Evidence map›Paper›PMID 21272379›Full record

ArticleBMC genomics2011

Eukaryote-wide sequence analysis of mitochondrial β-barrel outer membrane proteins.

Kenichiro Imai, Naoya Fujita, M Michael Gromiha, Paul Horton

Abstract read
In one paragraph

Article in BMC genomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021
    Review
  10. A C-Terminally Truncated Variant ofFrontiers in physiology · 2021
    Article
  11. Article
  12. Transport of Proteins into Mitochondria.The protein journal · 2019
    Review
  13. Article
  14. All-atom 3D structure prediction of transmembrane β-barrel proteins from sequences.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Article
  17. Article
  18. TMBB-DB: a transmembrane β-barrel proteome database.Bioinformatics (Oxford, England) · 2012
    Article
  19. Article
  20. VDAC proteomics: post-translation modifications.Biochimica et biophysica acta · 2012
    Review
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

4 authors.

Kenichiro ImaiAIST, Computational Biology Research Center, Tokyo, Aomi 135-0064, Japan.
Naoya Fujita
M Michael Gromiha
Paul Horton

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe outer membranes of mitochondria are thought to be homologous to the outer membranes of Gram negative bacteria, which contain 100's of distinct families of β-barrel membrane proteins (BOMPs) often forming channels for transport of nutrients or drugs. However, only four families of mitochondrial BOMPs (MBOMPs) have been confirmed to date. Although estimates as high as 100 have been made in the past, the number of yet undiscovered MBOMPs is an open question. Fortunately, the recent discovery of a membrane integration signal (the β-signal) for MBOMPs gave us an opportunity to look for undiscovered MBOMPs.

resultsWe present the results of a comprehensive survey of eukaryotic protein sequences intended to identify new MBOMPs. Our search employs recent results on β-signals as well as structural information and a novel BOMP predictor trained on both bacterial and mitochondrial BOMPs. Our principal finding is circumstantial evidence suggesting that few MBOMPs remain to be discovered, if one assumes that, like known MBOMPs, novel MBOMPs will be monomeric and β-signal dependent. In addition to this, our analysis of MBOMP homologs reveals some exceptions to the current model of the β-signal, but confirms its consistent presence in the C-terminal region of MBOMP proteins. We also report a β-signal independent search for MBOMPs against the yeast and Arabidopsis proteomes. We find no good candidates MBOMPs in yeast but the Arabidopsis results are less conclusive.

conclusionsOur results suggest there are no remaining MBOMPs left to discover in yeast; and if one assumes all MBOMPs are β-signal dependent, few MBOMP families remain undiscovered in any sequenced organism.

Indexed as

Artificial IntelligenceAmino Acid MotifsAmino Acid SequenceArabidopsisComputational BiologyConserved SequenceGenes, MitochondrialMitochondrial Membrane Transport ProteinsMolecular Sequence DataProtein Structure, SecondaryProteomeSaccharomyces cerevisiaeSequence Analysis, ProteinMitochondrial Membrane Transport ProteinsProteome

Identifiers

PMID21272379
PMCPMC3045335

What OpenQuestion holds

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LicenceCC BY
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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.