• Asian Pacific Journal of Cancer Prevention
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• 제16권9호
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• pp.3849-3856
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• 2015

Background: Cholangiocarcinoma (CCA), or bile duct cancer, is incurable with a high mortality rate due to a lack of effective early diagnosis and treatment. Identifying cytoplasmic membrane proteins of invasive CCA that facilitate cancer progression would contribute toward the development of novel tumor markers and effective chemotherapy. Materials and Methods: An invasive CCA cell line (KKU-100) was stimulated using TNF-${\alpha}$ and then biotinylated and purified for mass spectrometry analysis. Novel proteins expressed were selected and their mRNAs expression levels were determined by real-time RT-PCR. In addition, the expression of ALCAM was selected for further observation by Western blot analysis, immunofluorescent imaging, and antibody neutralization assay. Results: After comparing the proteomics profile of TNF-${\alpha}$ induced invasive with non-treated control cells, over-expression of seven novel proteins was observed in the cytoplasmic membrane of TNF-${\alpha}$ stimulated CCA cells. Among these, ALCAM is a novel candidate which showed significant higher mRNA- and protein levels. Immunofluorescent assay also supported that ALCAM was expressed on the cell membrane of the cancer, with increasing intensity associated with TNF-${\alpha}$. Conclusions: This study indicated that ALCAM may be a novel protein candidate expressed on cytoplasmic membranes of invasive CCA cells that could be used as a biomarker for development of diagnosis, prognosis, and drug or antibody-based targeted therapies in the future.

• Archives of Pharmacal Research
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• 제21권6호
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• pp.629-633
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• 1998

In addition to selecting proteins for degradation by the 26S proteasome, ubiqitination appears to serve other regulatory functions, including for endosomal/lysosomal targeting, protein translocation, and enzyme modification. Currently, little is known how multiubiquitin chains are recognized by these cellular mechanisms. Within the 26S proteasome, one subunit (Mcb1/S5a) has been identified that has affinity for multiubiquitin chains and may function as a ubiquitin receptor. We recently found that a non-proteasomal protein p62 also preferentially binds multiubiquitin chains and forms a novel cytoplasmic structure "sequestosome" which serves as a storage place for ubiquitinated proteins. In the present manuscript, the role and regulation of p62 in relation to the sequestosomal function will be reviewed.

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2003년도 International Symposium of Silkworm/Insect Biotechnology and Annual Meeting of Korea Society of Sericultural Science
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• pp.118-119
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• 2003

Baculovirus occlusion bodies have been recently engineered to incorporate foreign protein such as the Bacillus thuringiensis (Bt) CrylAc protein for improvement of insecticidal activity. In this study, polyhedrin, cylAc, egfp and crylCa genes were fused to produce occlusion bodies that contain novel recombinant crystal protein by homologous recombination between cylAc and crylCa genes in insect cells. (omitted)

• 대한방사성의약품학회지
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• 제2권2호
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• pp.69-72
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• 2016

Since the translocator protein (TSPO) is involved in neurodegeneration diseases, many scientists' interest has been focused on the development of a ligand targeting TSPO. A novel compound based on pyrazolo[1,5 -a] pyrimidine structure, DPA-714, has been studied and considered as a TSPO ligand with high affinity. In this highlight review, several researches for the novel radioligand for the translocator protein are illustrated.

• BMB Reports
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• 제47권11호
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• pp.643-648
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• 2014

Stanniocalcin (STC), a glycoprotein hormone originally discovered in fish, has been implicated in calcium and phosphate homeostasis. While fishes and mammals possess two STC homologs (STC1 and STC2), the physiological roles of STC2 are largely unknown compared with those of STC1. In this study, we identified Ran-binding protein M (RanBPM) as a novel binding partner of STC2 using yeast two-hybrid screening. The interaction between STC2 and RanBPM was confirmed in mammalian cells by immunoprecipitation. STC2 enhanced the RanBPM-mediated transactivation of liganded androgen receptor (AR), but not thyroid receptor ${\beta}$, glucocorticoid receptor, or estrogen receptor ${\beta}$. We also found that AR interacted with RanBPM in both the absence and presence of testosterone (T). Furthermore, we discovered that STC2 recruits RanBPM/AR complex in T-dependent manner. Taken together, our findings suggest that STC2 is a novel RanBPM-interacting protein that promotes AR transactivation.

• 생명과학회지
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• 제6권3호
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• pp.213-218
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• 1996

대장균의 GroEL과 상동성을 가지는 symbionin이 진딧물의 세포내 곤생미생물에서 유일하게 생산된다. 이것은 in vitro와 in vivo에서 moecular chaperone 활성을 가지는 것과 함께 자가인산화(autophosphory-lation)와 인산기전이효소(phosphotransferase)의 활성에 의해서 고에너지 인산기를 다른 곳에 줄 수 있다. Symbionin은 two component pathway의 센서분자의 역할을 하며, 지금까지 알려진 것과는 다른 성질을 가진 protein Kinase이다.

• 한국양봉학회지
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• 제34권2호
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• pp.161-167
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• 2019

There is an urgent need for novel protein sources as an alternative to meat production. Insects, such as honeybees, hold potential as a safe, nutritious and reliable protein source for the future. In the present study, we established optimal powder preprocessing conditions of drone pupae (Apis mellifera L.) for use as a novel food. The content of moisture, crude protein, crude fat, crude ash, carbohydrate and crude fiber in drone pupae(Apis mellifera L.) were analyzed. The crude protein content ranged from 48.5 to 51.8% was found in both freeze-dried and hot-air powdered drone pupae. However, the protein content in the freeze-dried powder was higher than that in the hot-air powder by 3.3%. According to the Korean Food Standard Codex test method, coliforms, Salmonella spp. Staphylcoccus aureus, and Enterohamorrhagice Escherichia coli were not detected in both freeze-dried and hot-air powder. Therefore, we suggest that the high protein content of the powdered drone pupae prepared in this study can serve as a novel food.

• Molecules and Cells
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• 제24권3호
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• pp.437-440
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• 2007

$OGL-20P^T$-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain $OGL-20P^T$, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments of $OGL-20P^T$-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily ${\alpha}$-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.

• 한국자기공명학회논문지
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• 제14권2호
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• pp.105-116
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• 2010

SH3YL1, a novel protein containing one Src homology 3 domain at the carboxyl terminus was first detected in mouse anagen skin cDNA. This protein had a significant homology with YHRO 16c/Ysc 84, the yeast Src homology 3 domain-containing protein. The sequence identity was remarkable at the carboxyl and amino-terminal Src homology 3 domain, suggesting that the novel protein is a mouse homolog of the yeast protein and thus was termed as SH3YL1. SH3YL1 is composed of two domains, a DUF500 at N-termini and a SH3 domain at C-termini. In our study we cloned the SH3 domain in bacterial expression system in Escherichia coli using pET32a vector with TEV protease cleavage site and purified as a monomer using affinity chromatography. The N-terminal poly-Histidine tag was cleaved with TEV protease and target protein was used for backbone studies. Our study showed that SH3 domain primarily consists of $\beta$-sheet which is in consistence with previous result performed on the truncated SH3 domain of SH3YL1.

• 전기전자학회논문지
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• 제13권3호
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• pp.18-23
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• 2009

FEATURE는 단백질 내에서 특정 기능이나 구조를 가지고 있는 site의 미세환경분포를 이용하여 다른 단백질 내에서 이와 유사한 미세환경을 가지고 있는 부분을 찾아 그 분분이 site일 확률을 수치적으로 제시해 줌으로써 사용자로 하여금 site의 존재 유무와 그 위치를 판단하는데 기준을 제공해주는 유용한 툴이다. 하지만 기존의 FEATURE에서 사용된 데이터 이외의 새로운 단백질 구조 데이터를 FEATURE에 적용하기 위해서는 FEATURE 내부의 module을 입력 데이터 구조에 맞게 수정해야 한다. 그러나 FEATURE 내부의 module 구조를 수정하는 방식이 직관적이지 않기 때문에 많은 연구자들이 FEATURE를 원활하게 사용하지 못하였다. 따라서 본 논문에서는 FEATURE의 내부 구조를 분석하고 FEATURE를 새로운 단백질 데이터에 적용하기 위한 방법을 제시한다.