• 한국지능시스템학회논문지
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• 제21권2호
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• pp.276-282
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• 2011

CoreNet은 한-중-일 다국어 텍스트의 분석, 언어 간 변환을 포함한 자연어처리에 유용한 자원이다. CoreNet의 보다 광범위한 분야 및 응용에의 활용을 장려하고 다국어 어휘의미망으로서의 국제적 위상을 제고하기 위해 SUMO에 연결하는 작업을 하였다. CoreNet과 SUMO를 매핑하기 위해 간접 매핑과 직접 매핑 방법을 모두 사용하였는데, CoreNet-KorLex-PWN-SUMO에 이르는 간접 매핑 작업을 통하여 한국어 중심의 CoreNet과 영어로 기술된 SUMO의 언어 간 변환의 어려움을 완화하고 CoreNet 개념에 대응하는 SUMO 클래스의 재현율을 극대화하였다.

• Journal of Plant Biotechnology
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• 제39권4호
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• pp.235-241
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• 2012

식물체에서 sumoylation 기작은 성장 및 발달에 중요한 기능을 수행할 것이다. 특히, SUMO E3 ligase는 SUMO 단백질을 목적 단백질로 전달해주는 마지막 단계의 sumoylation 기작 구성요소이며, 다양한 신호전달에 특이성을 나타내는 것으로 보고되고 있다. 본 연구에서는 벼에서 SUMO E3 ligase, SIZ1 유전자에 T-DNA가 삽입된 Ossiz1-2 돌연변이 식물체를 분석하였다. 그리고, OsSIZ1 단백질이 OsSUMO1 단백질과 상호작용함으로써 OsSIZ1이 SUMO E3 ligase의 기능을 수행할 것으로 예측하였다. Ossiz1-2 돌연변이 식물체는 형태학적으로 발달과 성장의 다양한 부분에서 미성숙상태로 유지됨이 보였다. 특히, 야생형인 동진벼와 비교하여 초장의 성장 및 등숙율에서 상당히 낮은 정도를 보여 주었다. 이와 같이, 벼에서 SUMO E3 ligase로써 OsSIZ1 단백질의 생리학적인 기능은 성장과 발달 그리고, 수확량에 관여하는 단백질을 sumoylation 시키는 기작에서 역할을 수행할 것으로 사려된다.

• Journal of Crop Science and Biotechnology
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• 제11권1호
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• pp.1-6
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• 2008

The covalent conjugation of SUMO(Small Ubiquitin-related MOdifier) protein to its substrates regulates numerous cellular processes, including protein stability and activity in eukaryotes as well as in plants. In this present review, we summarize biochemical aspects of SUMO conjugation and deconjugation and the functions of SUMO and sumoylation-related proteins in Arabidopsis and other plants. In particular, we provide an overview of the roles of the SUMO in widely different biological processes including the ABA response, floral induction, pathogen defense, abiotic stresses and hormone signaling. Furthermore, we explore the possible roles of SUMO in embryo and seed development.

• 운동영양학회지
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• 제25권3호
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• pp.36-43
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• 2021

[Purpose] Exercise is a key factor in preventing obesity and metabolic syndrome. Sumo wrestlers increase their body size from childhood for athletic advantage; however, the risk of metabolic syndrome in junior sumo wrestlers is undetermined. Preventive measures against pediatric obesity should be initiated during childhood to prevent obesity in adulthood, considering its high global incidence. We comparatively evaluated the risk factors for metabolic syndrome in junior sumo wrestlers and children with obesity. [Methods] We enrolled 70 male children (age 9-17 years [sumo group, n = 14] and 9-14 years [other sports and non-exercise groups, n = 28 each]) and evaluated their anthropometric parameters (height, weight, body mass index z-score, obesity rate, waist circumference, waist to height ratio) and hematological parameters (total, low-density, high-density, and non-high-density lipoprotein-cholesterol; triglycerides; plasma glucose, and glycated hemoglobin levels). [Results] The BMI z-score, obesity rate, waist circumference (p < 0.05, along with the non-exercise group), and systolic blood pressure were significantly higher and the high-density cholesterol level was lower in the sumo group than in the other sports group (p < 0.05). The waist to height ratio was significantly higher in the non-exercise group than in the other sports group (p < 0.05). No significant difference was found in other blood lipid, plasma glucose (significantly lower level than the reference range in the sumo group, p < 0.05), and glycated hemoglobin (within the reference range in all groups) levels among the three groups. [Conclusion] Junior sumo wrestlers had a larger body size and higher blood pressure than children with obesity who exercised regularly. This provides direction for future research into targeted preventive interventions against metabolic syndrome for junior sumo wrestlers with large body size.

• 한국육종학회지
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• 제42권4호
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• pp.339-343
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• 2010

Post-translational covalent modifications by small molecules or peptides remodel target proteins. One such modification, made by ubiquitin or small ubiquitin-related modifier (SUMO), is a rapidly expanding field in cell signaling pathways. Ubiquitin attachment controls the turnover and degradation of target proteins while SUMO conjugation regulates their activity and function. Recent studies report many examples of cross-talk between ubiquitin and SUMO pathways, indicating that the boundary is no longer clear. Here, we review recent progress concerning how ubiquitin and SUMO participate in new regulatory roles in plant cell, and how ubiquitination and sumoylation control plant growth and development.

• International Journal of Industrial Entomology and Biomaterials
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• 제32권2호
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• pp.90-97
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• 2016

The major structural proteins of porcine reproductive and respiratory syndrome virus (PRRSV) are derived from ORFs 4, 5, and 6. They have been considered very important to arouse the humoral and cellular immune responses against PRRSV infection and proposed to be the excellent candidate proteins in the design of PRRS bioengineering vaccine. However, the PRRSV structural proteins are produced in low levels in the infected cells because it forms insoluble protein and possesses several transmembrane regions. To overcome this problem, we fused the ORF4, ORF5, and ORF6 with SUMO (small ubiquitin-related modifier). The resulting fusion protein SUMO-ORF4, -ORF5, and -ORF6 were highly expressed in Bm5 cells. The level of protein expression using the Bombyx mori larvae was higher than that using Bm5 cells. In addition, fusion to SUMOstar, which is not processed by native SUMO proteases, significantly enhanced protein expression levels compared to SUMO fusion. This study demonstrated that SUMO or SUMOstar, when fused with PRRSV structural proteins, was able to promote its soluble expression. This may be a better method to produce PRRSV structural proteins for vaccine development.

• 한국컴퓨터정보학회:학술대회논문집
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• 한국컴퓨터정보학회 2017년도 제55차 동계학술대회논문집 25권1호
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• pp.193-194
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• 2017

본 논문에서는 VANET 환경에서 SUMO와 ns-3를 이용하여 속도 변화에 따라 AODV 프로토콜의 통신에 대해 모의실험을 수행하였다. 해당 시뮬레이션 결과에 따르면, AODV 라우팅 프로토콜은 VANET 환경에서 차량이 일정 속도 이상 빨라지게 되면 통신율이 급격히 하락함을 볼 수 있었다.

• BMB Reports
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• 제43권2호
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• pp.103-109
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• 2010

Modification of proteins by the reversible covalent addition of the small ubiquitin like modifier (SUMO) protein has important consequences affecting target protein stability, sub-cellular localization, and protein-protein interactions. SUMOylation involves a cascade of enzymatic reactions, which resembles the process of ubiquitination. In this study, we characterized the SUMOylation system from an important crop plant, rice, and show that it responds to cold, salt and ABA stress conditions on a protein level via the accumulation of SUMOylated proteins. We also characterized the transcriptional regulation of individual SUMOylation cascade components during stress and development. During stress conditions, majority of the SUMO cascade components are transcriptionally down regulated. SUMO conjugate proteins and SUMO cascade component transcripts accumulated differentially in various tissues during plant development with highest levels in reproductive tissues. Taken together, these data suggest a role for SUMOylation in rice development and stress responses.

• Molecules and Cells
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• 제22권3호
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• pp.247-253
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• 2006

Protein modification by small ubiquitin-like modifier (SUMO) controls diverse cellular functions of protein targets including transcription factors and coregulators mainly in the nucleus and participates in maintaining cellular homeostasis. In addition, SUMO system plays important roles in DNA damage repair and maintaining genome integrity. Thus, in some cases, the loss of control on SUMOylation or deSUMOylation processes causes a defect in maintaining homeostasis and hence gives a cue to cancer development. Furthermore, recent study showed that SUMO system is also involved in cancer metastasis. In this review, we will summarize and discuss the possible role of SUMO system in cancer development and metastasis.

• BMB Reports
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• 제47권4호
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• pp.233-238
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• 2014

Polypyrimidine tract-binding protein 1 (PTBP1) and its brain-specific homologue, PTBP2, are associated with pre-mRNAs and influence pre-mRNA processing, as well as mRNA metabolism and transport. They play important roles in neural differentiation and glioma development. In our study, we detected the expression of the two proteins in glioma cells and predicted that they may be sumoylated using SUMOplot analyses. We confirmed that PTBP1 and PTBP2 can be modified by SUMO1 with co-immunoprecipitation experiments using 293ET cells transiently co-expressing SUMO1 and either PTBP1 or PTBP2. We also found that SUMO1 modification of PTBP2 was enhanced by Ubc9 (E2). The mutation of the sumoylation site (Lys137) of PTBP2 markedly inhibited its modification by SUMO1. Interestingly, in T98G glioma cells, the level of sumoylated PTBP2 was reduced compared to that of normal brain cells. Overall, this study shows that PTBP2 is posttranslationally modified by SUMO1.