Evidence map›Paper›PMID 30183110›Full record

ArticleProteins2018

Structural and biochemical characterization of Plasmodium falciparum Hsp70-x reveals functional versatility of its C-terminal EEVN motif.

Blessing Mabate, Tawanda Zininga, Lebogang Ramatsui, Stanley Makumire, Ikechukwu Achilonu, Heini W Dirr, Addmore Shonhai

Open access · hybridAbstract read
In one paragraph

Article in Proteins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 10% of its field
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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Microorganisms · 2025
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  7. Frontiers in cell and developmental biology · 2022
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  8. Inhibition ofFrontiers in molecular biosciences · 2022
    Article
  9. Article
  10. Article
  11. Mutation of GGMP Repeat Segments ofInternational journal of molecular sciences · 2021
    Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Heat Shock Proteins of Malaria: Highlights and Future Prospects.Advances in experimental medicine and biology · 2021
    Article
  18. Role of Heat Shock Proteins in Immune Modulation in Malaria.Advances in experimental medicine and biology · 2021
    Article
  19. Chaperoning of asparagine repeat-containing proteins inJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2020
    Review
  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

7 authors at 2 institutions in 1 country.

Blessing MabateDepartment of Biochemistry, University of Venda, South Africa.
Tawanda ZiningaDepartment of Biochemistry, University of Venda, South Africa.
Lebogang RamatsuiDepartment of Biochemistry, University of Venda, South Africa.
Stanley MakumireDepartment of Biochemistry, University of Venda, South Africa.
Ikechukwu AchilonuProtein Structure-Function Research Unit, School of Molecular & Cell Biology, University of the Witwatersrand, Johannesburg, South Africa.
Heini W DirrProtein Structure-Function Research Unit, School of Molecular & Cell Biology, University of the Witwatersrand, Johannesburg, South Africa.
University of Venda · ZAUniversity of the Witwatersrand · ZA

Funding

Alexander von Humboldt-StiftungClaude Leon FoundationDeutsche Forschungsgemeinschaft L1/402/14-1National Research Foundation of South Africa 64788 7546492598
6 · The paper itself

Abstract

Plasmodium falciparum, the main agent of malaria expresses six members of the heat shock protein 70 (Hsp70) family. Hsp70s serve as protein folding facilitators in the cell. Amongst the six Hsp70 species that P. falciparum expresses, Hsp70-x (PfHsp70-x), is partially exported to the host red blood cell where it is implicated in host cell remodeling. Nearly 500 proteins of parasitic origin are exported to the parasite-infected red blood cell (RBC) along with PfHsp70-x. The role of PfHsp70-x in the infected human RBC remains largely unclear. One of the defining features of PfHsp70-x is the presence of EEVN residues at its C-terminus. In this regard, PfHsp70-x resembles canonical eukaryotic cytosol-localized Hsp70s which possess EEVD residues at their C-termini in place of the EEVN residues associated with PfHsp70-x. The EEVD residues of eukaryotic Hsp70s facilitate their interaction with co-chaperones. Characterization of the role of the EEVN residues of PfHsp70-x could provide insights into the function of this protein. In the current study, we expressed and purified recombinant PfHsp70-x (full length) and its EEVN minus form (PfHsp70-x

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsHomeodomain ProteinsHSP70 Heat-Shock ProteinsHumansMalaria, FalciparumPlasmodium falciparumProtein BindingProtein FoldingProtein Interaction MapsProtozoan ProteinsTumor Suppressor ProteinsAdenosine TriphosphatasesHomeodomain ProteinsHOPX protein, humanHSP70 Heat-Shock ProteinsProtozoan ProteinsTumor Suppressor Proteinsasparagine repeat rich peptidechaperoneEEVNheat shock proteinshuman hopPfHsp70-x

Identifiers

PMID30183110
PMCPMC6282620
OpenAlexW2892197171

What OpenQuestion holds

Textmetadata
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Read underepoch 390

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.