基本説明
This volume, along with its companion (volume 473), presents methods and protocols dealing with thiol oxidation-reduction reactions and their implications as they relate to cell signaling.
Full Description
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.
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
