• Proceedings of the Korean Society for Bioinformatics Conference
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• 2005.09a
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• pp.431-436
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• 2005

Living cells are sustained not by individual activities but rather by coordinated summative efforts of different biological functional modules. While recent research works have focused largely on finding individual functional modules, this paper attempts to explore the connections or relationships between different cellular functions through cross-function domain interaction maps. Exploring such a domain interaction map can help understand the underlying inter-function communication mechanisms. To construct a cross-function domain interaction map from existing genome-wide protein-protein interaction datasets, we propose a two-step procedure. First, we infer conserved domain-domain interactions from genome-wide protein-protein interactions of yeast, worm and fly. We then build a cross-function domain interaction map that shows the connections of different functions through various conserved domain interactions. The domain interaction maps reveal that conserved domain-domain interactions can be found in most detected cross-functional relationships and a f9w domains play pivotal roles in these relationships. Another important discovery in the paper is that conserved domains correspond to highly connected protein hubs that connect different functional modules together.

• 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.

• YAKHAK HOEJI
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• v.35 no.6
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• pp.461-465
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• 1991

Silica-based gel filtration chromatography has been used to characterize molecular weight of proteins. However, the molecular weight measured by this method was distorted by protein-silica interactions like hydrophobic and electrostatic forces. Therefore, we characterized protein-silica interaction using two forms of phytochrome (124 kDa) having different hydrophobicity and surface charge. PH and ionic strength affected the retention time of phytochrome suggesting that electrostatic force is the major interaction between protein and silica surface.

• Proceedings of the Korean Society of Computer Information Conference
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• 2009.01a
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• pp.77-84
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• 2009

Intracellular signal transduction is achieved by protein-protein interaction. In this paper, we suggest performance algorithm based on Yeast protein-protein interaction and protein location information. We compare if pathways predicted with high valued weights indicate similar tendency with pathways provided in KEGG.

• Journal of KIISE:Software and Applications
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• v.36 no.10
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• pp.851-860
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• 2009

Recently, among the computational methods of protein-protein interaction prediction, vast amounts of domain based methods originated from domain-domain relation consideration have been developed. However, it is true that multi domains collaboration is avowedly ignored because of computational complexity. In this paper, we implemented a protein interaction prediction system based the Interaction Significance matrix, which quantified an influence of domain combination pair on a protein interaction. Unlike conventional domain combination methods, IS matrix contains weighted domain combinations and domain combination pair power, which mean possibilities of domain collaboration and being the main body on a protein interaction. About 63% of sensitivity and 94% of specificity were measured when we use interaction data from DIP, IntAct and Pfam-A as a domain database. In addition, prediction accuracy gradually increased by growth of learning set size, The prediction software and learning data are currently available on the web site.

• The KIPS Transactions:PartB
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• v.13B no.1 s.104
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• pp.1-6
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• 2006

The prediction of protein function basically make use of a protein-protein interaction map based on the concept of guilt-by-association. The method however cannot determine the functions of proteins in case that the target protein does not interact with proteins with known functions directly. This paper studies protein function prediction considering the given problem as a K-class classification problem and proposes a predictive approach utilizing a modular neural network. The proposed method uses interaction data and protein related attributes as well. The experimental results demonstrate that the proposed approach can predict the functional roles of Yeast proteins whose interaction knowledge is not known and shows better performance than the graph-based models that use protein interaction data.

• Journal of KIISE:Computer Systems and Theory
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• v.33 no.5
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• pp.267-281
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• 2006

PPI(Protein-Protein Interaction) data has information about the organism has maintained a life with some kind of mechanism. So, it is used in study about cure research back, cause of disease, and new medicine development. This PPI data has been increased by geometric progression because high throughput methods are developed such as Yeast-two-hybrid, Mass spectrometry, and Correlated mRNA expression. So, it is impossible that a person directly manage and analyze PPI data. Fortunately, PPI data is able to abstract the graph which has proteins as nodes, interactions as edges. Consequently, Graph theory plentifully researched from the computer science until now is able to be applied to PPI data successfully. In this paper, we introduce Proteinca(PROTEin INteraction CAbaret) workbench system for easily managing, analyzing and visualizing PPI data. Proteinca assists the user understand PPI data intuitively as visualizing a PPI data in graph and provide various analytical function on graph theory. And Protenica provides a simplified visualization with gravity-rule.

• Journal of Microbiology and Biotechnology
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• v.12 no.2
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• pp.286-291
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• 2002

Histone deacetylase I (HDAC1) works as one of the components in a nucleosome remodeling (NuRD) complex that consists of several proteins, including metastasis-associated protein 1 (MTA1). Since the protein-protein interaction of HDAC1 and MTA1 would appear to be important for both the integrity and functionality of the HDAC1 complex, the interruption of the HDAC1 and MTA1 interaction may be an efficient way to regulate the biological function of the HDAC1 complex. Based on this idea, a yeast two-hybrid system was constructed with HDAC1 and MTA1 expressing vectors in the DNA binding and activation domains, respectively. To verify the efficiency of the assay system, 3,500 microbial metabolite libraries were tested using the paper disc method, and KB0699 was found to inhibit the HDAC1 and MTA1 interaction without any toxicity to the wild-type yeast. Furthermore, KB0699 blocked the interaction of HDAC1 and MTA1 in an in vitro GST pull down assay and induced morphological changes in B16/BL6 melanoma cells, indicating the interruption of the HDAC1 complex function. Accordingly, these results demonstrated that the yeast assay strain developed in this study could be a valuable tool for the isolation of a HDAC1 complex disruptor.

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2003.10a
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• pp.7-16
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• 2003

In this paper, we propose a probabilistic framework to predict the interaction probability of proteins. The notion of domain combination and domain combination pair is newly introduced and the prediction model in the framework takes domain combination pair as a basic unit of protein interactions to overcome the limitations of the conventional domain pair based prediction systems. The framework largely consists of prediction preparation and service stages. In the prediction preparation stage, two appearance pro-bability matrices, which hold information on appearance frequencies of domain combination pairs in the interacting and non-interacting sets of protein pairs, are constructed. Based on the appearance probability matrix, a probability equation is devised. The equation maps a protein pair to a real number in the range of 0 to 1. Two distributions of interacting and non-interacting set of protein pairs are obtained using the equation. In the prediction service stage, the interaction probability of a protein pair is predicted using the distributions and the equation. The validity of the prediction model is evaluated fur the interacting set of protein pairs in Yeast organism and artificially generated non-interacting set of protein pairs. When 80% of the set of interacting protein pairs in DIP database are used as foaming set of interacting protein pairs, very high sensitivity(86%) and specificity(56%) are achieved within our framework.

• Journal of KIISE:Computing Practices and Letters
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• v.11 no.6
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• pp.503-513
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• 2005

With the recognition of the importance of computational approach for protein-protein interaction prediction, many techniques have been developed to computationally predict protein-protein interactions. However, few techniques are actually implemented and announced in service form for general users to readily access and use the techniques. In this paper, we design and implement a protein interaction prediction service system based on the domain combination based protein-protein interaction prediction technique, which is known to show superior accuracy to other conventional computational protein-protein interaction prediction methods. In the prediction accuracy test of the method, high sensitivity($77\%$) and specificity($95\%$) are achieved for test protein pairs containing common domains with teaming sets of proteins in a Yeast. The stability of the method is also manifested through the testing over DIP CORE, HMS-PCI, and TAP data. Performance, openness and flexibility are the major design goals and they are achieved by adopting parallel execution techniques, web Services standards, and layered architecture respectively. In this paper, several representative user interfaces of the system are also introduced with comprehensive usage guides.