Evidence map›Paper›PMID 34569022›Full record

ReviewAdvances in experimental medicine and biology2021

Role of the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum.

Tanima Dutta, Eva-Rachele Pesce, Alexander G Maier, Gregory L Blatch

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in experimental medicine and biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
21.7field-weighted citation impact, top 1% 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

12 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. International journal of molecular sciences · 2025
    Article
  4. Article
  5. The J Domain Proteins ofInternational journal of molecular sciences · 2024
    Review
  6. Review
  7. Frontiers in molecular biosciences · 2023
    Article
  8. Review
  9. TheFrontiers in molecular biosciences · 2023
    Review
  10. Review
  11. Exported J domain proteins of the human malaria parasite.Frontiers in molecular biosciences · 2022
    Review
  12. Frontiers in cell and developmental biology · 2022
    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

4 authors at 4 institutions in 3 countries.

Tanima DuttaThe Vice Chancellery, The University of Notre Dame Australia, Fremantle, WA, Australia.
Eva-Rachele PesceCollege of Health and Biomedicine, Victoria University, Melbourne, VIC, Australia.
Alexander G MaierResearch School of Biology, The Australian National University, Canberra, Australia.
Gregory L BlatchThe Vice Chancellery, The University of Notre Dame Australia, Fremantle, WA, Australia. greg.blatch@nd.edu.au.ORCID https://orcid.org/0000-0003-0778-8577
Australian National University · AUHigher Colleges of Technology · AEMurdoch University · AUVictoria University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasmodium falciparum has dedicated an unusually large proportion of its genome to molecular chaperones (2% of all genes), with the heat shock protein 40 (Hsp40) family (now called J domain proteins, JDPs) exhibiting evolutionary radiation into 49 members. A large number of the P. falciparum JDPs (PfJDPs) are predicted to be exported, with certain members shown experimentally to be present in the erythrocyte cytosol (PFA0660w and PFE0055c) or erythrocyte membrane (ring-infected erythrocyte surface antigen, RESA). PFA0660w and PFE0055c are associated with an exported plasmodial Hsp70 (PfHsp70-x) within novel mobile structures called J-dots, which have been proposed to be dedicated to the trafficking of key membrane proteins such as erythrocyte membrane protein 1 (PfEMP1). Well over half of the PfJDPs appear to be essential, including the J-dot PfJDP, PFE0055c, while others have been found to be required for growth under febrile conditions (e.g. PFA0110w, the ring-infected erythrocyte surface antigen protein [RESA]) or involved in pathogenesis (e.g. PF10_0381 has been shown to be important for protrusions of the infected red blood cell membrane, the so-called knobs). Here we review what is known about those PfJDPs that have been well characterised, and may be directly or indirectly involved in the survival and pathogenesis of the malaria parasite.

Indexed as

HSP40 Heat-Shock ProteinsPlasmodium falciparumErythrocytesHSP70 Heat-Shock ProteinsMolecular ChaperonesProtozoan ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesProtozoan ProteinsHeat shock proteinHsp40J domain proteinMolecular chaperoneProtein foldingProtein transportVirulence

Identifiers

PMID34569022
OpenAlexW3203901671

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.