http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
신지은,Shenxiu Du,Nora Bujdoso,Yangjie Hu,Seth J. Davis 한국식물학회 2013 Journal of Plant Biology Vol.56 No.3
Plant experience diurnal changes in their environment that can be anticipated and responded to via the circadian clock. Integration of external signals by this clock ensures metabolic homeostasis and ultimately enhances fitness. TIME FOR COFFEE (TIC) is known to be associated to the circadian clock, being required to maintain rhythmic period and amplitude, and to regulate clock-driven physiological responses. The molecular function of TIC has so far only been studied with loss-of-function mutants. The biochemical activity of TIC remains elusive. To learn more about TIC in diverse physiological processes, here we generated TIC overexpressing plants (TICox) and characterized their impact on plant growth, development, and circadianclock activity. TICox plants displayed phenotypic similarity with tic mutants. This included defects in leaf morphology, the developmental transition from the vegetative to reproductive phase, and circadian-clock function. These observations allowed us to hypothesize that TIC is an element of protein complexes that are involved in global biological processes.
Yang, Su-Jeong,Thackray, Alana,Bujdoso, Raymond The Korean Society of Veterinary Service 2005 韓國家畜衛生學會誌 Vol.28 No.4
In prion pathogenesis, the structural conversion of the cellular prion protein $(PrP^c)$ to its abnormal isomer $(PrP^{Sc})$ is believed to be a major event. The susceptibility or resistance to natural sheep scrapie is associated with polymorphisms of host PrP gene (PRNP) at amino acid residues 136, to a lesser extent 154. The 112 residue in ovine PrP displays a natural polymorphism, Methionine to Threonine, which has not been thoroughly investigated. However the cell-free conversion assay showed that ARQ with Thr112 $(T_{112}ARQ)^{1)}$ presents lower convertibility to $PrP^{Sc}$than wild type ARQ $(M_{112}ARQ)$ [1] In this study we generated ovine recombinant PrPs of 112 allelic variants by metal chelate affinity chromatography and cation exchange chromatography. The final purity of the ovine PrP ARQ was more than $95\%$. These variants showed similar immunoreactivity against anti-PrP monoclonal antibodies in Western blot and ELISA. The refolded $M_{112}ARQ$ and $M_{112}ARQ$ presented the secondary structural content to similar extent via CD spectroscopy analysis. The inherited structural features of $M_{112}ARQ$ and $M_{112}ARQ$ under the different biophysical conditions are in the middle of investigation.
( Su Jeong Yang ),( Alana Thackray ),( Raymond Bujdoso ) 한국동물위생학회 2005 한국동물위생학회지 (KOJVS) Vol.28 No.4
In prion pathogenesis, the structural conversion of the cellular prion protein(PrPC) to its abnormal isomer(PrPSc) is believed to be a major event. The susceptibility or resistance to natural sheep scrapie is associated with polymorphisms of host PrP gene (PRNP) at amino acid residues 136, to a lesser extent 154. The 112 residue in ovine PrP displays a natural polymorphism, Methionine to Threonine, which has not been thoroughly investigated. However the cell-free conversion assay showed that ARQ with Thr112(T112ARQ)1) presents lower convertibility to PrPSc than wild type ARQ (M112ARQ) [1]. In this study we generated ovine recombinant PrPs of 112 allelic variants by metal chelate affinity chromatography and cation exchange chromatography. The final purity of the ovine PrP ARQ was more than 95%. These variants showed similar immunoreactivity against anti-PrP monoclonal antibodies in Western blot and ELISA. The refolded M112ARQ and T112ARQ presented the secondary structural content to similar extent via CD spectroscopy analysis. The inherited structural features of M112ARQ and T112ARQ under the different biophysical conditions are in the middle of investigation.