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Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds
Here, we detail our optimized protocol for the identification of drug targets in Leishmania donovani using thermal proteome profiling. This approach is based on the principle that binding of a drug to its protein target can significantly alter the thermal stability of that protein. By monitoring cha...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8384900/ https://www.ncbi.nlm.nih.gov/pubmed/34467225 http://dx.doi.org/10.1016/j.xpro.2021.100704 |
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author | Corpas-Lopez, Victoriano Wyllie, Susan |
author_facet | Corpas-Lopez, Victoriano Wyllie, Susan |
author_sort | Corpas-Lopez, Victoriano |
collection | PubMed |
description | Here, we detail our optimized protocol for the identification of drug targets in Leishmania donovani using thermal proteome profiling. This approach is based on the principle that binding of a drug to its protein target can significantly alter the thermal stability of that protein. By monitoring changes in the thermal stability of proteins within drug-treated and untreated cell lysates, using mass spectrometry combined with tandem mass tag labeling, putative targets of the drug can be identified in an unbiased manner. For further details on the use and application of this protocol, please refer to Paradela et al. (2021). |
format | Online Article Text |
id | pubmed-8384900 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-83849002021-08-30 Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds Corpas-Lopez, Victoriano Wyllie, Susan STAR Protoc Protocol Here, we detail our optimized protocol for the identification of drug targets in Leishmania donovani using thermal proteome profiling. This approach is based on the principle that binding of a drug to its protein target can significantly alter the thermal stability of that protein. By monitoring changes in the thermal stability of proteins within drug-treated and untreated cell lysates, using mass spectrometry combined with tandem mass tag labeling, putative targets of the drug can be identified in an unbiased manner. For further details on the use and application of this protocol, please refer to Paradela et al. (2021). Elsevier 2021-08-18 /pmc/articles/PMC8384900/ /pubmed/34467225 http://dx.doi.org/10.1016/j.xpro.2021.100704 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Protocol Corpas-Lopez, Victoriano Wyllie, Susan Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds |
title | Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds |
title_full | Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds |
title_fullStr | Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds |
title_full_unstemmed | Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds |
title_short | Utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds |
title_sort | utilizing thermal proteome profiling to identify the molecular targets of anti-leishmanial compounds |
topic | Protocol |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8384900/ https://www.ncbi.nlm.nih.gov/pubmed/34467225 http://dx.doi.org/10.1016/j.xpro.2021.100704 |
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