ArticleMolecules (Basel, Switzerland)2017
(-)-Epigallocatechin-3-Gallate Inhibits the Chaperone Activity of Plasmodium falciparum Hsp70 Chaperones and Abrogates Their Association with Functional Partners.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- Development of domain-specific probes ofAntimicrobial agents and chemotherapy · 2026Article
- Malaria Public Health Status: Global Context and Update on Gulf Cooperation Council Countries.Advances in experimental medicine and biology · 2026Review
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- The possibilities and challenges associated with selective targetingTransactions of the Royal Society of South Africa. Royal Society of South Africa · 2025Article
- Ursolic acid acetate and iso-mukaadial acetate bind to Plasmodium falciparum Hsp90, abrogating its chaperone function in vitro.Naunyn-Schmiedeberg's archives of pharmacology · 2024Article
- Iso-mukaadial acetate and ursolic acid acetate bind to Plasmodium Falciparum heat shock protein 70: towards targeting parasite protein folding pathway.BMC chemistry · 2024Article
- Human granzyme B binds Plasmodium falciparum Hsp70-x and mediates antiplasmodial activity in vitro.Cell stress & chaperones · 2023Article
- 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
- Inhibition ofFrontiers in molecular biosciences · 2022Article
- Neurotransmitters and molecular chaperones interactions in cerebral malaria: Is there a missing link?Frontiers in molecular biosciences · 2022Review
- Review
- Characterization of an AtypicalInternational journal of molecular sciences · 2021Article
- Article
- Mutation of GGMP Repeat Segments ofInternational journal of molecular sciences · 2021Article
- Review
- Comparative Characterization ofBiomolecules · 2020Article
- Screening for Small Molecule Modulators ofMarine drugs · 2020Article
- Mining Sudanese Medicinal Plants for Antiprotozoal Agents.Frontiers in pharmacology · 2020Article
- The Power of Phytochemicals Combination in Cancer Chemoprevention.Journal of Cancer · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock proteins (Hsps), amongst them, Hsp70 and Hsp90 families, serve mainly as facilitators of protein folding (molecular chaperones) of the cell. The Hsp70 family of proteins represents one of the most important molecular chaperones in the cell.
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What OpenQuestion holds
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.