<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Bouzon-Arnaiz I</submitter><funding>ERA-NET</funding><funding>Agència de Gestió d’Ajuts Universitaris i de Recerca</funding><funding>“la Caixa” Foundation</funding><funding>Ministerio de Ciencia e Innovación</funding><pagination>197</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9587658</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>20(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>By 2016, signs of emergence of Plasmodium falciparum resistance to artemisinin and partner drugs were detected in the Greater Mekong Subregion. Recently, the independent evolution of artemisinin resistance has also been reported in Africa and South America. This alarming scenario calls for the urgent development of new antimalarials with novel modes of action. We investigated the interference with protein aggregation, which is potentially toxic for the cell and occurs abundantly in all Plasmodium stages, as a hitherto unexplored drug target in the pathogen.&lt;h4>Results&lt;/h4>Attempts to exacerbate the P. falciparum proteome's propensity to aggregation by delivering endogenous aggregative peptides to in vitro cultures of this parasite did not significantly affect their growt</pubmed_abstract><journal>BMC biology</journal><pubmed_title>The protein aggregation inhibitor YAT2150 has potent antimalarial activity in Plasmodium falciparum in vitro cultures.</pubmed_title><pmcid>PMC9587658</pmcid><funding_grant_id>PID2021-128325OB-I00</funding_grant_id><funding_grant_id>PCIN-2017-100</funding_grant_id><funding_grant_id>AGL2017-84097-C2-2-R</funding_grant_id><funding_grant_id>2017-178</funding_grant_id><funding_grant_id>2017-SGR-908</funding_grant_id><funding_grant_id>HR17-00409</funding_grant_id><funding_grant_id>SAF2017-82771-R</funding_grant_id><funding_grant_id>CEX2018-000806-S</funding_grant_id><funding_grant_id>2017-SGR-106</funding_grant_id><funding_grant_id>PID2020-118127RB-I00</funding_grant_id><funding_grant_id>RTI2018-094579-B-I00</funding_grant_id><pubmed_authors>Fernandez-Busquets X</pubmed_authors><pubmed_authors>Biosca A</pubmed_authors><pubmed_authors>Avalos-Padilla Y</pubmed_authors><pubmed_authors>Valle J</pubmed_authors><pubmed_authors>Cano-Prades O</pubmed_authors><pubmed_authors>Arce EM</pubmed_authors><pubmed_authors>Andreu D</pubmed_authors><pubmed_authors>Prudencio M</pubmed_authors><pubmed_authors>Bouzon-Arnaiz I</pubmed_authors><pubmed_authors>Roman-Alamo L</pubmed_authors><pubmed_authors>Moita D</pubmed_authors><pubmed_authors>Munoz-Torrero D</pubmed_authors></additional><is_claimable>false</is_claimable><name>The protein aggregation inhibitor YAT2150 has potent antimalarial activity in Plasmodium falciparum in vitro cultures.</name><description>&lt;h4>Background&lt;/h4>By 2016, signs of emergence of Plasmodium falciparum resistance to artemisinin and partner drugs were detected in the Greater Mekong Subregion. Recently, the independent evolution of artemisinin resistance has also been reported in Africa and South America. This alarming scenario calls for the urgent development of new antimalarials with novel modes of action. We investigated the interference with protein aggregation, which is potentially toxic for the cell and occurs abundantly in all Plasmodium stages, as a hitherto unexplored drug target in the pathogen.&lt;h4>Results&lt;/h4>Attempts to exacerbate the P. falciparum proteome's propensity to aggregation by delivering endogenous aggregative peptides to in vitro cultures of this parasite did not significantly affect their growt</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Oct</publication><modification>2026-05-28T01:20:25.534Z</modification><creation>2025-02-18T23:29:54.942Z</creation></dates><accession>S-EPMC9587658</accession><cross_references><pubmed>36271358</pubmed><doi>10.1186/s12915-022-01374-4</doi></cross_references></HashMap>