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Glutathione Transferase (GST)-Activated Prodrugs

Glutathione transferase (formerly GST) catalyzes the inactivation of various electrophile-producing anticancer agents via conjugation to the tripeptide glutathione. Moreover, several data link the overexpression of some GSTs, in particular GSTP1-1, to both natural and acquired resistance to various...

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Detalles Bibliográficos
Autores principales: Ruzza, Paolo, Calderan, Andrea
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3834953/
https://www.ncbi.nlm.nih.gov/pubmed/24300447
http://dx.doi.org/10.3390/pharmaceutics5020220
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author Ruzza, Paolo
Calderan, Andrea
author_facet Ruzza, Paolo
Calderan, Andrea
author_sort Ruzza, Paolo
collection PubMed
description Glutathione transferase (formerly GST) catalyzes the inactivation of various electrophile-producing anticancer agents via conjugation to the tripeptide glutathione. Moreover, several data link the overexpression of some GSTs, in particular GSTP1-1, to both natural and acquired resistance to various structurally unrelated anticancer drugs. Tumor overexpression of these proteins has provided a rationale for the search of GST inhibitors and GST activated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of GST-activated cytotoxic compounds.
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spelling pubmed-38349532013-11-21 Glutathione Transferase (GST)-Activated Prodrugs Ruzza, Paolo Calderan, Andrea Pharmaceutics Review Glutathione transferase (formerly GST) catalyzes the inactivation of various electrophile-producing anticancer agents via conjugation to the tripeptide glutathione. Moreover, several data link the overexpression of some GSTs, in particular GSTP1-1, to both natural and acquired resistance to various structurally unrelated anticancer drugs. Tumor overexpression of these proteins has provided a rationale for the search of GST inhibitors and GST activated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of GST-activated cytotoxic compounds. MDPI 2013-04-02 /pmc/articles/PMC3834953/ /pubmed/24300447 http://dx.doi.org/10.3390/pharmaceutics5020220 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Ruzza, Paolo
Calderan, Andrea
Glutathione Transferase (GST)-Activated Prodrugs
title Glutathione Transferase (GST)-Activated Prodrugs
title_full Glutathione Transferase (GST)-Activated Prodrugs
title_fullStr Glutathione Transferase (GST)-Activated Prodrugs
title_full_unstemmed Glutathione Transferase (GST)-Activated Prodrugs
title_short Glutathione Transferase (GST)-Activated Prodrugs
title_sort glutathione transferase (gst)-activated prodrugs
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3834953/
https://www.ncbi.nlm.nih.gov/pubmed/24300447
http://dx.doi.org/10.3390/pharmaceutics5020220
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