Evidence map›Paper›PMID 26639022›Full record

ArticleScientific reports2015

Characterization of the 26S proteasome network in Plasmodium falciparum.

Lihui Wang, Claire Delahunty, Karin Fritz-Wolf, Stefan Rahlfs, Judith Helena Prieto, John R Yates, Katja Becker

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Ubiquitin-proteasome system inFrontiers in medicine · 2024
    Pooled it
  2. Characterization of the Regulatory AAA-ATPase Subunit Rpt3 inInternational journal of molecular sciences · 2025
    Article
  3. Article
  4. Covalent inhibition ofiScience · 2025
    Article
  5. Article
  6. Article
  7. Mutation in the 26S proteasome regulatory subunitFrontiers in cellular and infection microbiology · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Artemisinin Binds and Inhibits the Activity ofPathogens (Basel, Switzerland) · 2021
    Article
  13. A Proteasome Mutation SensitizesACS infectious diseases · 2021
    Article
  14. Article
  15. Article
  16. Dienone Compounds: Targets and Pharmacological Responses.Journal of medicinal chemistry · 2020
    Article
  17. ACS infectious diseases · 2020
    Article
  18. Review
  19. Article
  20. Article
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 4 institutions in 2 countries.

Lihui WangBiochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University, Giessen, Germany.
Claire DelahuntyDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, California.
Karin Fritz-WolfMax-Planck Institute for Medical Research, Heidelberg, Germany.
Stefan RahlfsBiochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University, Giessen, Germany.
Judith Helena PrietoDepartment of Chemistry, Western Connecticut State University, Danbury, Connecticut.
John R YatesMax-Planck Institute for Medical Research, Heidelberg, Germany.
Katja BeckerBiochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University, Giessen, Germany.
University of Giessen · DEMax Planck Institute for Medical Research · DEScripps Research Institute · USWestern Connecticut State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotic cells, the ubiquitin-proteasome system as a key regulator of protein quality control is an excellent drug target. We therefore aimed to analyze the 26S proteasome complex in the malaria parasite Plasmodium falciparum, which still threatens almost half of the world's population. First, we established an affinity purification protocol allowing for the isolation of functional 26S proteasome complexes from the parasite. Subunit composition of the proteasome and component stoichiometry were studied and physiologic interacting partners were identified via in situ protein crosslinking. Furthermore, intrinsic ubiquitin receptors of the plasmodial proteasome were determined and their roles in proteasomal substrate recognition were analyzed. Notably, PfUSP14 was characterized as a proteasome-associated deubiquitinase resulting in the concept that targeting proteasomal deubiquitinating activity in P. falciparum may represent a promising antimalarial strategy. The data provide insights into a profound network orchestrated by the plasmodial proteasome and identified novel drug target candidates in the ubiquitin-proteasome system.

Indexed as

AntimalarialsChromatography, AffinityCross-Linking ReagentsEnzyme InhibitorsErythrocytesFormaldehydeHumansMultiprotein ComplexesPlasmodium falciparumProteasome Endopeptidase ComplexProtein Structure, TertiaryProteomicsProtozoan ProteinsReceptors, Cell SurfaceStructural Homology, ProteinUbiquitinAntimalarialsATP dependent 26S proteaseCross-Linking ReagentsEnzyme InhibitorsFormaldehydeMultiprotein ComplexesProteasome Endopeptidase ComplexProtozoan ProteinsReceptors, Cell SurfaceUbiquitinUbiquitin-Specific Proteases

Identifiers

PMID26639022
PMCPMC4671066
OpenAlexW2189691210

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.