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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 [[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-9910841874603321 |
| Hoboken, N.J., : Wiley-Interscience, c2006 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||