• Title/Summary/Keyword: protein-protein interactions network

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Prediction of Protein-Protein Interactions from Sequences using a Correlation Matrix of the Physicochemical Properties of Amino Acids

  • Kopoin, Charlemagne N'Diffon;Atiampo, Armand Kodjo;N'Guessan, Behou Gerard;Babri, Michel
    • International Journal of Computer Science & Network Security
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    • v.21 no.3
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    • pp.41-47
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    • 2021
  • Detection of protein-protein interactions (PPIs) remains essential for the development of therapies against diseases. Experimental studies to detect PPI are longer and more expensive. Today, with the availability of PPI data, several computer models for predicting PPIs have been proposed. One of the big challenges in this task is feature extraction. The relevance of the information extracted by some extraction techniques remains limited. In this work, we first propose an extraction method based on correlation relationships between the physicochemical properties of amino acids. The proposed method uses a correlation matrix obtained from the hydrophobicity and hydrophilicity properties that it then integrates in the calculation of the bigram. Then, we use the SVM algorithm to detect the presence of an interaction between 2 given proteins. Experimental results show that the proposed method obtains better performances compared to the approaches in the literature. It obtains performances of 94.75% in accuracy, 95.12% in precision and 96% in sensitivity on human HPRD protein data.

A Machine Learning Based Method for the Prediction of G Protein-Coupled Receptor-Binding PDZ Domain Proteins

  • Eo, Hae-Seok;Kim, Sungmin;Koo, Hyeyoung;Kim, Won
    • Molecules and Cells
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    • v.27 no.6
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    • pp.629-634
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    • 2009
  • G protein-coupled receptors (GPCRs) are part of multi-protein networks called 'receptosomes'. These GPCR interacting proteins (GIPs) in the receptosomes control the targeting, trafficking and signaling of GPCRs. PDZ domain proteins constitute the largest protein family among the GIPs, and the predominant function of the PDZ domain proteins is to assemble signaling pathway components into close proximity by recognition of the last four C-terminal amino acids of GPCRs. We present here a machine learning based approach for the identification of GPCR-binding PDZ domain proteins. In order to characterize the network of interactions between amino acid residues that contribute to the stability of the PDZ domain-ligand complex and to encode the complex into a feature vector, amino acid contact matrices and physicochemical distance matrix were constructed and adopted. This novel machine learning based method displayed high performance for the identification of PDZ domain-ligand interactions and allowed the identification of novel GPCR-PDZ domain protein interactions.

Extraction of Protein-Protein Interactions based on Convolutional Neural Network (CNN) (Convolutional Neural Network (CNN) 기반의 단백질 간 상호 작용 추출)

  • Choi, Sung-Pil
    • KIISE Transactions on Computing Practices
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    • v.23 no.3
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    • pp.194-198
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    • 2017
  • In this paper, we propose a revised Deep Convolutional Neural Network (DCNN) model to extract Protein-Protein Interaction (PPIs) from the scientific literature. The proposed method has the merit of improving performance by applying various global features in addition to the simple lexical features used in conventional relation extraction approaches. In the experiments using AIMed, which is the most famous collection used for PPI extraction, the proposed model shows state-of-the art scores (78.0 F-score) revealing the best performance so far in this domain. Also, the paper shows that, without conducting feature engineering using complicated language processing, convolutional neural networks with embedding can achieve superior PPIE performance.

Computational approaches for prediction of protein-protein interaction between Foot-and-mouth disease virus and Sus scrofa based on RNA-Seq

  • Park, Tamina;Kang, Myung-gyun;Nah, Jinju;Ryoo, Soyoon;Wee, Sunghwan;Baek, Seung-hwa;Ku, Bokkyung;Oh, Yeonsu;Cho, Ho-seong;Park, Daeui
    • Korean Journal of Veterinary Service
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    • v.42 no.2
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    • pp.73-83
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    • 2019
  • Foot-and-Mouth Disease (FMD) is a highly contagious trans-boundary viral disease caused by FMD virus, which causes huge economic losses. FMDV infects cloven hoofed (two-toed) mammals such as cattle, sheep, goats, pigs and various wildlife species. To control the FMDV, it is necessary to understand the life cycle and the pathogenesis of FMDV in host. Especially, the protein-protein interaction between FMDV and host will help to understand the survival cycle of viruses in host cell and establish new therapeutic strategies. However, the computational approach for protein-protein interaction between FMDV and pig hosts have not been applied to studies of the onset mechanism of FMDV. In the present work, we have performed the prediction of the pig's proteins which interact with FMDV based on RNA-Seq data, protein sequence, and structure information. After identifying the virus-host interaction, we looked for meaningful pathways and anticipated changes in the host caused by infection with FMDV. A total of 78 proteins of pig were predicted as interacting with FMDV. The 156 interactions include 94 interactions predicted by sequence-based method and the 62 interactions predicted by structure-based method using domain information. The protein interaction network contained integrin as well as STYK1, VTCN1, IDO1, CDH3, SLA-DQB1, FER, and FGFR2 which were related to the up-regulation of inflammation and the down-regulation of cell adhesion and host defense systems such as macrophage and leukocytes. These results provide clues to the knowledge and mechanism of how FMDV affects the host cell.

Evolutionary Analyses of Hanwoo (Korean Cattle)-Specific Single-Nucleotide Polymorphisms and Genes Using Whole-Genome Resequencing Data of a Hanwoo Population

  • Lee, Daehwan;Cho, Minah;Hong, Woon-young;Lim, Dajeong;Kim, Hyung-Chul;Cho, Yong-Min;Jeong, Jin-Young;Choi, Bong-Hwan;Ko, Younhee;Kim, Jaebum
    • Molecules and Cells
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    • v.39 no.9
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    • pp.692-698
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    • 2016
  • Advances in next generation sequencing (NGS) technologies have enabled population-level studies for many animals to unravel the relationships between genotypic differences and traits of specific populations. The objective of this study was to perform evolutionary analysis of single nucleotide polymorphisms (SNP) in genes of Korean native cattle Hanwoo in comparison to SNP data from four other cattle breeds (Jersey, Simmental, Angus, and Holstein) and four related species (pig, horse, human, and mouse) obtained from public databases through NGS-based resequencing. We analyzed population structures and differentiation levels for the five cattle breeds and estimated species-specific SNPs with their origins and phylogenetic relationships among species. In addition, we identified Hanwoo-specific genes and proteins, and determined distinct changes in protein-protein interactions among five species (cattle, pig, horse, human, mouse) in the STRING network database by additionally considering indirect protein interactions. We found that the Hanwoo population was clearly different from the other four cattle populations. There were Hanwoo-specific genes related to its meat trait. Protein interaction rewiring analysis also confirmed that there were Hanwoo-specific protein-protein interactions that might have contributed to its unique meat quality.

Systems biology of virus-host signaling network interactions

  • Xue, Qiong;Miller-Jensen, Kathryn
    • BMB Reports
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    • v.45 no.4
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    • pp.213-220
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    • 2012
  • Viruses have evolved to manipulate the host cell machinery for virus propagation, in part by interfering with the host cellular signaling network. Molecular studies of individual pathways have uncovered many viral host-protein targets; however, it is difficult to predict how viral perturbations will affect the signaling network as a whole. Systems biology approaches rely on multivariate, context-dependent measurements and computational analysis to elucidate how viral infection alters host cell signaling at a network level. Here we describe recent advances in systems analyses of signaling networks in both viral and non-viral biological contexts. These approaches have the potential to uncover virus- mediated changes to host signaling networks, suggest new therapeutic strategies, and assess how cell-to-cell variability affects host responses to infection. We argue that systems approaches will both improve understanding of how individual virus-host protein interactions fit into the progression of viral pathogenesis and help to identify novel therapeutic targets.

Protein Interaction Databases and Its Application (단백질 상호작용 데이터베이스 현황 및 활용 방안)

  • Kim, Min Kyung;Park, Hyun Seok
    • IMMUNE NETWORK
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    • v.2 no.3
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    • pp.125-132
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    • 2002
  • In the past, bioinformatics was often regarded as a difficult and rather remote field, practiced only by computer scientists and not a practical tool available to biologists. However, the various on-going genome projects have had a serious impact on biological sciences in various ways and now there is little doubt that bioinformatics is an essential part of the research environment, with a wealth of biological information to analyze and predict. Fully sequenced genomes made us to have additional insights into the functional properties of the encoded proteins and made it possible to develop new tools and schemes for functional biology on a proteomic scale. Among those are the yeast two-hybrid system, mass spectrometry and microarray: the technology of choice to detect protein-protein interactions. These functional insights emerge as networks of interacting proteins, also known as "pathway informatics" or "interactomics". Without exception it is no longer possible to make advances in the signaling/regulatory pathway studies without integrating information technologies with experimental technologies. In this paper, we will introduce the databases of protein interaction worldwide and discuss several challenging issues regarding the actual implementation of databases.

Network Analyses of Gene Expression following Fascin Knockdown in Esophageal Squamous Cell Carcinoma Cells

  • Du, Ze-Peng;Wu, Bing-Li;Xie, Jian-Jun;Lin, Xuan-Hao;Qiu, Xiao-Yang;Zhan, Xiao-Fen;Wang, Shao-Hong;Shen, Jin-Hui;Li, En-Min;Xu, Li-Yan
    • Asian Pacific Journal of Cancer Prevention
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    • v.16 no.13
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    • pp.5445-5451
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    • 2015
  • Fascin-1 (FSCN1) is an actin-bundling protein that induces cell membrane protrusions, increases cell motility, and is overexpressed in various human epithelial cancers, including esophageal squamous cell carcinoma (ESCC). We analyzed various protein-protein interactions (PPI) of differentially-expressed genes (DEGs), in fascin knockdown ESCC cells, to explore the role of fascin overexpression. The node-degree distributions indicated these PPI sub-networks to be characterized as scale-free. Subcellular localization analysis revealed DEGs to interact with other proteins directly or indirectly, distributed in multiple layers of extracellular membrane-cytoskeleton/ cytoplasm-nucleus. The functional annotation map revealed hundreds of significant gene ontology (GO) terms, especially those associated with cytoskeleton organization of FSCN1. The Random Walk with Restart algorithm was applied to identify the prioritizations of these DEGs when considering their relationship with FSCN1. These analyses based on PPI network have greatly expanded our comprehension of the mRNA expression profile following fascin knockdown to future examine the roles and mechanisms of fascin action.

Analysis of a Large-scale Protein Structural Interactome: Ageing Protein structures and the most important protein domain

  • Bolser, Dan;Dafas, Panos;Harrington, Richard;Schroeder, Michael;Park, Jong
    • Proceedings of the Korean Society for Bioinformatics Conference
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    • 2003.10a
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    • pp.26-51
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    • 2003
  • Large scale protein interaction maps provide a new, global perspective with which to analyse protein function. PSIMAP, the Protein Structural Interactome Map, is a database of all the structurally observed interactions between superfamilies of protein domains with known three-dimensional structure in thePDB. PSIMAP incorporates both functional and evolutionary information into a single network. It makes it possible to age protein domains in terms of taxonomic diversity, interaction and function. One consequence of it is to predict the most important protein domain structure in evolution. We present a global analysis of PSIMAP using several distinct network measures relating to centrality, interactivity, fault-tolerance, and taxonomic diversity. We found the following results: ${\bullet}$ Centrality: we show that the center and barycenter of PSIMAP do not coincide, and that the superfamilies forming the barycenter relate to very general functions, while those constituting the center relate to enzymatic activity. ${\bullet}$ Interactivity: we identify the P-loop and immunoglobulin superfamilies as the most highly interactive. We successfully use connectivity and cluster index, which characterise the connectivity of a superfamily's neighbourhood, to discover superfamilies of complex I and II. This is particularly significant as the structure of complex I is not yet solved. ${\bullet}$ Taxonomic diversity: we found that highly interactive superfamilies are in general taxonomically very diverse and are thus amongst the oldest. This led to the prediction of the oldest and most important protein domain in evolution of lift. ${\bullet}$ Fault-tolerance: we found that the network is very robust as for the majority of superfamilies removal from the network will not break up the network. Overall, we can single out the P-loop containing nucleotide triphosphate hydrolases superfamily as it is the most highly connected and has the highest taxonomic diversity. In addition, this superfamily has the highest interaction rank, is the barycenter of the network (it has the shortest average path to every other superfamily in the network), and is an articulation vertex, whose removal will disconnect the network. More generally, we conclude that the graph-theoretic and taxonomic analysis of PSIMAP is an important step towards the understanding of protein function and could be an important tool for tracing the evolution of life at the molecular level.

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