Evidence map›Paper›PMID 28155710›Full record

ArticleBMC bioinformatics2016

Predicting MoRFs in protein sequences using HMM profiles.

Ronesh Sharma, Shiu Kumar, Tatsuhiko Tsunoda, Ashwini Patil, Alok Sharma

Open access · goldAbstract read
In one paragraph

Article in BMC bioinformatics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Computational prediction of disordered binding regions.Computational and structural biotechnology journal · 2023
    Review
  7. Review
  8. Review
  9. Article
  10. Predicting Protein Conformational Disorder and Disordered Binding Sites.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  11. Review
  12. Protein Secondary Structure Prediction With a Reductive Deep Learning Method.Frontiers in bioengineering and biotechnology · 2021
    Article
  13. Article
  14. Presence and structure-activity relationship of intrinsically disordered regions across mucins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Article
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

5 authors at 3 institutions in 2 countries.

Ronesh SharmaSchool of Electrical and Electronics Engineering, Fiji National University, Suva, Fiji.
Shiu KumarSchool of Electrical and Electronics Engineering, Fiji National University, Suva, Fiji.
Tatsuhiko TsunodaCREST, JST, Yokohama, 230-0045, Japan.
Ashwini PatilHuman Genome Center, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan. ashwini@hgc.jp.
Alok SharmaSchool of Engineering and Physics, The University of the South Pacific, Suva, Fiji. alok.fj@gmail.com.
University of the South Pacific · FJJapan Science and Technology Agency · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIntrinsically Disordered Proteins (IDPs) lack an ordered three-dimensional structure and are enriched in various biological processes. The Molecular Recognition Features (MoRFs) are functional regions within IDPs that undergo a disorder-to-order transition on binding to a partner protein. Identifying MoRFs in IDPs using computational methods is a challenging task.

methodsIn this study, we introduce hidden Markov model (HMM) profiles to accurately identify the location of MoRFs in disordered protein sequences. Using windowing technique, HMM profiles are utilised to extract features from protein sequences and support vector machines (SVM) are used to calculate a propensity score for each residue. Two different SVM kernels with high noise tolerance are evaluated with a varying window size and the scores of the SVM models are combined to generate the final propensity score to predict MoRF residues. The SVM models are designed to extract maximal information between MoRF residues, its neighboring regions (Flanks) and the remainder of the sequence (Others).

resultsTo evaluate the proposed method, its performance was compared to that of other MoRF predictors; MoRFpred and ANCHOR. The results show that the proposed method outperforms these two predictors.

conclusionsUsing HMM profile as a source of feature extraction, the proposed method indicates improvement in predicting MoRFs in disordered protein sequences.

Indexed as

Markov ChainsModels, TheoreticalSupport Vector MachineAlgorithmsComputational BiologyHumansIntrinsically Disordered ProteinsIntrinsically Disordered ProteinsHidden Markov model profilesIntrinsically disordered proteinsIntrinsically disordered regionsMolecular recognition featuresSupport vector machines

Identifiers

PMID28155710
PMCPMC5259822
OpenAlexW2561787309

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.