Protein abundance and folding rather than the redox state of Kelch13 determine the artemisinin susceptibility of Plasmodium falciparum
Author:
Funder
Baden-Württemberg Stiftung
Deutsche Forschungsgemeinschaft
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Clinical Biochemistry
Reference58 articles.
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2. Intrahost modeling of artemisinin resistance in Plasmodium falciparum;Saralamba;Proc. Natl. Acad. Sci. U. S. A.,2011
3. Novel phenotypic assays for the detection of artemisinin-resistant Plasmodium falciparum malaria in Cambodia: in-vitro and ex-vivo drug-response studies;Witkowski;Lancet Infect. Dis.,2013
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1. Impact of different mutations on Kelch13 protein levels, ART resistance, and fitness cost in Plasmodium falciparum parasites;mBio;2024-06-12
2. Artemisinin-resistantPlasmodium falciparumKelch13 mutant proteins display reduced heme-binding affinity and decreased artemisinin activation;2024-01-24
3. The Kelch13 compartment contains highly divergent vesicle trafficking proteins in malaria parasites;PLOS Pathogens;2023-12-01
4. Artemisinin resistance in P. falciparum: probing the interacting partners of Kelch13 protein in parasite;Journal of Global Antimicrobial Resistance;2023-12
5. The Kelch13 compartment is a hub of highly divergent vesicle trafficking proteins in malaria parasites;2022-12-15
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