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Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets

Malaria is a major global parasitic disease and a cause of enormous mortality and morbidity. Widespread drug resistance against currently available antimalarials warrants the identification of novel drug targets and development of new drugs. Malarial proteases are a group of molecules that serve as...

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Detalles Bibliográficos
Autor principal: Alam, Asrar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3988940/
https://www.ncbi.nlm.nih.gov/pubmed/24799897
http://dx.doi.org/10.1155/2014/453186
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author Alam, Asrar
author_facet Alam, Asrar
author_sort Alam, Asrar
collection PubMed
description Malaria is a major global parasitic disease and a cause of enormous mortality and morbidity. Widespread drug resistance against currently available antimalarials warrants the identification of novel drug targets and development of new drugs. Malarial proteases are a group of molecules that serve as potential drug targets because of their essentiality for parasite life cycle stages and feasibility of designing specific inhibitors against them. Proteases belonging to various mechanistic classes are found in P. falciparum, of which serine proteases are of particular interest due to their involvement in parasite-specific processes of egress and invasion. In P. falciparum, a number of serine proteases belonging to chymotrypsin, subtilisin, and rhomboid clans are found. This review focuses on the potential of P. falciparum serine proteases as antimalarial drug targets.
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spelling pubmed-39889402014-05-05 Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets Alam, Asrar Interdiscip Perspect Infect Dis Review Article Malaria is a major global parasitic disease and a cause of enormous mortality and morbidity. Widespread drug resistance against currently available antimalarials warrants the identification of novel drug targets and development of new drugs. Malarial proteases are a group of molecules that serve as potential drug targets because of their essentiality for parasite life cycle stages and feasibility of designing specific inhibitors against them. Proteases belonging to various mechanistic classes are found in P. falciparum, of which serine proteases are of particular interest due to their involvement in parasite-specific processes of egress and invasion. In P. falciparum, a number of serine proteases belonging to chymotrypsin, subtilisin, and rhomboid clans are found. This review focuses on the potential of P. falciparum serine proteases as antimalarial drug targets. Hindawi Publishing Corporation 2014 2014-03-11 /pmc/articles/PMC3988940/ /pubmed/24799897 http://dx.doi.org/10.1155/2014/453186 Text en Copyright © 2014 Asrar Alam. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Alam, Asrar
Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets
title Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets
title_full Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets
title_fullStr Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets
title_full_unstemmed Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets
title_short Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets
title_sort serine proteases of malaria parasite plasmodium falciparum: potential as antimalarial drug targets
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3988940/
https://www.ncbi.nlm.nih.gov/pubmed/24799897
http://dx.doi.org/10.1155/2014/453186
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