Evidence map›Paper›PMID 17981999›Full record

ArticleThe Plant cell2007

Functional definition of outer membrane proteins involved in preprotein import into mitochondria.

Ryan Lister, Chris Carrie, Owen Duncan, Lois H M Ho, Katharine A Howell, Monika W Murcha, James Whelan

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
4.0field-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

73 citing papers in PubMed, 158 citations in OpenAlex.

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  14. Overlapping Functions of the Paralogous Proteins AtPAP2 and AtPAP9 inInternational journal of molecular sciences · 2021
    Article
  15. Article
  16. Determinism and contingencies shaped the evolution of mitochondrial protein import.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Article
  19. Conserved and Opposite Transcriptome Patterns during Germination inInternational journal of molecular sciences · 2020
    Article
  20. Review

13 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

7 authors at 3 institutions in 1 country.

Ryan ListerAustralian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009, Western Australia, Australia.
Chris Carrie
Owen Duncan
Lois H M Ho
Katharine A Howell
Monika W Murcha
James Whelan
University of Western Australia · AUARC Centre of Excellence in Plant Energy Biology · AUAustralian Research Council · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of plant mitochondrial outer membrane proteins in the process of preprotein import was investigated, as some of the principal components characterized in yeast have been shown to be absent or evolutionarily distinct in plants. Three outer membrane proteins of Arabidopsis thaliana mitochondria were studied: TOM20 (translocase of the outer mitochondrial membrane), METAXIN, and mtOM64 (outer mitochondrial membrane protein of 64 kD). A single functional Arabidopsis TOM20 gene is sufficient to produce a normal multisubunit translocase of the outer membrane complex. Simultaneous inactivation of two of the three TOM20 genes changed the rate of import for some precursor proteins, revealing limited isoform subfunctionalization. Inactivation of all three TOM20 genes resulted in severely reduced rates of import for some but not all precursor proteins. The outer membrane protein METAXIN was characterized to play a role in the import of mitochondrial precursor proteins and likely plays a role in the assembly of beta-barrel proteins into the outer membrane. An outer mitochondrial membrane protein of 64 kD (mtOM64) with high sequence similarity to a chloroplast import receptor was shown to interact with a variety of precursor proteins. All three proteins have domains exposed to the cytosol and interacted with a variety of precursor proteins, as determined by pull-down and yeast two-hybrid interaction assays. Furthermore, inactivation of one resulted in protein abundance changes in the others, suggesting functional redundancy. Thus, it is proposed that all three components directly interact with precursor proteins to participate in early stages of mitochondrial protein import.

Indexed as

ArabidopsisArabidopsis ProteinsIntracellular MembranesMembrane ProteinsMitochondriaMitochondrial ProteinsMultigene FamilyMutationPlant LeavesProtein BindingProtein IsoformsProtein PrecursorsProtein TransportStarchArabidopsis ProteinsMembrane ProteinsMitochondrial ProteinsProtein IsoformsProtein PrecursorsStarch

Identifiers

PMID17981999
PMCPMC2174869
OpenAlexW2117553283

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.