ReviewFrontiers in molecular biosciences2015
Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle.
Review in Frontiers in molecular biosciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- Malaria Public Health Status: Global Context and Update on Gulf Cooperation Council Countries.Advances in experimental medicine and biology · 2026Review
- Is the Association of Granzyme B and the Exported Parasite Hsp70 a Possible Trojan Horse of Severe Malaria?Advances in experimental medicine and biology · 2026Article
- The impact of Iso-mukaadial acetate on Plasmodium falciparum transcriptional gene regulation.Scientific reports · 2025Article
- An Undefined Interaction between Polyamines and Heat Shock Proteins Leads to Cellular Protection inMolecules (Basel, Switzerland) · 2023Review
- HSP70 and their co-chaperones in the human malaria parasiteFrontiers in molecular biosciences · 2022Review
- A non-traditional crystal-based compound screening method targeting the ATP binding site ofFrontiers in molecular biosciences · 2022Article
- Exported J domain proteins of the human malaria parasite.Frontiers in molecular biosciences · 2022Review
- Review
- Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1.Cell stress & chaperones · 2021Article
- Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership.Cell stress & chaperones · 2021Article
- Introductory Chapter: The Importance of Heat Shock Proteins in Survival and Pathogenesis of the Malaria Parasite Plasmodium falciparum.Advances in experimental medicine and biology · 2021Article
- The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum.Advances in experimental medicine and biology · 2021Article
- The Role of Malaria Parasite Heat Shock Proteins in Protein Trafficking and Remodelling of Red Blood Cells.Advances in experimental medicine and biology · 2021Review
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Chaperoning of asparagine repeat-containing proteins inJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2020Review
- PV1 Protein fromInternational journal of molecular sciences · 2020Article
- Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites.Microorganisms · 2020Review
- Comparative Characterization ofBiomolecules · 2020Article
- Detection of Protein Aggregation in LiveAntimicrobial agents and chemotherapy · 2020Article
- Establishing Computational Approaches Towards Identifying Malarial Allosteric Modulators: A Case Study ofInternational journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human malaria parasite, Plasmodium falciparum, encodes a minimal complement of six heat shock protein 70s (PfHSP70s), some of which are highly expressed and are thought to play an important role in the survival and pathology of the parasite. In addition to canonical features of molecular chaperones, these HSP70s possess properties that reflect functional adaptation to a parasitic life style, including resistance to thermal insult during fever periods and host-parasite interactions. The parasite even exports an HSP70 to the host cell where it is likely to be involved in host cell modification. This review focuses on the features of the PfHSP70s, particularly with respect to their adaptation to the malaria parasite life cycle.
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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.