Evidence map›Paper›PMID 23921463›Full record

ArticleNature communications2013

The unusual dynamics of parasite actin result from isodesmic polymerization.

Kristen M Skillman, Christopher I Ma, Daved H Fremont, Karthikeyan Diraviyam, John A Cooper, David Sept, L David Sibley

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  4. Article
  5. Fungal-derived methyldeoxaphomins targetProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  9. bioRxiv : the preprint server for biology · 2023
    Article
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  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Unusual dynamics of the divergent malaria parasiteProceedings of the National Academy of Sciences of the United States of America · 2019
    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 2 institutions in 1 country.

Kristen M SkillmanDepartment of Molecular Microbiology, Washington University School of Medicine, St Louis, Missouri 63110-1093, USA.
Christopher I Ma
Daved H Fremont
Karthikeyan Diraviyam
John A Cooper
David Sept
L David Sibley
Washington University in St. Louis · USUniversity of Michigan–Ann Arbor · US

Funding

PROTEIN SECRETION &INTRACELLULAR SURVIVAL BY TOXOPLASMAR01AI034036 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 1993 to 2019
$7.9M
Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
Targeting the Actin Cytoskeleton in ParasitesR01AI073155 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 2007 to 2011
$1.7M
NIAID NIH HHS AI073155NIAID NIH HHS R01 AI034036NIAID NIH HHS R01 AI073155NIGMS NIH HHS GM38542NIGMS NIH HHS R01 GM038542
6 · The paper itself

Abstract

Previous reports have indicated that parasite actins are short and inherently unstable, despite being required for motility. Here we re-examine the polymerization properties of actin in Toxoplasma gondii, unexpectedly finding that it exhibits isodesmic polymerization in contrast to the conventional nucleation-elongation process of all previously studied actins from both eukaryotes and bacteria. Polymerization kinetics of actin in T. gondii lacks both a lag phase and critical concentration, normally characteristic of actins. Unique among actins, the kinetics of assembly can be fit with a single set of rate constants for all subunit interactions, without need for separate nucleation and elongation rates. This isodesmic model accurately predicts the assembly, disassembly and the size distribution of actin filaments in T. gondii in vitro, providing a mechanistic explanation for actin dynamics in vivo. Our findings expand the repertoire of mechanisms by which actin polymerization is governed and offer clues about the evolution of self-assembling, stabilized protein polymers.

Indexed as

PolymerizationActin CytoskeletonActinsAnimalsBuffersKineticsLightModels, BiologicalParasitesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsScattering, RadiationSolutionsToxoplasmaActinsBuffersSaccharomyces cerevisiae ProteinsSolutions

Identifiers

PMID23921463
PMCPMC3765016
OpenAlexW2108802950

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.