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Suppression of stray electrons in the negative ion accelerator of CRAFT NNBI test facility
Yang Yuwen,Wei Jianglong,Xie Junwei,Gu Yuming,Xie Yahong,Hu Chundong 한국원자력학회 2023 Nuclear Engineering and Technology Vol.55 No.3
Comprehensive Research Facility for Fusion Technology (CRAFT) is an integration of different demonstrating or testing facilities, which aim to develop the critical technology or composition system towards the fusion reactor. Due to the importance and challenge of the negative ion based neutral beam injection (NNBI), a NNBI test facility is included in the framework of CRAFT. The initial object of CRAFT NNBI test facility is to obtain a H0 beam power of 2 MW at the energy of 200e400 keV for the pulse duration of 100 s. Inside the negative ion accelerator of NNBI system, the interactions of the negative ions with the background gas and electrodes can generate abundant stray electrons. The stray electrons can be further accelerated and dumped on the electrodes or eject from the accelerator. The stray electrons, including the ejecting electrons, cause the unwanted particle and heat flux onto the electrodes and the inner components of beamline (especially the temperature sensitive cryopump). The suppression of the stray electrons from the CRAFT accelerator is carried out via a series of design and simulation works. The paper focuses the influence of different magnetic field configurations on the stray electrons and the character of the ejecting electrons.
Yuwen Li,Longzhen Piao,Keum-Jin Yang,Sanghee Shin,Eulsoon Shin,Kyung Ah Park,Hee Sun Byun,Minho Won,Byung Lyul Choi,Hyunji Lee,Young-Rae Kim,Jang Hee Hong,Gang Min Hur,Jeong-Lan Kim,Jae Youl Cho,Jeong 한국독성학회 2008 Toxicological Research Vol.24 No.3
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 2nd 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.
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>
Differentiation potential of Mesenchymal stem cell derived from Bone Marrow
Li, Yuwen,Shin, Eulsoon,Yang, Keum-Jin,Piao, Longzhen,Shin, Sanghee,Kim, Young-Rae,Byun, Hee Sun,Won, Minho,Park, Kyung Ah,Lee, Hyunji,Hur, Gangmin,Seok, Jeong Ho,Kim, Jeong-Lan,Kwon, Gye-Cheol,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.
Nanotherapeutics with immunoregulatory functions for the treatment of bacterial infection
Dongliang Yang,Meng Ding,Yanni Song,Yanling Hu,Weijun Xiu,Lihui Yuwen,Yannan Xie,Yingnan Song,Jinjun Shao,Xuejiao Song,Heng Dong 한국생체재료학회 2023 생체재료학회지 Vol.27 No.00
The advent of drug-resistant pathogens results in the occurrence of stubborn bacterial infections that cannot betreated with traditional antibiotics. Antibacterial immunotherapy by reviving or activating the body’s immune systemto eliminate pathogenic bacteria has confrmed promising therapeutic strategies in controlling bacterial infections. Subsequent studies found that antimicrobial immunotherapy has its own benefts and limitations, such as avoidingrecurrence of infection and autoimmunity-induced side efects. Current studies indicate that the various antibacterialtherapeutic strategies inducing immune regulation can achieve superior therapeutic efcacy compared with mono therapy alone. Therefore, summarizing the recent advances in nanomedicine with immunomodulatory functionsfor combating bacterial infections is necessary. Herein, we briefy introduce the crisis caused by drug-resistantbacteria and the opportunity for antibacterial immunotherapy. Then, immune-involved multimodal antibacterialtherapy for the treatment of infectious diseases was systematically summarized. Finally, the prospects and challengesof immune-involved combinational therapy are discussed.
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