UID:
almafu_9958132554502883
Format:
1 online resource (439 p.)
ISBN:
9786611011253
,
9781281011251
,
1281011258
,
9780080496962
,
0080496962
Series Statement:
Methods in enzymology ; v. 348
Content:
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.
Note:
Description based upon print version of record.
,
Front Cover; Protein Sensors and Reactive Oxygen Species; Copyright Page; Table of Contents; Contributors to Volume 348; Preface; Volume in Series; 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
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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
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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
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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
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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
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Chapter 27. Glutathione Reductase from Bovine Brain
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English
Additional Edition:
ISBN 9780121822514
Additional Edition:
ISBN 0121822516
Language:
English
