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Träfflista för sökning "WFRF:(Quaglia D.) srt2:(2017)"

Sökning: WFRF:(Quaglia D.) > (2017)

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1.
  • Grüttner, K., et al. (författare)
  • CONTREX : Design of embedded mixed-criticality CONTRol systems under consideration of EXtra-functional properties
  • 2017
  • Ingår i: Microprocessors and microsystems. - : Elsevier B.V.. - 0141-9331 .- 1872-9436. ; 51, s. 39-55
  • Tidskriftsartikel (refereegranskat)abstract
    • The increasing processing power of today's HW/SW platforms leads to the integration of more and more functions in a single device. Additional design challenges arise when these functions share computing resources and belong to different criticality levels. CONTREX complements current activities in the area of predictable computing platforms and segregation mechanisms with techniques to consider the extra-functional properties, i.e., timing constraints, power, and temperature. CONTREX enables energy efficient and cost aware design through analysis and optimization of these properties with regard to application demands at different criticality levels. This article presents an overview of the CONTREX European project, its main innovative technology (extension of a model based design approach, functional and extra-functional analysis with executable models and run-time management) and the final results of three industrial use-cases from different domain (avionics, automotive and telecommunication).
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2.
  • Piovesan, Damiano, et al. (författare)
  • DisProt 7.0 : a major update of the database of disordered proteins
  • 2017
  • Ingår i: Nucleic Acids Research. - : Oxford University Press (OUP). - 0305-1048 .- 1362-4962. ; 45:D1, s. d219-D227
  • Tidskriftsartikel (refereegranskat)abstract
    • The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance ( primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.
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