PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 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 33772588-0 2021 Induction of S-nitrosoglutathione reductase protects root growth from ammonium toxicity by regulating potassium homeostasis in Arabidopsis and rice. Ammonium Compounds 70-78 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 13-43 33772588-0 2021 Induction of S-nitrosoglutathione reductase protects root growth from ammonium toxicity by regulating potassium homeostasis in Arabidopsis and rice. Potassium 102-111 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 13-43 33772588-3 2021 Elevated NH4 + also stimulated the accumulation of GSNOR (S-nitrosoglutathione reductase) in roots. nh4 + 9-14 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 51-56 33772588-3 2021 Elevated NH4 + also stimulated the accumulation of GSNOR (S-nitrosoglutathione reductase) in roots. nh4 + 9-14 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 58-88 33772588-4 2021 GSNOR overexpression improved root tolerance to NH4 +. nh4 + 48-53 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-5 33772588-5 2021 Loss of GSNOR further induced NO accumulation, increased SNO1/SOS4 activity, and reduced tissue K + levels, enhancing root growth sensitivity to NH4 +. nh4 + 145-150 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 8-13 33772588-6 2021 Moreover, the GSNOR-like gene, OsGSNOR, is also required for NH4 + tolerance in rice. nh4 + 61-66 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 14-19 33772588-7 2021 Immunoblotting showed that the NH4 +-induced GSNOR protein accumulation was abolished in the VTC1 (Vitamin C 1) defective mutant vtc1-1, which is hypersensititive to NH4 + toxicity. nh4 + 31-36 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 45-50 33772588-7 2021 Immunoblotting showed that the NH4 +-induced GSNOR protein accumulation was abolished in the VTC1 (Vitamin C 1) defective mutant vtc1-1, which is hypersensititive to NH4 + toxicity. vitamin c 1 99-110 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 45-50 34956283-0 2021 Quantitative Proteome Profiling of a S-Nitrosoglutathione Reductase (GSNOR) Null Mutant Reveals a New Class of Enzymes Involved in Nitric Oxide Homeostasis in Plants. Nitric Oxide 131-143 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 37-67 34956283-0 2021 Quantitative Proteome Profiling of a S-Nitrosoglutathione Reductase (GSNOR) Null Mutant Reveals a New Class of Enzymes Involved in Nitric Oxide Homeostasis in Plants. Nitric Oxide 131-143 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 69-74 34956283-3 2021 The enzyme S-nitrosoglutathione reductase (GSNOR) is a major route of NADH-dependent GSNO catabolism and is critical to NO homeostasis. NAD 70-74 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 11-41 34956283-3 2021 The enzyme S-nitrosoglutathione reductase (GSNOR) is a major route of NADH-dependent GSNO catabolism and is critical to NO homeostasis. NAD 70-74 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 43-48 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 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 34956283-9 2021 These data uncover a new, NADPH-dependent component of NO metabolism that may be integrated with NADH-dependent GSNOR activity to control NO homeostasis in plants. NADP 26-31 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 112-117 34956283-9 2021 These data uncover a new, NADPH-dependent component of NO metabolism that may be integrated with NADH-dependent GSNOR activity to control NO homeostasis in plants. NAD 97-101 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 112-117 31467270-7 2019 GSNOR is also required for root tolerance to Fe-toxicity throughout higher plants such as legumes and monocots, which exposes an opportunity to address crop production under high-Fe conditions using natural GSNOR variants. Iron 179-181 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 207-212 33772588-7 2021 Immunoblotting showed that the NH4 +-induced GSNOR protein accumulation was abolished in the VTC1 (Vitamin C 1) defective mutant vtc1-1, which is hypersensititive to NH4 + toxicity. nh4 + 166-171 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 45-50 33772588-8 2021 GSNOR overexpression enhanced vtc1-1 root tolerance to NH4 +. nh4 + 55-60 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-5 33772588-9 2021 The findings suggest that induction of GSNOR increases NH4 + tolerance in Arabidopsis roots by counteracting NO-mediated suppression of tissue K +, which depends on VTC1 function. nh4 + 55-60 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 39-44 34919280-0 2022 ADH2/GSNOR1 is a key player in limiting genotoxic damage mediated by formaldehyde and UV-B in Arabidopsis. Formaldehyde 69-81 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-4 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-hydroxymethylglutathione 76-102 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-hydroxymethylglutathione 104-107 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 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. Formaldehyde 259-271 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 34919280-5 2022 Our results demonstrate an interplay between formaldehyde and UV-B that exacerbates genome instability, leading to severe DNA damage and impaired growth and development in Arabidopsis, and show that ADH2/GSNOR1 is a key player in combating these effects. Formaldehyde 45-57 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 199-203 31340034-5 2019 In WT and 35S::FLAG-GSNOR1, GSNOR was inactivated by Zn, and Zn-induced H2O2 is directly involved in the GSNOR activity loss. Zinc 53-55 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 28-33 31340034-5 2019 In WT and 35S::FLAG-GSNOR1, GSNOR was inactivated by Zn, and Zn-induced H2O2 is directly involved in the GSNOR activity loss. Zinc 61-63 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 20-25 31340034-8 2019 Our data collectively show that Zn-induced H2O2 may influence its own level, which involves GSNOR inactivation-triggered SNO signaling. Zinc 32-34 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 92-97 31340034-8 2019 Our data collectively show that Zn-induced H2O2 may influence its own level, which involves GSNOR inactivation-triggered SNO signaling. Hydrogen Peroxide 43-47 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 92-97 31467270-0 2019 GSNOR provides plant tolerance to iron toxicity via preventing iron-dependent nitrosative and oxidative cytotoxicity. Iron 34-38 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-5 31467270-0 2019 GSNOR provides plant tolerance to iron toxicity via preventing iron-dependent nitrosative and oxidative cytotoxicity. Iron 63-67 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-5 31467270-3 2019 Here, we identify S-nitrosoglutathione-reductase (GSNOR) variants underlying a major quantitative locus for root tolerance to Fe-toxicity in Arabidopsis using genome-wide association studies and allelic complementation. Iron 126-128 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 50-55 31467270-6 2019 GSNOR maintains root meristem activity and prevents cell death via inhibiting Fe-dependent nitrosative and oxidative cytotoxicity. Iron 78-80 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-5 31467270-7 2019 GSNOR is also required for root tolerance to Fe-toxicity throughout higher plants such as legumes and monocots, which exposes an opportunity to address crop production under high-Fe conditions using natural GSNOR variants. Iron 45-47 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-5 31467270-7 2019 GSNOR is also required for root tolerance to Fe-toxicity throughout higher plants such as legumes and monocots, which exposes an opportunity to address crop production under high-Fe conditions using natural GSNOR variants. Iron 45-47 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 207-212 31467270-7 2019 GSNOR is also required for root tolerance to Fe-toxicity throughout higher plants such as legumes and monocots, which exposes an opportunity to address crop production under high-Fe conditions using natural GSNOR variants. Iron 179-181 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-5 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 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). 1,1"-dimethyl-4,4"-bipyridinium dichloride 163-205 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 4-10 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). 1,1"-dimethyl-4,4"-bipyridinium dichloride 163-205 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 35-41 31245758-7 2019 By enriching glycoproteins in gsnor1-3 and mass spectrometry analysis, TGG2 (thioglucoside glucohydrolase2) was identified as one of co-substrates with high degradation rate and elevated N-glycosylation level in gsnor1-3 ost3/6. Nitrogen 187-188 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 30-36 31245758-8 2019 The S-nitrosylation and N-glycosylation profiles were also modified in dgl1-3 and gsnor1-3. Nitrogen 24-25 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 82-88 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 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 30254659-10 2018 Additionally, Fe-sufficient opt3-2 roots had higher "ethylene" and "GSNOR" than Fe-sufficient WT Columbia roots. Iron 14-16 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 68-73 30254659-11 2018 The increase of both "ethylene" and "GSNOR" was not related to the total root Fe content but to the absence of a Fe shoot signal (LODIS), and was associated with the up-regulation of Fe acquisition genes. Iron 78-80 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 37-42 30254659-12 2018 The possible relationship between GSNOR(GSNO) and ethylene is discussed. ethylene 50-58 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 34-39 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 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 27684709-7 2016 Overexpression of GSNOR intensified the salt sensitivity of cam4 mutant plants accompanied by a reduced internal NO level, whereas a gsnor deficiency increased the salt tolerance of cam4 plants accompanied by an increased internal NO level. Salts 40-44 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 18-23 27684709-7 2016 Overexpression of GSNOR intensified the salt sensitivity of cam4 mutant plants accompanied by a reduced internal NO level, whereas a gsnor deficiency increased the salt tolerance of cam4 plants accompanied by an increased internal NO level. Salts 164-168 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 133-138 27684709-8 2016 Physiological experiments showed that CaM4-GSNOR, acting through NO, reestablished the ion balance to increase plant resistance to salt stress. Salts 131-135 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 43-48 27891135-6 2016 Here we report that Arabidopsis thaliana GSNOR activity is reversibly inhibited by H2O2in vitro and by paraquat-induced oxidative stress in vivo. Hydrogen Peroxide 83-87 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 41-46 27891135-6 2016 Here we report that Arabidopsis thaliana GSNOR activity is reversibly inhibited by H2O2in vitro and by paraquat-induced oxidative stress in vivo. Paraquat 103-111 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 41-46 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 22767201-3 2012 An ARABIDOPSIS THALIANA S-NITROSOGLUTATHIONE (GSNO) REDUCTASE (AtGSNOR1) is thought to be the major regulator of total cellular SNO levels in this plant species. S-Nitrosothiols 71-74 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 87-95 24204370-1 2013 S-nitrosoglutathione reductase (GSNOR) is believed to modulate effects of reactive oxygen and nitrogen species through catabolism of S-nitrosoglutathione (GSNO). reactive oxygen and nitrogen species 74-110 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 0-30 24204370-1 2013 S-nitrosoglutathione reductase (GSNOR) is believed to modulate effects of reactive oxygen and nitrogen species through catabolism of S-nitrosoglutathione (GSNO). reactive oxygen and nitrogen species 74-110 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 32-37 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 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 24204370-9 2013 Six members of the plant specific, ROXY glutaredoxins and three BHLH transcription factors involved in iron homeostasis were strongly upregulated, supporting a role for GSNOR in redox and iron metabolism. Iron 103-107 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 169-174 24204370-9 2013 Six members of the plant specific, ROXY glutaredoxins and three BHLH transcription factors involved in iron homeostasis were strongly upregulated, supporting a role for GSNOR in redox and iron metabolism. Iron 188-192 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 169-174 23201478-1 2013 The enzyme S-nitrosoglutathione reductase (GSNOR) has an important role in the metabolism of S-nitrosothiols (SNO) and, consequently, in the modulation of nitric oxide (NO)-mediated processes. S-Nitrosothiols 93-108 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 43-48 23201478-1 2013 The enzyme S-nitrosoglutathione reductase (GSNOR) has an important role in the metabolism of S-nitrosothiols (SNO) and, consequently, in the modulation of nitric oxide (NO)-mediated processes. Nitric Oxide 155-167 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 43-48 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 23201478-7 2013 Analysis of oxygen uptake by isolated mitochondria showed that complex I and external NADH dehydrogenase activities were inhibited in GSNOR(OE) cells grown under nutritional stress. Oxygen 12-18 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 134-139 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 22504427-6 2012 Our results indicate that 500 muM arsenate (AsV) causes nitro-oxidative stress in Arabidopsis, being the glutathione reductase and the GSNOR activities clearly affected. arsenic acid 34-42 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 135-140 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 22371078-6 2012 Furthermore, extending previous work on the role of GSNOR in pathogenesis, it was shown that GSNO acts synergistically with salicylic acid in systemic acquired resistance activation. Salicylic Acid 124-138 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 52-57 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 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). Nitric Oxide 71-83 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). Nitric Oxide 71-83 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 158-163 19806166-2 2009 Previous studies showed that the Arabidopsis GSNOR1/HOT5 gene regulates salicylic acid signaling and thermotolerance by modulating the intracellular S-nitrosothiol level. Salicylic Acid 72-86 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 52-56 19806166-2 2009 Previous studies showed that the Arabidopsis GSNOR1/HOT5 gene regulates salicylic acid signaling and thermotolerance by modulating the intracellular S-nitrosothiol level. S-Nitrosothiols 149-163 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 52-56 17087482-1 2006 Glutathione (GSH)-dependent formaldehyde dehydrogenase (FALDH) is a highly conserved medium-chain dehydrogenase reductase and the main enzyme that metabolizes intracellular formaldehyde in eukaryotes. Glutathione 0-11 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 56-61 17087482-1 2006 Glutathione (GSH)-dependent formaldehyde dehydrogenase (FALDH) is a highly conserved medium-chain dehydrogenase reductase and the main enzyme that metabolizes intracellular formaldehyde in eukaryotes. Glutathione 13-16 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 56-61 17087482-1 2006 Glutathione (GSH)-dependent formaldehyde dehydrogenase (FALDH) is a highly conserved medium-chain dehydrogenase reductase and the main enzyme that metabolizes intracellular formaldehyde in eukaryotes. Formaldehyde 28-40 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 56-61 17087482-7 2006 Arabidopsis thaliana mutants with modified levels of FALDH (both by over- and under-expression of the FALDH-encoding gene) show a significant reduction of root length, and this phenotype correlates with an overall decrease of intracellular GSH levels and alteration of spatial distribution of GSH in the root meristem. Glutathione 240-243 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 53-58 17087482-7 2006 Arabidopsis thaliana mutants with modified levels of FALDH (both by over- and under-expression of the FALDH-encoding gene) show a significant reduction of root length, and this phenotype correlates with an overall decrease of intracellular GSH levels and alteration of spatial distribution of GSH in the root meristem. Glutathione 240-243 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 102-121 17087482-7 2006 Arabidopsis thaliana mutants with modified levels of FALDH (both by over- and under-expression of the FALDH-encoding gene) show a significant reduction of root length, and this phenotype correlates with an overall decrease of intracellular GSH levels and alteration of spatial distribution of GSH in the root meristem. Glutathione 293-296 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 53-58 17087482-7 2006 Arabidopsis thaliana mutants with modified levels of FALDH (both by over- and under-expression of the FALDH-encoding gene) show a significant reduction of root length, and this phenotype correlates with an overall decrease of intracellular GSH levels and alteration of spatial distribution of GSH in the root meristem. Glutathione 293-296 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 102-121 15911759-2 2005 Mutations in AtGSNOR1, an Arabidopsis thaliana GSNOR, modulate the extent of cellular S-nitrosothiol (SNO) formation in this model plant species. S-Nitrosothiols 86-100 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 13-21 15911759-6 2005 Here we demonstrate that AtGSNOR1 positively regulates the signaling network controlled by the plant immune system activator, salicylic acid. Salicylic Acid 126-140 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 25-33 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 18326829-8 2008 The hot5 null alleles show increased nitrate and nitroso species levels, and the heat sensitivity of both missense and null alleles is associated with increased NO species. Nitrates 37-44 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 4-8 18326829-8 2008 The hot5 null alleles show increased nitrate and nitroso species levels, and the heat sensitivity of both missense and null alleles is associated with increased NO species. nitroso 49-56 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 4-8 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 17277089-7 2007 Our data corroborate the data from other authors that GSNOR controls SNO in vivo levels, and shows that SNO content positively influences plant basal resistance and resistance-gene-mediated resistance as well. S-Nitrosothiols 69-72 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 54-59 12913179-0 2003 Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis. Formaldehyde 9-21 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 80-106 12913179-0 2003 Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis. Glutathione 58-69 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 80-106 12913179-1 2003 The ADH2 gene codes for the Arabidopsis glutathione-dependent formaldehyde dehydrogenase (FALDH), an enzyme involved in formaldehyde metabolism in eukaryotes. Formaldehyde 62-74 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 4-8 12913179-1 2003 The ADH2 gene codes for the Arabidopsis glutathione-dependent formaldehyde dehydrogenase (FALDH), an enzyme involved in formaldehyde metabolism in eukaryotes. Formaldehyde 62-74 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 90-95 12913179-2 2003 In the present work, we have investigated the potential role of FALDH in detoxification of exogenous formaldehyde. Formaldehyde 101-113 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 64-69 12913179-4 2003 Overexpression of Arabidopsis FALDH in this mutant confers high resistance to formaldehyde added exogenously, which demonstrates the functional conservation of the enzyme through evolution and supports its essential role in formaldehyde metabolism. Formaldehyde 78-90 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 30-35 12913179-4 2003 Overexpression of Arabidopsis FALDH in this mutant confers high resistance to formaldehyde added exogenously, which demonstrates the functional conservation of the enzyme through evolution and supports its essential role in formaldehyde metabolism. Formaldehyde 224-236 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 30-35 12913179-6 2003 Plants overexpressing the enzyme show a 25% increase in their efficiency to take up exogenous formaldehyde, whereas plants with reduced levels of FALDH (due to either a cosuppression phenotype or to the expression of an antisense construct) show a marked slower rate and reduced ability for formaldehyde detoxification as compared with the wild-type Arabidopsis. Formaldehyde 291-303 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 146-151 12913179-7 2003 These results show that the capacity to take up and detoxify high concentrations of formaldehyde is proportionally related to the FALDH activity in the plant, revealing the essential role of this enzyme in formaldehyde detoxification. Formaldehyde 84-96 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 130-135 12913179-7 2003 These results show that the capacity to take up and detoxify high concentrations of formaldehyde is proportionally related to the FALDH activity in the plant, revealing the essential role of this enzyme in formaldehyde detoxification. Formaldehyde 206-218 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 130-135 12753920-4 2003 Our results show that the gene encoding FALDH in Arabidopsis (ADH2) is down-regulated by wounding and activated by salicylic acid (SA). Salicylic Acid 115-129 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 40-45 12753920-4 2003 Our results show that the gene encoding FALDH in Arabidopsis (ADH2) is down-regulated by wounding and activated by salicylic acid (SA). Salicylic Acid 115-129 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 62-66 12753920-4 2003 Our results show that the gene encoding FALDH in Arabidopsis (ADH2) is down-regulated by wounding and activated by salicylic acid (SA). Salicylic Acid 131-133 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 40-45 12753920-4 2003 Our results show that the gene encoding FALDH in Arabidopsis (ADH2) is down-regulated by wounding and activated by salicylic acid (SA). Salicylic Acid 131-133 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 62-66 12753920-5 2003 In tobacco, FALDH levels and enzymatic activity decreased after jasmonate treatment, and increased in response to SA. Salicylic Acid 114-116 GroES-like zinc-binding dehydrogenase family protein Arabidopsis thaliana 12-17