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Protein sensors and reactive oxygen species. Volume 348, Part B, Thiol enzymes and proteins /
This volume of Methods in Enzymology is a companion to Volume 347 and addresses direct sensing of reactive oxygen species and related free radicals by thiol enzymes and proteins.
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
San Diego, Calif. :
Academic Press,
�2002.
|
| Colección: | Methods in enzymology ;
volume 348. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
MARC
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| 245 | 0 | 0 | |a Protein sensors and reactive oxygen species. |n Volume 348, |p Part B, |p Thiol enzymes and proteins / |c edited by Helmut Sies, Lester Packer. |
| 260 | |a San Diego, Calif. : |b Academic Press, |c �2002. | ||
| 300 | |a 1 online resource (xxxiv, 404 pages) : |b illustrations (some color) | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 490 | 1 | |a Methods in enzymology ; |v v. 348 | |
| 504 | |a Includes bibliographical references and indexes. | ||
| 520 | |a This volume of Methods in Enzymology is a companion to Volume 347 and addresses direct sensing of reactive oxygen species and related free radicals by thiol enzymes and proteins. | ||
| 588 | 0 | |a Print version record. | |
| 505 | 8 | |a Chapter 5. Disulfide Reduction in Major Histocompatibility Complex Class II-Restricted Antigen Processing by Interferon-?-InducChapter 6. Thiol Oxidation and Reduction in Major Histocompatibility Complex Class I-Restricted Antigen Processing and Presentation; Chapter 7. Disulfide Bond Formation in Periplasm Escherichia coli; Chapter 8. Protein Disulfide Isomerase as an Enzyme and a Chaperone in Protein Folding; Chapter 9. Characterization of Redox-Active Proteins on Cell Surface; Chapter 10. Measurement. | |
| 650 | 0 | |a Proteins. | |
| 650 | 0 | |a Active oxygen. | |
| 650 | 0 | |a Thiols. | |
| 650 | 2 | |a Proteins |0 (DNLM)D011506 | |
| 650 | 2 | |a Reactive Oxygen Species |0 (DNLM)D017382 | |
| 650 | 2 | |a Sulfhydryl Compounds |0 (DNLM)D013438 | |
| 650 | 6 | |a Prot�eines. |0 (CaQQLa)201-0008150 | |
| 650 | 6 | |a Oxyg�ene actif. |0 (CaQQLa)201-0023010 | |
| 650 | 6 | |a Thiols. |0 (CaQQLa)201-0015865 | |
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| 650 | 7 | |a Active oxygen |2 fast |0 (OCoLC)fst00796282 | |
| 650 | 7 | |a Proteins |2 fast |0 (OCoLC)fst01079711 | |
| 650 | 7 | |a Biof�isica. |2 larpcal | |
| 653 | 0 | 0 | |a redoxreacties |
| 653 | 0 | 0 | |a redox reactions |
| 653 | 0 | 0 | |a thiolen |
| 653 | 0 | 0 | |a thiols |
| 653 | 0 | 0 | |a enzymen |
| 653 | 0 | 0 | |a enzymes |
| 653 | 1 | 0 | |a Proteins and Enzymes |
| 653 | 1 | 0 | |a Eiwitten en enzymen |
| 700 | 1 | |a Sies, H. |q (Helmut), |d 1942- | |
| 700 | 1 | |a Packer, Lester. | |
| 776 | 0 | 8 | |i Print version: |t Protein sensors and reactive oxygen species. Part B, Thiol enzymes and proteins. |d San Diego, Calif. : Academic Press, �2002 |z 0121822516 |z 9780121822514 |w (OCoLC)49223849 |
| 830 | 0 | |a Methods in enzymology ; |v volume 348. | |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121822514 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/348 |z Texto completo |
| 880 | 0 | |6 505-00/(S |a Chapter 1. Thiols in Redox Mechanism of Ribonucleotide Reductase; Chapter 2. Tyrosyl Radicals and Ribonucleotide Reductase; Chapter 3. Flavin-Dependent Sulfhydryl Oxidases in Protein Disulfide Bond Formation; Chapter 4. Analyzing Cotranslational Protein Folding and Disulfide Formation by Diagonal Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis; Chapter 5. Disulfide Reduction in Major Histocompatibility Complex Class II-Restricted Antigen Processing by Interferon-γ-Inducible Lysosomal Thiol ReductaseChapter 6. Thiol Oxidation and Reduction in Major Histocompatibility Complex Class I-Restricted Antigen Processing and Presentation; Chapter 7. Disulfide Bond Formation in Periplasm Escherichia coli; Chapter 8. Protein Disulfide Isomerase as an Enzyme and a Chaperone in Protein Folding; Chapter 9. Characterization of Redox-Active Proteins on Cell Surface; Chapter 10. Measurement of Reduction of Disulfide Bonds in Plasmin by Phosphoglycerate KinaseChapter 11. Redox Potential of GSH/GSSG Couple: Assay and Biological Significance; Chapter 12. Role of Yeast Flavin-Containing Monooxygenase in Maintenance of Thiol-Disulfide Redox Potential; Chapter 13. Identification of Cysteine Sulfenic Acid in AhpC of Alkyl Hydroperoxide Reductase; Chapter 14. Glutaredoxins and Oxidative Stress Defense in Yeast; Chapter 15. Quantitation of Protein Sulfinic and Sulfonic Acid, Irreversibly Oxidized Protein Cysteine Sites in Cellular Proteins; Chapter 16. c-Jun Regulation by S-GlutathionylationChapter 17. S-Glutathionylation of Glyceraldehyde-3-phosphate Dehydrogenase: Role of Thiol Oxidation and Catalysis by Glutaredoxin; Chapter 18. Roles of Nrf2 in Activation of Antioxidant Enzyme Genes via Antioxidant Responsive Elements; Chapter 19. Enzymatic Pathways of β Elimination of Chemopreventive Selenocysteine Se Conjugates; Chapter 20. Gene Expression and Thiol Redox State; Chapter 21. Redox Flow as an Instrument of Gene Regulation; Chapter 22. Optical Methods for Measuring Zinc Binding and Release, Zinc Coordination Environments in Zinc Finger Proteins, and Redox Sensitivity and Activity of Zinc-Bound ThiolsChapter 23. Metallothionein Expression and Oxidative Stress in the Brain; Chapter 24. Reversible Oxidation of HIV-2 Protease; Chapter 25. Thiol Enzymes Protecting Mitochondria against Oxidative Damage; Chapter 26. Phenylarsine Oxide Affinity Chromatography to Identify Proteins Involved in Redox Regulation: Dithiol-Disulfide Equilibrium in Serine/ Threonine Phosphatase Calcineurin; Chapter 27. Glutathione Reductase from Bovine Brain | |