Selenoproteins and thioredoxin

Author(s)

• Sies, H. (Helmut)
• Packer, Lester
• Buchanan, Bob B.

Bibliographic Information

Selenoproteins and thioredoxin

edited by Helmut Sies, Lester Packer ; editorial advisory board, Bob Buchanan ... [et al.]

（Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 347 . Protein sensors and reactive oxygen species ; pt. A）

Academic Press, c2002

Note

Includes bibliographical references and indexes

Description and Table of Contents

Description

This volume of Methods in Enzymology is concerned with the rapidly developing field of selenoprotein synthesis and its related molecular genetics. Progressive information on the topics of proteins as redox sensors, selenoproteins, and the thioredoxin system is studied using methods such as bioinformatics, DNA chip technology, cell biology, molecular genetics, and enzymology. The information on novel selenoproteins identified from genomic sequence data, as well as current knowledge on glutathione peroxidases, selenoprotein P, iodothyronine deiodinases, and thioredoxin reductases, is presented in a method-based approach.

Table of Contents

Section I: Selenoproteins [1]: Selenoprotein Biosynthesis: Purification and Assay of Components Involved in Selenocysteine Biosynthesis and Insertion in Escherichia coli [2]: Selenocysteine Insertion Sequence Element Characterization and Selenoprotein Expression [3]: Transfer RNAs That Insert Selenocysteine [4]: Purification and Analysis of Selenocysteine Insertion Sequence-Binding Protein 2 [5]: Nonsense-Mediated Decay: Assaying for Effects on Selenoprotein mRNAs [6]: Novel Selenoproteins Identified from Genomic Sequence Data [7]: Semisynthesis of Proteins Containing Selenocysteine [8]: Mammalian Selenoprotein Gene Signature: Identification and Functional Analysis of Selenoprotein Genes Using Bioinformatics Methods [9]: Estimation of Individual Types of Glutathione Peroxidases [10]: High-Throughput 96-Well Microplate Assays for Determining Specific Activities of Glutathione Peroxidase and Thioredoxin Reductase [11]: Selenoprotein P [12]: Iodothyronine Deiodinases [13]: Expression and Regulation of Thioredoxin Reductases and Other Selenoproteins in Bone [14]: Selenoprotein W [15]: Genetic and Functional Analysis of Mammalian Sep15 Selenoprotein [16]: Selenocysteine Lyase from Mouse Liver [17]: Selenocysteine Methyltransferase [18]: Phospholipid-Hydroperoxide Glutathione Peroxidase in Sperm [19]: In Vivo Antioxidant Role of Glutathione Peroxidase: Evidence from Knockout Mice [20]: Recombinant Expression of Mammalian Selenocysteine-Containing Thioredoxin Reductase and Other Selenoproteins in Escherichia coli [21]: Mammalian Thioredoxln Reductases as Hydroperoxide Reductases [22]: Tryparedoxin and Tryparedoxin Peroxidase [23]: Trypanothione and Tryparedoxin in Ribonucleotide Reduction [24]: Selenium- and Vitamin E-Dependent Gene Expression in Rats: Analysis of Differentially Expressed mRNAs Section II: Thioredoxin [25]: Overview [26]: Thioredoxin and Glutaredoxin Isoforms [27]: Mammalian Thioredoxin Reductases [28]: Mitochondrial Thioredoxin Reductase and Thiol Status [29]: Protein Electrophoretic Mobility Shift Assay to Monitor Redox State of Thioredoxin in Cells [30]: Recycling of Vitamin C by Mammalian Thioredoxin Reductase [31]: Thioredoxin Cytokine Action [32]: Identification of Thioredoxin-Linked Proteins by Fluorescence Labeling Combined with Isoelectric Focusing/Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis [33]: Thioredoxin and Mechanism of Inflammatory Response [34]: Redox State of Cytoplasmic Thioredoxin [35]: Thioredoxin, Thioredoxin Reductase, and Thioredoxin Peroxidase of Malaria Parasite Plasmodium falciparum [36]: Human Placenta Thioredoxin Reductase: Preparation and Inhibitor Studies [37]: Classification of Plant Thioredoxins by Sequence Similarity and Intron Position [38]: Ferredoxin-Dependent Thioredoxin Reductase: A Unique Iron-Sulfur Protein [39]: Plant Thioredoxin Gene Expression: Control by Light, Circadian Clock, and Heavy Metals [40]: Thioredoxin Genes in Lens: Regulation by Oxidative Stress [41]: Thioredoxin Overexpression in Transgenic Mice [42]: Multiplex Reverse Transcription-Polymerase Chain Reaction for Determining Transcriptional Regulation of Thioredoxin and Glutaredoxin Pathways [43]: Redox Regulation of Cell Signaling by Thioredoxin Reductases Author index Subject index

by "Nielsen BookData"

Details

• NCID: BA56151423
• ISBN:
  • 0121822486
• Country Code: us
• Title Language Code: eng
• Text Language Code: eng
• Place of Publication: San Diego ; Tokyo
• Pages/Volumes: xxxvi, 511 p.
• Size: 24 cm
• Subject Headings:
  • MESH : Proteins
  • MESH : Active oxygen
  • MESH : Thiols
  • MESH : Thioredoxin
• Parent Bibliography ID:
  • BA00197543