ReviewBiophysical reviews2019
Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function.
Review in Biophysical reviews, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Malaria Public Health Status: Global Context and Update on Gulf Cooperation Council Countries.Advances in experimental medicine and biology · 2026Review
- The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly.Biophysical reviews · 2023Review
- Hsp90 and Associated Co-Chaperones of the Malaria Parasite.Biomolecules · 2022Review
- Inhibitors of theCells · 2021Review
- Synergistic Action between PfHsp90 Inhibitor and PfRad51 Inhibitor Induces Elevated DNA Damage Sensitivity in the Malaria Parasite.Antimicrobial agents and chemotherapy · 2021Article
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Role of Heat Shock Proteins in Immune Modulation in Malaria.Advances in experimental medicine and biology · 2021Article
- The search for molecular mimicry in proteins carried by extracellular vesicles secreted by cells infected withCommunicative & integrative biology · 2021Article
- Role of Hsp90 in Plasmodium falciparum Malaria.Advances in experimental medicine and biology · 2021Article
- Bioprospecting for Novel Heat Shock Protein Modulators: The New Frontier for Antimalarial Drug Discovery?Advances in experimental medicine and biology · 2021Article
- Heat Shock Proteins of Malaria: Highlights and Future Prospects.Advances in experimental medicine and biology · 2021Article
- 2019-A year in Biophysical Reviews.Biophysical reviews · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Heat shock protein 90 (Hsp90) is essential for the development of the main malaria agent, Plasmodium falciparum. Inhibitors that target Hsp90 function are known to not only kill the parasite, but also reverse resistance of the parasite to traditional antimalarials such as chloroquine. For this reason, Hsp90 has been tagged as a promising antimalarial drug target. As a molecular chaperone, Hsp90 facilitates folding of proteins such as steroid hormone receptors and kinases implicated in cell cycle and development. Central to Hsp90 function is its regulation by several co-chaperones. Various co-chaperones interact with Hsp90 to modulate its co-operation with other molecular chaperones such as Hsp70 and to regulate its interaction with substrates. The role of Hsp90 in the development of malaria parasites continues to receive research attention, and several Hsp90 co-chaperones have been mapped out. Recently, focus has shifted to P. falciparum R2TP proteins, which are thought to couple Hsp90 to a diverse set of client proteins. R2TP proteins are generally known to form a complex with Hsp90, and this complex drives multiple cellular processes central to signal transduction and cell division. Given the central role that the R2TP complex may play, the current review highlights the structure-function features of Hsp90 relative to R2TPs of P. falciparum.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.