Proteomics

Dataset Information

0

Intact-cell thermal PISA-MS target-engagement profiling of M5717 in Plasmodium falciparum


ABSTRACT: Here we demonstrate eEF1-alpha and eEF2 stabilisation by M5717 in the intact-cell P. falciparum-infected red blood cells, using thermal Proteome Integral Solubility Alteration (Thermal PISA) assay coupled with Data Independent Acquisition Mass Spectrometry (DIA-MS).

ORGANISM(S): Plasmodium (plasmodium)

SUBMITTER: Jerzy Dziekan, Alan Cowman 

PROVIDER: PXD059612 | JPOST Repository | Tue Feb 17 00:00:00 GMT 2026

REPOSITORIES: jPOST

Dataset's files

Source:
Action DRS
230925_BR1_37C_DMSO.raw Raw
230925_BR1_37C_M5717.raw Raw
230925_BR2_37C_DMSO.raw Raw
230925_BR2_37C_M5717.raw Raw
230925_BR3_37C_DMSO.raw Raw
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Publications

Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug.

Anton Leonie L   Cheng Wenjing W   Haile Meseret T MT   Dziekan Jerzy M JM   Cobb David W DW   Zhu Xiyan X   Han Leyan L   Li Emerson E   Nair Anjali A   Lee Carolyn L CL   Wang Hanyu H   Ke Hangjun H   Zhang Guoan G   Doud Emma H EH   Cowman Alan F AF   Ho Chi-Min CM  

Nature structural & molecular biology 20250818 11


Our understanding of cellular events is hampered by the gap between the resolution at which we can observe events inside cells and our ability to replicate physiological conditions in test tubes. Here, we show in Plasmodium falciparum, a non-model organism of high medical importance, that this gap can be bridged by using an integrated structural biology approach to visualize events inside the cell at molecular resolution. We determined eight high-resolution structures of the native malarial ribo  ...[more]

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