Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts

This article describes data related to a research article titled “The Busulfan Metabolite EdAG Irreversibly Glutathionylates Glutaredoxins” [1]. EdAG is an electrophilic GSH analog formed in vivo from busulfan, which is used in hematopoietic stem cell transplants. EdAG glutathionylates Glutaredoxins...

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Detalles Bibliográficos
Autores principales: Scian, Michele, Atkins, William M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Data Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4588412/
https://www.ncbi.nlm.nih.gov/pubmed/26501085
http://dx.doi.org/10.1016/j.dib.2015.09.002
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author Scian, Michele
Atkins, William M.
author_facet Scian, Michele
Atkins, William M.
author_sort Scian, Michele
collection PubMed
description This article describes data related to a research article titled “The Busulfan Metabolite EdAG Irreversibly Glutathionylates Glutaredoxins” [1]. EdAG is an electrophilic GSH analog formed in vivo from busulfan, which is used in hematopoietic stem cell transplants. EdAG glutathionylates Glutaredoxins (Grx's) but not glutathione transferase A1-1 (GSTA1-1) in vitro. This article includes a complete NMR characterization of synthetic EdAG including homonuclear and heteronuclear correlation spectra. Also included are mass spectra of peptides from Grx's or GSTA1-1 that have cys residues that do not react with EdAG.
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spelling pubmed-45884122015-10-23 Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts Scian, Michele Atkins, William M. Data Brief Data Article This article describes data related to a research article titled “The Busulfan Metabolite EdAG Irreversibly Glutathionylates Glutaredoxins” [1]. EdAG is an electrophilic GSH analog formed in vivo from busulfan, which is used in hematopoietic stem cell transplants. EdAG glutathionylates Glutaredoxins (Grx's) but not glutathione transferase A1-1 (GSTA1-1) in vitro. This article includes a complete NMR characterization of synthetic EdAG including homonuclear and heteronuclear correlation spectra. Also included are mass spectra of peptides from Grx's or GSTA1-1 that have cys residues that do not react with EdAG. Elsevier 2015-09-10 /pmc/articles/PMC4588412/ /pubmed/26501085 http://dx.doi.org/10.1016/j.dib.2015.09.002 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Scian, Michele
Atkins, William M.
Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts
title Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts
title_full Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts
title_fullStr Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts
title_full_unstemmed Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts
title_short Supporting data for characterization of the busulfan metabolite EdAG and the Glutaredoxins that it adducts
title_sort supporting data for characterization of the busulfan metabolite edag and the glutaredoxins that it adducts
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4588412/
https://www.ncbi.nlm.nih.gov/pubmed/26501085
http://dx.doi.org/10.1016/j.dib.2015.09.002
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