Evidence map›Paper›PMID 26083397›Full record

ArticlePloS one2015

Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein.

Tawanda Zininga, Ikechukwu Achilonu, Heinrich Hoppe, Earl Prinsloo, Heini W Dirr, Addmore Shonhai

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed.

  1. Development of domain-specific probes ofAntimicrobial agents and chemotherapy · 2026
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  3. International journal of molecular sciences · 2025
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  8. HSP70 and their co-chaperones in the human malaria parasiteFrontiers in molecular biosciences · 2022
    Review
  9. Article
  10. Mutation of GGMP Repeat Segments ofInternational journal of molecular sciences · 2021
    Article
  11. Review
  12. Article
  13. Heat Shock Proteins of Malaria: Highlights and Future Prospects.Advances in experimental medicine and biology · 2021
    Article
  14. Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery.Advances in experimental medicine and biology · 2021
    Article
  15. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Tawanda ZiningaDepartment of Biochemistry, School of Mathematical & Natural Sciences, University of Venda, Thohoyandou, 0950, South Africa.
Ikechukwu AchilonuProtein Structure-Function Research Unit, School of Molecular & Cell Biology, University of the Witwatersrand, Johannesburg 2050, South Africa.
Heinrich HoppeDepartment of Biochemistry, Microbiology & Biotechnology, Rhodes University, Grahamstown 6140, South Africa.
Earl PrinslooBiotechnology Innovation Centre, Rhodes University, Grahamstown 6140, South Africa.
Heini W DirrProtein Structure-Function Research Unit, School of Molecular & Cell Biology, University of the Witwatersrand, Johannesburg 2050, South Africa.
Addmore ShonhaiDepartment of Biochemistry, School of Mathematical & Natural Sciences, University of Venda, Thohoyandou, 0950, South Africa.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Six Hsp70-like genes are represented on the genome of Plasmodium falciparum. Of these two occur in the cytosol: P. falciparum Hsp70-z (PfHsp70-z) and PfHsp70-1. PfHsp70-1 is a well characterised canonical Hsp70 that facilitates protein quality control and is crucial for the development of malaria parasites. There is very little known about PfHsp70-z. However, PfHsp70-z is known to be essential and is implicated in suppressing aggregation of asparagine-rich proteins of P. falciparum. In addition, its expression at the clinical stage of malaria correlates with disease prognosis. Based on structural evidence PfHsp70-z belongs to the Hsp110 family of proteins. Since Hsp110 proteins have been described as nucleotide exchange factors (NEFs) of their canonical Hsp70 counterparts, it has been speculated that PfHsp70-z may serve as a NEF of PfHsp70-1. In the current study, P. falciparum cells cultured in vitro were subjected to heat stress, triggering the enhanced expression of PfHsp70-z. Biochemical assays conducted using recombinant PfHsp70-z protein demonstrated that the protein is heat stable and possesses ATPase activity. Furthermore, we observed that PfHsp70-z is capable of self-association. The structural-functional features of PfHsp70-z provide further evidence for its role as a chaperone and possible nucleotide exchange factor of PfHsp70-1.

Indexed as

Adenosine TriphosphatasesGene ExpressionHeat-Shock ResponseHSP70 Heat-Shock ProteinsPlasmodium falciparumProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryProtozoan ProteinsRecombinant ProteinsAdenosine TriphosphatasesHSP70 Heat-Shock ProteinsProtozoan ProteinsRecombinant Proteins

Identifiers

PMID26083397
PMCPMC4471362

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Registered trials

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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.