http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Quantitative Assay for the Binding of Jun-Fos Dimer and Activator Protein-1 Site
Lee, Sang-Kyou,Park, Se-Yeon,Jun, Gyo,Hahm, Eun-Ryeong,Lee, Dug-Keun,Yang, Chul-Hak Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.6
The Jun and Fos families of eukaryotic transcription factors form heterodimers capable of binding to their cognate DNA enhancer elements. We are interested in searching for inhibitors or antagonists of the binding of the Jun-Fos heterodimer to the activator protein-1 (AP-1) site. The basic-region leucine zipper (bZIP) domain of c-Fos was expressed as a fusion protein with glutathione S-transferase, and allowed to form a heterodimer with the bZIP domain of c-Jun. The heterodimer was bound to glutathione-agarose, to which were added radiolabeled AP-1 nucleotides. After thorough washing, the gel-bound radioactivity was counted. The assay is faster than the coventional electrophoretic mobility shift assay because the gel electrophoresis step and the autoradiography step are eliminated. Moreover, the assay is very sensitive, allowing the detection of picomolar quantities of nucleotides, and is not affected by up to 50% dimethylsulfoxide, a solvent for hydrophobic inhibitors. Curcumin and dihydroguaiaretic acid, recently known inhibitors of Jun-Fos-DNA complex formation, were applied to this Jun-GST-fused Fos system and revealed to decrease the dimer-DNA binding.
Quantitative Assay for the Binding of Jun-Fos Dimer and Activator Protein-1 Site
Yang, Chul Hak,Jun, Gyo,Lee, Dug Keun,Lee, Sang Kyou,Park, Se Yeon,Hahm, Eun Ryeong 생화학분자생물학회 1998 BMB Reports Vol.32 No.6
The Jun and Fos families of eukaryotic transcription factors form heterodimers capable of binding to their cognate DNA enhancer elements. We are interested in searching for inhibitors or antagonists of the binding of the Jun-Fos heterodimer to the activator protein-1 (AP-1) site. The basic-region leucine zipper (bZIP) domain of c-Fos was expressed as a fusion protein with glutathione S-transferase, and allowed to form a heterodimer with the bZIP domain of c-Jun. The heterodimer was bound to glutathione-agarose, to which were added radiolabeled AP-1 nucleotides. After thorough washing, the gel-bound radioactivity was counted. The assay is faster than the conventional electrophoretic mobility shift assay because the gel electrophoresis step and the autoradiography step are eliminated. Moreover, the assay is very sensitive, allowing the detection of picomolar quantities of nucleotides, and is not affected by up to 50% dimethylsulfoxide, a solvent for hydrophobic inhibitors. Curcumin and dihydroguaiaretic acid, recently known inhibitors of Jun-Fos-DNA complex formation, were applied to this Jun-GST-fused Fos system and revealed to decrease the dimer-DNA binding.
Quantitative Assay for the Binding of Jun-Fos Dimer and Activator Protein-1 Site
Yang,Chul-Hak,Jun,Gyo,Hahm,Eun-Ryeong,Lee,Sangkyou,Park,Seyeon,Lee,Dug-Keun The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.6
The Jun and Fos families of eukaryotic transcription factors form heterodimers capable of binding to their cognate DNA enhancer elements. We are interested in searching for inhibitors or antagonists of the binding of the Jun-Fos heterodimer to the activator protein-1 (AP-1) site. The basic-region leucine zipper (bZIP) domain of c-Fos was expressed as a fusion protein with glutathione S-transferase, and allowed to form a heterodimer with the bZIP domain of c-Jun. The heterodimer was bound to glutathione-agarose, to which were added radiolabeled AP-1 uncleotides. After thorough washing, the gel-bound radioactivity was counted. The assay is faster than the coventional electrophoretic mobility shift assay because the gel electrophoresis step and the autoradiography step are eliminated. Moreover, the assay is very sensitive, allowing the detection of picomolar quantities of nucleotides, and is not affected by up to 50% dimethylsulfoxide, a solvent for hydrophobic inhibitors. Curcumin and dihydroguaiaretic acid, recently known inhibitors of Jun-Fos-DNA complex formation, were applied to this Jun-GST-fused Fos system and revealed to decrease the dimer-DNA binding.
이선경,정준교 대한가정학회 2003 Family and Environment Research Vol.41 No.9
This study examined the clothing behavior in terms of creativity, individuality and conformity. The subjects were 317 boys(mean age: 18) and 312 girls(mean age: 18) in third grade of high school, in which were situated at north and south part of Han-River in Seoul. They were administered with the following questionnaires to measure the attitudinal and behavioral conformity, creativity, individuality, clothing conformity, clothing nonconformity, clothing confidence, aesthetic sense, clothing importance, fashionabdity. Results indicated that (1) high school students who have high creativity showed higher scores in clothing nonconformity, clothing confidence, aesthetic sew, clothing importance than those who have low creativity. But there were no significant differences between two groups in clothing conformity and fashionability(p<0.001). (2) High school students who have high individuality showed higher scores in clothing conformity clothing, nonconformity, clothing confidence, aesthetic sense, clothing importance and fashionability than those who have low individuality(p<0.001). (3) Students who have low attitudinal conformity showed higher scores in clothing nonconformity, clothing confidence and aesthetic sense(p<0.001) and lower score in information and norm specific clothing confirmity(p<0.05) than those who have high attitudinal conformity. And those who have high behavioral conformity showed higher score in clothing confirmity than those who have low behavioral confimity(p<0.05). From these findings, we could find that the importance of creativity and individuality was greater than that of conformity in clothing behavior. These results were discussed and following studies were suggested.
Isolation and Transcriptional Expression of CuZn Superoxide Dismutase from Codonopsis lanceolata
Lee,Kang,In,Jun-Gyo,Yu,Chang-Yeon,Yun,Song-Joong,Min,Byung-Hoon,Rho,Yeong-Deok,Kim,Moo-Sung,Yang,Deok-Chun 한국자원식물학회 2004 Plant Resources Vol.7 No.3
To investigate the defense mechanism against the abiotic stress, a cDNA clone encoding a CuZn superoxide dismutase (CuZnSOD) protein was isolated from a cDNA library prepared from tabroot mRNAs of Codonopsis lanceolata. The eDNA, designated ClSODCc, is 799 nucleotides long and has an open reading frame of 459 bp with a deduced amino acid sequence of 152 residues. The deduced amino acid sequence of ClSODCc matched to the previously reported CuZnSODs. Consensus amino acid residues (His-45, -47, -62, -70, -79, -119 and Asp-82) were involved in Cu-, Cu/Zn-, and Zn- binding ligands. The deduced amino acid sequence of ClSODCc showed high homologies (82%-86%) regardless of species. Expression of ClSODCc by oxidative stress was increased up to 1 h after treatment and declined gradually. Much earlier and stronger expression of ClSODCc was observed in the cold stress treatment.
정준교,이선경 한국의류학회 1999 한국의류학회지 Vol.23 No.3
This study examined the effect of abolition of school uniform on personality. The subjects were 317 boys(mean age: 18) and 312 girls(mean age: 18) in third grade of high school. The subjects were selected from 4 uniform high schools and 4 free-choice wearing clothes high school, in which were situated at north and south part of Han-River in Seoul. They were administered with the following questionnaires to measure the creativity, individuality, self-efficacy, conformity of behaviour, conformity of attitude, autonomy and responsibility. Results indicated that (1) in many personality variables, there were no effect of abolition of school uniform on personality, (2) the effect of abolition of school uniform on personality must be considered in the moderator effect of the preferred clothes of students. These results were discussed and its implication and following study were suggested.
Lee Jun-Won,In Jun-Gyo,Lee Bum-Soo,Choi Yong-Eui,Kim Jin-Ju,Yang Deok-Chun 한국자원식물학회 2005 Plant Resources Vol.8 No.1
A cDNA, PSOD1, encoding cytosolic copper/zinc superoxide dismutase (CuZn-SOD) was cloned and characterized from a full length cDNA library prepared from Populus alba×Populus glandulosa cultured in vitro. A PSOD1, is 725 nucleotides long and has an open reading frame of 459 bp with 152 amino acid residues (pI 5.43). The deduced amino acid sequence of PSOD1 perfect matched to the previously reported CuZn-SOD (CAC33845.1). Consensus amino acid residues (His-45, -47, -62, -70, -79, -119) were involved in Cu-, Cu/Zn-, and Zn- binding ligands. The deduced amino acid sequence of PSOD1 exhibited the high level of similarity from 100 to 85% among previously registered SOD genes. The expression of PSOD1 in poplar increased at the 1 mM H₂O₂ and drought stress during 30 min and 60 min, but the ozone treated poplar increased at 30 min in the early time and then decreased at 60 min.