Evidence map›Paper›PMID 20826799›Full record

ArticleThe Journal of biological chemistry2010

Malaria parasite actin polymerization and filament structure.

Stephan Schmitz, Iwan A T Schaap, Jens Kleinjung, Simone Harder, Munira Grainger, Lesley Calder, Peter B Rosenthal, Anthony A Holder, Claudia Veigel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
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  5. Unusual dynamics of the divergent malaria parasiteProceedings of the National Academy of Sciences of the United States of America · 2019
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  10. Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

9 authors at 4 institutions in 4 countries.

Stephan SchmitzDivision of Physical Biochemistry, National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom.
Iwan A T Schaap
Jens Kleinjung
Simone Harder
Munira Grainger
Lesley Calder
Peter B Rosenthal
Anthony A Holder
Claudia Veigel
Institute of Physical Chemistry · PLInstitute of Physical Chemistry · BGInstitute of Mathematical Statistics · USPhysical Sciences (United States) · US

Funding

Medical Research Council MC_U117532067Medical Research Council MC_U117581334Medical Research Council U117532067Medical Research Council U117570593Medical Research Council U117581331Medical Research Council U117581334
6 · The paper itself

Abstract

A novel form of acto-myosin regulation has been proposed in which polymerization of new actin filaments regulates motility of parasites of the apicomplexan class of protozoa. In vivo and in vitro parasite F-actin is very short and unstable, but the structural basis and details of filament dynamics remain unknown. Here, we show that long actin filaments can be obtained by polymerizing unlabeled rabbit skeletal actin (RS-actin) onto both ends of the short rhodamine-phalloidin-stabilized Plasmodium falciparum actin I (Pf-actin) filaments. Following annealing, hybrid filaments of micron length and "zebra-striped" appearance are observed by fluorescence microscopy that are stable enough to move over myosin class II motors in a gliding filament assay. Using negative stain electron microscopy we find that pure Pf-actin stabilized by jasplakinolide (JAS) also forms long filaments, indistinguishable in length from RS-actin filaments, and long enough to be characterized structurally. To compare structures in near physiological conditions in aqueous solution we imaged Pf-actin and RS-actin filaments by atomic force microscopy (AFM). We found the monomer stacking to be distinctly different for Pf-actin compared with RS-actin, such that the pitch of the double helix of Pf-actin filaments was 10% larger. Our results can be explained by a rotational angle between subunits that is larger in the parasite compared with RS-actin. Modeling of the AFM data using high-resolution actin filament models supports our interpretation of the data. The structural differences reported here may be a consequence of weaker inter- and intra-strand contacts, and may be critical for differences in filament dynamics and for regulation of parasite motility.

Indexed as

Actin CytoskeletonActinsAnimalsBlotting, WesternCell MovementCells, CulturedCytoskeletonMalaria, FalciparumMicroscopy, Atomic ForceModels, MolecularMuscle, SkeletalPhalloidinePlasmodium falciparumRabbitsRhodaminesActinsPhalloidinerhodamine-phalloidinRhodamines

Identifiers

PMID20826799
PMCPMC2978586
OpenAlexW2048117572

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.