• 정보처리학회논문지D
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• 제10D권4호
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• pp.679-688
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• 2003

지놈 서열 시퀀싱을 통해 생성되는 원시 데이터에 대한 단백질 기능 및 구조 예측에 사용되는 모티프 데이터베이스들은 원시 데이터들의 폭발적인 성장추세에 맞추어 그 사용빈도가 증가하고 있다. 그러나 이러한 모티프 데이터베이스들은 독자적으로 개발, 발전하여왔고 웹 기반 cross-reference를 이용한 논리적 통합을 추진하여왔기 때문에 이질적인 검색 결과와 복잡한 질의 처리 문제, 중복된 데이터베이스 엔트리 핸들링 문제 등을 갖고 있다. 따라서, 이 논문에서는 이런 문제점들을 개선하기 위하여 물리적인 모티프 자원 통합을 제안하고, 패밀리 기반 단백질 예측 메소드들에 대한 통합 검색 방법을 기술한다. 끝으로 모티프 통합 데이터베이스 구축 및 단백질 모티프 예측 시스템 구현을 통한 결과를 평가한다.

• 대한원격탐사학회:학술대회논문집
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• 대한원격탐사학회 2006년도 Proceedings of ISRS 2006 PORSEC Volume II
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• pp.812-815
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• 2006

Proteins are essential agents for controlling, effecting and modulating cellular functions, and proteins with similar sequences have diverged from a common ancestral gene, and have similar structures and functions. Function prediction of unknown proteins remains one of the most challenging problems in bioinformatics. Recently, various computational approaches have been developed for identification of short sequences that are conserved within a family of closely related protein sequence. Protein function is often correlated with highly conserved motifs. Motif is the smallest unit of protein structure and function, and intends to make core part among protein structural and functional components. Therefore, prediction methods using data mining or machine learning have been developed. In this paper, we describe an approach for protein function prediction of motif-based models using data mining. Our work consists of three phrases. We make training and test data set and construct classifier using a training set. Also, through experiments, we evaluate our classifier with other classifiers in point of the accuracy of resulting classification.

• Journal of the Korean Data and Information Science Society
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• 제17권4호
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• pp.1279-1287
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• 2006

The purpose of this paper is to present a new algorithm for extracting the consensus pattern, or motif from sequence belonging to the same family. Two methods are considered for feature interval partitioning based on equal probability and equal width interval partitioning. C2H2 zinc finger protein and epidermal growth factor protein sequences are used to demonstrate the effectiveness of the proposed algorithm for motif extraction. For two protein families, the equal width interval partitioning method performs better than the equal probability interval partitioning method.

• 한국식물학회:학술대회논문집
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• 한국식물학회 1996년도 제10회 식물생명공학심포지움 고등식물 발생생물학의 최근 진보
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• pp.40-47
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• 1996

The promoters of a variety of plant genes are characterized by the presence of TGACG motif-containing sequences. These genes often exhibit quite diverse expression characteristics and in many case the TGACG-motif has been demonstrated to be essential for expression. Here we report the isolation and characterization of a soybean cDNA that encodes a novel basic/leucine zipper (bZIP) protein, STF1, that specifically interacts with Hex (TGACGTGG) and CRE (TGACGTCA) sequences. This protein contains a bZIP motif at C-teminus and an acidic domain at N-terminus. DNA binding specificities, heterodimer formation, and expression characteristics of STF1 were compared with a soybean TGA1 protein, STGA1. The soybean STF1 interacts with TGACG-sequences containing an ACGT core, while STGA1 requires TGACG as a sufficient binding sequence. The flanking sequences to the TGACG motif affected DNA binding of STF1 siginificantly. The STF1 mRNA is found mainly in dark grown soybean seedling with higher expression in apical and elongating hypocotyl, while STGA1 mRNA is highly abundant in roots of light grown plants. Furthermore, we demonstrate that STF1 heterodimerzes with G-box binding factorss (GBFs) which was not observed with TGA1. The fact that STF1 possesses both distinct DNA binding speficities and heterodimerization properties suggest that STF1 belongs to a new family of plant bZIP proteins which recognize the Hex/CRE motif.

• BMB Reports
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• 제35권6호
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• pp.629-636
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• 2002

Protein kinase CKII (CKII) is required for progression through the cell division cycle. We recently reported that the $\beta$ subunit of protein kinase CKII ($CKII{\beta}$) associates with CKBBP1 that contains the Ring-H2 finger motif in the yeast two-hybrid system. We demonstrate here that the Ring-H2 finger-disrupted mutant of CKBBP1 does not interact with purified $CKII{\beta}$ in vitro, which shows that the Ring-H2 finger motif is critical for direct interaction with $CKII{\beta}$. The CKII holoenzyme is efficiently co-precipitated with the wild-type CKBBP1, but not with the Ring-H2 finger-disrupted CKBBP1, from whole cell extracts when epitope-tagged CKBBP1 is transiently expressed in HeLa cells. Disruption of the Ring-H2 finger motif does not affect the cellular localization of CKBBP1 in HeLa cells. The increased expression of either the wild-type CKBBP1 or Ring-H2 finger-disrupted CKBBP1 does not modulate the protein or the activity levels of CKII in HeLa cells. However, the stable expression of Ring-H2 finger-disrupted CKBBP1 in HeLa cells suppresses cell proliferation and causes the accumulation of the G1/G0 peak of the cell cycle. The Ring-H2 finger motif is required for maximal CKBBP1 phosphorylation by CKII, suggesting that the stable binding of CKBBP1 to CKII is necessary for its efficient phosphorylation. Taken together, these results suggest that the complex formation of $CKII{\beta}$ with CKBBP1 and/or CKII-mediated CKBBP1 phosphorylation is important for the G1/S phase transition of the cell cycle.

• 산업기술연구
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• 제29권B호
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• pp.115-119
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• 2009

Green fluorescent protein (GFPuv) was displayed on the surface of ethanol-producing bacteria Zymomonas mobilis using N-terminal domain of ice nucleation protein (INP) as an anchoring motif. To evaluate the ice nucleation protein as plausible anchor motif in Z. mobilis, GFPuv gene was subcloned into Zymomonas expression vector yielding pBBR1MCS-3/pPDC/INPN/GFPuv plasmid., INP-GFPuv fusion protein was expressed in Z. mobilis and its fluorescence was verified by confocal microscopy. The successful display of GFPuv on Zymomonas mobilis suggest that INP anchor motif could be used for future fusion partner in Z. mobilis strain improvement.

• Bulletin of the Korean Chemical Society
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• 제34권12호
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• pp.3577-3585
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• 2013

Syndecan-4 (heparan sulfate proteoglycan), biologically important in cell-to-cell interactions and tumor suppression, was studied through mutation of the GXXXG motif of its transmembrane domain (Syd4-TM), a motif which governs dimerization. The expression and purification of the mutant (mSyd4-TM) were optimized here to assess the function of the GXXXG motif in the dimerization of Syd4-TM. mSyd4-TM was obtained in M9 minimal media and its oligomerization was identified by SDS PAGE, Circular Dichroism (CD) spectroscopy, mass spectrometry and NMR spectroscopy. The mutant, unlike Syd4-TM, did not form dimers and was observed as monomers. The GXXXG motif of Syd-4TM was shown to be an important structural determinant of its dimerization.

• BMB Reports
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• 제49권6호
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• pp.337-343
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• 2016

Understanding of trafficking, processing, and degradation mechanisms of amyloid precursor protein (APP) is important because APP can be processed to produce β-amyloid (Aβ), a key pathogenic molecule in Alzheimer's disease (AD). Here, we found that APP contains KFERQ motif at its C-terminus, a consensus sequence for chaperone-mediated autophagy (CMA) or microautophagy which are another types of autophagy for degradation of pathogenic molecules in neurodegenerative diseases. Deletion of KFERQ in APP increased C-terminal fragments (CTFs) and secreted N-terminal fragments of APP and kept it away from lysosomes. KFERQ deletion did not abolish the interaction of APP or its cleaved products with heat shock cognate protein 70 (Hsc70), a protein necessary for CMA or microautophagy. These findings suggest that KFERQ motif is important for normal processing and degradation of APP to preclude the accumulation of APP-CTFs although it may not be important for CMA or microautophagy.

• Animal cells and systems
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• 제6권3호
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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.

• 한국전자통신학회논문지
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• 제13권6호
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• pp.1397-1404
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• 2018

입체적 단백질 구조를 이용한 단백질의 분석은 3차원 데이타를 생성하기 위한 기술적인 어려움과 요구되는 높은 비용으로 인해 크게 발전하지 못하였다. 모티프(motif)는 단백질이나 유전자 염기서열의 단편(segment) 정보로 정의된다. 단순성 때문에 모티프는 다양한 분야에서 활발하고 폭넓게 응용되고 있다. 그러나 모티프 자체에 대한 포괄적인 이해와 연구는 미미하다. 이 논문이 가지는 중요성은 인공지능 기법을 활용하여 인간 단백질을 분석하는 방법으로 3가지 측면에서 찾아볼 수 있다. (1) 현재 단백질 데이타 뱅크 (PDB)에 저장된 모든 인간의 단백질 구조를, 이에 상응하는 효소위원회 (EC)의 데이타베이스와 단백질의 구조적 특성에 따른 분류 데이타베이스 (SCOP)를 연동하여, 단백질이 가지는 고유의 특성을 모티프를 응용한 새로운 방법으로 컴퓨터를 이용하여, 분석한 최초의 종합적이고 심층적인 인간 단백질의 분석법이다. (2) 본 연구는 모티프에 의해 생성된 새로운 단백질의 특성을 계층적 클러스터링을 이용하여 단백질이 가지는 고유한 특징을 패턴 분석법과 통계 그리고 단백질 기능 분석의 세 가지 범주로 단백질의 특성을 분석한다. (3) 임의로 생성된 모티프가 단백질 내에서 가지는 빈도에 대해 빅 데이타를 활용하여 모티프의 길이를 다양화시킴과 동시에 접촉 염기와 단백질의 기능을 다각도로 분석할 수 있는 임의 모티프 빈도 (RMF)를 이용한 단백질 분석 방법론을 제안한다.