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Träfflista för sökning "WFRF:(Edstrom L) srt2:(2015-2019)"

Sökning: WFRF:(Edstrom L) > (2015-2019)

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1.
  • Reichel, L., et al. (författare)
  • From soft to hard magnetic Fe-Co-B by spontaneous strain : a combined first principles and thin film study
  • 2015
  • Ingår i: Journal of Physics. - : IOP Publishing. - 0953-8984 .- 1361-648X. ; 27:47
  • Tidskriftsartikel (refereegranskat)abstract
    • In order to convert the well-known Fe-Co-B alloy from a soft to a hard magnet, we propose tetragonal strain by interstitial boron. Density functional theory reveals that when B atoms occupy octahedral interstitial sites, the bcc Fe-Co lattice is strained spontaneously. Such highly distorted Fe-Co is predicted to reach a strong magnetocrystalline anisotropy which may compete with shape anisotropy. To probe this theoretical suggestion experimentally, epitaxial films are examined. A spontaneous strain up to 5% lattice distortion is obtained for B content up to 4 at%, which leads to uniaxial anisotropy constants exceeding 0.5 MJ m(-3). However, a further addition of B results in a partial amorphisation, which degrades both anisotropy and magnetisation.
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2.
  • Olive, M, et al. (författare)
  • Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions
  • 2019
  • Ingår i: Nature communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 10:1, s. 1396-
  • Tidskriftsartikel (refereegranskat)abstract
    • Myoglobin, encoded by MB, is a small cytoplasmic globular hemoprotein highly expressed in cardiac myocytes and oxidative skeletal myofibers. Myoglobin binds O2, facilitates its intracellular transport and serves as a controller of nitric oxide and reactive oxygen species. Here, we identify a recurrent c.292C>T (p.His98Tyr) substitution in MB in fourteen members of six European families suffering from an autosomal dominant progressive myopathy with highly characteristic sarcoplasmic inclusions in skeletal and cardiac muscle. Myoglobinopathy manifests in adulthood with proximal and axial weakness that progresses to involve distal muscles and causes respiratory and cardiac failure. Biochemical characterization reveals that the mutant myoglobin has altered O2 binding, exhibits a faster heme dissociation rate and has a lower reduction potential compared to wild-type myoglobin. Preliminary studies show that mutant myoglobin may result in elevated superoxide levels at the cellular level. These data define a recognizable muscle disease associated with MB mutation.
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