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- W3087581532 abstract "Abstract Resistance towards known antimalarial drugs poses a significant problem, urging for novel drugs that target vital proteins in the malaria parasite Plasmodium falciparum . However, recombinant production of malaria proteins is notoriously difficult. To address this, we have investigated two putative K + channels, PfKch1 and PfKch2, identified in the P. falciparum genome. We show that PfKch1 and PfKch2 and a C-terminally truncated version of PfKch1 (PfKch1 1−1094 ) could indeed be functionally expressed in vivo, since a K + -uptake deficient Saccharomyces cerevisiae strain was complemented by the P. falciparum cDNAs. PfKch1 1−1094 -GFP and GFP-PfKch2 fusion proteins were overexpressed in yeast, purified and reconstituted in lipid bilayers to determine their electrophysiological activity. Single channel conductance amounted to 16 ± 1 pS for PfKch1 1−1094 -GFP and 28 ± 2 pS for GFP-PfKch2. We predicted regulator of K + -conductance (RCK) domains in the C-terminals of both channels, and we accordingly measured channel activity in the presence of Ca 2+." @default.
- W3087581532 created "2020-09-25" @default.
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- W3087581532 date "2020-09-21" @default.
- W3087581532 modified "2023-10-16" @default.
- W3087581532 title "Purification and initial characterization of Plasmodium falciparum K+ channels, PfKch1 and PfKch2 produced in Saccharomyces cerevisiae" @default.
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- W3087581532 doi "https://doi.org/10.1186/s12934-020-01437-7" @default.
- W3087581532 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7507820" @default.
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