Evidence map›Paper›PMID 22253438›Full record

ArticleThe Journal of biological chemistry2012

Biosynthesis, localization, and macromolecular arrangement of the Plasmodium falciparum translocon of exported proteins (PTEX).

Hayley E Bullen, Sarah C Charnaud, Ming Kalanon, David T Riglar, Chaitali Dekiwadia, Niwat Kangwanrangsan, Motomi Torii, Takafumi Tsuboi, Jacob Baum, Stuart A Ralph and 4 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
–field-weighted citation impact
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

83 citing papers in PubMed.

  1. mSphere · 2026
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  18. Dissecting EXP2 sequence requirements for protein export in malaria parasites.Frontiers in cellular and infection microbiology · 2023
    Article
  19. The delayed bloodstream clearance ofFrontiers in cellular and infection microbiology · 2023
    Article
  20. Article

23 more citing papers are in PubMed but not listed here.

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

14 authors.

Hayley E BullenMacfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Victoria 3004, Australia.
Sarah C Charnaud
Ming Kalanon
David T Riglar
Chaitali Dekiwadia
Niwat Kangwanrangsan
Motomi Torii
Takafumi Tsuboi
Jacob Baum
Stuart A Ralph
Alan F Cowman
Tania F de Koning-Ward
Brendan S Crabb
Paul R Gilson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To survive within its host erythrocyte, Plasmodium falciparum must export hundreds of proteins across both its parasite plasma membrane and surrounding parasitophorous vacuole membrane, most of which are likely to use a protein complex known as PTEX (Plasmodium translocon of exported proteins). PTEX is a putative protein trafficking machinery responsible for the export of hundreds of proteins across the parasitophorous vacuole membrane and into the human host cell. Five proteins are known to comprise the PTEX complex, and in this study, three of the major stoichiometric components are investigated including HSP101 (a AAA(+) ATPase), a protein of no known function termed PTEX150, and the apparent membrane component EXP2. We show that these proteins are synthesized in the preceding schizont stage (PTEX150 and HSP101) or even earlier in the life cycle (EXP2), and before invasion these components reside within the dense granules of invasive merozoites. From these apical organelles, the protein complex is released into the host cell where it resides with little turnover in the parasitophorous vacuole membrane for most of the remainder of the following cell cycle. At this membrane, PTEX is arranged in a stable macromolecular complex of >1230 kDa that includes an ∼600-kDa apparently homo-oligomeric complex of EXP2 that can be separated from the remainder of the PTEX complex using non-ionic detergents. Two different biochemical methods undertaken here suggest that PTEX components associate as EXP2-PTEX150-HSP101, with EXP2 associating with the vacuolar membrane. Collectively, these data support the hypothesis that EXP2 oligomerizes and potentially forms the putative membrane-spanning pore to which the remainder of the PTEX complex is attached.

Indexed as

HumansIntracellular MembranesMembrane ProteinsMultiprotein ComplexesPlasmodium falciparumProtein TransportProtozoan ProteinsSchizontsVacuolesMembrane ProteinsMultiprotein ComplexesProtozoan Proteins

Identifiers

PMID22253438
PMCPMC3318755

What OpenQuestion holds

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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.