Evidence map›Paper›PMID 19428662›Full record

ArticleMolecular and biochemical parasitology2009

The C-terminal domain of Plasmodium falciparum merozoite surface protein 3 self-assembles into alpha-helical coiled coil tetramer.

Claire Gondeau, Giampietro Corradin, Frédéric Heitz, Christian Le Peuch, Andrea Balbo, Peter Schuck, Andrey V Kajava

Open access · greenAbstract read
In one paragraph

Article in Molecular and biochemical parasitology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

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  10. Identification of invasion proteins of Cryptosporidium parvum.World journal of microbiology & biotechnology · 2015
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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

7 authors at 4 institutions in 3 countries.

Claire GondeauCentre de Recherches de Biochimie Macromoléculaire, CNRS UMR-5237, University of Montpellier 1 and 2, Montpellier, France.
Giampietro Corradin
Frédéric Heitz
Christian Le Peuch
Andrea Balbo
Peter Schuck
Andrey V Kajava
Centre National de la Recherche Scientifique · FRNational Institutes of Health · USUniversité de Montpellier · FRUniversity of Lausanne · CH

Funding

Dynamics of Protein Assemblies by Analytical UltracentrifugationZIAEB000051 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2025
$7.9M
Biophysical Characterization Of MacromoleculesZIAEB000008 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2019
$1.7M
Multi-Method Approaches for the Study of Complex Protein InteractionsZIAEB000050 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2025
$1.7M
Development of Biosensor Technology for Protein InteractionsZIAEB000049 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2013
$465k
Biophysical Characterization Of MacromoleculesZ01EB000008 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2007 to 2008
$333k
Multi-Method Approaches for the Study of Complex Protein InteractionsZ01EB000050 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2007 to 2008
$111k
Dynamics of Protein Assemblies by Analytical UltracentrifugationZ01EB000051 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2007 to 2008
$111k
Development of Biosensor Technology for Protein InteractionsZ01EB000049 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2007 to 2008
$79k
Intramural NIH HHS Z01 EB000008Intramural NIH HHS Z01 EB000049Intramural NIH HHS Z01 EB000050Intramural NIH HHS Z01 EB000051
6 · The paper itself

Abstract

Proteins located on the surface of the pathogenic malaria parasite Plasmodium falciparum are objects of intensive studies due to their important role in the invasion of human cells and the accessibility to host antibodies thus making these proteins attractive vaccine candidates. One of these proteins, merozoite surface protein 3 (MSP3) represents a leading component among vaccine candidates; however, little is known about its structure and function. Our biophysical studies suggest that the 40 residue C-terminal domain of MSP3 protein self-assembles into a four-stranded alpha-helical coiled coil structure where alpha-helices are packed "side-by-side". A bioinformatics analysis provides an extended list of known and putative proteins from different species of Plasmodium which have such MSP3-like C-terminal domains. This finding allowed us to extend some conclusions of our studies to a larger group of the malaria surface proteins. Possible structural and functional roles of these highly conserved oligomerization domains in the intact merozoite surface proteins are discussed.

Indexed as

Models, MolecularPlasmodium falciparumAnimalsAntigens, ProtozoanPolymersProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProtozoan ProteinsUltracentrifugationAntigens, Protozoanmerozoite surface protein 3, PlasmodiumPolymersProtozoan Proteins

Identifiers

PMID19428662
PMCPMC2680791
OpenAlexW2064829342

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.