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Yang, Keum-Jin,Shin, Sanghee,Piao, Longzhen,Shin, Eulsoon,Li, Yuwen,Park, Kyeong Ah,Byun, Hee Sun,Won, Minho,Hong, Janghee,Kweon, Gi Ryang,Hur, Gang Min,Seok, Jeong Ho,Chun, Taehoon,Brazil, Derek P,He American Society for Biochemistry and Molecular Bi 2008 The Journal of biological chemistry Vol.283 No.3
<P>3-Phosphoinositide-dependent protein kinase-1 (PDK1) appears to play a central regulatory role in many cell signalings between phosphoinositide-3 kinase and various intracellular serine/threonine kinases. In resting cells, PDK1 is known to be constitutively active and is further activated by tyrosine phosphorylation (Tyr(9) and Tyr(373/376)) following the treatment of the cell with insulin or pervanadate. However, little is known about the mechanisms for this additional activation of PDK1. Here, we report that the SH2 domain of Src, Crk, and GAP recognized tyrosine-phosphorylated PDK1 in vitro. Destabilization of PDK1 induced by geldanamycin (a Hsp90 inhibitor) was partially blocked in HEK 293 cells expressing PDK1-Y9F. Co-expression of Hsp90 enhanced PDK1-Src complex formation and led to further increased PDK1 activity toward PKB and SGK. Immunohistochemical analysis with anti-phospho-Tyr(9) antibodies showed that the level of Tyr(9) phosphorylation was markedly increased in tumor samples compared with normal. Taken together, these data suggest that phosphorylation of PDK1 on Tyr(9), distinct from Tyr(373/376), is important for PDK1/Src complex formation, leading to PDK1 activation. Furthermore, Tyr(9) phosphorylation is critical for the stabilization of both PDK1 and the PDK1/Src complex via Hsp90-mediated protection of PDK1 degradation.</P>
Yang, Kyung Mo,Cho, Hong-Il,Choi, Hyuck Jae,Piao, Yuanzhe The Royal Society of Chemistry 2014 Journal of Materials Chemistry B Vol.2 No.21
<P>We reported the synthesis of highly water-stable iron oxide nanoparticles by a simple one-pot reaction. Non-toxic polyethylene glycol MW 600 (PEG) acted as a solvent, capping agent and reducing agent in the synthesis of iron oxide nanoparticles. As a result of the synthesis, PEGylated small-size (4.2 ± 0.39 nm average diameter and 7.2 ± 1.9 nm hydrodynamic sizes measuring by DLS) iron oxide nanoparticles (USPIO) were obtained, which show great colloidal stability in water and tolerate high salt concentration (0.75 M sodium chloride) and a wide pH range of 4 to 12. Oxidation of PEG was observed during the synthesis of iron oxide nanoparticles, which makes USPIO easy to functionalize with other molecules. Functionalization of the USPIO surface with fluorescein isothiocyanate (FITC) was conducted for investigating the possibility for multimodal imaging. Also the cytotoxicity test and lymph node imaging were performed by using the FITC labelled USPIO (FITC@USPIO). According to these results, the stable water dispersed USPIO and FITC@USPIO are expected to apply for multimodal <I>in vivo</I> imaging.</P>
Genomic distribution of simple sequence repeats in Brassica rapa
Hong, Chang Pyo,Piao, Zhong Yun,Kang, Tae Wook,Batley, Jacqueline,Yang, Tae Jin,Hur, Yoon Kang,Bhak, Jong,Park, Beom Seok,Edwards, David,Lim, Yong Pyo Korean Society for Molecular and Cellular Biology 2007 Molecules and cells Vol.23 No.3
Effects of Melittin on Oxidative Stress Mediated Induction of Apoptosis in Prostate Cancer Cell
Shin, Eulsoon,Yang, Keum Jin,Piao, Longzhen,Shin, Sanghee,Li, Yuwen,Kim, Young-Rae,Byun, Hee Sun,Won, Minho,Park, Kyung Ah,Lee, Hyunji,Choi, Byung Lyul,Hong, Jang Hee,Hur, Gangmin,Seok, Jeong Ho,Park, 충남대학교 형질전환복제돼지연구센터 2007 논문집 Vol. No.10
Li, Yuwen,Piao, Longzhen,Yang, Keum-Jin,Shin, Sang-Hee,Shin, Eul-Soon,Park, Kyung-Ah,Byun, Hee-Sun,Won, Min-Ho,Choi, Byung-Lyul,Lee, Hyun-Ji,Kim, Young-Rae,Hong, Jang-Hee,Hur, Gang-Min,Kim, Jeong-Lan Korean Society of ToxicologyKorea Environmental Mu 2008 Toxicological Research Vol.25 No.4
DNA-dependent protein kinase(DNA-PK) is involved in joining DNA double-strand breaks induced by ionizing radiation or V(D)J recombination and is activated by DNA ends and composed of a DNA binding subunit, Ku, and a catalytic subunit, DNA-PKcs. It has been suggested that DNA-PK might be $2^{nd}$ upstream kinase for protein kinase B(PKB). In this report, we showed that Ser473 phosphorylation in the hydrophobic-motif of PKB is blocked in DNA-PK knockout mouse embryonic fibroblast cells(MEFs) following insulin stimulation, while there is no effect on Ser473 phosphorylation in DNA-PK wild type MEF cells. The observation is further confirmed in human glioblastoma cells expressing a mutant form of DNA-PK(M059J) and a wild-type of DNA-PK(M059K), indicating that DNA-PK is indeed important for PKB activation. Furthermore, the treatment of cells with doxorubicin, DNA-damage inducing agent, leads to PKB phosphorylation on Ser473 in control MEF cells while there is no response in DNA-PK knockout MEF cells. Together, these results proposed that DNA-PK has a potential role in insulin signaling as well as DNA-repair signaling pathway.
Melittin, a Amphipathic Cationic Peptide that Causes ROS-Mediated Apoptosis in Prostate Cancer Cell
Shin, Eulsoon,Yang, Keum-Jin,Piao, Longzhen,Shin, Sanghee,Li, Yuwen,Kim, Young-Rae,Byun, Hee Sun,Won, Minho,Park, Kyung Ah,Lee, Hyunji,Choi, Byung Lyul,Hong, Jang Hee,Hur, Gangmin,Seok, Jeong Ho,Park, 충남대학교 형질전환복제돼지연구센터 2007 논문집 Vol. No.10