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Lee, Dae-Weon,Seo, Jong Bok,Nam, Myung Hee,Kang, Jae Soon,Kim, Soo Young,Kim, A-Young,Kim, Won Tae,Choi, Jin Kyu,Um, Yurry,Lee, Yi,Moon, Il-Sung,Han, Hye Rim,Koh, Sang-Hyun,Je, Yeon Ho,Lim, Kook Jin,L American Society for Biochemistry and Molecular Bi 2011 Molecular & cellular proteomics Vol.10 No.2
정상적인 위내시경 소견을 보이는 사람의 위점막 조직에서 cagA 유전자 존재의 의의
박주상,윤광희,홍원선,남승우,민영일,정훈용,고진규,김해련,양석균,이미헌,강경훈 대한소화기학회 1998 대한소화기학회지 Vol.31 No.6
Background/Aims: It becomes clear that clinical manifestation of H. pylori infection has marked diversity mainly due to the strain diversity of H. pylori and host susceptibility. Many attempts have been made to identify the pathogenic strains of H. pylori, and have shown that the strain with the gene coding for cagA may be a pathogenic strain. To determine the role of cagA gene in the developrnent of gastroduodenal diseases, it is important to test cagA gene in gastric tissues without gross abwrmality. Methods: In a total of forty-seven persons without abnormal gastroscopic findings, the prevalence of H. pylori was determined by polymerase chain reaction (PCR), CLO test, culture, and histological examination. Genomic DNA was amplified by PCR using the primer specific for the 109-bp product of 16S rRNA gene of H. pylori. The prevalence of cagA gene was examined in 37 persons who were positive in PCR for 16S rRNA gene of H. pylori. The PCR product using primer set specific for cagA gene was a 350-bp sized and represented mid-region of cagA gene. Resnlts: Thirty-two (68.1%) out of 47 persons were infected by H. pylori. Thirty-seven (78.7%) persons showed positive PCR result for H. pylori. The cagA was identified in 28 (75.7%) among 37 H. pylori positive persons. Conclusions: The high prevalence of cagA gene in H, pylori-infeced gastric mucosa was observed in the persons with no specific gross abnormality in gastroscapic examination. These results indicate that the expression of cagA gene is common in H. pylori infected gastric mucosa in Korea. To canfirm the cytotoxie activity, the further studies using other primers are needed.
Chung, Heejae,Cho, Kyung-Sang,Koh, Weon-Kyu,Kim, Dongho,Kim, Jiwon The Royal Society of Chemistry 2016 Nanoscale Vol.8 No.29
<P>Although Group II-VI quantum dots (QDs) have attracted much attention due to their wide range of applications in QD-based devices, the presence of toxic ions in II-VI QDs raises environmental concerns. To fulfill the demands of nontoxic QDs, synthetic routes for III-V QDs have been developed. However, only a few comparative analyses on optical properties of III-V QDs have been performed. In this study, the composition-related energetic trap distributions have been explored by using three different types of core/multishell QDs: CdSe-CdS (CdSe/CdS/ZnS), InP-ZnSe (InP/ZnSe/ZnS), and InP-GaP (InP/GaP/ZnS). It was shown that CdSe-CdS QDs have much larger trap densities than InP-shell QDs at higher energy states (at least 1E(g) (band gap energy) above the lowest conduction band edge) based on probability density plots and Auger ionization efficiencies which are determined by analyses of photoluminescence blinking dynamics. This result suggests that the composition of encapsulated QDs is closely associated with the charge trapping processes, and also provides an insight into the development of more environmentally friendly QD-based devices.</P>
Generation and Characterization of Monoclonal Antibodies Specific to <i>Drosophila presenilin</i>
Cuc, Ho Thi Thu,Seo, Jong Bok,Choi, Jin Kyu,Kim, Won Tae,Park, Seok Jou,Lee, Dae Weon,Kim, Yong Sun,Fortini, Mark E.,Koh, Young Ho Mary Ann Liebert 2009 Hybridoma Vol.28 No.3
<P>The development of a monoclonal antibody (MAb) specific to Drosophila presenilin (Psn) proteins in vivo was the major aim of this study, since the absence of specific antibodies recognizing Psn proteins hampered our progress in understanding Psn functions during development, differentiation, and pathogenesis. By dot blot and immunofluorescence screenings, we found that MAb Psn2G6 specifically recognized Psn proteins in wing imaginal discs and brains of wild-type control W1118 larvae. MAb Psn2G6 also transgenically expressed a long form of wild-type Psn (Psn + 14 WT) proteins in wing imaginal discs of two independent transgenic lines. Transgenic expression of Psn + 14 WT proteins in psn(B3) larvae completely rescued the expression patterns of Psn proteins and the development of wing imaginal discs. In addition, neural hyperplasia observed in wing imaginal discs of psn(B3) larvae was also suppressed.</P>