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- W2559139569 endingPage "423" @default.
- W2559139569 startingPage "409" @default.
- W2559139569 abstract "During their life cycle Plasmodium parasites rely upon an arsenal of proteins that establish key interactions with the host and vector, and between the parasite sexual stages, with the purpose of ensuring infection, reproduction and proliferation. Among these is a group of secreted or membrane-anchored proteins known as the six-cysteine (6-cys) family. This is a small but important family with only 14 members thus far identified, each stage-specifically expressed during the parasite life cycle. 6-cys proteins often localise at the parasite surface or interface with the host and vector, and are conserved in different Plasmodium species. The unifying feature of the family is the s48/45 domain, presumably involved in adhesion and structurally related to Ephrins, the ligands of Eph receptors. The most prominent s48/45 members are currently under functional investigation and are being pursued as vaccine candidates. In this review, we examine what is known about the 6-cys family, their structure and function, and discuss future research directions." @default.
- W2559139569 created "2016-12-08" @default.
- W2559139569 creator A5014639053 @default.
- W2559139569 creator A5025622592 @default.
- W2559139569 date "2017-06-01" @default.
- W2559139569 modified "2023-10-12" @default.
- W2559139569 title "The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle" @default.
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