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Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases

Escalating drug resistance in malaria parasites and lack of vaccine entails the discovery of novel drug targets and inhibitor molecules. The multi-component protein translation machinery is a rich source of such drug targets. Malaria parasites contain three translational compartments: the cytoplasm,...

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Autor principal: Khan, Sameena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4828885/
https://www.ncbi.nlm.nih.gov/pubmed/27068331
http://dx.doi.org/10.1186/s12936-016-1247-0
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author Khan, Sameena
author_facet Khan, Sameena
author_sort Khan, Sameena
collection PubMed
description Escalating drug resistance in malaria parasites and lack of vaccine entails the discovery of novel drug targets and inhibitor molecules. The multi-component protein translation machinery is a rich source of such drug targets. Malaria parasites contain three translational compartments: the cytoplasm, apicoplast and mitochondrion, of which the latter two are of the prokaryotic type. Recent explorations by many groups into the malaria parasite protein translation enzymes, aminoacyl-tRNA synthetases (aaRSs), have yielded many promising inhibitors. The understanding of the biology of this unique set of 36 enzymes has become much clearer in recent times. Current review discusses the advances made in understanding of crucial aaRSs from Plasmodium and also the specific inhibitors found against malaria aaRSs.
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spelling pubmed-48288852016-04-13 Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases Khan, Sameena Malar J Review Escalating drug resistance in malaria parasites and lack of vaccine entails the discovery of novel drug targets and inhibitor molecules. The multi-component protein translation machinery is a rich source of such drug targets. Malaria parasites contain three translational compartments: the cytoplasm, apicoplast and mitochondrion, of which the latter two are of the prokaryotic type. Recent explorations by many groups into the malaria parasite protein translation enzymes, aminoacyl-tRNA synthetases (aaRSs), have yielded many promising inhibitors. The understanding of the biology of this unique set of 36 enzymes has become much clearer in recent times. Current review discusses the advances made in understanding of crucial aaRSs from Plasmodium and also the specific inhibitors found against malaria aaRSs. BioMed Central 2016-04-12 /pmc/articles/PMC4828885/ /pubmed/27068331 http://dx.doi.org/10.1186/s12936-016-1247-0 Text en © Khan. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Review
Khan, Sameena
Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases
title Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases
title_full Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases
title_fullStr Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases
title_full_unstemmed Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases
title_short Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases
title_sort recent advances in the biology and drug targeting of malaria parasite aminoacyl-trna synthetases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4828885/
https://www.ncbi.nlm.nih.gov/pubmed/27068331
http://dx.doi.org/10.1186/s12936-016-1247-0
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