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RISS 인기검색어
- 검색키워드
- 저자 : Bagley, Mark J (검색결과 3 건)
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The Mixed-Use Supertall and the Hybridization of Program
Bagley, Forth Council on Tall Building and Urban Habitat Korea 2018 International journal of high-rise buildings Vol.7 No.1
Increasingly, mixed-use, multi-program complexes are emerging as the standard development model around the world. As their prominence grows, these projects are becoming increasingly complex. Program adjacencies are ever more intertwined as developers (and the architects who support them) are becoming more comfortable blurring the traditional boundaries between office, retail, residential and hospitality. This article discusses a second generation of mixed-use projects that embrace this hybridization, honing in on supertall architecture, their hybrid program offerings, and innovative sky lobbies. It concludes that programmatic advancements will continue to expand and find integration within single structures, both repositioned and built from the ground up.
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Kim, Kyung Seok,Bagley, Mark J,Coates, Brad S,Hellmich, Richard L,Sappington, Thomas W Entomological Society of America 2009 Environmental entomology Vol.38 No.4
<P>European corn borer, Ostrinia nubilalis (Hübner), adults were sampled at 13 sites along two perpendicular 720-km transects intersecting in central Iowa and for the following two generations at four of the same sites separated by 240 km in the cardinal directions. More than 50 moths from each sample location and time were genotyped at eight microsatellite loci. Spatial analyses indicated that there is no spatial genetic structuring between European corn borer populations sampled 720 km apart at the extremes of the transects and no pattern of genetic isolation by distance at that geographic scale. Although these results suggest high gene flow over the spatial scale tested, it is possible that populations have not had time to diverge since the central Corn Belt was invaded by this insect approximately 60 yr ago. However, temporal analyses of genetic changes in single locations over time suggest that the rate of migration is indeed very high. The results of this study suggest that the geographic dimensions of European corn borer populations are quite large, indicating that monitoring for resistance to transgenic Bt corn at widely separated distances is justified, at least in the central Corn Belt. High gene flow further implies that resistance to Bt corn may be slow to evolve, but once it does develop, it may spread geographically with such speed that mitigation strategies will have to be implemented quickly to be effective.</P>
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Kwon, Min Jee,Han, Myeong Hoon,Bagley, Joshua A.,Hyeon, Do Young,Ko, Byung Su,Lee, Yun Mi,Cha, In Jun,Kim, Seung Yeol,Kim, Dong Young,Kim, Ho Min,Hwang, Daehee,Lee, Sung Bae,Jan, Yuh Nung National Academy of Sciences 2018 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.115 No.45
<P><B>Significance</B></P><P>It remains unclear how the structural properties of polyglutamine (polyQ) proteins, which underlie several neurodegenerative disorders, including Huntington’s disease and spinocerebellar ataxias (SCAs), translate into the toxicity of these proteins. Here, we demonstrate that coiled-coil structures in expanded polyQ regions of SCA type 3 (SCA3) proteins cause dendrite defects in <I>Drosophila</I> neurons, as well as behavioral abnormalities. Moreover, interactions of SCA3 with Foxo mediated by coiled-coil domains of these two proteins resulted in functional impairment of this transcription factor, whereas its overexpression significantly rescued the SCA3-induced defects. Our study expanded the current understanding of neuronal pathology mediated by polyQ proteins via the coiled-coil–mediated interactions. These results may have important implications in therapeutic strategies for polyQ protein-related diseases.</P><P>Neurodegenerative disorders, such as Huntington’s diseases and spinocerebellar ataxias (SCAs), are driven by proteins with expanded polyglutamine (polyQ) tracts. Recently, coiled-coil structures in polyQ regions of such proteins were shown to facilitate aggregate formation and ultimately lead to cell death. However, the molecular mechanism linking these structural domains to neuronal toxicity of polyQ proteins remains elusive. Here, we demonstrate that coiled-coil structures in the Q repeat region of SCA type 3 (SCA3) polyQ proteins confer protein toxicity in <I>Drosophila</I> neurons. To functionally characterize coiled-coil structures in the Q repeat regions, we generated three structural variants of SCA3 polyQ proteins: (<I>i</I>) MJDtr-76Q, containing both α-helical coiled-coil and β-sheet hairpin structures in the Q repeat region; (<I>ii</I>) MJDtr-70Q_cc0, possessing only α-helical coiled-coil structures due to the incorporation of β-sheet–breaking residues (Q-to-N or Q-to-E mutations); and (<I>iii</I>) MJDtr-70Q_pQp, with no secondary structure due to the introduced proline residues (Q-to-P mutations). Through comparative analysis of these variants, we found that coiled-coil structures facilitated nuclear localization of SCA3 polyQ proteins and induced dendrite defects in <I>Drosophila</I> dendritic arborization neurons. Furthermore, genetic and functional screening identified the transcription factor Foxo as a target of polyQ proteins, and coiled-coil–mediated interactions of Foxo and polyQ proteins in the nucleus resulted in the observed dendrite and behavioral defects in <I>Drosophila</I>. These results demonstrate that coiled-coil structures of polyQ proteins are crucial for their neuronal toxicity, which is conferred through coiled-coil to coiled-coil interactions with the nuclear targets of these proteins.</P>
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