Evidence map›Paper›PMID 11470820›Full record

ArticleThe Journal of cell biology2001

Targeting of an abundant cytosolic form of the protein import receptor at Toc159 to the outer chloroplast membrane.

A Hiltbrunner, J Bauer, P A Vidi, S Infanger, P Weibel, M Hohwy, F Kessler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 129 citations in OpenAlex.

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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.

A HiltbrunnerInstitute of Plant Sciences, Plant Physiology and Biochemistry Group, 8092 Zürich, Switzerland.
J Bauer
P A Vidi
S Infanger
P Weibel
M Hohwy
F Kessler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast biogenesis requires the large-scale import of cytosolically synthesized precursor proteins. A trimeric translocon (Toc complex) containing two homologous GTP-binding proteins (atToc33 and atToc159) and a channel protein (atToc75) facilitates protein translocation across the outer envelope membrane. The mechanisms governing function and assembly of the Toc complex are not yet understood. This study demonstrates that atToc159 and its pea orthologue exist in an abundant, previously unrecognized soluble form, and partition between cytosol-containing soluble fractions and the chloroplast outer membrane. We show that soluble atToc159 binds directly to the cytosolic domain of atToc33 in a homotypic interaction, contributing to the integration of atToc159 into the chloroplast outer membrane. The data suggest that the function of the Toc complex involves switching of atToc159 between a soluble and an integral membrane form.

Indexed as

Arabidopsis ProteinsArabidopsisBinding, CompetitiveChloroplastsCytosolFluorescent Antibody TechniqueGTP PhosphohydrolasesIntracellular MembranesMacromolecular SubstancesMembrane ProteinsPisum sativumPlant LeavesPlant ProteinsProtein PrecursorsProtein TransportSubcellular FractionsArabidopsis ProteinsGTP PhosphohydrolasesMacromolecular SubstancesMembrane ProteinsOEP75 protein precursor, plantPlant ProteinsProtein PrecursorsTOC159 protein, ArabidopsisToc33 protein, ArabidopsisTOC75 protein, Arabidopsis

Identifiers

PMID11470820
PMCPMC2150772
OpenAlexW2135859490

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.