Cargando…
Nitric oxide. Part F, Oxidative and nitrosative stress in redox regulation of cell signaling /
The discovery that nitrogen monoxide or nitric oxide (NO)is a biologically produced free radical has revolutionized our thinking about physiological and pathological processes. This discovery has ignited enormous interest in the scientific community. When generated at low levels, NO is a signaling m...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Amsterdam ; Boston :
Elsevier/Academic Press,
2008.
|
| Colección: | Methods in enzymology ;
v. 440. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
MARC
| LEADER | 00000cam a2200000Ia 4500 | ||
|---|---|---|---|
| 001 | SCIDIR_ocn234380042 | ||
| 003 | OCoLC | ||
| 005 | 20231117015116.0 | ||
| 006 | m o d | ||
| 007 | cr cnu---unuuu | ||
| 008 | 080722s2008 ne a ob 001 0 eng d | ||
| 040 | |a N$T |b eng |e pn |c N$T |d OCLCQ |d CDX |d IDEBK |d OCLCQ |d COF |d OCLCQ |d OPELS |d OCLCQ |d OPELS |d OCLCF |d VVL |d KUK |d YDXCP |d EBLCP |d DEBSZ |d OCLCQ |d OCLCO |d OCLCA |d ANS |d WYU |d ESU |d YOU |d OCLCO |d OCLCA |d SOI |d OCLCO |d LEAUB |d OCLCO |d OCLCQ |d WURST |d OCLCQ |d OCLCA |d OCLCQ |d OCLCA |d OCLCO |d OCLCQ |d OCL |d OCLCO | ||
| 019 | |a 254160549 |a 808681975 | ||
| 020 | |a 9780080877617 |q (electronic bk.) | ||
| 020 | |a 0080877613 |q (electronic bk.) | ||
| 020 | |a 0123739675 |q (electronic bk.) | ||
| 020 | |a 9780123739674 |q (electronic bk.) | ||
| 035 | |a (OCoLC)234380042 |z (OCoLC)254160549 |z (OCoLC)808681975 | ||
| 050 | 4 | |a QP601 |b .M49eb vol. 440 | |
| 060 | 4 | |a W1 |b ME9615K v.440 2008 | |
| 060 | 4 | |a QV 126 |b N73148 2008 | |
| 072 | 7 | |a SCI |x 007000 |2 bisacsh | |
| 082 | 0 | 4 | |a 572.54 |2 22 |
| 245 | 0 | 0 | |a Nitric oxide. |n Part F, |p Oxidative and nitrosative stress in redox regulation of cell signaling / |c edited by Enrique Cadenas, Lester Packer. |
| 246 | 3 | 0 | |a Oxidative and nitrosative stress in redox regulation of cell signaling |
| 260 | |a Amsterdam ; |a Boston : |b Elsevier/Academic Press, |c 2008. | ||
| 300 | |a 1 online resource (xlvi, 466 pages) : |b illustrations. | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 347 | |a data file |2 rda | ||
| 490 | 1 | |a Methods in enzymology ; |v v. 440 | |
| 504 | |a Includes bibliographical references and index. | ||
| 588 | 0 | |a Print version record. | |
| 520 | |a The discovery that nitrogen monoxide or nitric oxide (NO)is a biologically produced free radical has revolutionized our thinking about physiological and pathological processes. This discovery has ignited enormous interest in the scientific community. When generated at low levels, NO is a signaling molecule, but at high concentration, NO is a cytotoxic molecule. The physiological and pathological processes of NO production and metabolism and its targets, currently areas of intensive research, have important pharmacologic implications for health and disease. | ||
| 505 | 0 | |a Cover; Contents; Contributors; Volumes in Series; Section 1: Molecular Methods; Chapter 1: Mass Spectrometric Characterization of Proteins Modified by Nitric Oxide-Derived Species; Abstract; 1. Introduction; 2. Reagents; 3. Preparation of Nitrated BSA; 4. In-Gel Protein Digestion and Mass Spectrometric Analysis; 5. Data Analysis; 6. MALDI-TOF Peptide Mass Fingerprinting; 7. LC-ESI-IT Fragment Fingerprinting upon Collisional Fragmentation; 8. Concluding Remarks; Acknowledgments; References; Chapter 2: Detecting Nitrated Proteins by Proteomic Technologies; Abstract; 1. Introduction; 2. Methods. | |
| 505 | 8 | |a 3. ConclusionsAcknowledgments; References; Chapter 3: Using Tandem Mass Spectrometry to Quantify Site-Specific Chlorination and Nitration of Proteins: Model System Studies with High-Density Lipoprotein Oxidized by Myeloperoxidase; Abstract; 1. Introduction; 2. High-Density Lipoprotein Biology; 3. Advantages of HDL as a Model System; 4. Advantages of LC-ESI-MS/MS When Analyzing Posttranslational Modifications of Proteins; 5. Isolating HDL, ApoA-I, and MPO; 6. Oxidative Reactions; 7. Proteolytic Digestion of Proteins. | |
| 505 | 8 | |a 8. Liquid Chromatography-Electrospray Ionization Mass Spectrometry (LC-ESI-MS and MS/MS)9. A Combination of Tryptic and Glu-C Digests Provides Complete Sequence Coverage of ApoA-I; 10. HOCl or MPO Preferentially Chlorinates Tyrosine 192 in Lipid-Free ApoA-I; 11. Reagent ONOO-and MPO Nitrate All the Tyrosine Residues in Lipid-Free ApoA-I, but Tyrosine 192 Is the Main Target; 12. HOCl Quantitatively Converts All Three Methionine Residues in ApoA-I to Methionine Sulfoxide; 13. HOCl Generates Hydroxytryptophan and Dihydroxytryptophan Residues in ApoA-I. | |
| 505 | 8 | |a 14. Reactive Nitrogen Species Generates Nitrotryptophan Residues in Lipid-Free ApoA-I15. The YXXK Motif Directs ApoA-I Chlorination; 16. Quantitative Analysis of Posttranslational Modifications of Proteins; 17. ApoA-I Oxidation Impairs Cholesterol Transport by the ABCA1 System; 18. Conclusions; Acknowledgments; References; Chapter 4: Influence of Intramolecular Electron Transfer Mechanism in Biological Nitration, Nitrosation, and Oxidation of Redox-Sensitive Amino Acids; Abstract; 1. Introduction; 2. Methods; 3. Results; Acknowledgments; References. | |
| 505 | 8 | |a Chapter 5: Protein Thiol Modification by Peroxynitrite Anion and Nitric Oxide DonorsAbstract; 1. Introduction; 2. Protein Cysteine Oxidation by ONOO-; 3. Methodology to Detect Protein Thiol Modification; 4. Iodoacetamide Labeling of Proteins after Oxidant Treatment; 5. HPLC Separation of Fluorescein-Labeled Peptides; 6. Detection of Interchain Disulfides by Western Blot; 7. Repair of Protein Disulfides by Thioredoxin Reductase and Glutaredoxin Systems; 8. Thioredoxin Reductase Repair of Protein Disulfides; 9. Quantitation of Protein Disulfides by Measuring NADPH Oxidation. | |
| 650 | 0 | |a Nitric oxide. | |
| 650 | 0 | |a Oxidation-reduction reaction. | |
| 650 | 0 | |a Oxidative stress. | |
| 650 | 0 | |a Cellular signal transduction. | |
| 650 | 1 | 2 | |a Nitric Oxide |x physiology |0 (DNLM)D009569Q000502 |
| 650 | 2 | 2 | |a Oxidation-Reduction |0 (DNLM)D010084 |
| 650 | 2 | 2 | |a Oxidative Stress |0 (DNLM)D018384 |
| 650 | 2 | 2 | |a Signal Transduction |0 (DNLM)D015398 |
| 650 | 6 | |a Oxydor�eduction. |0 (CaQQLa)201-0081574 | |
| 650 | 6 | |a Stress oxydatif. |0 (CaQQLa)201-0352197 | |
| 650 | 6 | |a Transduction du signal cellulaire. |0 (CaQQLa)201-0206812 | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a Oxidative stress |2 fast |0 (OCoLC)fst01049566 | |
| 650 | 7 | |a Oxidation-reduction reaction |2 fast |0 (OCoLC)fst01049564 | |
| 650 | 7 | |a Cellular signal transduction |2 fast |0 (OCoLC)fst00850288 | |
| 650 | 7 | |a Nitric oxide |2 fast |0 (OCoLC)fst01037984 | |
| 653 | 0 | 0 | |a stikstofoxide |
| 653 | 0 | 0 | |a nitric oxide |
| 653 | 0 | 0 | |a fysicochemische eigenschappen |
| 653 | 0 | 0 | |a physicochemical properties |
| 653 | 0 | 0 | |a nitrosoverbindingen |
| 653 | 0 | 0 | |a nitroso compounds |
| 653 | 0 | 0 | |a oxidatie |
| 653 | 0 | 0 | |a oxidation |
| 653 | 0 | 0 | |a redoxreacties |
| 653 | 0 | 0 | |a redox reactions |
| 653 | 1 | 0 | |a Biochemistry |
| 653 | 1 | 0 | |a Biochemie |
| 700 | 1 | |a Packer, Lester. | |
| 700 | 1 | |a Cadenas, Enrique. | |
| 776 | 0 | 8 | |i Print version: |t Nitric oxide. Part F, Oxidative and nitrosative stress in redox regulation of cell signaling. |d Amsterdam ; Boston : Elsevier/Academic Press, 2008 |z 9780123739674 |z 0123739675 |w (OCoLC)227051816 |
| 830 | 0 | |a Methods in enzymology ; |v v. 440. | |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780123739674 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/440 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/440 |z Texto completo |