Evidence map›Paper›PMID 21668595›Full record

ArticleTraffic (Copenhagen, Denmark)2011

Plasmodium falciparum apicoplast transit peptides are unstructured in vitro and during apicoplast import.

John R Gallagher, Krista A Matthews, Sean T Prigge

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 9% 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, 43 citations in OpenAlex.

  1. Article
  2. Exploring the repertoire of rhomboid proteases inFrontiers in cellular and infection microbiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Comparative chemical genomics inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. TheeLife · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Host biotin is required for liver stage development in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  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

3 authors at 1 institution in 1 country.

John R GallagherDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Room E5132, 615 North Wolfe Street, Baltimore, MD 21205, USA.
Krista A Matthews
Sean T Prigge
Johns Hopkins University · US

Funding

Institute for Clinical and Translational Research (UL1)UL1RR025005 · NCRR · JOHNS HOPKINS UNIVERSITY · PI FORD, DANIEL ERNEST · 2007 to 2011
$75.8M
Training: Molecular & Cellular Bases of Infectious DiseasesT32AI007417 · NIAID · JOHNS HOPKINS UNIVERSITY · PI Arturo Casadevall · 1994 to 2026
$11.9M
Roles of Lipoate Pathways in Plasmodium SurvivalR01AI065853 · NIAID · JOHNS HOPKINS UNIVERSITY · PI PRIGGE, SEAN TAYLOR · 2006 to 2010
$2.0M
Roles of lipoate pathways in Plasmodium survivalR56AI065853 · NIAID · JOHNS HOPKINS UNIVERSITY · PI PRIGGE, SEAN TAYLOR · 2012 to 2012
$400k
NCRR NIH HHS UL1 RR025005NIAID NIH HHS R01 AI065853NIAID NIH HHS R56 AI065853NIAID NIH HHS T32 AI007417NIAID NIH HHS T32AI007417
6 · The paper itself

Abstract

Trafficking of soluble proteins to the apicoplast in Plasmodium falciparum is determined by an N-terminal transit peptide (TP) which is necessary and sufficient for apicoplast import. Apicoplast precursor proteins are synthesized at the rough endoplasmic reticulum, but are then specifically sorted from other proteins in the secretory pathway. The mechanism of TP recognition is presently unknown. Apicoplast TPs do not contain a conserved sequence motif; therefore, we asked whether they contain an essential structural motif. Using nuclear magnetic resonance to study a model TP from acyl carrier protein, we found a short, low-occupancy helix, but the TP was otherwise disordered. Using an in vivo localization assay, we blocked TP secondary structure by proline mutagenesis, but found robust apicoplast localization. Alternatively, we increased the helical content of the TP through mutation while maintaining established TP characteristics. Apicoplast import was disrupted in a helical mutant TP, but import was then restored by the further addition of a single proline. We conclude that structure in the TP interferes with apicoplast import, and therefore TPs are functionally disordered. These results provide an explanation for the amino acid bias observed in apicoplast TPs.

Indexed as

Amino Acid SequenceMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularOrganellesPeptidesPlasmodium falciparumProtein Sorting SignalsProtein Structure, SecondaryProtein TransportProtozoan ProteinsRecombinant Fusion ProteinsPeptidesProtein Sorting SignalsProtozoan ProteinsRecombinant Fusion Proteins

Identifiers

PMID21668595
PMCPMC3629917
OpenAlexW2066255872

What OpenQuestion holds

Textmetadata
LicenceTDM
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.