Selenoprotein Structure and Function

by Eranthie Weerapana (Editor)

Overview

Selenoprotein Structure and Function, Volume 662 in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters written by an international board of authors. Chapters in this new release include Identification of Selenoprotein O substrates using a biotinylated ATP analog, Selenium-encoded isotopic signature targeted profiling, Designing tRNASec variants for efficient selenocysteine incorporation using Sec-specific reporters, Preparation of selenoprotein S by chemical ligation, Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells, SecMS analysis of selenoprotein with selenocysteine insertion sequence and beyond, Selenocysteine substitutions in thiyl radical enzymes, and much more.

Additional chapters cover Recombinant selenoprotein expression in E. coli based upon the redefinition of a UAG codon in an RF1-depleted host strain, Metabolic labeling with radioactive selenium in zebrafish, Low pH isoTOP-ABPP to identify selenocysteines, Expression of selenoproteins via genetic code expansion in mammalian cells, Alpha-methyl selenocysteine as a tool for the study of selenoproteins, Selective selenol fluorescent probes: design, synthesis, structural determinants, and biological applications, and much more.

Product Details

ISBN-13:	9780323907354
Publisher:	Elsevier Science
Publication date:	02/04/2022
Series:	Methods in Enzymology , #662
Pages:	416
Product dimensions:	6.00(w) x 9.00(h) x (d)

About the Author

Eranthie Weerapana is an Associate Professor of Chemistry at Boston College. She received her B.S. in Chemistry from Yale University, and her Ph.D. in Chemistry from MIT, where she worked with Professor Barbara Imperiali, investigating glycosyltransferases involved in N-linked glycosylation in the gram negative bacterium Campylobacter jejuni. She then performed postdoctoral studies at The Scripps Research Institute, La Jolla where she worked with Professor Benjamin F. Cravatt to develop chemical-proteomic methods to investigate reactive cysteines in complex proteomes. Her interdisciplinary research program focuses on applying mass-spectrometry methods to identify regulatory cysteine residues in the human proteome, and chemical biology approaches to develop covalent small-molecule modulators for cysteine-mediated protein activities.

Table of Contents

1. Identification of Selenoprotein O substrates using a biotinylated ATP analog
Anju Sreelatha
2. Selenium-encoded isotopic signature targeted profiling
Chu Wang
3. Designing tRNASec variants for efficient selenocysteine incorporation using Sec-specific reporters
Dieter Söll
4. Preparation of selenoprotein S by chemical ligation
Sharon Rozovsky
5. Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells
Dohoon Kim
6. SecMS analysis of selenoprotein with selenocysteine insertion sequence and beyond
Yaoyang Zhang
7. Selenocysteine substitutions in thiyl radical enzymes
Brandon Greene
8. Recombinant selenoprotein expression in E. coli based upon the redefinition of a UAG codon in an RF1-depleted host strain
Elias S.J. Arnér
9. Metabolic labeling with radioactive selenium in　zebrafish
Paul Copeland
10. Low pH isoTOP-ABPP to identify selenocysteines
Daniel Bak
11. Expression of selenoproteins via genetic code expansion in mammalian cells
Jennifer Peeler
12. Alpha-methyl selenocysteine as a tool for the study of selenoproteins
Robert Hondal
13. Selective selenol fluorescent probes: design, synthesis, structural determinants, and biological applications
Jianguo Fang and Baoxin Zhang
14. Diselenide-selenoester ligation
Richard Payne
15. Modeling selenocysteine-derived reactive intermediates utilizing a molecular cradle
Kei Goto
16. Methods for accurate and reproducible studies of pharmacological effects of selenium in cancer
Mikael Björnstedt

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From the Publisher

Edited by some of the best scientists in the field, this series presents the latest updates in the field of enzymology