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dc.contributor.authorGuttery, David S.
dc.contributor.authorPoulin, Benoit
dc.contributor.authorRamaprasad, Abhinay
dc.contributor.authorWall, Richard J.
dc.contributor.authorFerguson, David J.P.
dc.contributor.authorBrady, Declan
dc.contributor.authorPatzewitz, Eva-Maria
dc.contributor.authorWhipple, Sarah
dc.contributor.authorStraschil, Ursula
dc.contributor.authorWright, Megan H.
dc.contributor.authorAbdel-Haleem, Alyaa M.
dc.contributor.authorRadhakrishnan, Anand
dc.contributor.authorArold, Stefan T.
dc.contributor.authorTate, Edward W.
dc.contributor.authorHolder, Anthony A.
dc.contributor.authorWickstead, Bill
dc.contributor.authorPain, Arnab
dc.contributor.authorTewari, Rita
dc.date.accessioned2014-11-11T14:30:25Z
dc.date.available2014-11-11T14:30:25Z
dc.date.issued2014-07-09
dc.identifier.citationGuttery DS, Poulin B, Ramaprasad A, Wall RJ, Ferguson DJP, et al. (2014) Genome-wide Functional Analysis of Plasmodium Protein Phosphatases Reveals Key Regulators of Parasite Development and Differentiation. Cell Host and Microbe 16: 128-140. doi:10.1016/j.chom.2014.05.020.
dc.identifier.issn19313128
dc.identifier.pmid25011111
dc.identifier.doi10.1016/j.chom.2014.05.020
dc.identifier.urihttp://hdl.handle.net/10754/334576
dc.description.abstractReversible protein phosphorylation regulated by kinases and phosphatases controls many cellular processes. Although essential functions for the malaria parasite kinome have been reported, the roles of most protein phosphatases (PPs) during Plasmodium development are unknown. We report a functional analysis of the Plasmodium berghei protein phosphatome, which exhibits high conservation with the P. falciparum phosphatome and comprises 30 predicted PPs with differential and distinct expression patterns during various stages of the life cycle. Gene disruption analysis of P. berghei PPs reveals that half of the genes are likely essential for asexual blood stage development, whereas six are required for sexual development/sporogony in mosquitoes. Phenotypic screening coupled with transcriptome sequencing unveiled morphological changes and altered gene expression in deletion mutants of two N-myristoylated PPs. These findings provide systematic functional analyses of PPs in Plasmodium, identify how phosphatases regulate parasite development and differentiation, and can inform the identification of drug targets for malaria. © 2014 The Authors.
dc.language.isoen
dc.publisherElsevier BV
dc.rightsThis is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/). Open Access funded by Medical Research Council
dc.rightsArchived with thanks to Cell Host and Microbe
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/
dc.titleGenome-wide functional analysis of plasmodium protein phosphatases reveals key regulators of parasite development and differentiation
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.contributor.departmentPathogen Genomics Laboratory
dc.contributor.departmentStructural Biology and Engineering
dc.identifier.journalCell Host & Microbe
dc.identifier.pmcidPMC4094981
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionCentre for Genetics and Genomics, School of Life Sciences, University of Nottingham, Nottingham NG2 7UH, United Kingdom
dc.contributor.institutionNuffield Department of Clinical Laboratory Science, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom
dc.contributor.institutionDivision of Cell and Molecular Biology, Imperial College London, Exhibition Road, London SW7 2AZ, United Kingdom
dc.contributor.institutionDepartment of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, United Kingdom
dc.contributor.institutionDivision of Parasitology, MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom
dc.contributor.institutionDepartment of Cancer Studies and Molecular Medicine, University of Leicester, Leicester Royal Infirmary, P.O. Box 65, Leicester LE2 7LX, United Kingdom
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personRamaprasad, Abhinay
kaust.personRadhakrishnan, Anand
kaust.personArold, Stefan T.
kaust.personPain, Arnab
kaust.personAbdel-Haleem, Alyaa M.
refterms.dateFOA2018-06-14T04:39:07Z
dc.date.published-online2014-07-09
dc.date.published-print2014-07


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This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/). Open Access funded by Medical Research Council
Except where otherwise noted, this item's license is described as This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/). Open Access funded by Medical Research Council