scholarly journals SETS: A Seed-Dense-Expanding Model-Based Topological Structure for the Prediction of Overlapping Protein Complexes

2021 ◽  
Vol 29 (2) ◽  
Author(s):  
Soheir Noori ◽  
Nabeel Al-A’araji ◽  
Eman Al-Shamery
Keyword(s):  
Protein Interaction ◽  
Execution Time ◽  
Topological Structure ◽  
Protein Complexes ◽  
Biological Cell ◽  
Ppi Network ◽  
High Similarity ◽  
Protein Protein Interaction ◽  
Ppi Networks ◽  
F Measure

Defining protein complexes by analysing the protein–protein interaction (PPI) networks is a crucial task in understanding the principles of a biological cell. In the last few decades, researchers have proposed numerous methods to explore the topological structure of a PPI network to detect dense protein complexes. In this paper, the overlapping protein complexes with different densities are predicted within an acceptable execution time using seed expanding model and topological structure of the PPI network (SETS). SETS depend on the relation between the seed and its neighbours. The algorithm was compared with six algorithms on six datasets: five for yeast and one for human. The results showed that SETS outperformed other algorithms in terms of F-measure, coverage rate and the number of complexes that have high similarity with real complexes.

scholarly journals A Least Square Method Based Model for Identifying Protein Complexes in Protein-Protein Interaction Network

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Qiguo Dai ◽  
Maozu Guo ◽  
Yingjie Guo ◽  
Xiaoyan Liu ◽  
Yang Liu ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Least Squares Method ◽  
Protein Complexes ◽  
Interaction Network ◽  
Least Square Method ◽  
Least Square ◽  
Great Effort ◽  
Ppi Network ◽  
Protein Protein Interaction ◽  
Ppi Networks

Protein complex formed by a group of physical interacting proteins plays a crucial role in cell activities. Great effort has been made to computationally identify protein complexes from protein-protein interaction (PPI) network. However, the accuracy of the prediction is still far from being satisfactory, because the topological structures of protein complexes in the PPI network are too complicated. This paper proposes a novel optimization framework to detect complexes from PPI network, named PLSMC. The method is on the basis of the fact that if two proteins are in a common complex, they are likely to be interacting. PLSMC employs this relation to determine complexes by a penalized least squares method. PLSMC is applied to several public yeast PPI networks, and compared with several state-of-the-art methods. The results indicate that PLSMC outperforms other methods. In particular, complexes predicted by PLSMC can match known complexes with a higher accuracy than other methods. Furthermore, the predicted complexes have high functional homogeneity.

scholarly journals A Non-negative Matrix Factorization Based Method for Identifying Essential Proteins

2021 ◽  
Author(s):  
Zhihong Zhang ◽  
Sai Hu ◽  
Wei Yan ◽  
Bihai Zhao ◽  
Lei Wang
Keyword(s):  
Protein Interaction ◽  
Matrix Factorization ◽  
Biological Data ◽  
Protein Domain ◽  
Biological Information ◽  
Ppi Network ◽  
Essential Proteins ◽  
Protein Protein Interaction ◽  
Ppi Networks ◽  
Non Negative Matrix Factorization

Abstract BackgroundIdentification of essential proteins is very important for understanding the basic requirements to sustain a living organism. In recent years, various different computational methods have been proposed to identify essential proteins based on protein-protein interaction (PPI) networks. However, there has been reliable evidence that a huge amount of false negatives and false positives exist in PPI data. Therefore, it is necessary to reduce the influence of false data on accuracy of essential proteins prediction by integrating multi-source biological information with PPI networks.ResultsIn this paper, we proposed a non-negative matrix factorization and multiple biological information based model (NDM) for identifying essential proteins. The first stage in this progress was to construct a weighted PPI network by combing the information of protein domain, protein complex and the topology characteristic of the original PPI network. Then, the non-negative matrix factorization technique was used to reconstruct an optimized PPI network with whole enough weight of edges. In the final stage, the ranking score of each protein was computed by the PageRank algorithm in which the initial scores were calculated with homologous and subcellular localization information. In order to verify the effectiveness of the NDM method, we compared the NDM with other state-of-the-art essential proteins prediction methods. The comparison of the results obtained from different methods indicated that our NDM model has better performance in predicting essential proteins.ConclusionEmploying the non-negative matrix factorization and integrating multi-source biological data can effectively improve quality of the PPI network, which resulted in the led to optimization of the performance essential proteins identification. This will also provide a new perspective for other prediction based on protein-protein interaction networks.

scholarly journals PPInfer: a Bioconductor package for inferring functionally related proteins using protein interaction networks

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 1969
Author(s):  
Dongmin Jung ◽  
Xijin Ge
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Networks ◽  
Interaction Networks ◽  
Biological Processes ◽  
Bioconductor Package ◽  
Biological Functions ◽  
Ppi Network ◽  
Protein Protein Interaction ◽  
Ppi Networks ◽  
Related Proteins

Interactions between proteins occur in many, if not most, biological processes. This fact has motivated the development of a variety of experimental methods for the identification of protein-protein interaction (PPI) networks. Leveraging PPI data available STRING database, we use network-based statistical learning methods to infer the putative functions of proteins from the known functions of neighboring proteins on a PPI network. This package identifies such proteins often involved in the same or similar biological functions. The package is freely available at the Bioconductor web site (http://bioconductor.org/packages/PPInfer/).

scholarly journals PPInfer: a Bioconductor package for inferring functionally related proteins using protein interaction networks

F1000Research ◽  
2018 ◽  
Vol 6 ◽  
pp. 1969 ◽  
Author(s):  
Dongmin Jung ◽  
Xijin Ge
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Networks ◽  
Interaction Networks ◽  
Biological Processes ◽  
Bioconductor Package ◽  
Biological Functions ◽  
Ppi Network ◽  
Protein Protein Interaction ◽  
Ppi Networks ◽  
Related Proteins

Interactions between proteins occur in many, if not most, biological processes. This fact has motivated the development of a variety of experimental methods for the identification of protein-protein interaction (PPI) networks. Leveraging PPI data available in the STRING database, we use a network-based statistical learning methods to infer the putative functions of proteins from the known functions of neighboring proteins on a PPI network. This package identifies such proteins often involved in the same or similar biological functions. The package is freely available at the Bioconductor web site (http://bioconductor.org/packages/PPInfer/).

Nonessential-Nonhub Proteins in the Protein-Protein Interaction Network

2014 ◽  
Vol 934 ◽  
pp. 159-164
Author(s):  
Yun Yuan Dong ◽  
Xian Chun Zhang
Keyword(s):  
Protein Interaction ◽  
Interaction Network ◽  
Clustering Coefficient ◽  
Centrality Measures ◽  
Ppi Network ◽  
Protein Protein Interaction ◽  
Ppi Networks ◽  
Comparison Results ◽  
A Cell ◽  
High Degree

Protein-protein interaction (PPI) networks provide a simplified overview of the web of interactions that take place inside a cell. According to the centrality-lethality rule, hub proteins (proteins with high degree) tend to be essential in the PPI network. Moreover, there are also many low degree proteins in the PPI network, but they have different lethality. Some of them are essential proteins (essential-nonhub proteins), and the others are not (nonessential-nonhub proteins). In order to explain why nonessential-nonhub proteins don’t have essentiality, we propose a new measure n-iep (the number of essential neighbors) and compare nonessential-nonhub proteins with essential-nonhub proteins from topological, evolutionary and functional view. The comparison results show that there are statistical differences between nonessential-nonhub proteins and essential-nonhub proteins in centrality measures, clustering coefficient, evolutionary rate and the number of essential neighbors. These are reasons why nonessential-nonhub proteins don’t have lethality.

A METHOD BASED ON LOCAL DENSITY AND RANDOM WALKS FOR COMPLEXES DETECTION IN PROTEIN INTERACTION NETWORKS

2010 ◽  
Vol 08 (supp01) ◽  
pp. 47-62 ◽  
Author(s):  
LIANG YU ◽  
LIN GAO ◽  
KUI LI
Keyword(s):  
Random Walks ◽  
Protein Interaction ◽  
Local Density ◽  
Protein Complexes ◽  
Biological Significance ◽  
Protein Protein Interaction ◽  
Ppi Networks ◽  
Comprehensive Comparison ◽  
Attachment Proteins ◽  
Two Stages

In this paper, we present a method based on local density and random walks (LDRW) for core-attachment complexes detection in protein-protein interaction (PPI) networks whether they are weighted or not. Our LDRW method consists of two stages. Firstly, it finds all the protein-complex cores based on local density of subnetwork. Then it uses random walks with restarts for finding the attachment proteins of each detected core to form complexes. We evaluate the effectiveness of our method using two different yeast PPI networks and validate the biological significance of the predicted protein complexes using known complexes in the Munich Information Center for Protein Sequence (MIPS) and Gene Ontology (GO) databases. We also perform a comprehensive comparison between our method and other existing methods. The results show that our method can find more protein complexes with high biological significance and obtains a significant improvement. Furthermore, our method is able to identify biologically significant overlapped protein complexes.

Heuristic Modularity for Complex Identification in Protein-Protein Interaction Networks

2019 ◽  
pp. 1846-1859
Author(s):  
Amenah H. H. Abdulateef ◽  
Bara'a A. Attea ◽  
Ahmed N. Rashid
Keyword(s):  
Protein Interaction ◽  
Protein Complexes ◽  
Building Blocks ◽  
Detection Accuracy ◽  
Protein Protein Interaction ◽  
Protein Levels ◽  
Cellular Processes ◽  
Ppi Networks ◽  
Protein Protein Interaction Networks ◽  
Different Levels

     Due to the significant role in understanding cellular processes, the decomposition of Protein-Protein Interaction (PPI) networks into essential building blocks, or complexes, has received much attention for functional bioinformatics research in recent years. One of the well-known bi-clustering descriptors for identifying communities and complexes in complex networks, such as PPI networks, is modularity function.   The contribution of this paper is to introduce heuristic optimization models that can collaborate with the modularity function to improve its detection ability. The definitions of the formulated heuristics are based on nodes and different levels of their neighbor properties.  The modularity function and the formulated heuristics are then injected into the mechanism of a single objective Evolutionary Algorithm (EA) tailored specifically to tackle the problem, and thus, to identify possible complexes from PPI networks. In the experiments, different overlapping scores are used to evaluate the detection accuracy in both complex and protein levels. According to the evaluation metrics, the results reveal that the introduced heuristics have the ability to harness the accuracy of the existing modularity while identifying protein complexes in the tested PPI networks.

Identifying Protein Complexes by Combining Network Topology and Biological Characteristics

2016 ◽  
Vol 13 (10) ◽  
pp. 7666-7675 ◽  
Author(s):  
Buwen Cao ◽  
Jiawei Luo ◽  
Cheng Liang ◽  
Shulin Wang
Keyword(s):  
Protein Interaction ◽  
Network Topology ◽  
Protein Complexes ◽  
Positive Interactions ◽  
Data Sets ◽  
Disease Treatment ◽  
Weighting Method ◽  
Protein Protein Interaction ◽  
Ppi Networks ◽  
Physical Interactions

Protein–protein interaction (PPI) data derived from biological experiments include many false-positive interactions which are treated equally as other real physical interactions, thereby complicating the detection of real protein complexes from protein–protein interaction (PPI) networks. In this paper, a new weighting method, named as cwMINE (combined weight of module identification in networks), for detecting protein complexes efficiently in protein interaction networks is presented. cwMINE has a good combination between network topology and biological feature, which can solve false positives efficiently of PPI networks and make discovered protein complexes higher quality. In addition, a new expanding rule during the detection process, namely, expanding coefficient, is developed to filter edges with lower weights. The proposed method is compared with several state- of-the-art algorithms in three yeast PPI networks with two benchmark data sets. The experimental results show that the proposed method outperforms the other algorithms in most datasets in terms of the evaluation metrics. We further validate the effectiveness of our method on a human PPI network constructed from the HPRD dataset to identify important disease-related functional modules and provided valuable indications for disease treatment.

scholarly journals From the static interactome to dynamic protein complexes: Three challenges

2015 ◽  
Vol 13 (02) ◽  
pp. 1571001 ◽  
Author(s):  
Chern Han Yong ◽  
Limsoon Wong
Keyword(s):  
Protein Interactions ◽  
Protein Complexes ◽  
Clustering Algorithms ◽  
Ppi Network ◽  
Protein Protein Interaction ◽  
Static Interaction ◽  
Ppi Networks ◽  
Interaction Screening ◽  
Discovery Algorithms ◽  
Insight Into

Protein interactions and complexes behave in a dynamic fashion, but this dynamism is not captured by interaction screening technologies, and not preserved in protein–protein interaction (PPI) networks. The analysis of static interaction data to derive dynamic protein complexes leads to several challenges, of which we identify three. First, many proteins participate in multiple complexes, leading to overlapping complexes embedded within highly-connected regions of the PPI network. This makes it difficult to accurately delimit the boundaries of such complexes. Second, many condition- and location-specific PPIs are not detected, leading to sparsely-connected complexes that cannot be picked out by clustering algorithms. Third, the majority of complexes are small complexes (made up of two or three proteins), which are extra sensitive to the effects of extraneous edges and missing co-complex edges. We show that many existing complex-discovery algorithms have trouble predicting such complexes, and show that our insight into the disparity between the static interactome and dynamic protein complexes can be used to improve the performance of complex discovery.

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