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Redox conditions in selected principal aquifers of the United States [[electronic resource] /] / [McMahon, P.B. ... and others]
| Redox conditions in selected principal aquifers of the United States [[electronic resource] /] / [McMahon, P.B. ... and others] |
| Pubbl/distr/stampa | [Reston, Va.] : , : U.S. Dept. of the Interior, U.S. Geological Survey, , [2009] |
| Descrizione fisica | 6 pages : $b digital, PDF file |
| Altri autori (Persone) | McMahonPeter B |
| Collana | Fact sheet |
| Soggetto topico |
Groundwater - Quality - Oxidation - United States
Oxidation-reduction reaction |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910698906603321 |
| [Reston, Va.] : , : U.S. Dept. of the Interior, U.S. Geological Survey, , [2009] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Redox proteomics [[electronic resource] ] : from protein modifications to cellular dysfunction and diseases / / edited by Isabella Dalle-Donne, Andrea Scaloni, and D. Allan Butterfield
| Redox proteomics [[electronic resource] ] : from protein modifications to cellular dysfunction and diseases / / edited by Isabella Dalle-Donne, Andrea Scaloni, and D. Allan Butterfield |
| Pubbl/distr/stampa | Hoboken, N.J., : Wiley-Interscience, c2006 |
| Descrizione fisica | 1 online resource (978 p.) |
| Disciplina |
572.6
612.3/98 |
| Altri autori (Persone) |
Dalle-DonneIsabella <1964->
ScaloniAndrea ButterfieldD. Allan |
| Collana | Wiley-interscience series in mass spectrometry |
| Soggetto topico |
Proteomics
Oxidation-reduction reaction Pathology, Cellular Proteins Genomics |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-45036-3
9786610450367 0-470-32490-2 0-471-97312-2 0-471-97311-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
REDOX PROTEOMICS; CONTENTS; Preface; Contributors; PART I OXIDATIVELY MODIFIED PROTEINS AND PROTEOMIC TECHNOLOGIES; 1 Chemical Modification of Proteins by Reactive Oxygen Species; 1.1 Introduction; 1.2 Peptide Bond Cleavage; 1.3 b-Scission; 1.4 Oxidation of Amino Acid Residue Side Chains; 1.4.1 Oxidation of Aromatic and Heterocyclic Amino Acid Residues; 1.4.2 Methionine Oxidation; 1.4.3 Protein Carbonylation; 1.4.4 Protein-Protein Cross-Linkage; 1.4.5 Protein Modification by Reactive Nitrogen Species; 1.4.6 Chlorination Reactions; 1.4.7 Accumulation of Oxidized Proteins
2 The Chemistry of Protein Modifications Elicited by Nitric Oxide and Related Nitrogen Oxides2.1 Introduction; 2.2 Chemical Biology of NO; 2.2.1 Direct Effects; 2.2.2 Indirect Mechanisms; 2.3 Chemistry of Metabolite Formation; 2.3.1 Nitrite and Nitrate Formation; 2.3.2 Metal Nitrosyl Formation; 2.3.3 Nitrosation; 2.3.4 Nitration; 3 Mass Spectrometry Approaches for the Molecular Characterization of Oxidatively/Nitrosatively Modified Proteins; 3.1 Introduction; 3.2 Mass Spectrometry Analysis of Oxidatively/Nitrosatively Modified Proteins 3.2.1 Analysis of Oxidized/Nitrosated Products of Protein Thiols3.2.2 Analysis of Oxidized/Nitrated Products of Tyrosine; 3.2.3 Analysis of Oxidized Products of Methionine; 3.2.4 Analysis of Protein Carbonylation Products; 3.2.5 Analysis of Oxidatively/Nitr(os)atively Products of Tryptophan and Histidine; 3.3 Proteomic Strategies for the Identification of ROS/RNS Protein Targets in Biological Matrices; 3.4 Conclusions; 4 Thiol-Disulfide Oxidoreduction of Protein Cysteines: Old Methods Revisited for Proteomics; 4.1 Introduction: Protein Thiols from Oxidative Stress to Redox Regulation 4.2 Different Redox States of Protein Cysteines4.2.1 Disulfides; 4.2.2 Mixed Disulfides; 4.2.3 Higher Oxidation States; 4.3 Methodologies to Identify and Quantify the Redox State of Protein Cysteines; 4.3.1 Methods Based on Reagents That Label Free Cysteine; 4.3.2 Methods Based on Different Electrophoretic Mobility: Diagonal Electrophoresis; 4.4 Methods to Detect Specific Modifications; 4.4.1 Methods Based on a Series of Alkylation, Reduction, and Labeling Steps; 4.4.2 Methods Based on Incorporation of Labeled Glutathione to Identify Glutathionylated Proteins; 4.4.3 Immunological Methods 4.5 Methods for Enriching Redox-Regulated Proteins4.5.1 Enrichment of Proteins with Specific Forms of Cysteine Oxidation; 4.5.2 Membrane Proteins; 4.6 Structural and Physicochemical Determinants for the Susceptibility of Cysteines toward Oxidation; 4.7 Perspective; 5 Carbonylated Proteins and Their Implication in Physiology and Pathology; 5.1 Introduction; 5.2 Types of Oxidative Modifications and Choice of Marker; 5.3 Methodological Considerations; 5.4 Selected Studies; 5.5 Carbonylation during Aging; 6 S-Nitrosation of Cysteine Thiols as a Redox Signal; 6.1 Introduction 6.2 Mechanisms of Formation of S-Nitrosothiols |
| Record Nr. | UNINA-9910143394503321 |
| Hoboken, N.J., : Wiley-Interscience, c2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Redox proteomics [[electronic resource] ] : from protein modifications to cellular dysfunction and diseases / / edited by Isabella Dalle-Donne, Andrea Scaloni, and D. Allan Butterfield
| Redox proteomics [[electronic resource] ] : from protein modifications to cellular dysfunction and diseases / / edited by Isabella Dalle-Donne, Andrea Scaloni, and D. Allan Butterfield |
| Pubbl/distr/stampa | Hoboken, N.J., : Wiley-Interscience, c2006 |
| Descrizione fisica | 1 online resource (978 p.) |
| Disciplina |
572.6
612.3/98 |
| Altri autori (Persone) |
Dalle-DonneIsabella <1964->
ScaloniAndrea ButterfieldD. Allan |
| Collana | Wiley-interscience series in mass spectrometry |
| Soggetto topico |
Proteomics
Oxidation-reduction reaction Pathology, Cellular Proteins Genomics |
| ISBN |
1-280-45036-3
9786610450367 0-470-32490-2 0-471-97312-2 0-471-97311-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
REDOX PROTEOMICS; CONTENTS; Preface; Contributors; PART I OXIDATIVELY MODIFIED PROTEINS AND PROTEOMIC TECHNOLOGIES; 1 Chemical Modification of Proteins by Reactive Oxygen Species; 1.1 Introduction; 1.2 Peptide Bond Cleavage; 1.3 b-Scission; 1.4 Oxidation of Amino Acid Residue Side Chains; 1.4.1 Oxidation of Aromatic and Heterocyclic Amino Acid Residues; 1.4.2 Methionine Oxidation; 1.4.3 Protein Carbonylation; 1.4.4 Protein-Protein Cross-Linkage; 1.4.5 Protein Modification by Reactive Nitrogen Species; 1.4.6 Chlorination Reactions; 1.4.7 Accumulation of Oxidized Proteins
2 The Chemistry of Protein Modifications Elicited by Nitric Oxide and Related Nitrogen Oxides2.1 Introduction; 2.2 Chemical Biology of NO; 2.2.1 Direct Effects; 2.2.2 Indirect Mechanisms; 2.3 Chemistry of Metabolite Formation; 2.3.1 Nitrite and Nitrate Formation; 2.3.2 Metal Nitrosyl Formation; 2.3.3 Nitrosation; 2.3.4 Nitration; 3 Mass Spectrometry Approaches for the Molecular Characterization of Oxidatively/Nitrosatively Modified Proteins; 3.1 Introduction; 3.2 Mass Spectrometry Analysis of Oxidatively/Nitrosatively Modified Proteins 3.2.1 Analysis of Oxidized/Nitrosated Products of Protein Thiols3.2.2 Analysis of Oxidized/Nitrated Products of Tyrosine; 3.2.3 Analysis of Oxidized Products of Methionine; 3.2.4 Analysis of Protein Carbonylation Products; 3.2.5 Analysis of Oxidatively/Nitr(os)atively Products of Tryptophan and Histidine; 3.3 Proteomic Strategies for the Identification of ROS/RNS Protein Targets in Biological Matrices; 3.4 Conclusions; 4 Thiol-Disulfide Oxidoreduction of Protein Cysteines: Old Methods Revisited for Proteomics; 4.1 Introduction: Protein Thiols from Oxidative Stress to Redox Regulation 4.2 Different Redox States of Protein Cysteines4.2.1 Disulfides; 4.2.2 Mixed Disulfides; 4.2.3 Higher Oxidation States; 4.3 Methodologies to Identify and Quantify the Redox State of Protein Cysteines; 4.3.1 Methods Based on Reagents That Label Free Cysteine; 4.3.2 Methods Based on Different Electrophoretic Mobility: Diagonal Electrophoresis; 4.4 Methods to Detect Specific Modifications; 4.4.1 Methods Based on a Series of Alkylation, Reduction, and Labeling Steps; 4.4.2 Methods Based on Incorporation of Labeled Glutathione to Identify Glutathionylated Proteins; 4.4.3 Immunological Methods 4.5 Methods for Enriching Redox-Regulated Proteins4.5.1 Enrichment of Proteins with Specific Forms of Cysteine Oxidation; 4.5.2 Membrane Proteins; 4.6 Structural and Physicochemical Determinants for the Susceptibility of Cysteines toward Oxidation; 4.7 Perspective; 5 Carbonylated Proteins and Their Implication in Physiology and Pathology; 5.1 Introduction; 5.2 Types of Oxidative Modifications and Choice of Marker; 5.3 Methodological Considerations; 5.4 Selected Studies; 5.5 Carbonylation during Aging; 6 S-Nitrosation of Cysteine Thiols as a Redox Signal; 6.1 Introduction 6.2 Mechanisms of Formation of S-Nitrosothiols |
| Record Nr. | UNINA-9910830092103321 |
| Hoboken, N.J., : Wiley-Interscience, c2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Redox proteomics : from protein modifications to cellular dysfunction and diseases / / edited by Isabella Dalle-Donne, Andrea Scaloni, and D. Allan Butterfield
| Redox proteomics : from protein modifications to cellular dysfunction and diseases / / edited by Isabella Dalle-Donne, Andrea Scaloni, and D. Allan Butterfield |
| Pubbl/distr/stampa | Hoboken, N.J., : Wiley-Interscience, c2006 |
| Descrizione fisica | 1 online resource (978 p.) |
| Disciplina | 612.3/98 |
| Altri autori (Persone) |
Dalle-DonneIsabella <1964->
ScaloniAndrea ButterfieldD. Allan |
| Collana | Wiley-interscience series in mass spectrometry |
| Soggetto topico |
Proteomics
Oxidation-reduction reaction Pathology, Cellular Proteins Genomics |
| ISBN |
1-280-45036-3
9786610450367 0-470-32490-2 0-471-97312-2 0-471-97311-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
REDOX PROTEOMICS; CONTENTS; Preface; Contributors; PART I OXIDATIVELY MODIFIED PROTEINS AND PROTEOMIC TECHNOLOGIES; 1 Chemical Modification of Proteins by Reactive Oxygen Species; 1.1 Introduction; 1.2 Peptide Bond Cleavage; 1.3 b-Scission; 1.4 Oxidation of Amino Acid Residue Side Chains; 1.4.1 Oxidation of Aromatic and Heterocyclic Amino Acid Residues; 1.4.2 Methionine Oxidation; 1.4.3 Protein Carbonylation; 1.4.4 Protein-Protein Cross-Linkage; 1.4.5 Protein Modification by Reactive Nitrogen Species; 1.4.6 Chlorination Reactions; 1.4.7 Accumulation of Oxidized Proteins
2 The Chemistry of Protein Modifications Elicited by Nitric Oxide and Related Nitrogen Oxides2.1 Introduction; 2.2 Chemical Biology of NO; 2.2.1 Direct Effects; 2.2.2 Indirect Mechanisms; 2.3 Chemistry of Metabolite Formation; 2.3.1 Nitrite and Nitrate Formation; 2.3.2 Metal Nitrosyl Formation; 2.3.3 Nitrosation; 2.3.4 Nitration; 3 Mass Spectrometry Approaches for the Molecular Characterization of Oxidatively/Nitrosatively Modified Proteins; 3.1 Introduction; 3.2 Mass Spectrometry Analysis of Oxidatively/Nitrosatively Modified Proteins 3.2.1 Analysis of Oxidized/Nitrosated Products of Protein Thiols3.2.2 Analysis of Oxidized/Nitrated Products of Tyrosine; 3.2.3 Analysis of Oxidized Products of Methionine; 3.2.4 Analysis of Protein Carbonylation Products; 3.2.5 Analysis of Oxidatively/Nitr(os)atively Products of Tryptophan and Histidine; 3.3 Proteomic Strategies for the Identification of ROS/RNS Protein Targets in Biological Matrices; 3.4 Conclusions; 4 Thiol-Disulfide Oxidoreduction of Protein Cysteines: Old Methods Revisited for Proteomics; 4.1 Introduction: Protein Thiols from Oxidative Stress to Redox Regulation 4.2 Different Redox States of Protein Cysteines4.2.1 Disulfides; 4.2.2 Mixed Disulfides; 4.2.3 Higher Oxidation States; 4.3 Methodologies to Identify and Quantify the Redox State of Protein Cysteines; 4.3.1 Methods Based on Reagents That Label Free Cysteine; 4.3.2 Methods Based on Different Electrophoretic Mobility: Diagonal Electrophoresis; 4.4 Methods to Detect Specific Modifications; 4.4.1 Methods Based on a Series of Alkylation, Reduction, and Labeling Steps; 4.4.2 Methods Based on Incorporation of Labeled Glutathione to Identify Glutathionylated Proteins; 4.4.3 Immunological Methods 4.5 Methods for Enriching Redox-Regulated Proteins4.5.1 Enrichment of Proteins with Specific Forms of Cysteine Oxidation; 4.5.2 Membrane Proteins; 4.6 Structural and Physicochemical Determinants for the Susceptibility of Cysteines toward Oxidation; 4.7 Perspective; 5 Carbonylated Proteins and Their Implication in Physiology and Pathology; 5.1 Introduction; 5.2 Types of Oxidative Modifications and Choice of Marker; 5.3 Methodological Considerations; 5.4 Selected Studies; 5.5 Carbonylation during Aging; 6 S-Nitrosation of Cysteine Thiols as a Redox Signal; 6.1 Introduction 6.2 Mechanisms of Formation of S-Nitrosothiols |
| Record Nr. | UNINA-9910877134303321 |
| Hoboken, N.J., : Wiley-Interscience, c2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Redox signaling and biomarkers in ageing / / edited by Ufuk Çakatay
| Redox signaling and biomarkers in ageing / / edited by Ufuk Çakatay |
| Pubbl/distr/stampa | Cham, Switzerland : , : Springer, , [2022] |
| Descrizione fisica | 1 online resource (447 pages) |
| Disciplina | 571.878 |
| Collana | Healthy Ageing and Longevity |
| Soggetto topico |
Biochemical markers
Oxidation-reduction reaction Aging - Molecular aspects |
| ISBN |
9783030849658
9783030849641 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910523764103321 |
| Cham, Switzerland : , : Springer, , [2022] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Redox signaling and regulation in biology and medicine [[electronic resource] /] / edited by Claus Jacob, Paul G. Winyard
| Redox signaling and regulation in biology and medicine [[electronic resource] /] / edited by Claus Jacob, Paul G. Winyard |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2009 |
| Descrizione fisica | 1 online resource (517 p.) |
| Disciplina | 541.393 |
| Altri autori (Persone) |
JacobClaus
WinyardPaul G. <1959-> |
| Soggetto topico |
Oxidation-reduction reaction
Cellular signal transduction |
| ISBN |
1-282-29206-4
9786612292064 3-527-62758-8 3-527-62759-6 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Redox Signaling and Regulation in Biology and Medicine; Contents; Preface; The Editors; List of Authors; 1 Introduction; 2 Biological Systems Relevant for Redox Signaling and Control; 2.1 Introduction; 2.2 Reactive Oxygen Species; 2.2.1 The Superoxide Radical; 2.2.1.1 Generation of the Superoxide Radical; 2.2.1.2 The Superoxide Radical as a Redox Signal; 2.2.1.3 Decomposition of the Superoxide Radical; 2.2.2 Hydrogen Peroxide; 2.2.2.1 Generation of Hydrogen Peroxide; 2.2.2.2 Mechanisms of Hydrogen Peroxide Signaling; 2.2.2.3 Decomposition of Hydrogen Peroxide; 2.3 Reactive Nitrogen Species
2.3.1 Nitric Oxide2.3.1.1 Generation of Nitric Oxide; 2.3.1.2 Mechanisms of Nitric Oxide Signaling; 2.3.1.3 Decomposition of Nitric Oxide; 2.3.2 Peroxynitrite and Reactive Nitrogen Species; 2.3.2.1 Generation of Peroxynitrite and Other Important Reactive Nitrogen Species; 2.3.2.2 Mechanisms of Peroxynitrite- and Reactive Nitrogen Species-Mediated Redox Signaling; 2.4 Lipid Peroxidation Products; 2.4.1 Generation of Lipid Peroxidation Products; 2.4.2 Mechanisms of Signaling with Lipid Peroxidation Products; 2.4.3 Decomposition of Lipid Peroxides; 2.5 Conclusions; References 3 Cellular Generation of Oxidants: Relation to Oxidative Stress3.1 Introduction; 3.2 Molecular Oxygen and Reactive Oxygen Species: Biochemical Relations and Endogenous Sources; 3.2.1 Endogenous Sources of Superoxide and Superoxide-Derived Reactive Oxygen Species; 3.2.2 Singlet Oxygen; 3.2.3 ""Secondary"" Reactive Oxygen Species Generated in Radical Chain Reactions; 3.3 Generation of Oxidative Stress Under the Influence of Xenobiotics and Stressful Stimuli; 3.3.1 Quinones and Other Redox Cyclers; 3.3.2 Antioxidant Depletion by Alkylation: Acetaminophen Toxicity; 3.3.3 Ultraviolet Radiation 3.3.4 Ultrafine or NanoparticlesReferences; 4 The Chemical Basis of Biological Redox Control; 4.1 Introduction; 4.2 Forms of Elemental Oxygen as Reactive Oxygen Species; 4.2.1 Reactive Oxygen Species and Related Cellular Oxidants; 4.2.2 Singlet Oxygen (1O2); 4.2.3 Ozone (O3); 4.3 Reduced, Yet Oxidizing: the Chemistry of Oxygen in Oxidation States between 0 and -2; 4.3.1 Superoxide Radicals (O2 ̇ ̄ ); 4.3.2 The Superoxide to Peroxide Conversion as a Key Event in Redox Signaling; 4.3.3 Hydrogen Peroxide (H2O2); 4.3.4 Hydroxyl Radicals (HO·) 4.3.5 Enzymatic Reduction of Hydrogen Peroxide by Peroxiredoxins, Catalase and Glutathione Peroxidase4.4 The Role of Labile Metal Ions in Oxidative Stress; 4.5 Follow-on Species Generated by Chemical Interactions of Reactive Oxygen Species; 4.5.1 Hypochlorous Acid (HOCl); 4.5.2 Peroxynitrite (ONOO ̄ ); 4.6 Nitrogen Monoxide and Reactive Nitrogen Species; 4.6.1 Reactive Nitrogen Species; 4.6.2 S-Nitrosothiols; 4.7 Sulfur as a Prime Target of Oxidative Stress; 4.7.1 Thiol Groups in Peptides and Proteins; 4.7.2 The Concept of Reactive Sulfur Species; 4.7.3 Sulfur-Centered Radicals 4.7.4 Disulfide-S-Oxides (RS(O)xSR') |
| Record Nr. | UNINA-9910143128903321 |
| Weinheim, : Wiley-VCH, c2009 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Redox signaling and regulation in biology and medicine / / edited by Claus Jacob, Paul G. Winyard
| Redox signaling and regulation in biology and medicine / / edited by Claus Jacob, Paul G. Winyard |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2009 |
| Descrizione fisica | 1 online resource (517 p.) |
| Disciplina | 541.393 |
| Altri autori (Persone) |
JacobClaus
WinyardPaul G. <1959-> |
| Soggetto topico |
Oxidation-reduction reaction
Cellular signal transduction |
| ISBN |
1-282-29206-4
9786612292064 3-527-62758-8 3-527-62759-6 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Redox Signaling and Regulation in Biology and Medicine; Contents; Preface; The Editors; List of Authors; 1 Introduction; 2 Biological Systems Relevant for Redox Signaling and Control; 2.1 Introduction; 2.2 Reactive Oxygen Species; 2.2.1 The Superoxide Radical; 2.2.1.1 Generation of the Superoxide Radical; 2.2.1.2 The Superoxide Radical as a Redox Signal; 2.2.1.3 Decomposition of the Superoxide Radical; 2.2.2 Hydrogen Peroxide; 2.2.2.1 Generation of Hydrogen Peroxide; 2.2.2.2 Mechanisms of Hydrogen Peroxide Signaling; 2.2.2.3 Decomposition of Hydrogen Peroxide; 2.3 Reactive Nitrogen Species
2.3.1 Nitric Oxide2.3.1.1 Generation of Nitric Oxide; 2.3.1.2 Mechanisms of Nitric Oxide Signaling; 2.3.1.3 Decomposition of Nitric Oxide; 2.3.2 Peroxynitrite and Reactive Nitrogen Species; 2.3.2.1 Generation of Peroxynitrite and Other Important Reactive Nitrogen Species; 2.3.2.2 Mechanisms of Peroxynitrite- and Reactive Nitrogen Species-Mediated Redox Signaling; 2.4 Lipid Peroxidation Products; 2.4.1 Generation of Lipid Peroxidation Products; 2.4.2 Mechanisms of Signaling with Lipid Peroxidation Products; 2.4.3 Decomposition of Lipid Peroxides; 2.5 Conclusions; References 3 Cellular Generation of Oxidants: Relation to Oxidative Stress3.1 Introduction; 3.2 Molecular Oxygen and Reactive Oxygen Species: Biochemical Relations and Endogenous Sources; 3.2.1 Endogenous Sources of Superoxide and Superoxide-Derived Reactive Oxygen Species; 3.2.2 Singlet Oxygen; 3.2.3 ""Secondary"" Reactive Oxygen Species Generated in Radical Chain Reactions; 3.3 Generation of Oxidative Stress Under the Influence of Xenobiotics and Stressful Stimuli; 3.3.1 Quinones and Other Redox Cyclers; 3.3.2 Antioxidant Depletion by Alkylation: Acetaminophen Toxicity; 3.3.3 Ultraviolet Radiation 3.3.4 Ultrafine or NanoparticlesReferences; 4 The Chemical Basis of Biological Redox Control; 4.1 Introduction; 4.2 Forms of Elemental Oxygen as Reactive Oxygen Species; 4.2.1 Reactive Oxygen Species and Related Cellular Oxidants; 4.2.2 Singlet Oxygen (1O2); 4.2.3 Ozone (O3); 4.3 Reduced, Yet Oxidizing: the Chemistry of Oxygen in Oxidation States between 0 and -2; 4.3.1 Superoxide Radicals (O2 ̇ ̄ ); 4.3.2 The Superoxide to Peroxide Conversion as a Key Event in Redox Signaling; 4.3.3 Hydrogen Peroxide (H2O2); 4.3.4 Hydroxyl Radicals (HO·) 4.3.5 Enzymatic Reduction of Hydrogen Peroxide by Peroxiredoxins, Catalase and Glutathione Peroxidase4.4 The Role of Labile Metal Ions in Oxidative Stress; 4.5 Follow-on Species Generated by Chemical Interactions of Reactive Oxygen Species; 4.5.1 Hypochlorous Acid (HOCl); 4.5.2 Peroxynitrite (ONOO ̄ ); 4.6 Nitrogen Monoxide and Reactive Nitrogen Species; 4.6.1 Reactive Nitrogen Species; 4.6.2 S-Nitrosothiols; 4.7 Sulfur as a Prime Target of Oxidative Stress; 4.7.1 Thiol Groups in Peptides and Proteins; 4.7.2 The Concept of Reactive Sulfur Species; 4.7.3 Sulfur-Centered Radicals 4.7.4 Disulfide-S-Oxides (RS(O)xSR') |
| Record Nr. | UNINA-9910808721703321 |
| Weinheim, : Wiley-VCH, c2009 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Standard reference materials : comparison of redox standards/ / K. M. Sappenfield, G. Marinenko
| Standard reference materials : comparison of redox standards/ / K. M. Sappenfield, G. Marinenko |
| Autore | Sappenfield K. M |
| Pubbl/distr/stampa | Gaithersburg, MD : , : U.S. Dept. of Commerce, National Institute of Standards and Technology, , 1972 |
| Descrizione fisica | 1 online resource |
| Altri autori (Persone) |
MarinenkoG
SappenfieldK. M |
| Collana | NBS special publication |
| Soggetto topico |
Arsenic trioxide - Analysis
Chemical tests and reagents - Specifications - United States Oxidation-reduction reaction Potassium dichromate - Analysis |
| Soggetto non controllato | Sodium oxalate |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Altri titoli varianti | Standard reference materials |
| Record Nr. | UNINA-9910709537103321 |
Sappenfield K. M
|
||
| Gaithersburg, MD : , : U.S. Dept. of Commerce, National Institute of Standards and Technology, , 1972 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Thiol metabolism and redox regulation of cellular functions [[electronic resource] /] / [edited by] Alfonso Pompella, Gabor Banhegyi, Maria Wellman-Rousseau
| Thiol metabolism and redox regulation of cellular functions [[electronic resource] /] / [edited by] Alfonso Pompella, Gabor Banhegyi, Maria Wellman-Rousseau |
| Pubbl/distr/stampa | Amsterdam ; ; Washington, DC, : IOS Press, c2002 |
| Descrizione fisica | 1 online resource (365 p.) |
| Disciplina | 572.7 |
| Altri autori (Persone) |
PompellaAlfonso
BánhegyiGábor Wellman-RousseauMaria |
| Collana | NATO science series. Series I, Life and behavioural sciences |
| Soggetto topico |
Antioxidants
Thiols - Physiological effect Glutathione - Physiological effect Oxidation-reduction reaction Cell respiration |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-50567-2
9786610505678 600-00-0589-X 1-60129-472-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cover; Title page; Foreword; Preface; Contributors; Contents; Oxidative Signaling and Glutathione Synthesis; Cell Survival and Changes in Gene Expression in Cells Unable to Synthesize Glutathione; Role of Glutathione in the Regulation of Liver Metabolism; Glutathione Transport in the Endo/Sarcoplasmic Reticulum; Role of Ascorbate in Oxidative Protein Folding; Cytophotometric Investigations on Oscillating Thiol-Disulfide Equilibria and Oxidized Protein Sulfur; Protection by Pantothenic Acid against Apoptosis and Cell Damage by Oxygen Free Radicals - The Role of Glutathione
Thiols as Major Determinants of the Total Antioxidant CapacityEnzymes of the Thiol-dependent Hydroperoxide Metabolism in Pathogens as Potential Drug Targets; Is there a Role of Glutathione Peroxidases in Signaling and Differentiation?; Multidrug Resistance-associated Proteins: Export Pumps for Conjugates with Glutathione, Glucuronate or Sulfate; Detoxification of Electrophilic Compounds by Glutathione S-Transferase Catalysis: Determinants of Individual Response to Chemical Carcinogens and...; Transcriptional Regulation of Glutathione S-Transferase P1-1 in Human Leukemia Mechanism of γ-Glutamyltranspeptidase Folding and Activation in the Endoplasmic ReticulumThe Role of γ-Glutamyl Transpeptidase in the Biosynthesis of Glutathione; Role of γ-Glutamyltransferase in the Homeostasis of Glutathione during Oxidative and Nitrosative Stress; The Importance of gamma-Glutamyl Transferase in Lung Glutathione Homeostasis and Antioxidant Defense; The Role of gamma-Glutamyltranspeptidase in the Metabolism and Cytotoxicity of 4-Hydroxynonenal-Glutathione Conjugate: Evidence and Hypothesis; γ-Glutamyltransferase-Dependent Prooxidant Reactions: a Factor in Multiple Processes Serum gamma-Glutamyl Transpeptidase: a Prognostic Marker in Cardiovascular DiseasesLipoic Acid: a Multifunctional Antioxidant; Is Glutathione an Important Neuroprotective Effector Molecule against Amyloid Beta Toxicity?; Antioxidants in Cancer Therapy: is there a Rationale to Recommend Antioxidants during Cancer Therapy?; Disulfide Exchange in CD4; Redox Regulation in Protein Folding and Chaperone Function; Reduction of the Endoplasmic Reticulum Accompanies the Oxidative Damage of Diabetes Mellitus; Analytical Developments in the Assay of Intra- and Extracellular GSH Homeostasis Signalling Potential and Protein Modifying Ability of Physiological ThiolsRedox Signaling and the Map Kinase Pathways; Redox Regulation of Mitochondrial Permeability Transition: Contrasting Effects of Lipoic Acid and its Positively Charged Analog LA-Plus; Redox State of Glutathione and Thioredoxin in Differentiation and Apoptosis; Redox Regulation of DNA Repair; Author Index |
| Record Nr. | UNINA-9910455910303321 |
| Amsterdam ; ; Washington, DC, : IOS Press, c2002 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Thiol metabolism and redox regulation of cellular functions / / [edited by] Alfonso Pompella, Gabor Banhegyi, Maria Wellman-Rousseau
| Thiol metabolism and redox regulation of cellular functions / / [edited by] Alfonso Pompella, Gabor Banhegyi, Maria Wellman-Rousseau |
| Pubbl/distr/stampa | Amsterdam ; ; Washington, DC : , : IOS Press, , 2002 |
| Descrizione fisica | 1 online resource (365 pages) : illustrations |
| Disciplina | 572.7 |
| Altri autori (Persone) |
PompellaAlfonso
BánhegyiGábor Wellman-RousseauMaria |
| Collana | NATO science series. Series I, Life and behavioural sciences |
| Soggetto topico |
Antioxidants
Thiols - Physiological effect Glutathione - Physiological effect Oxidation-reduction reaction Cell respiration |
| ISBN |
1-280-50567-2
9786610505678 600-00-0589-X 1-60129-472-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cover; Title page; Foreword; Preface; Contributors; Contents; Oxidative Signaling and Glutathione Synthesis; Cell Survival and Changes in Gene Expression in Cells Unable to Synthesize Glutathione; Role of Glutathione in the Regulation of Liver Metabolism; Glutathione Transport in the Endo/Sarcoplasmic Reticulum; Role of Ascorbate in Oxidative Protein Folding; Cytophotometric Investigations on Oscillating Thiol-Disulfide Equilibria and Oxidized Protein Sulfur; Protection by Pantothenic Acid against Apoptosis and Cell Damage by Oxygen Free Radicals - The Role of Glutathione
Thiols as Major Determinants of the Total Antioxidant Capacity; Enzymes of the Thiol-dependent Hydroperoxide Metabolism in Pathogens as Potential Drug Targets; Is there a Role of Glutathione Peroxidases in Signaling and Differentiation?; Multidrug Resistance-associated Proteins: Export Pumps for Conjugates with Glutathione, Glucuronate or Sulfate; Detoxification of Electrophilic Compounds by Glutathione S-Transferase Catalysis: Determinants of Individual Response to Chemical Carcinogens and...; Transcriptional Regulation of Glutathione S-Transferase P1-1 in Human Leukemia Mechanism of γ-Glutamyltranspeptidase Folding and Activation in the Endoplasmic Reticulum; The Role of γ-Glutamyl Transpeptidase in the Biosynthesis of Glutathione; Role of γ-Glutamyltransferase in the Homeostasis of Glutathione during Oxidative and Nitrosative Stress; The Importance of gamma-Glutamyl Transferase in Lung Glutathione Homeostasis and Antioxidant Defense; The Role of gamma-Glutamyltranspeptidase in the Metabolism and Cytotoxicity of 4-Hydroxynonenal-Glutathione Conjugate: Evidence and Hypothesis; γ-Glutamyltransferase-Dependent Prooxidant Reactions: a Factor in Multiple Processes Serum gamma-Glutamyl Transpeptidase: a Prognostic Marker in Cardiovascular Diseases; Lipoic Acid: a Multifunctional Antioxidant; Is Glutathione an Important Neuroprotective Effector Molecule against Amyloid Beta Toxicity?; Antioxidants in Cancer Therapy: is there a Rationale to Recommend Antioxidants during Cancer Therapy?; Disulfide Exchange in CD4; Redox Regulation in Protein Folding and Chaperone Function; Reduction of the Endoplasmic Reticulum Accompanies the Oxidative Damage of Diabetes Mellitus; Analytical Developments in the Assay of Intra- and Extracellular GSH Homeostasis Signalling Potential and Protein Modifying Ability of Physiological Thiols; Redox Signaling and the Map Kinase Pathways; Redox Regulation of Mitochondrial Permeability Transition: Contrasting Effects of Lipoic Acid and its Positively Charged Analog LA-Plus; Redox State of Glutathione and Thioredoxin in Differentiation and Apoptosis; Redox Regulation of DNA Repair; Author Index |
| Record Nr. | UNINA-9910780468403321 |
| Amsterdam ; ; Washington, DC : , : IOS Press, , 2002 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
