Evidence map›Paper›PMID 15070403›Full record

ArticleBMC bioinformatics2004

A Hidden Markov Model method, capable of predicting and discriminating beta-barrel outer membrane proteins.

Pantelis G Bagos, Theodore D Liakopoulos, Ioannis C Spyropoulos, Stavros J Hamodrakas

Abstract readComparative Study
In one paragraph

Article in BMC bioinformatics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Review
  2. Article
  3. General features of transmembrane beta barrels from a large database.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  4. Article
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  7. Identification of amino acid domains ofFrontiers in cellular and infection microbiology · 2022
    Article
  8. Article
  9. Computational prediction of secreted proteins in gram-negative bacteria.Computational and structural biotechnology journal · 2021
    Review
  10. Hidden neural networks for transmembrane protein topology prediction.Computational and structural biotechnology journal · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Iron and Virulence inFrontiers in cellular and infection microbiology · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Article

10 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

4 authors.

Pantelis G BagosDepartment of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 15701, GREECE. pbagos@biol.uoa.gr
Theodore D Liakopoulos
Ioannis C Spyropoulos
Stavros J Hamodrakas

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIntegral membrane proteins constitute about 20-30% of all proteins in the fully sequenced genomes. They come in two structural classes, the alpha-helical and the beta-barrel membrane proteins, demonstrating different physicochemical characteristics, structure and localization. While transmembrane segment prediction for the alpha-helical integral membrane proteins appears to be an easy task nowadays, the same is much more difficult for the beta-barrel membrane proteins. We developed a method, based on a Hidden Markov Model, capable of predicting the transmembrane beta-strands of the outer membrane proteins of gram-negative bacteria, and discriminating those from water-soluble proteins in large datasets. The model is trained in a discriminative manner, aiming at maximizing the probability of correct predictions rather than the likelihood of the sequences.

resultsThe training has been performed on a non-redundant database of 14 outer membrane proteins with structures known at atomic resolution; it has been tested with a jacknife procedure, yielding a per residue accuracy of 84.2% and a correlation coefficient of 0.72, whereas for the self-consistency test the per residue accuracy was 88.1% and the correlation coefficient 0.824. The total number of correctly predicted topologies is 10 out of 14 in the self-consistency test, and 9 out of 14 in the jacknife. Furthermore, the model is capable of discriminating outer membrane from water-soluble proteins in large-scale applications, with a success rate of 88.8% and 89.2% for the correct classification of outer membrane and water-soluble proteins respectively, the highest rates obtained in the literature. That test has been performed independently on a set of known outer membrane proteins with low sequence identity with each other and also with the proteins of the training set.

conclusionBased on the above, we developed a strategy, that enabled us to screen the entire proteome of E. coli for outer membrane proteins. The results were satisfactory, thus the method presented here appears to be suitable for screening entire proteomes for the discovery of novel outer membrane proteins. A web interface available for non-commercial users is located at: http://bioinformatics.biol.uoa.gr/PRED-TMBB, and it is the only freely available HMM-based predictor for beta-barrel outer membrane protein topology.

Indexed as

Markov ChainsModels, StatisticalDatabases, ProteinEscherichia coli ProteinsMembrane ProteinsPeptidesPredictive Value of TestsProtein Structure, TertiaryEscherichia coli ProteinsMembrane ProteinsPeptides

Identifiers

PMID15070403
PMCPMC385222

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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.