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Sökning: WFRF:(Bottcher S) > (2005-2009)

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  • Figge, S, et al. (författare)
  • Optoelectronic devices on bulk GaN
  • 2005
  • Ingår i: Journal of Crystal Growth. - : Elsevier BV. - 0022-0248 .- 1873-5002. ; 281:1, s. 101-106
  • Tidskriftsartikel (refereegranskat)abstract
    • The homoeptaxial fabrication of GaN-based devices has advantages against heteroepitaxial realization on substrates such as sapphire or SiC, since heteroepitaxy implies a lot of problems like lattice mismatch, different thermal expansion coefficients, and needs an extensive optimization of the growth at the heterointerface. In this paper we will discuss GaN-based light-emitting devices grown by homoepitaxy in comparison to devices grown on sapphire. A special emphasis is laid on the pretreatment of the GaN substrate and the device characteristics on different substrates. In detail will be discussed the advantages of the higher thermal conductivity of GaN and how this effects the device performance. (c) 2005 Elsevier B.V. All rights reserved.
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3.
  • Maynard, Christa J., et al. (författare)
  • Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment
  • 2009
  • Ingår i: Proceedings of the National Academy of Sciences. - : Proceedings of the National Academy of Sciences. - 1091-6490 .- 0027-8424. ; 106:33, s. 13986-13991
  • Tidskriftsartikel (refereegranskat)abstract
    • Aggregation-prone proteins have been suggested to overwhelm and impair the ubiquitin/proteasome system (UPS) in polyglutamine (polyQ) disorders, such as Huntington's disease (HD). Overexpression of an N-terminal fragment of mutant huntingtin (N-mutHtt), an aggregation-prone polyQ protein responsible for HD, obstructs the UPS in cellular models. Furthermore, based on the accumulation of polyubiquitin conjugates in brains of R6/2 mice, which express human N-mutHtt and are one of the most severe polyQ disorder models, it has been proposed that UPS dysfunction is a consistent feature of this pathology, occurring in both in vitro and in vivo models. Here, we have exploited transgenic mice that ubiquitously express a ubiquitin fusion degradation proteasome substrate to directly assess the functionality of the UPS in R6/2 mice or the slower onset R6/1 mice. Although expression of N-mutHtt caused a general inhibition of the UPS in PC12 cells, we did not observe an increase in the levels of proteasome reporter substrate in the brains of R6/2 and R6/1 mice. We show that the increase in ubiquitin conjugates in R6/2 mice can be primarily attributed to an accumulation of large ubiquitin conjugates that are different from the conjugates observed upon UPS inhibition. Together our data show that polyubiquitylated proteins accumulate in R6/2 brain despite a largely operative UPS, and suggest that neurons are able to avoid or compensate for the inhibitory effects of N-mutHtt.
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