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Second of a two-volume treatment dealing with thiol oxidation-reduction specifically in relation to cell signaling

Table of Contents

His-tag switch method for the analysis of S-nitrosylated proteins
Identification of Protein Thiols in Mitochondrial Oxidative Phosphorylation Complexes
Mitochondrial thioredoxin reductase: purification, inhibitor studies, and role in cell signaling
assessing cell surface thiol status
Induction of Thioredoxin for Mediating Preconditioning-induced Cellular Responses
A trans sarcoplasmic reticulum membrane redox sensor in the striated muscle: exploring redox sensitivity of the ryanodine receptor calcium release channel
Rapid approach for the detection, quantification and discovery of novel sulphenic acid or S-nitrosothiol modified proteins using a biotin-switch method
Direct identification by mass spectrometry of in vivo S-nitrosylated peptides
Changing paradigms in theology: From antioxidant defence to redox regulation
Determination of GSNO formation in biological samples by HPLC electrochemical detection
Alteration of thioredoxin reductase 1 levels in elucidating cancer etiology
thiol-labeling technology in proteomics
Analytical methods for the determination of sulfur metabolite concentrations in cell extracts
Chemical tagging and mass spectrometry-based identification of protein thiols modified by lipid peroxidation-derived a,b-unsaturated aldehydes
Measuring protein thiol redox changes in mitochondria
Engineering of redox domains for monitoring electron transfers spectroscopically
Approaches to detection of cysteine sulfenic acids in proteins using dimedone-based chemical probes
Evaluation of conditions affecting degree of sulfenic acid labeling in redox-sensitive proteins
Colorimetric and spectrophotometric assays of sulfiredoxin
Quantifying disulfides in specific proteins
A simple method of detecting oxidatively-modified proteins
Role of Glutathione Conjugates in Cell Signaling
Regulation of Protein Function by Sulfinic Acid Formation
Mass spectrometry approaches for the study of the oxidation state of protein cysteine residues
assays of protein tyrosine phosphatase oxidation
oxidation state of cellular 2-Cys peroxiredoxins (reduced thiol, disulfide and hyperoxidised) by non-reducing SDS-PAGE and immunoblotting

About the Author

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.