Internet-based Framework to Support Integration of Customer in the Design of Customizable Products

A necessary element to design and produce customer-centric products is the integration of customers in the design process. Challenges faced during customer integration into the design process include generating models of the customized product, performing analysis of these to determine feasibility, and optimizing to increase the performance. These tasks have to be performed relatively quickly, if not in real time, to provide feedback to the customer. The focus of this article is to present a framework that utilizes CAD, finite element analysis (FEA), and optimization to integrate the customer into the design process via the Internet for delivering user customized products. The design analysis, evaluation, and optimization need to be automated and enhanced to enable operation over the Internet. A product family CAD/FEA template has been developed to perform analysis, along with a general formulation to optimize the customized product. The CAD/FEA template generalizes the geometry building and analysis of each configuration developed using a product platform approach. The proposed setup is demonstrated through the use of a bicycle frame family. In this study, the focus is on the application of optimization and FEA to facilitate the design of customer-centric products.Yeshttps://us.sagepub.com/en-us/nam/manuscript-submission-guideline

Hsc70 Focus Formation at the Periphery of HSV-1 Transcription Sites Requires ICP27

The cellular chaperone protein Hsc70, along with components of the 26S proteasome and ubiquitin-conjugated proteins have been shown to be sequestered in discrete foci in the nuclei of herpes simplex virus 1 (HSV-1) infected cells. We recently reported that cellular RNA polymerase II (RNAP II) undergoes proteasomal degradation during robust HSV-1 transcription, and that the immediate early protein ICP27 interacts with the C-terminal domain and is involved in the recruitment of RNAP II to viral transcription/replication compartments.Here we show that ICP27 also interacts with Hsc70, and is required for the formation of Hsc70 nuclear foci. During infection with ICP27 mutants that are unable to recruit RNAP II to viral replication sites, viral transcript levels were greatly reduced, viral replication compartments were poorly formed and Hsc70 focus formation was curtailed. Further, a dominant negative Hsc70 mutant that cannot hydrolyze ATP, interfered with RNAP II degradation during HSV-1 infection, and an increase in ubiquitinated forms of RNAP II was observed. There was also a decrease in virus yields, indicating that proteasomal degradation of stalled RNAP II complexes during robust HSV-1 transcription and replication benefits viral gene expression.We propose that one function of the Hsc70 nuclear foci may be to serve to facilitate the process of clearing stalled RNAP II complexes from viral genomes during times of highly active transcription