• BMB Reports
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• v.34 no.5
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• pp.452-456
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• 2001

Surface plasmon resonance has been used for a biospecific interaction analysis between two macromolecules in real time. Determination of an antibody that is capable of specifically interacting with the native form of antigen is very useful for many biological and medical applications. Twenty monoclonal antibodies against the $\alpha$ subunit of E. coli DNA polymerase III were screened for specifically recognizing the native form of protein using surface plasmon resonance. Only four monoclonal antibodies among them specifically recognized the native $\alpha$ protein, although all of the antibodies were able to specifically interact with the denatured $\alpha$ subunit. These antibodies failed to interfere with the interaction between the $\tau$ and $\alpha$ subunits that were required for dimerization of the two polymerases at the DNA replication fork. This real-time analysis using surface plasmon resonance provides an easy method to screen antibodies that are capable of binding to the native form of the antigen molecule and determine the biological interaction between the two molecules.

• Genomics & Informatics
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• v.5 no.3
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• pp.133-136
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• 2007

The Gene Set network viewer (GSnet) visualizes the functional enrichment of a given gene set with a protein interaction network and is implemented as a plug-in for the Cytoscape platform. The functional enrichment of a given gene set is calculated using a hypergeometric test based on the Gene Ontology annotation. The protein interaction network is estimated using public data. Set operations allow a complex protein interaction network to be decomposed into a functionally-enriched module of interest. GSnet provides a new framework for gene set analysis by integrating a priori knowledge of a biological network with functional enrichment analysis.

• 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.

• Proceedings of the KAIS Fall Conference
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• 2010.05b
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• pp.1197-1200
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• 2010

Post-genomic 시대에 접어들면서 단백질의 기능의 주석이 중요한 문제로 떠오르기 시작하였다. 이런 단백질 기능을 예측하기 위해 단백질 상호작용(Protein-Protein interaction) 데이터를 이용한 방법들이 지난 10여 년간 발표되어왔다. 단백질 상호작용(Protein-Protein interaction) 데이터는 단백질들 간의 서열 등의 특징을 이용해 상호간의 연결 관련성이 있는 단백질끼리의 관계를 네트워크로 나타낸 자료이다. 현재 이러한 단백질 상호작용(Protein-Protein interaction) 데이터들은 MIPS, DIP, BioGrid등 약 5~6군데에서 제공되고 있다. 각각의 데이터는 다른 형식을 가지고 있고, 중복되는 정보도 포함하고 있다. 여러 연구 방법에서 데이터를 사용할 때 한군데에서만 추출하기 보다는 여러 데이터에서 추출하는 경우가 많기 때문에 다른 형식의 데이터를 이용하는데 불필요한 수고가 들어가게 된다. 때문에 여러군데의 데이터를 한 가지 형식으로 맞추어 통합적으로 구축하여 연구 시 데이터 사용에 용이하도록 설계 하였다. 또한 발표된 단백질 기능 예측 방법에 대한 정리를 통해 앞으로의 연구를 하는데 있어서 필요한 자료를 얻고 열람할 수 있도록 설계하였다. 이를 통해 관련 연구를 하거나 관심이 있는 사람들의 데이터를 검색하는데 많은 도움이 될 것이다.

• Molecules and Cells
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• v.27 no.3
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• pp.271-277
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• 2009

Proteins interact with each other within a cell, and those interactions give rise to the biological function and dynamical behavior of cellular systems. Generally, the protein interactions are temporal, spatial, or condition dependent in a specific cell, where only a small part of interactions usually take place under certain conditions. Recently, although a large amount of protein interaction data have been collected by high-throughput technologies, the interactions are recorded or summarized under various or different conditions and therefore cannot be directly used to identify signaling pathways or active networks, which are believed to work in specific cells under specific conditions. However, protein interactions activated under specific conditions may give hints to the biological process underlying corresponding phenotypes. In particular, responsive functional modules consist of protein interactions activated under specific conditions can provide insight into the mechanism underlying biological systems, e.g. protein interaction subnetworks found for certain diseases rather than normal conditions may help to discover potential biomarkers. From computational viewpoint, identifying responsive functional modules can be formulated as an optimization problem. Therefore, efficient computational methods for extracting responsive functional modules are strongly demanded due to the NP-hard nature of such a combinatorial problem. In this review, we first report recent advances in development of computational methods for extracting responsive functional modules or active pathways from protein interaction network and microarray data. Then from computational aspect, we discuss remaining obstacles and perspectives for this attractive and challenging topic in the area of systems biology.

• Korean Journal of Food Science and Technology
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• v.19 no.2
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• pp.89-96
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• 1987

The denaturation mechanism of the protein during heating of myosin and paramyosin extracted from the ordinary muscle of yellowtail (Seriola qrinqueradits) and the adductor muscle of whelk (Neptunea arthritica cuming) were investigated by analyzing the hydrophobicity, solubility, SH group and protein-protein interaction. The free hydrophobic residue of the two proteins were increased by increase of heating temperature up to $65^{\circ}C$ and then decreased for further temperature raise. The protein-protein interaction was proportional to the increment of the free hydrophobic residue. The aggregation of protein was begun from $65^{\circ}C$ with the decrease of the free hydrophobic residues. The results of Arrhenius equation for the data on proteinprotein interaction showed that the denaturation course was made up with multi-steps in the myosin and two-steps in the paramyosin. The number of free hydrophobic residue and SH group, solubility and protein-protein interaction were significantly differed with the denaturation temperature (p<0.01).

• Journal of the Korean Magnetic Resonance Society
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• v.15 no.1
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• pp.80-89
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• 2011

3D structures of STAM1 UIM-ubiquitin complex were presented to predict and analyze the interaction between UIM and ubiquitin. To generate the protein-peptide complex structure, the RosettaDock method was used with and without NMR restraints. High resolution complex structure was acquired successfully and evaluated electrostatic interaction in the protein-peptide binding with several charged residues at the binding site. From docking results, the Rosettadock method could be useful to acquire essential information of protein-protein or protein-peptide interaction with minimal biological evidences.

• Journal of Integrative Natural Science
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• v.11 no.1
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• pp.9-13
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• 2018

KiSS1-derived peptide receptor, a GPCR protein, binds with the hormone Kisspeptin plays a major role in the neuroendocrine regulation of reproduction. It is important in the onset of puberty and triggers the release of gonadotrophin-releasing hormone. It is a potential drug target for the disorders related to GnRH, hence, analysing the structural features of the receptor becomes important. The three dimensional of the receptor modelled in a previous study was utilised. In this study, we have analysed the protein - protein interaction of the receptor with Kisspeptin 10 and 15. The study revealed the important residues which are involved in the interaction. The result of this study could be helpful in understanding the mechanism of Kiss1 receptor activation and the pathophysiology of the disorders related to the receptor.

• Animal cells and systems
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• v.6 no.3
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• pp.277-282
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• 2002

Topoisomearse II is an essential enzyme in all organisms with several independent roles in DNA metabolism. Recently, it has been demonstrated that the C-terminal region of topoisomerases II is associated with hetero-logous protein-protein interactions in human and yeast. In this study, we identified that RTP1, a rat homologue of EIA binding protein BS69, is another topoisomerae II interacting protein by yeast two-hybrid screening. RTP1 has an E1A-binding domain and a MYND motif, which are known to be required for transcriptional regulation by binding to other proteins and interaction with the leucine zipper motif of topoisomerase II. The physical interaction between RTP1 and topoisomerase ll$\alpha$ was examined by GST pull-down assay in vitro. The expression level of RTP1 peaks in S phase as that of topoisomerase ll$\alpha$. These results suggest that the interaction between topoisomerase ll$\alpha$ and RTP1 might play an important role in regulating the transcription of genes involved in DNA metabolism in higher eukaryotes.

• Textile Coloration and Finishing
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• v.19 no.4
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• pp.32-37
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• 2007

In this study, we have obtained the protein patterns using the membrane patterning of soft-lithography technique. The rapid detection of protein including bovine serum albumin (BSA) was resulted from the interaction with 1,3-bisdicyanovinylindane. For the proof of the interaction between BSA and dye, the UV-vis absorption spectra of BSA and dye were observed at 278 nm and 580 nm, respectively. As expected, the absorption spectrum of the interaction between BSA and dye was observed at 584nm. The absorption spectrum of the interaction was red-shifted. In addition, the optical images of the selectively reacted protein patterns showed the distinctive change of patterned color at different pH conditions. Because the dye has negative charges, the charge of BSA at different pH conditions could influence the interaction behavior between dye and BSA. Therefore, in the case of pH 7, the selectively patterned protein substrates obtained deep blue color pattern caused by electrostatic interaction between negative charges of the dye and positive charges of the BSA. However, in the case of pH 10, selectively patterned protein substrates obtained light blue color pattern because the electrostatic interaction was relatively lower than pH 7 due to the change of overall charge distribution of BSA.