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성미숙 대한영상의학회 1992 대한영상의학회지 Vol.28 No.3
To analyze the progression of white matter maturation and white matter pathology, MR imaging of the brain was obtained in 38 children with delayed development. Children with developmental delay showed a high incidence of MR abnormalities (34/38, 89.5%). Delayed pattern of myelination and gray-white matter differentiation was seen in 13 patients. Twenty-two patients had whits matter patholgy, including 14 with white matter hypoplasia, seven with focal small infarction, five with periventricular leukomalacia, and three with high signal intensities on T2 weighted image. Associated structural abnormalities were also evaluated. The most common lesions in decreasing frequency were cerebral atrophy and dysgenesis of the corpus callosum, pachygyria and/or polymicrogyria, porencephailc cyst and Leigh's disease. Twenty-three of 34 children had multiple abnormalities on MRI. The MRI was useful in depicting the progression of myelination and other white matter lesions, and serial follow-u MR is recommended for patients with delayed or lack of myelination and gray-white matter differentiation.
PC12 cell에 있어서의 ERK protein의 활성화
成美淑 관동대학교 1996 關大論文集 Vol.24 No.1
The microtube-associated protein tau is a major component of the paired helical filament (PHFs) observed in Alzheimer's disease brains. The pathological tau is distinguished from normal tau by its status of phosphorylation, higher apparent molecular weight and reaction with certain antibodies. However, the protein kinases have not been characterized so far. Here I describe a protein kinase, pk40 which specifically induces the Alzeheimer-like state in tau protein. The pk40 protein as a member of MAP kinase, also called ERK(extracellular signal regulated kinases) appears to play important role in converting tyrosine phosphorylation into the serine/threonine phosphorylations that regulates downstream events. This study is focused on the activation of pk40 protein upon cell stimulation in PC12 cells. In order to indentify pk40 protein as a MAP protein in vivo, immunoblot analysis was performed with PC12 cell extracts using SMI antibodies.
성미숙,Sung, Mee-Sook Korean Society of Life Science 2007 생명과학회지 Vol.17 No.3
We wished to create a set of small molecular weight PDZ domain ligands that may be used in functional studies on the proteins AF6, PSD-95 and Shank. As a starting point, the Shank3 PDZ domain was cloned, purified, and characterized the structure of Shank3 PDZ domain by 1D $^1H-NMR$. The chemical shift dispersion of the proton signals indicates that the purified Shank3 PDZ protein is very pure and globally well folded. Currently, we are working on improving the yield of the protein production for complete NMR structural analysis of the Shank3 PDZ domain. PDZ 도메인을 통하여 여러 단백질과 상호작용하며 신경전달 기전에 관여하는 단백질로 Shank1, Shank2, Shank3, PDS-95, AF있다. 본 연구는 Shank3 PDZ 도메인의 구조를 밝히기 위한 첫 단계로서 Shank3 단백질의 PDZ 도메인을 동정하였고, E. coli에서 발현하여 생성된 단백질을 정제한 후 1차 NMR 구조분석을 시도하였다. 그 결과에 의하면 정제된 Shank3 PDZ 단백질은 순도가 높고 안정적인 접힘(folding)구조를 제시하고있다. 현재 완전한 NMR 구조분석을 위해 좀더 많은 양의 정제된 Shank3 PDZ 단백질을 얻고자 연구하고 있다.