Evidence map›Paper›PMID 33048996›Full record

ReviewPloS one2020

Maximizing cohesion and separation for detecting protein functional modules in protein-protein interaction networks.

Kuo-Ching Ying, Shih-Wei Lin

Abstract readReview
In one paragraph

Review in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Molecular Modelling Hurdle in the Next-Generation Sequencing Era.International journal of molecular sciences · 2022
    Article
  4. 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

2 authors.

Kuo-Ching YingDepartment of Industrial Engineering and Management, National Taipei University of Technology, Taipei, Taiwan.
Shih-Wei LinDepartment of Information Management, Chang Gung University, Taoyuan, Taiwan.ORCID 0000-0003-1343-0838

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein Function Module (PFM) identification in Protein-Protein Interaction Networks (PPINs) is one of the most important and challenging tasks in computational biology. The quick and accurate detection of PFMs in PPINs can contribute greatly to the understanding of the functions, properties, and biological mechanisms in research on various diseases and the development of new medicines. Despite the performance of existing detection approaches being improved to some extent, there are still opportunities for further enhancements in the efficiency, accuracy, and robustness of such detection methods. Based on the uniqueness of the network-clustering problem in the context of PPINs, this study proposed a very effective and efficient model based on the Lin-Kernighan-Helsgaun algorithm for detecting PFMs in PPINs. To demonstrate the effectiveness and efficiency of the proposed model, computational experiments are performed using three different categories of species datasets. The computational results reveal that the proposed model outperforms existing detection techniques in terms of two key performance indices, i.e., the degree of polymerization inside PFMs (cohesion) and the deviation degree between PFMs (separation), while being very fast and robust. The proposed model can be used to help researchers decide whether to conduct further expensive and time-consuming biological experiments and to select target proteins from large-scale PPI data for further detailed research.

Indexed as

Models, BiologicalProtein Interaction MapsAlgorithmsCluster AnalysisComputational BiologyHumansProtein Interaction Mapping

Identifiers

PMID33048996
PMCPMC7553341

What OpenQuestion holds

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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.