Mixed results with mixed disulfides
A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Brigelius-Flohé, Regina [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
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| Schlagwörter: |
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| Umfang: |
7 |
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| Übergeordnetes Werk: |
Enthalten in: Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study - Mohammed Ilyas, M.I. ELSEVIER, 2017, ABB, San Diego, Calif |
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| Übergeordnetes Werk: |
volume:595 ; year:2016 ; day:1 ; month:04 ; pages:81-87 ; extent:7 |
| Links: |
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| DOI / URN: |
10.1016/j.abb.2015.11.011 |
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| 520 | |a A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. | ||
| 520 | |a A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. | ||
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10.1016/j.abb.2015.11.011 doi GBVA2016020000022.pica (DE-627)ELV035575956 (ELSEVIER)S0003-9861(15)00365-3 DE-627 ger DE-627 rakwb eng 500 540 570 500 DE-600 540 DE-600 570 DE-600 610 VZ 610 VZ 44.52 bkl Brigelius-Flohé, Regina verfasserin aut Mixed results with mixed disulfides 2016transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. Mixed disulfides Elsevier Nitrofurantoin Elsevier Glucose-6-phosphate dehydrogenase Elsevier Paraquat Elsevier Glutathionylation Elsevier Protein thiols Elsevier Enthalten in Elsevier Mohammed Ilyas, M.I. ELSEVIER Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study 2017 ABB San Diego, Calif (DE-627)ELV020434308 volume:595 year:2016 day:1 month:04 pages:81-87 extent:7 https://doi.org/10.1016/j.abb.2015.11.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_60 GBV_ILN_72 GBV_ILN_162 44.52 Therapie Medizin VZ AR 595 2016 1 0401 81-87 7 045F 500 |
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10.1016/j.abb.2015.11.011 doi GBVA2016020000022.pica (DE-627)ELV035575956 (ELSEVIER)S0003-9861(15)00365-3 DE-627 ger DE-627 rakwb eng 500 540 570 500 DE-600 540 DE-600 570 DE-600 610 VZ 610 VZ 44.52 bkl Brigelius-Flohé, Regina verfasserin aut Mixed results with mixed disulfides 2016transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. Mixed disulfides Elsevier Nitrofurantoin Elsevier Glucose-6-phosphate dehydrogenase Elsevier Paraquat Elsevier Glutathionylation Elsevier Protein thiols Elsevier Enthalten in Elsevier Mohammed Ilyas, M.I. ELSEVIER Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study 2017 ABB San Diego, Calif (DE-627)ELV020434308 volume:595 year:2016 day:1 month:04 pages:81-87 extent:7 https://doi.org/10.1016/j.abb.2015.11.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_60 GBV_ILN_72 GBV_ILN_162 44.52 Therapie Medizin VZ AR 595 2016 1 0401 81-87 7 045F 500 |
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10.1016/j.abb.2015.11.011 doi GBVA2016020000022.pica (DE-627)ELV035575956 (ELSEVIER)S0003-9861(15)00365-3 DE-627 ger DE-627 rakwb eng 500 540 570 500 DE-600 540 DE-600 570 DE-600 610 VZ 610 VZ 44.52 bkl Brigelius-Flohé, Regina verfasserin aut Mixed results with mixed disulfides 2016transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. Mixed disulfides Elsevier Nitrofurantoin Elsevier Glucose-6-phosphate dehydrogenase Elsevier Paraquat Elsevier Glutathionylation Elsevier Protein thiols Elsevier Enthalten in Elsevier Mohammed Ilyas, M.I. ELSEVIER Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study 2017 ABB San Diego, Calif (DE-627)ELV020434308 volume:595 year:2016 day:1 month:04 pages:81-87 extent:7 https://doi.org/10.1016/j.abb.2015.11.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_60 GBV_ILN_72 GBV_ILN_162 44.52 Therapie Medizin VZ AR 595 2016 1 0401 81-87 7 045F 500 |
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10.1016/j.abb.2015.11.011 doi GBVA2016020000022.pica (DE-627)ELV035575956 (ELSEVIER)S0003-9861(15)00365-3 DE-627 ger DE-627 rakwb eng 500 540 570 500 DE-600 540 DE-600 570 DE-600 610 VZ 610 VZ 44.52 bkl Brigelius-Flohé, Regina verfasserin aut Mixed results with mixed disulfides 2016transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. Mixed disulfides Elsevier Nitrofurantoin Elsevier Glucose-6-phosphate dehydrogenase Elsevier Paraquat Elsevier Glutathionylation Elsevier Protein thiols Elsevier Enthalten in Elsevier Mohammed Ilyas, M.I. ELSEVIER Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study 2017 ABB San Diego, Calif (DE-627)ELV020434308 volume:595 year:2016 day:1 month:04 pages:81-87 extent:7 https://doi.org/10.1016/j.abb.2015.11.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_60 GBV_ILN_72 GBV_ILN_162 44.52 Therapie Medizin VZ AR 595 2016 1 0401 81-87 7 045F 500 |
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10.1016/j.abb.2015.11.011 doi GBVA2016020000022.pica (DE-627)ELV035575956 (ELSEVIER)S0003-9861(15)00365-3 DE-627 ger DE-627 rakwb eng 500 540 570 500 DE-600 540 DE-600 570 DE-600 610 VZ 610 VZ 44.52 bkl Brigelius-Flohé, Regina verfasserin aut Mixed results with mixed disulfides 2016transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. Mixed disulfides Elsevier Nitrofurantoin Elsevier Glucose-6-phosphate dehydrogenase Elsevier Paraquat Elsevier Glutathionylation Elsevier Protein thiols Elsevier Enthalten in Elsevier Mohammed Ilyas, M.I. ELSEVIER Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study 2017 ABB San Diego, Calif (DE-627)ELV020434308 volume:595 year:2016 day:1 month:04 pages:81-87 extent:7 https://doi.org/10.1016/j.abb.2015.11.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_60 GBV_ILN_72 GBV_ILN_162 44.52 Therapie Medizin VZ AR 595 2016 1 0401 81-87 7 045F 500 |
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Enthalten in Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study San Diego, Calif volume:595 year:2016 day:1 month:04 pages:81-87 extent:7 |
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Breast conservation surgery without frozen section study control for intra operative margin status – a prospective study |
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A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. |
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A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. |
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A period of research with Helmut Sies in the 1980s is recalled. Our experiments aimed at an in-depth understanding of metabolic changes due to oxidative challenges under near-physiological conditions, i.e. perfused organs. A major focus were alterations of the glutathione and the NADPH/NADP+ system by different kinds of oxidants, in particular formation of glutathione mixed disulfides with proteins. To analyze mixed disulfides, a test was adapted which is widely used until today. The observations in perfused rat livers let us believe that glutathione-6-phosphate dehydrogenase (G6PDH), i.a. might be activated by glutathionylation. Although we did not succeed to verify this hypothesis for the special case of G6PDH, the regulation of enzyme/protein activities by glutathionylation today is an accepted posttranslational mechanism in redox biology in general. Our early experimental approaches are discussed in the context of present knowledge. |
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