Thiol Redox Transitions in Cell Signaling, Part A - 1st Edition - ISBN: 9780123813459, 9780123813466

Thiol Redox Transitions in Cell Signaling, Part A, Volume 473

1st Edition

Chemistry and Biochemistry of Low Molecular Weight and Protein Thiols

Serial Volume Editors: Enrique Cadenas Lester Packer
Hardcover ISBN: 9780123813459
eBook ISBN: 9780123813466
Imprint: Academic Press
Published Date: 14th June 2010
Page Count: 416
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Table of Contents

     

    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

    Description

       

      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

      Key Features

      Along with companion volume, provides a full overview of techniques necessary to the study of thiol redox in relation to cell signaling
      Gathers tried and tested techniques from global labs, offering both new and tried-and-true methods
      * Relevant background and reference information given for procedures can be used as a guide to developing protocols in a number of disciplines

      Readership

      Researchers and students in biochemistry, cardiology, cell and molecular biology, neuroscience, pharmacology, endocrinology.


      Details

      No. of pages:
      416
      Language:
      English
      Copyright:
      © Academic Press 2010
      Published:
      Imprint:
      Academic Press
      eBook ISBN:
      9780123813466
      Hardcover ISBN:
      9780123813459

      About the Serial Volume Editors

      Enrique Cadenas Serial Volume Editor

      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.

      Affiliations and Expertise

      Pharmacology & Pharmaceutical Sciences, School of Pharmacy, University of Southern California, USA

      Lester Packer Serial Volume Editor

      Lester Packer received a PhD in Microbiology and Biochemistry in 1956 from Yale University. In 1961, he joined the University of California at Berkeley serving as Professor of Cell and Molecular Biology until 2000, and then was appointed Adjunct Professor, Pharmacology and Pharmaceutical Sciences, School of Pharmacy at the University of Southern California.

      Dr Packer received numerous distinctions including three honorary doctoral degrees, several distinguished Professor appointments. He was awarded Chevalier de l’Ordre National du Merite (Knight of the French National Order of Merit) and later promoted to the rank of Officier. He served as President of the Society for Free Radical Research International (SFRRI), founder and Honorary President of the Oxygen Club of California.

      He has edited numerous books and published research; some of the most cited articles have become classics in the field of free radical biology:

      Dr Packer is a member of many professional societies and editorial boards. His research elucidated - the Antioxidant Network concept. Exogenous lipoic acid was discovered to be one of the most potent natural antioxidants and placed as the ultimate reductant or in the pecking order of the “Antioxidant Network” regenerating vitamins C and E and stimulating glutathione synthesis, thereby improving the overall cellular antioxidant defense. The Antioxidant Network is a concept addressing the cell’s redox status. He established a world-wide network of research programs by supporting and co-organizing conferences on free radical research and redox biology in Asia, Europe, and America.

      Affiliations and Expertise

      Department of Molecular Pharmacology and Toxicology, School of Pharmaceutical Sciences, University of Southern California, USA