Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids
The search for novel chemical entities targeting essential and parasite-specific pathways is considered a priority for neglected diseases such as trypanosomiasis and leishmaniasis. The thiol-dependent redox metabolism of trypanosomatids relies on bis-glutathionylspermidine [trypanothione, T(SH)2],...
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Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | article artículo publishedVersion |
Lenguaje: | Inglés |
Publicado: |
Public Library of Science (PLOS)
2020
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Materias: | |
Acceso en línea: | http://hdl.handle.net/2133/19536 http://hdl.handle.net/2133/19536 |
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id |
I15-R121-2133-19536 |
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record_format |
dspace |
institution |
Universidad Nacional de Rosario |
institution_str |
I-15 |
repository_str |
R-121 |
collection |
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) |
language |
Inglés |
orig_language_str_mv |
eng |
topic |
Neglected Diseases Trypanothione Synthetase Inhibitors Pathogenic Trypanosomatids Leishmania Trypanosoma |
spellingShingle |
Neglected Diseases Trypanothione Synthetase Inhibitors Pathogenic Trypanosomatids Leishmania Trypanosoma Benítez, Diego Medeiros, Andrea Fiestas, Lucía Panozzo Zénere, Esteban Andrés Maiwald, Franziska Prousis, Kyriakos C. Roussaki, Marina Calogeropoulou, Theodora Detsi, Anastasia Jaeger, Timo Šarlauskas, Jonas Peterlin Mašič, Lucíja Kunick, Conrad Labadie, Guillermo Roberto Flohé, Leopold Comini, Marcelo A. Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids |
topic_facet |
Neglected Diseases Trypanothione Synthetase Inhibitors Pathogenic Trypanosomatids Leishmania Trypanosoma |
description |
The search for novel chemical entities targeting essential and parasite-specific pathways is
considered a priority for neglected diseases such as trypanosomiasis and leishmaniasis.
The thiol-dependent redox metabolism of trypanosomatids relies on bis-glutathionylspermidine [trypanothione, T(SH)2], a low molecular mass cosubstrate absent in the host. In pathogenic trypanosomatids, a single enzyme, trypanothione synthetase (TryS), catalyzes
trypanothione biosynthesis, which is indispensable for parasite survival. Thus, TryS qualifies as an attractive drug target candidate. |
format |
article artículo publishedVersion |
author |
Benítez, Diego Medeiros, Andrea Fiestas, Lucía Panozzo Zénere, Esteban Andrés Maiwald, Franziska Prousis, Kyriakos C. Roussaki, Marina Calogeropoulou, Theodora Detsi, Anastasia Jaeger, Timo Šarlauskas, Jonas Peterlin Mašič, Lucíja Kunick, Conrad Labadie, Guillermo Roberto Flohé, Leopold Comini, Marcelo A. |
author_facet |
Benítez, Diego Medeiros, Andrea Fiestas, Lucía Panozzo Zénere, Esteban Andrés Maiwald, Franziska Prousis, Kyriakos C. Roussaki, Marina Calogeropoulou, Theodora Detsi, Anastasia Jaeger, Timo Šarlauskas, Jonas Peterlin Mašič, Lucíja Kunick, Conrad Labadie, Guillermo Roberto Flohé, Leopold Comini, Marcelo A. |
author_sort |
Benítez, Diego |
title |
Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids |
title_short |
Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids |
title_full |
Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids |
title_fullStr |
Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids |
title_full_unstemmed |
Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids |
title_sort |
identification of novel chemical scaffolds inhibiting trypanothione synthetase from pathogenic trypanosomatids |
publisher |
Public Library of Science (PLOS) |
publishDate |
2020 |
url |
http://hdl.handle.net/2133/19536 http://hdl.handle.net/2133/19536 |
work_keys_str_mv |
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bdutipo_str |
Repositorios |
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1764820410928463873 |