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Gyumee Cheon,Yongsoo Cheon 보안공학연구지원센터 2016 International Journal of u- and e- Service, Scienc Vol.9 No.10
Recently, as CSR activities have come into the spotlight and customers have begun to sensitively respond to CSR issues, various studies about CSR have also been carried out in various areas such as corporate study, marketing study, business ethics study, and business strategy study. In this context, a hotel company’s CSR activity needs to be regarded as the top value not only for the realization of fair society, but also for the improvements of the corporate image and the customers’ satisfaction. For these reasons, this study aims to explore “the relationship between H-CSR activity and the service value and satisfaction perceived by customers” and “how service value affects customers’ satisfaction for hotel companies.” The results revealed as follows. First, the factor of public or social dimension and legal order has a significant influence on quality value, price value, and customer satisfaction. Second, quality value and price value have significant influences on customer satisfaction. The results also imply that hotel customers feel their satisfaction in terms of hotels’ quality and price values. That is, rather than time and efforts to get satisfaction, direct factors such as quality and price values have more effects on customer satisfaction.
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Park, Cheon-Gyu,Park, Yongsoo,Suh, Byung-Chang The Rockefeller University Press 2017 The Journal of general physiology Vol.149 No.2
<P>The β subunit of voltage-gated Ca<SUP>2+</SUP> (Ca<SUB>V</SUB>) channels plays an important role in regulating gating of the α1 pore-forming subunit and its regulation by phosphatidylinositol 4,5-bisphosphate (PIP<SUB>2</SUB>). Subcellular localization of the Ca<SUB>V</SUB> β subunit is critical for this effect; N-terminal–dependent membrane targeting of the β subunit slows inactivation and decreases PIP<SUB>2</SUB> sensitivity. Here, we provide evidence that the HOOK region of the β subunit plays an important role in the regulation of Ca<SUB>V</SUB> biophysics. Based on amino acid composition, we broadly divide the HOOK region into three domains: S (polyserine), A (polyacidic), and B (polybasic). We show that a β subunit containing only its A domain in the HOOK region increases inactivation kinetics and channel inhibition by PIP<SUB>2</SUB> depletion, whereas a β subunit with only a B domain decreases these responses. When both the A and B domains are deleted, or when the entire HOOK region is deleted, the responses are elevated. Using a peptide-to-liposome binding assay and confocal microscopy, we find that the B domain of the HOOK region directly interacts with anionic phospholipids via polybasic and two hydrophobic Phe residues. The β2c-short subunit, which lacks an A domain and contains fewer basic amino acids and no Phe residues in the B domain, neither associates with phospholipids nor affects channel gating dynamically. Together, our data suggest that the flexible HOOK region of the β subunit acts as an important regulator of Ca<SUB>V</SUB> channel gating via dynamic electrostatic and hydrophobic interaction with the plasma membrane.</P>
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