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In the rapidly developing world of information technology, computers have been used in various settings for clinical medicine application. Studies have focused on computerized physician order entry (CPOE) system interface design and functional development to achieve a successful technology adoption process. Therefore, the purpose of this study was to evaluate physician satisfaction with the CPOE system. This survey included user attitude toward interface design, operation functions/usage effectiveness, interface usability, and user satisfaction. We used questionnaires for data collection from June to August 2008, and 225 valid questionnaires were returned with a response rate of 84.5 %. Canonical correlation was applied to explore the relationship of personal attributes and usability with user satisfaction. The results of the data analysis revealed that certain demographic groups showed higher acceptance and satisfaction levels, especially residents, those with less pressure when using computers or those with less experience with the CPOE systems. Additionally, computer use pressure and usability were the best predictors of user satisfaction. Based on the study results, it is suggested that future CPOE development should focus on interface design and content links, as well as providing educational training programs for the new users; since a learning curve period should be considered as an indespensible factor for CPOE adoption.

The assembly of four pore-forming ␣-subunits into tetramers is a prerequisite for the formation of functional K ؉ channels. A short carboxyl assembly domain (CAD) in the distal end of the cytoplasmic carboxyl terminus has been implicated in the assembly of Eag ␣-subunits, a subfamily of the ether-à-go-go K ؉ channel family. The precise role of CAD in the formation of Eag tetrameric channels, however, remains unclear. Moreover, it has not been determined whether other protein regions also contribute to the assembly of Eag subunits. We addressed these questions by studying the biophysical properties of a series of different rat Eag1 (rEag1) truncation mutants. Two truncation mutants without CAD (K848X and W823X) yielded functional phenotypes similar to those for wild-type (WT) rEag1 channels. Furthermore, nonfunctional rEag1 truncation mutants lacking the distal region of the carboxyl terminus displayed substantial dominant-negative effects on the functional expression of WT as well as K848X and W823X channels. Our co-immunoprecipitation studies further revealed that truncation mutants containing no CAD indeed displayed significant association with rEag1-WT subunits. Finally, surface biotinylation and protein glycosylation analyses demonstrated that progressive truncations of the carboxyl terminus resulted in aggravating disruptions of membrane trafficking and glycosylation of rEag1 proteins. Overall, our data suggest that the distal carboxyl terminus, including CAD, is dispensable for the assembly of rEag1 K ؉ channels but may instead be essential for ensuring proper protein biosynthesis. We propose that the S6 segment and the proximal carboxyl terminus may constitute the principal subunit recognition site for the assembly of rEag1 channels.

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