Protein Sensors of Reactive Oxygen Species, Part A: Selenoproteins and Thioredoxin

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