Thiol Redox Transitions in Cell Signaling, Part B: Methods in Enzymology, cartea 474
Enrique Cadenas, Lester Packeren Limba Engleză Hardback – 18 aug 2010
- 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
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Specificații
ISBN-13: 9780123810038
ISBN-10: 0123810035
Pagini: 392
Dimensiuni: 152 x 229 x 23 mm
Greutate: 0.75 kg
Editura: ELSEVIER SCIENCE
Seria Methods in Enzymology
ISBN-10: 0123810035
Pagini: 392
Dimensiuni: 152 x 229 x 23 mm
Greutate: 0.75 kg
Editura: ELSEVIER SCIENCE
Seria Methods in Enzymology
Public țintă
Researchers and students in biochemistry, cardiology, cell and molecular biology, neuroscience, pharmacology, endocrinology.Cuprins
- 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