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연광흠,송인호,정성종,Yeon Kwang-Heum,Song In-Ho,Chung Sung-Chong 대한기계학회 2005 大韓機械學會論文集A Vol.29 No.10
Injection-molded products serve a wide range of applications in our modem lives and their significance is ever increasing. However, difficulty of communication among related companies under the present system results in increase of lead time and decrease of production efficiency. The objective of this paper is the development of a web-based draft verification system in mold design processes. Although several commercial CAD systems offer draft verification functions, those systems are very expensive and inadequate to perform collaborative works. For collaborative work under the distributed environment, the proposed system uses native file transforming of CAD data into optimal format by using the ACIS kernel and InterOp. Functions of draft verification modules are constructed over the ActiveX control using the visual C++ and OpenGL. Therefore, collaborators related to the development of a new product are able to verify the draft and undercut over the Internet without commercial CAD systems. The system helps to reduce production cost, errors and lead-time to the market. Performance of the system is confirmed through various case studies.
The PPLA Motif of Glycogen Synthase Kinase 3beta Is Required for Interaction with Fe65
이은정,현성희,전재순,신성화,이경은,연광흠,박태윤,강상순 한국분자세포생물학회 2008 Molecules and cells Vol.26 No.1
Glycogen synthase kinase 3β (GSK 3β) is a serine/ threonine kinase that phosphorylates substrates such as β-catenin and is involved in a variety of biological processes, including embryonic development, metabolism, tumorigenesis, and cell death. Here, we present evidence that human GSK 3β is associated with Fe65, which has the characteristics of an adaptor protein, possessing a WW domain, and two phosphotyrosine interaction domains, PID1 and PID2. The GSK 3β catalytic domain also contains a putative WW domain binding motif (371PPLA374), and we observed, using a pull down approach and co-immunoprecipitation, that it interacts physically with Fe65 via this motif. In addition, we detected co-localization of GSK 3β and Fe65 by confocal microscopy, and this co-localization was disrupted by mutation of the putative WW domain binding motif of GSK 3β. Finally, in transient transfection assays interaction of GSK 3β (wt) with Fe65 induced substantial cell apoptosis, whereas interaction with the GSK 3β AALA mutant (371AALA374) did not, and we noted that phosphorylation of the Tyr 216 residue of the GSK 3β AALA mutant was significantly reduced compared to that of GSK 3β wild type. Thus, our observations indicate that GSK 3β binds to Fe65 through its 371PPLA374 motif and that this interaction regulates apoptosis and phosphorylation of Tyr 216 of GSK 3β.