• 생명과학회지
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• 제8권4호
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• pp.360-365
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• 1998

The genetic of a recently described virus, hepatitis G virus(HGV) was investigated. HGV envelope 1 (E1) nucleotide sequences isolated from six Korean hepatitis b virus-positive patients by using a reverse transcription-poly-merase chain reaction procedure, were analysed and compared to the seven previously reported HGV isolates. Sequence homology among the Korean isolates was 88-97% whereas among the isolates from different geographic areas was 80-92%, indicating geographical divergence of HGV. Nucleotide substitutions spread uniformly throughiut the E1 fragment. Furthermore, compared to the prototype HGV sequence, frameshift mutations were observed in most of the Korean isolating that a different translating initiation site for the polyprotein exists in the Korean type HGV.

• 대한치주과학회:학술대회논문집
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• 대한치주과학회 2002년도 제42회 종합학술대회 연제초록
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• pp.87-87
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• 2002

• 한국동물학회:학술대회논문집
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• 한국동물학회 1995년도 한국생물과학협회 학술발표대회
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• pp.335.2-335
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• 1995

No Abstract, See Full Text

• Parasites, Hosts and Diseases
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• 제56권1호
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• pp.61-70
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• 2018

We developed a Rapid Diagnostic Test (RDT) kit for detecting IgG/IgM antibodies against Zika virus (ZIKV) using monoclonal antibodies to the envelope (E) and non-structural protein 1 (NS1) of ZIKV. These proteins were produced using baculovirus expression vector with Sf9 cells. Monoclonal antibodies J2G7 to NS1 and J5E1 to E protein were selected and conjugated with colloidal gold to produce the Zika IgG/IgM RDT kit (Zika RDT). Comparisons with ELISA, plaque reduction neutralization test (PRNT), and PCR were done to investigate the analytical sensitivity of Zika RDT, which resulted in 100% identical results. Sensitivity and specificity of Zika RDT in a field test was determined using positive and negative samples from Brazil and Korea. The diagnostic accuracy of Zika RDT was fairly high; sensitivity and specificity for IgG was 99.0 and 99.3%, respectively, while for IgM it was 96.7 and 98.7%, respectively. Cross reaction with dengue virus was evaluated using anti-Dengue Mixed Titer Performance Panel (PVD201), in which the Zika RDT showed cross-reactions with DENV in 16.7% and 5.6% in IgG and IgM, respectively. Cross reactions were not observed with West Nile, yellow fever, and hepatitis C virus infected sera. Zika RDT kit is very simple to use, rapid to assay, and very sensitive, and highly specific. Therefore, it would serve as a choice of method for point-of-care diagnosis and large scale surveys of ZIKV infection under clinical or field conditions worldwide in endemic areas.

• Journal of Plant Biotechnology
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• 제31권4호
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• pp.273-278
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• 2004

Differential display 방법으로 NaCl에 의하여 발현이 증가되는 cDNA들을 분리하였으며 그중 하나가 식물유래의 outer envelope membrane protein과 높은 유사성을 보였으므로 이를 ShOEP로 명명하였다. ShOEP는 1293 bp 길이에 359개의 아미노산으로 구성된 open reading frame을 포함하고 있으며, 이로부터 추정되는 분자량은 8.9 kDa이었다. ShOEP 단백질은 애기장대의 OEP와는 40.6%, 시금치와는 38%의 유사성을 나타내었다. Northern 분석결과, ShOEP 유전자는 NaCl의 농도가 증가함에 따라 발현량이 급격히 증가하는 것으로 나타났다. 염생식물인 퉁퉁마디의 OEP는 PEG에 의하여 발현이 증가하는 반면 비염생식물인 애기장대의 OEP는 큰 차이를 보이지 않았다. 효모 complementation 실험결과 ShOEP는 NaCl에 특이적이었으며 식물의 염분스트레스 내성 기작에 직접적으로 관여하고 있음을 알 수 있었다.

• Molecules and Cells
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• 제26권3호
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• pp.270-277
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• 2008

This study addresses the physiological functions of the Ran-binding protein homolog NbRanBP1 in Nicotiana benthamiana. Virus-induced gene silencing (VIGS) of NbRanBP1 caused stunted growth, leaf yellowing, and abnormal leaf morphology. The NbRanBP1 gene was constitutively expressed in diverse tissues and an NbRanBP1:GFP fusion protein was primarily localized to the nuclear rim and the cytosol. BiFC analysis revealed in vivo interaction between NbRanBP1 and NbRan1 in the nuclear envelope and the cytosol. Depletion of NbRanBP1 or NbRan1 reduced nuclear accumulation of a NbBTF3:GFP marker protein. In the later stages of development, NbRanBP1 VIGS plants showed stress responses such as reduced mitochondrial membrane potential, excessive production of reactive oxygen species, and induction of defense-related genes. The molecular role of RanBP1 in plants is discussed in comparison with RanBP1 function in yeast and mammals.

• 식물조직배양학회지
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• 제27권5호
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• pp.407-409
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• 2000

Outer envelope membrane proteins of chloroplasts encoded by the nuclear genome are transported without the N-terminal transit peptide. Here, we investigated the targeting mechanism of AtOEP7, an Arabidopsis homolog of small outer envelope membrane proteins in vivo. AtOEP7 was expressed transiently in protoplasts or stably in transgenic plants as fusion proteins with GFP. In both cases AtOEP7:GFP was targeted to the outer envelope membrane when assayed under a fluorescent microscope or by Western blot analysis. Except the transmembrane domain, deletions of the N- or C-terminal regions of AtOEP7 did not affect targeting although a region closed to the C-terminal side of the transmembrane domain affected the targeting efficiency. Targeting experiments with various hybrid transmembrane mutants revealed that the amino acid sequence of the transmembrane domain determines the targeting specificity The targeting mechanism was further studied using a fusion protein, AtOEP7：NLS：GFP, that had a nuclear localization signal. AtOEP7：NLS：GFP was efficiently targeted to the chloroplast envelope despite the presence of the nuclear localization signal. Taken together, these results suggest that the transmembrane domain of AtOEP7 functions as the sole determinant of targeting specificity and that AtOEP7 may be associated with a cytosolic component during translocation to the chloroplast envelope membrane.

• 한국동물학회:학술대회논문집
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• 한국동물학회 1997년도 한국생물과학협회 학술발표대회
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• pp.237.1-237
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• 1997

No Abstract, See Full Text

• 한국동물학회지
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• 제34권1호
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• pp.44-53
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• 1991

Distribution of the antigens during the cell cycle of amoebae was followed by immunof-luorescence microscopy using a monoclonal antibody against the nucleus as a probe. While the cells were in the interphase, the antigen was localized on the nucleus membrane. But it was dispersed all over the cytoplasm during mitosis and cytokinesis. The molecular weights of the immunoreacted antigens were 210 KD and 190 KD as determined by SDS PAGE and western blotting of the purified nuclei. The antigens were not soluble in non-ionic detergent, but were released from the nucleus by incubation with 0.05 M sodium carbonate, pH 10.6 or with 8 M urea at serial chemical extraction. Thus the antigens appeared to be peripheral proteins of the nurBeus envelope. The isoelectic point of both antigens was 7.64 as determined by 2 D PAGE and transfer blotting. Considering the peiipherd association with the nucleus membrane and the dispersed distribution during mitosis, the antigens could be lamin like proteins. Hourever, it appears also possible that they are the component molecules of the unusually structured aurous lamina of amoeba nucleus since they have the large molecular weight and the basic pl.

• Biotechnology and Bioprocess Engineering:BBE
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• 제11권2호
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• pp.173-177
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• 2006

In this study, a novel strategy was developed for the highly selective immobilization of proteins, using the polyhydroxyalkanoate (PHA) depolymerase substrate binding domain (SBD) as an active binding domain. In order to determine the appropriacy of this method for immunodiagnostic assays, the single-chain antibody (ScFv) against the hepatitis B virus (HBV) preS2 surface protein and the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope protein (SCVe) were fused to the SBD, then directly immobilized on PH A-coated slides via microspotting. The fluorescence-labeled HBV antigen and the antibody against SCVe were then utilized to examine specific interactions on the PHA-coated surfaces. Fluorescence signals were detected only at the spotted positions, thereby indicating a high degree of affinity and selectivity for their corresponding antigens/antibodies. Furthermore, we detected small amounts of ScFv-SBD (2.7 ng/mL) and SCVe-SBD fusion proteins (0.6ng/mL). Therefore, this microarray platform technology, using PHA and SBD, appears generally appropriate for immunodiagnosis, with no special requirements with regard to synthetic or chemical modification of the biomolecules or the solid surface.