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Träfflista för sökning "WFRF:(Krogh Vittorio) ;pers:(Olsen Anja);srt2:(2010);pers:(Clavel Chapelon Francoíse)"

Sökning: WFRF:(Krogh Vittorio) > Olsen Anja > (2010) > Clavel Chapelon Francoíse

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  • Buck, Dietrich, 1990-, et al. (författare)
  • Production and In-Plane Compression Mechanics of Alternatively Angled Layered Cross-Laminated Timber
  • 2018
  • Ingår i: BioResources. - : University of North Carolina Press. - 1930-2126 .- 1930-2126. ; 13:2, s. 4029-4045
  • Tidskriftsartikel (refereegranskat)abstract
    • Increasing awareness of sustainable building materials has led to interest in enhancing the structural performance of engineered wood products. This paper reports mechanical properties of cross-laminated timber (CLT) panels constructed with layers angled in an alternative configuration on a modified industrial CLT production line. Timber lamellae were adhesively bonded together in a single-step press procedure to form CLT panels. Transverse layers were laid at an angle of 45°, instead of the conventional 90° angle with respect to the longitudinal layers’ 0° angle. Tests were carried out on 20 five-layered CLT panels divided into two matched groups with either a 45° or a 90° configuration; an in-plane uniaxial compressive loading was applied in the principal orientation of the panels. These tests showed that the 45°-configured panels had a 30% higher compression stiffness and a 15% higher compression strength than the 90° configuration. The results also revealed that the 45°-configured CLT can be industrially produced without using more material than is required for conventional CLT 90° panels. In addition, the design possibility that the 45°-configured CLT can carry a given load while using less material also suggests that it is possible to use CLT in a wider range of structural applications.
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  • Voss, Sylvia, et al. (författare)
  • The Choline-binding Protein PspC of Streptococcus pneumoniae Interacts with the C-terminal Heparin-binding Domain of Vitronectin
  • 2013
  • Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 288:22, s. 15614-15627
  • Tidskriftsartikel (refereegranskat)abstract
    • Adherence of Streptococcus pneumoniae is directly mediated by interactions of adhesins with eukaryotic cellular receptors or indirectly by exploiting matrix and serum proteins as molecular bridges. Pneumococci engage vitronectin, the human adhesive glycoprotein and complement inhibitor, to facilitate attachment to epithelial cells of the mucosal cavity, thereby modulating host cell signaling. In this study, we identified PspC as a vitronectin-binding protein interacting with the C-terminal heparin-binding domain of vitronectin. PspC is a multifunctional surface-exposed choline-binding protein displaying various adhesive properties. Vitronectin binding required the R domains in the mature PspC protein, which are also essential for the interaction with the ectodomain of the polymeric immunoglobulin receptor and secretory IgA. Consequently, secretory IgA competitively inhibited binding of vitronectin to purified PspC and to PspC-expressing pneumococci. In contrast, Factor H, which binds to the N-terminal part of mature PspC molecules, did not interfere with the PspC-vitronectin interaction. Using a series of vitronectin peptides, the C-terminal heparin-binding domain was shown to be essential for the interaction of soluble vitronectin with PspC. Binding experiments with immobilized vitronectin suggested a region N-terminal to the identified heparin-binding domain as an additional binding region for PspC, suggesting that soluble, immobilized, as well as cellularly bound vitronectin possesses different conformations. Finally, vitronectin bound to PspC was functionally active and inhibited the deposition of the terminal complement complex. In conclusion, this study identifies and characterizes (on the molecular level) the interaction between the pneumococcal adhesin PspC and the human glycoprotein vitronectin.
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