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Estrella Díaz,Rocío Carranza,Carlos Sánchez-Camacho,David Martín-Consuegra 글로벌지식마케팅경영학회 2018 Global Marketing Conference Vol.2018 No.07
In today’s highly dynamic tourism and hospitality environment, the role of customer engagement (CE) in customer experience and value is receiving increasing attention from practitioners and academics (Harrigan, Evers, Miles, & Daly, 2017). Despite this interest, scholarly analysis into the concept and its associated elements has been limited to date. For these reasons, the objective of this study is to present a science mapping approach to analysing the thematic evolution of customer engagement, specifically in the tourism/hospitality and marketing industries. The study applies a bibliometric approach combining co-citation analysis with co-word analysis to reveal and visualize the evolution of customer engagement in the hospitality and tourism areas. Specifically, authors use the SciMat software in order to discover the most important research themes and its conceptual evolution. This technique returns a set of clusters, which can be understood as conglomerates of different scientific aspects. They allow researchers the analysis of the research topics’ dynamic evolution by measuring continuance across consecutive sub-periods. Authors followed the ranking of hospitality and tourism journals considered by Gursoy and Sandstrom (2016) and, the marketing journal ranking developed by Hunt Reimann and Schilke (2009) as criteria for journal selection process. This study has considered the Web of Science (WoS) as the main academic database for collecting research contributions. Findings indicate symptoms of a research field in constant evolution that has not yet reached a stage of maturity. Initially, customer engagement was seen as an important element, but its examination was scarce and has gradually come to be recognized as a key goal within organizations to serve as a basis for the development of various study models. The results obtained from this study will enable future authors studying customer engagement to focus their studies more effectively.
Estrella D?az,Roc?o Carranza,Carlos S?nchez-Camacho,?gueda Esteban,David Mart?n-Consuegra 글로벌지식마케팅경영학회 2023 Global Marketing Conference Vol.2023 No.07
Smart technologies are critical for businesses to develop these dynamic connections, as technologies enable them to network with others and exchange resources seamlessly. This fact makes it possible to modify the tasks performed by employees of tourism organizations that are in contact with consumers/tourists.
Estrella, Liezel L.,Lee, Sang Hee,Kim, Dong Hee Elsevier 2019 Dyes and pigments Vol.165 No.-
<P><B>Abstract</B></P> <P>Four novel dyes featuring new semi-rigid triphenylamine donor groups have been synthesized and successfully employed as sensitizers in dye-sensitized solar cells (DSSCs). Opting for the new semi-rigid triphenylamine (tPA) electron-donating unit yielded a better <I>V</I> <SUB>oc</SUB> and <I>J</I> <SUB>sc</SUB> resulting to a power conversion efficiency (PCE) which is 16% higher compared to a reference dye whose electron-donating group is a conventional tPA unit. Density functional theory (DFT) and time-dependent DFT calculations revealed the more favorable charge-transport properties of the dye based on the new semi-rigid donor unit. Among the synthesized dyes, the DSSC device based on <B>Dhkx-4</B> dye in conjunction with iodine-based electrolyte achieved a PCE of 6.23%, with <I>V</I> <SUB>oc</SUB> of 0.661 V, <I>J</I> <SUB>sc</SUB> of 13.31 mAcm<SUP>−2</SUP>, and <I>FF</I> of 0.71 under simulated AM 1.5 G condition. Therefore, the novel semi-rigid tPA donor unit presented in this work is a promising donor group for a sensitizer in DSSCs and systematic structural engineering of the presented designs could offer valuable contributions for the development of the photovoltaic devices.</P> <P><B>Highlights</B></P> <P> <UL> <LI> D-π-A dyes based on a new semi-rigid triphenylamine donor were synthesized for DSSCs. </LI> <LI> The new <B>Dhkx-1</B> dye attained a PCE that is 16% higher than the <B>L1</B> reference dye. </LI> <LI> The experimental data are interpreted well by the results of DFT/TD-DFT calculation. </LI> <LI> The solar cell device based on a simple <B>Dhkx-4</B> dye attained the highest PCE of 6.23%. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
Binding of Lichen Phenolics to Purified Secreted Arginase from the Lichen Evernia prunastri
Legaz, Maria-Estrella,Vicente, Carlos,Pedrosa, Mercedes M. Korean Society for Biochemistry and Molecular Biol 2001 Journal of biochemistry and molecular biology Vol.34 No.3
Secreted arginase from Evernia prunastri thallus has been purified 616-fold from the incubation medium. Purified arginase was resolved as only one peak in a capillary electrophoresis with a pI value of 5.35. The protein contained high amounts of acidic amino acids, such as Asx and Glx, and a relatively high quantity of Ser and Gly. The molecular mass of native, purified arginase was estimated as about 26 kDa by SE-HPLC. Substrate saturated kinetic showed a typical Michaelis-Menten relationship with a K_m value of 3.3 mM L-arginine. Atranorin behaved as a mixed activator of the enzyme (apparent $K_m$ = 0.96 mM); whereas evernic and usnic acid were revealed as non competitive inhibitors (apparent $K_m$ values were 3.16 mM and 3.05 mM, respectively). Kinetics of atranorin binding indicated that saturation was reached from 0.18 ${\mu}mol$ of the total atranorin and the occurrence of multiple sites for the ligand. This agrees with a possible aggregation of several enzyme subunits during the interaction process. A value of binding sites of about 12 was obtained. The binding of evernic acid was saturated from 23 nmol of total phenol. The number of binding sites was about 5. The loss of the binding ability of evernic acid could be interpreted as a single negative cooperatively. Usnic acid behaves in a similar way to evernic acid, although the binding saturation occurs at $0.14\;{\mu}moles$ of the ligand. This binding appears to be unspecific, and has 28 usnic acid binding sites to the protein.
Binding of Lichen Phenolics to Purified Secreted Arginase from the Lichen Evernia prunastri
Legaz, Maria Estrella,Vicente, Carlos,Pedrosa, Mercedes M . 생화학분자생물학회 1970 BMB Reports Vol.34 No.3
Secreted arginase from Evernia prunnstri thallus has been purified 616-fold from the incubation medium. Purified arginase was resolved as only one peak in a capillary electrophoresis with a pI value of 5.35. The protein contained high amounts of acidic amino acids, such as Asx and Glx, and a relatively high quantity of Ser and Gly. The molecular mass of native, purified arginase was estimated as about 26 kDa by SE-HPLC. Substrate saturated kinetic showed a typical Michaelis-Menten relationship with a K_m value of 3.3 mM L-arginine. Atranorin behaved as a mixed activator of the enzyme (apparent K_m = 0.96 mM); whereas evernic and usnic acid were revealed as non competitive inhibitors (apparent K_m values were 3.16 mM and 3.05 mM, respectively). Kinetics of atranorin binding indicated that saturation was reached from 0.18 μmol of the total atranorin and the occurrence of multiple sites for the ligand. This agrees with a possible aggregation of several enzyme subunits during the interaction process. A value of binding sites of about 12 was obtained. The binding of evernic acid was saturated from 23 nmol of total phenol. The number of binding sites was about 5. The loss of the binding ability of evernic acid could be interpreted as a single negative cooperatively. Usnic acid behaves in a similar way to evernic acid, although the binding saturation occurs at 0.14 μmoles of the ligand. This binding appears to be unspecific, and has 28 usnic acid binding sites to the protein.
Fam83h is Associated with Intracellular Vesicles and ADHCAI
Ding, Y.,Estrella, M.R.P.,Hu, Y.Y.,Chan, H.L.,Zhang, H.D.,Kim, J.-W.,Simmer, J.P.,Hu, J.C.-C. SAGE Publications 2009 Journal of dental research Vol.88 No.11
<P>Defects in <I>FAM83H</I> on human chromosome 8q24.3 cause autosomal-dominant hypocalcified amelogenesis imperfecta (ADHCAI). <I>FAM83H</I> does not encode a recognizable signal peptide, so we predicted that the Fam83h protein functions within the cell. We tested this hypothesis by constitutively expressing mouse Fam83h with green fluorescent protein (GFP) fused to its C-terminus in HEK293 and HeLa cell lines. Green fluorescent signal from the Fam83h-GFP fusion protein was associated with perinuclear vesicles, usually in the vicinity of the Golgi apparatus. No signal was observed within the nucleus. In addition, we identified <I> FAM83H</I> nonsense mutations in Hispanic (C1330C>T; p.Q444X) and Caucasian (c.1192C>T; p.Q398X) families with ADHCAI. We conclude that Fam83h localizes in the intracellular environment, is associated with vesicles, and plays an important role in dental enamel formation. <I>FAM83H</I> is the first gene involved in the etiology of amelogenesis imperfecta (AI) that does not encode a secreted protein.</P>