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천명기,Fedor Simkovic,Amand Faessler 한국물리학회 2008 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.53 No.2
We investigated the effects of nucleon pairing interactions, which include like nucleon pairing (neutron-neutron and proton-proton pairing) and unlike nucleon pairing (neutron-proton) interac- tions, on nuclear structure. In specic, the importance of the unlike pairing is detailed in medium heavy nuclei, such as isotopes of Ge and Zr. Al calculations are carried out within the Hartree Fock Bogoliubob theory in the Nilson basis in order to consider the deformation of the nuclei, which is a typical phenomenon in the exotic nuclei relevant to nucleosynthesis. Our results show that the unlike pairing interactions could play vital roles in understanding the nuclear structure. Even the ordinary nuclei, which are not usualy expected to have such large unlike proton pairing interac- tions, because of large Fermi energy gaps between protons and neutrons, could have unlike pairing interactions strong enough to be deliberately included. Our results are applied to the 64-76Ge and the 80-100Zr isotope series, which nuclei have recently been exploited as important isotopes in the rapid proton process in nucleosynthesis.
Challenges and implemented technologies used in autonomous drone racing
Moon, Hyungpil,Martinez-Carranza, Jose,Cieslewski, Titus,Faessler, Matthias,Falanga, Davide,Simovic, Alessandro,Scaramuzza, Davide,Li, Shuo,Ozo, Michael,De Wagter, Christophe,de Croon, Guido,Hwang, Su Springer-Verlag 2019 INTELLIGENT SERVICE ROBOTICS Vol.12 No.2
Mo, Jung-Soon,Kim, Mi-Yeon,Han, Seung-Ok,Kim, In-Sook,Ann, Eun-Jung,Lee, Kyu Shik,Seo, Mi-Sun,Kim, Jin-Young,Lee, Seung-Chul,Park, Jeen-Woo,Choi, Eui-Ju,Seong, Jae Young,Joe, Cheol O.,Faessler, Reinha American Society for Microbiology 2007 Molecular and cellular biology Vol.27 No.15
<B>ABSTRACT</B><P>Integrin-linked kinase (ILK) is a scaffold and protein kinase that acts as a pivotal effector in integrin signaling for various cellular functions. In this study, we found that ILK remarkably reduced the protein stability of Notch1 through Fbw7. The kinase activity of ILK was essential for the inhibition of Notch1 signaling. Notably, the protein level and transcriptional activity of the endogenous Notch1 intracellular domain (Notch1-IC) were higher in ILK-null cells than in ILK wild-type cells, and the level of endogenous Notch1-IC was increased by the blocking of the proteasome, suggesting that ILK enhances the proteasomal degradation of Notch1-IC. ILK directly bound and phosphorylated Notch1-IC, thereby facilitating proteasomal protein degradation through Fbw7. Furthermore, we found down-regulation of Notch1-IC and up-regulation of ILK in basal cell carcinoma and melanoma patients but not in squamous cell carcinoma patients. These results suggest that ILK down-regulated the protein stability of Notch1-IC through the ubiquitin-proteasome pathway by means of Fbw7.</P>