Selenoprotein Structure and Function

Eranthie Weerapana

2022-01 · Methods in Enzymology 662 knyga · Academic Press

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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. - Provides the authority and expertise of leading contributors from an international board of authors - Presents the latest release in the Methods in Enzymology series - Updated release includes the latest information on Selenoprotein Structure and Function

Apie autorių

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.

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