The Kinomics of Malaria

Mathieu Brochet, Andrew B Tobin, Oliver Billker, Christian Daniel Doerig

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Otherpeer-review

3 Citations (Scopus)

Abstract

Reversible phosphorylation regulates many aspects of protein function and properties, such as proper folding, localization, binding potential, enzymatic activity, or stability. This chapter focuses on the Plasmodium kinome and on the biology of protein phosphorylation in Plasmodium. It discusses the potential and initial progress in antimalarial drug discovery based on the inhibition of the protein kinases of both the parasite and its host erythrocyte. Methods to manipulate the Plasmodium genome have been developed only relatively recently. The most commonly used methods rely on the transfection of asexual erythrocytic stages of the life cycle, in which the parasite is haploid and replicates continuously, facilitating genetic manipulation and selection of recombinants. The rapid expansion of mass spectrometry-based proteomic techniques has provided a method of producing a snapshot of the global phosphorylation status of organisms such as yeast and bacteria, as well as cultured eukaryotic cells, and tissues such as the liver. ? 2015 Wiley-VCH Verlag GmbH Co. KGaA,. All rights reserved.
Original languageEnglish
Title of host publicationKinomics
Subtitle of host publicationApproaches and Applications
EditorsHeinz-Bernhard Kraatz, Sanela Martic
Place of PublicationWeinheim Germany
PublisherWiley-VCH Verlag GmbH & Co. KGaA
Pages115-135
Number of pages21
Edition1st
ISBN (Print)9783527337651
DOIs
Publication statusPublished - 2015

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