| 1. |
- Cui, Daqing, et al.
(författare)
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Reductive immobilization of Se-79 by iron canister under simulated repository environment
- 2009
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Ingår i: Journal of Radioanalytical and Nuclear Chemistry. - : Springer Science and Business Media LLC. - 0236-5731 .- 1588-2780. ; 282:2, s. 349-354
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Tidskriftsartikel (refereegranskat)abstract
- To understand the fate of Se-79 in a repository-like environment, the interactions between iron canister surface with dissolved selenite (SeO3 (2-)) and selenate (SeO4 (2-)) in anaerobic solutions have been investigated. Se(IV) immobilization on iron surface was observed to be about 100 times faster than that of Se(VI) at same conditions. An iron surface coated with a FeCO3 layer corrosion product is more reactive than a polished iron to immobilize Se(IV) and Se(VI). The reacted iron surfaces were analysed by scanning electron microscopy (SEM) and energy dispersive spectrometer (EDS), X-ray diffraction (XRD), Raman spectrometry and micro-X-ray Absorption Spectroscopy (XAS). The result show that Se(IV) and Se(VI) were reduced and precipitated. The dominating phase was found to be FeSe2..
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| 2. |
- Jutzi, D, et al.
(författare)
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Aberrant interaction of FUS with the U1 snRNA provides a molecular mechanism of FUS induced amyotrophic lateral sclerosis
- 2020
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Ingår i: Nature communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 11:1, s. 6341-
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Tidskriftsartikel (refereegranskat)abstract
- Mutations in the RNA-binding protein Fused in Sarcoma (FUS) cause early-onset amyotrophic lateral sclerosis (ALS). However, a detailed understanding of central RNA targets of FUS and their implications for disease remain elusive. Here, we use a unique blend of crosslinking and immunoprecipitation (CLIP) and NMR spectroscopy to identify and characterise physiological and pathological RNA targets of FUS. We find that U1 snRNA is the primary RNA target of FUS via its interaction with stem-loop 3 and provide atomic details of this RNA-mediated mode of interaction with the U1 snRNP. Furthermore, we show that ALS-associated FUS aberrantly contacts U1 snRNA at the Sm site with its zinc finger and traps snRNP biogenesis intermediates in human and murine motor neurons. Altogether, we present molecular insights into a FUS toxic gain-of-function involving direct and aberrant RNA-binding and strengthen the link between two motor neuron diseases, ALS and spinal muscular atrophy (SMA).
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