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A Methodological Shift in Building Design through Development of Collaborative Design Platforms
Schumacher, Jonatan,Naugle, Matthew Council on Tall Building and Urban Habitat Korea 2014 International journal of high-rise buildings Vol.3 No.4
This paper introduces two platforms created by the development team at CORE studio, Thornton Tomasetti's global innovation studio. Collaborative platforms change the way that parties communicate and develop projects. Wikipedia is one of many great examples for a platform that supports collaborative development of a product - the world's largest encyclopedia. In the AEC industry, no such platform exists that can be used for collaborative development of a building project, and hence, information exchange between the parties involved, and modeling programs used in a project is slow and opaque. The platforms introduced in this paper allow for much greater transparency at all stages of the building design process, and hence improve the flow of information between parties involved in the process, both firm-internal and external. While traditionally, the use of a large number of different modeling and analysis platforms is hard to manage by a project team; this paper introduces methods that strengthen the design process by using a multitude of programs needed in the different building design phases.
Involvement of 14-3-3 in tubulin instability and impaired axon development is mediated by Tau
Joo, Yuyoung,Schumacher, Benjamin,Landrieu, Isabelle,Bartel, Maria,Smet-Nocca, Caroline,Jang, Ahram,Choi, Hee Soon,Jeon, Noo Li,Chang, Keun-A,Kim, Hye-Sun,Ottmann, Christian,Suh, Yoo-Hun The Federation of American Societies for Experimen 2015 The FASEB Journal Vol.29 No.10
<P>14-3-3 proteins act as adapters that exert their function by interacting with their various protein partners. 14-3-3 proteins have been implicated in a variety of human diseases including neurodegenerative diseases. 14-3-3 proteins have recently been reported to be abundant in the neurofibrillary tangles (NFTs) observed inside the neurons of brains affected by Alzheimer’s disease (AD). These NFTs are mainly constituted of phosphorylated Tau protein, a microtubule-associated protein known to bind 14-3-3. Despite this indication of 14-3-3 protein involvement in the AD pathogenesis, the role of 14-3-3 in the Tauopathy remains to be clarified. In the present study, we shed light on the role of 14-3-3 proteins in the molecular pathways leading to Tauopathies. Overexpression of the 14-3-3σ isoform resulted in a disruption of the tubulin cytoskeleton and prevented neuritic outgrowth in neurons. NMR studies validated the phosphorylated residues pSer214 and pSer324 in Tau as the 2 primary sites for 14-3-3 binding, with the crystal structure of 14-3-3σ in complex with Tau-pSer214 and Tau-pSer324 revealing the molecular details of the interaction. These data suggest a rationale for a possible pharmacologic intervention of the Tau/14-3-3 interaction.—Joo, Y., Schumacher, B., Landrieu, I., Bartel, M., Smet-Nocca, C., Jang, A., Choi, H. S., Jeon, N. L., Chang, K.-A., Kim, H.-S., Ottmann, C., Suh, Y.-H. Involvement of 14-3-3 in tubulin instability and impaired axon development is mediated by Tau.</P>