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Träfflista för sökning "WFRF:(Blixt A) srt2:(2005-2009);srt2:(2008)"

Sökning: WFRF:(Blixt A) > (2005-2009) > (2008)

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1.
  • Ryazhkin, A. V., et al. (författare)
  • Local atomic structure of Fe-Ni/V multilayer nanostructures : EXAFS spectroscopy and synchrotron radiation data
  • 2008
  • Ingår i: Journal of Structural Chemistry. - : Springer Science and Business Media LLC. - 0022-4766 .- 1573-8779. ; 49:1, s. S129-S137
  • Tidskriftsartikel (refereegranskat)abstract
    • Fe, Ni, and V K EXAFS spectroscopic experiments were carried out at the European Synchrotron Radiation Center (ESRF) in the fluorescent mode on the 26 angstrom line with the use of the [(Fe82Ni18)(5)/V-6](25) and [(Fe82Ni18)(10)/V-6](25) samples of multilayer nanoheterostructures prepared by magnetron spraying (at Uppsala University). The partial interatomic distances were determined by the regularization technique. The existing distortions of the bee lattice in (Fe82N18)/V multilayer nanostructures depend strongly on the thickness of the ferromagnetic layers of the permalloy and also affect vanadium layers.
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2.
  • Stowell, Sean R, et al. (författare)
  • Galectins-1, -2 and -3 exhibit differential recognition of sialylated glycans and blood group antigens
  • 2008
  • Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 283:15, s. 10109-10123
  • Tidskriftsartikel (refereegranskat)abstract
    • Human galectins have functionally divergent roles, although most of the members of the galectin family bind weakly to the simple disaccharide lactose (Galss1-4Glc). To assess galectin-glycan interactions in more detail, we explored the binding of several important galectins (Gal-1, Gal-2, and Gal-3) on a glycan microarray containing hundreds of structurally diverse glycans. All three galectins exhibited unique glycan binding characteristics. Only Gal-1 and Gal-2 bound complex-type N-glycans and extended core 1 O-glycans with high affinity, while Gal-2 and Gal-3, but not Gal-1, bound A and B blood group antigens. Gal-2 failed to recognize any sialylated glycans regardless of linkage, whereas Gal-1 and Gal-3 bound a2-3, but not a2-6 sialylated glycans. All galectins showed higher binding to sulfated glycans relative to unsulfated ones. Each galectin exhibited higher binding for glycans with poly-N-acetyllactosamine (PL) sequences (Galss1-4GlcNAc)n when compared to N-acetyllactosamine (Galss1-4GlcNAc) in the microarray. However, only Gal-3 preferred PL when assessed by solution-based surface plasmon resonance. Removal of the terminal galactose residue in PL abrogated its recognition by Gal-1 and Gal-2 while having no substantial effect on Gal-3 recognition, demonstrating that Gal-3 recognizes internal N-acetyllactosamine units. These results provide novel insights into the functional constraints of glycan recognition by each galectin and underscore the basis for differences in biological activity.
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