 2010 In acellular assays, bovine CP stimulated the generation of the nitrosating NO(+) species from the NO donors propylaminepropylamine-NONOate (PAPA/NO), S-nitroso-N-acetylpenicillamine, and S-nitrosoglutathione. S-Nitrosoglutathione 188-208 ceruloplasmin and hephaestin like 1 Bos taurus 28-30 21224496-3 2010 Incubation of rat pulmonary artery smooth muscle cells (rPaSMCs) with the NO-donor compound S-nitroso-glutathione (GSNO) increased PDE3A gene expression in a dose- and time-dependent manner. S-Nitrosoglutathione 92-113 phosphodiesterase 3A Homo sapiens 131-136 21224496-3 2010 Incubation of rat pulmonary artery smooth muscle cells (rPaSMCs) with the NO-donor compound S-nitroso-glutathione (GSNO) increased PDE3A gene expression in a dose- and time-dependent manner. S-Nitrosoglutathione 115-119 phosphodiesterase 3A Homo sapiens 131-136 21224496-6 2010 The effects of GSNO on PDE3A gene expression were mimicked by the soluble guanylate cyclase (sGC) activators YC-1 and BAY 41-2272 and blocked by the sGC inhibitor ODQ. S-Nitrosoglutathione 15-19 phosphodiesterase 3A Rattus norvegicus 23-28 21224496-6 2010 The effects of GSNO on PDE3A gene expression were mimicked by the soluble guanylate cyclase (sGC) activators YC-1 and BAY 41-2272 and blocked by the sGC inhibitor ODQ. S-Nitrosoglutathione 15-19 guanylate cyclase 1 soluble subunit beta 2 Rattus norvegicus 66-91 21224496-6 2010 The effects of GSNO on PDE3A gene expression were mimicked by the soluble guanylate cyclase (sGC) activators YC-1 and BAY 41-2272 and blocked by the sGC inhibitor ODQ. S-Nitrosoglutathione 15-19 guanylate cyclase 1 soluble subunit beta 2 Rattus norvegicus 93-96 21224496-6 2010 The effects of GSNO on PDE3A gene expression were mimicked by the soluble guanylate cyclase (sGC) activators YC-1 and BAY 41-2272 and blocked by the sGC inhibitor ODQ. S-Nitrosoglutathione 15-19 guanylate cyclase 1 soluble subunit beta 2 Rattus norvegicus 149-152 21224496-8 2010 Actinomycin D, an inhibitor of RNA polymerase, blocked the GSNO-induced increase of PDE3A mRNA levels, whereas cycloheximide, an inhibitor of protein translation, did not. S-Nitrosoglutathione 59-63 phosphodiesterase 3A Rattus norvegicus 84-89 21103380-8 2010 The ability of GSNO-R to be activated by S-nitrosylation was confirmed by: 1) the ability of S-nitrosoglutathione (GSNO) to increase the activity of GSNO-R in murine pulmonary endothelial cells and 2) reduced activity of GSNO-R in lung homogenates from eNOS(-/-) mice. S-Nitrosoglutathione 15-19 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 149-155 20392170-2 2010 Our purpose was to determine whether SIRT1 activity is sensitive to the low molecular weight nitrosothiol, S-nitrosoglutathione (GSNO), which can transduce oxidative signals into physiological responses. S-Nitrosoglutathione 129-133 sirtuin 1 Homo sapiens 37-42 20392170-3 2010 SIRT1 formed mixed disulfides with GSNO-Sepharose, and mass spectrometry identified several cysteines that are modified by GSNO, including Cys-67 which was S-glutathiolated. S-Nitrosoglutathione 35-39 sirtuin 1 Homo sapiens 0-5 20405162-2 2010 As altered S-nitrosoglutathione levels are often associated with disease, compounds that modulate ADH3 activity might be of therapeutic interest. S-Nitrosoglutathione 11-31 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 98-102 20660346-5 2010 Here we used an optimized mass spectrometric method to demonstrate that Trx1 is itself nitrosylated by S-nitrosoglutathione at Cys(73) only after the formation of a Cys(32)-Cys(35) disulfide bond upon which the disulfide reductase and denitrosylase activities of Trx1 are attenuated. S-Nitrosoglutathione 103-123 thioredoxin Homo sapiens 72-76 20699398-6 2010 The opposite response was observed in a basipetal auxin transport impaired mutant aux1-7, which was slightly rescued by exogenous GSNO application. S-Nitrosoglutathione 130-134 Transmembrane amino acid transporter family protein Arabidopsis thaliana 82-88 20683964-8 2010 Moreover, the biliary secretion of NO species was significantly diminished in UDCA-infused transport mutant [ATP-binding cassette C2 (ABCC2)/multidrug resistance-associated protein 2 (Mrp2)-deficient] rats, and this finding was consistent with the involvement of the glutathione carrier ABCC2/Mrp2 in the canalicular transport of GSNO. S-Nitrosoglutathione 330-334 ATP binding cassette subfamily C member 2 Rattus norvegicus 109-132 20534503-1 2010 The endogenous signaling molecule S-nitrosoglutathione (GSNO) and other S-nitrosylating agents can cause full maturation of the abnormal gene product DeltaF508 cystic fibrosis (CF) transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 34-54 CF transmembrane conductance regulator Homo sapiens 218-222 20716698-4 2010 Here, we report the effect of the physiological nitric oxide donor S-nitrosoglutathione on the NPR1/TGA1 regulation system in Arabidopsis thaliana. S-Nitrosoglutathione 67-87 natriuretic peptide receptor 1 Homo sapiens 95-99 20716698-4 2010 Here, we report the effect of the physiological nitric oxide donor S-nitrosoglutathione on the NPR1/TGA1 regulation system in Arabidopsis thaliana. S-Nitrosoglutathione 67-87 bZIP transcription factor family protein Arabidopsis thaliana 100-104 20716698-5 2010 Using the biotin switch method, we demonstrate that both NPR1 and TGA1 are S-nitrosylated after treatment with S-nitrosoglutathione. S-Nitrosoglutathione 111-131 regulatory protein (NPR1) Arabidopsis thaliana 57-61 20716698-5 2010 Using the biotin switch method, we demonstrate that both NPR1 and TGA1 are S-nitrosylated after treatment with S-nitrosoglutathione. S-Nitrosoglutathione 111-131 bZIP transcription factor family protein Arabidopsis thaliana 66-70 20716698-6 2010 Mass spectrometry analyses revealed that the Cys residues 260 and 266 of TGA1 are S-nitrosylated and S-glutathionylated even at GSNO concentrations in the low micromolar range. S-Nitrosoglutathione 128-132 bZIP transcription factor family protein Arabidopsis thaliana 73-77 20716698-7 2010 Furthermore, we showed that S-nitrosoglutathione protects TGA1 from oxygen-mediated modifications and enhances the DNA binding activity of TGA1 to the as-1 element in the presence of NPR1. S-Nitrosoglutathione 28-48 bZIP transcription factor family protein Arabidopsis thaliana 58-62 20716698-7 2010 Furthermore, we showed that S-nitrosoglutathione protects TGA1 from oxygen-mediated modifications and enhances the DNA binding activity of TGA1 to the as-1 element in the presence of NPR1. S-Nitrosoglutathione 28-48 bZIP transcription factor family protein Arabidopsis thaliana 139-143 20716698-7 2010 Furthermore, we showed that S-nitrosoglutathione protects TGA1 from oxygen-mediated modifications and enhances the DNA binding activity of TGA1 to the as-1 element in the presence of NPR1. S-Nitrosoglutathione 28-48 regulatory protein (NPR1) Arabidopsis thaliana 183-187 20534503-8 2010 We conclude that GSNO corrects DeltaF508 CFTR trafficking by inhibiting Hop expression, and that combination therapies--using differing mechanisms of action--may have additive benefits in treating CF. S-Nitrosoglutathione 17-21 stress induced phosphoprotein 1 Homo sapiens 72-75 20534503-1 2010 The endogenous signaling molecule S-nitrosoglutathione (GSNO) and other S-nitrosylating agents can cause full maturation of the abnormal gene product DeltaF508 cystic fibrosis (CF) transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 56-60 CF transmembrane conductance regulator Homo sapiens 218-222 20534503-3 2010 Here we show that Hsp70/Hsp90 organizing protein (Hop) is a critical target of GSNO, and its S-nitrosylation results in DeltaF508 CFTR maturation and cell surface expression. S-Nitrosoglutathione 79-83 stress induced phosphoprotein 1 Homo sapiens 18-48 20534503-3 2010 Here we show that Hsp70/Hsp90 organizing protein (Hop) is a critical target of GSNO, and its S-nitrosylation results in DeltaF508 CFTR maturation and cell surface expression. S-Nitrosoglutathione 79-83 stress induced phosphoprotein 1 Homo sapiens 50-53 20534503-3 2010 Here we show that Hsp70/Hsp90 organizing protein (Hop) is a critical target of GSNO, and its S-nitrosylation results in DeltaF508 CFTR maturation and cell surface expression. S-Nitrosoglutathione 79-83 CF transmembrane conductance regulator Homo sapiens 130-134 20534503-4 2010 S-nitrosylation by GSNO inhibited the association of Hop with CFTR in the endoplasmic reticulum. S-Nitrosoglutathione 19-23 stress induced phosphoprotein 1 Homo sapiens 53-56 20534503-4 2010 S-nitrosylation by GSNO inhibited the association of Hop with CFTR in the endoplasmic reticulum. S-Nitrosoglutathione 19-23 CF transmembrane conductance regulator Homo sapiens 62-66 20534503-5 2010 This effect was necessary and sufficient to mediate GSNO-induced cell-surface expression of DeltaF508 CFTR. S-Nitrosoglutathione 52-56 CF transmembrane conductance regulator Homo sapiens 102-106 20534503-6 2010 Hop knockdown using siRNA recapitulated the effect of GSNO on DeltaF508 CFTR maturation and expression. S-Nitrosoglutathione 54-58 stress induced phosphoprotein 1 Homo sapiens 0-3 20534503-6 2010 Hop knockdown using siRNA recapitulated the effect of GSNO on DeltaF508 CFTR maturation and expression. S-Nitrosoglutathione 54-58 CF transmembrane conductance regulator Homo sapiens 72-76 20534503-7 2010 Moreover, GSNO acted additively with decreased temperature, which promoted mutant CFTR maturation through a Hop-independent mechanism. S-Nitrosoglutathione 10-14 CF transmembrane conductance regulator Homo sapiens 82-86 20534503-7 2010 Moreover, GSNO acted additively with decreased temperature, which promoted mutant CFTR maturation through a Hop-independent mechanism. S-Nitrosoglutathione 10-14 stress induced phosphoprotein 1 Homo sapiens 108-111 20534503-8 2010 We conclude that GSNO corrects DeltaF508 CFTR trafficking by inhibiting Hop expression, and that combination therapies--using differing mechanisms of action--may have additive benefits in treating CF. S-Nitrosoglutathione 17-21 CF transmembrane conductance regulator Homo sapiens 41-45 20091246-4 2010 GSNO attenuated EAE disease by reducing the production of IL17 (from Th(i) or Th17 cells) and the infiltration of CD4 T cells into the central nervous system without affecting the levels of Th1 (IFN gamma) and Th2 (IL4) immune responses. S-Nitrosoglutathione 0-4 interleukin 4 Homo sapiens 215-218 20091246-6 2010 In vitro studies showed that the phosphorylation of STAT3 and expression of ROR gamma, key regulators of IL17 signaling, were reduced while phosphorylation of STAT4 or STAT6 and expression of T-bet or GATA3 remained unaffected, suggesting that GSNO preferentially targets Th17 cells. S-Nitrosoglutathione 244-248 signal transducer and activator of transcription 3 Homo sapiens 52-57 20091246-3 2010 Oral administration of GSNO (0.5 or 1.0 mg/kg) reduced disease progression in chronic models (SJL and C57BL/6) of EAE induced with PLP((139-151)) or MOG((35-55)) peptides, respectively. S-Nitrosoglutathione 23-27 proteolipid protein 1 Homo sapiens 131-134 20091246-4 2010 GSNO attenuated EAE disease by reducing the production of IL17 (from Th(i) or Th17 cells) and the infiltration of CD4 T cells into the central nervous system without affecting the levels of Th1 (IFN gamma) and Th2 (IL4) immune responses. S-Nitrosoglutathione 0-4 interleukin 17A Homo sapiens 58-62 20091246-7 2010 Collectively, GSNO attenuated EAE via modulation of Th17 cells and its effects are independent of Th1 or Th2 cells functions, indicating that it may have therapeutic potential for Th17-mediated autoimmune diseases. S-Nitrosoglutathione 14-18 negative elongation factor complex member C/D Homo sapiens 52-55 20153346-0 2010 The induction of reactive oxygen species and loss of mitochondrial Omi/HtrA2 is associated with S-nitrosoglutathione-induced apoptosis in human endothelial cells. S-Nitrosoglutathione 96-116 HtrA serine peptidase 2 Homo sapiens 71-76 20091246-4 2010 GSNO attenuated EAE disease by reducing the production of IL17 (from Th(i) or Th17 cells) and the infiltration of CD4 T cells into the central nervous system without affecting the levels of Th1 (IFN gamma) and Th2 (IL4) immune responses. S-Nitrosoglutathione 0-4 negative elongation factor complex member C/D Homo sapiens 78-81 20223829-5 2010 We characterized S-glutathionylation of A9; GSSG and GSNO generated S-glutathionylated A8 (A8-SSG) and A9 (A9-SSG) in vitro, whereas only A9-SSG was detected in cytosol of neutrophils activated with phorbol myristate acetate (PMA) but not with fMLP or opsonized zymosan. S-Nitrosoglutathione 53-57 brain protein 8 Mus musculus 87-89 20223829-5 2010 We characterized S-glutathionylation of A9; GSSG and GSNO generated S-glutathionylated A8 (A8-SSG) and A9 (A9-SSG) in vitro, whereas only A9-SSG was detected in cytosol of neutrophils activated with phorbol myristate acetate (PMA) but not with fMLP or opsonized zymosan. S-Nitrosoglutathione 53-57 brain protein 8 Mus musculus 91-97 20223829-5 2010 We characterized S-glutathionylation of A9; GSSG and GSNO generated S-glutathionylated A8 (A8-SSG) and A9 (A9-SSG) in vitro, whereas only A9-SSG was detected in cytosol of neutrophils activated with phorbol myristate acetate (PMA) but not with fMLP or opsonized zymosan. S-Nitrosoglutathione 53-57 UDP glucuronosyltransferase 1 family, polypeptide A6B Mus musculus 103-105 20223829-5 2010 We characterized S-glutathionylation of A9; GSSG and GSNO generated S-glutathionylated A8 (A8-SSG) and A9 (A9-SSG) in vitro, whereas only A9-SSG was detected in cytosol of neutrophils activated with phorbol myristate acetate (PMA) but not with fMLP or opsonized zymosan. S-Nitrosoglutathione 53-57 UDP glucuronosyltransferase 1 family, polypeptide A6B Mus musculus 107-113 20335826-4 2010 The enzyme, S-nitrosoglutathione reductase (GSNOR), which regulates levels of the endogenous bronchodilator S-nitrosoglutathione, has been shown to modulate the response to beta2-agonists. S-Nitrosoglutathione 12-32 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 44-49 20335826-4 2010 The enzyme, S-nitrosoglutathione reductase (GSNOR), which regulates levels of the endogenous bronchodilator S-nitrosoglutathione, has been shown to modulate the response to beta2-agonists. S-Nitrosoglutathione 12-32 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 173-178 20153346-7 2010 The inhibition of NADPH oxidase activation and Omi/HtrA2 by a pharmacological approach provided significant protection against caspase-3 activation and GSNO-induced cell death, confirming that GSNO triggers the death cascade in endothelial cells in a mitochondria-dependent manner. S-Nitrosoglutathione 152-156 HtrA serine peptidase 2 Homo sapiens 51-56 20153346-7 2010 The inhibition of NADPH oxidase activation and Omi/HtrA2 by a pharmacological approach provided significant protection against caspase-3 activation and GSNO-induced cell death, confirming that GSNO triggers the death cascade in endothelial cells in a mitochondria-dependent manner. S-Nitrosoglutathione 193-197 HtrA serine peptidase 2 Homo sapiens 51-56 20153346-7 2010 The inhibition of NADPH oxidase activation and Omi/HtrA2 by a pharmacological approach provided significant protection against caspase-3 activation and GSNO-induced cell death, confirming that GSNO triggers the death cascade in endothelial cells in a mitochondria-dependent manner. S-Nitrosoglutathione 193-197 caspase 3 Homo sapiens 127-136 19808678-4 2009 Hydrogen peroxide and GSNO treatment of IDE reduces the V(max) for Abeta degradation, increases IDE oligomerization, and decreases IDE thermostability. S-Nitrosoglutathione 22-26 insulin degrading enzyme Homo sapiens 96-99 20064573-3 2010 In the present study, we found that carboxy-terminal PDZ ligand of nNOS (CAPON) mainly located in the nucleus of astrocytes stimulated with NO donor sodium nitroprusside (SNP) or GSNO or N-methyl-d-aspartate (NMDA) receptor agonist-NMDA. S-Nitrosoglutathione 179-183 nitric oxide synthase 1 Homo sapiens 67-71 20064573-3 2010 In the present study, we found that carboxy-terminal PDZ ligand of nNOS (CAPON) mainly located in the nucleus of astrocytes stimulated with NO donor sodium nitroprusside (SNP) or GSNO or N-methyl-d-aspartate (NMDA) receptor agonist-NMDA. S-Nitrosoglutathione 179-183 nitric oxide synthase 1 adaptor protein Homo sapiens 73-78 20083653-7 2010 However, this restoration of Foxp3 by pharmacological drugs was reversed by S-nitrosoglutathione, an NO donor. S-Nitrosoglutathione 76-96 forkhead box P3 Homo sapiens 29-34 19879353-3 2010 In this mechanism, initial binding of glutathione to ferric cytochrome c is followed by reaction of NO with this complex, yielding ferrous cytochrome c and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 156-176 cytochrome c, somatic Homo sapiens 60-72 19879353-3 2010 In this mechanism, initial binding of glutathione to ferric cytochrome c is followed by reaction of NO with this complex, yielding ferrous cytochrome c and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 178-182 cytochrome c, somatic Homo sapiens 60-72 20431245-2 2010 Recent studies have shown that S-nitrosoglutathione (GSNO) reductase (GSNOR) catalyzes the degradation of GSNO and indirectly regulates the level of RSNO in vivo. S-Nitrosoglutathione 53-57 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 70-75 20609912-4 2010 This NO-dependent cell signaling pathway of the redox protein Trx may play a key role in the cellular protective mechanism of several potential neuroprotective agents such as S-nitrosoglutathione (GSNO), 17beta-estradiol, selegiline as well as ebeselen, sildenafil, and rasagiline. S-Nitrosoglutathione 175-195 thioredoxin Homo sapiens 62-65 20609912-4 2010 This NO-dependent cell signaling pathway of the redox protein Trx may play a key role in the cellular protective mechanism of several potential neuroprotective agents such as S-nitrosoglutathione (GSNO), 17beta-estradiol, selegiline as well as ebeselen, sildenafil, and rasagiline. S-Nitrosoglutathione 197-201 thioredoxin Homo sapiens 62-65 19808678-2 2009 Human IDE has 13 cysteines and is inhibited by hydrogen peroxide and S-nitrosoglutathione (GSNO), donors of reactive oxygen and nitrogen species, respectively. S-Nitrosoglutathione 69-89 insulin degrading enzyme Homo sapiens 6-9 19808678-2 2009 Human IDE has 13 cysteines and is inhibited by hydrogen peroxide and S-nitrosoglutathione (GSNO), donors of reactive oxygen and nitrogen species, respectively. S-Nitrosoglutathione 91-95 insulin degrading enzyme Homo sapiens 6-9 19808678-4 2009 Hydrogen peroxide and GSNO treatment of IDE reduces the V(max) for Abeta degradation, increases IDE oligomerization, and decreases IDE thermostability. S-Nitrosoglutathione 22-26 insulin degrading enzyme Homo sapiens 40-43 19963048-1 2010 Formaldehyde dehydrogenase, formally Class III alcohol dehydrogenase (ADH3), has recently been discovered to partially regulate nitrosothiol homeostasis by catalyzing the reduction of the endogenous nitrosylating agent S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 219-239 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-26 19963048-1 2010 Formaldehyde dehydrogenase, formally Class III alcohol dehydrogenase (ADH3), has recently been discovered to partially regulate nitrosothiol homeostasis by catalyzing the reduction of the endogenous nitrosylating agent S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 219-239 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 70-74 19963048-1 2010 Formaldehyde dehydrogenase, formally Class III alcohol dehydrogenase (ADH3), has recently been discovered to partially regulate nitrosothiol homeostasis by catalyzing the reduction of the endogenous nitrosylating agent S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 241-245 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-26 19963048-1 2010 Formaldehyde dehydrogenase, formally Class III alcohol dehydrogenase (ADH3), has recently been discovered to partially regulate nitrosothiol homeostasis by catalyzing the reduction of the endogenous nitrosylating agent S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 241-245 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 70-74 19963048-3 2010 While ADH3 has received considerable attention in the biomedical literature where it is often referred to as GSNO reductase (GSNOR), ADH3-mediated GSNO reduction has received comparatively less attention in the environmental toxicology community. S-Nitrosoglutathione 109-113 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 6-10 19963048-3 2010 While ADH3 has received considerable attention in the biomedical literature where it is often referred to as GSNO reductase (GSNOR), ADH3-mediated GSNO reduction has received comparatively less attention in the environmental toxicology community. S-Nitrosoglutathione 109-113 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 125-130 19808678-4 2009 Hydrogen peroxide and GSNO treatment of IDE reduces the V(max) for Abeta degradation, increases IDE oligomerization, and decreases IDE thermostability. S-Nitrosoglutathione 22-26 insulin degrading enzyme Homo sapiens 96-99 19808678-6 2009 Our mutational analysis of IDE and peptide mass fingerprinting of GSNO-treated IDE using Fourier transform-ion cyclotron resonance mass spectrometer reveal a surprising interplay of Cys-178 with Cys-110 and Cys-819 for catalytic activity and with Cys-789 and Cys-966 for oligomerization. S-Nitrosoglutathione 66-70 insulin degrading enzyme Homo sapiens 79-82 19765213-5 2009 RESULTS: S-nitrosoglutathione (GSNO) inhibited platelet aggregation on immobilized VWF under static and flow conditions, but had no effect on platelet adhesion. S-Nitrosoglutathione 9-29 von Willebrand factor Homo sapiens 83-86 19806166-1 2009 Metabolism of S-nitrosoglutathione (GSNO), a major biologically active nitric oxide (NO) species, is catalyzed by the evolutionally conserved GSNO reductase (GSNOR). S-Nitrosoglutathione 14-34 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 142-156 19806166-1 2009 Metabolism of S-nitrosoglutathione (GSNO), a major biologically active nitric oxide (NO) species, is catalyzed by the evolutionally conserved GSNO reductase (GSNOR). S-Nitrosoglutathione 14-34 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 158-163 19806166-1 2009 Metabolism of S-nitrosoglutathione (GSNO), a major biologically active nitric oxide (NO) species, is catalyzed by the evolutionally conserved GSNO reductase (GSNOR). S-Nitrosoglutathione 36-40 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 142-156 19806166-1 2009 Metabolism of S-nitrosoglutathione (GSNO), a major biologically active nitric oxide (NO) species, is catalyzed by the evolutionally conserved GSNO reductase (GSNOR). S-Nitrosoglutathione 36-40 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 158-163 20097961-8 2009 In addition, we found that conversion of SNOG was significantly accelerated by glutathione reductase (GTR). S-Nitrosoglutathione 41-45 glutathione-disulfide reductase Homo sapiens 79-100 20097961-8 2009 In addition, we found that conversion of SNOG was significantly accelerated by glutathione reductase (GTR). S-Nitrosoglutathione 41-45 glutathione-disulfide reductase Homo sapiens 102-105 19765213-5 2009 RESULTS: S-nitrosoglutathione (GSNO) inhibited platelet aggregation on immobilized VWF under static and flow conditions, but had no effect on platelet adhesion. S-Nitrosoglutathione 31-35 von Willebrand factor Homo sapiens 83-86 19643045-4 2009 Notably, an increase in GAPDH expression following GSNO treatment was detected in RGC-5 cells through Western blotting as well as proteomics. S-Nitrosoglutathione 51-55 glyceraldehyde-3-phosphate dehydrogenase Mus musculus 24-29 19747166-4 2009 The reaction of isolated myosin with S-nitrosoglutathione results in S-nitrosylation at multiple cysteine thiols and produces two populations of protein-bound SNOs with different stabilities. S-Nitrosoglutathione 37-57 myosin heavy chain 14 Homo sapiens 25-31 19889224-9 2009 RESULTS: Treatment of the TBI animals with GSNO reduced BBB disruption as evidenced by decreased Evan"s blue extravasation across brain, infiltration/activation of macrophages (ED1 positive cells), and reduced expression of ICAM-1 and MMP-9. S-Nitrosoglutathione 43-47 intercellular adhesion molecule 1 Rattus norvegicus 224-230 19889224-9 2009 RESULTS: Treatment of the TBI animals with GSNO reduced BBB disruption as evidenced by decreased Evan"s blue extravasation across brain, infiltration/activation of macrophages (ED1 positive cells), and reduced expression of ICAM-1 and MMP-9. S-Nitrosoglutathione 43-47 matrix metallopeptidase 9 Rattus norvegicus 235-240 19889224-10 2009 The GSNO treatment also restored CCI-mediated reduced expression of BBB integrity proteins ZO-1 and occludin. S-Nitrosoglutathione 4-8 tight junction protein 1 Rattus norvegicus 91-108 19889224-12 2009 GSNO-mediated reduced expression of iNOS in macrophages as well as decreased neuronal cell death may be responsible for the histological improvement and reduced exacerbations. S-Nitrosoglutathione 0-4 nitric oxide synthase 2 Rattus norvegicus 36-40 19596685-4 2009 We report three compounds that exclude GSNOR substrate, S-nitrosoglutathione (GSNO) from its binding site in GSNOR and cause an accumulation of SNOs inside the cells. S-Nitrosoglutathione 56-76 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 109-114 19596685-4 2009 We report three compounds that exclude GSNOR substrate, S-nitrosoglutathione (GSNO) from its binding site in GSNOR and cause an accumulation of SNOs inside the cells. S-Nitrosoglutathione 39-43 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 109-114 19809847-5 2009 Our results showed, when compared with control aliquots, that the presence of fibrinogen modulates the NO mobilization in erythrocytes by (1) decreasing erythrocyte NO efflux levels (P < 0.001); (2) increasing levels of intraerythrocytic NO oxidative metabolites, namely, nitrite (P < 0.0001) and nitrate (P < 0.0001); and (3) enhancing the formation of GSNO (P < 0.001). S-Nitrosoglutathione 363-367 fibrinogen beta chain Homo sapiens 78-88 19643045-5 2009 The increased GAPDH expression in response to GSNO treatment was accompanied by an increase in Herc6 protein, an E3 ubiquitin ligase. S-Nitrosoglutathione 46-50 glyceraldehyde-3-phosphate dehydrogenase Mus musculus 14-19 19643045-5 2009 The increased GAPDH expression in response to GSNO treatment was accompanied by an increase in Herc6 protein, an E3 ubiquitin ligase. S-Nitrosoglutathione 46-50 hect domain and RLD 6 Mus musculus 95-100 19349119-3 2009 In this study the polyacrylamide gel electrophoresis (PAGE) and nitroblue tetrazolium (NBT) photoreduction methods were used to analyze the effects of GSNO on the activities of lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G6PD), aconitase and superoxide dismutase (SOD). S-Nitrosoglutathione 151-155 ETH_00005300 Eimeria tenella 177-198 19428112-8 2009 These results, together with our previous report showing NO donor S-nitrosoglutathione (GSNO)-mediated neuroprotective effects against 3-NP toxicity, suggest that BDNF may protect neurons from mitochondrial dysfunction at least partly via activation of the signaling cascades involving NOS/NO, PKG, thioredoxin and Bcl-2. S-Nitrosoglutathione 66-86 brain derived neurotrophic factor Homo sapiens 163-167 19428112-8 2009 These results, together with our previous report showing NO donor S-nitrosoglutathione (GSNO)-mediated neuroprotective effects against 3-NP toxicity, suggest that BDNF may protect neurons from mitochondrial dysfunction at least partly via activation of the signaling cascades involving NOS/NO, PKG, thioredoxin and Bcl-2. S-Nitrosoglutathione 88-92 brain derived neurotrophic factor Homo sapiens 163-167 19349119-3 2009 In this study the polyacrylamide gel electrophoresis (PAGE) and nitroblue tetrazolium (NBT) photoreduction methods were used to analyze the effects of GSNO on the activities of lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G6PD), aconitase and superoxide dismutase (SOD). S-Nitrosoglutathione 151-155 ETH_00005300 Eimeria tenella 200-203 19349119-5 2009 The results showed that the activities of LDH, G6PD, aconitase and SOD in fresh unsporulated and sporulated oocysts could be distinctly detected after treatment by GSNO or without treatment. S-Nitrosoglutathione 164-168 ETH_00005300 Eimeria tenella 42-45 19325130-4 2009 We further show that S-nitrosylated HIF-1alpha binds to the vascular endothelial growth factor (VEGF) gene, thus identifying a role for GSNO in angiogenesis and myocardial protection. S-Nitrosoglutathione 136-140 hypoxia inducible factor 1, alpha subunit Mus musculus 36-46 19428350-0 2009 Medium-chain fatty acids and glutathione derivatives as inhibitors of S-nitrosoglutathione reduction mediated by alcohol dehydrogenase 3. S-Nitrosoglutathione 70-90 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 113-136 19428350-1 2009 Alcohol dehydrogenase 3 (ADH3) has emerged as an important regulator of protein S-nitrosation in its function as S-nitrosoglutathione (GSNO) reductase. S-Nitrosoglutathione 113-133 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 0-23 19428350-1 2009 Alcohol dehydrogenase 3 (ADH3) has emerged as an important regulator of protein S-nitrosation in its function as S-nitrosoglutathione (GSNO) reductase. S-Nitrosoglutathione 113-133 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 25-29 19428350-1 2009 Alcohol dehydrogenase 3 (ADH3) has emerged as an important regulator of protein S-nitrosation in its function as S-nitrosoglutathione (GSNO) reductase. S-Nitrosoglutathione 135-139 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 0-23 19428350-1 2009 Alcohol dehydrogenase 3 (ADH3) has emerged as an important regulator of protein S-nitrosation in its function as S-nitrosoglutathione (GSNO) reductase. S-Nitrosoglutathione 135-139 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 25-29 19428350-2 2009 GSNO depletion is associated with various disease conditions, emphasizing the potential value of a specific ADH3 inhibitor. S-Nitrosoglutathione 0-4 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 108-112 19428350-3 2009 The present study investigated inhibition of ADH3-mediated GSNO reduction by various substrate analogues, including medium-chain fatty acids and glutathione derivatives. S-Nitrosoglutathione 59-63 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 45-49 19428350-8 2009 The experimental results as well as docking simulations with GSNO and S-methylglutathione suggest that for ADH3 ligands with a glutathione scaffold, in contrast to fatty acids, a zinc-binding moiety is imperative for correct orientation and stabilization of the hydrophilic glutathione scaffold within a predominantly hydrophobic active site. S-Nitrosoglutathione 61-65 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 107-111 19357237-9 2009 Here we report studies of the effects of the NO donor S-nitrosoglutathione (GSNO) on the electrical properties and fluorescent-dye permeability of wild-type Cx46 and mutant hemichannels expressed in Xenopus laevis oocytes. S-Nitrosoglutathione 54-74 gap junction protein alpha 3 Homo sapiens 157-161 19357237-9 2009 Here we report studies of the effects of the NO donor S-nitrosoglutathione (GSNO) on the electrical properties and fluorescent-dye permeability of wild-type Cx46 and mutant hemichannels expressed in Xenopus laevis oocytes. S-Nitrosoglutathione 76-80 gap junction protein alpha 3 Homo sapiens 157-161 19357237-10 2009 GSNO enhanced hemichannel voltage sensitivity, increased tail-current amplitude, and changed activation and closing kinetics in Cx46 and Cx46-CT43 (Cx46 mutant in which the COOH terminus was replaced with that of Cx43), but not in Cx46-C3A (Cx46 in which the intracellular and transmembrane helix 4 cysteines were mutated to alanine). S-Nitrosoglutathione 0-4 gap junction protein alpha 3 Homo sapiens 128-132 19357237-10 2009 GSNO enhanced hemichannel voltage sensitivity, increased tail-current amplitude, and changed activation and closing kinetics in Cx46 and Cx46-CT43 (Cx46 mutant in which the COOH terminus was replaced with that of Cx43), but not in Cx46-C3A (Cx46 in which the intracellular and transmembrane helix 4 cysteines were mutated to alanine). S-Nitrosoglutathione 0-4 gap junction protein alpha 3 Homo sapiens 137-141 19357237-10 2009 GSNO enhanced hemichannel voltage sensitivity, increased tail-current amplitude, and changed activation and closing kinetics in Cx46 and Cx46-CT43 (Cx46 mutant in which the COOH terminus was replaced with that of Cx43), but not in Cx46-C3A (Cx46 in which the intracellular and transmembrane helix 4 cysteines were mutated to alanine). S-Nitrosoglutathione 0-4 gap junction protein alpha 3 Homo sapiens 137-141 19357237-10 2009 GSNO enhanced hemichannel voltage sensitivity, increased tail-current amplitude, and changed activation and closing kinetics in Cx46 and Cx46-CT43 (Cx46 mutant in which the COOH terminus was replaced with that of Cx43), but not in Cx46-C3A (Cx46 in which the intracellular and transmembrane helix 4 cysteines were mutated to alanine). S-Nitrosoglutathione 0-4 gap junction protein alpha 1 Homo sapiens 213-217 19357237-10 2009 GSNO enhanced hemichannel voltage sensitivity, increased tail-current amplitude, and changed activation and closing kinetics in Cx46 and Cx46-CT43 (Cx46 mutant in which the COOH terminus was replaced with that of Cx43), but not in Cx46-C3A (Cx46 in which the intracellular and transmembrane helix 4 cysteines were mutated to alanine). S-Nitrosoglutathione 0-4 gap junction protein alpha 3 Homo sapiens 137-141 19357237-10 2009 GSNO enhanced hemichannel voltage sensitivity, increased tail-current amplitude, and changed activation and closing kinetics in Cx46 and Cx46-CT43 (Cx46 mutant in which the COOH terminus was replaced with that of Cx43), but not in Cx46-C3A (Cx46 in which the intracellular and transmembrane helix 4 cysteines were mutated to alanine). S-Nitrosoglutathione 0-4 gap junction protein alpha 3 Homo sapiens 137-141 19325130-4 2009 We further show that S-nitrosylated HIF-1alpha binds to the vascular endothelial growth factor (VEGF) gene, thus identifying a role for GSNO in angiogenesis and myocardial protection. S-Nitrosoglutathione 136-140 vascular endothelial growth factor A Mus musculus 60-94 19325130-4 2009 We further show that S-nitrosylated HIF-1alpha binds to the vascular endothelial growth factor (VEGF) gene, thus identifying a role for GSNO in angiogenesis and myocardial protection. S-Nitrosoglutathione 136-140 vascular endothelial growth factor A Mus musculus 96-100 19082896-0 2009 Nonlinear cooperation of p53-ING1-induced bax expression and protein S-nitrosylation in GSNO-induced thymocyte apoptosis: a quantitative approach with cross-platform validation. S-Nitrosoglutathione 88-92 tumor protein p53 Homo sapiens 25-28 18820947-8 2009 GSNO produced the similar effects as cytokines on KKU-OCA17, in contrast, GSNO induced increase of NQO1 activity in HeLa Chang liver cells. S-Nitrosoglutathione 74-78 NAD(P)H quinone dehydrogenase 1 Homo sapiens 99-103 18820947-9 2009 The treatment of cytokines or GSNO suppressed expression of NQO1 in KKU-OCA17 and HeLa Chang liver cells. S-Nitrosoglutathione 30-34 NAD(P)H quinone dehydrogenase 1 Homo sapiens 60-64 19038239-12 2009 These findings provided evidence for formaldehyde-induced, ADH3-mediated GSNO depletion with potential direct implications for asthma. S-Nitrosoglutathione 73-77 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 59-63 19082896-0 2009 Nonlinear cooperation of p53-ING1-induced bax expression and protein S-nitrosylation in GSNO-induced thymocyte apoptosis: a quantitative approach with cross-platform validation. S-Nitrosoglutathione 88-92 inhibitor of growth family member 1 Homo sapiens 29-33 19119849-4 2009 Furthermore, low concentrations of GSNO caused a time-dependent loss in BCAT activity (50 +/- 3% and 77 +/- 2% for hBCATc and hBCATm, respectively) correlating with the loss of four and one to two thiol groups, respectively, confirming the thiols as targets for NO modification. S-Nitrosoglutathione 35-39 branched chain amino acid transaminase 1 Homo sapiens 115-121 18786560-5 2009 The Mrp proteins mediate not only GSH efflux, but they also export oxidized glutathione derivatives (e.g., glutathione disulfide (GSSG), S-nitrosoglutathione (GS-NO), and glutathione-metal complexes), as well as other glutathione S-conjugates. S-Nitrosoglutathione 137-157 ATP binding cassette subfamily C member 1 Homo sapiens 4-7 18786560-5 2009 The Mrp proteins mediate not only GSH efflux, but they also export oxidized glutathione derivatives (e.g., glutathione disulfide (GSSG), S-nitrosoglutathione (GS-NO), and glutathione-metal complexes), as well as other glutathione S-conjugates. S-Nitrosoglutathione 159-164 ATP binding cassette subfamily C member 1 Homo sapiens 4-7 19119849-4 2009 Furthermore, low concentrations of GSNO caused a time-dependent loss in BCAT activity (50 +/- 3% and 77 +/- 2% for hBCATc and hBCATm, respectively) correlating with the loss of four and one to two thiol groups, respectively, confirming the thiols as targets for NO modification. S-Nitrosoglutathione 35-39 branched chain amino acid transaminase 2 Homo sapiens 126-132 19119849-5 2009 Analysis of GSNO-modified hBCATc by quadrupole time-of-flight mass spectrometry identified a major peak containing three NO adducts and a minor peak equivalent to two NO adducts and one glutathione (GSH) molecule, the latter confirmed by Western blot analysis. S-Nitrosoglutathione 12-16 branched chain amino acid transaminase 1 Homo sapiens 26-32 19119849-6 2009 Moreover, prolonged exposure or increased levels of GSNO caused increased S-glutathionylation and partial dimerization of hBCATc, suggesting a possible shift from regulation by NO to one of adaptation during nitrosated stress. S-Nitrosoglutathione 52-56 branched chain amino acid transaminase 1 Homo sapiens 122-128 19119849-7 2009 Although GSNO inactivated hBCATm, neither S-nitrosation, S-glutathionylation, nor dimerization could be detected, suggesting differential mechanisms of regulation through NO between isoforms in the mitochondria and cytosol. S-Nitrosoglutathione 9-13 branched chain amino acid transaminase 2 Homo sapiens 26-32 19000649-0 2009 A kinetic study of gamma-glutamyltransferase (GGT)-mediated S-nitrosoglutathione catabolism. S-Nitrosoglutathione 60-80 inactive glutathione hydrolase 2 Homo sapiens 46-49 19000649-2 2009 It is known that gamma-glutamyl transpeptidase (GGT) is one of the enzymes involved in the enzyme-mediated decomposition of GSNO, but no kinetics studies of the reaction GSNO-GGT are reported in literature. S-Nitrosoglutathione 170-174 inactive glutathione hydrolase 2 Homo sapiens 175-178 19000649-2 2009 It is known that gamma-glutamyl transpeptidase (GGT) is one of the enzymes involved in the enzyme-mediated decomposition of GSNO, but no kinetics studies of the reaction GSNO-GGT are reported in literature. S-Nitrosoglutathione 124-128 inactive glutathione hydrolase 2 Homo sapiens 17-46 19000649-3 2009 In this study we directly investigated the kinetics of GGT with respect to GSNO as a substrate and glycyl-glycine (GG) as acceptor co-substrate by spectrophotometry at 334 nm. S-Nitrosoglutathione 75-79 inactive glutathione hydrolase 2 Homo sapiens 55-58 19000649-2 2009 It is known that gamma-glutamyl transpeptidase (GGT) is one of the enzymes involved in the enzyme-mediated decomposition of GSNO, but no kinetics studies of the reaction GSNO-GGT are reported in literature. S-Nitrosoglutathione 124-128 inactive glutathione hydrolase 2 Homo sapiens 48-51 19000649-4 2009 GGT hydrolyses the gamma-glutamyl moiety of GSNO to give S-nitroso-cysteinylglycine (CGNO) and gamma-glutamyl-GG. S-Nitrosoglutathione 44-48 inactive glutathione hydrolase 2 Homo sapiens 0-3 19000649-2 2009 It is known that gamma-glutamyl transpeptidase (GGT) is one of the enzymes involved in the enzyme-mediated decomposition of GSNO, but no kinetics studies of the reaction GSNO-GGT are reported in literature. S-Nitrosoglutathione 124-128 inactive glutathione hydrolase 2 Homo sapiens 175-178 19000649-6 2009 The ancillary reaction allowed us to study directly the GSNO/GGT kinetics by following the decrease of the characteristic absorbance of nitrosothiols at 334 nm. S-Nitrosoglutathione 56-60 inactive glutathione hydrolase 2 Homo sapiens 61-64 19000649-7 2009 A K(m) of GGT for GSNO of 0.398+/-31 mM was thus found, comparable with K(m) values reported for other gamma-glutamyl substrates of GGT. S-Nitrosoglutathione 18-22 inactive glutathione hydrolase 2 Homo sapiens 10-13 19000649-2 2009 It is known that gamma-glutamyl transpeptidase (GGT) is one of the enzymes involved in the enzyme-mediated decomposition of GSNO, but no kinetics studies of the reaction GSNO-GGT are reported in literature. S-Nitrosoglutathione 170-174 inactive glutathione hydrolase 2 Homo sapiens 17-46 19000649-2 2009 It is known that gamma-glutamyl transpeptidase (GGT) is one of the enzymes involved in the enzyme-mediated decomposition of GSNO, but no kinetics studies of the reaction GSNO-GGT are reported in literature. S-Nitrosoglutathione 170-174 inactive glutathione hydrolase 2 Homo sapiens 48-51 18841476-7 2008 It has also been found that GSNO-mediated accumulation of p53 depends on activation of ASK1 since no GSNO-induced p53 stabilisation was observed in THP-1 cells transfected with dominant-negative form of this kinase. S-Nitrosoglutathione 28-32 tumor protein p53 Homo sapiens 58-61 19053230-4 2008 Rather, activation and S-nitrosylation of RyR2 required S-nitrosoglutathione. S-Nitrosoglutathione 56-76 ryanodine receptor 2 Homo sapiens 42-46 19053230-6 2008 Our results indicate that both RyR1 and RyR2 are pO(2)-responsive yet point to different mechanisms by which NO and S-nitrosoglutathione influence cardiac and skeletal muscle sarcoplasmic reticulum Ca(2+) release. S-Nitrosoglutathione 116-136 ryanodine receptor 1 Homo sapiens 31-35 19053230-6 2008 Our results indicate that both RyR1 and RyR2 are pO(2)-responsive yet point to different mechanisms by which NO and S-nitrosoglutathione influence cardiac and skeletal muscle sarcoplasmic reticulum Ca(2+) release. S-Nitrosoglutathione 116-136 ryanodine receptor 2 Homo sapiens 40-44 18841476-3 2008 In this study we have found that NO derived from S-nitrosoglutathione (GSNO) activates ASK1 in THP-1 human myeloid macrophages in a concentration and time-dependent manner. S-Nitrosoglutathione 49-69 mitogen-activated protein kinase kinase kinase 5 Homo sapiens 87-91 18841476-3 2008 In this study we have found that NO derived from S-nitrosoglutathione (GSNO) activates ASK1 in THP-1 human myeloid macrophages in a concentration and time-dependent manner. S-Nitrosoglutathione 49-69 GLI family zinc finger 2 Homo sapiens 95-100 19296407-6 2009 Further, modification of recombinant human lens ALDH1A1 with nitric oxide donors such as S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione (GSNO) significantly inhibited the enzyme activity. S-Nitrosoglutathione 132-152 aldehyde dehydrogenase 1 family member A1 Homo sapiens 48-55 19258725-5 2009 p38 inhibitors also reduced neuronal death induced by the NO donor S-nitrosoglutathione. S-Nitrosoglutathione 67-87 mitogen-activated protein kinase 14 Homo sapiens 0-3 18826943-6 2008 We further demonstrate that the structural isostere of HMGSH, S-nitrosoglutathione, is an ideal hCBR1 substrate (Km = 30 microm, kcat = 450 min(-1)) with kinetic constants comparable with the best known hCBR1 substrates. S-Nitrosoglutathione 62-82 carbonyl reductase 1 Homo sapiens 96-101 18826943-6 2008 We further demonstrate that the structural isostere of HMGSH, S-nitrosoglutathione, is an ideal hCBR1 substrate (Km = 30 microm, kcat = 450 min(-1)) with kinetic constants comparable with the best known hCBR1 substrates. S-Nitrosoglutathione 62-82 carbonyl reductase 1 Homo sapiens 203-208 18826943-7 2008 Furthermore, we demonstrate that hCBR1 dependent GSNO reduction occurs in A549 lung adenocarcinoma cell lysates and suggest that hCBR1 may be involved in regulation of tissue levels of GSNO. S-Nitrosoglutathione 49-53 carbonyl reductase 1 Homo sapiens 33-38 18826943-7 2008 Furthermore, we demonstrate that hCBR1 dependent GSNO reduction occurs in A549 lung adenocarcinoma cell lysates and suggest that hCBR1 may be involved in regulation of tissue levels of GSNO. S-Nitrosoglutathione 49-53 carbonyl reductase 1 Homo sapiens 129-134 18826943-7 2008 Furthermore, we demonstrate that hCBR1 dependent GSNO reduction occurs in A549 lung adenocarcinoma cell lysates and suggest that hCBR1 may be involved in regulation of tissue levels of GSNO. S-Nitrosoglutathione 185-189 carbonyl reductase 1 Homo sapiens 33-38 18826943-7 2008 Furthermore, we demonstrate that hCBR1 dependent GSNO reduction occurs in A549 lung adenocarcinoma cell lysates and suggest that hCBR1 may be involved in regulation of tissue levels of GSNO. S-Nitrosoglutathione 185-189 carbonyl reductase 1 Homo sapiens 129-134 18841476-3 2008 In this study we have found that NO derived from S-nitrosoglutathione (GSNO) activates ASK1 in THP-1 human myeloid macrophages in a concentration and time-dependent manner. S-Nitrosoglutathione 71-75 mitogen-activated protein kinase kinase kinase 5 Homo sapiens 87-91 18841476-3 2008 In this study we have found that NO derived from S-nitrosoglutathione (GSNO) activates ASK1 in THP-1 human myeloid macrophages in a concentration and time-dependent manner. S-Nitrosoglutathione 71-75 GLI family zinc finger 2 Homo sapiens 95-100 18841476-4 2008 It also induces accumulation of HIF-1alpha protein in a concentration-dependent manner, which peaks at 4 h of exposure to 1 mM GSNO. S-Nitrosoglutathione 127-131 hypoxia inducible factor 1 subunit alpha Homo sapiens 32-42 18841476-6 2008 In addition, GSNO was found to induce accumulation of p53 in normal but not HIF-1alpha knockdown THP-1 cells, where expression of this protein was silenced by specific siRNA. S-Nitrosoglutathione 13-17 tumor protein p53 Homo sapiens 54-57 18841476-7 2008 It has also been found that GSNO-mediated accumulation of p53 depends on activation of ASK1 since no GSNO-induced p53 stabilisation was observed in THP-1 cells transfected with dominant-negative form of this kinase. S-Nitrosoglutathione 28-32 mitogen-activated protein kinase kinase kinase 5 Homo sapiens 87-91 18841476-8 2008 However, in both HIF-1alpha knockdown THP-1 cells and those transfected with the dominant-negative form of ASK1, GSNO was able to induce cell death as detected by the MTS cell viability assay leading to an increase in release of LDH. S-Nitrosoglutathione 113-117 hypoxia inducible factor 1 subunit alpha Homo sapiens 17-27 18841476-8 2008 However, in both HIF-1alpha knockdown THP-1 cells and those transfected with the dominant-negative form of ASK1, GSNO was able to induce cell death as detected by the MTS cell viability assay leading to an increase in release of LDH. S-Nitrosoglutathione 113-117 GLI family zinc finger 2 Homo sapiens 38-43 18841476-8 2008 However, in both HIF-1alpha knockdown THP-1 cells and those transfected with the dominant-negative form of ASK1, GSNO was able to induce cell death as detected by the MTS cell viability assay leading to an increase in release of LDH. S-Nitrosoglutathione 113-117 mitogen-activated protein kinase kinase kinase 5 Homo sapiens 107-111 18544525-6 2008 We found that S-nitrosoglutathione-mediated S-nitrosylation at physiological pH is critically dependent on the redox state of Trx. S-Nitrosoglutathione 14-34 thioredoxin Homo sapiens 126-129 19011746-4 2008 Through the GSNO reductase activity, ADH3 can affect the transnitrosation equilibrium between GSNO and S-nitrosated proteins, arguing for an important role in NO homeostasis. S-Nitrosoglutathione 12-16 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 37-41 19011746-5 2008 Recent findings suggest that ADH3-mediated GSNO reduction and subsequent product formation responds to redox states in terms of NADH availability and glutathione levels. S-Nitrosoglutathione 43-47 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 29-33 18786557-0 2008 Thioredoxin-1 promotes survival in cells exposed to S-nitrosoglutathione: Correlation with reduction of intracellular levels of nitrosothiols and up-regulation of the ERK1/2 MAP Kinases. S-Nitrosoglutathione 52-72 thioredoxin Homo sapiens 0-13 18786557-0 2008 Thioredoxin-1 promotes survival in cells exposed to S-nitrosoglutathione: Correlation with reduction of intracellular levels of nitrosothiols and up-regulation of the ERK1/2 MAP Kinases. S-Nitrosoglutathione 52-72 mitogen-activated protein kinase 3 Homo sapiens 167-173 18786557-6 2008 A role for TRX-1 expression on GSNO catabolism and cell viability was demonstrated by the concentration-dependent effects of GSNO on decreasing TRX-1 expression, activation of caspase-3, and increasing cell death. S-Nitrosoglutathione 31-35 thioredoxin Homo sapiens 11-16 18786557-6 2008 A role for TRX-1 expression on GSNO catabolism and cell viability was demonstrated by the concentration-dependent effects of GSNO on decreasing TRX-1 expression, activation of caspase-3, and increasing cell death. S-Nitrosoglutathione 125-129 thioredoxin Homo sapiens 11-16 18786557-6 2008 A role for TRX-1 expression on GSNO catabolism and cell viability was demonstrated by the concentration-dependent effects of GSNO on decreasing TRX-1 expression, activation of caspase-3, and increasing cell death. S-Nitrosoglutathione 125-129 thioredoxin Homo sapiens 144-149 18786557-6 2008 A role for TRX-1 expression on GSNO catabolism and cell viability was demonstrated by the concentration-dependent effects of GSNO on decreasing TRX-1 expression, activation of caspase-3, and increasing cell death. S-Nitrosoglutathione 125-129 caspase 3 Homo sapiens 176-185 18786557-7 2008 The over-expression of TRX-1 in HeLa cells partially attenuated caspase-3 activation and enhanced cell viability upon GSNO treatment. S-Nitrosoglutathione 118-122 thioredoxin Homo sapiens 23-28 18786557-11 2008 In cells over-expressing TRX-1, basal phosphorylation levels of ERK1/2 MAP kinases were higher and further increased after GSNO treatment. S-Nitrosoglutathione 123-127 thioredoxin Homo sapiens 25-30 18786557-11 2008 In cells over-expressing TRX-1, basal phosphorylation levels of ERK1/2 MAP kinases were higher and further increased after GSNO treatment. S-Nitrosoglutathione 123-127 mitogen-activated protein kinase 3 Homo sapiens 64-70 18816065-11 2008 278, 14607-14613], hGrx2 catalyzes glutathione-thiyl radical (GS (*)) scavenging, and it also mediates GS transfer (protein S-glutathionylation) reactions, where GS (*) serves as a superior glutathionyl donor substrate for formation of GAPDH-SSG, compared to GSNO and GSSG. S-Nitrosoglutathione 259-263 glutaredoxin 2 Homo sapiens 19-24 18635760-4 2008 We report that S-nitrosylation of NPR1 by S-nitrosoglutathione (GSNO) at cysteine-156 facilitates its oligomerization, which maintains protein homeostasis upon SA induction. S-Nitrosoglutathione 42-62 natriuretic peptide receptor 1 Homo sapiens 34-38 18635760-4 2008 We report that S-nitrosylation of NPR1 by S-nitrosoglutathione (GSNO) at cysteine-156 facilitates its oligomerization, which maintains protein homeostasis upon SA induction. S-Nitrosoglutathione 64-68 natriuretic peptide receptor 1 Homo sapiens 34-38 18635760-7 2008 Thus, the regulation of NPR1 is through the opposing action of GSNO and TRX. S-Nitrosoglutathione 63-67 natriuretic peptide receptor 1 Homo sapiens 24-28 18544525-8 2008 Treatment of a two-disulfide form of Trx1 with S-nitrosoglutathione resulted in nitrosylation of Cys(73), which can act as a trans-nitrosylating agent as observed by others to control caspase 3 activity (Mitchell, D. A., and Marletta, M. A. S-Nitrosoglutathione 47-67 thioredoxin Homo sapiens 37-41 18544525-8 2008 Treatment of a two-disulfide form of Trx1 with S-nitrosoglutathione resulted in nitrosylation of Cys(73), which can act as a trans-nitrosylating agent as observed by others to control caspase 3 activity (Mitchell, D. A., and Marletta, M. A. S-Nitrosoglutathione 47-67 caspase 3 Homo sapiens 184-193 18412547-0 2008 Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate alcohols via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors. S-Nitrosoglutathione 13-33 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 37-60 18412547-7 2008 Hence, considering the high cytosolic NAD(+)/NADH ratio, formaldehyde probably triggers ADH3-mediated GSNO reduction by enzyme-bound cofactor recycling and might result in a decrease in cellular S-NO (S-nitrosothiol) content in vivo. S-Nitrosoglutathione 102-106 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 88-92 18458510-7 2008 GSNO was also shown to preserve the aggregability of frozen platelets because in the presence of GSNO the delta percent change of P-selectin expression and fibrinogen binding of frozen platelets increased significantly irrelevant to DMSO. S-Nitrosoglutathione 0-4 selectin P Homo sapiens 130-140 18670085-6 2008 Further studies showed that AK1 activity in the rat heart extracts was significantly inhibited by GSNO but not oxidized glutathione (GSSG), and the inhibition was completely reversed by dithiothreitol (DTT) post-treatment, demonstrating that S-nitrosylation might serve as a new regulatory mechanism in controlling AK1 activity. S-Nitrosoglutathione 98-102 adenylate kinase 1 Rattus norvegicus 28-31 18298409-3 2008 The addition of GSSG, and much more efficiently of S-nitrosoglutathione, was shown to inactivate the enzymes from Arabidopsis thaliana (isoforms GapC1 and 2), spinach, yeast and rabbit muscle. S-Nitrosoglutathione 51-71 glyceraldehyde-3-phosphate dehydrogenase C subunit 1 Arabidopsis thaliana 145-156 18325324-0 2008 The nitric oxide-sensitive p21Ras-ERK pathway mediates S-nitrosoglutathione-induced apoptosis. S-Nitrosoglutathione 55-75 HRas proto-oncogene, GTPase Homo sapiens 27-33 18325324-0 2008 The nitric oxide-sensitive p21Ras-ERK pathway mediates S-nitrosoglutathione-induced apoptosis. S-Nitrosoglutathione 55-75 mitogen-activated protein kinase 1 Homo sapiens 34-37 18325324-3 2008 In this study, we demonstrated that the p21Ras-ERK pathway regulates THP-1 monocyte/macrophage apoptosis induced by S-nitrosoglutathione (SNOG). S-Nitrosoglutathione 116-136 HRas proto-oncogene, GTPase Homo sapiens 40-46 18325324-3 2008 In this study, we demonstrated that the p21Ras-ERK pathway regulates THP-1 monocyte/macrophage apoptosis induced by S-nitrosoglutathione (SNOG). S-Nitrosoglutathione 116-136 mitogen-activated protein kinase 1 Homo sapiens 47-50 18325324-3 2008 In this study, we demonstrated that the p21Ras-ERK pathway regulates THP-1 monocyte/macrophage apoptosis induced by S-nitrosoglutathione (SNOG). S-Nitrosoglutathione 138-142 HRas proto-oncogene, GTPase Homo sapiens 40-46 18325324-3 2008 In this study, we demonstrated that the p21Ras-ERK pathway regulates THP-1 monocyte/macrophage apoptosis induced by S-nitrosoglutathione (SNOG). S-Nitrosoglutathione 138-142 mitogen-activated protein kinase 1 Homo sapiens 47-50 18325324-6 2008 It was observed that only the activation of ERK1/2 MAP kinases by SNOG in THP-1 cells was attributable to p21Ras. S-Nitrosoglutathione 66-70 mitogen-activated protein kinase 3 Homo sapiens 44-50 18325324-6 2008 It was observed that only the activation of ERK1/2 MAP kinases by SNOG in THP-1 cells was attributable to p21Ras. S-Nitrosoglutathione 66-70 HRas proto-oncogene, GTPase Homo sapiens 106-112 18325324-7 2008 The inhibition of the ERK pathway by PD98059 markedly attenuated apoptosis in SNOG-treated THP-1 cells, but had a marginal effect on SNOG-treated THP-1 cells expressing NO-insensitive p21Ras. S-Nitrosoglutathione 78-82 mitogen-activated protein kinase 1 Homo sapiens 22-25 18325324-11 2008 These results indicate that the redox sensitive p21Ras-ERK pathway plays a critical role in sensing and delivering the pro-apoptotic signaling mediated by SNOG. S-Nitrosoglutathione 155-159 HRas proto-oncogene, GTPase Homo sapiens 48-54 18325324-11 2008 These results indicate that the redox sensitive p21Ras-ERK pathway plays a critical role in sensing and delivering the pro-apoptotic signaling mediated by SNOG. S-Nitrosoglutathione 155-159 mitogen-activated protein kinase 1 Homo sapiens 55-58 18458510-7 2008 GSNO was also shown to preserve the aggregability of frozen platelets because in the presence of GSNO the delta percent change of P-selectin expression and fibrinogen binding of frozen platelets increased significantly irrelevant to DMSO. S-Nitrosoglutathione 0-4 fibrinogen beta chain Homo sapiens 156-166 18458510-7 2008 GSNO was also shown to preserve the aggregability of frozen platelets because in the presence of GSNO the delta percent change of P-selectin expression and fibrinogen binding of frozen platelets increased significantly irrelevant to DMSO. S-Nitrosoglutathione 97-101 selectin P Homo sapiens 130-140 18204475-5 2008 KEY RESULTS: GSNO stimulated PDE5 phosphorylation and activity and increased cGMP levels in gastric smooth muscle cells. S-Nitrosoglutathione 13-17 phosphodiesterase 5A Homo sapiens 29-33 18204475-6 2008 Concurrent activation of cells with ACh augmented GSNO-stimulated PDE5 phosphorylation and activity, and attenuated cGMP levels. S-Nitrosoglutathione 50-54 phosphodiesterase 5A Homo sapiens 66-70 18097950-2 2008 Recent studies on asthma and airway biology implicate changes in nitric oxide (NO) disposition in the adverse effects of formaldehyde, principally because enzymatic reduction of the endogenous bronchodilator S-nitrosoglutathione (GSNO) is dependent upon GSNO reductase (formally designated as alcohol dehydrogenase-3, ADH3), which also serves as the primary enzyme for cellular detoxification of formaldehyde. S-Nitrosoglutathione 208-228 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 318-322 18029351-6 2008 The addition of the NO donor, S-nitrosoglutathione, to isolated cell lysates or purified recombinant human cPLA(2)alpha protein induced S-nitrosylation of cPLA(2)alpha in vitro. S-Nitrosoglutathione 30-50 phospholipase A2 group IVA Homo sapiens 107-119 18029351-6 2008 The addition of the NO donor, S-nitrosoglutathione, to isolated cell lysates or purified recombinant human cPLA(2)alpha protein induced S-nitrosylation of cPLA(2)alpha in vitro. S-Nitrosoglutathione 30-50 phospholipase A2 group IVA Homo sapiens 155-167 18326829-3 2008 HOT5 encodes S-nitrosoglutathione reductase (GSNOR), which metabolizes the NO adduct S-nitrosoglutathione. S-Nitrosoglutathione 13-33 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-4 18326829-3 2008 HOT5 encodes S-nitrosoglutathione reductase (GSNOR), which metabolizes the NO adduct S-nitrosoglutathione. S-Nitrosoglutathione 13-33 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 45-50 18171019-0 2008 Reaction of the XPA zinc finger with S-nitrosoglutathione. S-Nitrosoglutathione 37-57 XPA, DNA damage recognition and repair factor Homo sapiens 16-19 18171019-3 2008 In this study, we focused on a GSNO reaction with a Cys4 zinc finger (ZF) sequence of human protein XPA, crucial to the nucleotide excision repair pathway of DNA repair. S-Nitrosoglutathione 31-35 XPA, DNA damage recognition and repair factor Homo sapiens 100-103 18097950-3 2008 Considering recent evidence that regulation of bronchodilators like GSNO might play a more important role in asthma than inflammation per se, formaldehyde also needs to be considered as influencing ADH3-mediated GSNO catabolism. S-Nitrosoglutathione 68-72 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 198-202 18097950-3 2008 Considering recent evidence that regulation of bronchodilators like GSNO might play a more important role in asthma than inflammation per se, formaldehyde also needs to be considered as influencing ADH3-mediated GSNO catabolism. S-Nitrosoglutathione 212-216 alcohol dehydrogenase 1C (class I), gamma polypeptide Homo sapiens 198-202 18059133-6 2007 Moreover, the NOS inhibitor (L-NAME) and a NO-dependent cyclic GMP cascade inhibitor (ODQ) reduced SOD1 aggregation, whereas an exogenous NO donor (GSNO) increased mutant SOD1 aggregation, which was also prevented by NOS or cGMP cascade inhibitor. S-Nitrosoglutathione 148-152 superoxide dismutase 1 Homo sapiens 171-175 19017469-12 2008 The increase in catalase activity due to incubation with GSNO was not found in a strain defective in Yap1p, a master regulator of yeast adaptive response to oxidative stress. S-Nitrosoglutathione 57-61 DNA-binding transcription factor YAP1 Saccharomyces cerevisiae S288C 101-106 18069763-7 2007 Treatment with GSNO for 2-48 h reduced NAT1 activity without affecting the GSH ratio. S-Nitrosoglutathione 15-19 N-acetyltransferase 1 Homo sapiens 39-43 18069763-8 2007 Moreover, inflammatory cytokines and GSNO suppressed NAT1 mRNA expression. S-Nitrosoglutathione 37-41 N-acetyltransferase 1 Homo sapiens 53-57 19017469-13 2008 The obtained data demonstrate that exposure of yeast cells to the *NO-donor S-nitrosoglutathione induced mild oxidative/nitrosative stress and Yap1p may co-ordinate the up-regulation of antioxidant enzymes under these conditions. S-Nitrosoglutathione 76-96 Yes1 associated transcriptional regulator Homo sapiens 143-148 17892445-6 2007 On the other hand, exogenous application of the NO donor S-nitrosoglutathione enhanced the accumulation of FER, LeFRO1 and LeIRT1 mRNA in roots of iron-deficient plants. S-Nitrosoglutathione 57-77 ferric-chelate reductase Solanum lycopersicum 112-118 17869219-9 2007 Co-stimulation with the NO donor SNOG at concentrations of 0, 100, 300 and 600 microM reduced in a concentration dependent way the PHA-induced upregulation of WT1 that correlated with a reduction in T cell proliferation. S-Nitrosoglutathione 33-37 WT1 transcription factor Homo sapiens 159-162 17576200-4 2007 Furthermore, the NO-donor GSNO (S-nitrosogluthathione) induces NO-mediated modification of GLO1 and enhances the TNF-induced phosphorylation of this NO-responsive form. S-Nitrosoglutathione 26-30 glyoxalase I Homo sapiens 91-95 17576200-4 2007 Furthermore, the NO-donor GSNO (S-nitrosogluthathione) induces NO-mediated modification of GLO1 and enhances the TNF-induced phosphorylation of this NO-responsive form. S-Nitrosoglutathione 26-30 tumor necrosis factor Homo sapiens 113-116 17576200-5 2007 GSNO also strongly promotes TNF-induced cell death. S-Nitrosoglutathione 0-4 tumor necrosis factor Homo sapiens 28-31 17850672-11 2007 The IL-8 inducing effects of DFO were mediated by a nitric oxide donor (S-nitrosoglutathione), and by pyrrolidine dithiocarbamate, an inhibitor of NF-kappaB, as well as by wortmannin, which inhibits the phosphatidylinositol 3-kinase-dependent activation of NAD(P)H oxidase. S-Nitrosoglutathione 74-92 C-X-C motif chemokine ligand 8 Homo sapiens 4-8 17541013-0 2007 Akt-mediated activation of HIF-1 in pulmonary vascular endothelial cells by S-nitrosoglutathione. S-Nitrosoglutathione 76-96 AKT serine/threonine kinase 1 Homo sapiens 0-3 17541013-0 2007 Akt-mediated activation of HIF-1 in pulmonary vascular endothelial cells by S-nitrosoglutathione. S-Nitrosoglutathione 76-96 hypoxia inducible factor 1 subunit alpha Homo sapiens 27-32 17541013-1 2007 S-nitrosoglutathione (GSNO) stabilizes the alpha-subunit of hypoxia inducible factor-1 (HIF-1) in normoxic cells, but not in the presence of PI3K inhibitors. S-Nitrosoglutathione 0-20 hypoxia inducible factor 1 subunit alpha Homo sapiens 88-93 17541013-1 2007 S-nitrosoglutathione (GSNO) stabilizes the alpha-subunit of hypoxia inducible factor-1 (HIF-1) in normoxic cells, but not in the presence of PI3K inhibitors. S-Nitrosoglutathione 22-26 hypoxia inducible factor 1 subunit alpha Homo sapiens 88-93 17541013-2 2007 In this report, the biochemical pathway by which GSNO alters PI3K/Akt activity to modify HIF-1 expression was characterized in Cos cells and primary pulmonary vascular endothelial cells. S-Nitrosoglutathione 49-53 AKT serine/threonine kinase 1 Homo sapiens 66-69 17541013-2 2007 In this report, the biochemical pathway by which GSNO alters PI3K/Akt activity to modify HIF-1 expression was characterized in Cos cells and primary pulmonary vascular endothelial cells. S-Nitrosoglutathione 49-53 hypoxia inducible factor 1 subunit alpha Homo sapiens 89-94 17541013-3 2007 GSNO increased Akt kinase activity--and downstream HIF-1alpha protein accumulation and DNA-binding activity--in a dose- and time-dependent manner. S-Nitrosoglutathione 0-4 AKT serine/threonine kinase 1 Homo sapiens 15-18 17541013-3 2007 GSNO increased Akt kinase activity--and downstream HIF-1alpha protein accumulation and DNA-binding activity--in a dose- and time-dependent manner. S-Nitrosoglutathione 0-4 hypoxia inducible factor 1 subunit alpha Homo sapiens 51-61 17541013-6 2007 GSNO-induced Akt kinase activity and downstream HIF-1alpha stabilization were blocked by acivicin, an inhibitor of gamma-glutamyl transpeptidase (gammaGT), a transmembrane protein that can translate extracellular GSNO to intracellular S-nitrosocysteinylglycine. S-Nitrosoglutathione 0-4 AKT serine/threonine kinase 1 Homo sapiens 13-16 17541013-6 2007 GSNO-induced Akt kinase activity and downstream HIF-1alpha stabilization were blocked by acivicin, an inhibitor of gamma-glutamyl transpeptidase (gammaGT), a transmembrane protein that can translate extracellular GSNO to intracellular S-nitrosocysteinylglycine. S-Nitrosoglutathione 0-4 hypoxia inducible factor 1 subunit alpha Homo sapiens 48-58 17541013-6 2007 GSNO-induced Akt kinase activity and downstream HIF-1alpha stabilization were blocked by acivicin, an inhibitor of gamma-glutamyl transpeptidase (gammaGT), a transmembrane protein that can translate extracellular GSNO to intracellular S-nitrosocysteinylglycine. S-Nitrosoglutathione 0-4 inactive glutathione hydrolase 2 Homo sapiens 115-144 17541013-6 2007 GSNO-induced Akt kinase activity and downstream HIF-1alpha stabilization were blocked by acivicin, an inhibitor of gamma-glutamyl transpeptidase (gammaGT), a transmembrane protein that can translate extracellular GSNO to intracellular S-nitrosocysteinylglycine. S-Nitrosoglutathione 213-217 AKT serine/threonine kinase 1 Homo sapiens 13-16 17541013-6 2007 GSNO-induced Akt kinase activity and downstream HIF-1alpha stabilization were blocked by acivicin, an inhibitor of gamma-glutamyl transpeptidase (gammaGT), a transmembrane protein that can translate extracellular GSNO to intracellular S-nitrosocysteinylglycine. S-Nitrosoglutathione 213-217 inactive glutathione hydrolase 2 Homo sapiens 115-144 17664146-1 2007 The Cu,Zn-superoxide dismutase (SOD1) has been reported to exert an S-nitrosylated glutathione (GSNO) denitrosylase activity that was augmented by a familial amyotrophic lateral sclerosis (FALS)-associated mutation in this enzyme. S-Nitrosoglutathione 96-100 superoxide dismutase 1 Homo sapiens 32-36 17541013-7 2007 Dithiothreitol blocked GSNO-induced Akt kinase activity and HIF-1alpha stabilization. S-Nitrosoglutathione 23-27 AKT serine/threonine kinase 1 Homo sapiens 36-39 17541013-7 2007 Dithiothreitol blocked GSNO-induced Akt kinase activity and HIF-1alpha stabilization. S-Nitrosoglutathione 23-27 hypoxia inducible factor 1 subunit alpha Homo sapiens 60-70 17541013-8 2007 Moreover, the 3"-phosphatase of phosphoinositides, PTEN (phosphatase and tensin homolog deleted on chromosome ten) was S-nitrosylated by GSNO in pulmonary arterial endothelial cells, which was reversed by dithiothreitol and ultraviolet light. S-Nitrosoglutathione 137-141 phosphatase and tensin homolog Homo sapiens 51-55 17541013-10 2007 Taken together, these results suggest that GSNO induction of Akt appears to be mediated by S-nitrosylation chemistry rather than classic NO signaling through guanylate cyclase/cGMP. S-Nitrosoglutathione 43-47 AKT serine/threonine kinase 1 Homo sapiens 61-64 17664146-5 2007 SOD1 weakly increased the rate of decomposition of GSNO, but did so only when GSH was present; and FALS-associated mutant forms of SOD1 were not more active in this regard than was the wild type. S-Nitrosoglutathione 51-55 superoxide dismutase 1 Homo sapiens 0-4 17591795-5 2007 Chromosomal inactivation of either adhC or nmlR(HI) resulted in sensitivity to S-nitrosoglutathione and decreased S-nitrosoglutathione reductase activity. S-Nitrosoglutathione 79-99 S-(hydroxymethyl)glutathione dehydrogenase Haemophilus influenzae Rd KW20 35-39 17767703-6 2007 Our results showed the following: (i) S-nitrosoglutathione (GSNO) induced a burst of RSNO in GSH-depleted R2 cells, the majority of which were primarily contributed by the S-nitrosylation of proteins (Pro-SNOs), and was followed by severe neuronal necrosis; (ii) the elevation in the level of Pro-SNOs resulted from a dysfunction of S-nitroglutathione reductase (GSNOR) as a result of its substrate, GSNO, being unavailable in GSH-depleted cells. S-Nitrosoglutathione 38-58 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 363-368 17767703-6 2007 Our results showed the following: (i) S-nitrosoglutathione (GSNO) induced a burst of RSNO in GSH-depleted R2 cells, the majority of which were primarily contributed by the S-nitrosylation of proteins (Pro-SNOs), and was followed by severe neuronal necrosis; (ii) the elevation in the level of Pro-SNOs resulted from a dysfunction of S-nitroglutathione reductase (GSNOR) as a result of its substrate, GSNO, being unavailable in GSH-depleted cells. S-Nitrosoglutathione 60-64 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 363-368 17483091-3 2007 On activation by GSNO or H(2)O(2), JNK formed a stable association with oligomeric Apaf-1 in a approximately 1.4-2.0 mDa pre-apoptosome complex. S-Nitrosoglutathione 17-21 mitogen-activated protein kinase 8 Homo sapiens 35-38 17492650-10 2007 Similar to SNP, exposure of human chondrocytes to S-nitrosoglutathione (GSNO), another NO donor, caused significant increases in Cyt c levels, caspase-3 activity, and DNA fragmentation, and induced cell apoptosis. S-Nitrosoglutathione 50-70 cytochrome c, somatic Homo sapiens 129-134 17492650-10 2007 Similar to SNP, exposure of human chondrocytes to S-nitrosoglutathione (GSNO), another NO donor, caused significant increases in Cyt c levels, caspase-3 activity, and DNA fragmentation, and induced cell apoptosis. S-Nitrosoglutathione 50-70 caspase 3 Homo sapiens 143-152 17492650-10 2007 Similar to SNP, exposure of human chondrocytes to S-nitrosoglutathione (GSNO), another NO donor, caused significant increases in Cyt c levels, caspase-3 activity, and DNA fragmentation, and induced cell apoptosis. S-Nitrosoglutathione 72-76 cytochrome c, somatic Homo sapiens 129-134 17492650-10 2007 Similar to SNP, exposure of human chondrocytes to S-nitrosoglutathione (GSNO), another NO donor, caused significant increases in Cyt c levels, caspase-3 activity, and DNA fragmentation, and induced cell apoptosis. S-Nitrosoglutathione 72-76 caspase 3 Homo sapiens 143-152 17543375-2 2007 S-nitrosoglutathione reductase (GSNOR; also known as alcohol dehydrogenase 5 or formaldehyde dehydrogenase) catalyzes the metabolism of S-nitrosoglutathione (GSNO) and controls intracellular levels of S-nitrosothiols. S-Nitrosoglutathione 0-20 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 32-37 17543375-2 2007 S-nitrosoglutathione reductase (GSNOR; also known as alcohol dehydrogenase 5 or formaldehyde dehydrogenase) catalyzes the metabolism of S-nitrosoglutathione (GSNO) and controls intracellular levels of S-nitrosothiols. S-Nitrosoglutathione 0-20 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 80-106 17543375-2 2007 S-nitrosoglutathione reductase (GSNOR; also known as alcohol dehydrogenase 5 or formaldehyde dehydrogenase) catalyzes the metabolism of S-nitrosoglutathione (GSNO) and controls intracellular levels of S-nitrosothiols. S-Nitrosoglutathione 32-36 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-30 17543375-2 2007 S-nitrosoglutathione reductase (GSNOR; also known as alcohol dehydrogenase 5 or formaldehyde dehydrogenase) catalyzes the metabolism of S-nitrosoglutathione (GSNO) and controls intracellular levels of S-nitrosothiols. S-Nitrosoglutathione 32-36 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 80-106 17566772-5 2007 Unlike aortic rings with endothelium from controls, those from angiotensin II-infused rats exhibited persistent hyporesponsiveness to phenylephrine after pre-exposure to GSNO, as well as relaxation upon addition of N-acetylcysteine (NAC, which can displace NO from cysteine-NO residues) or HgCl(2) (which cleaves S-NO bonds). S-Nitrosoglutathione 170-174 angiotensinogen Rattus norvegicus 63-77 17566772-6 2007 In aorta from angiotensin II-infused rats, GSNO also induced a persistent increase in cysteine-NO residues (as determined using anti-cysteine-NO antiserum), which was blunted by NAC and HgCl(2). S-Nitrosoglutathione 43-47 angiotensinogen Rattus norvegicus 14-28 17483091-3 2007 On activation by GSNO or H(2)O(2), JNK formed a stable association with oligomeric Apaf-1 in a approximately 1.4-2.0 mDa pre-apoptosome complex. S-Nitrosoglutathione 17-21 apoptotic peptidase activating factor 1 Homo sapiens 83-89 17630850-3 2007 Western blotting and immunocytochemistry for p53 showed that p53 was increased in whole cell lysates by GSNO: 0.001 mM GSNO led to 1.3 +/- 0.5-fold increase compared to control, and significantly (p < 0.05) increased to 1.6 +/- 0.2-fold after 0.01 mM GSNO. S-Nitrosoglutathione 104-108 tumor protein p53 Homo sapiens 45-48 17630850-3 2007 Western blotting and immunocytochemistry for p53 showed that p53 was increased in whole cell lysates by GSNO: 0.001 mM GSNO led to 1.3 +/- 0.5-fold increase compared to control, and significantly (p < 0.05) increased to 1.6 +/- 0.2-fold after 0.01 mM GSNO. S-Nitrosoglutathione 119-123 tumor protein p53 Homo sapiens 45-48 17630850-3 2007 Western blotting and immunocytochemistry for p53 showed that p53 was increased in whole cell lysates by GSNO: 0.001 mM GSNO led to 1.3 +/- 0.5-fold increase compared to control, and significantly (p < 0.05) increased to 1.6 +/- 0.2-fold after 0.01 mM GSNO. S-Nitrosoglutathione 104-108 tumor protein p53 Homo sapiens 61-64 17630850-3 2007 Western blotting and immunocytochemistry for p53 showed that p53 was increased in whole cell lysates by GSNO: 0.001 mM GSNO led to 1.3 +/- 0.5-fold increase compared to control, and significantly (p < 0.05) increased to 1.6 +/- 0.2-fold after 0.01 mM GSNO. S-Nitrosoglutathione 119-123 tumor protein p53 Homo sapiens 61-64 17630850-3 2007 Western blotting and immunocytochemistry for p53 showed that p53 was increased in whole cell lysates by GSNO: 0.001 mM GSNO led to 1.3 +/- 0.5-fold increase compared to control, and significantly (p < 0.05) increased to 1.6 +/- 0.2-fold after 0.01 mM GSNO. S-Nitrosoglutathione 119-123 tumor protein p53 Homo sapiens 45-48 17630850-13 2007 Translocation of p53 from the cytosol to the nucleus occurred with a maximal increase of 2.9-fold in the nucleus following 1.0 mM GSNO for 24 h. These data indicate that in cardiomyocytes, NO induced marked DNA damage and translocation of p53 to the nucleus, suggesting that p53 is involved in the cellular response to NO, perhaps to modulate the genomic response to NO-induced cellular toxicity. S-Nitrosoglutathione 130-134 tumor protein p53 Homo sapiens 17-20 17630850-13 2007 Translocation of p53 from the cytosol to the nucleus occurred with a maximal increase of 2.9-fold in the nucleus following 1.0 mM GSNO for 24 h. These data indicate that in cardiomyocytes, NO induced marked DNA damage and translocation of p53 to the nucleus, suggesting that p53 is involved in the cellular response to NO, perhaps to modulate the genomic response to NO-induced cellular toxicity. S-Nitrosoglutathione 130-134 tumor protein p53 Homo sapiens 239-242 17630850-3 2007 Western blotting and immunocytochemistry for p53 showed that p53 was increased in whole cell lysates by GSNO: 0.001 mM GSNO led to 1.3 +/- 0.5-fold increase compared to control, and significantly (p < 0.05) increased to 1.6 +/- 0.2-fold after 0.01 mM GSNO. S-Nitrosoglutathione 119-123 tumor protein p53 Homo sapiens 61-64 17630850-13 2007 Translocation of p53 from the cytosol to the nucleus occurred with a maximal increase of 2.9-fold in the nucleus following 1.0 mM GSNO for 24 h. These data indicate that in cardiomyocytes, NO induced marked DNA damage and translocation of p53 to the nucleus, suggesting that p53 is involved in the cellular response to NO, perhaps to modulate the genomic response to NO-induced cellular toxicity. S-Nitrosoglutathione 130-134 tumor protein p53 Homo sapiens 239-242 17412510-2 2007 Previously, we have reported that formation of S-nitrosoglutathione (GSNO) in glioma cells overexpressing inducible nitric oxide synthase (iNOS) contributed to nitric oxide (NO)-dependent carbamoylating chemoresistance against BCNU. S-Nitrosoglutathione 47-67 nitric oxide synthase 2 Rattus norvegicus 106-137 17593005-0 2007 S-nitrosoglutathione prevents interphotoreceptor retinoid-binding protein (IRBP(161-180))-induced experimental autoimmune uveitis. S-Nitrosoglutathione 0-20 retinol binding protein 3, interstitial Mus musculus 30-73 17593005-0 2007 S-nitrosoglutathione prevents interphotoreceptor retinoid-binding protein (IRBP(161-180))-induced experimental autoimmune uveitis. S-Nitrosoglutathione 0-20 retinol binding protein 3, interstitial Mus musculus 75-79 17593005-4 2007 The efficacy of GSNO treatment on interphotoreceptor retinoid-binding protein (IRBP)-induced EAU was investigated, using functional, histologic, and immunologic readouts. S-Nitrosoglutathione 16-20 retinol binding protein 3, interstitial Mus musculus 34-77 17593005-4 2007 The efficacy of GSNO treatment on interphotoreceptor retinoid-binding protein (IRBP)-induced EAU was investigated, using functional, histologic, and immunologic readouts. S-Nitrosoglutathione 16-20 retinol binding protein 3, interstitial Mus musculus 79-83 17593005-9 2007 Daily oral GSNO treatment from days 1-14 following immunization was found to be effective against IRBP-induced EAU. S-Nitrosoglutathione 11-15 retinol binding protein 3, interstitial Mus musculus 98-102 17593005-11 2007 The GSNO treatment of EAU animals significantly attenuated the levels of TNF-alpha, IL-1beta, IFN-gamma, and IL-10 in retinas, as measured by quantitative real-time polymerase chain reaction analysis. S-Nitrosoglutathione 4-8 tumor necrosis factor Mus musculus 73-82 17593005-11 2007 The GSNO treatment of EAU animals significantly attenuated the levels of TNF-alpha, IL-1beta, IFN-gamma, and IL-10 in retinas, as measured by quantitative real-time polymerase chain reaction analysis. S-Nitrosoglutathione 4-8 interleukin 1 beta Mus musculus 84-92 17593005-11 2007 The GSNO treatment of EAU animals significantly attenuated the levels of TNF-alpha, IL-1beta, IFN-gamma, and IL-10 in retinas, as measured by quantitative real-time polymerase chain reaction analysis. S-Nitrosoglutathione 4-8 interferon gamma Mus musculus 94-103 17593005-11 2007 The GSNO treatment of EAU animals significantly attenuated the levels of TNF-alpha, IL-1beta, IFN-gamma, and IL-10 in retinas, as measured by quantitative real-time polymerase chain reaction analysis. S-Nitrosoglutathione 4-8 interleukin 10 Mus musculus 109-114 17593005-12 2007 The splenocytes isolated from EAU- and GSNO-treated mice had lower antigen-specific T-cell proliferation in response to IRBP protein, and their cytokine production was inhibited. S-Nitrosoglutathione 39-43 retinol binding protein 3, interstitial Mus musculus 120-124 17412510-2 2007 Previously, we have reported that formation of S-nitrosoglutathione (GSNO) in glioma cells overexpressing inducible nitric oxide synthase (iNOS) contributed to nitric oxide (NO)-dependent carbamoylating chemoresistance against BCNU. S-Nitrosoglutathione 47-67 nitric oxide synthase 2 Rattus norvegicus 139-143 17412510-2 2007 Previously, we have reported that formation of S-nitrosoglutathione (GSNO) in glioma cells overexpressing inducible nitric oxide synthase (iNOS) contributed to nitric oxide (NO)-dependent carbamoylating chemoresistance against BCNU. S-Nitrosoglutathione 69-73 nitric oxide synthase 2 Rattus norvegicus 106-137 17412510-2 2007 Previously, we have reported that formation of S-nitrosoglutathione (GSNO) in glioma cells overexpressing inducible nitric oxide synthase (iNOS) contributed to nitric oxide (NO)-dependent carbamoylating chemoresistance against BCNU. S-Nitrosoglutathione 69-73 nitric oxide synthase 2 Rattus norvegicus 139-143 19704805-5 2007 In vitro exposure of chloroplasts to a NO-donor (GSNO) decreased both ascorbyl radical content and the activity of ascorbate peroxidase, without modification of the total ascorbate content. S-Nitrosoglutathione 49-53 peroxidase Glycine max 125-135 17349934-0 2007 Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: mechanisms and relative contributions to aconitase inactivation. S-Nitrosoglutathione 52-72 aconitase 2 Homo sapiens 0-23 17250805-3 2007 NO-donors, GSNO and NOC-18 decreased cell surface expression of AQP5, concentration- and time-dependently, whereas they did not affect the amount of AQP5 in whole cell lysates. S-Nitrosoglutathione 11-15 aquaporin 5 Mus musculus 64-68 17277089-2 2007 Levels of SNOs in vivo are controlled by nitric oxide synthesis (which in plants is achieved by different routes) and by S-nitrosoglutathione turnover, which is mainly performed by the S-nitrosoglutathione reductase (GSNOR). S-Nitrosoglutathione 121-141 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 185-215 17277089-2 2007 Levels of SNOs in vivo are controlled by nitric oxide synthesis (which in plants is achieved by different routes) and by S-nitrosoglutathione turnover, which is mainly performed by the S-nitrosoglutathione reductase (GSNOR). S-Nitrosoglutathione 121-141 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 217-222 17408650-10 2007 GSNO regulation of mucosal barrier function was associated directly with an increased expression of perijunctional F-actin and tight-junction-associated proteins zonula occludens-1 and occludin. S-Nitrosoglutathione 0-4 occludin Mus musculus 185-193 16990041-1 2007 In this study, we investigated the role of protein disulphide isomerase (PDI) in rapid metabolism of S-nitrosoglutathione (GSNO) and S-nitrosoalbumin (albSNO) and in NO delivery from these compounds into cells. S-Nitrosoglutathione 101-121 prolyl 4-hydroxylase subunit beta Homo sapiens 43-71 16990041-8 2007 Immunoprecipitation experiments showed that GSNO caused a concentration-dependent loss of thiol reactivity of PDI. S-Nitrosoglutathione 44-48 prolyl 4-hydroxylase subunit beta Homo sapiens 110-113 16990041-9 2007 Our data indicate that PDI is involved in both rapid metabolism of GSNO and intracellular NO delivery and that during this process PDI is itself altered by thiol modification. S-Nitrosoglutathione 67-71 prolyl 4-hydroxylase subunit beta Homo sapiens 23-26 17260951-1 2007 We have determined the 1.65 A crystal structure of human thioredoxin-1 after treatment with S-nitrosoglutathione, providing a high-resolution view of this important protein modification and mechanistic insight into protein transnitrosation. S-Nitrosoglutathione 92-112 thioredoxin Homo sapiens 57-68 16990041-5 2007 PDI activity was present in MEG-01 conditioned medium, and was inhibited by high concentrations of GSNO (500 microM). S-Nitrosoglutathione 99-103 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 16990041-1 2007 In this study, we investigated the role of protein disulphide isomerase (PDI) in rapid metabolism of S-nitrosoglutathione (GSNO) and S-nitrosoalbumin (albSNO) and in NO delivery from these compounds into cells. S-Nitrosoglutathione 101-121 prolyl 4-hydroxylase subunit beta Homo sapiens 73-76 16990041-1 2007 In this study, we investigated the role of protein disulphide isomerase (PDI) in rapid metabolism of S-nitrosoglutathione (GSNO) and S-nitrosoalbumin (albSNO) and in NO delivery from these compounds into cells. S-Nitrosoglutathione 123-127 prolyl 4-hydroxylase subunit beta Homo sapiens 43-71 16990041-1 2007 In this study, we investigated the role of protein disulphide isomerase (PDI) in rapid metabolism of S-nitrosoglutathione (GSNO) and S-nitrosoalbumin (albSNO) and in NO delivery from these compounds into cells. S-Nitrosoglutathione 123-127 prolyl 4-hydroxylase subunit beta Homo sapiens 73-76 16990041-2 2007 Incubation of GSNO or albSNO (1 microM) with the megakaryocyte cell line MEG-01 resulted in a cell-mediated removal of each compound which was inhibited by blocking cell surface thiols with 5,5"-dithiobis 2-nitrobenzoic acid (DTNB) (100 microM) or inhibiting PDI with bacitracin (5mM). S-Nitrosoglutathione 14-18 prolyl 4-hydroxylase subunit beta Homo sapiens 259-262 16990041-4 2007 cGMP accumulation in response to GSNO (1 microM) was inhibited by MEG-01 treatment with bacitracin or DTNB, suggesting a role for PDI and surface thiols in NO delivery. S-Nitrosoglutathione 33-37 prolyl 4-hydroxylase subunit beta Homo sapiens 130-133 17019693-7 2007 The mechanism by which GSNO modulated CAMs expression appeared to be via S-nitrosylation of p65, which consequently inhibited nuclear factor kappa B (NF-kappaB) activation in endothelial cells. S-Nitrosoglutathione 23-27 synaptotagmin 1 Rattus norvegicus 92-95 17051422-0 2007 Kinetic and proteomic analyses of S-nitrosoglutathione-treated hexokinase A: consequences for cancer energy metabolism. S-Nitrosoglutathione 34-54 hexokinase 1 Homo sapiens 63-73 17051422-2 2007 Given the important role of this enzyme in metabolic pathways and diseases, the effect of S-nitrosoglutathione (GSNO) on HXK A structure and activity was studied. S-Nitrosoglutathione 90-110 hexokinase 1 Homo sapiens 121-124 17051422-2 2007 Given the important role of this enzyme in metabolic pathways and diseases, the effect of S-nitrosoglutathione (GSNO) on HXK A structure and activity was studied. S-Nitrosoglutathione 112-116 hexokinase 1 Homo sapiens 121-124 17051422-4 2007 Biologically relevant [GSNO]/[HXK] caused a significant decrease in V(max) with glucose (but not with fructose), along with oxidation of 5 Met and nitration of 4 Tyr. S-Nitrosoglutathione 23-27 hexokinase 1 Homo sapiens 30-33 17051422-5 2007 Preincubation of HXK with glucose abrogated the effect of GSNO whereas fructose was ineffective. S-Nitrosoglutathione 58-62 hexokinase 1 Homo sapiens 17-20 17051422-9 2007 Considering that changes in primary structure are envisioned at high [GSNO]/[HXK] ratios, like those present under normal conditions, it could be hypothesized that the high concentration of hexokinase present in fast growing tumors may serve not only to sustain high glycolysis rates, but also to minimize protein damage that might result in activity decline, compromising energy metabolism. S-Nitrosoglutathione 70-74 hexokinase 1 Homo sapiens 190-200 17019693-8 2007 These observations suggest that GSNO exerts its protective effects in EAE by inhibition of cellular infiltration into the CNS by S-nitrosylation of p65, thereby modulating NF-kappaB-CAMs pathway in endothelial cells. S-Nitrosoglutathione 32-36 synaptotagmin 1 Rattus norvegicus 148-151 16597834-3 2006 We have determined the crystal structure of GSNO bound to dimeric human glutathione transferase P1-1 (hGSTP1-1) at 1.4 A resolution. S-Nitrosoglutathione 44-48 glutathione S-transferase pi 1 Homo sapiens 102-110 17403694-3 2007 In this investigation, we found that S-nitrosoglutathion (GSNO), a nitric oxide donor and also an S-nitrosating agent, effectively stimulated nuclear export of APE1 in a CRM1-independent manner. S-Nitrosoglutathione 58-62 apurinic/apyrimidinic endodeoxyribonuclease 1 Homo sapiens 160-164 17403694-3 2007 In this investigation, we found that S-nitrosoglutathion (GSNO), a nitric oxide donor and also an S-nitrosating agent, effectively stimulated nuclear export of APE1 in a CRM1-independent manner. S-Nitrosoglutathione 58-62 exportin 1 Homo sapiens 170-174 17403694-6 2007 In structure, the region aa.64-80 and the beta-strand aa.311-316 in proximity to Cys93 and Cys310 were important for GSNO-induced APE1 relocalization. S-Nitrosoglutathione 117-121 apurinic/apyrimidinic endodeoxyribonuclease 1 Homo sapiens 130-134 17041735-0 2006 [Formation of platelets from cord blood CD34+ cells-derived megakaryocytes induced by S-nitrosoglutathione]. S-Nitrosoglutathione 86-106 CD34 molecule Homo sapiens 40-44 17022806-1 2006 BACKGROUND: It has been suggested that low microM concentrations of S-nitrosoglutathione (GSNO), an endogenous bronchodilator, may promote maturation of the defective cystic fibrosis (CF) transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 68-88 CF transmembrane conductance regulator Homo sapiens 167-223 17022806-1 2006 BACKGROUND: It has been suggested that low microM concentrations of S-nitrosoglutathione (GSNO), an endogenous bronchodilator, may promote maturation of the defective cystic fibrosis (CF) transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 68-88 CF transmembrane conductance regulator Homo sapiens 225-229 17022806-1 2006 BACKGROUND: It has been suggested that low microM concentrations of S-nitrosoglutathione (GSNO), an endogenous bronchodilator, may promote maturation of the defective cystic fibrosis (CF) transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 90-94 CF transmembrane conductance regulator Homo sapiens 167-223 17022806-1 2006 BACKGROUND: It has been suggested that low microM concentrations of S-nitrosoglutathione (GSNO), an endogenous bronchodilator, may promote maturation of the defective cystic fibrosis (CF) transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 90-94 CF transmembrane conductance regulator Homo sapiens 225-229 17022806-7 2006 The effect of GSNO on Cl- efflux in CFBE cells could be inhibited both by a specific thiazolidinone CFTR inhibitor (CFTRinh-172) and by 4,4"-diisothiocyanatodihydrostilbene-2,2"-disulfonic acid (H2DIDS). S-Nitrosoglutathione 14-18 CF transmembrane conductance regulator Homo sapiens 100-104 17022806-11 2006 CONCLUSION: Previous studies have suggested that treatment with GSNO promotes maturation of delF508-CFTR, consistent with our results in this study. S-Nitrosoglutathione 64-68 CF transmembrane conductance regulator Homo sapiens 100-104 16877677-4 2006 (p. 1435) in this issue report on the capability of S-nitrosoglutathione (GSNO) to increase the expression, trafficking, and function of mutant and wild-type cystic fibrosis transmembrane regulator (CFTR). S-Nitrosoglutathione 52-72 CF transmembrane conductance regulator Homo sapiens 199-203 16877677-4 2006 (p. 1435) in this issue report on the capability of S-nitrosoglutathione (GSNO) to increase the expression, trafficking, and function of mutant and wild-type cystic fibrosis transmembrane regulator (CFTR). S-Nitrosoglutathione 74-78 CF transmembrane conductance regulator Homo sapiens 199-203 16877677-7 2006 The authors use GSNO as a lead compound to restore mutant CFTR function. S-Nitrosoglutathione 16-20 CF transmembrane conductance regulator Homo sapiens 58-62 16877677-8 2006 Earlier contradictory reports that GSNO decreased CFTR function by oxidative modification (glutathionylation) may now be explained by high concentrations of GSNO associated with decreased CFTR transcription and disruption of CFTR function. S-Nitrosoglutathione 35-39 CF transmembrane conductance regulator Homo sapiens 50-54 16877677-8 2006 Earlier contradictory reports that GSNO decreased CFTR function by oxidative modification (glutathionylation) may now be explained by high concentrations of GSNO associated with decreased CFTR transcription and disruption of CFTR function. S-Nitrosoglutathione 35-39 CF transmembrane conductance regulator Homo sapiens 188-192 16877677-8 2006 Earlier contradictory reports that GSNO decreased CFTR function by oxidative modification (glutathionylation) may now be explained by high concentrations of GSNO associated with decreased CFTR transcription and disruption of CFTR function. S-Nitrosoglutathione 35-39 CF transmembrane conductance regulator Homo sapiens 188-192 16877677-8 2006 Earlier contradictory reports that GSNO decreased CFTR function by oxidative modification (glutathionylation) may now be explained by high concentrations of GSNO associated with decreased CFTR transcription and disruption of CFTR function. S-Nitrosoglutathione 157-161 CF transmembrane conductance regulator Homo sapiens 188-192 16877677-8 2006 Earlier contradictory reports that GSNO decreased CFTR function by oxidative modification (glutathionylation) may now be explained by high concentrations of GSNO associated with decreased CFTR transcription and disruption of CFTR function. S-Nitrosoglutathione 157-161 CF transmembrane conductance regulator Homo sapiens 188-192 16877677-10 2006 show that at physiologic concentrations, GSNO and the constitutively active S-nitroso-glutathione diethyl ester stimulate CFTR transcription through SP1 and SP3 and promote normal trafficking. S-Nitrosoglutathione 41-45 CF transmembrane conductance regulator Homo sapiens 122-126 16877677-10 2006 show that at physiologic concentrations, GSNO and the constitutively active S-nitroso-glutathione diethyl ester stimulate CFTR transcription through SP1 and SP3 and promote normal trafficking. S-Nitrosoglutathione 41-45 Sp3 transcription factor Homo sapiens 157-160 16923892-8 2006 The roo mutant was more strongly inhibited than the wild type by the nitric oxide (NO)-generating compound S-nitrosoglutathione, indicating that Roo may also serve as an NO reductase in vivo. S-Nitrosoglutathione 107-127 roO Desulfovibrio vulgaris str. Hildenborough 4-7 16765486-6 2006 NO generated from GSNO acts as second messenger molecular which through S-nitrosylation has been shown to control important cellular processes by regulation of expression/activity of certain proteins such as NF-kappaB. S-Nitrosoglutathione 18-22 nuclear factor kappa B subunit 1 Homo sapiens 208-217 16386761-4 2006 Furthermore, GSH was detected by HPLC from the MGST1 which was incubated with ONOO(-) plus GSH or S-nitrosoglutathione followed by DTT treatment. S-Nitrosoglutathione 98-118 microsomal glutathione S-transferase 1 Rattus norvegicus 47-52 16386761-5 2006 In addition, the MGST1 activity increased by nitric oxide (NO) donors such as S-nitrosoglutathione, S-nitrosocysteine or the non-thiol NO donor 1-hydroxy-2-oxo-3 (3-aminopropyl)-3-isopropyl was restored by the DTT treatment. S-Nitrosoglutathione 78-98 microsomal glutathione S-transferase 1 Homo sapiens 17-22 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 114-133 thioredoxin interacting protein Homo sapiens 168-199 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 114-133 thioredoxin interacting protein Homo sapiens 201-206 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 114-133 thioredoxin Homo sapiens 168-179 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 114-133 thioredoxin reductase 2 Homo sapiens 272-295 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 135-139 thioredoxin interacting protein Homo sapiens 168-199 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 135-139 thioredoxin interacting protein Homo sapiens 201-206 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 135-139 thioredoxin Homo sapiens 168-179 17023680-3 2006 METHODS AND RESULTS: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 micromol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). S-Nitrosoglutathione 135-139 thioredoxin reductase 2 Homo sapiens 272-295 17023680-4 2006 GSNO increased thioredoxin activity (1.9+/-0.5-fold after 4 hours; P<0.05 versus control). S-Nitrosoglutathione 0-4 thioredoxin Homo sapiens 15-26 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 134-157 superoxide dismutase 1 Homo sapiens 19-39 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 134-157 superoxide dismutase 1 Homo sapiens 41-44 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 134-157 superoxide dismutase 1 Homo sapiens 56-82 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 134-157 superoxide dismutase 1 Homo sapiens 84-91 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 159-163 superoxide dismutase 1 Homo sapiens 19-39 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 159-163 superoxide dismutase 1 Homo sapiens 41-44 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 159-163 superoxide dismutase 1 Homo sapiens 56-82 17042490-1 2006 In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). S-Nitrosoglutathione 159-163 superoxide dismutase 1 Homo sapiens 84-91 17042490-6 2006 Measurements of both the time course of SNO absorption decay at 333 nm and oxymyoglobin scavenging of the NO that is released confirmed that the chelators inhibit CuZnSOD catalysis of GSNO reductive decomposition by GSH. S-Nitrosoglutathione 184-188 superoxide dismutase 1 Homo sapiens 163-170 16857740-1 2006 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), increases expression, maturation, and function of both the wild-type and the DeltaF508 mutant of the cystic fibrosis transmembrane conductance regulatory protein (CFTR). S-Nitrosoglutathione 31-51 CF transmembrane conductance regulator Homo sapiens 161-221 16857740-1 2006 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), increases expression, maturation, and function of both the wild-type and the DeltaF508 mutant of the cystic fibrosis transmembrane conductance regulatory protein (CFTR). S-Nitrosoglutathione 31-51 CF transmembrane conductance regulator Homo sapiens 223-227 16857740-1 2006 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), increases expression, maturation, and function of both the wild-type and the DeltaF508 mutant of the cystic fibrosis transmembrane conductance regulatory protein (CFTR). S-Nitrosoglutathione 53-57 CF transmembrane conductance regulator Homo sapiens 161-221 16857740-1 2006 The endogenous bronchodilator, S-nitrosoglutathione (GSNO), increases expression, maturation, and function of both the wild-type and the DeltaF508 mutant of the cystic fibrosis transmembrane conductance regulatory protein (CFTR). S-Nitrosoglutathione 53-57 CF transmembrane conductance regulator Homo sapiens 223-227 16857740-2 2006 Though transcriptional mechanisms of action have been identified, GSNO seems also to have post-transcriptional effects on CFTR maturation. S-Nitrosoglutathione 66-70 CF transmembrane conductance regulator Homo sapiens 122-126 16857740-4 2006 These data suggest that GSNO is one of a class of S-nitrosylating agents that act independently of the classic NO radical/cyclic GMP pathway to increase CFTR expression and maturation. S-Nitrosoglutathione 24-28 5'-nucleotidase, cytosolic II Homo sapiens 129-132 16857740-4 2006 These data suggest that GSNO is one of a class of S-nitrosylating agents that act independently of the classic NO radical/cyclic GMP pathway to increase CFTR expression and maturation. S-Nitrosoglutathione 24-28 CF transmembrane conductance regulator Homo sapiens 153-157 16899233-10 2006 But under broken cell conditions, when samples were incubated directly with GSNO, MGST1 S-nitrosylation was indeed detectable in both the microsomal and mitochondrial proteins, indicating that previous failure in detecting MGST1 S-nitrosylation in microsomes is due to the limitations of biotin switch method. S-Nitrosoglutathione 76-80 microsomal glutathione S-transferase 1 Rattus norvegicus 82-87 16923892-8 2006 The roo mutant was more strongly inhibited than the wild type by the nitric oxide (NO)-generating compound S-nitrosoglutathione, indicating that Roo may also serve as an NO reductase in vivo. S-Nitrosoglutathione 107-127 roO Desulfovibrio vulgaris str. Hildenborough 145-148 16524750-8 2006 GSNO also prevented the I/R-induced increase in mRNA expression of ICAM-1 and E-Selectin. S-Nitrosoglutathione 0-4 intercellular adhesion molecule 1 Rattus norvegicus 67-73 16524750-8 2006 GSNO also prevented the I/R-induced increase in mRNA expression of ICAM-1 and E-Selectin. S-Nitrosoglutathione 0-4 selectin E Rattus norvegicus 78-88 16732493-3 2006 We have studied the viable-apoptotic switch in S-nitrosoglutathione (GSNO)-induced mouse thymocyte apoptosis in real-time by means of a novel technique, intensified charge coupled device (ICCD)-based real-time fluorescence micro-imaging, coupled with Annexin V-FITC labeling for phosphatidylserine (PS) translocation in cell membrane. S-Nitrosoglutathione 47-67 annexin A5 Mus musculus 251-260 16732493-3 2006 We have studied the viable-apoptotic switch in S-nitrosoglutathione (GSNO)-induced mouse thymocyte apoptosis in real-time by means of a novel technique, intensified charge coupled device (ICCD)-based real-time fluorescence micro-imaging, coupled with Annexin V-FITC labeling for phosphatidylserine (PS) translocation in cell membrane. S-Nitrosoglutathione 69-73 annexin A5 Mus musculus 251-260 16470420-4 2006 Exogenous NO donated by S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione (GSNO) resulted in significant reduction in levels of IRS-1 in both cells, when compared to the insulin-stimulated control (p<0.001). S-Nitrosoglutathione 67-87 insulin receptor substrate 1 Rattus norvegicus 142-147 16470420-4 2006 Exogenous NO donated by S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione (GSNO) resulted in significant reduction in levels of IRS-1 in both cells, when compared to the insulin-stimulated control (p<0.001). S-Nitrosoglutathione 89-93 insulin receptor substrate 1 Rattus norvegicus 142-147 16551637-8 2006 The role of NO in the expression of CD11b was corroborated further by the expression of microglial CD11b by GSNO, an NO donor. S-Nitrosoglutathione 108-112 integrin subunit alpha M Homo sapiens 36-41 16551637-8 2006 The role of NO in the expression of CD11b was corroborated further by the expression of microglial CD11b by GSNO, an NO donor. S-Nitrosoglutathione 108-112 integrin subunit alpha M Homo sapiens 99-104 16551637-10 2006 Inhibition of LPS- and GSNO-mediated up-regulation of CD11b either by NS2028 (a specific inhibitor of GC) or by KT5823 and Rp-8-bromo-cGMP (specific inhibitors of PKG), and increase in CD11b expression either by 8-bromo-cGMP or by MY-5445 (a specific inhibitor of cGMP phosphodiesterase) alone suggest that NO increases microglial expression of CD11b via GC-cGMP-PKG. S-Nitrosoglutathione 23-27 integrin subunit alpha M Homo sapiens 54-59 16551637-10 2006 Inhibition of LPS- and GSNO-mediated up-regulation of CD11b either by NS2028 (a specific inhibitor of GC) or by KT5823 and Rp-8-bromo-cGMP (specific inhibitors of PKG), and increase in CD11b expression either by 8-bromo-cGMP or by MY-5445 (a specific inhibitor of cGMP phosphodiesterase) alone suggest that NO increases microglial expression of CD11b via GC-cGMP-PKG. S-Nitrosoglutathione 23-27 protein kinase cGMP-dependent 1 Homo sapiens 163-166 16551637-10 2006 Inhibition of LPS- and GSNO-mediated up-regulation of CD11b either by NS2028 (a specific inhibitor of GC) or by KT5823 and Rp-8-bromo-cGMP (specific inhibitors of PKG), and increase in CD11b expression either by 8-bromo-cGMP or by MY-5445 (a specific inhibitor of cGMP phosphodiesterase) alone suggest that NO increases microglial expression of CD11b via GC-cGMP-PKG. S-Nitrosoglutathione 23-27 integrin subunit alpha M Homo sapiens 185-190 16551637-10 2006 Inhibition of LPS- and GSNO-mediated up-regulation of CD11b either by NS2028 (a specific inhibitor of GC) or by KT5823 and Rp-8-bromo-cGMP (specific inhibitors of PKG), and increase in CD11b expression either by 8-bromo-cGMP or by MY-5445 (a specific inhibitor of cGMP phosphodiesterase) alone suggest that NO increases microglial expression of CD11b via GC-cGMP-PKG. S-Nitrosoglutathione 23-27 integrin subunit alpha M Homo sapiens 185-190 16551637-10 2006 Inhibition of LPS- and GSNO-mediated up-regulation of CD11b either by NS2028 (a specific inhibitor of GC) or by KT5823 and Rp-8-bromo-cGMP (specific inhibitors of PKG), and increase in CD11b expression either by 8-bromo-cGMP or by MY-5445 (a specific inhibitor of cGMP phosphodiesterase) alone suggest that NO increases microglial expression of CD11b via GC-cGMP-PKG. S-Nitrosoglutathione 23-27 protein kinase cGMP-dependent 1 Homo sapiens 363-366 16551637-11 2006 In addition, GSNO induced the activation of cAMP response element-binding protein (CREB) via PKG that was involved in the up-regulation of CD11b. S-Nitrosoglutathione 13-17 cAMP responsive element binding protein 1 Homo sapiens 44-81 16551637-11 2006 In addition, GSNO induced the activation of cAMP response element-binding protein (CREB) via PKG that was involved in the up-regulation of CD11b. S-Nitrosoglutathione 13-17 cAMP responsive element binding protein 1 Homo sapiens 83-87 16551637-11 2006 In addition, GSNO induced the activation of cAMP response element-binding protein (CREB) via PKG that was involved in the up-regulation of CD11b. S-Nitrosoglutathione 13-17 protein kinase cGMP-dependent 1 Homo sapiens 93-96 16551637-11 2006 In addition, GSNO induced the activation of cAMP response element-binding protein (CREB) via PKG that was involved in the up-regulation of CD11b. S-Nitrosoglutathione 13-17 integrin subunit alpha M Homo sapiens 139-144 16672668-7 2006 The role of NO in the expression of GFAP was supported further by increased expression of GFAP by S-nitroso glutathione (GSNO), an NO donor. S-Nitrosoglutathione 98-119 glial fibrillary acidic protein Homo sapiens 36-40 16672668-7 2006 The role of NO in the expression of GFAP was supported further by increased expression of GFAP by S-nitroso glutathione (GSNO), an NO donor. S-Nitrosoglutathione 98-119 glial fibrillary acidic protein Homo sapiens 90-94 16672668-7 2006 The role of NO in the expression of GFAP was supported further by increased expression of GFAP by S-nitroso glutathione (GSNO), an NO donor. S-Nitrosoglutathione 121-125 glial fibrillary acidic protein Homo sapiens 36-40 16672668-7 2006 The role of NO in the expression of GFAP was supported further by increased expression of GFAP by S-nitroso glutathione (GSNO), an NO donor. S-Nitrosoglutathione 121-125 glial fibrillary acidic protein Homo sapiens 90-94 16597834-6 2006 The binding of GSNO to wild-type hGSTP1-1 induces a negative cooperativity with a kinetic process concomitant to the binding process occurring at more physiological temperatures. S-Nitrosoglutathione 15-19 glutathione S-transferase pi 1 Homo sapiens 33-41 16299053-3 2006 Incubation of rPASMC with S-nitroso-l-glutathione (GSNO) increased expression of a PDE isoform that specifically metabolizes cAMP (PDE4B) in a dose- and time-dependent manner. S-Nitrosoglutathione 26-49 phosphodiesterase 4B Rattus norvegicus 131-136 16421103-0 2006 Mechanisms of cystic fibrosis transmembrane conductance regulator activation by S-nitrosoglutathione. S-Nitrosoglutathione 80-100 CF transmembrane conductance regulator Homo sapiens 14-65 16421103-1 2006 We investigated the mechanisms by which S-nitrosoglutathione (GSNO) alters cystic fibrosis transmembrane conductance regulator (CFTR) mediated chloride (Cl(-)) secretion across Calu-3 cells, an extensively used model of human airway gland serous cells. S-Nitrosoglutathione 40-60 CF transmembrane conductance regulator Homo sapiens 75-126 16421103-1 2006 We investigated the mechanisms by which S-nitrosoglutathione (GSNO) alters cystic fibrosis transmembrane conductance regulator (CFTR) mediated chloride (Cl(-)) secretion across Calu-3 cells, an extensively used model of human airway gland serous cells. S-Nitrosoglutathione 40-60 CF transmembrane conductance regulator Homo sapiens 128-132 16421103-1 2006 We investigated the mechanisms by which S-nitrosoglutathione (GSNO) alters cystic fibrosis transmembrane conductance regulator (CFTR) mediated chloride (Cl(-)) secretion across Calu-3 cells, an extensively used model of human airway gland serous cells. S-Nitrosoglutathione 62-66 CF transmembrane conductance regulator Homo sapiens 75-126 16421103-1 2006 We investigated the mechanisms by which S-nitrosoglutathione (GSNO) alters cystic fibrosis transmembrane conductance regulator (CFTR) mediated chloride (Cl(-)) secretion across Calu-3 cells, an extensively used model of human airway gland serous cells. S-Nitrosoglutathione 62-66 CF transmembrane conductance regulator Homo sapiens 128-132 16415251-0 2006 Endogenous S-nitrosoglutathione modifies 5-lipoxygenase expression in airway epithelial cells. S-Nitrosoglutathione 11-31 arachidonate 5-lipoxygenase Homo sapiens 41-55 16415251-8 2006 The effect of 1 microM GSNO on 5-LO expression was prevented by the gamma-GT inhibitor, acivicin, suggesting a convergence of GSNO and CysLT metabolic pathway that may be relevant to asthma. S-Nitrosoglutathione 23-27 inactive glutathione hydrolase 2 Homo sapiens 68-76 16299053-7 2006 The GSNO-induced increase in PDE4B mRNA levels was blocked by actinomycin D but augmented by cycloheximide. S-Nitrosoglutathione 4-8 phosphodiesterase 4B Rattus norvegicus 29-34 16299053-8 2006 Infection of rPASMC with an adenovirus specifying a dominant negative cAMP response element binding protein (CREB) mutant inhibited the GSNO-induced increase of PDE4B gene expression. S-Nitrosoglutathione 136-140 cAMP responsive element binding protein 1 Rattus norvegicus 70-107 16415251-8 2006 The effect of 1 microM GSNO on 5-LO expression was prevented by the gamma-GT inhibitor, acivicin, suggesting a convergence of GSNO and CysLT metabolic pathway that may be relevant to asthma. S-Nitrosoglutathione 126-130 inactive glutathione hydrolase 2 Homo sapiens 68-76 16299053-3 2006 Incubation of rPASMC with S-nitroso-l-glutathione (GSNO) increased expression of a PDE isoform that specifically metabolizes cAMP (PDE4B) in a dose- and time-dependent manner. S-Nitrosoglutathione 51-55 phosphodiesterase 4B Rattus norvegicus 131-136 16299053-8 2006 Infection of rPASMC with an adenovirus specifying a dominant negative cAMP response element binding protein (CREB) mutant inhibited the GSNO-induced increase of PDE4B gene expression. S-Nitrosoglutathione 136-140 cAMP responsive element binding protein 1 Rattus norvegicus 109-113 16299053-8 2006 Infection of rPASMC with an adenovirus specifying a dominant negative cAMP response element binding protein (CREB) mutant inhibited the GSNO-induced increase of PDE4B gene expression. S-Nitrosoglutathione 136-140 phosphodiesterase 4B Rattus norvegicus 161-166 16299053-4 2006 GSNO increased PDE4B protein levels, and rolipram-inhibitable PDE activity was 2.3 +/- 1.0-fold greater in GSNO-treated rPASMC than in untreated cells. S-Nitrosoglutathione 0-4 phosphodiesterase 4B Rattus norvegicus 15-20 16299053-10 2006 The GSNO-induced increase of PDE4B gene expression is CREB dependent. S-Nitrosoglutathione 4-8 phosphodiesterase 4B Rattus norvegicus 29-34 16299053-5 2006 The soluble guanylate cyclase (sGC) inhibitor, 1H-[1,2,4]oxadiazolo[4,3,-a]quinoxalin-1-one, and the cAMP-dependent protein kinase inhibitor, H89, prevented induction of PDE4B gene expression by GSNO, but the protein kinase G (PKG) inhibitors, Rp-8-pCPT-cGMPs and KT-5823, did not. S-Nitrosoglutathione 195-199 guanylate cyclase 1 soluble subunit beta 2 Rattus norvegicus 4-29 16299053-10 2006 The GSNO-induced increase of PDE4B gene expression is CREB dependent. S-Nitrosoglutathione 4-8 cAMP responsive element binding protein 1 Rattus norvegicus 54-58 16365035-5 2006 Our data showed that incubation with GSNO resulted in blunt, reversible inhibition of MAT1, whereas MAT2 and MAT3 were not significantly affected. S-Nitrosoglutathione 37-41 S-adenosylmethionine synthetase 1 Arabidopsis thaliana 86-90 16365035-9 2006 The inhibitory effect of GSNO was drastically reduced when Cys-114 of MAT1 was replaced by arginine, and mass spectrometric analyses of Cys-114-containing peptides obtained after chymotryptic digestion demonstrated that Cys-114 of MAT1 is indeed S-nitrosylated. S-Nitrosoglutathione 25-29 S-adenosylmethionine synthetase 1 Arabidopsis thaliana 70-74 16365035-9 2006 The inhibitory effect of GSNO was drastically reduced when Cys-114 of MAT1 was replaced by arginine, and mass spectrometric analyses of Cys-114-containing peptides obtained after chymotryptic digestion demonstrated that Cys-114 of MAT1 is indeed S-nitrosylated. S-Nitrosoglutathione 25-29 S-adenosylmethionine synthetase 1 Arabidopsis thaliana 231-235 16441149-1 2006 The reactions of aquacobalamin (Cbl(III)H2O, vitamin B12a) and reduced cobalamin (Cbl(II), vitamin B12r) with the nitrosothiols S-nitrosoglutathione (GSNO) and S-nitroso-N-acetylpenicillamine (SNAP) were studied in aqueous solution at pH 7.4. S-Nitrosoglutathione 128-148 Cbl proto-oncogene Homo sapiens 32-35 16441149-1 2006 The reactions of aquacobalamin (Cbl(III)H2O, vitamin B12a) and reduced cobalamin (Cbl(II), vitamin B12r) with the nitrosothiols S-nitrosoglutathione (GSNO) and S-nitroso-N-acetylpenicillamine (SNAP) were studied in aqueous solution at pH 7.4. S-Nitrosoglutathione 128-148 Cbl proto-oncogene Homo sapiens 82-85 16441149-4 2006 Reactions of aquacobalamin with GSNO and SNAP involve initial formation of Cbl(III)-RSNO adducts followed by nitrosothiol decomposition via heterolytic S-NO bond cleavage. S-Nitrosoglutathione 32-36 Cbl proto-oncogene Homo sapiens 75-78 16441149-7 2006 In the case of GSNO, the overall reaction is fast (k approximately 1.2 x 10(6) M(-1) s(-1)) and leads to formation of glutathionylcobalamin (Cbl(III)SG) and nitrosylcobalamin (Cbl(III)(NO-)) as the final cobalamin products. S-Nitrosoglutathione 15-19 Cbl proto-oncogene Homo sapiens 141-151 16441149-7 2006 In the case of GSNO, the overall reaction is fast (k approximately 1.2 x 10(6) M(-1) s(-1)) and leads to formation of glutathionylcobalamin (Cbl(III)SG) and nitrosylcobalamin (Cbl(III)(NO-)) as the final cobalamin products. S-Nitrosoglutathione 15-19 Cbl proto-oncogene Homo sapiens 141-144 16847746-0 2006 S-nitrosoglutathione modulates CXCR4 and ICOS expression. S-Nitrosoglutathione 0-20 C-X-C motif chemokine receptor 4 Homo sapiens 31-36 16847746-0 2006 S-nitrosoglutathione modulates CXCR4 and ICOS expression. S-Nitrosoglutathione 0-20 inducible T cell costimulator Homo sapiens 41-45 16847746-3 2006 We examined the influence of S-nitrosoglutathione (SNG), an inhibitor of Vacuolar H+-ATPase (V-ATPase), on the expression of CXCR4 and ICOS in PMA/Ionomycin-treated peripheral mononuclear cells (PBMC), and of CXCR4 alone in lymphoid cell lines. S-Nitrosoglutathione 29-49 C-X-C motif chemokine receptor 4 Homo sapiens 125-130 16847746-3 2006 We examined the influence of S-nitrosoglutathione (SNG), an inhibitor of Vacuolar H+-ATPase (V-ATPase), on the expression of CXCR4 and ICOS in PMA/Ionomycin-treated peripheral mononuclear cells (PBMC), and of CXCR4 alone in lymphoid cell lines. S-Nitrosoglutathione 29-49 inducible T cell costimulator Homo sapiens 135-139 17468957-8 2006 S-Nitrosoglutathione (GSNO) activated Cl(-) conductance in the presence of Zn(2+) ions, indicating that ClC-2 channel function was not affected by GSNO. S-Nitrosoglutathione 22-26 galectin 14 Homo sapiens 104-109 17059693-3 2006 In particular, we could show that the nitric oxide (NO) donor, GSNO, induces IRAK-M overexpression in human monocytes. S-Nitrosoglutathione 63-67 interleukin 1 receptor associated kinase 3 Homo sapiens 77-83 17059693-4 2006 Here we study the expression of another important negative regulator of cytokine signaling, SOCS-1, in human monocytes exposed to GSNO. S-Nitrosoglutathione 130-134 suppressor of cytokine signaling 1 Homo sapiens 92-98 17059693-8 2006 A blocking antibody against TNF-alpha impaired SOCS-1 expression upon GSNO treatment and re-instated IL-6 and IP-10 mRNA levels after LPS challenge in cultures pretreated with the NO donor. S-Nitrosoglutathione 70-74 tumor necrosis factor Homo sapiens 28-37 17059693-8 2006 A blocking antibody against TNF-alpha impaired SOCS-1 expression upon GSNO treatment and re-instated IL-6 and IP-10 mRNA levels after LPS challenge in cultures pretreated with the NO donor. S-Nitrosoglutathione 70-74 suppressor of cytokine signaling 1 Homo sapiens 47-53 16277524-5 2005 Herein, we present experimental evidence that two ubiquitous cellular dithiols, thioredoxin and dihydrolipoic acid, catalyze the denitrosation of S-nitrosoglutathione, S-nitrosocaspase 3, S-nitrosoalbumin, and S-nitrosometallothionenin to their reduced state with concomitant generation of nitroxyl (HNO), the one-electron reduction product of NO. S-Nitrosoglutathione 146-166 thioredoxin Homo sapiens 80-91 15967436-7 2005 Incubation of HLEC with SNAP or GSNO reduced AR activity. S-Nitrosoglutathione 32-36 aldo-keto reductase family 1 member B1 Rattus norvegicus 45-47 15967436-8 2005 A similar reduction in AR activity and sorbitol accumulation was observed when diabetic and non-diabetic rat lenses were cultured in the presence of SNAP and GSNO. S-Nitrosoglutathione 158-162 aldo-keto reductase family 1 member B1 Rattus norvegicus 23-25 16185646-7 2005 Analysis of intracellular proteins on DAF gels indicated that the NO donor compound S-nitrosoglutathione S-nitrosylates significantly more proteins in mitochondrial lysates than in cytoplasmic lysates. S-Nitrosoglutathione 84-104 CD55 molecule (Cromer blood group) Homo sapiens 38-41 15967877-4 2005 In the present study, we show that S-nitrosocysteine (CSNO), S-nitrosoglutathione (GSNO), and S-nitroso-N-acetylpenicillamine (SNAP) reversibly oxidized recombinant PTEN. S-Nitrosoglutathione 61-81 phosphatase and tensin homolog Homo sapiens 165-169 16225875-4 2005 Nitric oxide (NO) donors (S-nitrosoglutathione and dinitrosyl iron complex) reversibly inhibited activity of n-SMase and decreased level of lipid peroxidation products. S-Nitrosoglutathione 26-46 sphingomyelin phosphodiesterase 2, neutral Mus musculus 109-116 16242127-4 2005 NO donors such as S-nitrosoglutathione (GSNO), S-nitroso-N-acetylpenicillamine, and 3-morpholinosydnonimine significantly increased the nitrite concentration while they inhibited the ALDH2 activity. S-Nitrosoglutathione 18-38 aldehyde dehydrogenase 2 family member Rattus norvegicus 183-188 16242127-4 2005 NO donors such as S-nitrosoglutathione (GSNO), S-nitroso-N-acetylpenicillamine, and 3-morpholinosydnonimine significantly increased the nitrite concentration while they inhibited the ALDH2 activity. S-Nitrosoglutathione 40-44 aldehyde dehydrogenase 2 family member Rattus norvegicus 183-188 16242127-5 2005 Addition of GSH-ethylester (GSH-EE) completely blocked the GSNO-mediated ALDH2 inhibition and increased nitrite concentration. S-Nitrosoglutathione 59-63 aldehyde dehydrogenase 2 family member Rattus norvegicus 73-78 16242127-7 2005 The anti-nitrosocysteine antibody recognized the immunopurified ALDH2 only from the GSNO-treated samples. S-Nitrosoglutathione 84-88 aldehyde dehydrogenase 2 family member Rattus norvegicus 64-69 15930734-6 2005 The decrease inf GSNO was accelerated in the presence of superoxide+catalase. S-Nitrosoglutathione 17-21 catalase Homo sapiens 68-76 15987648-3 2005 Nitric oxide generated by nitric oxide synthase or released from an endogenous S-nitrosothiol, S-nitrosoglutathione may up-regulate antioxidative thioredoxin system and antiapototic Bcl-2 protein through a cGMP-dependent mechanism. S-Nitrosoglutathione 95-115 thioredoxin Homo sapiens 146-157 15987648-3 2005 Nitric oxide generated by nitric oxide synthase or released from an endogenous S-nitrosothiol, S-nitrosoglutathione may up-regulate antioxidative thioredoxin system and antiapototic Bcl-2 protein through a cGMP-dependent mechanism. S-Nitrosoglutathione 95-115 BCL2 apoptosis regulator Homo sapiens 182-187 15998242-5 2005 Likewise, the combined S-glutathionylation and S-nitrosylation of RyR1 induced by GSNO increased by fourfold the Kd of CaCaM binding to triads and abolished apoCaM binding. S-Nitrosoglutathione 82-86 ryanodine receptor 1 Homo sapiens 66-70 15998248-5 2005 In this study, we have investigated the possible occurrence of S-glutathionylation during reaction of GSNO with papain, creatine phosphokinase, glyceraldehyde-3-phosphate dehydrogenase, alcohol dehydrogenase, bovine serum albumin, and actin. S-Nitrosoglutathione 102-106 aldo-keto reductase family 1 member A1 Homo sapiens 186-207 15998248-5 2005 In this study, we have investigated the possible occurrence of S-glutathionylation during reaction of GSNO with papain, creatine phosphokinase, glyceraldehyde-3-phosphate dehydrogenase, alcohol dehydrogenase, bovine serum albumin, and actin. S-Nitrosoglutathione 102-106 albumin Homo sapiens 216-229 15998248-6 2005 Our results show that papain, creatine phosphokinase, and glyceraldehyde-3-phosphate dehydrogenase were significantly both S-nitrosated and S-glutathionylated by GSNO, whereas alcohol dehydrogenase, bovine serum albumin, and actin appeared nearly only S-nitrosated. S-Nitrosoglutathione 162-166 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 58-98 15998241-7 2005 Therefore, S-nitrosoglutathione (GSNO) was tested for its ability to modify TH. S-Nitrosoglutathione 11-31 tyrosine hydroxylase Homo sapiens 76-78 15998241-7 2005 Therefore, S-nitrosoglutathione (GSNO) was tested for its ability to modify TH. S-Nitrosoglutathione 33-37 tyrosine hydroxylase Homo sapiens 76-78 15998241-9 2005 Dimedone, a sulfenic acid trap, prevents S-thiolation of TH when included with GSNO during its decomposition. S-Nitrosoglutathione 79-83 tyrosine hydroxylase Homo sapiens 57-59 15998241-12 2005 Glutathione disulfide S-oxide, which forms spontaneously in the decomposition of GSNO and which is found in tissue undergoing oxidative stress, may be the species that S-thiolates TH. S-Nitrosoglutathione 81-85 tyrosine hydroxylase Homo sapiens 180-182 15998242-1 2005 This study shows that the combination of glutathione (GSH) plus hydrogen peroxide (H2O2) promotes the S-glutathionylation of ryanodine receptor type 1 (RyR1) Ca2+ release channels, and confirms their joint S-glutathionylation and S-nitrosylation by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 249-269 ryanodine receptor 1 Homo sapiens 125-150 15998242-1 2005 This study shows that the combination of glutathione (GSH) plus hydrogen peroxide (H2O2) promotes the S-glutathionylation of ryanodine receptor type 1 (RyR1) Ca2+ release channels, and confirms their joint S-glutathionylation and S-nitrosylation by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 249-269 ryanodine receptor 1 Homo sapiens 152-156 15998242-1 2005 This study shows that the combination of glutathione (GSH) plus hydrogen peroxide (H2O2) promotes the S-glutathionylation of ryanodine receptor type 1 (RyR1) Ca2+ release channels, and confirms their joint S-glutathionylation and S-nitrosylation by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 271-275 ryanodine receptor 1 Homo sapiens 125-150 15998242-1 2005 This study shows that the combination of glutathione (GSH) plus hydrogen peroxide (H2O2) promotes the S-glutathionylation of ryanodine receptor type 1 (RyR1) Ca2+ release channels, and confirms their joint S-glutathionylation and S-nitrosylation by S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 271-275 ryanodine receptor 1 Homo sapiens 152-156 15998242-2 2005 In addition, we show that 35S-labeled 12-kDa FK506-binding protein ([35S]FKBP12) bound with a Kd of 13.1 nM to RyR1 present in triads or heavy sarcoplasmic reticulum vesicles; RyR1 S-nitrosylation by NOR-3 or GSNO, but not S-glutathionylation, specifically increased by four- to fivefold this Kd value. S-Nitrosoglutathione 209-213 FKBP prolyl isomerase 1A pseudogene 3 Homo sapiens 73-79 15998242-2 2005 In addition, we show that 35S-labeled 12-kDa FK506-binding protein ([35S]FKBP12) bound with a Kd of 13.1 nM to RyR1 present in triads or heavy sarcoplasmic reticulum vesicles; RyR1 S-nitrosylation by NOR-3 or GSNO, but not S-glutathionylation, specifically increased by four- to fivefold this Kd value. S-Nitrosoglutathione 209-213 ryanodine receptor 1 Homo sapiens 111-115 16142585-5 2005 GSNO treatment effectively stimulated activation of the ERK1/2 and p38 kinase in both types of cells. S-Nitrosoglutathione 0-4 mitogen-activated protein kinase 3 Homo sapiens 56-62 15611098-1 2005 S-nitrosoglutathione (GSNO) denitrosation activity of recombinant human protein disulfide isomerase (PDI) has been kinetically characterized by monitoring the loss of the S-NO absorbance, using a NO electrode, and with the aid of the fluorogenic NOx probe 2,3-diaminonaphthalene. S-Nitrosoglutathione 0-20 prolyl 4-hydroxylase subunit beta Homo sapiens 72-99 15611098-1 2005 S-nitrosoglutathione (GSNO) denitrosation activity of recombinant human protein disulfide isomerase (PDI) has been kinetically characterized by monitoring the loss of the S-NO absorbance, using a NO electrode, and with the aid of the fluorogenic NOx probe 2,3-diaminonaphthalene. S-Nitrosoglutathione 0-20 prolyl 4-hydroxylase subunit beta Homo sapiens 101-104 15611098-1 2005 S-nitrosoglutathione (GSNO) denitrosation activity of recombinant human protein disulfide isomerase (PDI) has been kinetically characterized by monitoring the loss of the S-NO absorbance, using a NO electrode, and with the aid of the fluorogenic NOx probe 2,3-diaminonaphthalene. S-Nitrosoglutathione 22-26 prolyl 4-hydroxylase subunit beta Homo sapiens 72-99 15611098-1 2005 S-nitrosoglutathione (GSNO) denitrosation activity of recombinant human protein disulfide isomerase (PDI) has been kinetically characterized by monitoring the loss of the S-NO absorbance, using a NO electrode, and with the aid of the fluorogenic NOx probe 2,3-diaminonaphthalene. S-Nitrosoglutathione 22-26 prolyl 4-hydroxylase subunit beta Homo sapiens 101-104 15793233-3 2005 Exogenous NO donated by S-nitrosoglutathione (GSNO) induced in vitro and in vivo S-nitrosation of the insulin receptor beta subunit (IRbeta) and protein kinase B/Akt (Akt) and reduced their kinase activity in muscle. S-Nitrosoglutathione 24-44 thymoma viral proto-oncogene 1 Mus musculus 162-165 15793233-3 2005 Exogenous NO donated by S-nitrosoglutathione (GSNO) induced in vitro and in vivo S-nitrosation of the insulin receptor beta subunit (IRbeta) and protein kinase B/Akt (Akt) and reduced their kinase activity in muscle. S-Nitrosoglutathione 24-44 thymoma viral proto-oncogene 1 Mus musculus 167-170 15793233-3 2005 Exogenous NO donated by S-nitrosoglutathione (GSNO) induced in vitro and in vivo S-nitrosation of the insulin receptor beta subunit (IRbeta) and protein kinase B/Akt (Akt) and reduced their kinase activity in muscle. S-Nitrosoglutathione 46-50 thymoma viral proto-oncogene 1 Mus musculus 162-165 15793233-3 2005 Exogenous NO donated by S-nitrosoglutathione (GSNO) induced in vitro and in vivo S-nitrosation of the insulin receptor beta subunit (IRbeta) and protein kinase B/Akt (Akt) and reduced their kinase activity in muscle. S-Nitrosoglutathione 46-50 thymoma viral proto-oncogene 1 Mus musculus 167-170 15793233-4 2005 Insulin receptor substrate (IRS)-1 was also rapidly S-nitrosated, and its expression was reduced after chronic GSNO treatment. S-Nitrosoglutathione 111-115 insulin receptor substrate 1 Mus musculus 0-34 15749390-5 2005 This GSNO-mediated neuroprotection appeared to involve activation of cGMP-dependent protein kinase (PKG), phosphatidylinositol 3-kinase (PI3K), and extracellular signal-regulated kinase (ERK). S-Nitrosoglutathione 5-9 protein kinase cGMP-dependent 1 Homo sapiens 100-103 15749390-5 2005 This GSNO-mediated neuroprotection appeared to involve activation of cGMP-dependent protein kinase (PKG), phosphatidylinositol 3-kinase (PI3K), and extracellular signal-regulated kinase (ERK). S-Nitrosoglutathione 5-9 phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta Homo sapiens 106-135 15749390-5 2005 This GSNO-mediated neuroprotection appeared to involve activation of cGMP-dependent protein kinase (PKG), phosphatidylinositol 3-kinase (PI3K), and extracellular signal-regulated kinase (ERK). S-Nitrosoglutathione 5-9 mitogen-activated protein kinase 1 Homo sapiens 148-185 15749390-5 2005 This GSNO-mediated neuroprotection appeared to involve activation of cGMP-dependent protein kinase (PKG), phosphatidylinositol 3-kinase (PI3K), and extracellular signal-regulated kinase (ERK). S-Nitrosoglutathione 5-9 mitogen-activated protein kinase 1 Homo sapiens 187-190 16142585-5 2005 GSNO treatment effectively stimulated activation of the ERK1/2 and p38 kinase in both types of cells. S-Nitrosoglutathione 0-4 mitogen-activated protein kinase 1 Homo sapiens 67-70 16142585-9 2005 Inhibition of ERK1/2 with PD098059, or of p38 kinase with SB203580, reduced the GSNO-induced cell cycle arrest of the G0/G1 phase in SW620 cells. S-Nitrosoglutathione 80-84 mitogen-activated protein kinase 3 Homo sapiens 14-20 16142585-9 2005 Inhibition of ERK1/2 with PD098059, or of p38 kinase with SB203580, reduced the GSNO-induced cell cycle arrest of the G0/G1 phase in SW620 cells. S-Nitrosoglutathione 80-84 mitogen-activated protein kinase 1 Homo sapiens 42-45 15647746-5 2005 Treatment with GSNO reduced the expression of tumor necrosis factor-alpha, interleukin-1beta, and iNOS; inhibited the activation of microglia/macrophage (ED1, CD11-b); and downregulated the expression of leukocyte function-associated antigen-1 and intercellular adhesion molecule-1 in the ischemic brain. S-Nitrosoglutathione 15-19 tumor necrosis factor Rattus norvegicus 46-73 15660100-5 2005 We found that NO donors ((+/-)-S-nitroso-N-acetylpenicillamine, S-nitrosoglutathione, and NONOates) dose-dependently inhibited caspase-3 and -9 activity induced by STS and camptothecin. S-Nitrosoglutathione 64-84 caspase 3 Homo sapiens 127-143 15647746-5 2005 Treatment with GSNO reduced the expression of tumor necrosis factor-alpha, interleukin-1beta, and iNOS; inhibited the activation of microglia/macrophage (ED1, CD11-b); and downregulated the expression of leukocyte function-associated antigen-1 and intercellular adhesion molecule-1 in the ischemic brain. S-Nitrosoglutathione 15-19 interleukin 1 beta Rattus norvegicus 75-92 15647746-5 2005 Treatment with GSNO reduced the expression of tumor necrosis factor-alpha, interleukin-1beta, and iNOS; inhibited the activation of microglia/macrophage (ED1, CD11-b); and downregulated the expression of leukocyte function-associated antigen-1 and intercellular adhesion molecule-1 in the ischemic brain. S-Nitrosoglutathione 15-19 nitric oxide synthase 2 Rattus norvegicus 98-102 15647746-5 2005 Treatment with GSNO reduced the expression of tumor necrosis factor-alpha, interleukin-1beta, and iNOS; inhibited the activation of microglia/macrophage (ED1, CD11-b); and downregulated the expression of leukocyte function-associated antigen-1 and intercellular adhesion molecule-1 in the ischemic brain. S-Nitrosoglutathione 15-19 integrin subunit alpha M Rattus norvegicus 159-165 15647746-5 2005 Treatment with GSNO reduced the expression of tumor necrosis factor-alpha, interleukin-1beta, and iNOS; inhibited the activation of microglia/macrophage (ED1, CD11-b); and downregulated the expression of leukocyte function-associated antigen-1 and intercellular adhesion molecule-1 in the ischemic brain. S-Nitrosoglutathione 15-19 intercellular adhesion molecule 1 Rattus norvegicus 204-281 15647746-6 2005 The number of apoptotic cells (including neurons) and the activity of caspase-3 were also decreased after GSNO treatment. S-Nitrosoglutathione 106-110 caspase 3 Rattus norvegicus 70-79 15647746-7 2005 Further, the antiinflammatory effect of GSNO on expression of iNOS and activation of NF-kappaB machinery in rat primary astrocytes and in the murine microglial cell line BV2 was tested. S-Nitrosoglutathione 40-44 nitric oxide synthase 2 Rattus norvegicus 62-66 15647746-8 2005 Cytokine-mediated expression of iNOS and activation of NF-kappaB were inhibited by GSNO treatment. S-Nitrosoglutathione 83-87 nitric oxide synthase 2 Rattus norvegicus 32-36 15590070-3 2004 The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of Ca(II) to S100A1 and of Ca(II) and Zn(II) to S100B. S-Nitrosoglutathione 4-8 carbonic anhydrase 2 Homo sapiens 110-116 15657297-3 2005 Here we show that CFTR channel activity in excised membrane patches is markedly inhibited by several oxidized forms of glutathione (i.e., GSSG, GSNO, and glutathione treated with diamide, a strong thiol oxidizer). S-Nitrosoglutathione 144-148 CF transmembrane conductance regulator Homo sapiens 18-22 15590070-3 2004 The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of Ca(II) to S100A1 and of Ca(II) and Zn(II) to S100B. S-Nitrosoglutathione 4-8 S100 calcium binding protein A1 Homo sapiens 120-126 15590070-3 2004 The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of Ca(II) to S100A1 and of Ca(II) and Zn(II) to S100B. S-Nitrosoglutathione 4-8 carbonic anhydrase 2 Homo sapiens 134-140 15590070-3 2004 The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of Ca(II) to S100A1 and of Ca(II) and Zn(II) to S100B. S-Nitrosoglutathione 4-8 S100 calcium binding protein B Homo sapiens 155-160 15580027-6 2004 GSNO significantly inhibited superoxide production and suppressed NF-kappa B activation, iNOS induction, and 3-nitrotyrosine expression, but up-regulated endothelial NOS expression in the flap vessels. S-Nitrosoglutathione 0-4 nitric oxide synthase 2 Rattus norvegicus 89-93 15580027-8 2004 CONCLUSION: Exogenous NO donation by GSNO can scavenge superoxide and suppress iNOS induction, resulting in better flap survival after prolonged ischemia. S-Nitrosoglutathione 37-41 nitric oxide synthase 2 Rattus norvegicus 79-83 15275856-5 2004 S-Nitroso-glutathione (NO generator; GSNO) and YC-1 (NO-independent sGC activator) stimulated sGC in the cytosol to synthesise cGMP. S-Nitrosoglutathione 0-21 guanylate cyclase 1 soluble subunit alpha 1 Rattus norvegicus 94-97 15171728-0 2004 Platelet cell-surface protein disulphide-isomerase mediated S-nitrosoglutathione consumption. S-Nitrosoglutathione 60-80 prolyl 4-hydroxylase subunit beta Homo sapiens 22-50 15275856-6 2004 The combination of GSNO and YC-1 stimulated sGC synergistically. S-Nitrosoglutathione 19-23 guanylate cyclase 1 soluble subunit alpha 1 Rattus norvegicus 44-47 15171728-6 2004 The presence of known PDI inhibitors phenylarsine oxide and anti-PDI antibodies prevented GSNO denitrosation. S-Nitrosoglutathione 90-94 prolyl 4-hydroxylase subunit beta Homo sapiens 22-25 15171728-6 2004 The presence of known PDI inhibitors phenylarsine oxide and anti-PDI antibodies prevented GSNO denitrosation. S-Nitrosoglutathione 90-94 prolyl 4-hydroxylase subunit beta Homo sapiens 65-68 15275856-8 2004 Amylase release stimulated by carbachol and GSNO was inhibited by addition of the sGC inhibitor, ODQ, and cGMP-dependent protein kinase inhibitor, KT-5823. S-Nitrosoglutathione 44-48 guanylate cyclase 1 soluble subunit alpha 1 Rattus norvegicus 82-85 15171728-7 2004 The fact that, in the presence of GSNO plus the cell-permeable guanylate cyclase inhibitor 1H-[1,2,4]oxadiazolo-[4,3-a]quinoxaline-1-one, the initial rates of ADP-induced platelet aggregation and the maximum DeltaOD were diminished by approximately 40% shows that RSNOs have dual inhibitory effects on platelets, which are mediated through PDI. S-Nitrosoglutathione 34-38 prolyl 4-hydroxylase subunit beta Homo sapiens 340-343 15524165-2 2004 In this study, we examined the possible diabetogenicity of NO by noting differences in the cellular binding of insulin in dogs treated with the NO donor, S-nitrosoglutathione (GSNO) compared to captopril-treated controls. S-Nitrosoglutathione 154-174 insulin Canis lupus familiaris 111-118 27520663-2 2004 In this study, we examined the possible diabetogenicity of NO by noting differences in the cellular binding of insulin in dogs treated with the NO donor, S-nitrosoglutathione (GSNO) compared to captopril-treated controls. S-Nitrosoglutathione 154-174 insulin Canis lupus familiaris 111-118 15277664-7 2004 When hTrx was partially S-nitrosated by preincubation with S-nitrosoglutathione, its cardioprotective effect was markedly enhanced. S-Nitrosoglutathione 59-79 thioredoxin Homo sapiens 5-9 15524165-2 2004 In this study, we examined the possible diabetogenicity of NO by noting differences in the cellular binding of insulin in dogs treated with the NO donor, S-nitrosoglutathione (GSNO) compared to captopril-treated controls. S-Nitrosoglutathione 176-180 insulin Canis lupus familiaris 111-118 27520663-2 2004 In this study, we examined the possible diabetogenicity of NO by noting differences in the cellular binding of insulin in dogs treated with the NO donor, S-nitrosoglutathione (GSNO) compared to captopril-treated controls. S-Nitrosoglutathione 176-180 insulin Canis lupus familiaris 111-118 15524165-3 2004 GSNO administration resulted in an abnormality in glucose metabolism which was attributed to decreased binding of insulin to its receptor on the cell membrane of mononuclear leucocytes, 11.60 +/- 0.60% in GSNO-treated dogs compared with 18.10 +/- 1.90% in captopril-treated control (p < 0.05). S-Nitrosoglutathione 0-4 insulin Canis lupus familiaris 114-121 27520663-3 2004 GSNO administration resulted in an abnormality in glucose metabolism which was attributed to decreased binding of insulin to its receptor on the cell membrane of mononuclear leucocytes, 11.60 +- 0.60% in GSNO-treated dogs compared with 18.10 +- 1.90% in captopril-treated control (p < 0.05). S-Nitrosoglutathione 0-4 insulin Canis lupus familiaris 114-121 27520663-3 2004 GSNO administration resulted in an abnormality in glucose metabolism which was attributed to decreased binding of insulin to its receptor on the cell membrane of mononuclear leucocytes, 11.60 +- 0.60% in GSNO-treated dogs compared with 18.10 +- 1.90% in captopril-treated control (p < 0.05). S-Nitrosoglutathione 204-208 insulin Canis lupus familiaris 114-121 15524165-3 2004 GSNO administration resulted in an abnormality in glucose metabolism which was attributed to decreased binding of insulin to its receptor on the cell membrane of mononuclear leucocytes, 11.60 +/- 0.60% in GSNO-treated dogs compared with 18.10 +/- 1.90% in captopril-treated control (p < 0.05). S-Nitrosoglutathione 205-209 insulin Canis lupus familiaris 114-121 27520663-4 2004 The decreased insulin binding was attributed to decreased insulin receptor sites per cell, 21.43 +- 2.51 x 10(4) in GSNO-treated dogs compared with 26.60 +- 1.57 x 10(4) in captopril-treated controls (p < 0.05). S-Nitrosoglutathione 116-120 insulin Canis lupus familiaris 14-21 27520663-4 2004 The decreased insulin binding was attributed to decreased insulin receptor sites per cell, 21.43 +- 2.51 x 10(4) in GSNO-treated dogs compared with 26.60 +- 1.57 x 10(4) in captopril-treated controls (p < 0.05). S-Nitrosoglutathione 116-120 insulin receptor Canis lupus familiaris 58-74 27520663-7 2004 It appears that GSNO is exerting its effect by decreasing the number of insulin receptor sites and/or decreasing the average receptor affinity. S-Nitrosoglutathione 16-20 insulin receptor Canis lupus familiaris 72-88 15524165-4 2004 The decreased insulin binding was attributed to decreased insulin receptor sites per cell, 21.43 +/- 2.51 x 10(4) in GSNO-treated dogs compared with 26.60 +/- 1.57 x 10(4) in captopril-treated controls (p < 0.05). S-Nitrosoglutathione 117-121 insulin Canis lupus familiaris 14-21 15524165-4 2004 The decreased insulin binding was attributed to decreased insulin receptor sites per cell, 21.43 +/- 2.51 x 10(4) in GSNO-treated dogs compared with 26.60 +/- 1.57 x 10(4) in captopril-treated controls (p < 0.05). S-Nitrosoglutathione 117-121 insulin receptor Canis lupus familiaris 58-74 15524165-7 2004 It appears that GSNO is exerting its effect by decreasing the number of insulin receptor sites and/or decreasing the average receptor affinity. S-Nitrosoglutathione 16-20 insulin receptor Canis lupus familiaris 72-88 15223363-4 2004 At the same time, GSNO downregulated the expression of the antiapoptotic gene Sarco/endoplasmic reticulum calcium-ATPase (SERCA2b) in parallel with the downregulation of the antiapoptotic ER chaperones-glucose-regulated protein genes (Grp78 and Grp94). S-Nitrosoglutathione 18-22 heat shock protein family A (Hsp70) member 5 Homo sapiens 235-240 15223363-4 2004 At the same time, GSNO downregulated the expression of the antiapoptotic gene Sarco/endoplasmic reticulum calcium-ATPase (SERCA2b) in parallel with the downregulation of the antiapoptotic ER chaperones-glucose-regulated protein genes (Grp78 and Grp94). S-Nitrosoglutathione 18-22 heat shock protein 90 beta family member 1 Homo sapiens 245-250 15126088-2 2004 Using an inferior epigastric artery skin flap as a flap ischemia/reperfusion (I/R) injury model, we investigated whether the administration of a nitric oxide (NO) donor, nitrosoglutathione (GSNO), could decrease platelet activation and modulate the NO synthase (NOS) activity of platelets and promote flap survival. S-Nitrosoglutathione 170-188 nitric oxide synthase 2 Homo sapiens 249-260 15275867-5 2004 Hence, we have analyzed the expression of IRAK-M in human monocytes following exposure to a NO donor (GSNO) and we have observed that GSNO was capable of inducing IRAK-M mRNA and protein expression 8 and 20 h after stimulation, respectively. S-Nitrosoglutathione 102-106 interleukin 1 receptor associated kinase 3 Homo sapiens 42-48 15275867-5 2004 Hence, we have analyzed the expression of IRAK-M in human monocytes following exposure to a NO donor (GSNO) and we have observed that GSNO was capable of inducing IRAK-M mRNA and protein expression 8 and 20 h after stimulation, respectively. S-Nitrosoglutathione 134-138 interleukin 1 receptor associated kinase 3 Homo sapiens 42-48 15275867-5 2004 Hence, we have analyzed the expression of IRAK-M in human monocytes following exposure to a NO donor (GSNO) and we have observed that GSNO was capable of inducing IRAK-M mRNA and protein expression 8 and 20 h after stimulation, respectively. S-Nitrosoglutathione 134-138 interleukin 1 receptor associated kinase 3 Homo sapiens 163-169 15275867-7 2004 Furthermore, the expression of IRAK-M induced by GSNO was inhibited by the presence of a blocking antibody raised against TNF-alpha. S-Nitrosoglutathione 49-53 interleukin 1 receptor associated kinase 3 Homo sapiens 31-37 15275867-7 2004 Furthermore, the expression of IRAK-M induced by GSNO was inhibited by the presence of a blocking antibody raised against TNF-alpha. S-Nitrosoglutathione 49-53 tumor necrosis factor Homo sapiens 122-131 15126088-8 2004 Survival areas were assessed at 7 days postoperatively RESULTS: An optimal dose of GSNO (0.6 mg/kg), significantly decreased in CD62P expression on platelets (P < 0.001) and its deposition on the flap vessels, selectively suppressed iNOS induction of platelet, and significantly improved blood perfusion and the flap survival rate (59.8 +/- 4.9% versus 22.1 +/- 6.1%, P < 0.001). S-Nitrosoglutathione 83-87 selectin P Homo sapiens 128-133 15126088-8 2004 Survival areas were assessed at 7 days postoperatively RESULTS: An optimal dose of GSNO (0.6 mg/kg), significantly decreased in CD62P expression on platelets (P < 0.001) and its deposition on the flap vessels, selectively suppressed iNOS induction of platelet, and significantly improved blood perfusion and the flap survival rate (59.8 +/- 4.9% versus 22.1 +/- 6.1%, P < 0.001). S-Nitrosoglutathione 83-87 nitric oxide synthase 2 Homo sapiens 236-240 15126088-10 2004 CONCLUSION: This study suggests that GSNO can appropriately donate NO to suppress platelet activation and platelet iNOS induction, resulting in less platelet activation, better blood perfusion, and flap survival after I/R injury. S-Nitrosoglutathione 37-41 nitric oxide synthase 2 Homo sapiens 115-119 14641087-4 2003 Exposure of platelets to GSNO (S-nitrosoglutathione) for as little as 5 s inhibited thrombin-induced platelet aggregation by >95%; however, AlbSNO (S-nitrosoalbumin) was much less effective over these short time periods. S-Nitrosoglutathione 25-29 coagulation factor II, thrombin Homo sapiens 84-92 15110396-3 2004 Herein we report experimental evidence supporting the contention that this NOS2 effect is mediated, at least in part, by S-nitrosoglutathione (GSNO), a potent antioxidant derived from interaction of NO and glutathione. S-Nitrosoglutathione 121-141 nitric oxide synthase 2 Homo sapiens 75-79 15110396-3 2004 Herein we report experimental evidence supporting the contention that this NOS2 effect is mediated, at least in part, by S-nitrosoglutathione (GSNO), a potent antioxidant derived from interaction of NO and glutathione. S-Nitrosoglutathione 143-147 nitric oxide synthase 2 Homo sapiens 75-79 15110396-7 2004 Finally, neocuproine, a selective cuprous ion chelator known to neutralize GSNO actions, abolished NOS2-mediated chemoresistance against carbamoylating agents. S-Nitrosoglutathione 75-79 nitric oxide synthase 2 Homo sapiens 99-103 15110396-8 2004 Our results reveal a novel action of NOS2/GSNO that may potentially contribute to the development of chemoresistance against BCNU, which remains a mainstay in chemotherapy for glioblastoma multiforme. S-Nitrosoglutathione 42-46 nitric oxide synthase 2 Homo sapiens 37-41 14657004-4 2004 Treatment with the NO donor sodium nitroprusside reduced levels of HIF-1alpha, whereas NO donors, NOC-18 and S-nitrosoglutathione, increased HIF-1alpha levels. S-Nitrosoglutathione 109-129 hypoxia inducible factor 1 subunit alpha Homo sapiens 141-151 14766015-0 2004 Concentration-dependent effects of endogenous S-nitrosoglutathione on gene regulation by specificity proteins Sp3 and Sp1. S-Nitrosoglutathione 46-66 Sp3 transcription factor Homo sapiens 110-113 14766015-2 2004 In the present study, we have studied the effect of physiological (low microM) concentrations of the endogenous S-nitrosothiol, GSNO (S-nitrosoglutathione), on the activities of nuclear regulatory proteins Sp3 and Sp1 (specificity proteins 3 and 1). S-Nitrosoglutathione 128-132 Sp3 transcription factor Homo sapiens 206-209 14766015-2 2004 In the present study, we have studied the effect of physiological (low microM) concentrations of the endogenous S-nitrosothiol, GSNO (S-nitrosoglutathione), on the activities of nuclear regulatory proteins Sp3 and Sp1 (specificity proteins 3 and 1). S-Nitrosoglutathione 134-154 Sp3 transcription factor Homo sapiens 206-209 14766015-3 2004 Low concentrations of GSNO increased Sp3 binding, as well as Sp3-dependent transcription of the cystic fibrosis transmembrane conductance regulatory gene, cftr. S-Nitrosoglutathione 22-26 Sp3 transcription factor Homo sapiens 37-40 14766015-3 2004 Low concentrations of GSNO increased Sp3 binding, as well as Sp3-dependent transcription of the cystic fibrosis transmembrane conductance regulatory gene, cftr. S-Nitrosoglutathione 22-26 CF transmembrane conductance regulator Homo sapiens 155-159 14766015-4 2004 However, higher GSNO levels prevented Sp3 binding, augmented Sp1 binding and prevented both cftr transcription and CFTR (cystic fibrosis transmembrane conductance regulator) expression. S-Nitrosoglutathione 16-20 Sp3 transcription factor Homo sapiens 38-41 14766015-4 2004 However, higher GSNO levels prevented Sp3 binding, augmented Sp1 binding and prevented both cftr transcription and CFTR (cystic fibrosis transmembrane conductance regulator) expression. S-Nitrosoglutathione 16-20 CF transmembrane conductance regulator Homo sapiens 92-96 14766015-4 2004 However, higher GSNO levels prevented Sp3 binding, augmented Sp1 binding and prevented both cftr transcription and CFTR (cystic fibrosis transmembrane conductance regulator) expression. S-Nitrosoglutathione 16-20 CF transmembrane conductance regulator Homo sapiens 115-119 14766015-4 2004 However, higher GSNO levels prevented Sp3 binding, augmented Sp1 binding and prevented both cftr transcription and CFTR (cystic fibrosis transmembrane conductance regulator) expression. S-Nitrosoglutathione 16-20 CF transmembrane conductance regulator Homo sapiens 121-172 14766015-5 2004 We conclude that low concentrations of GSNO favour Sp3 binding to "housekeeping" genes such as cftr, whereas nitrosative stress-associated GSNO concentrations shut off Sp3-dependent transcription, possibly to redirect cellular resources. S-Nitrosoglutathione 39-43 Sp3 transcription factor Homo sapiens 51-54 14766015-5 2004 We conclude that low concentrations of GSNO favour Sp3 binding to "housekeeping" genes such as cftr, whereas nitrosative stress-associated GSNO concentrations shut off Sp3-dependent transcription, possibly to redirect cellular resources. S-Nitrosoglutathione 39-43 CF transmembrane conductance regulator Homo sapiens 95-99 14766015-6 2004 Since low micromolar concentrations of GSNO also increase the maturation and activity of a clinically common CFTR mutant, whereas higher concentrations have the opposite effect, these observations may have implications for dosing of S-nitrosylating agents used in cystic fibrosis clinical trials. S-Nitrosoglutathione 39-43 CF transmembrane conductance regulator Homo sapiens 109-113 15041968-0 2004 Nitrosoglutathione improves blood perfusion and flap survival by suppressing iNOS but protecting eNOS expression in the flap vessels after ischemia/reperfusion injury. S-Nitrosoglutathione 0-18 nitric oxide synthase 2 Rattus norvegicus 77-81 15041968-0 2004 Nitrosoglutathione improves blood perfusion and flap survival by suppressing iNOS but protecting eNOS expression in the flap vessels after ischemia/reperfusion injury. S-Nitrosoglutathione 0-18 nitric oxide synthase 3 Rattus norvegicus 97-101 15041968-13 2004 CONCLUSION: This study indicates that intravenous administration of exogenous GSNO can appropriately donate NO to suppress iNOS induction and enhance eNOS expression in pedicle vessels, resulting in better blood perfusion and a higher flap survival after I/R injury. S-Nitrosoglutathione 78-82 nitric oxide synthase 2 Rattus norvegicus 123-127 15041968-13 2004 CONCLUSION: This study indicates that intravenous administration of exogenous GSNO can appropriately donate NO to suppress iNOS induction and enhance eNOS expression in pedicle vessels, resulting in better blood perfusion and a higher flap survival after I/R injury. S-Nitrosoglutathione 78-82 nitric oxide synthase 3 Rattus norvegicus 150-154 14600153-4 2004 We demonstrate that exposure of cells to the NO donor NOC18 or S-nitrosoglutathione induces HIF-1alpha expression and transcriptional activity. S-Nitrosoglutathione 63-83 hypoxia inducible factor 1 subunit alpha Homo sapiens 92-102 14641087-4 2003 Exposure of platelets to GSNO (S-nitrosoglutathione) for as little as 5 s inhibited thrombin-induced platelet aggregation by >95%; however, AlbSNO (S-nitrosoalbumin) was much less effective over these short time periods. S-Nitrosoglutathione 31-51 coagulation factor II, thrombin Homo sapiens 84-92 14641087-6 2003 The gamma-glutamyl transpeptidase inhibitor acivicin (100 microM) partially decreased GSNO decay, whereas the membrane-impermeable thiol-blocking agent 5,5"-dithiobis-(2-nitrobenzoic acid) (100 microM) completely blocked cell-mediated GSNO decay and partially blocked AlbSNO decay. S-Nitrosoglutathione 86-90 inactive glutathione hydrolase 2 Homo sapiens 4-33 12837761-0 2003 Mammalian osmolytes and S-nitrosoglutathione promote Delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) protein maturation and function. S-Nitrosoglutathione 24-44 CF transmembrane conductance regulator Homo sapiens 117-121 14624585-8 2003 Addition of 1 microM GSNO (Cysbeta93/GSNO = 1) to solutions diluted 10(4)-fold from physiological concentrations of oxyHb and CuZnSOD resulted largely in metHb formation. S-Nitrosoglutathione 21-25 superoxide dismutase 1 Homo sapiens 126-133 14624585-9 2003 Thus, this work reports the following key findings: CuZnSOD is an efficient catalyst of NO transfer between GSNO and Cysbeta93 of oxyHb; metHb is not detected in oxyHb/GSNO incubates containing close to the physiological concentration (5 mM) of Hb and CuZnSOD when the Cysbeta93/GSNO molar ratio is 0.5 to 1.0, but metHb is detected when the total Hb concentration is low micromolar. S-Nitrosoglutathione 108-112 superoxide dismutase 1 Homo sapiens 52-59 14624585-9 2003 Thus, this work reports the following key findings: CuZnSOD is an efficient catalyst of NO transfer between GSNO and Cysbeta93 of oxyHb; metHb is not detected in oxyHb/GSNO incubates containing close to the physiological concentration (5 mM) of Hb and CuZnSOD when the Cysbeta93/GSNO molar ratio is 0.5 to 1.0, but metHb is detected when the total Hb concentration is low micromolar. S-Nitrosoglutathione 168-172 superoxide dismutase 1 Homo sapiens 52-59 14624585-9 2003 Thus, this work reports the following key findings: CuZnSOD is an efficient catalyst of NO transfer between GSNO and Cysbeta93 of oxyHb; metHb is not detected in oxyHb/GSNO incubates containing close to the physiological concentration (5 mM) of Hb and CuZnSOD when the Cysbeta93/GSNO molar ratio is 0.5 to 1.0, but metHb is detected when the total Hb concentration is low micromolar. S-Nitrosoglutathione 168-172 superoxide dismutase 1 Homo sapiens 52-59 14624585-10 2003 These results suggest that erythrocyte CuZnSOD may play a critical role in preserving the biological activity of NO by targeting it from GSNO to Cysbeta93 of oxyHb rather than to its oxyheme. S-Nitrosoglutathione 137-141 superoxide dismutase 1 Homo sapiens 39-46 14568959-4 2003 S-nitrosoglutathione or S-nitroso-N-acetyl-D-penicillamine, but not their non-NO-releasing analogues, inhibited proliferation induced by PHA or IL-2, the effect declining progressively from 48 to 0 h pre-exposure to the mitogen. S-Nitrosoglutathione 0-20 interleukin 2 Homo sapiens 144-148 12962704-7 2003 Low molecular weight NO donors, such as S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione (GSNO), inactivate rhodanese and are much more effective in this regard (100% inhibition at 2.5mM) than such known inhibitors of this enzyme, as N-ethylmaleimide (NEM) (25 mM < 50%) or sulfates(IV) (90% inhibition at 5mM). S-Nitrosoglutathione 83-103 thiosulfate sulfurtransferase Bos taurus 123-132 12962704-7 2003 Low molecular weight NO donors, such as S-nitroso-N-acetylpenicillamine (SNAP) and S-nitrosoglutathione (GSNO), inactivate rhodanese and are much more effective in this regard (100% inhibition at 2.5mM) than such known inhibitors of this enzyme, as N-ethylmaleimide (NEM) (25 mM < 50%) or sulfates(IV) (90% inhibition at 5mM). S-Nitrosoglutathione 105-109 thiosulfate sulfurtransferase Bos taurus 123-132 14732341-4 2003 We now report that formaldehyde dehydrogenase, an enzyme that decomposes S-nitrosoglutathione, can indirectly regulate the level of cellular protein S-nitrosation. S-Nitrosoglutathione 73-93 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 19-45 14732341-12 2003 Inhibition of glutathione reductase, the enzyme that converts oxidized to reduced glutathione, by dehydroepiandrosterone similarly increased protein S-nitrosation and S-nitrosoglutathione levels in both cell lines. S-Nitrosoglutathione 167-187 glutathione-disulfide reductase Homo sapiens 14-35 14732341-13 2003 Our results provide the first evidence that formaldehyde dehydrogenase-dependent decomposition of S-nitrosoglutathione plays a role in protecting against nitrogen oxide-mediated protein S-nitrosation. S-Nitrosoglutathione 98-118 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 44-70 12837761-10 2003 Interestingly, a small molecule, S-nitrosoglutathione, which is a substrate for gamma glutamyltranspeptidase, an abundant enzyme in the kidney, likewise promoted Delta F508 CFTR maturation and function. S-Nitrosoglutathione 33-53 inactive glutathione hydrolase 2 Homo sapiens 80-108 12837761-10 2003 Interestingly, a small molecule, S-nitrosoglutathione, which is a substrate for gamma glutamyltranspeptidase, an abundant enzyme in the kidney, likewise promoted Delta F508 CFTR maturation and function. S-Nitrosoglutathione 33-53 CF transmembrane conductance regulator Homo sapiens 173-177 12837761-11 2003 S-Nitrosoglutathione-corrected Delta F508 CFTR exhibited a shorter half-life as compared with wild type CFTR. S-Nitrosoglutathione 0-20 CF transmembrane conductance regulator Homo sapiens 42-46 12837761-11 2003 S-Nitrosoglutathione-corrected Delta F508 CFTR exhibited a shorter half-life as compared with wild type CFTR. S-Nitrosoglutathione 0-20 CF transmembrane conductance regulator Homo sapiens 104-108 13678430-5 2003 Moreover, GSNO induced a dose-dependent decrease of IL-10 and enhancement of tumor necrosis factor-alpha (TNF-alpha) release from mature DCs. S-Nitrosoglutathione 10-14 interleukin 10 Homo sapiens 52-57 12925778-3 2003 We determined molecular mechanisms of HIF-1alpha accumulation under the impact of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 82-102 hypoxia inducible factor 1 subunit alpha Homo sapiens 38-48 12925778-3 2003 We determined molecular mechanisms of HIF-1alpha accumulation under the impact of S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 104-108 hypoxia inducible factor 1 subunit alpha Homo sapiens 38-48 12925778-4 2003 In human embryonic kidney cells GSNO provoked nuclear accumulation of HIF-1alpha. S-Nitrosoglutathione 32-36 hypoxia inducible factor 1 subunit alpha Homo sapiens 70-80 12925778-6 2003 Indeed, GSNO as well as the hypoxia mimic CoCl2 decreased ubiquitination of HIF-1alpha and GSNO-induced HIF-1alpha failed to coimmunoprecipitate with pVHL (von Hippel Lindau protein). S-Nitrosoglutathione 8-12 hypoxia inducible factor 1 subunit alpha Homo sapiens 76-86 12925778-7 2003 Considering that HIF-1alpha-pVHL interactions require prolyl hydroxylation of HIF-1alpha, we went on to demonstrate inhibition of HIF-1alpha prolyl hydroxylases (PHDs) by GSNO. S-Nitrosoglutathione 171-175 hypoxia inducible factor 1 subunit alpha Homo sapiens 17-27 12925778-7 2003 Considering that HIF-1alpha-pVHL interactions require prolyl hydroxylation of HIF-1alpha, we went on to demonstrate inhibition of HIF-1alpha prolyl hydroxylases (PHDs) by GSNO. S-Nitrosoglutathione 171-175 von Hippel-Lindau tumor suppressor Homo sapiens 28-32 12925778-7 2003 Considering that HIF-1alpha-pVHL interactions require prolyl hydroxylation of HIF-1alpha, we went on to demonstrate inhibition of HIF-1alpha prolyl hydroxylases (PHDs) by GSNO. S-Nitrosoglutathione 171-175 hypoxia inducible factor 1 subunit alpha Homo sapiens 78-88 12925778-7 2003 Considering that HIF-1alpha-pVHL interactions require prolyl hydroxylation of HIF-1alpha, we went on to demonstrate inhibition of HIF-1alpha prolyl hydroxylases (PHDs) by GSNO. S-Nitrosoglutathione 171-175 hypoxia inducible factor 1 subunit alpha Homo sapiens 78-88 12925778-8 2003 In vitro HIF-1alpha-pVHL interactions revealed that GSNO dose-dependently inhibits PHD activity but not the interaction of a synthetic peptide resembling the hydroxylated oxygen-dependent degradation domain of HIF-1alpha with pVHL. S-Nitrosoglutathione 52-56 von Hippel-Lindau tumor suppressor Homo sapiens 20-24 12925778-9 2003 We conclude that GSNO-attenuated prolyl hydroxylase activity accounts for HIF-1alpha accumulation under conditions of NO formation during normoxia and that PHD activity is subject to regulation by NO. S-Nitrosoglutathione 17-21 hypoxia inducible factor 1 subunit alpha Homo sapiens 74-84 12897144-2 2003 Both GSNO and SNAP increased Akt phosphorylation and activity, which were blocked by cotreatment with the PI3 kinase inhibitor wortmannin. S-Nitrosoglutathione 5-9 AKT serine/threonine kinase 1 Homo sapiens 29-32 12801522-4 2003 Stimulation of HEK-293 cells with S-nitrosoglutathione (GSNO) for 2, 4, 8, and 16h also caused Trx S-nitrosylation, which showed straight correlation with ASK1 activation based on Western blot detection of the enzyme, immunoprecipitation assay, and measurement of its catalytic activity. S-Nitrosoglutathione 34-54 thioredoxin Homo sapiens 95-98 12801522-4 2003 Stimulation of HEK-293 cells with S-nitrosoglutathione (GSNO) for 2, 4, 8, and 16h also caused Trx S-nitrosylation, which showed straight correlation with ASK1 activation based on Western blot detection of the enzyme, immunoprecipitation assay, and measurement of its catalytic activity. S-Nitrosoglutathione 34-54 mitogen-activated protein kinase kinase kinase 5 Homo sapiens 155-159 12801522-4 2003 Stimulation of HEK-293 cells with S-nitrosoglutathione (GSNO) for 2, 4, 8, and 16h also caused Trx S-nitrosylation, which showed straight correlation with ASK1 activation based on Western blot detection of the enzyme, immunoprecipitation assay, and measurement of its catalytic activity. S-Nitrosoglutathione 56-60 thioredoxin Homo sapiens 95-98 12801522-4 2003 Stimulation of HEK-293 cells with S-nitrosoglutathione (GSNO) for 2, 4, 8, and 16h also caused Trx S-nitrosylation, which showed straight correlation with ASK1 activation based on Western blot detection of the enzyme, immunoprecipitation assay, and measurement of its catalytic activity. S-Nitrosoglutathione 56-60 mitogen-activated protein kinase kinase kinase 5 Homo sapiens 155-159 12801522-6 2003 Treatment of cells with N-acetyl-cysteine for 2h after 8h of pretreatment with GSNO caused an increase in glutathione and nullified ASK1 activation. S-Nitrosoglutathione 79-83 mitogen-activated protein kinase kinase kinase 5 Homo sapiens 132-136 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 54-74 CD40 ligand Homo sapiens 153-164 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 54-74 interferon gamma Homo sapiens 284-300 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 54-74 interferon gamma Homo sapiens 302-311 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 54-74 interleukin 5 Homo sapiens 335-348 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 54-74 interleukin 5 Homo sapiens 350-354 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 76-80 CD40 ligand Homo sapiens 153-164 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 76-80 interferon gamma Homo sapiens 284-300 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 76-80 interferon gamma Homo sapiens 302-311 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 76-80 interleukin 5 Homo sapiens 335-348 13678430-3 2003 In this study, we found that addition of the NO donor S-nitrosoglutathione (GSNO) to monocyte-derived DCs matured by lipopolysaccharide (LPS) or soluble CD40 ligand led to a decreased capacity to activate naive allogeneic T cells but a more prominent Th1 polarization, with increased interferon-gamma (IFN-gamma) secretion and reduced interleukin-5 (IL-5) release. S-Nitrosoglutathione 76-80 interleukin 5 Homo sapiens 350-354 13678430-5 2003 Moreover, GSNO induced a dose-dependent decrease of IL-10 and enhancement of tumor necrosis factor-alpha (TNF-alpha) release from mature DCs. S-Nitrosoglutathione 10-14 tumor necrosis factor Homo sapiens 77-104 13678430-5 2003 Moreover, GSNO induced a dose-dependent decrease of IL-10 and enhancement of tumor necrosis factor-alpha (TNF-alpha) release from mature DCs. S-Nitrosoglutathione 10-14 tumor necrosis factor Homo sapiens 106-115 13678430-7 2003 Finally, GSNO significantly reduced the release of IP-10/CXCL10 and RANTES/CCL5 but not IL-8/CXCL8 by mature DCs. S-Nitrosoglutathione 9-13 C-X-C motif chemokine ligand 10 Homo sapiens 51-56 13678430-7 2003 Finally, GSNO significantly reduced the release of IP-10/CXCL10 and RANTES/CCL5 but not IL-8/CXCL8 by mature DCs. S-Nitrosoglutathione 9-13 C-X-C motif chemokine ligand 10 Homo sapiens 57-63 13678430-7 2003 Finally, GSNO significantly reduced the release of IP-10/CXCL10 and RANTES/CCL5 but not IL-8/CXCL8 by mature DCs. S-Nitrosoglutathione 9-13 C-C motif chemokine ligand 5 Homo sapiens 68-74 13678430-7 2003 Finally, GSNO significantly reduced the release of IP-10/CXCL10 and RANTES/CCL5 but not IL-8/CXCL8 by mature DCs. S-Nitrosoglutathione 9-13 C-C motif chemokine ligand 5 Homo sapiens 75-79 12556467-10 2003 GRx also enhanced the rate of S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase with GSSG or S-nitrosoglutathione, but these glutathionyl donors were much less efficient. S-Nitrosoglutathione 107-127 glutaredoxin Homo sapiens 0-3 12901850-2 2003 We have observed that nitrosoglutathione or another NO-generating compound spermine NONOate caused significant accumulation of IL-8 mRNA. S-Nitrosoglutathione 22-40 C-X-C motif chemokine ligand 8 Homo sapiens 127-131 14608681-3 2003 Taking into account the character of DNA damages being formed under NO activity, we proposed a formation of the SOS signal and induction the SOS DNA repair response in E. coli cells treated with NO physiological donors--DNIC and GSNO. S-Nitrosoglutathione 229-233 xylosyltransferase 2 Homo sapiens 112-115 14608681-3 2003 Taking into account the character of DNA damages being formed under NO activity, we proposed a formation of the SOS signal and induction the SOS DNA repair response in E. coli cells treated with NO physiological donors--DNIC and GSNO. S-Nitrosoglutathione 229-233 xylosyltransferase 2 Homo sapiens 141-144 12566444-8 2003 Moreover, S-nitrosoglutathione and S-nitroso-N-acetylpenicillamine directly blocked the activity of recombinant caspase-3, which was reversed by the reducing agent dithiothreitol, whereas PAPA or DEA NONOate did not block the enzymatic activity of caspase-3. S-Nitrosoglutathione 10-30 caspase 3 Homo sapiens 112-121 12566444-8 2003 Moreover, S-nitrosoglutathione and S-nitroso-N-acetylpenicillamine directly blocked the activity of recombinant caspase-3, which was reversed by the reducing agent dithiothreitol, whereas PAPA or DEA NONOate did not block the enzymatic activity of caspase-3. S-Nitrosoglutathione 10-30 caspase 3 Homo sapiens 248-257 12641465-1 2003 Mass spectrometry and UV-vis absorption results support a mechanism for NO donation by S-nitrosoglutathione (GSNO) to recombinant human brain calbindin D(28K) (rHCaBP) that requires the presence of trace copper, added as either Cu,Zn-superoxide dismutase (CuZnSOD) or CuSO(4). S-Nitrosoglutathione 87-107 superoxide dismutase 1 Homo sapiens 228-254 12620896-7 2003 Addition of the structurally unrelated NO donors S-nitrosoglutathione (300 microM) or sodium nitroprusside (1 mM) before low shear stress significantly increased cytoplasmic IkappaBalpha and concomitantly reduced NF-kappaB binding activity and kappaB-dependent VCAM-1 promoter activity. S-Nitrosoglutathione 49-69 NFKB inhibitor alpha Homo sapiens 174-186 12620896-7 2003 Addition of the structurally unrelated NO donors S-nitrosoglutathione (300 microM) or sodium nitroprusside (1 mM) before low shear stress significantly increased cytoplasmic IkappaBalpha and concomitantly reduced NF-kappaB binding activity and kappaB-dependent VCAM-1 promoter activity. S-Nitrosoglutathione 49-69 nuclear factor kappa B subunit 1 Homo sapiens 213-222 12620896-7 2003 Addition of the structurally unrelated NO donors S-nitrosoglutathione (300 microM) or sodium nitroprusside (1 mM) before low shear stress significantly increased cytoplasmic IkappaBalpha and concomitantly reduced NF-kappaB binding activity and kappaB-dependent VCAM-1 promoter activity. S-Nitrosoglutathione 49-69 nuclear factor kappa B subunit 1 Homo sapiens 175-181 12620896-7 2003 Addition of the structurally unrelated NO donors S-nitrosoglutathione (300 microM) or sodium nitroprusside (1 mM) before low shear stress significantly increased cytoplasmic IkappaBalpha and concomitantly reduced NF-kappaB binding activity and kappaB-dependent VCAM-1 promoter activity. S-Nitrosoglutathione 49-69 vascular cell adhesion molecule 1 Homo sapiens 261-267 12727790-6 2003 GSNO increased PGE(2) production and induced COX-1 and COX-2 protein expression in a dose- and time-dependent manner. S-Nitrosoglutathione 0-4 mitochondrially encoded cytochrome c oxidase I Homo sapiens 45-50 12727790-6 2003 GSNO increased PGE(2) production and induced COX-1 and COX-2 protein expression in a dose- and time-dependent manner. S-Nitrosoglutathione 0-4 prostaglandin-endoperoxide synthase 2 Homo sapiens 55-60 12641465-1 2003 Mass spectrometry and UV-vis absorption results support a mechanism for NO donation by S-nitrosoglutathione (GSNO) to recombinant human brain calbindin D(28K) (rHCaBP) that requires the presence of trace copper, added as either Cu,Zn-superoxide dismutase (CuZnSOD) or CuSO(4). S-Nitrosoglutathione 87-107 superoxide dismutase 1 Homo sapiens 256-263 12641465-1 2003 Mass spectrometry and UV-vis absorption results support a mechanism for NO donation by S-nitrosoglutathione (GSNO) to recombinant human brain calbindin D(28K) (rHCaBP) that requires the presence of trace copper, added as either Cu,Zn-superoxide dismutase (CuZnSOD) or CuSO(4). S-Nitrosoglutathione 109-113 superoxide dismutase 1 Homo sapiens 228-254 12641465-1 2003 Mass spectrometry and UV-vis absorption results support a mechanism for NO donation by S-nitrosoglutathione (GSNO) to recombinant human brain calbindin D(28K) (rHCaBP) that requires the presence of trace copper, added as either Cu,Zn-superoxide dismutase (CuZnSOD) or CuSO(4). S-Nitrosoglutathione 109-113 superoxide dismutase 1 Homo sapiens 256-263 12641465-9 2003 S-nitrosation is rapidly gaining recognition as a major form of protein posttranslational modification, and the efficient S-nitrosation of CaBP by CuZnSOD/GSNO is speculated to be of neurochemical importance given that CaBP and CuZnSOD are abundant in neurons. S-Nitrosoglutathione 155-159 S100 calcium binding protein G Homo sapiens 139-143 12641465-9 2003 S-nitrosation is rapidly gaining recognition as a major form of protein posttranslational modification, and the efficient S-nitrosation of CaBP by CuZnSOD/GSNO is speculated to be of neurochemical importance given that CaBP and CuZnSOD are abundant in neurons. S-Nitrosoglutathione 155-159 superoxide dismutase 1 Homo sapiens 147-154 12641465-9 2003 S-nitrosation is rapidly gaining recognition as a major form of protein posttranslational modification, and the efficient S-nitrosation of CaBP by CuZnSOD/GSNO is speculated to be of neurochemical importance given that CaBP and CuZnSOD are abundant in neurons. S-Nitrosoglutathione 155-159 S100 calcium binding protein G Homo sapiens 219-223 12509428-7 2003 Here we report that the NO donors NOC-12 and S-nitrosoglutathione both activate RyR1 by release of NO but do so independently of pO(2). S-Nitrosoglutathione 45-65 ryanodine receptor 1 Homo sapiens 80-84 12509428-9 2003 In contrast, S-nitrosoglutathione activates RyR1 by oxidation and S-nitrosylation of thiols other than Cys-3635 (and calmodulin is not involved). S-Nitrosoglutathione 13-33 ryanodine receptor 1 Homo sapiens 44-48 12484756-2 2002 Human glutathione-dependent formaldehyde dehydrogenase plays an important role in the metabolism of glutathione adducts such as S-(hydroxymethyl)glutathione and S-nitrosoglutathione. S-Nitrosoglutathione 161-181 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 6-54 12604202-4 2003 ADH3 (glutathione-dependent formaldehyde dehydrogenase) has been shown to catalyze the reductive breakdown of S-nitrosoglutathione, indicating involvement in nitric oxide metabolism. S-Nitrosoglutathione 110-130 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 0-4 12560087-5 2003 In vitro NO+ donating NO donors such as GSNO and SNAP provoked massive S-nitrosation of purified HIF-1 alpha. S-Nitrosoglutathione 40-44 hypoxia inducible factor 1 subunit alpha Homo sapiens 97-108 12560087-10 2003 In RCC4 and HEK293 cells GSNO or SNAP reproduced S-nitrosation of HIF-1 alpha, however with a significantly reduced potency that amounted to modification of three to four thiols, only. S-Nitrosoglutathione 25-29 solute carrier family 49 member 4 Homo sapiens 3-7 12560087-10 2003 In RCC4 and HEK293 cells GSNO or SNAP reproduced S-nitrosation of HIF-1 alpha, however with a significantly reduced potency that amounted to modification of three to four thiols, only. S-Nitrosoglutathione 25-29 hypoxia inducible factor 1 subunit alpha Homo sapiens 66-77 12496411-4 2003 The NO donors S-nitrosoglutathione and S-nitroso-N-acetylpenicillamine strongly down-regulated the adhesion of HMC-1 to FN. S-Nitrosoglutathione 14-34 fibronectin 1 Homo sapiens 120-122 12604204-1 2003 Human Class III alcohol dehydrogenase (ADH), also known as glutathione-dependent formaldehyde dehydrogenase plays an important role in the formaldehyde detoxification and reduction of the nitric oxide metabolite s-nitrosoglutathione (GSNO). S-Nitrosoglutathione 212-232 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 39-42 12604204-1 2003 Human Class III alcohol dehydrogenase (ADH), also known as glutathione-dependent formaldehyde dehydrogenase plays an important role in the formaldehyde detoxification and reduction of the nitric oxide metabolite s-nitrosoglutathione (GSNO). S-Nitrosoglutathione 212-232 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 81-107 12604204-1 2003 Human Class III alcohol dehydrogenase (ADH), also known as glutathione-dependent formaldehyde dehydrogenase plays an important role in the formaldehyde detoxification and reduction of the nitric oxide metabolite s-nitrosoglutathione (GSNO). S-Nitrosoglutathione 234-238 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 39-42 12604204-1 2003 Human Class III alcohol dehydrogenase (ADH), also known as glutathione-dependent formaldehyde dehydrogenase plays an important role in the formaldehyde detoxification and reduction of the nitric oxide metabolite s-nitrosoglutathione (GSNO). S-Nitrosoglutathione 234-238 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 81-107 12388547-8 2002 This effect was mimicked by the NO donor GSNO, suggesting that the inhibition of CB(1) expression was due to HIV-1 Tat + IFN-gamma-induced NO overexpression. S-Nitrosoglutathione 41-45 Tat Human immunodeficiency virus 1 115-118 12194971-3 2002 In vascular cells, agents that release NO and donate nitrosonium cation (NO(+)), such as S-nitrosoglutathione, are potent inducers of the antioxidant protein heme oxygenase 1 (HO-1) (Foresti, R., Clark, J. E., Green, C. J., and Motterlini, R. (1997) J. Biol. S-Nitrosoglutathione 89-109 heme oxygenase 1 Rattus norvegicus 158-174 12466243-16 2002 The release of TIMP-4 was reduced by prostacyclin and S-nitroso-glutathione (GSNO), an NO donor. S-Nitrosoglutathione 54-75 TIMP metallopeptidase inhibitor 4 Homo sapiens 15-21 12466243-16 2002 The release of TIMP-4 was reduced by prostacyclin and S-nitroso-glutathione (GSNO), an NO donor. S-Nitrosoglutathione 77-81 TIMP metallopeptidase inhibitor 4 Homo sapiens 15-21 12466243-20 2002 The recombinant TIMP-4 potentiated the recruitment inhibitor effects of GSNO. S-Nitrosoglutathione 72-76 TIMP metallopeptidase inhibitor 4 Homo sapiens 16-22 12194971-3 2002 In vascular cells, agents that release NO and donate nitrosonium cation (NO(+)), such as S-nitrosoglutathione, are potent inducers of the antioxidant protein heme oxygenase 1 (HO-1) (Foresti, R., Clark, J. E., Green, C. J., and Motterlini, R. (1997) J. Biol. S-Nitrosoglutathione 89-109 heme oxygenase 1 Rattus norvegicus 176-180 12199706-0 2002 Inactivation of annexin II tetramer by S-nitrosoglutathione. S-Nitrosoglutathione 39-59 annexin A2 Homo sapiens 16-26 12270130-3 2002 The ability of S-nitrosoglutathione to direct the DeltaF508-CFTR to the plasma membrane and restore the function of the cAMP-dependent chloride transport in cultured human airway epithelial cells has been studied. S-Nitrosoglutathione 15-35 CF transmembrane conductance regulator Homo sapiens 60-64 12270130-4 2002 Immunocytochemistry showed a time- and dose-dependent increase of apically located CFTR after GSNO treatment. S-Nitrosoglutathione 94-98 CF transmembrane conductance regulator Homo sapiens 83-87 12230634-5 2002 The elevated blood glucose levels were due to significant reduction in plasma insulin levels in the dogs treated with vitamin C and GSNO, or vitamin C and SNAP (P < 0.05). S-Nitrosoglutathione 132-136 insulin Canis lupus familiaris 78-85 12230634-6 2002 The decreased insulin response was associated with significant elevation of nitric oxide produced from GSNO and SNAP co-administered with vitamin C, as assessed by plasma nitrate/nitrite levels. S-Nitrosoglutathione 103-107 insulin Canis lupus familiaris 14-21 12368213-3 2002 In this study, we investigated whether the NO donors, S-nitrosoglutathione (GS-NO) and NOR-1, could regulate chemokine production by human keratinocytes activated with interferon-gamma and tumor necrosis factor-alpha. S-Nitrosoglutathione 54-74 interferon gamma Homo sapiens 168-216 12270130-0 2002 S-Nitrosoglutathione induces functional DeltaF508-CFTR in airway epithelial cells. S-Nitrosoglutathione 0-20 CF transmembrane conductance regulator Homo sapiens 50-54 12270130-2 2002 GSNO has recently been shown to increase maturation of CFTR in CF cell lines at physiological concentrations. S-Nitrosoglutathione 0-4 CF transmembrane conductance regulator Homo sapiens 55-59 12223547-2 2002 KOR was constitutively expressed in postnatal day 19 (P19) embryonal carcinoma stem cells and is suppressed by NO donors [sodium nitroprusside (SNP), 3-morpholinosydnonimine-1, and S-nitrosoglutathione] in P19 stem cells within 4 hr. S-Nitrosoglutathione 181-201 opioid receptor, kappa 1 Mus musculus 0-3 12110001-3 2002 This effect was mediated at least in part by inhibitory effects of GSNO on the transcription factor early growth response gene-1 (Egr-1) [10]. S-Nitrosoglutathione 67-71 early growth response 1 Rattus norvegicus 100-128 12200144-3 2002 SNAP, GSNO, NOC18, and NOR4 enhanced the VEGF reporter activity under normoxia and modulated the hypoxic induction. S-Nitrosoglutathione 6-10 vascular endothelial growth factor A Homo sapiens 41-45 12200144-7 2002 SNAP, GSNO, and NOC18 induced the accumulation of HIF-1alpha protein, while others did not. S-Nitrosoglutathione 6-10 hypoxia inducible factor 1 subunit alpha Homo sapiens 50-60 12200144-8 2002 These results suggest that SNAP, GSNO, and NOC compounds are suitable for pharmacological studies in HIF-1-mediated VEGF gene activation by NO. S-Nitrosoglutathione 33-37 vascular endothelial growth factor A Homo sapiens 116-120 12193733-3 2002 NO-releasing compounds (100 micro M S-nitrosoglutathione or 50 micro M spermine-NONOate) as well as inducible NO synthase induction provoked activation of PPARgamma. S-Nitrosoglutathione 36-56 peroxisome proliferator activated receptor gamma Homo sapiens 155-164 12110001-3 2002 This effect was mediated at least in part by inhibitory effects of GSNO on the transcription factor early growth response gene-1 (Egr-1) [10]. S-Nitrosoglutathione 67-71 early growth response 1 Rattus norvegicus 130-135 12110001-7 2002 RESULTS: Cultured rat MCs treated with GSNO for 8 hours were compared with unstimulated MCs and the CTGF mRNA was found to be down-regulated. S-Nitrosoglutathione 39-43 cellular communication network factor 2 Rattus norvegicus 100-104 12110001-9 2002 In parallel, down-regulation of CTGF protein by GSNO was observed by Western blot analysis. S-Nitrosoglutathione 48-52 cellular communication network factor 2 Rattus norvegicus 32-36 11967020-6 2002 RESULTS: Twenty-four hour treatment of mesangial cells with GSNO and SNAP (100 micromol/L each) increased the maximal binding of ADM to its receptor from 52%+/- 4% to 101%+/- 4% (P < 0.001) and 81%+/- 2% (P < 0.001), respectively. S-Nitrosoglutathione 60-64 adrenomedullin Rattus norvegicus 129-132 12089331-1 2002 S-nitrosoglutathione (GSNO, 50 microM) inhibited the initial rate of thrombin-catalyzed human and bovine fibrinogen polymerization by approximately 50% to 68% respectively. S-Nitrosoglutathione 0-20 coagulation factor II, thrombin Homo sapiens 69-77 12089331-1 2002 S-nitrosoglutathione (GSNO, 50 microM) inhibited the initial rate of thrombin-catalyzed human and bovine fibrinogen polymerization by approximately 50% to 68% respectively. S-Nitrosoglutathione 0-20 fibrinogen beta chain Homo sapiens 105-115 12089331-1 2002 S-nitrosoglutathione (GSNO, 50 microM) inhibited the initial rate of thrombin-catalyzed human and bovine fibrinogen polymerization by approximately 50% to 68% respectively. S-Nitrosoglutathione 22-26 coagulation factor II, thrombin Homo sapiens 69-77 12089331-1 2002 S-nitrosoglutathione (GSNO, 50 microM) inhibited the initial rate of thrombin-catalyzed human and bovine fibrinogen polymerization by approximately 50% to 68% respectively. S-Nitrosoglutathione 22-26 fibrinogen beta chain Homo sapiens 105-115 12089331-3 2002 The fact that the same concentration of GSNO had no effect on thrombin-dependent hydrolysis of tosylglycylprolylarginine-4-nitroanilide acetate suggested that this inhibition was due to GSNO-induced changes in fibrinogen structure. S-Nitrosoglutathione 186-190 fibrinogen beta chain Homo sapiens 210-220 12089331-4 2002 This result was confirmed by CD spectroscopy where GSNO or S-nitrosohomocysteine increased the alpha-helical content of fibrinogen by approximately 15% and 11%, respectively. S-Nitrosoglutathione 51-55 fibrinogen beta chain Homo sapiens 120-130 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 32-36 fibrinogen beta chain Homo sapiens 21-31 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 32-36 fibrinogen beta chain Homo sapiens 110-120 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 32-36 fibrinogen beta chain Homo sapiens 110-120 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 68-72 fibrinogen beta chain Homo sapiens 21-31 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 68-72 fibrinogen beta chain Homo sapiens 110-120 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 68-72 fibrinogen beta chain Homo sapiens 110-120 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 68-72 fibrinogen beta chain Homo sapiens 21-31 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 68-72 fibrinogen beta chain Homo sapiens 110-120 12089331-7 2002 Further evidence for fibrinogen-GSNO interactions was obtained from GSNO-dependent quenching of the intrinsic fibrinogen Trp fluorescence and the perturbation of the GSNO circular dichroic absorbance as a function of [fibrinogen]. S-Nitrosoglutathione 68-72 fibrinogen beta chain Homo sapiens 110-120 12089331-8 2002 The K(d)s of 3 to 10 microM for fibrinogen-GSNO interactions with a stoichiometry of 2:1 (GSNO:fibrinogen) were estimated from isothermal titration calorimetry and fluorescence quenching, respectively. S-Nitrosoglutathione 43-47 fibrinogen beta chain Homo sapiens 32-42 12089331-8 2002 The K(d)s of 3 to 10 microM for fibrinogen-GSNO interactions with a stoichiometry of 2:1 (GSNO:fibrinogen) were estimated from isothermal titration calorimetry and fluorescence quenching, respectively. S-Nitrosoglutathione 43-47 fibrinogen beta chain Homo sapiens 95-105 12180126-6 2002 Extensive inhibition of nitric oxide synthases with N-monomethyl-L-arginine however resulted in a larger increase in blood pressure, and infusion of the nitric oxide donor nitrosoglutathione caused less reduction in blood pressure in the EC-SOD null mice. S-Nitrosoglutathione 172-190 superoxide dismutase 3 Homo sapiens 238-244 12076958-7 2002 (3) The antioxidative potency of Trx was approximately 100 and 1,000 times greater than GSNO and GSH, respectively. S-Nitrosoglutathione 88-92 thioredoxin Homo sapiens 33-36 12119401-3 2002 Incubation of recombinant human Trx with glutathione disulfide or S-nitrosoglutathione led to the formation of glutathionylated Trx, identified by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. S-Nitrosoglutathione 66-86 thioredoxin Homo sapiens 32-35 12119401-3 2002 Incubation of recombinant human Trx with glutathione disulfide or S-nitrosoglutathione led to the formation of glutathionylated Trx, identified by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. S-Nitrosoglutathione 66-86 thioredoxin Homo sapiens 128-131 11947902-10 2002 Stabilisation of p53 was prevented by preincubation with the NO-donor GSNO or 8-br-cGMP, thus implying a downmodulatory effect of cGMP on pathways that upregulate the tumor suppressor p53. S-Nitrosoglutathione 70-74 tumor protein p53 Homo sapiens 17-20 11947902-10 2002 Stabilisation of p53 was prevented by preincubation with the NO-donor GSNO or 8-br-cGMP, thus implying a downmodulatory effect of cGMP on pathways that upregulate the tumor suppressor p53. S-Nitrosoglutathione 70-74 tumor protein p53 Homo sapiens 184-187 11967020-9 2002 In contrast, ADM receptor gene expression was reduced significantly by different concentrations of GSNO, SNAP, and by 50 micromol/L 8-bromo-cGMP, but not by 8-bromo-cAMP. S-Nitrosoglutathione 99-103 adrenomedullin Rattus norvegicus 13-16 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 cyclin dependent kinase inhibitor 1A Homo sapiens 228-232 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 heat shock protein family A (Hsp70) member 4 Homo sapiens 26-31 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 tumor protein p53 Homo sapiens 128-131 11996880-3 2002 In the present study, preincubation of purified rat liver microsomal GST with S-nitrosoglutathione (GSNO) or the nitric oxide (NO) donor, 1,1-diethyl-2-hydroxy-2-nitrosohydrazine (DEA/NO), resulted in a 2-fold increase in enzyme activity. S-Nitrosoglutathione 78-98 hematopoietic prostaglandin D synthase Rattus norvegicus 69-72 11996880-3 2002 In the present study, preincubation of purified rat liver microsomal GST with S-nitrosoglutathione (GSNO) or the nitric oxide (NO) donor, 1,1-diethyl-2-hydroxy-2-nitrosohydrazine (DEA/NO), resulted in a 2-fold increase in enzyme activity. S-Nitrosoglutathione 100-104 hematopoietic prostaglandin D synthase Rattus norvegicus 69-72 11996880-5 2002 The initial treatment of microsomal GST with either GSNO or DEA/NO was associated with an 85% loss of free sulfhydryl groups. S-Nitrosoglutathione 52-56 hematopoietic prostaglandin D synthase Rattus norvegicus 36-39 11890743-9 2002 The results demonstrate that cdb3 and GAPD contain reactive thiols that can be transnitrosylated mainly by means of GSNO; these can ultimately influence GAPD translocation/activity and the glycolytic flux. S-Nitrosoglutathione 116-120 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 38-42 11877318-14 2002 Both PGI(2) and GSNO reduced PAR agonist-induced aggregation and diminished GPIIb/IIIa up-regulation. S-Nitrosoglutathione 16-20 nuclear receptor subfamily 1 group I member 2 Homo sapiens 29-32 11877318-14 2002 Both PGI(2) and GSNO reduced PAR agonist-induced aggregation and diminished GPIIb/IIIa up-regulation. S-Nitrosoglutathione 16-20 integrin subunit alpha 2b Homo sapiens 76-81 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 cyclin dependent kinase inhibitor 1A Homo sapiens 147-150 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 cyclin dependent kinase inhibitor 1A Homo sapiens 151-155 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 cyclin dependent kinase inhibitor 1A Homo sapiens 156-160 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 cyclin dependent kinase inhibitor 1A Homo sapiens 169-173 11879190-3 2002 Incubation of control and Hsp70-transfected macrophages with S-nitrosoglutathione induced accumulation of the tumour suppressor p53, expression of p21(WAF1/CIP1) (where WAF1 corresponds to wild-type p53-activated fragment 1 and CIP1 corresponds to cyclin-dependent kinase-interacting protein 1) and G(1) cell-cycle arrest. S-Nitrosoglutathione 61-81 tumor protein p53 Homo sapiens 199-202 11890743-3 2002 Two highly reactive Cys residues were identified by transnitrosylation with nitrosoglutathione (GSNO) of cdb3 and GAPD (K(2) = 73.7 and 101.5 M(-1) s(-1), respectively). S-Nitrosoglutathione 96-100 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 114-118 11890743-4 2002 The Cys 149 located in the catalytic site of GAPD is exclusively involved in the GSNO-induced nitrosylation. S-Nitrosoglutathione 81-85 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 45-49 11890743-9 2002 The results demonstrate that cdb3 and GAPD contain reactive thiols that can be transnitrosylated mainly by means of GSNO; these can ultimately influence GAPD translocation/activity and the glycolytic flux. S-Nitrosoglutathione 116-120 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 153-157 11752221-4 2002 Using a CYP2D6 promoter-luciferase construct, we found that NOR4 and another NO donor, S-nitrosoglutathione (GSNO), reduced the luciferase activity in a concentration-dependent manner. S-Nitrosoglutathione 87-107 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 8-14 11818458-4 2002 This conclusion is supported by experiments using a chemical NO donor GSNO, in which RON activation directly blocked GSNO-induced apoptotic death of Raw264.7 cells and inhibited LPS-induced p53 accumulation. S-Nitrosoglutathione 70-74 macrophage stimulating 1 receptor Homo sapiens 85-88 11818458-4 2002 This conclusion is supported by experiments using a chemical NO donor GSNO, in which RON activation directly blocked GSNO-induced apoptotic death of Raw264.7 cells and inhibited LPS-induced p53 accumulation. S-Nitrosoglutathione 70-74 transformation related protein 53, pseudogene Mus musculus 190-193 11818458-4 2002 This conclusion is supported by experiments using a chemical NO donor GSNO, in which RON activation directly blocked GSNO-induced apoptotic death of Raw264.7 cells and inhibited LPS-induced p53 accumulation. S-Nitrosoglutathione 117-121 macrophage stimulating 1 receptor Homo sapiens 85-88 11752221-4 2002 Using a CYP2D6 promoter-luciferase construct, we found that NOR4 and another NO donor, S-nitrosoglutathione (GSNO), reduced the luciferase activity in a concentration-dependent manner. S-Nitrosoglutathione 109-113 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 8-14 11752221-8 2002 The DNA-binding activity of HNF4 was directly inhibited by NO donors, GSNO, and S-nitroso-N-acetyl-penicillamine in a concentration-dependent manner. S-Nitrosoglutathione 70-74 hepatocyte nuclear factor 4 alpha Homo sapiens 28-32 11698471-6 2001 S-nitrosoglutathione up-regulated both mRNA and protein expression of CD8alpha in PMC compared with that in sham-treated cells, while NO synthase inhibitors down-regulated OX8 Ab-induced CD8alpha expression. S-Nitrosoglutathione 0-20 CD8a molecule Homo sapiens 70-78 11734646-6 2001 Electron microscopy confirmed that Meg-01 cells treated with TPO and GSNO yielded platelet-sized particles with morphological features specific for platelet forms. S-Nitrosoglutathione 69-73 protein tyrosine phosphatase non-receptor type 4 Homo sapiens 35-38 11737190-9 2001 GSNO or LPS inhibited serum-induced MAPK activation, and both effects were partially reversed by inhibition of guanylate cyclase or phospholipase A2. S-Nitrosoglutathione 0-4 phospholipase A2 group IB Rattus norvegicus 132-148 11518706-3 2001 In the presence of glutathione, A4V SOD and G37R SOD catalyzed S-nitrosoglutathione breakdown three times more efficiently than WT SOD. S-Nitrosoglutathione 63-83 superoxide dismutase 1 Homo sapiens 36-39 11682459-15 2001 Flow cytometry performed with PAC-1 antibodies that bind only to the activated GPIIb/IIIa revealed that GSNO (100 microM) caused inhibition of activation of GPIIb/IIIa. S-Nitrosoglutathione 104-108 dual specificity phosphatase 2 Homo sapiens 30-35 11682459-15 2001 Flow cytometry performed with PAC-1 antibodies that bind only to the activated GPIIb/IIIa revealed that GSNO (100 microM) caused inhibition of activation of GPIIb/IIIa. S-Nitrosoglutathione 104-108 integrin subunit alpha 2b Homo sapiens 79-84 11682459-15 2001 Flow cytometry performed with PAC-1 antibodies that bind only to the activated GPIIb/IIIa revealed that GSNO (100 microM) caused inhibition of activation of GPIIb/IIIa. S-Nitrosoglutathione 104-108 integrin subunit alpha 2b Homo sapiens 157-162 11408616-6 2001 The blockade of CYP2B1 down-regulation by NO synthase inhibitors was reversed by arginine, and the NO donors S-nitrosoglutathione and S-nitroso-N-acetylpenicillamine mimicked CYP2B1 protein suppression. S-Nitrosoglutathione 109-129 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 175-181 11551528-9 2001 Although we failed to detect accumulation of MG under conditions of Glo I inactivation, these results suggest that the inhibitory effects of GSNO on cell proliferation and DNA synthesis might be at least partly due to inactivation of Glo I. S-Nitrosoglutathione 141-145 glyoxalase I Homo sapiens 234-239 11534855-4 2001 Incubation of J774 cells with LPS caused an increase of prostaglandin E2 production and COX-2 protein expression which was prevented in a concentration-dependent fashion by pre-incubating cells with sodium nitroprusside (SNP) and S-nitroso-glutathione (GSNO), two NO-generating agents. S-Nitrosoglutathione 230-251 cytochrome c oxidase II, mitochondrial Mus musculus 88-93 11534855-4 2001 Incubation of J774 cells with LPS caused an increase of prostaglandin E2 production and COX-2 protein expression which was prevented in a concentration-dependent fashion by pre-incubating cells with sodium nitroprusside (SNP) and S-nitroso-glutathione (GSNO), two NO-generating agents. S-Nitrosoglutathione 253-257 cytochrome c oxidase II, mitochondrial Mus musculus 88-93 11534855-6 2001 SNP and GSNO also inhibited nuclear factor-interleukin-6 (NF-IL6) activation. S-Nitrosoglutathione 8-12 CCAAT/enhancer binding protein (C/EBP), beta Mus musculus 58-64 11534855-7 2001 These results show for the first time that SNP and GSNO down-regulate LPS-induced COX-2 expression by inhibiting NF-kappaB and NF-IL6 activation and suggest a negative feed-back mechanism that may be important for limiting excessive or prolonged PGs production in pathological events. S-Nitrosoglutathione 51-55 cytochrome c oxidase II, mitochondrial Mus musculus 82-87 11534855-7 2001 These results show for the first time that SNP and GSNO down-regulate LPS-induced COX-2 expression by inhibiting NF-kappaB and NF-IL6 activation and suggest a negative feed-back mechanism that may be important for limiting excessive or prolonged PGs production in pathological events. S-Nitrosoglutathione 51-55 CCAAT/enhancer binding protein (C/EBP), beta Mus musculus 127-133 11320084-5 2001 Incubation with nitrosoglutathione at 42 degrees C also promoted the conversion of HSF1 to ox-HSF1; at 25 degrees C, however, nitrosoglutathione was by itself without effect but blocked the formation of ox-hHSF1 in the presence of diamide. S-Nitrosoglutathione 16-34 heat shock transcription factor 1 Homo sapiens 83-87 11320084-5 2001 Incubation with nitrosoglutathione at 42 degrees C also promoted the conversion of HSF1 to ox-HSF1; at 25 degrees C, however, nitrosoglutathione was by itself without effect but blocked the formation of ox-hHSF1 in the presence of diamide. S-Nitrosoglutathione 16-34 heat shock transcription factor 1 Homo sapiens 94-98 11320084-5 2001 Incubation with nitrosoglutathione at 42 degrees C also promoted the conversion of HSF1 to ox-HSF1; at 25 degrees C, however, nitrosoglutathione was by itself without effect but blocked the formation of ox-hHSF1 in the presence of diamide. S-Nitrosoglutathione 16-34 heat shock transcription factor 1 Homo sapiens 206-211 11320084-5 2001 Incubation with nitrosoglutathione at 42 degrees C also promoted the conversion of HSF1 to ox-HSF1; at 25 degrees C, however, nitrosoglutathione was by itself without effect but blocked the formation of ox-hHSF1 in the presence of diamide. S-Nitrosoglutathione 126-144 heat shock transcription factor 1 Homo sapiens 83-87 11320084-5 2001 Incubation with nitrosoglutathione at 42 degrees C also promoted the conversion of HSF1 to ox-HSF1; at 25 degrees C, however, nitrosoglutathione was by itself without effect but blocked the formation of ox-hHSF1 in the presence of diamide. S-Nitrosoglutathione 126-144 heat shock transcription factor 1 Homo sapiens 206-211 11461922-7 2001 S-Nitrosoglutathione inhibits ornithine decarboxylase by an oxygen-independent mechanism likely by S-transnitrosation. S-Nitrosoglutathione 0-20 ornithine decarboxylase 1 Homo sapiens 30-53 11374871-2 2001 We hypothesized that GSNO would increase expression and maturation of the cystic fibrosis transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 21-25 CF transmembrane conductance regulator Homo sapiens 74-125 11374871-2 2001 We hypothesized that GSNO would increase expression and maturation of the cystic fibrosis transmembrane conductance regulator (CFTR). S-Nitrosoglutathione 21-25 CF transmembrane conductance regulator Homo sapiens 127-131 11374871-6 2001 Unlike proteasome inhibitors, GSNO resulted in an increase CFTR maturation. S-Nitrosoglutathione 30-34 CF transmembrane conductance regulator Homo sapiens 59-63 11374871-8 2001 These observations suggest that GSNO leads to maturation of mutated DeltaF508 CFTR, a process associated with restoration of CFTR function. S-Nitrosoglutathione 32-36 CF transmembrane conductance regulator Homo sapiens 78-82 11374871-8 2001 These observations suggest that GSNO leads to maturation of mutated DeltaF508 CFTR, a process associated with restoration of CFTR function. S-Nitrosoglutathione 32-36 CF transmembrane conductance regulator Homo sapiens 125-129 11305591-0 2001 Chelation of cellular Cu(I) raised the degree of glyoxalase I inactivation in human endothelial cells upon exposure to S-nitrosoglutathione through stabilization of S-nitrosothiols. S-Nitrosoglutathione 119-139 glyoxalase I Homo sapiens 49-61 11506896-2 2001 Cell treatment with the NO-generating compound nitrosoglutathione (GSNO) caused a significant accumulation of 4.4 kb VEGF mRNA, a major VEGF mRNA isoform expressing in chondrocytes. S-Nitrosoglutathione 47-65 vascular endothelial growth factor A Homo sapiens 117-121 11506896-2 2001 Cell treatment with the NO-generating compound nitrosoglutathione (GSNO) caused a significant accumulation of 4.4 kb VEGF mRNA, a major VEGF mRNA isoform expressing in chondrocytes. S-Nitrosoglutathione 47-65 vascular endothelial growth factor A Homo sapiens 136-140 11506896-2 2001 Cell treatment with the NO-generating compound nitrosoglutathione (GSNO) caused a significant accumulation of 4.4 kb VEGF mRNA, a major VEGF mRNA isoform expressing in chondrocytes. S-Nitrosoglutathione 67-71 vascular endothelial growth factor A Homo sapiens 117-121 11506896-2 2001 Cell treatment with the NO-generating compound nitrosoglutathione (GSNO) caused a significant accumulation of 4.4 kb VEGF mRNA, a major VEGF mRNA isoform expressing in chondrocytes. S-Nitrosoglutathione 67-71 vascular endothelial growth factor A Homo sapiens 136-140 11506896-5 2001 The GSNO-stimulated induction of VEGF mRNA was slightly attenuated by MAP protein kinase inhibitors PD98058 and SB203580, but was completely blocked in cells incubated with GSNO in the presence of catalase and superoxide dismutase, enzymes scavenging reactive oxygen species (ROS), or in the presence of thiol-containing antioxidants, N-acetyl cysteine and reduced glutathione. S-Nitrosoglutathione 4-8 vascular endothelial growth factor A Homo sapiens 33-37 11506896-5 2001 The GSNO-stimulated induction of VEGF mRNA was slightly attenuated by MAP protein kinase inhibitors PD98058 and SB203580, but was completely blocked in cells incubated with GSNO in the presence of catalase and superoxide dismutase, enzymes scavenging reactive oxygen species (ROS), or in the presence of thiol-containing antioxidants, N-acetyl cysteine and reduced glutathione. S-Nitrosoglutathione 4-8 catalase Homo sapiens 197-205 11506896-5 2001 The GSNO-stimulated induction of VEGF mRNA was slightly attenuated by MAP protein kinase inhibitors PD98058 and SB203580, but was completely blocked in cells incubated with GSNO in the presence of catalase and superoxide dismutase, enzymes scavenging reactive oxygen species (ROS), or in the presence of thiol-containing antioxidants, N-acetyl cysteine and reduced glutathione. S-Nitrosoglutathione 173-177 vascular endothelial growth factor A Homo sapiens 33-37 11506896-5 2001 The GSNO-stimulated induction of VEGF mRNA was slightly attenuated by MAP protein kinase inhibitors PD98058 and SB203580, but was completely blocked in cells incubated with GSNO in the presence of catalase and superoxide dismutase, enzymes scavenging reactive oxygen species (ROS), or in the presence of thiol-containing antioxidants, N-acetyl cysteine and reduced glutathione. S-Nitrosoglutathione 173-177 catalase Homo sapiens 197-205 11506896-6 2001 These results suggest that in articular chondrocytes the GSNO-induced VEGF gene transcriptional activation is dependent on endogenous ROS production and oxidative thiol modifications. S-Nitrosoglutathione 57-61 vascular endothelial growth factor A Homo sapiens 70-74 11379760-3 2001 S-Nitrosoglutathione (GSNO), a NO donor, stimulated tropoelastin synthesis in cultured SMCs during both the quiescent and proliferating phases. S-Nitrosoglutathione 0-20 elastin Homo sapiens 52-64 11379760-3 2001 S-Nitrosoglutathione (GSNO), a NO donor, stimulated tropoelastin synthesis in cultured SMCs during both the quiescent and proliferating phases. S-Nitrosoglutathione 22-26 elastin Homo sapiens 52-64 11379760-5 2001 Maximum stimulation was detected by treatment with 100 nM GSNO for 24 h. 8-Bromoguanosine 3",5"-cyclic monophosphate (8-Br-cGMP), an exogenous cyclic GMP analog, also upregulated tropoelastin synthesis. S-Nitrosoglutathione 58-62 elastin Gallus gallus 179-191 11379760-6 2001 Tropoelastin and lysyl oxidase mRNA expression, as assessed by Northern blot analysis, was also stimulated by GSNO. S-Nitrosoglutathione 110-114 elastin Gallus gallus 0-12 11379760-7 2001 Administration of KT5823, a cyclic GMP-dependent protein kinase inhibitor, inhibited the GSNO-induced tropoelastin synthesis. S-Nitrosoglutathione 89-93 elastin Gallus gallus 102-114 11256959-2 2001 In this study, purified H-ras was modified by thiol oxidants such as hydrogen peroxide (H(2)O(2)), S-nitrosoglutathione, diamide, glutathione disulphide (GSSG) and cystamine, producing as many as four charge-isomeric forms of the protein. S-Nitrosoglutathione 99-119 Harvey rat sarcoma virus oncogene Mus musculus 24-29 11256959-5 2001 S-nitrosoglutathione could S-nitrosylate H-ras on four cysteine residues, while reduced glutathione (GSH) and H(2)O(2) mediate S-glutathiolation on at least one cysteine of H-ras. S-Nitrosoglutathione 0-20 Harvey rat sarcoma virus oncogene Mus musculus 41-46 11256959-5 2001 S-nitrosoglutathione could S-nitrosylate H-ras on four cysteine residues, while reduced glutathione (GSH) and H(2)O(2) mediate S-glutathiolation on at least one cysteine of H-ras. S-Nitrosoglutathione 0-20 Harvey rat sarcoma virus oncogene Mus musculus 173-178 11305591-6 2001 We recently demonstrated that human glyoxalase I (Glo I) interacts with GSNO in vitro and within cells. S-Nitrosoglutathione 72-76 glyoxalase I Homo sapiens 36-48 11305591-6 2001 We recently demonstrated that human glyoxalase I (Glo I) interacts with GSNO in vitro and within cells. S-Nitrosoglutathione 72-76 glyoxalase I Homo sapiens 50-55 11305591-7 2001 When Glo I interacts with GSNO, Glo I is inactivated and is chemically modified with pI alteration on 2D gels. S-Nitrosoglutathione 26-30 glyoxalase I Homo sapiens 5-10 11305591-7 2001 When Glo I interacts with GSNO, Glo I is inactivated and is chemically modified with pI alteration on 2D gels. S-Nitrosoglutathione 26-30 glyoxalase I Homo sapiens 32-37 11305591-9 2001 As a result, chelation of cellular Cu(I) by BCS enhanced the inactivation and chemical modification of Glo I by GSNO. S-Nitrosoglutathione 112-116 glyoxalase I Homo sapiens 103-108 11305591-10 2001 The Glo I response could be detected when the cells were exposed to GSNO at 10 microM, corresponding to the concentration of RSNO under physiological conditions, with pretreatment of BCS. S-Nitrosoglutathione 68-72 glyoxalase I Homo sapiens 4-9 11071882-5 2000 We demonstrated that S-nitrosoglutathione induces HIF-1 alpha accumulation and concomitant DNA binding. S-Nitrosoglutathione 21-41 hypoxia inducible factor 1 subunit alpha Homo sapiens 50-61 11237724-1 2001 We previously reported that nitric oxide (NO) released from S-nitrosoglutathione induces conformational change of the p53 tumor-suppressor protein that impairs its DNA-binding activity in vitro. S-Nitrosoglutathione 60-80 tumor protein p53 Homo sapiens 118-121 11237724-5 2001 On the other hand, cells incubated for 16 h in the presence of 1 mM S-nitrosoglutathione underwent apoptosis with accumulation of the pro-apoptotic protein Bax. S-Nitrosoglutathione 68-88 BCL2 associated X, apoptosis regulator Homo sapiens 156-159 11179198-4 2001 The NO donor S:-nitrosoglutathione (GSNO) induced caspase-dependent apoptosis in neonatal rat cardiac myocytes, preceded by a rapid (<10-minute) and significant (approximately 50-fold) activation of JNK1/2. S-Nitrosoglutathione 15-34 mitogen-activated protein kinase 8 Homo sapiens 202-206 11179198-4 2001 The NO donor S:-nitrosoglutathione (GSNO) induced caspase-dependent apoptosis in neonatal rat cardiac myocytes, preceded by a rapid (<10-minute) and significant (approximately 50-fold) activation of JNK1/2. S-Nitrosoglutathione 36-40 mitogen-activated protein kinase 8 Homo sapiens 202-206 11179198-5 2001 Activation of JNK was cGMP dependent and was inversely related to NO concentration; it was maximal at the lowest dose of GSNO (10 micromol/L) and negligible at 1 mmol/L. S-Nitrosoglutathione 121-125 mitogen-activated protein kinase 8 Homo sapiens 14-17 11313716-3 2001 Incubation of cells with sodium nitroprusside (SNP) and S-nitroso-glutathione (GSNO), two NO-generating compounds, caused: (a) inhibition of constitutive NF-kappaB/DNA binding activity; (b) decrease of cell viability; (c) DNA fragmentation; (d) ApopTag positivity. S-Nitrosoglutathione 56-77 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 154-163 11313716-3 2001 Incubation of cells with sodium nitroprusside (SNP) and S-nitroso-glutathione (GSNO), two NO-generating compounds, caused: (a) inhibition of constitutive NF-kappaB/DNA binding activity; (b) decrease of cell viability; (c) DNA fragmentation; (d) ApopTag positivity. S-Nitrosoglutathione 79-83 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 154-163 11313716-5 2001 Furthermore, SNP and GSNO as well as PDTC and TLCK significantly increased the cytoplasmic level of IkappaBalpha. S-Nitrosoglutathione 21-25 nuclear factor of kappa light polypeptide gene enhancer in B cells inhibitor, alpha Mus musculus 100-112 11289659-0 2001 S-nitrosoglutathione inhibits TNF-alpha-induced NFkappaB activation in neutrophils. S-Nitrosoglutathione 0-20 tumor necrosis factor Homo sapiens 30-39 11289659-0 2001 S-nitrosoglutathione inhibits TNF-alpha-induced NFkappaB activation in neutrophils. S-Nitrosoglutathione 0-20 nuclear factor kappa B subunit 1 Homo sapiens 48-56 11289659-6 2001 Effects of GSNO on activation of IkappaB alpha, which inhibits intranuclear translocation of NFkappaB, were measured by Western immunoblot technique. S-Nitrosoglutathione 11-15 NFKB inhibitor alpha Homo sapiens 33-46 11289659-6 2001 Effects of GSNO on activation of IkappaB alpha, which inhibits intranuclear translocation of NFkappaB, were measured by Western immunoblot technique. S-Nitrosoglutathione 11-15 nuclear factor kappa B subunit 1 Homo sapiens 93-101 11306076-2 2001 Incubation of human recombinant AR with S-nitrosoglutathione (GSNO) led to inactivation of the enzyme and the formation of an AR-glutathione adduct. S-Nitrosoglutathione 40-60 aldo-keto reductase family 1 member B Homo sapiens 32-34 11306076-2 2001 Incubation of human recombinant AR with S-nitrosoglutathione (GSNO) led to inactivation of the enzyme and the formation of an AR-glutathione adduct. S-Nitrosoglutathione 40-60 aldo-keto reductase family 1 member B Homo sapiens 126-128 11306076-2 2001 Incubation of human recombinant AR with S-nitrosoglutathione (GSNO) led to inactivation of the enzyme and the formation of an AR-glutathione adduct. S-Nitrosoglutathione 62-66 aldo-keto reductase family 1 member B Homo sapiens 32-34 11306076-2 2001 Incubation of human recombinant AR with S-nitrosoglutathione (GSNO) led to inactivation of the enzyme and the formation of an AR-glutathione adduct. S-Nitrosoglutathione 62-66 aldo-keto reductase family 1 member B Homo sapiens 126-128 11196190-10 2001 NO donors such as S-nitroso-n-acetylpenicillamine and S-nitrosoglutathione (both at 0.01-100 microM) inhibited TCIPA and MMP-2 release from platelets and tumor cells. S-Nitrosoglutathione 54-74 matrix metallopeptidase 2 Homo sapiens 121-126 11060308-4 2001 Each of these compounds and GSNO were tested for their efficacies to modify rat brain neurogranin/RC3 (Ng) and neuromodulin/GAP-43 (Nm). S-Nitrosoglutathione 28-32 neurogranin Rattus norvegicus 86-97 11289659-9 2001 GSNO (500 microM) decreased TNFalpha-induced NFkappaB activity (p<0.05) and inhibited NFkappaB activity whether given prior to or during TNFalpha exposure. S-Nitrosoglutathione 0-4 tumor necrosis factor Homo sapiens 28-36 11289659-9 2001 GSNO (500 microM) decreased TNFalpha-induced NFkappaB activity (p<0.05) and inhibited NFkappaB activity whether given prior to or during TNFalpha exposure. S-Nitrosoglutathione 0-4 nuclear factor kappa B subunit 1 Homo sapiens 45-53 11289659-9 2001 GSNO (500 microM) decreased TNFalpha-induced NFkappaB activity (p<0.05) and inhibited NFkappaB activity whether given prior to or during TNFalpha exposure. S-Nitrosoglutathione 0-4 nuclear factor kappa B subunit 1 Homo sapiens 89-97 11289659-9 2001 GSNO (500 microM) decreased TNFalpha-induced NFkappaB activity (p<0.05) and inhibited NFkappaB activity whether given prior to or during TNFalpha exposure. S-Nitrosoglutathione 0-4 tumor necrosis factor Homo sapiens 140-148 11289659-11 2001 GSNO exposure (500 microM) inhibited IkappaB alpha degradation in the presence of TNFalpha. S-Nitrosoglutathione 0-4 NFKB inhibitor alpha Homo sapiens 37-50 11289659-11 2001 GSNO exposure (500 microM) inhibited IkappaB alpha degradation in the presence of TNFalpha. S-Nitrosoglutathione 0-4 tumor necrosis factor Homo sapiens 82-90 11289659-14 2001 GSNO inhibits NFkappaB activity in association with inhibiting TNFalpha-induced degradation of IkappaB alpha. S-Nitrosoglutathione 0-4 nuclear factor kappa B subunit 1 Homo sapiens 14-22 11289659-14 2001 GSNO inhibits NFkappaB activity in association with inhibiting TNFalpha-induced degradation of IkappaB alpha. S-Nitrosoglutathione 0-4 tumor necrosis factor Homo sapiens 63-71 11289659-14 2001 GSNO inhibits NFkappaB activity in association with inhibiting TNFalpha-induced degradation of IkappaB alpha. S-Nitrosoglutathione 0-4 NFKB inhibitor alpha Homo sapiens 95-108 11289659-16 2001 Inhibition of NF kappaB could represent a potential anti-inflammatory effect of GSNO. S-Nitrosoglutathione 80-84 nuclear factor kappa B subunit 1 Homo sapiens 14-23 11025451-5 2000 (i) Expression of MRP1 and gamma-GCSh genes were induced by treating the cells with NO donors, i.e., S-nitro-N-acetyl-D,L-penicillamide (SNAP) and S-nitroso-L-glutathione, in a concentration-dependent manner. S-Nitrosoglutathione 147-170 ATP binding cassette subfamily C member 1 Homo sapiens 18-22 11023998-3 2000 Similar to nuclear redox factor-1 (Ref-1), mRNA of human neuronal nitric oxide synthase (hNOS1) was maximally up-regulated within 2 h after oxidative stress and down-regulated by NO/GSNO and hydroxyl radical (OH) scavenger. S-Nitrosoglutathione 182-186 apurinic/apyrimidinic endodeoxyribonuclease 1 Homo sapiens 35-40 11023998-3 2000 Similar to nuclear redox factor-1 (Ref-1), mRNA of human neuronal nitric oxide synthase (hNOS1) was maximally up-regulated within 2 h after oxidative stress and down-regulated by NO/GSNO and hydroxyl radical (OH) scavenger. S-Nitrosoglutathione 182-186 nitric oxide synthase 1 Homo sapiens 89-94 11025451-5 2000 (i) Expression of MRP1 and gamma-GCSh genes were induced by treating the cells with NO donors, i.e., S-nitro-N-acetyl-D,L-penicillamide (SNAP) and S-nitroso-L-glutathione, in a concentration-dependent manner. S-Nitrosoglutathione 147-170 glutamate-cysteine ligase catalytic subunit Homo sapiens 27-37 11003590-6 2000 Cell treatment with the NOS inhibitor N(G)-nitro-L-arginine methyl ester (L-NAME; 1 mmol/l) significantly diminished the TNF-alpha-mediated sustained downregulation of UCP-2 expression, whereas cell treatment with a nitric oxide (NO) donor (10(-3) mol/l S-nitroso-L-glutathione) mimicked the TNF-alpha effect on UCP-2 expression. S-Nitrosoglutathione 254-277 tumor necrosis factor Homo sapiens 121-130 11046081-4 2000 N-(3-(Aminomethyl)benzyl)acetamidine (1400W), a selective inhibitor of iNOS, restored activation of the current by GSNO in cytokine-treated cells, indicating a crucial role for iNOS in this process. S-Nitrosoglutathione 115-119 nitric oxide synthase 2 Homo sapiens 71-75 11046081-4 2000 N-(3-(Aminomethyl)benzyl)acetamidine (1400W), a selective inhibitor of iNOS, restored activation of the current by GSNO in cytokine-treated cells, indicating a crucial role for iNOS in this process. S-Nitrosoglutathione 115-119 nitric oxide synthase 2 Homo sapiens 177-181 11011147-7 2000 Taken together, these results reveal that Glo I can interact directly with GSNO, and that the interaction converts Glo I into an inactive form. S-Nitrosoglutathione 75-79 glyoxalase I Homo sapiens 42-47 11059836-5 2000 S-nitroso-L-glutathione inhibited the release of both interferone-gamma and interleukin-2 produced by Th1 cells and tumor necrosis factor-alpha and interleukin-1beta produced by macrophages, but did not affect the release of interleukin-4 and interleukin-10 produced by Th2 cells. S-Nitrosoglutathione 0-23 interleukin 2 Mus musculus 76-89 11059836-5 2000 S-nitroso-L-glutathione inhibited the release of both interferone-gamma and interleukin-2 produced by Th1 cells and tumor necrosis factor-alpha and interleukin-1beta produced by macrophages, but did not affect the release of interleukin-4 and interleukin-10 produced by Th2 cells. S-Nitrosoglutathione 0-23 tumor necrosis factor Mus musculus 116-143 11059836-5 2000 S-nitroso-L-glutathione inhibited the release of both interferone-gamma and interleukin-2 produced by Th1 cells and tumor necrosis factor-alpha and interleukin-1beta produced by macrophages, but did not affect the release of interleukin-4 and interleukin-10 produced by Th2 cells. S-Nitrosoglutathione 0-23 interleukin 4 Mus musculus 225-238 11059836-5 2000 S-nitroso-L-glutathione inhibited the release of both interferone-gamma and interleukin-2 produced by Th1 cells and tumor necrosis factor-alpha and interleukin-1beta produced by macrophages, but did not affect the release of interleukin-4 and interleukin-10 produced by Th2 cells. S-Nitrosoglutathione 0-23 interleukin 10 Mus musculus 243-257 11011147-4 2000 S-Nitrosoglutathione (GSNO), an adduct of GSH and NO, lowers the activity of purified human Glo I, while S-nitrosocysteine (CysNO) inactivates the enzyme only in the presence of GSH. S-Nitrosoglutathione 0-20 glyoxalase I Homo sapiens 92-97 11011147-4 2000 S-Nitrosoglutathione (GSNO), an adduct of GSH and NO, lowers the activity of purified human Glo I, while S-nitrosocysteine (CysNO) inactivates the enzyme only in the presence of GSH. S-Nitrosoglutathione 22-26 glyoxalase I Homo sapiens 92-97 11011147-5 2000 This indicates that a dysfunction in Glo I would require the formation of GSNO in situ. S-Nitrosoglutathione 74-78 glyoxalase I Homo sapiens 37-42 11011147-8 2000 Moreover, the data suggest that the substrate recognition site of Glo I might be involved in the interaction with GSNO. S-Nitrosoglutathione 114-118 glyoxalase I Homo sapiens 66-71 10880356-2 2000 Here, we show that GSNO-Sepharose mimicks site-specific S-glutathionylation of the transcription factors c-Jun and p50 by free GSNO in vitro. S-Nitrosoglutathione 19-23 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 105-110 10801823-4 2000 S-nitrosocysteine (SNC) and, to a more modest extent, S-nitrosoglutathione were found to rapidly increase [(3)H]palmitate incorporation into cellular or oncogenic Ha-Ras in NIH 3T3 cells. S-Nitrosoglutathione 54-74 Harvey rat sarcoma virus oncogene Mus musculus 163-169 10880356-2 2000 Here, we show that GSNO-Sepharose mimicks site-specific S-glutathionylation of the transcription factors c-Jun and p50 by free GSNO in vitro. S-Nitrosoglutathione 19-23 nuclear factor kappa B subunit 1 Homo sapiens 115-118 10880356-2 2000 Here, we show that GSNO-Sepharose mimicks site-specific S-glutathionylation of the transcription factors c-Jun and p50 by free GSNO in vitro. S-Nitrosoglutathione 127-131 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 105-110 10880356-2 2000 Here, we show that GSNO-Sepharose mimicks site-specific S-glutathionylation of the transcription factors c-Jun and p50 by free GSNO in vitro. S-Nitrosoglutathione 127-131 nuclear factor kappa B subunit 1 Homo sapiens 115-118 10880356-3 2000 Both c-Jun and p50 were found to bind to immobilized GSNO through the formation of a mixed disulphide, involving a conserved cysteine residue located in the DNA-binding domains of these transcription factors. S-Nitrosoglutathione 53-57 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 5-10 10880356-3 2000 Both c-Jun and p50 were found to bind to immobilized GSNO through the formation of a mixed disulphide, involving a conserved cysteine residue located in the DNA-binding domains of these transcription factors. S-Nitrosoglutathione 53-57 nuclear factor kappa B subunit 1 Homo sapiens 15-18 10880356-4 2000 Furthermore, we show that c-Jun, p50, glycogen phosphorylase b, glyceraldehyde-3-phosphate dehydrogenase, creatine kinase, glutaredoxin and caspase-3 can be precipitated from a mixture of purified thiol-containing proteins by the formation of a mixed-disulphide bond with GSNO-Sepharose. S-Nitrosoglutathione 272-276 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 26-31 10880356-4 2000 Furthermore, we show that c-Jun, p50, glycogen phosphorylase b, glyceraldehyde-3-phosphate dehydrogenase, creatine kinase, glutaredoxin and caspase-3 can be precipitated from a mixture of purified thiol-containing proteins by the formation of a mixed-disulphide bond with GSNO-Sepharose. S-Nitrosoglutathione 272-276 caspase 3 Homo sapiens 140-149 10871052-10 2000 In RAW 264.7 cells the GR activity was reported to be inhibited by GSNO. S-Nitrosoglutathione 67-71 glutathione reductase Mus musculus 23-25 10938898-1 2000 S-Nitrosoglutathione and sodium nitroprusside, two activators of the soluble guanylate cyclase, inhibit the intracellular calcium rise evoked by thrombin at an early step of the activation cascade. S-Nitrosoglutathione 0-20 coagulation factor II, thrombin Homo sapiens 145-153 10938898-0 2000 Attenuation of alkalizing effect of thrombin by S-nitrosoglutathione in human platelets. S-Nitrosoglutathione 48-68 coagulation factor II, thrombin Homo sapiens 36-44 10938898-7 2000 After a 10-min preincubation at 37 degrees C in 100 mumol/l S-nitrosoglutathione the change in pHi produced by thrombin was reduced by 35 +/- 5%, but only 12 +/- 4% after preincubation in 100 mumol/l sodium nitroprusside. S-Nitrosoglutathione 60-80 coagulation factor II, thrombin Homo sapiens 111-119 10872747-12 2000 ERK and p38 inhibitors also suppressed induction of HO-1 by SNAP and GSNO. S-Nitrosoglutathione 69-73 mitogen-activated protein kinase 1 Homo sapiens 0-3 10872747-12 2000 ERK and p38 inhibitors also suppressed induction of HO-1 by SNAP and GSNO. S-Nitrosoglutathione 69-73 mitogen-activated protein kinase 1 Homo sapiens 8-11 10872747-12 2000 ERK and p38 inhibitors also suppressed induction of HO-1 by SNAP and GSNO. S-Nitrosoglutathione 69-73 heme oxygenase 1 Homo sapiens 52-56 10631110-5 2000 Incubation with 2 mM S-nitrosoglutathione induced a significant increase in the nitrotyrosine level in p53 protein compared to nontreated cells. S-Nitrosoglutathione 21-41 tumor protein p53 Homo sapiens 103-106 10710524-5 2000 These results show that in CTSM strips contracted with KCl, GSNO decreases Ca(2+) sensitivity by affecting the level of rMLC phosphorylation for a given [Ca(2+)](i), suggesting that myosin light chain kinase is inhibited or that smooth muscle protein phosphatases are activated by GSNO. S-Nitrosoglutathione 60-64 myosin light chain kinase Homo sapiens 182-207 10710524-5 2000 These results show that in CTSM strips contracted with KCl, GSNO decreases Ca(2+) sensitivity by affecting the level of rMLC phosphorylation for a given [Ca(2+)](i), suggesting that myosin light chain kinase is inhibited or that smooth muscle protein phosphatases are activated by GSNO. S-Nitrosoglutathione 281-285 myosin light chain kinase Homo sapiens 182-207 10684635-1 2000 Superinduction of cyclooxygenase-2, in murine RAW 264.7 macrophages as well as human pulmonary type II A549 epithelial cells, is achieved by the simultaneous addition of agonists such as lipopolysaccharide or interleukin-1beta and the NO(*) donor S-nitrosoglutathione. S-Nitrosoglutathione 247-267 prostaglandin-endoperoxide synthase 2 Mus musculus 18-34 10684635-8 2000 Enhanced expression of cyclooxygenase-2 by lipopolysaccharide/S-nitrosoglutathione-treatment was attenuated in TAM-67 transfectants, while the response to lipopolysaccharide alone remained unaffected. S-Nitrosoglutathione 62-82 prostaglandin-endoperoxide synthase 2 Homo sapiens 23-39 10679579-3 2000 Two phorbol esters, 4-beta-phorbol 12-myristate-13-acetate (PMA) and 4-beta-phorbol 12,13-dibutyrate (PDBu); the cGMP-dependent PK activators sodium nitroprusside (SNP) and S-nitrosoglutathione (SNOG); and the PP inhibitor okadaic acid (OA) reduced the amplitude of the GABA-induced currents, whilst the PK inhibitor staurosporine potentiated it. S-Nitrosoglutathione 173-193 cyclin-dependent kinase 2 S homeolog Xenopus laevis 128-130 10679579-3 2000 Two phorbol esters, 4-beta-phorbol 12-myristate-13-acetate (PMA) and 4-beta-phorbol 12,13-dibutyrate (PDBu); the cGMP-dependent PK activators sodium nitroprusside (SNP) and S-nitrosoglutathione (SNOG); and the PP inhibitor okadaic acid (OA) reduced the amplitude of the GABA-induced currents, whilst the PK inhibitor staurosporine potentiated it. S-Nitrosoglutathione 195-199 cyclin-dependent kinase 2 S homeolog Xenopus laevis 128-130 10725742-8 2000 Two NO donors, S-nitroglutathione (GSNO) and (+/-)-S-nitroso-N-acetylpenicillamine (SNAP), directly inhibited macrophage RON expression when added to the cell cultures. S-Nitrosoglutathione 35-39 macrophage stimulating 1 receptor (c-met-related tyrosine kinase) Mus musculus 121-124 10725742-10 2000 In Raw264.7 cells transiently transfected with a report vector, GSNO or SNAP inhibited the luciferase activities driven by the RON gene promoter. S-Nitrosoglutathione 64-68 macrophage stimulating 1 receptor (c-met-related tyrosine kinase) Mus musculus 127-130 10725742-11 2000 Moreover, GSNO or SNAP inhibited the macrophage-stimulating protein-induced RON phosphorylation and macrophage migration. S-Nitrosoglutathione 10-14 macrophage stimulating 1 receptor (c-met-related tyrosine kinase) Mus musculus 76-79 10671549-2 2000 Tumor suppressor protein p53 and cell cycle inhibitor p21 accumulate as an early sign of S-nitrosoglutathione-mediated toxicity. S-Nitrosoglutathione 89-109 tumor protein p53 Homo sapiens 25-28 10671549-2 2000 Tumor suppressor protein p53 and cell cycle inhibitor p21 accumulate as an early sign of S-nitrosoglutathione-mediated toxicity. S-Nitrosoglutathione 89-109 H3 histone pseudogene 16 Homo sapiens 54-57 10727020-2 2000 Overexpression of Bcl-2 in NIH3T3 cells can prevent GSNO-induced (S-nitrosoglutathione-induced) apoptosis. S-Nitrosoglutathione 52-56 B cell leukemia/lymphoma 2 Mus musculus 18-23 10727020-2 2000 Overexpression of Bcl-2 in NIH3T3 cells can prevent GSNO-induced (S-nitrosoglutathione-induced) apoptosis. S-Nitrosoglutathione 66-86 B cell leukemia/lymphoma 2 Mus musculus 18-23 10727020-3 2000 The experimental results indicated that activation of NF-kappaB by GSNO is involved in inducing apoptosis. S-Nitrosoglutathione 67-71 nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105 Mus musculus 54-63 10496957-3 1999 The NO donor S-nitrosoglutathione time- and concentration-dependently promoted apoptotic cell death as detected by JNK1/2 and caspase-3 activation as well as DNA fragmentation. S-Nitrosoglutathione 13-33 mitogen-activated protein kinase 8 Homo sapiens 115-121 10620189-4 2000 Here we investigated the effect of S-nitrosoglutathione (GSNO) on the proliferation of MCs, specifically asking how GSNO regulates the transcription factor Egr-1, which we have previously shown to be critical for the induction of MC mitogenesis. S-Nitrosoglutathione 35-55 early growth response 1 Homo sapiens 156-161 10620189-4 2000 Here we investigated the effect of S-nitrosoglutathione (GSNO) on the proliferation of MCs, specifically asking how GSNO regulates the transcription factor Egr-1, which we have previously shown to be critical for the induction of MC mitogenesis. S-Nitrosoglutathione 57-61 early growth response 1 Homo sapiens 156-161 10620189-4 2000 Here we investigated the effect of S-nitrosoglutathione (GSNO) on the proliferation of MCs, specifically asking how GSNO regulates the transcription factor Egr-1, which we have previously shown to be critical for the induction of MC mitogenesis. S-Nitrosoglutathione 116-120 early growth response 1 Homo sapiens 156-161 10620189-7 2000 Electrophoretic mobility shift assays (EMSAs) and chloramphenicol acetyltransferase (CAT) assays were performed to test whether GSNO modulates DNA binding and transcriptional activation of Egr-1. S-Nitrosoglutathione 128-132 early growth response 1 Homo sapiens 189-194 10620189-9 2000 A mild inhibition of serum-induced Egr-1 mRNA was observed at GSNO concentrations from 50 to 200 micromol/L, whereas mRNA levels increased again at concentrations above 500 micromol/L. S-Nitrosoglutathione 62-66 early growth response 1 Homo sapiens 35-40 10620189-12 2000 EMSAs indicated that GSNO inhibited specific binding of Egr-1 to its DNA consensus sequence. S-Nitrosoglutathione 21-25 early growth response 1 Homo sapiens 56-61 10620189-13 2000 Moreover, transcriptional activation by Egr-1 in CAT assays using a reporter plasmid bearing three Egr-1 binding sites was strongly suppressed by GSNO. S-Nitrosoglutathione 146-150 early growth response 1 Homo sapiens 40-45 10620189-13 2000 Moreover, transcriptional activation by Egr-1 in CAT assays using a reporter plasmid bearing three Egr-1 binding sites was strongly suppressed by GSNO. S-Nitrosoglutathione 146-150 early growth response 1 Homo sapiens 99-104 10620189-15 2000 This antimitogenic property is mediated at least in part by inhibitory effects of GSNO on Egr-1 protein levels and by reducing the ability of Egr-1 to activate transcription by impairing its DNA binding activity. S-Nitrosoglutathione 82-86 early growth response 1 Homo sapiens 90-95 10630687-2 1999 GSNO and *NO terminate oxidant stress in the brain by (i) inhibiting iron-stimulated hydroxyl radicals formation or the Fenton reaction, (ii) terminating lipid peroxidation, (iii) augmenting the antioxidative potency of glutathione (GSH), (iv) mediating neuroprotective action of brain-derived neurotrophin (BDNF), and (v) inhibiting cysteinyl proteases. S-Nitrosoglutathione 0-4 brain derived neurotrophic factor Homo sapiens 294-306 10630687-2 1999 GSNO and *NO terminate oxidant stress in the brain by (i) inhibiting iron-stimulated hydroxyl radicals formation or the Fenton reaction, (ii) terminating lipid peroxidation, (iii) augmenting the antioxidative potency of glutathione (GSH), (iv) mediating neuroprotective action of brain-derived neurotrophin (BDNF), and (v) inhibiting cysteinyl proteases. S-Nitrosoglutathione 0-4 brain derived neurotrophic factor Homo sapiens 308-312 10637127-1 1999 The present study investigates the pharmacological activity of the nitric oxide (NO) donor S-nitrosoglutathione (GSNO) on the plasma glucose and insulin levels in healthy normoglycemic dogs. S-Nitrosoglutathione 91-111 insulin Homo sapiens 145-152 10637127-1 1999 The present study investigates the pharmacological activity of the nitric oxide (NO) donor S-nitrosoglutathione (GSNO) on the plasma glucose and insulin levels in healthy normoglycemic dogs. S-Nitrosoglutathione 113-117 insulin Homo sapiens 145-152 10637127-12 1999 These results suggests that in healthy normoglycaemic dogs: (a) nitric oxide released from GSNO increases postprandial plasma glucose levels and inhibits glucose-stimulated insulin secretion, (b) ascorbic acid enhances the postprandial hyperglycaemic effect of GSNO, probably by increasing the release of NO, and (c) GSNO decreases mean arterial blood pressure and increase heart rate in normotensive dogs. S-Nitrosoglutathione 91-95 insulin Canis lupus familiaris 173-180 10597241-4 1999 S-nitrosoglutathione and spermine-NO caused a fast p53 accumulation, followed by Bcl-xL downregulation, Cyt c release, and caspase activation. S-Nitrosoglutathione 0-20 tumor protein p53 Homo sapiens 51-54 10597241-4 1999 S-nitrosoglutathione and spermine-NO caused a fast p53 accumulation, followed by Bcl-xL downregulation, Cyt c release, and caspase activation. S-Nitrosoglutathione 0-20 BCL2 like 1 Homo sapiens 81-87 10597241-4 1999 S-nitrosoglutathione and spermine-NO caused a fast p53 accumulation, followed by Bcl-xL downregulation, Cyt c release, and caspase activation. S-Nitrosoglutathione 0-20 cytochrome c, somatic Homo sapiens 104-109 10521264-3 1999 The S-nitroso derivatives of glutathione (GSNO) and N-acetylpenicillamine (SNAP) and the non-thiol NO donors NOR-1 and NOR-3 all inhibited the activity of purified cathepsin K in a time- and concentration-dependent manner (IC(50) values after 15 min of preincubation at pH 7.5 of 28, 105, 0.4, and 10 microM, respectively). S-Nitrosoglutathione 42-46 cathepsin K Cricetulus griseus 164-175 10521264-5 1999 GSNO at 100 microM also completely inhibited the autocatalytic maturation at pH 4.0 of procathepsin K to cathepsin K. S-Nitrosoglutathione 0-4 cathepsin K Cricetulus griseus 90-101 10521264-6 1999 The inhibition of cathepsin K by GSNO was rapidly reversed by DTT, but inhibition by NOR-1 was not reversed by DTT, and analysis of the inhibited cathepsin K for S-nitrosylation using the Greiss reaction gave negative results in both cases. S-Nitrosoglutathione 33-37 cathepsin K Cricetulus griseus 18-29 10521264-7 1999 Analysis of the protein by electrospray liquid chromatography/mass spectrometry showed that the inhibition of cathepsin K by GSNO resulted in a mass increase of 306 +/- 2 Da, consistent with the formation of a glutathione adduct. S-Nitrosoglutathione 125-129 cathepsin K Cricetulus griseus 110-121 10521264-8 1999 Prior inhibition of cathepsin K by the active site thiol-modifying inhibitor E-64 blocked the modification by GSNO, indicating that the glutathione adduct is likely formed at the active site cysteine. S-Nitrosoglutathione 110-114 cathepsin K Cricetulus griseus 20-31 10602776-6 1999 RESULTS: We verified resistance of murine and human macrophages against NO donors such as S-nitrosoglutathione or spermine-NO by pre-exposing cells to lipophilic cAMP analogs or by pretreatment with lipopolysaccaride, interferon-gamma, and N(G)-nitroarginine-methylester for 15 hr. S-Nitrosoglutathione 90-110 interferon gamma Homo sapiens 218-234 10597028-0 1999 Suppression of N-methyl-N"-nitro-N-nitrosoguanidine- and S-nitrosoglutathione-induced apoptosis by Bcl-2 through inhibiting glutathione-S-transferase pi in NIH3T3 cells. S-Nitrosoglutathione 57-77 B cell leukemia/lymphoma 2 Mus musculus 99-104 10597028-2 1999 Bcl-2-expressing NIH3T3 prevented N-methyl-N"-nitro-N-nitrosoguanidine (MNNG)- and S-nitrosoglutathione (GSNO)-induced apoptosis as compared with the control NIH3T3 cells. S-Nitrosoglutathione 83-103 B cell leukemia/lymphoma 2 Mus musculus 0-5 10597028-2 1999 Bcl-2-expressing NIH3T3 prevented N-methyl-N"-nitro-N-nitrosoguanidine (MNNG)- and S-nitrosoglutathione (GSNO)-induced apoptosis as compared with the control NIH3T3 cells. S-Nitrosoglutathione 105-109 B cell leukemia/lymphoma 2 Mus musculus 0-5 10597028-7 1999 Furthermore, both MNNG- and GSNO-induced apoptosis of NIH3T3 cells were accompanied with a decrease in the level of glutathione (GSH); whereas Bcl-2 overexpression led to an increase in total cellular glutathione. S-Nitrosoglutathione 28-32 B cell leukemia/lymphoma 2 Mus musculus 143-148 10559795-0 1999 Induction of apoptosis by S-nitrosoglutathione and Cu2+ or Ni2+ ion through modulation of bax, bad, and bcl-2 proteins in human colon adenocarcinoma cells. S-Nitrosoglutathione 26-46 BCL2 associated X, apoptosis regulator Homo sapiens 90-93 10559795-0 1999 Induction of apoptosis by S-nitrosoglutathione and Cu2+ or Ni2+ ion through modulation of bax, bad, and bcl-2 proteins in human colon adenocarcinoma cells. S-Nitrosoglutathione 26-46 BCL2 apoptosis regulator Homo sapiens 104-109 10559795-8 1999 We also found that copper ions modulated the expression of bad, bax, and bcl-2 in GSNO-treated HT 29 cells. S-Nitrosoglutathione 82-86 BCL2 associated X, apoptosis regulator Homo sapiens 64-67 10559795-8 1999 We also found that copper ions modulated the expression of bad, bax, and bcl-2 in GSNO-treated HT 29 cells. S-Nitrosoglutathione 82-86 BCL2 apoptosis regulator Homo sapiens 73-78 10559795-9 1999 The levels of bax and bad proteins in treated cells were significantly elevated about fourfold to sixfold when compared with mock-treated cells 24 h after combined treatment with GSNO plus Cu(2+) or Ni(2+). S-Nitrosoglutathione 179-183 BCL2 associated X, apoptosis regulator Homo sapiens 14-17 10559795-10 1999 On the other hand, significant inhibition of bcl-2 occurred in HT 29 cells with simultaneous treatment of GSNO with Cu(2+) (or Ni(2+)). S-Nitrosoglutathione 106-110 BCL2 apoptosis regulator Homo sapiens 45-50 10496957-3 1999 The NO donor S-nitrosoglutathione time- and concentration-dependently promoted apoptotic cell death as detected by JNK1/2 and caspase-3 activation as well as DNA fragmentation. S-Nitrosoglutathione 13-33 caspase 3 Homo sapiens 126-135 10480920-6 1999 Among the various heavy metal ions and copper-containing enzymes and proteins examined, only copper ion (Cu(2+)) and CP showed potent RS-NO (S-nitrosoglutathione)-producing activity. S-Nitrosoglutathione 141-161 ceruloplasmin Homo sapiens 117-119 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. S-Nitrosoglutathione 172-176 heme oxygenase 2 Homo sapiens 102-106 10438918-0 1999 The ectoenzyme gamma-glutamyl transpeptidase regulates antiproliferative effects of S-nitrosoglutathione on human T and B lymphocytes. S-Nitrosoglutathione 84-104 inactive glutathione hydrolase 2 Homo sapiens 15-44 10453032-4 1999 Preactivation of RAW 264.7 cells with a nontoxic dose of the redox cycler 2,3-dimethoxy-1,4-naphthoquinone (5 microM) for 15 h attenuated S-nitrosoglutathione (1 mM)-initiated apoptotic cell death and averted accumulation of the tumor suppressor p53, which is indicative for macrophage apoptosis. S-Nitrosoglutathione 138-158 transformation related protein 53, pseudogene Mus musculus 246-249 10438918-4 1999 In vitro, purified GGT also metabolizes the naturally occurring nitrosothiol, S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 78-98 inactive glutathione hydrolase 2 Homo sapiens 19-22 10438918-4 1999 In vitro, purified GGT also metabolizes the naturally occurring nitrosothiol, S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 100-104 inactive glutathione hydrolase 2 Homo sapiens 19-22 10438918-7 1999 In the presence of cells lacking GGT, GSNO is extremely stable. S-Nitrosoglutathione 38-42 inactive glutathione hydrolase 2 Homo sapiens 33-36 10438918-8 1999 In contrast, GGT-expressing cells rapidly metabolize GSNO leading to nitric oxide release. S-Nitrosoglutathione 53-57 inactive glutathione hydrolase 2 Homo sapiens 13-16 10438918-11 1999 GSNO also caused a rapid, GGT-dependent cytostatic effect in Hut-78, a human T cell lymphoma, as well as in activated peripheral blood T cells. S-Nitrosoglutathione 0-4 inactive glutathione hydrolase 2 Homo sapiens 26-29 10438918-13 1999 These data show that GGT, a regulated ectoenzyme on T cells, controls the rate of nitric oxide production from GSNO and thus markedly affects the physiological response to this biologically active nitrosothiol. S-Nitrosoglutathione 111-115 inactive glutathione hydrolase 2 Homo sapiens 21-24 10423162-2 1999 The expression levels of heme oxygenase-1 mRNA were increased significantly in DLD-1 human colorectal adenocarcinoma cells by treatment with each of three NO donors: sodium nitroprusside (SNP), S-nitroso-L-glutathione (GSNO), and 3-morpholinosydnonimine (SIN-1). S-Nitrosoglutathione 194-217 heme oxygenase 1 Homo sapiens 25-41 10423162-2 1999 The expression levels of heme oxygenase-1 mRNA were increased significantly in DLD-1 human colorectal adenocarcinoma cells by treatment with each of three NO donors: sodium nitroprusside (SNP), S-nitroso-L-glutathione (GSNO), and 3-morpholinosydnonimine (SIN-1). S-Nitrosoglutathione 219-223 heme oxygenase 1 Homo sapiens 25-41 10423162-3 1999 A combination of SIN-1 plus SNP or GSNO additively increased heme oxygenase-1 mRNA expression, whereas synergistic induction was seen with SNP plus GSNO. S-Nitrosoglutathione 35-39 heme oxygenase 1 Homo sapiens 61-77 10391892-5 1999 In support of this hypothesis, both exposure of cells to S-nitrosoglutathione and stimulation of endogenous nitric oxide production by lipopolysaccharide/interferon-gamma treatment result in inhibition of proteasome activity as measured in vitro by the degradation of the proteasome-specific substrate succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin-7-amide. S-Nitrosoglutathione 57-77 interferon gamma Homo sapiens 154-170 10377238-1 1999 Treatment of glyceraldehyde-3-phosphate - dehydrogenase (GA (GAPDH) with the NO donors S-nitrosoglutathione, 3-morpholinosydnonimine or diethylamine NONOate (diethylamine diazeniumdiolate) in vitro, inhibited its dehydrogenase activity and induced its acyl phosphatase activity. S-Nitrosoglutathione 87-107 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 13-55 10377238-1 1999 Treatment of glyceraldehyde-3-phosphate - dehydrogenase (GA (GAPDH) with the NO donors S-nitrosoglutathione, 3-morpholinosydnonimine or diethylamine NONOate (diethylamine diazeniumdiolate) in vitro, inhibited its dehydrogenase activity and induced its acyl phosphatase activity. S-Nitrosoglutathione 87-107 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 57-59 10377238-1 1999 Treatment of glyceraldehyde-3-phosphate - dehydrogenase (GA (GAPDH) with the NO donors S-nitrosoglutathione, 3-morpholinosydnonimine or diethylamine NONOate (diethylamine diazeniumdiolate) in vitro, inhibited its dehydrogenase activity and induced its acyl phosphatase activity. S-Nitrosoglutathione 87-107 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 61-66 10447771-9 1999 The NO donors sodium nitroprusside and S-nitrosoglutathione mimicked the effect of IFN-gamma. S-Nitrosoglutathione 39-59 interferon gamma Rattus norvegicus 83-92 10348862-8 1999 In addition, when a microaerophilic culture entered into the stationary phase at 20 days, transcription of hmp increased to a small extent after exposure to S-nitrosoglutathione (a nitric oxide [NO] releaser) and sodium nitroprusside (an NO+ donor) and decreased after exposure to paraquat (a superoxide generator) and H2O2. S-Nitrosoglutathione 157-177 inner membrane mitochondrial protein Homo sapiens 107-110 10318860-3 1999 The results demonstrate that the NO donor S-nitrosoglutathione (S-NO-glutathione) inhibits the stimulation of PI3-kinase associated with tyrosine-phosphorylated proteins and of p85/PI3-kinase associated with the SRC family kinase member LYN following the exposure of platelets to thrombin receptor-activating peptide. S-Nitrosoglutathione 42-62 phosphoinositide-3-kinase regulatory subunit 2 Homo sapiens 177-180 10336489-5 1999 Furthermore, we provide experimental evidence that nitric oxide-induced S-glutathionylation and inhibition of c-Jun involves the formation of S-nitrosoglutathione. S-Nitrosoglutathione 142-162 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 110-115 10318860-3 1999 The results demonstrate that the NO donor S-nitrosoglutathione (S-NO-glutathione) inhibits the stimulation of PI3-kinase associated with tyrosine-phosphorylated proteins and of p85/PI3-kinase associated with the SRC family kinase member LYN following the exposure of platelets to thrombin receptor-activating peptide. S-Nitrosoglutathione 42-62 LYN proto-oncogene, Src family tyrosine kinase Homo sapiens 237-240 10092623-4 1999 In contrast, the NO-releasing compound S-nitrosoglutathione (GSNO) promoted S-glutathionylation of a thiol group of GAPDH both in vitro and under cellular conditions. S-Nitrosoglutathione 39-59 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 116-121 10224230-2 1999 We identified a Cu/Zn superoxide dismutase (SOD) that was strongly induced in these cells by treatment with S-nitroso-glutathione as a NO-donating agent. S-Nitrosoglutathione 108-129 superoxide dismutase 1 Rattus norvegicus 44-47 10092623-4 1999 In contrast, the NO-releasing compound S-nitrosoglutathione (GSNO) promoted S-glutathionylation of a thiol group of GAPDH both in vitro and under cellular conditions. S-Nitrosoglutathione 61-65 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 116-121 10092794-5 1999 PKC transfectants (PKC-beta II, -delta, and -eta) showed substantial protection from cell death induced by the exposure to NO donors such as SNP and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 149-169 protein kinase C, delta Mus musculus 19-48 10068442-3 1999 Acivicin (AT-125), an inhibitor of gamma-glutamyltransferase (gamma-GTP), prolonged the depressor effect of GS-NO but not of Cys-NO. S-Nitrosoglutathione 108-113 gamma-glutamyltransferase 1 Rattus norvegicus 35-60 10070107-13 1999 Incubation with GSNO increased cell death at 2, 4, and 24 h. GSNO incubation for 24 h significantly increased DNA fragmentation in a dose-dependent fashion at 0.5 (median 126% of control value; P = 0.002) and 5 mM (185% of control value; P = 0.002) by terminal deoxynucleotidyltransferase-mediated fluorescence-labeled dUTP nick end labeling and at 0.5 mM by ELISA (164% of control value; P = 0.03). S-Nitrosoglutathione 16-20 DNA nucleotidylexotransferase Homo sapiens 252-288 10070107-13 1999 Incubation with GSNO increased cell death at 2, 4, and 24 h. GSNO incubation for 24 h significantly increased DNA fragmentation in a dose-dependent fashion at 0.5 (median 126% of control value; P = 0.002) and 5 mM (185% of control value; P = 0.002) by terminal deoxynucleotidyltransferase-mediated fluorescence-labeled dUTP nick end labeling and at 0.5 mM by ELISA (164% of control value; P = 0.03). S-Nitrosoglutathione 61-65 DNA nucleotidylexotransferase Homo sapiens 252-288 10092794-5 1999 PKC transfectants (PKC-beta II, -delta, and -eta) showed substantial protection from cell death induced by the exposure to NO donors such as SNP and S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 171-175 protein kinase C, delta Mus musculus 19-48 9917330-7 1999 When crude mixtures of proteins from rat liver (containing carbonic anhydrase III) or from E. coli (containing an overexpressed form of H-ras) were exposed to fresh GSNO, both the S-nitrosylated and the S-glutathiolated forms of the proteins were observed. S-Nitrosoglutathione 165-169 HRas proto-oncogene, GTPase Rattus norvegicus 136-141 10024512-4 1999 Using S-nitroso-glutathione (GSNO) as an NO-donating agent, VEGF expression was strongly induced, whereas expression of its FLT-1 receptor simultaneously decreased. S-Nitrosoglutathione 6-27 vascular endothelial growth factor A Rattus norvegicus 60-64 10024512-4 1999 Using S-nitroso-glutathione (GSNO) as an NO-donating agent, VEGF expression was strongly induced, whereas expression of its FLT-1 receptor simultaneously decreased. S-Nitrosoglutathione 29-33 vascular endothelial growth factor A Rattus norvegicus 60-64 10024512-4 1999 Using S-nitroso-glutathione (GSNO) as an NO-donating agent, VEGF expression was strongly induced, whereas expression of its FLT-1 receptor simultaneously decreased. S-Nitrosoglutathione 29-33 Fms related receptor tyrosine kinase 1 Rattus norvegicus 124-129 10024512-5 1999 Expressional regulation of VEGF and FLT-1 mRNA was transient and occurred rapidly within 1-3 h after GSNO treatment. S-Nitrosoglutathione 101-105 vascular endothelial growth factor A Rattus norvegicus 27-31 10024512-5 1999 Expressional regulation of VEGF and FLT-1 mRNA was transient and occurred rapidly within 1-3 h after GSNO treatment. S-Nitrosoglutathione 101-105 Fms related receptor tyrosine kinase 1 Rattus norvegicus 36-41 10029520-6 1999 Activation of JNK1/2 by GSNO showed maximal kinase activities between 2 and 8 h. Attenuating JNK1/2 by antisense-depletion eliminated the pro-apoptotic action of low GSNO concentrations (250 microM), whereas apoptosis proceeded independently of JNK1/2 at higher doses of the NO donor (500 microM). S-Nitrosoglutathione 166-170 mitogen-activated protein kinase 8 Homo sapiens 93-99 10029520-7 1999 Decreased apoptosis by JNK1/2 depletion prevented p53 accumulation after the addition of GSNO, which positions JNK1/2 upstream of the p53 response at low agonist concentrations. S-Nitrosoglutathione 89-93 mitogen-activated protein kinase 8 Homo sapiens 23-27 10029520-7 1999 Decreased apoptosis by JNK1/2 depletion prevented p53 accumulation after the addition of GSNO, which positions JNK1/2 upstream of the p53 response at low agonist concentrations. S-Nitrosoglutathione 89-93 tumor protein p53 Homo sapiens 50-53 10029520-7 1999 Decreased apoptosis by JNK1/2 depletion prevented p53 accumulation after the addition of GSNO, which positions JNK1/2 upstream of the p53 response at low agonist concentrations. S-Nitrosoglutathione 89-93 mitogen-activated protein kinase 8 Homo sapiens 111-115 10029520-7 1999 Decreased apoptosis by JNK1/2 depletion prevented p53 accumulation after the addition of GSNO, which positions JNK1/2 upstream of the p53 response at low agonist concentrations. S-Nitrosoglutathione 89-93 tumor protein p53 Homo sapiens 134-137 10029520-9 1999 However, with higher GSNO concentrations apoptotic transducing pathways, including p53 accumulation, were JNK1/2 unrelated. S-Nitrosoglutathione 21-25 tumor protein p53 Homo sapiens 83-86 10029520-9 1999 However, with higher GSNO concentrations apoptotic transducing pathways, including p53 accumulation, were JNK1/2 unrelated. S-Nitrosoglutathione 21-25 mitogen-activated protein kinase 8 Homo sapiens 106-110 10029520-4 1999 ERK1/2 became activated in response to GSNO after 4 h and remained active for the next 20 h. Blocking the ERK1/2 pathway by the mitogen-activated protein kinase kinase inhibitor PD 98059 enhanced GSNO-elicited apoptosis. S-Nitrosoglutathione 39-43 mitogen-activated protein kinase 3 Homo sapiens 0-6 10029520-4 1999 ERK1/2 became activated in response to GSNO after 4 h and remained active for the next 20 h. Blocking the ERK1/2 pathway by the mitogen-activated protein kinase kinase inhibitor PD 98059 enhanced GSNO-elicited apoptosis. S-Nitrosoglutathione 39-43 mitogen-activated protein kinase 3 Homo sapiens 106-112 10029520-4 1999 ERK1/2 became activated in response to GSNO after 4 h and remained active for the next 20 h. Blocking the ERK1/2 pathway by the mitogen-activated protein kinase kinase inhibitor PD 98059 enhanced GSNO-elicited apoptosis. S-Nitrosoglutathione 196-200 mitogen-activated protein kinase 3 Homo sapiens 0-6 10029520-4 1999 ERK1/2 became activated in response to GSNO after 4 h and remained active for the next 20 h. Blocking the ERK1/2 pathway by the mitogen-activated protein kinase kinase inhibitor PD 98059 enhanced GSNO-elicited apoptosis. S-Nitrosoglutathione 196-200 mitogen-activated protein kinase 3 Homo sapiens 106-112 10029520-6 1999 Activation of JNK1/2 by GSNO showed maximal kinase activities between 2 and 8 h. Attenuating JNK1/2 by antisense-depletion eliminated the pro-apoptotic action of low GSNO concentrations (250 microM), whereas apoptosis proceeded independently of JNK1/2 at higher doses of the NO donor (500 microM). S-Nitrosoglutathione 24-28 mitogen-activated protein kinase 8 Homo sapiens 14-20 10029520-6 1999 Activation of JNK1/2 by GSNO showed maximal kinase activities between 2 and 8 h. Attenuating JNK1/2 by antisense-depletion eliminated the pro-apoptotic action of low GSNO concentrations (250 microM), whereas apoptosis proceeded independently of JNK1/2 at higher doses of the NO donor (500 microM). S-Nitrosoglutathione 24-28 mitogen-activated protein kinase 8 Homo sapiens 14-18 10029520-6 1999 Activation of JNK1/2 by GSNO showed maximal kinase activities between 2 and 8 h. Attenuating JNK1/2 by antisense-depletion eliminated the pro-apoptotic action of low GSNO concentrations (250 microM), whereas apoptosis proceeded independently of JNK1/2 at higher doses of the NO donor (500 microM). S-Nitrosoglutathione 24-28 mitogen-activated protein kinase 8 Homo sapiens 93-99 10029520-6 1999 Activation of JNK1/2 by GSNO showed maximal kinase activities between 2 and 8 h. Attenuating JNK1/2 by antisense-depletion eliminated the pro-apoptotic action of low GSNO concentrations (250 microM), whereas apoptosis proceeded independently of JNK1/2 at higher doses of the NO donor (500 microM). S-Nitrosoglutathione 166-170 mitogen-activated protein kinase 8 Homo sapiens 14-20 10029520-6 1999 Activation of JNK1/2 by GSNO showed maximal kinase activities between 2 and 8 h. Attenuating JNK1/2 by antisense-depletion eliminated the pro-apoptotic action of low GSNO concentrations (250 microM), whereas apoptosis proceeded independently of JNK1/2 at higher doses of the NO donor (500 microM). S-Nitrosoglutathione 166-170 mitogen-activated protein kinase 8 Homo sapiens 14-18 9950682-4 1999 Cox-2 induction by low-dose GSNO demanded activation of both NF-kappaB and activator protein-1 (AP-1). S-Nitrosoglutathione 28-32 prostaglandin-endoperoxide synthase 2 Homo sapiens 0-5 9950682-4 1999 Cox-2 induction by low-dose GSNO demanded activation of both NF-kappaB and activator protein-1 (AP-1). S-Nitrosoglutathione 28-32 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 75-94 9950682-4 1999 Cox-2 induction by low-dose GSNO demanded activation of both NF-kappaB and activator protein-1 (AP-1). S-Nitrosoglutathione 28-32 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 96-100 10064155-3 1999 On aortic rings, VIPGC-NO exhibited a dose-dependent vasorelaxation similar to S-nitrosoglutathione (GSNO), and both induced complete vasorelaxation at 1 microM, whereas, VIP at 1 microM only produced 19% relaxation. S-Nitrosoglutathione 101-105 vasoactive intestinal peptide Rattus norvegicus 17-20 10064155-8 1999 On rabbit sphincter of Oddi, VIP, VIPGC-NO and VIPGC inhibited both basic and acetylcholine-induced contraction frequency and amplitude, whereas, GSNO was less potent than VIP and its derivatives over a range of 2 log units in this respect. S-Nitrosoglutathione 146-150 VIP peptides Oryctolagus cuniculus 34-37 9915771-8 1999 The NO donor S-nitrosoglutathione also induced apoptosis and cell levels of Bak, but not of Bcl-x(L). S-Nitrosoglutathione 13-33 BCL2 antagonist/killer 1 Homo sapiens 76-79 9927624-7 1999 NO donors (S-nitroso-acetyl-DL-penicillamine, S-nitroso-DL-penicillamine, or S-nitroso-glutathione) decreased, in a time- and dose-dependent manner, the binding of [3H]triamcinolone to immunoprecipitated GR from mouse L929 fibroblasts. S-Nitrosoglutathione 77-98 nuclear receptor subfamily 3, group C, member 1 Mus musculus 204-206 9794418-8 1998 In vitro dephosphorylation of activated and immunoprecipitated p42/p44 by cytosolic phosphatases was sensitive to the readdition of NO and was found to be inhibited in cytosol of S-nitrosoglutathione-stimulated cells. S-Nitrosoglutathione 179-199 mitogen activated protein kinase 3 Rattus norvegicus 67-70 9882463-3 1999 The objective of this study was to determine what effect Cu, Zn superoxide dismutase (CuZn-SOD) has on the stability of certain S-nitrosothiols such as S-nitrosoglutathione (GSNO) in vitro. S-Nitrosoglutathione 152-172 superoxide dismutase 1 Homo sapiens 57-84 9882463-3 1999 The objective of this study was to determine what effect Cu, Zn superoxide dismutase (CuZn-SOD) has on the stability of certain S-nitrosothiols such as S-nitrosoglutathione (GSNO) in vitro. S-Nitrosoglutathione 152-172 superoxide dismutase 1 Homo sapiens 86-94 9882463-3 1999 The objective of this study was to determine what effect Cu, Zn superoxide dismutase (CuZn-SOD) has on the stability of certain S-nitrosothiols such as S-nitrosoglutathione (GSNO) in vitro. S-Nitrosoglutathione 174-178 superoxide dismutase 1 Homo sapiens 57-84 9882463-3 1999 The objective of this study was to determine what effect Cu, Zn superoxide dismutase (CuZn-SOD) has on the stability of certain S-nitrosothiols such as S-nitrosoglutathione (GSNO) in vitro. S-Nitrosoglutathione 174-178 superoxide dismutase 1 Homo sapiens 86-94 9882463-4 1999 We found that CuZn-SOD (20 microM) but not Mn-SOD in the presence of GSH catalyzed the decomposition of GSNO with a Vmax of 6.7 +/- 0.4 microM/min and a Km of 5.6 +/- 0.5 microM at 37 degreesC. S-Nitrosoglutathione 104-108 superoxide dismutase 1 Homo sapiens 14-22 9882463-5 1999 Increasing GSH concentrations with respect to CuZn-SOD resulted in complete decomposition of GSNO at concentrations of GSH:SOD of 2:1. S-Nitrosoglutathione 93-97 superoxide dismutase 1 Homo sapiens 46-54 9882463-5 1999 Increasing GSH concentrations with respect to CuZn-SOD resulted in complete decomposition of GSNO at concentrations of GSH:SOD of 2:1. S-Nitrosoglutathione 93-97 superoxide dismutase 1 Homo sapiens 51-54 9882463-6 1999 Increasing GSH concentrations further from 0.1 to 10 mM resulted in a concentration-dependent attenuation in GSNO decomposition suggesting that SOD-catalyzed decomposition of GSNO would be maximal at concentrations of GSH known to be present in extracellular fluids (e.g., plasma). S-Nitrosoglutathione 109-113 superoxide dismutase 1 Homo sapiens 144-147 9882463-6 1999 Increasing GSH concentrations further from 0.1 to 10 mM resulted in a concentration-dependent attenuation in GSNO decomposition suggesting that SOD-catalyzed decomposition of GSNO would be maximal at concentrations of GSH known to be present in extracellular fluids (e.g., plasma). S-Nitrosoglutathione 175-179 superoxide dismutase 1 Homo sapiens 144-147 9882463-7 1999 The decomposition of GSNO by CuZn-SOD resulted in the sustained production of NO. S-Nitrosoglutathione 21-25 superoxide dismutase 1 Homo sapiens 29-37 9852090-9 1998 In addition, 8-Br-cGMP and S-nitrosoglutathione induced apoptosis in serum-deprived RPaSMC infected with Ad.PKG, but not in uninfected cells or in cells infected with a control adenovirus. S-Nitrosoglutathione 27-47 protein kinase cGMP-dependent 1 Homo sapiens 108-111 9671115-8 1998 Rbcl2-2, a Bcl-2 overexpressing clone, suppressed DNA fragmentation and U1-70kDa digestion in response to GSNO, although allowing delayed but complete poly(ADP-ribose) polymerase degradation. S-Nitrosoglutathione 106-110 BCL2 apoptosis regulator Homo sapiens 11-16 21781879-8 1998 The level of expression of bcl-2 was dramatically decreased in cells treated with SIN-1 or GSNO, while the expression level of bax, the heterodimer of bcl-2, did not significant change. S-Nitrosoglutathione 91-95 BCL2 apoptosis regulator Homo sapiens 27-32 9767577-0 1998 A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the "NO releaser", S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. S-Nitrosoglutathione 114-134 inner membrane mitochondrial protein Homo sapiens 64-67 9767577-0 1998 A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the "NO releaser", S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. S-Nitrosoglutathione 114-134 inner membrane mitochondrial protein Homo sapiens 207-210 9767577-2 1998 We now show that hmp expression is also upregulated by S-nitrosoglutathione (GSNO, widely used as an NO releaser) and sodium nitroprusside (SNP, which is a NO+ donor). S-Nitrosoglutathione 55-75 inner membrane mitochondrial protein Homo sapiens 17-20 9767577-2 1998 We now show that hmp expression is also upregulated by S-nitrosoglutathione (GSNO, widely used as an NO releaser) and sodium nitroprusside (SNP, which is a NO+ donor). S-Nitrosoglutathione 77-81 inner membrane mitochondrial protein Homo sapiens 17-20 9767577-5 1998 Mutations in metR abolished hmp induction by GSNO and SNP, and hmp expression became insensitive to Hcy. S-Nitrosoglutathione 45-49 inner membrane mitochondrial protein Homo sapiens 28-31 9767577-7 1998 Although two MetR binding sites are present in this region, only the higher affinity site proximal to hmp is required for hmp induction by GSNO and SNP. S-Nitrosoglutathione 139-143 inner membrane mitochondrial protein Homo sapiens 102-105 9767577-7 1998 Although two MetR binding sites are present in this region, only the higher affinity site proximal to hmp is required for hmp induction by GSNO and SNP. S-Nitrosoglutathione 139-143 inner membrane mitochondrial protein Homo sapiens 122-125 9767577-10 1998 As GSNO and SNP upregulate hmp similarly, the NO released in the former case on reaction with homocysteine cannot be involved in hmp regulation. S-Nitrosoglutathione 3-7 inner membrane mitochondrial protein Homo sapiens 27-30 9699892-5 1998 Expression of VCAM-1 in endothelial cells after exposure to tumour necrosis factor-alpha (TNF-alpha) or interleukin 1beta (IL-1beta) was quantified by ELISA and shown to be partially inhibited by 17beta-estradiol (40-60% inhibition) or by S-nitroso-L-glutathione, a nitric oxide donor (20-25%). S-Nitrosoglutathione 239-262 vascular cell adhesion molecule 1 Homo sapiens 14-20 9699892-5 1998 Expression of VCAM-1 in endothelial cells after exposure to tumour necrosis factor-alpha (TNF-alpha) or interleukin 1beta (IL-1beta) was quantified by ELISA and shown to be partially inhibited by 17beta-estradiol (40-60% inhibition) or by S-nitroso-L-glutathione, a nitric oxide donor (20-25%). S-Nitrosoglutathione 239-262 tumor necrosis factor Homo sapiens 90-99 9699892-5 1998 Expression of VCAM-1 in endothelial cells after exposure to tumour necrosis factor-alpha (TNF-alpha) or interleukin 1beta (IL-1beta) was quantified by ELISA and shown to be partially inhibited by 17beta-estradiol (40-60% inhibition) or by S-nitroso-L-glutathione, a nitric oxide donor (20-25%). S-Nitrosoglutathione 239-262 interleukin 1 beta Homo sapiens 123-131 9647775-1 1998 S-nitrosylation by S-nitrosoglutathione (GSNO), a nitric oxide (NO) donor, suppresses the phosphotransferase activity of cJun N-terminal kinase 2 (JNK2)/stress activated protein kinase (SAPK) in dose- and time-dependent manners in vitro. S-Nitrosoglutathione 19-39 mitogen-activated protein kinase 9 Homo sapiens 121-145 9647775-1 1998 S-nitrosylation by S-nitrosoglutathione (GSNO), a nitric oxide (NO) donor, suppresses the phosphotransferase activity of cJun N-terminal kinase 2 (JNK2)/stress activated protein kinase (SAPK) in dose- and time-dependent manners in vitro. S-Nitrosoglutathione 19-39 mitogen-activated protein kinase 9 Homo sapiens 147-151 9647775-1 1998 S-nitrosylation by S-nitrosoglutathione (GSNO), a nitric oxide (NO) donor, suppresses the phosphotransferase activity of cJun N-terminal kinase 2 (JNK2)/stress activated protein kinase (SAPK) in dose- and time-dependent manners in vitro. S-Nitrosoglutathione 41-45 mitogen-activated protein kinase 9 Homo sapiens 121-145 9647775-1 1998 S-nitrosylation by S-nitrosoglutathione (GSNO), a nitric oxide (NO) donor, suppresses the phosphotransferase activity of cJun N-terminal kinase 2 (JNK2)/stress activated protein kinase (SAPK) in dose- and time-dependent manners in vitro. S-Nitrosoglutathione 41-45 mitogen-activated protein kinase 9 Homo sapiens 147-151 9647775-2 1998 JNK2 activity is significantly decreased at 10 microM of GSNO, which is dramatically reversed by adding 10 mM of DTT. S-Nitrosoglutathione 57-61 mitogen-activated protein kinase 9 Homo sapiens 0-4 9647775-3 1998 Reduced form of glutathione protects the GSNO-induced suppression of JNK2 activation in a dose-dependent fashion. S-Nitrosoglutathione 41-45 mitogen-activated protein kinase 9 Homo sapiens 69-73 9647775-4 1998 However, GSNO-treated Sek1 does not affect the JNK2 activity of phosphotransferation toward c-Jun N-terminal1-79 protein. S-Nitrosoglutathione 9-13 mitogen-activated protein kinase kinase 4 Homo sapiens 22-26 9497319-4 1998 Kinetic analysis showed that the degradation of S-nitrosothiols in the presence of superoxide proceeded at second order rate constants of 76,900 M-1 s-1 (S-nitrosocysteine) and 12,800 M-1 s-1 (S-nitrosoglutathione), respectively, with a stoichiometric ratio of 1 mol of S-nitrosothiol per 2 mol of superoxide. S-Nitrosoglutathione 193-213 tumor associated calcium signal transducer 2 Homo sapiens 184-191 9630353-0 1998 Evidence for a cyclic GMP-independent mechanism in the anti-platelet action of S-nitrosoglutathione. S-Nitrosoglutathione 79-99 5'-nucleotidase, cytosolic II Homo sapiens 22-25 9630353-13 1998 The rate of NO release from GSNO, and its ability both to stimulate intra-platelet cyclic GMP accumulation and to inhibit platelet aggregation, were all significantly diminished by the copper (I) (Cu+) chelating agent bathocuproine disulphonic acid (BCS). S-Nitrosoglutathione 28-32 5'-nucleotidase, cytosolic II Homo sapiens 90-93 9630353-16 1998 Cyclic GMP accumulation in response to GSNO (10(-9) 10(-5) M) was undetectable following treatment of platelets with ODQ (100 microM), a selective inhibitor of soluble guanylate cyclase. S-Nitrosoglutathione 39-43 5'-nucleotidase, cytosolic II Homo sapiens 7-10 9630353-20 1998 The cyclic GMP-independent action of GSNO, observed in ODQ-treated platelets, could not be explained by an increase in intra-platelet cyclic AMP. S-Nitrosoglutathione 37-41 5'-nucleotidase, cytosolic II Homo sapiens 11-14 9630353-23 1998 Additional treatment with GSNO failed to increase the degree of aggregation inhibition, suggesting that a common pathway of thiol modification might be utilized by both GSNO and CMPS to elicit cyclic GMP-independent inhibition of platelet aggregation. S-Nitrosoglutathione 169-173 5'-nucleotidase, cytosolic II Homo sapiens 200-203 9560225-4 1998 Although caspase 3 activity was stimulated in the apoptotic macrophages, inhibition of caspase 3 by the inhibitor DEVD-CHO (N-acetyl-Asp-Glu-Val-Asp-aldehyde) did not reverse the apoptosis induced by the NO donor S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 213-233 caspase 3 Homo sapiens 87-96 9560225-4 1998 Although caspase 3 activity was stimulated in the apoptotic macrophages, inhibition of caspase 3 by the inhibitor DEVD-CHO (N-acetyl-Asp-Glu-Val-Asp-aldehyde) did not reverse the apoptosis induced by the NO donor S-nitrosoglutathione (GSNO). S-Nitrosoglutathione 235-239 caspase 3 Homo sapiens 87-96 9560225-9 1998 Treatment with the MEK inhibitor also reversed both the caspase 3 activity and poly(ADP ribose) polymerase cleavage in cells treated with GSNO. S-Nitrosoglutathione 138-142 mitogen-activated protein kinase kinase 7 Homo sapiens 19-22 9560225-9 1998 Treatment with the MEK inhibitor also reversed both the caspase 3 activity and poly(ADP ribose) polymerase cleavage in cells treated with GSNO. S-Nitrosoglutathione 138-142 caspase 3 Homo sapiens 56-65 9531510-0 1998 S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme. S-Nitrosoglutathione 0-20 alcohol dehydrogenase 5 (class III), chi polypeptide Rattus norvegicus 44-75 9546215-3 1998 Human glutathione reductase (hGR), a central enzyme of cellular antioxidant defense, is inhibited by S-nitrosoglutathione (GSNO) and by diglutathionyl-dinitroso-iron (DNIC-[GSH]2), two in vivo transport forms of NO. S-Nitrosoglutathione 101-121 glutathione-disulfide reductase Homo sapiens 6-27 9546215-3 1998 Human glutathione reductase (hGR), a central enzyme of cellular antioxidant defense, is inhibited by S-nitrosoglutathione (GSNO) and by diglutathionyl-dinitroso-iron (DNIC-[GSH]2), two in vivo transport forms of NO. S-Nitrosoglutathione 123-127 glutathione-disulfide reductase Homo sapiens 6-27 9461573-8 1998 NF-kappaB activation was also strongly inhibited by S-nitrosoglutathione but was marginally affected by N-(2-aminoethyl)-N-(2-hydroxy-2-nitrosohydrazino)-1, 2-ethylenediamine. S-Nitrosoglutathione 52-72 nuclear factor kappa B subunit 1 Homo sapiens 0-9 9452441-9 1998 The product of NOS and GSH was identified as the thionitrite GSNO, which activated sGC through Cu+-catalyzed release of free NO. S-Nitrosoglutathione 61-65 guanylate cyclase 1 soluble subunit beta 2 Rattus norvegicus 83-86 9419178-4 1998 However, lipopolysaccharide-induced IL-8 production was increased in a dose-dependent manner by a combination of sodium nitroprusside and N-acetylcysteine (P = .03) or by S-nitrosoglutathione (P = .004). S-Nitrosoglutathione 171-191 C-X-C motif chemokine ligand 8 Homo sapiens 36-40 9544795-8 1998 In contrast, heme oxygenase-1 expression remained elevated under conditions of GSNO/DMNQ coadministration. S-Nitrosoglutathione 79-83 heme oxygenase 1 Rattus norvegicus 13-29 9699005-6 1998 Incubation with H202 or the NO donor S-nitrosylated GSH (GSNO), diminish MAT activity in a dose-and time-dependent manner. S-Nitrosoglutathione 57-61 methionine adenosyltransferase 1A Homo sapiens 73-76 9496265-2 1997 Consequently, the effects have been investigated of the NO-releasing compounds 3-morpholino-sydnonimine (SIN-1) and S-nitroso-glutathione (GSNO) on the in vitro adhesion of human melanocytic cells to fibronectin. S-Nitrosoglutathione 116-137 fibronectin 1 Homo sapiens 200-211 9393673-1 1997 Human glutathione reductase (GR) and rat liver glutathione-S-transferases (GSTs) had been shown to be inhibited by the nitric oxide (NO) carrier S-nitroso-glutathione (GSNO). S-Nitrosoglutathione 145-166 glutathione-disulfide reductase Rattus norvegicus 6-27 9393673-1 1997 Human glutathione reductase (GR) and rat liver glutathione-S-transferases (GSTs) had been shown to be inhibited by the nitric oxide (NO) carrier S-nitroso-glutathione (GSNO). S-Nitrosoglutathione 145-166 glutathione-disulfide reductase Rattus norvegicus 29-31 9393673-1 1997 Human glutathione reductase (GR) and rat liver glutathione-S-transferases (GSTs) had been shown to be inhibited by the nitric oxide (NO) carrier S-nitroso-glutathione (GSNO). S-Nitrosoglutathione 145-166 glutathione S-transferase kappa 1 Homo sapiens 75-79 9393673-1 1997 Human glutathione reductase (GR) and rat liver glutathione-S-transferases (GSTs) had been shown to be inhibited by the nitric oxide (NO) carrier S-nitroso-glutathione (GSNO). S-Nitrosoglutathione 168-172 glutathione-disulfide reductase Rattus norvegicus 6-27 9393673-1 1997 Human glutathione reductase (GR) and rat liver glutathione-S-transferases (GSTs) had been shown to be inhibited by the nitric oxide (NO) carrier S-nitroso-glutathione (GSNO). S-Nitrosoglutathione 168-172 glutathione-disulfide reductase Rattus norvegicus 29-31 9393673-1 1997 Human glutathione reductase (GR) and rat liver glutathione-S-transferases (GSTs) had been shown to be inhibited by the nitric oxide (NO) carrier S-nitroso-glutathione (GSNO). S-Nitrosoglutathione 168-172 glutathione S-transferase kappa 1 Homo sapiens 75-79 9393673-13 1997 Inactivation of GR by DNIC-[GSH]2 is by two orders of magnitude more effective than modification by GSNO; this result and the very efficient inhibition of GST point to a role of DNIC-[RSH]2 in glutathione metabolism. S-Nitrosoglutathione 100-104 glutathione-disulfide reductase Homo sapiens 16-18 9877228-3 1998 The presence of either S-nitrosoglutathione (GS-NO) or sodium nitroprusside (SNP) (10(-6)-10(-4) M) at the time of the assay caused a significant increase in TPO activity. S-Nitrosoglutathione 23-43 thyroid peroxidase Homo sapiens 158-161 9398310-0 1997 Modification of aldose reductase by S-nitrosoglutathione. S-Nitrosoglutathione 36-56 aldo-keto reductase family 1 member B Homo sapiens 16-32 9398310-1 1997 Kinetic and structural changes in recombinant human aldose reductase (AR) due to modification by S-nitrosoglutathione (GSNO) were investigated. S-Nitrosoglutathione 97-117 aldo-keto reductase family 1 member B Homo sapiens 52-68 9398310-1 1997 Kinetic and structural changes in recombinant human aldose reductase (AR) due to modification by S-nitrosoglutathione (GSNO) were investigated. S-Nitrosoglutathione 97-117 aldo-keto reductase family 1 member B Homo sapiens 70-72 9398310-1 1997 Kinetic and structural changes in recombinant human aldose reductase (AR) due to modification by S-nitrosoglutathione (GSNO) were investigated. S-Nitrosoglutathione 119-123 aldo-keto reductase family 1 member B Homo sapiens 52-68 9398310-1 1997 Kinetic and structural changes in recombinant human aldose reductase (AR) due to modification by S-nitrosoglutathione (GSNO) were investigated. S-Nitrosoglutathione 119-123 aldo-keto reductase family 1 member B Homo sapiens 70-72 9398310-2 1997 Incubation of the enzyme with 10-50 microM GSNO led to a time- and concentration-dependent inactivation of the enzyme, with a second-order rate constant of 0.087 +/- 0.009 M-1 min-1. S-Nitrosoglutathione 43-47 CD59 molecule (CD59 blood group) Homo sapiens 176-181 9398310-12 1997 These results suggest that inactivation of AR by GSNO is due to the selective formation of a single mixed disulfide between glutathione and Cys-298 located at the NADP(H)-binding site of the enzyme. S-Nitrosoglutathione 49-53 aldo-keto reductase family 1 member B Homo sapiens 43-45 9423805-5 1997 Platelet P-selectin expression increased during bypass both in controls and patients receiving GSNO. S-Nitrosoglutathione 95-99 selectin P Homo sapiens 9-19 9278333-4 1997 This increase in M-CSF expression was attenuated by a nitric oxide donor, S-nitrosoglutathione (GSNO), and by a nonspecific oxidase inhibitor, diphenylene iodonium. S-Nitrosoglutathione 74-94 colony stimulating factor 1 Homo sapiens 17-22 9278333-6 1997 Transient transfection studies using deletional M-CSF promoter constructs demonstrated that TGF-beta1 produced a 13-fold induction in M-CSF promoter activity that was repressed by >85% with GSNO and catalase, in part through inhibitory effects on kappaB cis-acting elements. S-Nitrosoglutathione 193-197 transforming growth factor beta 1 Homo sapiens 92-101 9285487-6 1997 In parallel, preactivation of RAW cells with a low, nontoxic dose of S-nitrosoglutathione promoted protection and cyclooxygenase-2 up-regulation. S-Nitrosoglutathione 69-89 prostaglandin-endoperoxide synthase 2 Rattus norvegicus 114-130 9278333-6 1997 Transient transfection studies using deletional M-CSF promoter constructs demonstrated that TGF-beta1 produced a 13-fold induction in M-CSF promoter activity that was repressed by >85% with GSNO and catalase, in part through inhibitory effects on kappaB cis-acting elements. S-Nitrosoglutathione 193-197 colony stimulating factor 1 Homo sapiens 134-139 9278333-4 1997 This increase in M-CSF expression was attenuated by a nitric oxide donor, S-nitrosoglutathione (GSNO), and by a nonspecific oxidase inhibitor, diphenylene iodonium. S-Nitrosoglutathione 96-100 colony stimulating factor 1 Homo sapiens 17-22 9278333-7 1997 Electrophoretic mobility shift assays revealed that the activation of nuclear factor-kappaB by TGF-beta1 was also inhibited by GSNO and catalase, but not by superoxide dismutase. S-Nitrosoglutathione 127-131 transforming growth factor beta 1 Homo sapiens 95-104 9233642-4 1997 Furthermore, the nitric oxide donors sodium nitroprusside and S-nitrosoglutathione inhibited degranulation, and this effect was direct, since it was seen equally on purified and unfractionated mast cells and occurred independently of IFN-gammaR expression. S-Nitrosoglutathione 62-82 interferon gamma receptor 1 Mus musculus 234-244 9235967-8 1997 However, GSNO decreased BK-stimulated Galphai2, Galphai3, and Galphaq/11 GTP binding activity by 93, 61, and 90%, respectively, whereas epinephrine-stimulated Galphas GTP binding activity was unaffected. S-Nitrosoglutathione 9-13 kininogen 1 Homo sapiens 24-26 9259594-4 1997 Sodium nitroprusside and S-nitroso-glutathione decreased sGC subunit mRNA and protein levels, as well as sGC enzyme activity. S-Nitrosoglutathione 25-46 guanylate cyclase 1 soluble subunit beta 2 Rattus norvegicus 57-60 9208127-7 1997 TPA (100 nM) attentuated p53 up-regulation elicited by the NO-releasing compounds, S-nitrosoglutathione (1 mM) and sodium nitroprusside (1 mM), and suppressed p53 protein accumulation in response to endogenously generated NO. S-Nitrosoglutathione 83-103 transformation related protein 53, pseudogene Mus musculus 25-28 9354392-2 1997 Treatment with each of three NO donors, sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione, caused noticeable increases in the expression levels of heme oxygenase- mRNA, but not heme oxygenase-2 mRNA. S-Nitrosoglutathione 91-114 heme oxygenase 2 Homo sapiens 202-218 9163341-3 1997 gamma-GT accelerated the decomposition of GSNO, forming S-nitrosocysteinylglycine (CG-SNO) by a mechanism inhibitable by the gamma-GT inhibitors acivicin and S-methylglutathione. S-Nitrosoglutathione 42-46 gamma-glutamyltransferase 1 Rattus norvegicus 0-8 9144512-16 1997 Manipulation of the endogenous NO./O2- ratio by exogenous, sublethal S-nitrosoglutathione in addition to cytokines produced death, which was antagonized by inducible nitric oxide synthase (iNOS) inhibition. S-Nitrosoglutathione 69-89 nitric oxide synthase 2 Rattus norvegicus 156-187 9144512-16 1997 Manipulation of the endogenous NO./O2- ratio by exogenous, sublethal S-nitrosoglutathione in addition to cytokines produced death, which was antagonized by inducible nitric oxide synthase (iNOS) inhibition. S-Nitrosoglutathione 69-89 nitric oxide synthase 2 Rattus norvegicus 189-193 9163341-0 1997 S-Nitrosoglutathione as a substrate for gamma-glutamyl transpeptidase. S-Nitrosoglutathione 0-20 gamma-glutamyltransferase 1 Rattus norvegicus 40-69 9163341-2 1997 In this study we have examined the possibility that GSNO is a substrate for gamma-glutamyl transpeptidase (gamma-GT), an enzyme that hydrolyses the gamma-glutamyl moiety of glutathione to give glutamate and cysteinylglycine. S-Nitrosoglutathione 52-56 gamma-glutamyltransferase 1 Rattus norvegicus 76-105 9163341-3 1997 gamma-GT accelerated the decomposition of GSNO, forming S-nitrosocysteinylglycine (CG-SNO) by a mechanism inhibitable by the gamma-GT inhibitors acivicin and S-methylglutathione. S-Nitrosoglutathione 42-46 gamma-glutamyltransferase 1 Rattus norvegicus 125-133 9163341-2 1997 In this study we have examined the possibility that GSNO is a substrate for gamma-glutamyl transpeptidase (gamma-GT), an enzyme that hydrolyses the gamma-glutamyl moiety of glutathione to give glutamate and cysteinylglycine. S-Nitrosoglutathione 52-56 gamma-glutamyltransferase 1 Rattus norvegicus 107-115 9163341-4 1997 The Km of gamma-GT for GSNO was found to be 28 microM. S-Nitrosoglutathione 23-27 gamma-glutamyltransferase 1 Rattus norvegicus 10-18 9163341-5 1997 In the presence of contaminating transition metal ions, gamma-GT accelerated the release of ;NO from GSNO, as CG-SNO is more susceptible to transition metal ion-dependent decomposition than GSNO. S-Nitrosoglutathione 101-105 gamma-glutamyltransferase 1 Rattus norvegicus 56-64 9163341-5 1997 In the presence of contaminating transition metal ions, gamma-GT accelerated the release of ;NO from GSNO, as CG-SNO is more susceptible to transition metal ion-dependent decomposition than GSNO. S-Nitrosoglutathione 190-194 gamma-glutamyltransferase 1 Rattus norvegicus 56-64 9163341-9 1997 It is likely therefore that gamma-GT is involved in the decomposition of GSNO in the kidney but not in the heart. S-Nitrosoglutathione 73-77 gamma-glutamyltransferase 1 Rattus norvegicus 28-36 8944732-1 1996 We have previously shown that nitric oxide (NO) donors, such as nitrosoglutathione, inhibit endothelial cell (EC) xanthine dehydrogenase (XD)/xanthine oxidase (XO) activity. S-Nitrosoglutathione 64-82 xanthine dehydrogenase Rattus norvegicus 114-136 8960071-1 1997 Glutathione transferase (GST)-catalysed S-nitrosoglutathione (GSNO) formation from alkyl nitrites was determined with the homodimers 1-1, 2-2, 3-3, and 4-4 isolated from rat liver. S-Nitrosoglutathione 40-60 glutathione S-transferase alpha 4 Rattus norvegicus 0-23 8960071-1 1997 Glutathione transferase (GST)-catalysed S-nitrosoglutathione (GSNO) formation from alkyl nitrites was determined with the homodimers 1-1, 2-2, 3-3, and 4-4 isolated from rat liver. S-Nitrosoglutathione 62-66 glutathione S-transferase alpha 4 Rattus norvegicus 0-23 8962079-13 1996 When, in the presence of SOD, glutathione was added, S-nitrosoglutathione was detected. S-Nitrosoglutathione 53-73 superoxide dismutase 1 Homo sapiens 25-28 8960071-0 1997 Subunit specificity and organ distribution of glutathione transferase-catalysed S-nitrosoglutathione formation from alkyl nitrites in the rat. S-Nitrosoglutathione 80-100 glutathione S-transferase alpha 4 Rattus norvegicus 46-69 8995451-8 1997 Finally, endogenous NO formation, induced in hepatocytes stimulated with interferon-gamma and interleukin-1beta, led to the formation of GSNO and GSSG, induced HSP70, and attenuated TNFalpha-mediated cytotoxicity. S-Nitrosoglutathione 137-141 interferon gamma Rattus norvegicus 73-89 8995451-8 1997 Finally, endogenous NO formation, induced in hepatocytes stimulated with interferon-gamma and interleukin-1beta, led to the formation of GSNO and GSSG, induced HSP70, and attenuated TNFalpha-mediated cytotoxicity. S-Nitrosoglutathione 137-141 interleukin 1 beta Rattus norvegicus 94-111 8954910-2 1996 The cellular response to the NO donor S-nitrosoglutathione (GSNO) comprises an apoptotic morphology and DNA fragmentation, which largely depends on the accumulation of the tumor suppressor gene product p53. S-Nitrosoglutathione 38-58 tumor protein p53 Homo sapiens 202-205 8954910-2 1996 The cellular response to the NO donor S-nitrosoglutathione (GSNO) comprises an apoptotic morphology and DNA fragmentation, which largely depends on the accumulation of the tumor suppressor gene product p53. S-Nitrosoglutathione 60-64 tumor protein p53 Homo sapiens 202-205 8954910-3 1996 Pre-treatment of macrophages with LPS, IFN-gamma in the presence of NG-monomethyl-L-arginine (NMMA) imparts resistance to apoptotic cell death, normally elicited by exogenously-supplied GSNO. S-Nitrosoglutathione 186-190 interferon gamma Homo sapiens 39-48 8836116-3 1996 H2O2 strongly enhanced the inhibitory effects of S-nitrosoglutathione (GSNO) on thrombin-induced aggregation of WP. S-Nitrosoglutathione 49-69 coagulation factor II, thrombin Homo sapiens 80-88 8870682-4 1996 With the use of S-nitroglutathione (GSNO) we correlated a dose-dependent p53 up-regulation to DNA fragmentation measured after 4 h and 8 h, respectively. S-Nitrosoglutathione 36-40 tumor protein p53 Homo sapiens 73-76 8870682-7 1996 Clones with down-regulated p53 levels in response to GSNO exhibited a marked reduction in DNA fragmentation. S-Nitrosoglutathione 53-57 tumor protein p53 Homo sapiens 27-30 8894174-5 1996 The biological action of GSNO could be mediated by NO released from S-nitrosocystylglycine, following enzymatic cleavage of GSNO by gamma-glutamyl transpeptidase. S-Nitrosoglutathione 25-29 inactive glutathione hydrolase 2 Homo sapiens 132-161 8894174-5 1996 The biological action of GSNO could be mediated by NO released from S-nitrosocystylglycine, following enzymatic cleavage of GSNO by gamma-glutamyl transpeptidase. S-Nitrosoglutathione 124-128 inactive glutathione hydrolase 2 Homo sapiens 132-161 8894174-11 1996 Breakdown of GSNO showed a non-significant acceleration in the presence of cysteine, from 0.56 +/- 0.22 to 1.77 +/- 0.27 nmol min-1 (mean +/- s.e.mean) (P = 0.064, n = 4), and its ability to inhibit platelet aggregation was not enhanced by cysteine. S-Nitrosoglutathione 13-17 CD59 molecule (CD59 blood group) Homo sapiens 126-131 8836116-3 1996 H2O2 strongly enhanced the inhibitory effects of S-nitrosoglutathione (GSNO) on thrombin-induced aggregation of WP. S-Nitrosoglutathione 71-75 coagulation factor II, thrombin Homo sapiens 80-88 8660704-7 1996 3-Morpholinosynodiomine.HCl (SIN-1) and sodium nitroprusside (SNP) enhanced hydrogen peroxide-mediated cytotoxicity, while S-nitrosoglutathione (GSNO), and S-nitroso-N-acetylpenicillamine (SNAP) afforded protection. S-Nitrosoglutathione 123-143 MAPK associated protein 1 Homo sapiens 29-34 8702745-5 1996 Bcl-2 transfectants showed substantial protection from cell death induced following the exposure to NO donors such as S-nitrosoglutathione (GSNO) and spermine-NO. S-Nitrosoglutathione 118-138 B cell leukemia/lymphoma 2 Mus musculus 0-5 8702745-5 1996 Bcl-2 transfectants showed substantial protection from cell death induced following the exposure to NO donors such as S-nitrosoglutathione (GSNO) and spermine-NO. S-Nitrosoglutathione 140-144 B cell leukemia/lymphoma 2 Mus musculus 0-5 8702745-10 1996 GSNO induced p53 expression in Bcl-2 transfectants at levels comparable with nontransfected RAW macrophages. S-Nitrosoglutathione 0-4 transformation related protein 53, pseudogene Mus musculus 13-16 8702745-10 1996 GSNO induced p53 expression in Bcl-2 transfectants at levels comparable with nontransfected RAW macrophages. S-Nitrosoglutathione 0-4 B cell leukemia/lymphoma 2 Mus musculus 31-36 8702745-11 1996 Moreover, GSNO induced increases in the steady-state levels of Bax protein in parental and Bcl-2-transfected cells. S-Nitrosoglutathione 10-14 BCL2-associated X protein Mus musculus 63-66 8702745-11 1996 Moreover, GSNO induced increases in the steady-state levels of Bax protein in parental and Bcl-2-transfected cells. S-Nitrosoglutathione 10-14 B cell leukemia/lymphoma 2 Mus musculus 91-96 8764571-4 1996 In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs. S-Nitrosoglutathione 140-163 heme oxygenase 1 Homo sapiens 212-228 8764571-4 1996 In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs. S-Nitrosoglutathione 140-163 heme oxygenase 2 Homo sapiens 259-275 8702596-0 1996 S-nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide. S-Nitrosoglutathione 0-20 thioredoxin Homo sapiens 39-50 8702596-2 1996 We discovered that GSNO is an NADPH oxidizing substrate for human or calf thymus thioredoxin reductase (TR) with an apparent Km value of 60 microM and a Kcat of 0.6 x s-1. S-Nitrosoglutathione 19-23 thioredoxin Bos taurus 81-92 8702596-4 1996 Escherichia coli TR lacked activity with GSNO, but with E. coli Trx present, GSNO was reduced without inhibition of the enzyme. S-Nitrosoglutathione 77-81 thioredoxin Homo sapiens 64-67 8702596-5 1996 Chemically reduced E. coli Trx-(SH)2 was oxidized to Trx-S2 by GSNO with a rate constant of 760 M-1s-1 (7-fold faster than by GSSG) as measured by tryptophan fluorescence. S-Nitrosoglutathione 63-67 thioredoxin Homo sapiens 27-30 8702596-5 1996 Chemically reduced E. coli Trx-(SH)2 was oxidized to Trx-S2 by GSNO with a rate constant of 760 M-1s-1 (7-fold faster than by GSSG) as measured by tryptophan fluorescence. S-Nitrosoglutathione 63-67 thioredoxin Homo sapiens 53-56 8702596-9 1996 These results demonstrate a homolytic cleavage mechanism of GSNO, giving rise to GSH and NO.. GSNO efficiently inhibited the protein disulfide reductase activity of the complete human or calf thymus thioredoxin systems. S-Nitrosoglutathione 60-64 thioredoxin Bos taurus 199-210 8702596-9 1996 These results demonstrate a homolytic cleavage mechanism of GSNO, giving rise to GSH and NO.. GSNO efficiently inhibited the protein disulfide reductase activity of the complete human or calf thymus thioredoxin systems. S-Nitrosoglutathione 94-98 thioredoxin Bos taurus 199-210 8702596-10 1996 Our results demonstrate enzymatic cleavage of GSNO by TR or Trx and suggest novel mechanisms for redox signaling. S-Nitrosoglutathione 46-50 thioredoxin Homo sapiens 60-63 8615678-8 1996 The level of the tumor suppressor p53 increases in response to NO donors like GSNO and effectively senses NO intoxication in macrophages. S-Nitrosoglutathione 78-82 tumor protein p53 Homo sapiens 34-37 8612815-2 1996 With the use of NO donors such as S-nitrosoglutathione or spermine-NO we established that PARP digestion occurs in parallel with DNA fragmentation, and is preceded by accumulation of the tumor suppressor gene product p53. S-Nitrosoglutathione 34-54 poly(ADP-ribose) polymerase 1 Homo sapiens 90-94 8612815-2 1996 With the use of NO donors such as S-nitrosoglutathione or spermine-NO we established that PARP digestion occurs in parallel with DNA fragmentation, and is preceded by accumulation of the tumor suppressor gene product p53. S-Nitrosoglutathione 34-54 tumor protein p53 Homo sapiens 217-220 8615678-9 1996 GSNO removal concomitantly allows p53 to decline with only a small percentage of cells showing DNA fragmentation. S-Nitrosoglutathione 0-4 tumor protein p53 Homo sapiens 34-37 8536691-0 1995 Inhibition of human glutathione reductase by S-nitrosoglutathione. S-Nitrosoglutathione 45-65 glutathione-disulfide reductase Homo sapiens 20-41 8548426-6 1996 In both AMI and UA, S-nitrosoglutathione reduced P-selectin (P < .001) and glycoprotein IIb/IIIa (P < .05) expression, as did glyceryl trinitrate (P < .02 and P < .01, respectively). S-Nitrosoglutathione 20-40 selectin P Homo sapiens 49-59 8536691-2 1995 Since NO and GSNO have been shown to modulate the function of various proteins, we studied the influence of GSNO and other NO donors on human glutathione reductase (GR). S-Nitrosoglutathione 108-112 glutathione-disulfide reductase Homo sapiens 165-167 8536691-4 1995 GSNO was found to inhibit crystalline erythrocyte GR in two ways: (a) as a reversible inhibitor GSNO is competitive with glutathione disulfide (GSSG), the Ki being appr. S-Nitrosoglutathione 0-4 glutathione-disulfide reductase Homo sapiens 50-52 8536691-4 1995 GSNO was found to inhibit crystalline erythrocyte GR in two ways: (a) as a reversible inhibitor GSNO is competitive with glutathione disulfide (GSSG), the Ki being appr. S-Nitrosoglutathione 96-100 glutathione-disulfide reductase Homo sapiens 50-52 8536691-5 1995 0.5 mM; (b) as an irreversible inhibitor; after 1 h (3 h) incubation with 1 mM GSNO, GR (2.5 U/ml, representing intraerythrocytic concentrations) was inhibited by 70% (90%). S-Nitrosoglutathione 79-83 glutathione-disulfide reductase Homo sapiens 85-87 8536691-8 1995 In a GR sample inhibited by 90% with GSNO, the Km values for the substrates GSSG and NADPH were not significantly changed nor did the modification induce oxidase activity of the enzyme. S-Nitrosoglutathione 37-41 glutathione-disulfide reductase Homo sapiens 5-7 8536691-9 1995 GSNO was found not to be a substrate in the forward reaction of GR. S-Nitrosoglutathione 0-4 glutathione-disulfide reductase Homo sapiens 64-66 8536691-13 1995 GSNO inhibition patterns comparable to purified authentic GR were obtained for purified recombinant GR, a GR mutant lacking the 15 N-terminal amino acids including Cys2, and for the enzyme present in diluted fresh haemolysates (0.02 U/ml); in concentrated haemolysates the inhibition was less pronounced. S-Nitrosoglutathione 0-4 glutathione-disulfide reductase Homo sapiens 100-102 8536691-13 1995 GSNO inhibition patterns comparable to purified authentic GR were obtained for purified recombinant GR, a GR mutant lacking the 15 N-terminal amino acids including Cys2, and for the enzyme present in diluted fresh haemolysates (0.02 U/ml); in concentrated haemolysates the inhibition was less pronounced. S-Nitrosoglutathione 0-4 glutathione-disulfide reductase Homo sapiens 100-102 8536691-15 1995 Our results suggest that the irreversible inhibition of GR by GSNO involves nitrosylation of Cys63 and/or Cys58 at the catalytic site of the enzyme. S-Nitrosoglutathione 62-66 glutathione-disulfide reductase Homo sapiens 56-58 8536691-16 1995 To further investigate the mechanism of inactivation we have crystallized GSNO-modified GR for X-ray diffraction analysis. S-Nitrosoglutathione 74-78 glutathione-disulfide reductase Homo sapiens 88-90 7573405-3 1995 In this study, we investigated the mechanism involved in NO-mediated GAPDH inhibition and found that S-nitrosoglutathione (GSNO) inhibited GAPDH activity in both purified enzyme preparations and endothelial cells. S-Nitrosoglutathione 123-127 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 69-74 7573405-3 1995 In this study, we investigated the mechanism involved in NO-mediated GAPDH inhibition and found that S-nitrosoglutathione (GSNO) inhibited GAPDH activity in both purified enzyme preparations and endothelial cells. S-Nitrosoglutathione 123-127 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 139-144 7573405-0 1995 S-nitrosoglutathione reversibly inhibits GAPDH by S-nitrosylation. S-Nitrosoglutathione 0-20 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 41-46 7573405-4 1995 Furthermore, GSNO-mediated GAPDH inhibition occurred by modification of the active site cysteine residue in GAPDH, since increasing concentrations of the substrate, glyceraldehyde-3-phosphate, which interacts with the active site cysteine residue, protected GAPDH from inhibition by GSNO. S-Nitrosoglutathione 13-17 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 27-32 7573405-3 1995 In this study, we investigated the mechanism involved in NO-mediated GAPDH inhibition and found that S-nitrosoglutathione (GSNO) inhibited GAPDH activity in both purified enzyme preparations and endothelial cells. S-Nitrosoglutathione 101-121 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 69-74 7573405-3 1995 In this study, we investigated the mechanism involved in NO-mediated GAPDH inhibition and found that S-nitrosoglutathione (GSNO) inhibited GAPDH activity in both purified enzyme preparations and endothelial cells. S-Nitrosoglutathione 101-121 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 139-144 7573405-4 1995 Furthermore, GSNO-mediated GAPDH inhibition occurred by modification of the active site cysteine residue in GAPDH, since increasing concentrations of the substrate, glyceraldehyde-3-phosphate, which interacts with the active site cysteine residue, protected GAPDH from inhibition by GSNO. S-Nitrosoglutathione 13-17 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-113 7573405-4 1995 Furthermore, GSNO-mediated GAPDH inhibition occurred by modification of the active site cysteine residue in GAPDH, since increasing concentrations of the substrate, glyceraldehyde-3-phosphate, which interacts with the active site cysteine residue, protected GAPDH from inhibition by GSNO. S-Nitrosoglutathione 13-17 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-113 7573405-4 1995 Furthermore, GSNO-mediated GAPDH inhibition occurred by modification of the active site cysteine residue in GAPDH, since increasing concentrations of the substrate, glyceraldehyde-3-phosphate, which interacts with the active site cysteine residue, protected GAPDH from inhibition by GSNO. S-Nitrosoglutathione 283-287 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 27-32 7573405-4 1995 Furthermore, GSNO-mediated GAPDH inhibition occurred by modification of the active site cysteine residue in GAPDH, since increasing concentrations of the substrate, glyceraldehyde-3-phosphate, which interacts with the active site cysteine residue, protected GAPDH from inhibition by GSNO. S-Nitrosoglutathione 283-287 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-113 7573405-4 1995 Furthermore, GSNO-mediated GAPDH inhibition occurred by modification of the active site cysteine residue in GAPDH, since increasing concentrations of the substrate, glyceraldehyde-3-phosphate, which interacts with the active site cysteine residue, protected GAPDH from inhibition by GSNO. S-Nitrosoglutathione 283-287 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-113 7573405-5 1995 Although under certain conditions both GSNO and the NO donor, sodium nitroprusside (SNP), led to the covalent NAD(+)-dependent modification of GAPDH, this putative ADP ribosylation was unlikely to be the primary mechanism for inhibition, since the stoichiometry was extremely low, and, in the case of GSNO, inhibition was completely reversed by thiol reagents. S-Nitrosoglutathione 39-43 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 143-148 7573405-6 1995 Furthermore, GSNO effectively S-nitrosylated GAPDH, and the extent of nitrosylation was linearly correlated with the degree of inhibition such that addition of 1 mole of NO per mole of GAPDH monomer was necessary to inhibit the enzyme. S-Nitrosoglutathione 13-17 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 45-50 7573405-6 1995 Furthermore, GSNO effectively S-nitrosylated GAPDH, and the extent of nitrosylation was linearly correlated with the degree of inhibition such that addition of 1 mole of NO per mole of GAPDH monomer was necessary to inhibit the enzyme. S-Nitrosoglutathione 13-17 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 185-190 7573405-7 1995 Consistent with this finding, GSNO-mediated GAPDH inhibition was reversible with low-molecular-weight thiols, and the reversal of inhibition correlated with the "denitrosylation" of GAPDH. S-Nitrosoglutathione 30-34 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 44-49 7573405-7 1995 Consistent with this finding, GSNO-mediated GAPDH inhibition was reversible with low-molecular-weight thiols, and the reversal of inhibition correlated with the "denitrosylation" of GAPDH. S-Nitrosoglutathione 30-34 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 182-187 1978674-1 1990 In the presence of oxidized low-density lipoprotein the stimulatory effects of nitric oxide, sodium nitroprusside and S-nitrosoglutathione on soluble guanylate cyclase partially purified from bovine platelets were diminished in a concentration-dependent manner with IC50 values around 100 micrograms total cholesterol/ml. S-Nitrosoglutathione 118-138 guanylate cyclase Bos taurus 150-167 7780643-4 1995 Chelation of trace copper with BCS (10 microM) in washed platelet suspensions reduced the inhibition of thrombin-induced platelet aggregation by GSNO; however, BCS had no significant effect on the anti-aggregatory action of cysNO. S-Nitrosoglutathione 145-149 coagulation factor II, thrombin Homo sapiens 104-112 7526102-8 1994 GSNO significantly inhibited the PTCA-induced increase in platelet surface expression of P-selectin and glycoprotein IIb/IIIa without altering blood pressure. S-Nitrosoglutathione 0-4 selectin P Homo sapiens 89-99 7831682-4 1994 On fibrinogen spreading was inhibited by NO donors in the order of potency: S-nitroso-acetylpenicillamine > sodium nitroprusside > S-nitroso-glutathione. S-Nitrosoglutathione 137-158 fibrinogen beta chain Homo sapiens 3-13 7622526-3 1995 The induction of M-CSF mRNA expression by either oxidized low density lipoprotein (ox-LDL) or tumor necrosis factor-alpha (TNF alpha) was attenuated by NO donors, S-nitrosoglutathione (GSNO), sodium nitroprusside (SNP), and 3-morpholinosydnonimine, but not by cGMP analogues, glutathione, or nitrite. S-Nitrosoglutathione 163-183 colony stimulating factor 1 Homo sapiens 17-22 7622526-3 1995 The induction of M-CSF mRNA expression by either oxidized low density lipoprotein (ox-LDL) or tumor necrosis factor-alpha (TNF alpha) was attenuated by NO donors, S-nitrosoglutathione (GSNO), sodium nitroprusside (SNP), and 3-morpholinosydnonimine, but not by cGMP analogues, glutathione, or nitrite. S-Nitrosoglutathione 163-183 tumor necrosis factor Homo sapiens 123-132 7622526-3 1995 The induction of M-CSF mRNA expression by either oxidized low density lipoprotein (ox-LDL) or tumor necrosis factor-alpha (TNF alpha) was attenuated by NO donors, S-nitrosoglutathione (GSNO), sodium nitroprusside (SNP), and 3-morpholinosydnonimine, but not by cGMP analogues, glutathione, or nitrite. S-Nitrosoglutathione 185-189 colony stimulating factor 1 Homo sapiens 17-22 7622526-3 1995 The induction of M-CSF mRNA expression by either oxidized low density lipoprotein (ox-LDL) or tumor necrosis factor-alpha (TNF alpha) was attenuated by NO donors, S-nitrosoglutathione (GSNO), sodium nitroprusside (SNP), and 3-morpholinosydnonimine, but not by cGMP analogues, glutathione, or nitrite. S-Nitrosoglutathione 185-189 tumor necrosis factor Homo sapiens 94-121 7622526-3 1995 The induction of M-CSF mRNA expression by either oxidized low density lipoprotein (ox-LDL) or tumor necrosis factor-alpha (TNF alpha) was attenuated by NO donors, S-nitrosoglutathione (GSNO), sodium nitroprusside (SNP), and 3-morpholinosydnonimine, but not by cGMP analogues, glutathione, or nitrite. S-Nitrosoglutathione 185-189 tumor necrosis factor Homo sapiens 123-132 7622526-6 1995 Electrophoretic mobility shift assays demonstrated that activation of NF-kappa B by L-NMA, ox-LDL, and TNF alpha was attenuated by GSNO and SNP, but not by glutathione or cGMP analogues. S-Nitrosoglutathione 131-135 nuclear factor kappa B subunit 1 Homo sapiens 70-80 7622526-6 1995 Electrophoretic mobility shift assays demonstrated that activation of NF-kappa B by L-NMA, ox-LDL, and TNF alpha was attenuated by GSNO and SNP, but not by glutathione or cGMP analogues. S-Nitrosoglutathione 131-135 tumor necrosis factor Homo sapiens 103-112 21043729-9 1995 Platelet GGT may influence intracellular S-nitrosoglutathione (a putative nitric oxide donor) levels. S-Nitrosoglutathione 41-61 gamma-glutamyltransferase light chain family member 3 Homo sapiens 9-12 34956283-3 2021 The enzyme S-nitrosoglutathione reductase (GSNOR) is a major route of NADH-dependent GSNO catabolism and is critical to NO homeostasis. S-Nitrosoglutathione 85-89 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 11-41 34919280-4 2022 Although the ADH2/GSNOR1 enzyme can act on different substrates, notably on S-hydroxymethylglutathione (HMG) and S-nitrosoglutathione (GSNO), our study provides several lines of evidence that the sensitivity of gsnor1 to UV-B is caused mainly by UV-B-induced formaldehyde accumulation rather than other factors such as alteration of the GSNO concentration. S-Nitrosoglutathione 113-133 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 13-17 34919280-4 2022 Although the ADH2/GSNOR1 enzyme can act on different substrates, notably on S-hydroxymethylglutathione (HMG) and S-nitrosoglutathione (GSNO), our study provides several lines of evidence that the sensitivity of gsnor1 to UV-B is caused mainly by UV-B-induced formaldehyde accumulation rather than other factors such as alteration of the GSNO concentration. S-Nitrosoglutathione 135-139 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 13-17 34919280-4 2022 Although the ADH2/GSNOR1 enzyme can act on different substrates, notably on S-hydroxymethylglutathione (HMG) and S-nitrosoglutathione (GSNO), our study provides several lines of evidence that the sensitivity of gsnor1 to UV-B is caused mainly by UV-B-induced formaldehyde accumulation rather than other factors such as alteration of the GSNO concentration. S-Nitrosoglutathione 337-341 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 13-17 34956283-3 2021 The enzyme S-nitrosoglutathione reductase (GSNOR) is a major route of NADH-dependent GSNO catabolism and is critical to NO homeostasis. S-Nitrosoglutathione 85-89 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 43-48 34956283-7 2021 Because specific AKRs have been linked to NO metabolism in mammals, we expressed and purified A. thaliana AKR4C8 and 9 and close homologs AKR4C10 and 11 and determined that they have NADPH-dependent activity in GSNO and S-nitroso-coenzyme A (SNO-CoA) reduction. S-Nitrosoglutathione 211-215 NAD(P)-linked oxidoreductase superfamily protein Arabidopsis thaliana 106-118 34956283-7 2021 Because specific AKRs have been linked to NO metabolism in mammals, we expressed and purified A. thaliana AKR4C8 and 9 and close homologs AKR4C10 and 11 and determined that they have NADPH-dependent activity in GSNO and S-nitroso-coenzyme A (SNO-CoA) reduction. S-Nitrosoglutathione 211-215 NAD(P)-linked oxidoreductase superfamily protein Arabidopsis thaliana 138-145 34730552-5 2021 Incubation of Caco-2 cells with all concentrations GSNO for 3 h led to a decrease in the amount of PXR. S-Nitrosoglutathione 51-55 nuclear receptor subfamily 1 group I member 2 Homo sapiens 99-102 34885789-6 2021 The interaction of the expressed Lb with oxidative and nitrosative stress inducers (nitrosoglutathione, tert-butyl hydroperoxide, and benzylviologen) was studied by enzymatic methods and spectrophotometry. S-Nitrosoglutathione 84-102 leghemoglobin A Glycine max 33-35 34730552-6 2021 Incubation with GSNO (1-50 muM) for 24 h was accompanied by an increase in the amount of PXR, while at a concentration of 100 muM this indicator did not significantly differ from the control, at a concentration of 500 muM it was lower. S-Nitrosoglutathione 16-20 nuclear receptor subfamily 1 group I member 2 Homo sapiens 89-92 34730552-7 2021 Prolonged incubation (72 h) enhanced NS and led to a normalization (1 muM GSNO) or a decrease of the PXR level (10-500 muM GSNO). S-Nitrosoglutathione 123-127 nuclear receptor subfamily 1 group I member 2 Homo sapiens 101-104 34730552-8 2021 The induction of PXR by GSNO was mediated by the effect of the nitrosative stress product bityrosine on the transcription factor. S-Nitrosoglutathione 24-28 nuclear receptor subfamily 1 group I member 2 Homo sapiens 17-20 34462873-7 2022 In vitro treatment with ADM or S-Nitrosoglutathione (GSNO) significantly increased the ANX II surface expression, but not its total expression in the JEG-3 cells. S-Nitrosoglutathione 31-51 annexin A2 Homo sapiens 87-93 34573023-7 2021 H2S production by recombinant human CSE was found to be inhibited by the physiological nitrosating agent s-nitrosoglutathione (GSNO), while reduced glutathione had no effect. S-Nitrosoglutathione 105-125 cystathionine gamma-lyase Homo sapiens 36-39 34573023-7 2021 H2S production by recombinant human CSE was found to be inhibited by the physiological nitrosating agent s-nitrosoglutathione (GSNO), while reduced glutathione had no effect. S-Nitrosoglutathione 127-131 cystathionine gamma-lyase Homo sapiens 36-39 34573023-10 2021 By generating conservative Cys-to-Ser variants of the identified s-nitrosated cysteines, Cys137 was identified as most significantly contributing to the GSNO-mediated CSE inhibition. S-Nitrosoglutathione 153-157 cystathionine gamma-lyase Homo sapiens 167-170 34175668-3 2021 Here, we report that S-nitrosoglutathione (GSNO) and GSNO-reductase (GSNOR) inhibitor N6022 drive upregulation of regulatory cytokine (IL-10) and downregulation of pathogenic effector cytokine (IL-6) in B cells and protected against the neuroinflammatory disease of experimental autoimmune encephalomyelitis (EAE). S-Nitrosoglutathione 21-41 interleukin 10 Mus musculus 135-140 34175668-3 2021 Here, we report that S-nitrosoglutathione (GSNO) and GSNO-reductase (GSNOR) inhibitor N6022 drive upregulation of regulatory cytokine (IL-10) and downregulation of pathogenic effector cytokine (IL-6) in B cells and protected against the neuroinflammatory disease of experimental autoimmune encephalomyelitis (EAE). S-Nitrosoglutathione 21-41 interleukin 6 Mus musculus 194-198 34175668-3 2021 Here, we report that S-nitrosoglutathione (GSNO) and GSNO-reductase (GSNOR) inhibitor N6022 drive upregulation of regulatory cytokine (IL-10) and downregulation of pathogenic effector cytokine (IL-6) in B cells and protected against the neuroinflammatory disease of experimental autoimmune encephalomyelitis (EAE). S-Nitrosoglutathione 43-47 interleukin 10 Mus musculus 135-140 34175668-3 2021 Here, we report that S-nitrosoglutathione (GSNO) and GSNO-reductase (GSNOR) inhibitor N6022 drive upregulation of regulatory cytokine (IL-10) and downregulation of pathogenic effector cytokine (IL-6) in B cells and protected against the neuroinflammatory disease of experimental autoimmune encephalomyelitis (EAE). S-Nitrosoglutathione 43-47 interleukin 6 Mus musculus 194-198 34175668-4 2021 In human and mouse B cells, the GSNO/N6022-mediated regulation of IL-10 vs. IL-6 was not limited to regulatory B cells but also to a broad range of B cell subsets and antibody-secreting cells. S-Nitrosoglutathione 32-36 interleukin 10 Mus musculus 66-71 34175668-4 2021 In human and mouse B cells, the GSNO/N6022-mediated regulation of IL-10 vs. IL-6 was not limited to regulatory B cells but also to a broad range of B cell subsets and antibody-secreting cells. S-Nitrosoglutathione 32-36 interleukin 6 Mus musculus 76-80 34175668-6 2021 The data presented here provide evidence of the role of GSNO in shifting B cell immune balance (IL-10 > IL-6) and the preclinical relevance of N6022, a first-in-class drug targeting GSNOR with proven human safety, as therapeutics for autoimmune disorders including multiple sclerosis. S-Nitrosoglutathione 56-60 interleukin 10 Homo sapiens 96-101 34175668-6 2021 The data presented here provide evidence of the role of GSNO in shifting B cell immune balance (IL-10 > IL-6) and the preclinical relevance of N6022, a first-in-class drug targeting GSNOR with proven human safety, as therapeutics for autoimmune disorders including multiple sclerosis. S-Nitrosoglutathione 56-60 interleukin 6 Homo sapiens 104-108 34462873-7 2022 In vitro treatment with ADM or S-Nitrosoglutathione (GSNO) significantly increased the ANX II surface expression, but not its total expression in the JEG-3 cells. S-Nitrosoglutathione 53-57 annexin A2 Homo sapiens 87-93 34416229-8 2021 Mitochondrial Complex I activity normalised to citrate synthase activity was higher after GSNO compared to control (p=0.02), with no difference between low and high dose GSNO. S-Nitrosoglutathione 90-94 citrate synthase Sus scrofa 47-63 35394650-7 2022 Taken together, the present study highlights the role of the GSH-GSNO module in regulating subcellular Fe homeostasis by transcriptional activation of the Fe transporters AtNRAMP3, AtNRAMP4, and AtPIC1 via S-nitrosylation of bHLH TFs during Fe deficiency. S-Nitrosoglutathione 65-69 natural resistance associated macrophage protein 4 Arabidopsis thaliana 181-189 34790975-6 2021 S-nitrosoglutathione (GSNO)-treated iPSCWT and human (h)iPSCs also demonstrated reduced expression of GSK3beta. S-Nitrosoglutathione 0-20 glycogen synthase kinase 3 alpha Homo sapiens 102-110 34790975-6 2021 S-nitrosoglutathione (GSNO)-treated iPSCWT and human (h)iPSCs also demonstrated reduced expression of GSK3beta. S-Nitrosoglutathione 22-26 glycogen synthase kinase 3 alpha Homo sapiens 102-110 35394650-5 2022 Pharmacological experiments, mutant analysis, and promoter assays revealed that this regulation involves the transcriptional activation of Fe transporter genes by a GSH-GSNO module. S-Nitrosoglutathione 169-173 general transcription factor IIE subunit 1 Homo sapiens 139-141 35394650-7 2022 Taken together, the present study highlights the role of the GSH-GSNO module in regulating subcellular Fe homeostasis by transcriptional activation of the Fe transporters AtNRAMP3, AtNRAMP4, and AtPIC1 via S-nitrosylation of bHLH TFs during Fe deficiency. S-Nitrosoglutathione 65-69 general transcription factor IIE subunit 1 Homo sapiens 103-105 34356361-4 2021 Remarkably, the endogenous GSNO level is tightly controlled by S-nitrosoglutathione reductase (GSNOR) that irreversibly inactivates the glutathione-bound NO to ammonium. S-Nitrosoglutathione 27-31 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 95-100 35394650-7 2022 Taken together, the present study highlights the role of the GSH-GSNO module in regulating subcellular Fe homeostasis by transcriptional activation of the Fe transporters AtNRAMP3, AtNRAMP4, and AtPIC1 via S-nitrosylation of bHLH TFs during Fe deficiency. S-Nitrosoglutathione 65-69 translocon at inner membrane of chloroplasts 21 Arabidopsis thaliana 195-201 35394650-7 2022 Taken together, the present study highlights the role of the GSH-GSNO module in regulating subcellular Fe homeostasis by transcriptional activation of the Fe transporters AtNRAMP3, AtNRAMP4, and AtPIC1 via S-nitrosylation of bHLH TFs during Fe deficiency. S-Nitrosoglutathione 65-69 general transcription factor IIE subunit 1 Homo sapiens 155-157 35394650-7 2022 Taken together, the present study highlights the role of the GSH-GSNO module in regulating subcellular Fe homeostasis by transcriptional activation of the Fe transporters AtNRAMP3, AtNRAMP4, and AtPIC1 via S-nitrosylation of bHLH TFs during Fe deficiency. S-Nitrosoglutathione 65-69 natural resistance-associated macrophage protein 3 Arabidopsis thaliana 171-179 35527375-3 2022 The study showed that a short-term exposure to GSNO for 3 h at 500 microM concentration caused increase in the concentration of peroxynitrite in Caco-2 cells, which reduced the activity, but not the amount of Pgp. S-Nitrosoglutathione 47-51 ATP binding cassette subfamily B member 1 Homo sapiens 209-212 35409411-5 2022 Both the pathogen and S-nitrosoglutathione (GSNO) altered the methylation status of H4R3sme2 by transient reduction in the repressive mark in the promoter of defense genes, R3a and HSR203J (a resistance marker), thereby elevating their transcription. S-Nitrosoglutathione 22-42 probable carboxylesterase 15 Solanum tuberosum 181-188 35409411-5 2022 Both the pathogen and S-nitrosoglutathione (GSNO) altered the methylation status of H4R3sme2 by transient reduction in the repressive mark in the promoter of defense genes, R3a and HSR203J (a resistance marker), thereby elevating their transcription. S-Nitrosoglutathione 44-48 probable carboxylesterase 15 Solanum tuberosum 181-188 35624350-3 2022 It was shown that GSNO in concentrations of 10 and 50 muM increased the content and activity of Pgp. S-Nitrosoglutathione 18-22 phosphoglycolate phosphatase Homo sapiens 96-99 35527375-4 2022 Increase in the duration of exposure to 24 h increased the amount and activity of Pgp at GSNO concentrations of 10 and 50 microM, increased the amount without increasing activity at 100 microM concentration, and decreased the amount of the transporter protein at 500 microM. S-Nitrosoglutathione 89-93 ATP binding cassette subfamily B member 1 Homo sapiens 82-85 35527375-5 2022 Duration of exposure to GSNO of 72 h at concentration of 10 microM resulted in the increase of the amount and activity of Pgp, while at concentration of 100 and 500 microM it decreased the amount of the transport protein. S-Nitrosoglutathione 24-28 ATP binding cassette subfamily B member 1 Homo sapiens 122-125 35527375-6 2022 At the same time, it was shown using specific inhibitors that the increase in the amount of Pgp under the influence of low concentrations of GSNO was realized through the NO-cGMP signaling pathway, and the effect of the higher concentration of GSNO and the respective development of nitrosative stress was realized through Nrf2 and the constitutive androstane receptor. S-Nitrosoglutathione 141-145 ATP binding cassette subfamily B member 1 Homo sapiens 92-95 35527375-6 2022 At the same time, it was shown using specific inhibitors that the increase in the amount of Pgp under the influence of low concentrations of GSNO was realized through the NO-cGMP signaling pathway, and the effect of the higher concentration of GSNO and the respective development of nitrosative stress was realized through Nrf2 and the constitutive androstane receptor. S-Nitrosoglutathione 141-145 NFE2 like bZIP transcription factor 2 Homo sapiens 323-327 35527375-6 2022 At the same time, it was shown using specific inhibitors that the increase in the amount of Pgp under the influence of low concentrations of GSNO was realized through the NO-cGMP signaling pathway, and the effect of the higher concentration of GSNO and the respective development of nitrosative stress was realized through Nrf2 and the constitutive androstane receptor. S-Nitrosoglutathione 244-248 ATP binding cassette subfamily B member 1 Homo sapiens 92-95 35527375-6 2022 At the same time, it was shown using specific inhibitors that the increase in the amount of Pgp under the influence of low concentrations of GSNO was realized through the NO-cGMP signaling pathway, and the effect of the higher concentration of GSNO and the respective development of nitrosative stress was realized through Nrf2 and the constitutive androstane receptor. S-Nitrosoglutathione 244-248 NFE2 like bZIP transcription factor 2 Homo sapiens 323-327 35437002-4 2022 Furthermore, we validate that S-nitrosylation of the trihelix transcription factor GT-1 by S-nitrosoglutathione promotes its binding to NO-responsive elements in the HsfA2 promoter and that loss of function of GT-1 disrupts the activation of HsfA2 and heat tolerance, revealing that GT-1 is the long-sought mediator linking signal perception to the activation of cellular heat responses. S-Nitrosoglutathione 91-111 Homeodomain-like superfamily protein Arabidopsis thaliana 83-87 35219905-6 2022 Application of the SP3-Rox method to cellular proteomes identified cysteines sensitive to the oxidative stressor GSNO and cysteine oxidation state changes that occur during T cell activation. S-Nitrosoglutathione 113-117 Sp3 transcription factor Homo sapiens 19-22 35219905-6 2022 Application of the SP3-Rox method to cellular proteomes identified cysteines sensitive to the oxidative stressor GSNO and cysteine oxidation state changes that occur during T cell activation. S-Nitrosoglutathione 113-117 MAX network transcriptional repressor Homo sapiens 23-26 35437002-4 2022 Furthermore, we validate that S-nitrosylation of the trihelix transcription factor GT-1 by S-nitrosoglutathione promotes its binding to NO-responsive elements in the HsfA2 promoter and that loss of function of GT-1 disrupts the activation of HsfA2 and heat tolerance, revealing that GT-1 is the long-sought mediator linking signal perception to the activation of cellular heat responses. S-Nitrosoglutathione 91-111 heat shock transcription factor A2 Arabidopsis thaliana 166-171 35106650-8 2022 Additionally, GSNO or GR24 treatment also up-regulated the expression of SLs synthesis genes (SlCCD7, SlCCD8, SlD27 and SlMAX1) and its signal transduction genes (SlD14 and SlMAX2) in tomato seedlings under salt stress. S-Nitrosoglutathione 14-18 carotenoid cleavage dioxygenase 7 Solanum lycopersicum 94-100 35106650-7 2022 Moreover, GR24 or GSNO treatment effectively increased the content of chlorophyll, carotenoids and ascorbic acid (ASA), and enhanced the activities of antioxidant enzymes (superoxide dismutase, peroxidase, catalase, and ascorbate peroxidase), glutathione reductase (GR) and cleavage dioxygenase (CCD) enzyme. S-Nitrosoglutathione 18-22 iron superoxide dismutase Solanum lycopersicum 172-192 35106650-7 2022 Moreover, GR24 or GSNO treatment effectively increased the content of chlorophyll, carotenoids and ascorbic acid (ASA), and enhanced the activities of antioxidant enzymes (superoxide dismutase, peroxidase, catalase, and ascorbate peroxidase), glutathione reductase (GR) and cleavage dioxygenase (CCD) enzyme. S-Nitrosoglutathione 18-22 peroxidase Solanum lycopersicum 194-204 35106650-7 2022 Moreover, GR24 or GSNO treatment effectively increased the content of chlorophyll, carotenoids and ascorbic acid (ASA), and enhanced the activities of antioxidant enzymes (superoxide dismutase, peroxidase, catalase, and ascorbate peroxidase), glutathione reductase (GR) and cleavage dioxygenase (CCD) enzyme. S-Nitrosoglutathione 18-22 catalase isozyme 1 Solanum lycopersicum 206-214 35106650-7 2022 Moreover, GR24 or GSNO treatment effectively increased the content of chlorophyll, carotenoids and ascorbic acid (ASA), and enhanced the activities of antioxidant enzymes (superoxide dismutase, peroxidase, catalase, and ascorbate peroxidase), glutathione reductase (GR) and cleavage dioxygenase (CCD) enzyme. S-Nitrosoglutathione 18-22 peroxidase Solanum lycopersicum 230-240 35106650-7 2022 Moreover, GR24 or GSNO treatment effectively increased the content of chlorophyll, carotenoids and ascorbic acid (ASA), and enhanced the activities of antioxidant enzymes (superoxide dismutase, peroxidase, catalase, and ascorbate peroxidase), glutathione reductase (GR) and cleavage dioxygenase (CCD) enzyme. S-Nitrosoglutathione 18-22 glutathione reductase Solanum lycopersicum 243-264 35106650-7 2022 Moreover, GR24 or GSNO treatment effectively increased the content of chlorophyll, carotenoids and ascorbic acid (ASA), and enhanced the activities of antioxidant enzymes (superoxide dismutase, peroxidase, catalase, and ascorbate peroxidase), glutathione reductase (GR) and cleavage dioxygenase (CCD) enzyme. S-Nitrosoglutathione 18-22 glutathione reductase Solanum lycopersicum 266-268