Thiol Redox Transitions in Cell Signaling, Part a

Chemistry and Biochemistry of Low Molecular Weight and Protein Thiols Volume 473
Herausgegeben:Cadenas, Enrique; Packer, Lester

• Gebundenes Buch

Produktbeschreibung

Thiol Redox Transitions in Cell Signaling, Part A, along with its companion (volume 475), presents methods and protocols dealing with thiol oxidation-reduction reactions and their implications as they relate to cell signaling. This first installment of Cadenas and Packer's two-volume treatment specifically deals with glutathionylation and dethiolation, and peroxide removal by peroxiredoxins/thioredoxins and glutathione peroxidases.

The critically acclaimed laboratory standard for 40 years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Over 450 volumes have been published to date, and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.

Produktdetails

• Methods in Enzymology Volume 473
• Verlag: Academic Press / Elsevier Science & Technology
• Artikelnr. des Verlages: C2009-0-01955-2
• Seitenzahl: 416
• Erscheinungstermin: 14. Juni 2010
• Englisch
• Abmessung: 234mm x 159mm x 28mm
• Gewicht: 810g
• ISBN-13: 9780123813459
• ISBN-10: 012381345X
• Artikelnr.: 28436435

Autorenporträt

ENRIQUE CADENAS, MD, PhD, received his PhD in biochemistry from the University of Buenos Aires, School of Medicine. He is professor of pharmacology and pharmaceutical sciences at the University of Southern California School of Pharmacy and of biochemistry and molecular biology at the University of Southern California Keck School of Medicine, and doctor honoris causa (medicine) at the University of Linköping, Sweden. Cadenas was president of the Society for Free Radical Research International (SFRRI) and is fellow of the Society for Free Radical Biology & Medicine. He served the scientific community by participating on NIH study sections (2002-2006; chair 2006-2008). His research interests include energy and redox metabolism in brain aging and the coordinated inflammatory-metabolic responses in brain and neurodegenerative diseases.

Inhaltsangabe

1. His-tag switch method for the analysis of S-nitrosylated proteins



2. Identification of Protein Thiols in Mitochondrial Oxidative Phosphorylation Complexes



3. Mitochondrial thioredoxin reductase: purification, inhibitor studies, and role in cell signaling



4. assessing cell surface thiol status



5. Induction of Thioredoxin for Mediating Preconditioning-induced Cellular Responses



6. A trans sarcoplasmic reticulum membrane redox sensor in the striated muscle: exploring redox sensitivity of the ryanodine receptor calcium release channel



7. Rapid approach for the detection, quantification and discovery of novel sulphenic acid or S-nitrosothiol modified proteins using a biotin-switch method



8. Direct identification by mass spectrometry of in vivo S-nitrosylated peptides



9. Changing paradigms in theology: From antioxidant defence to redox regulation



10. Determination of GSNO formation in biological samples by HPLC electrochemical detection



11. Alteration of thioredoxin reductase 1 levels in elucidating cancer etiology



12. thiol-labeling technology in proteomics



13. Analytical methods for the determination of sulfur metabolite concentrations in cell extracts



14. Chemical tagging and mass spectrometry-based identification of protein thiols modified by lipid peroxidation-derived a,b-unsaturated aldehydes



15. Measuring protein thiol redox changes in mitochondria



16. Engineering of redox domains for monitoring electron transfers spectroscopically



17. Approaches to detection of cysteine sulfenic acids in proteins using dimedone-based chemical probes



18. Evaluation of conditions affecting degree of sulfenic acid labeling in redox-sensitive proteins



19. Colorimetric and spectrophotometric assays of sulfiredoxin



20. Quantifying disulfides in specific proteins



21. A simple method of detecting oxidatively-modified proteins



22. Role of Glutathione Conjugates in Cell Signaling



23. Regulation of Protein Function by Sulfinic Acid Formation



24. Mass spectrometry approaches for the study of the oxidation state of protein cysteine residues



25. assays of protein tyrosine phosphatase oxidation



26. oxidation state of cellular 2-Cys peroxiredoxins (reduced thiol, disulfide and hyperoxidised) by non-reducing SDS-PAGE and immunoblotting