Evidence map›Paper›PMID 25946106›Full record

ArticlePloS one2015

Predicting protein-protein interactions from primary protein sequences using a novel multi-scale local feature representation scheme and the random forest.

Zhu-Hong You, Keith C C Chan, Pengwei Hu

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Trial
  2. Review
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  6. AΙ-Driven Drug Repurposing: Applications and Challenges.Medicines (Basel, Switzerland) · 2025
    Review
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  15. Article
  16. Machine Learning Methods in Protein-Protein Docking.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Review

11 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

3 authors.

Zhu-Hong YouDepartment of Computing, The Hong Kong Polytechnic University, Hong Kong, China; School of Electronics and Information Engineering, Tongji University, Shanghai, China.
Keith C C ChanDepartment of Computing, The Hong Kong Polytechnic University, Hong Kong, China.
Pengwei HuDepartment of Computing, The Hong Kong Polytechnic University, Hong Kong, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of protein-protein interactions (PPIs) can be very important for the understanding of biological cellular functions. However, detecting PPIs in the laboratories are both time-consuming and expensive. For this reason, there has been much recent effort to develop techniques for computational prediction of PPIs as this can complement laboratory procedures and provide an inexpensive way of predicting the most likely set of interactions at the entire proteome scale. Although much progress has already been achieved in this direction, the problem is still far from being solved. More effective approaches are still required to overcome the limitations of the current ones. In this study, a novel Multi-scale Local Descriptor (MLD) feature representation scheme is proposed to extract features from a protein sequence. This scheme can capture multi-scale local information by varying the length of protein-sequence segments. Based on the MLD, an ensemble learning method, the Random Forest (RF) method, is used as classifier. The MLD feature representation scheme facilitates the mining of interaction information from multi-scale continuous amino acid segments, making it easier to capture multiple overlapping continuous binding patterns within a protein sequence. When the proposed method is tested with the PPI data of Saccharomyces cerevisiae, it achieves a prediction accuracy of 94.72% with 94.34% sensitivity at the precision of 98.91%. Extensive experiments are performed to compare our method with existing sequence-based method. Experimental results show that the performance of our predictor is better than several other state-of-the-art predictors also with the H. pylori dataset. The reason why such good results are achieved can largely be credited to the learning capabilities of the RF model and the novel MLD feature representation scheme. The experiment results show that the proposed approach can be very promising for predicting PPIs and can be a useful tool for future proteomic studies.

Indexed as

Protein Interaction MapsAlgorithmsAmino Acid SequenceBacterial ProteinsComputational BiologyFungal ProteinsHelicobacter pyloriProtein Interaction MappingProteomeProteomicsSaccharomyces cerevisiaeSequence Analysis, ProteinSupport Vector MachineBacterial ProteinsFungal ProteinsProteome

Identifiers

PMID25946106
PMCPMC4422660

What OpenQuestion holds

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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.