SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "WFRF:(Frank Göran) ;lar1:(cth)"

Search: WFRF:(Frank Göran) > Chalmers University of Technology

  • Result 1-10 of 16
Sort/group result
   
EnumerationReferenceCoverFind
1.
  • Citrin, J., et al. (author)
  • Tractable flux-driven temperature, density, and rotation profile evolution with the quasilinear gyrokinetic transport model QuaLiKiz
  • 2017
  • In: Plasma Physics and Controlled Fusion. - : IOP Publishing. - 1361-6587 .- 0741-3335. ; 59:12
  • Journal article (peer-reviewed)abstract
    • Quasilinear turbulent transport models are a successful tool for prediction of core tokamak plasma profiles in many regimes. Their success hinges on the reproduction of local nonlinear gyrokinetic fluxes. We focus on significant progress in the quasilinear gyrokinetic transport model QuaLiKiz (Bourdelle et al 2016 Plasma Phys. Control. Fusion 58 014036), which employs an approximated solution of the mode structures to significantly speed up computation time compared to full linear gyrokinetic solvers. Optimisation of the dispersion relation solution algorithm within integrated modelling applications leads to flux calculations x 10(6-7) faster than local nonlinear simulations. This allows tractable simulation of flux-driven dynamic profile evolution including all transport channels: ion and electron heat, main particles, impurities, and momentum. Furthermore, QuaLiKiz now includes the impact of rotation and temperature anisotropy induced poloidal asymmetry on heavy impurity transport, important for W-transport applications. Application within the JETTO integrated modelling code results in 1 s of JET plasma simulation within 10 h using 10 CPUs. Simultaneous predictions of core density, temperature, and toroidal rotation profiles for both JET hybrid and baseline experiments are
  •  
2.
  • 2018
  • In: Nuclear Fusion. - : IOP Publishing. - 1741-4326 .- 0029-5515. ; 58:1
  • Research review (peer-reviewed)
  •  
3.
  •  
4.
  •  
5.
  •  
6.
  • Nasir, Waqas, et al. (author)
  • Histo-Blood Group Antigen Presentation Is Critical for Binding of Norovirus VLP to Glycosphingolipids in Model Membranes
  • 2017
  • In: Acs Chemical Biology. - : American Chemical Society (ACS). - 1554-8929 .- 1554-8937. ; 12:5, s. 1288-1296
  • Journal article (peer-reviewed)abstract
    • Virus entry depends on biomolecular recognition at the surface of cell membranes. In the case of glycolipid receptors, these events are expected to be influenced by how the glycan epitope close to the membrane is presented to the virus. This presentation of membrane associated glycans is more restricted than that of glycans in solution, particularly because of orientational constraints imposed on the glycolipid through its lateral interactions with other membrane lipids and proteins. We have developed and employed a total internal reflection fluorescence microscopy-based binding assay and. a scheme for molecular dynamics (MD) membrane simulations to investigate the consequences of various glycan presentation effects. The system studied was histo-blood group antigen (HBGA) epitopes of membrane-bound glycosphingolipids (GSLs) derived from small intestinal epithelium of humans (type 1 chain) and dogs (type 2 chain) interacting with GII.4 norovirus-like particles. Our experimental results showed strong binding to all lipid-linked type 1 chain HBGAs but no or only weak binding to the corresponding type 2 chain HBGAs. This is in contrast to results derived from STD experiments with free HBGAs in solution where binding was observed for Lewis x. The MD data suggest that the strong binding to type 1 chain glycolipids was due to the well-exposed (1,2)-linked alpha-L-Fucp and (1,4)- linked alpha-L-Fucp residues, while the weaker binding or lack of binding to type 2 chain HBGAs was due to the very restricted accessibility of the (1,3) -linked alpha-L-Fucp residue when the glycolipid is embedded in a phospholipid membrane. Our results not only contribute to a general understanding of protein carbohydrate interactions on model membrane surfaces, particularly in the context of virus binding, but also suggest a possible role of human intestinal GSLs as potential receptors for norovirus uptake.
  •  
7.
  •  
8.
  •  
9.
  •  
10.
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-10 of 16
Type of publication
journal article (12)
conference paper (3)
research review (1)
Type of content
peer-reviewed (16)
Author/Editor
Enoksson, Peter, 195 ... (6)
Stemme, Göran, 1958 (6)
Niklaus, Frank (5)
Kälvesten, Edvard, 1 ... (5)
Persson, Frank, 1970 (4)
Nylund, Göran M., 19 ... (4)
show more...
Pavia, Henrik, 1964 (4)
Hermansson, Malte, 1 ... (4)
Cervin, Gunnar, 1967 (3)
Rubel, Marek (2)
Frassinetti, Lorenzo (2)
Menmuir, Sheena (2)
Hellsten, Torbjörn (2)
Petrzilka, V (2)
Strand, Pär, 1968 (2)
Cecconello, Marco (2)
Zychor, I (2)
Garcia-Munoz, M. (2)
Andersson, Helene (2)
Bykov, Igor (2)
Garcia-Carrasco, Alv ... (2)
Rachlew, Elisabeth, ... (2)
Ström, Petter (2)
Tholerus, Emmi (2)
Weckmann, Armin (2)
Andersson Sundén, Er ... (2)
Binda, Federico, 198 ... (2)
Conroy, Sean (2)
Dzysiuk, Nataliia (2)
Ericsson, Göran (2)
Eriksson, Jacob, Dr, ... (2)
Hellesen, Carl, 1980 ... (2)
Possnert, Göran, 195 ... (2)
Sjöstrand, Henrik, 1 ... (2)
Skiba, Mateusz, 1985 ... (2)
Weiszflog, Matthias (2)
Bonanomi, N. (2)
Camenen, Y. (2)
Casson, FJ (2)
Citrin, J. (2)
Ratynskaia, Svetlana (2)
Stefanikova, Estera (2)
Imrišek, M. (2)
Szepesi, G. (2)
Olivares, Pablo Vall ... (2)
Vondráček, P. (2)
Zhou, Yushun (2)
Tolias, Panagiotis (2)
Griss, Patrick (2)
Jenko, Frank (2)
show less...
University
University of Gothenburg (6)
Royal Institute of Technology (2)
Uppsala University (2)
Örebro University (1)
Language
English (16)
Research subject (UKÄ/SCB)
Natural sciences (10)
Engineering and Technology (6)
Medical and Health Sciences (1)

Year

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view