ReviewBiophysical reviews2019
Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Development of domain-specific probes ofAntimicrobial agents and chemotherapy · 2026Article
- In silico identification of selective cyclodecapeptide inhibitors targeting Plasmodium falciparum Grp78 chaperone.Journal of computer-aided molecular design · 2026Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- TargetingiScience · 2024Article
- Swapping the linkers of canonical Hsp70 and Hsp110 chaperones compromises both self-association and client selection.Heliyon · 2024Article
- Inhibition ofFrontiers in molecular biosciences · 2022Article
- A non-traditional crystal-based compound screening method targeting the ATP binding site ofFrontiers in molecular biosciences · 2022Article
- Host cell stress response as a predictor of COVID-19 infectivity and disease progression.Frontiers in molecular biosciences · 2022Review
- Characterization of an AtypicalInternational journal of molecular sciences · 2021Article
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- Mutation of GGMP Repeat Segments ofInternational journal of molecular sciences · 2021Article
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- Chaperoning of asparagine repeat-containing proteins inJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2020Review
- Comparative Characterization ofBiomolecules · 2020Article
- 2019-A year in Biophysical Reviews.Biophysical reviews · 2019Article
- Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites.International journal of molecular sciences · 2019Review
- Review
- Biophysical Reviews: promoting the African synchrotron facility, partnering with national biophysical societies, highlighting advances in structural biology.Biophysical reviews · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heat shock protein 70 (Hsp70) family of molecular chaperones are crucial for the survival and pathogenicity of the main agent of malaria, Plasmodium falciparum. Hsp70 is central to cellular proteostasis and some of its isoforms are essential for survival of the malaria parasite. In addition, they are also implicated in the development of antimalarial drug resistance. For these reasons, they are thought to be potential drug targets, especially in antimalarial combination therapies. However, their high sequence conservation across species presents a hurdle with respect to their selective targeting. The human genome encodes 17 Hsp70 isoforms while P. falciparum encodes for only 6. The structural architecture of Hsp70s is typically characterized by a highly conserved N-terminal nucleotide-binding domain (NBD) and a less conserved C-terminal substrate-binding domain (SBD). The two domains are connected by a highly conserved linker. In spite of their fairly high sequence conservation, Hsp70s from various species possess unique signature motifs that appear to uniquely influence their function. In addition, their cooperation with co-chaperones further regulates their functional specificity. In the current review, bioinformatics tools were used to identify conserved and unique signature motifs in Hsp70s of P. falciparum versus their human counterparts. We discuss the common and distinctive structure-function features of these proteins. This information is important towards elucidating the prospects of selective targeting of parasite heat shock proteins as part of antimalarial design efforts.
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